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Conserved domains on  [gi|1776025254|ref|WP_153952139|]
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polyketide synthase PksJ [Bacillus subtilis]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
801-1698 0e+00

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


:

Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 963.55  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  801 PLVRVMSFSRSEQEHFLLVVIHHLIFDGVSSVTFIHSLFDTYQLLLKGQQPEIAVSPAIYHDFAAWEKNMLAGKDGVKHR 880
Cdd:COG1020    129 PLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLLLAELLRLYLAAYAGAPLPLPPLPIQYADYALWQREWLQGEELARQL 208
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  881 TYWQKQLSGTLPNLQLP-KVSASSVSEFREDTYTRRLSSGFMNQVRMFAKEHSVNVTTVFLSCYMMLLGRYTGQKEQIVG 959
Cdd:COG1020    209 AYWRQQLAGLPPLLELPtDRPRPAVQSYRGARVSFRLPAELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVG 288
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  960 MPAMVRPEERFDDAIGHFLNMLPIRSELNPADTFSSFISKLQLTILDGLDHAAYPFPKMVRDLNIPRSQAGSPVFQTAFF 1039
Cdd:COG1020    289 TPVAGRPRPELEGLVGFFVNTLPLRVDLSGDPSFAELLARVRETLLAAYAHQDLPFERLVEELQPERDLSRNPLFQVMFV 368
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1040 YQNFLQSGsyqsllsryADF--FSVDYVEYIHQEGEYELVFELWETEEKMELNIKYNTGLFDAASISAMFDHFVYVTEQA 1117
Cdd:COG1020    369 LQNAPADE---------LELpgLTLEPLELDSGTAKFDLTLTVVETGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEAL 439
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1118 MLNPSQPLKEYSLLPEAEKQMILKTWNATGKTYP-YITFHELFEQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQ 1196
Cdd:COG1020    440 AADPDQPLGDLPLLTAAERQQLLAEWNATAAPYPaDATLHELFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLR 519
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1197 AHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLEDSEVFITLTTSELVNTLSWNGVTTALLDQ 1276
Cdd:COG1020    520 ALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYMLEDAGARLVLTQSALAARLPELGVPVLALDA 599
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1277 dwDEIAQTASDRkvLTRTVTPENLAYVIYTSGSTGKPKGVMIPHKALTNFLVSMGETPGLTAEDKMLAVTTYCFDIAALE 1356
Cdd:COG1020    600 --LALAAEPATN--PPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFDASVWE 675
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1357 LFLPLIKGAHCYICQTEHTKDVEKLKRDIRTIKPTVMQATPATWKMLFYSGWENEENVK-ILCGGEALPETLKRYFLDTG 1435
Cdd:COG1020    676 IFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLLRALLDAAPEALPSLRlVLVGGEALPPELVRRWRARL 755
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1436 SEA--WNMFGPTETTIWSAVQRINDECSRA---TIGRPIANTQIYITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELT 1510
Cdd:COG1020    756 PGArlVNLYGPTETTVDSTYYEVTPPDADGgsvPIGRPIANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELT 835
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1511 DSRFIDNPF-EPGSKLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMDN-----L 1584
Cdd:COG1020    836 AERFVADPFgFPGARLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDApgdkrL 915
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1585 AAYYTAkHANASLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLKNIDLSGEQlkQRQTSPKNIQDTVFT 1664
Cdd:COG1020    916 VAYVVP-EAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAAAAAA--AAAAPPAEEEEEEAA 992
                          890       900       910
                   ....*....|....*....|....*....|....
gi 1776025254 1665 IWQEVLKTSDIEWDDGFFDVGGDSLLAVTVADRI 1698
Cdd:COG1020    993 LALLLLLVVVVGDDDFFFFGGGLGLLLLLALARA 1026
A_NRPS_TubE_like cd05906
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ...
20-561 0e+00

The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


:

Pssm-ID: 341232 [Multi-domain]  Cd Length: 540  Bit Score: 866.98  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254   20 PLHISEKQPATIPEVLYRtAAELGDTKGIIYLQPDGTEVYQSYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNSQLLP 99
Cdd:cd05906      1 PLHRPEGAPRTLLELLLR-AAERGPTKGITYIDADGSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  100 AFWGCVLTGVVPAPLAVPPTYAESSSGTQKLKDAWTLLDKPAVITDRGMHQEMLDWAKEQGLEGFRAIIVEDLLSAEADT 179
Cdd:cd05906     80 AFWACVLAGFVPAPLTVPPTYDEPNARLRKLRHIWQLLGSPVVLTDAELVAEFAGLETLSGLPGIRVLSIEELLDTAADH 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  180 DWHQSSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDHVGGIGMLHLRDVYLGCQEIN 259
Cdd:cd05906    160 DLPQSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHVGGLVELHLRAVYLGCQQVH 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  260 VSSETILMEPLKWLDWIDHYRASVTWAPNFAFGLVTDFAEEIKDRKWDLSSMRYMLNGGEAMVAKVGRRILELLEPHGLP 339
Cdd:cd05906    240 VPTEEILADPLRWLDLIDRYRVTITWAPNFAFALLNDLLEEIEDGTWDLSSLRYLVNAGEAVVAKTIRRLLRLLEPYGLP 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  340 ADAIRPAWGMSETSSGVIFSHEFTRAGTSDDDHFVEIGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGYYQRPD 419
Cdd:cd05906    320 PDAIRPAFGMTETCSGVIYSRSFPTYDHSQALEFVSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPE 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  420 LNESVFTEDGWFETGDLGFLRNGRLTITGRTKDAIIINGINYYSHAIESAVEELSEIETSYTAACAVRLGQNSTDQLAIF 499
Cdd:cd05906    400 ANAEAFTEDGWFRTGDLGFLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPSFTAAFAVRDPGAETEELAIF 479
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1776025254  500 FVTSAKLNDeQMSQLLRNIQSHVSQVIGVTPEYLLPVQKEEIPKTAIGKIQRTQLKTSFENG 561
Cdd:cd05906    480 FVPEYDLQD-ALSETLRAIRSVVSREVGVSPAYLIPLPKEEIPKTSLGKIQRSKLKAAFEAG 540
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
3339-3881 0e+00

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


:

Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 814.49  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3339 EPVAIVGISGRFPGAMDIDEFWKNLEEGKDSITEVPKDRWDWREHYGNPDTDVNKTDIKWGGFIDGVAEFDPLFFGISPR 3418
Cdd:COG3321      4 EPIAIIGMACRFPGADDPEEFWRNLRAGRDAITEVPADRWDADAYYDPDPDAPGKTYVRWGGFLDDVDEFDALFFGISPR 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3419 EADYVDPQQRLLMTYVWKALEDAGCPPQSLSGTGTGIFIGTGNTGYKDLFHRANLPIEGHAATGhMIPSVGPNRMSYFLN 3498
Cdd:COG3321     84 EAEAMDPQQRLLLEVAWEALEDAGYDPESLAGSRTGVFVGASSNDYALLLLADPEAIDAYALTG-NAKSVLAGRISYKLD 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3499 IHGPSEPVETACSSSLVAIHRAVTAMQNGDCEMAIAGGVNTILTEEAHISYSKAGMLSKDGRCKTFSADANGYVRGEGVG 3578
Cdd:COG3321    163 LRGPSVTVDTACSSSLVAVHLACQSLRSGECDLALAGGVNLMLTPESFILFSKGGMLSPDGRCRAFDADADGYVRGEGVG 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3579 MVMLKKLEDAERDGNHIYGVIRGTAENHGGRANTLTSPNPKAQADLLVRAYRQAGIDPSTVTYIEAHGTGTELGDPIEIN 3658
Cdd:COG3321    243 VVVLKRLSDALRDGDRIYAVIRGSAVNQDGRSNGLTAPNGPAQAAVIRRALADAGVDPATVDYVEAHGTGTPLGDPIEAA 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3659 GLKAAFKELsnmRGESQPdvpdhrCGIGSVKSNIGHLELAAGISGLIKVLLQMKHKTLVKSLHCETLNPYLQLTDSPFYI 3738
Cdd:COG3321    323 ALTAAFGQG---RPADQP------CAIGSVKSNIGHLEAAAGVAGLIKAVLALRHGVLPPTLHFETPNPHIDFENSPFYV 393
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3739 VQEKQEWKSvtdcdgNELPRRAGISSFGIGGVNAHIVIEEYMPKANSEHTATEQPNVIVLSAKNKSRLIDRASQLLEAIR 3818
Cdd:COG3321    394 NTELRPWPA------GGGPRRAGVSSFGFGGTNAHVVLEEAPAAAPAAAAAARPPQLLVLSAKTEEALRALAARLAAFLE 467
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1776025254 3819 NKkyTDQGLHRIAYTLQVGREEMDERLACVAGTMQELEEKLQAFVDGKEETDEFFRGQSHRNK 3881
Cdd:COG3321    468 AH--PDLDLADVAYTLATGRAHFEHRLAVVASSREELAAKLRALAAGEAAPGVVTGAAAAAPK 528
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
1759-2291 0e+00

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


:

Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 644.62  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1759 DDSVAIIGISCEFPGAKNHDEFWENLRDGKESIAFFNKEEL--QRFGISKEIAENADYVPAKASIEGKDRFDPSFFQISP 1836
Cdd:COG3321      3 DEPIAIIGMACRFPGADDPEEFWRNLRAGRDAITEVPADRWdaDAYYDPDPDAPGKTYVRWGGFLDDVDEFDALFFGISP 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1837 KDAEFMDPQLRMLLTHSWKAIEDAGYAAGQIP--QTSVFMSASNNSYRALLPSDttesLETPDGYVSWVLAQSgTIPTMI 1914
Cdd:COG3321     83 REAEAMDPQQRLLLEVAWEALEDAGYDPESLAgsRTGVFVGASSNDYALLLLAD----PEAIDAYALTGNAKS-VLAGRI 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1915 SHKLGLRGPSYFVHANCSSSLIGLHSAYKSLLSAESDYALVGGATLHTESNIGYVHQPGLNFSSDGHIKAFDASADGMIG 1994
Cdd:COG3321    158 SYKLDLRGPSVTVDTACSSSLVAVHLACQSLRSGECDLALAGGVNLMLTPESFILFSKGGMLSPDGRCRAFDADADGYVR 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1995 GEGVAVVLLKKAADAVKDGDHIYALLRGIGVNNDGADKvGFYAPSVKGQADVVQQVMNQTKIHPESICYVEAHGTGTKLG 2074
Cdd:COG3321    238 GEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRSN-GLTAPNGPAQAAVIRRALADAGVDPATVDYVEAHGTGTPLG 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2075 DPIELAALTNVYRQYTNKTQFCGIGSVKTNIGHLDTAAGLAGCIKVVMSLYHQELAPSINYKEPNPNTDLASSPFYVVDQ 2154
Cdd:COG3321    317 DPIEAAALTAAFGQGRPADQPCAIGSVKSNIGHLEAAAGVAGLIKAVLALRHGVLPPTLHFETPNPHIDFENSPFYVNTE 396
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2155 KKTLSREIQTHRAALSSFGLGGTNTHAIFEQF--KRDSDKGKIDGTCIVPISAKNKERLQEYAEDILAYLERRGLENsqL 2232
Cdd:COG3321    397 LRPWPAGGGPRRAGVSSFGFGGTNAHVVLEEApaAAPAAAAAARPPQLLVLSAKTEEALRALAARLAAFLEAHPDLD--L 474
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1776025254 2233 PDFAYTLQVGREAMEHRVVFIADHVNELKQRLTDFINGKTAiEGCFQGSKHNAREVSWL 2291
Cdd:COG3321    475 ADVAYTLATGRAHFEHRLAVVASSREELAAKLRALAAGEAA-PGVVTGAAAAAPKVAFL 532
PKS cd00833
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ...
4588-4989 4.14e-135

polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different products, called polyketides, by successive decarboxylating Claisen condensations. PKSs can be divided into 2 groups, modular type I PKSs consisting of one or more large multifunctional proteins and iterative type II PKSs, complexes of several monofunctional subunits.


:

Pssm-ID: 238429 [Multi-domain]  Cd Length: 421  Bit Score: 431.21  E-value: 4.14e-135
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4588 EGIAVVGLSCRFPGAETLESYWSLLSEGRSSIGPIPAERWGCKTPY------------YAGVIDGVSYFDPDFFLLHEED 4655
Cdd:cd00833      1 EPIAIVGMACRFPGAADPDEFWENLLEGRDAISEIPEDRWDADGYYpdpgkpgktytrRGGFLDDVDAFDAAFFGISPRE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4656 VRAMDPQALLVLEECLKLLYHAGYTPEEIKGKPVGVYIGGRS---QHKPDEDSLDHAKNPIVTVGQNYLAANLSQFFDVR 4732
Cdd:cd00833     81 AEAMDPQQRLLLEVAWEALEDAGYSPESLAGSRTGVFVGASSsdyLELLARDPDEIDAYAATGTSRAFLANRISYFFDLR 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4733 GPSVVVDTACSSALVGMNMAIQALRGGDIQSAIVGGVSLLSSDASHRLFDRRGILSKHSSFHVFDERADGVVLGEGVGMV 4812
Cdd:cd00833    161 GPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLSPDGRCRPFDADADGYVRGEGVGVV 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4813 MLKTVKQALEDGDTIYAVVKAASVNNDGRTAGPATPNLEAQKEVMKDALFKSGKKPEDISYLEANGSGSIVTDLLELKAI 4892
Cdd:cd00833    241 VLKRLSDALRDGDRIYAVIRGSAVNQDGRTKGITAPSGEAQAALIRRAYARAGVDPSDIDYVEAHGTGTPLGDPIEVEAL 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4893 QSVYRSGHS--SPLSLGSIKPNIGHPLCAEGIASFIKVVLMLKERRFVPFLSGEKEMAHFDQQKANITFSRALEKW-TDS 4969
Cdd:cd00833    321 AKVFGGSRSadQPLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKIDFEESPLRVPTEARPWpAPA 400
                          410       420
                   ....*....|....*....|.
gi 1776025254 4970 QP-TAAINCFADGGTNVHVIV 4989
Cdd:cd00833    401 GPrRAGVSSFGFGGTNAHVIL 421
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
2672-3082 9.55e-130

ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes both KR domains of the Bacillus subtilis Pks J,-L, and PksM, and all three KR domains of PksN, components of the megacomplex bacillaene synthase, which synthesizes the antibiotic bacillaene. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


:

Pssm-ID: 187656 [Multi-domain]  Cd Length: 436  Bit Score: 416.38  E-value: 9.55e-130
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2672 LEPVWEKQNEEREDEDLSYTEHIIVLFETERSVTDSIASHMKDARvitlneavghiaeryQCYMQNIFELLQ-SKVRELS 2750
Cdd:cd08953     36 LQPVWAPAALASAFLALAYEAALLGLAAAEAALLDALSALDPAAA---------------LQLLESLQRLLKaGLLAARA 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2751 AGRIIIQAIVPLEKEKQL------FAGVSGLLKTAEIEFSKLTAQVIEIEKPEEMID-LHLKLKDDSQRPFDKQIRYEAG 2823
Cdd:cd08953    101 SGRALLQVVTGLPGALGLdaldpaGAGLAGLLRTLAQEYPGLTCRLIDLDAGEASAEaLARELAAELAAPGAAEVRYRDG 180
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2824 HRFVKGWREMVLPSADTLHMPWRDEGVYLITGGAGSLGLLFAKEIANRTGRsTIVLTGRSVLSEDKENE---LEALRSIG 2900
Cdd:cd08953    181 LRYVQTLEPLPLPAGAAASAPLKPGGVYLVTGGAGGIGRALARALARRYGA-RLVLLGRSPLPPEEEWKaqtLAALEALG 259
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2901 AEVVYREADVSDQHAVHHLFEEIKERYGTLNGIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSGLLHVDECSKDFPLDFFI 2980
Cdd:cd08953    260 ARVLYISADVTDAAAVRRLLEKVRERYGAIDGVIHAAGVLRDALLAQKTAEDFEAVLAPKVDGLLNLAQALADEPLDFFV 339
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2981 FFSSVSGCLGNAGQADYAAANSFMDAFAEYRRSLAAskkrFGSTISFNWPLWEEGGMQVGAEDEkRMLKTTGMVPMPTDS 3060
Cdd:cd08953    340 LFSSVSAFFGGAGQADYAAANAFLDAFAAYLRQRGP----QGRVLSINWPAWREGGMAADLGAR-ELLARAGLLPIEPEE 414
                          410       420
                   ....*....|....*....|..
gi 1776025254 3061 GLKAFYQGIASDKPQVFVMEGQ 3082
Cdd:cd08953    415 GLQALEQALSSDLPQVLVSPGD 436
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
4029-4401 1.70e-109

ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes both KR domains of the Bacillus subtilis Pks J,-L, and PksM, and all three KR domains of PksN, components of the megacomplex bacillaene synthase, which synthesizes the antibiotic bacillaene. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


:

Pssm-ID: 187656 [Multi-domain]  Cd Length: 436  Bit Score: 358.22  E-value: 1.70e-109
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4029 DWKEFDGLVDVIGCGWDDeGRLDWIEWVQRLVEF----GHKEGLRLLCVTKGLESFQNTS-VRMAGASRAGLYRMLQCEY 4103
Cdd:cd08953     61 LAAAEAALLDALSALDPA-AALQLLESLQRLLKAgllaARASGRALLQVVTGLPGALGLDaLDPAGAGLAGLLRTLAQEY 139
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4104 SHLISRHMDAEEVTDHP-RLAKLIADEfYSESYDAEVCYRDGLRYQSFLKAHPETGKATeQSAVFPKDHVLLITGGTRGI 4182
Cdd:cd08953    140 PGLTCRLIDLDAGEASAeALARELAAE-LAAPGAAEVRYRDGLRYVQTLEPLPLPAGAA-ASAPLKPGGVYLVTGGAGGI 217
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4183 GLLCARHFAECYGvKKLVLTGREQLPPREEWARfktsntslaekiQAVRELEAKGVQVEMLSLTLSDDAQVEQTLQHIKR 4262
Cdd:cd08953    218 GRALARALARRYG-ARLVLLGRSPLPPEEEWKA------------QTLAALEALGARVLYISADVTDAAAVRRLLEKVRE 284
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4263 TLGPIGGVIHCAGLTDMDTLafIRKTSDDIQRVMEPKVSGLTTLYRHVCNEPLQFFVLFSSVSAIIPelSAGQADYAMAN 4342
Cdd:cd08953    285 RYGAIDGVIHAAGVLRDALL--AQKTAEDFEAVLAPKVDGLLNLAQALADEPLDFFVLFSSVSAFFG--GAGQADYAAAN 360
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1776025254 4343 SYMDYFAEAHQK---HVPIISVQWPNWKETGMGEV--TNQAYRESGLFSITNSEGLRFLDQIVS 4401
Cdd:cd08953    361 AFLDAFAAYLRQrgpQGRVLSINWPAWREGGMAADlgARELLARAGLLPIEPEEGLQALEQALS 424
PS-DH pfam14765
Polyketide synthase dehydratase; This is the dehydratase domain of polyketide synthases. ...
2373-2658 1.08e-61

Polyketide synthase dehydratase; This is the dehydratase domain of polyketide synthases. Structural analysis shows these DH domains are double hotdogs in which the active site contains a histidine from the N-terminal hotdog and an aspartate from the C-terminal hotdog. Studies have uncovered that a substrate tunnel formed between the DH domains may be essential for loading substrates and unloading products.


:

Pssm-ID: 434191  Cd Length: 296  Bit Score: 214.93  E-value: 1.08e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2373 HPLL-HQNTS-DFSEQKFSSVFTGDEF-FLRDHVVRGKPVLPGVAYLEMAYAAINQAAGSEIG---QDVRIRlnhtvwvQ 2446
Cdd:pfam14765    1 HPLLgSRVPSpSDLEPVWRNRLRLADLpWLRDHRVGGTVVLPGAGYLEMALEAARQLFGGSGAvalRDVSIL-------K 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2447 PVVVDRHSA-QVDISLFPEEDG---KITFDIYSTQEDGDDPVIHSQGSAELASAAETPVADLTEISRRC----GKGKMSP 2518
Cdd:pfam14765   74 ALVLPEDDPvEVQTSLTPEEDGadsWWEFEIFSRAGGGWEWTLHATGTVRLAPGEPAAPVDLESLPARCaqpaDPRSVSS 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2519 DQFYEEGRSRGMFHGPAFQGIKNVNIGNREVLAQLQLPEIVSGTNEQFVLHPSIMDSALQT-ATICIMQELTDQKLILPF 2597
Cdd:pfam14765  154 AEFYERLAARGLFYGPAFQGLRRIWRGDGEALAEARLPEAAAGGESPYLLHPALLDAALQLlGAALPAEAEHADQAYLPV 233
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1776025254 2598 ALEELEVIKG--CSSSMWAYARLSDSDHSGGVvqkADIDVIDESGSVCVRIKGFSTRVLEGEV 2658
Cdd:pfam14765  234 GIERLRIYRSlpPGEPLWVHARLERRGGRTIV---GDLTLVDEDGRVVARIEGLRLRRVEREA 293
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
3111-3185 2.32e-13

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


:

Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 68.43  E-value: 2.32e-13
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1776025254  3111 QTRKLEAALIQMVGAILKVNTDD-IDVNTELSEYGFDSVTFTVFTNKINEKFQLELTPTIFFEYGSVQSLAEYVVA 3185
Cdd:smart00823    9 RRRLLLDLVREQVAAVLGHAAAEaIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHLAA 84
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
3221-3281 1.28e-12

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


:

Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 66.50  E-value: 1.28e-12
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1776025254  3221 VSAILKVNSED-IDVNTELSEYGFDSVTFTVFTNKINEEFQLELTPTIFFEYGSIHSLAEYL 3281
Cdd:smart00823   21 VAAVLGHAAAEaIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHL 82
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
592-666 5.73e-12

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


:

Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 64.10  E-value: 5.73e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1776025254  592 REEIQEHLLTCLTEELHVSRDWVEPNAN-IQSLGVNSIKMMKLIRSIEKNYHIKLTAREIHQYPTIERLASYLSEH 666
Cdd:COG0236      3 REELEERLAEIIAEVLGVDPEEITPDDSfFEDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEEK 78
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
4465-4525 2.21e-11

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.


:

Pssm-ID: 425746 [Multi-domain]  Cd Length: 62  Bit Score: 61.81  E-value: 2.21e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1776025254 4465 SWLIDLFTEELRIDREDFEIDGLFQDYGVDSIILAQVLQRINRKLEAALDPSILYEYPTIQ 4525
Cdd:pfam00550    1 ERLRELLAEVLGVPAEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLA 61
C_NRPS-like super family cl40425
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
695-894 2.46e-07

Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long, with various activities such as antibiotic, antifungal, antitumor and immunosuppression. There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


The actual alignment was detected with superfamily member cd19534:

Pssm-ID: 394795 [Multi-domain]  Cd Length: 428  Bit Score: 56.88  E-value: 2.46e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  695 PLSEVQKglWTLQKMSPEKSAYHVPLCFKFSSGLHLETLQQAFGLVLNQHPILKHVIQEKDGVPILKNEPALSIEIKTEn 774
Cdd:cd19534      3 PLTPIQR--WFFEQNLAGRHHFNQSVLLRVPQGLDPDALRQALRALVEHHDALRMRFRREDGGWQQRIRGDVEELFRLE- 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  775 ISSMKESDIPAFLRKKVkEPYVK----ENSPLVRVMSFSRSEQEHFLLVVIHHLIFDGVSSVTFIHSLFDTYQLLLKGQQ 850
Cdd:cd19534     80 VVDLSSLAQAAAIEALA-AEAQSsldlEEGPLLAAALFDGTDGGDRLLLVIHHLVVDGVSWRILLEDLEAAYEQALAGEP 158
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1776025254  851 PEIAVSPAiYHDFAAWEKNMLAGKDGVKHRTYWQKQLSGTLPNL 894
Cdd:cd19534    159 IPLPSKTS-FQTWAELLAEYAQSPALLEELAYWRELPAADYWGL 201
PksD super family cl43841
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
3909-4006 7.68e-07

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


The actual alignment was detected with superfamily member COG3321:

Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 56.03  E-value: 7.68e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3909 LADLWVKGVSIQWNTLYGETKPRLISLPSYPFAKDHYWVPAKEHSERDKKELVNAIEDRAACFLTKQWSLSPIGSAVPGT 3988
Cdd:COG3321    837 LAQLWVAGVPVDWSALYPGRGRRRVPLPTYPFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAA 916
                           90
                   ....*....|....*...
gi 1776025254 3989 RTVAILCCQETADLAAEV 4006
Cdd:COG3321    917 AALALAAAALAALLALVA 934
PksD super family cl43841
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
2313-2347 1.02e-06

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


The actual alignment was detected with superfamily member COG3321:

Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 55.65  E-value: 1.02e-06
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1776025254 2313 LAEMWSKGAHIDWMQLYKGERPNRMSLPTYPFAKE 2347
Cdd:COG3321    837 LAQLWVAGVPVDWSALYPGRGRRRVPLPTYPFQRE 871
KAsynt_C_assoc super family cl24694
Ketoacyl-synthetase C-terminal extension; KAsynt_C_assoc represents the very C-terminus of a ...
4973-5010 2.77e-04

Ketoacyl-synthetase C-terminal extension; KAsynt_C_assoc represents the very C-terminus of a subset of proteins from the keto-acyl-synthetase 2 family. It is found in proteins ranging from bacteria to human.


The actual alignment was detected with superfamily member pfam16197:

Pssm-ID: 465059 [Multi-domain]  Cd Length: 111  Bit Score: 43.30  E-value: 2.77e-04
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1776025254 4973 AAINCFADGGTNVHVIVEAWEKdeKHAIKRSPKSPPQL 5010
Cdd:pfam16197   27 VGVNSFGFGGANAHVILKSNPK--PKIPPESPDNLPRL 62
 
Name Accession Description Interval E-value
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
801-1698 0e+00

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 963.55  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  801 PLVRVMSFSRSEQEHFLLVVIHHLIFDGVSSVTFIHSLFDTYQLLLKGQQPEIAVSPAIYHDFAAWEKNMLAGKDGVKHR 880
Cdd:COG1020    129 PLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLLLAELLRLYLAAYAGAPLPLPPLPIQYADYALWQREWLQGEELARQL 208
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  881 TYWQKQLSGTLPNLQLP-KVSASSVSEFREDTYTRRLSSGFMNQVRMFAKEHSVNVTTVFLSCYMMLLGRYTGQKEQIVG 959
Cdd:COG1020    209 AYWRQQLAGLPPLLELPtDRPRPAVQSYRGARVSFRLPAELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVG 288
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  960 MPAMVRPEERFDDAIGHFLNMLPIRSELNPADTFSSFISKLQLTILDGLDHAAYPFPKMVRDLNIPRSQAGSPVFQTAFF 1039
Cdd:COG1020    289 TPVAGRPRPELEGLVGFFVNTLPLRVDLSGDPSFAELLARVRETLLAAYAHQDLPFERLVEELQPERDLSRNPLFQVMFV 368
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1040 YQNFLQSGsyqsllsryADF--FSVDYVEYIHQEGEYELVFELWETEEKMELNIKYNTGLFDAASISAMFDHFVYVTEQA 1117
Cdd:COG1020    369 LQNAPADE---------LELpgLTLEPLELDSGTAKFDLTLTVVETGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEAL 439
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1118 MLNPSQPLKEYSLLPEAEKQMILKTWNATGKTYP-YITFHELFEQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQ 1196
Cdd:COG1020    440 AADPDQPLGDLPLLTAAERQQLLAEWNATAAPYPaDATLHELFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLR 519
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1197 AHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLEDSEVFITLTTSELVNTLSWNGVTTALLDQ 1276
Cdd:COG1020    520 ALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYMLEDAGARLVLTQSALAARLPELGVPVLALDA 599
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1277 dwDEIAQTASDRkvLTRTVTPENLAYVIYTSGSTGKPKGVMIPHKALTNFLVSMGETPGLTAEDKMLAVTTYCFDIAALE 1356
Cdd:COG1020    600 --LALAAEPATN--PPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFDASVWE 675
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1357 LFLPLIKGAHCYICQTEHTKDVEKLKRDIRTIKPTVMQATPATWKMLFYSGWENEENVK-ILCGGEALPETLKRYFLDTG 1435
Cdd:COG1020    676 IFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLLRALLDAAPEALPSLRlVLVGGEALPPELVRRWRARL 755
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1436 SEA--WNMFGPTETTIWSAVQRINDECSRA---TIGRPIANTQIYITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELT 1510
Cdd:COG1020    756 PGArlVNLYGPTETTVDSTYYEVTPPDADGgsvPIGRPIANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELT 835
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1511 DSRFIDNPF-EPGSKLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMDN-----L 1584
Cdd:COG1020    836 AERFVADPFgFPGARLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDApgdkrL 915
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1585 AAYYTAkHANASLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLKNIDLSGEQlkQRQTSPKNIQDTVFT 1664
Cdd:COG1020    916 VAYVVP-EAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAAAAAA--AAAAPPAEEEEEEAA 992
                          890       900       910
                   ....*....|....*....|....*....|....
gi 1776025254 1665 IWQEVLKTSDIEWDDGFFDVGGDSLLAVTVADRI 1698
Cdd:COG1020    993 LALLLLLVVVVGDDDFFFFGGGLGLLLLLALARA 1026
A_NRPS_TubE_like cd05906
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ...
20-561 0e+00

The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341232 [Multi-domain]  Cd Length: 540  Bit Score: 866.98  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254   20 PLHISEKQPATIPEVLYRtAAELGDTKGIIYLQPDGTEVYQSYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNSQLLP 99
Cdd:cd05906      1 PLHRPEGAPRTLLELLLR-AAERGPTKGITYIDADGSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  100 AFWGCVLTGVVPAPLAVPPTYAESSSGTQKLKDAWTLLDKPAVITDRGMHQEMLDWAKEQGLEGFRAIIVEDLLSAEADT 179
Cdd:cd05906     80 AFWACVLAGFVPAPLTVPPTYDEPNARLRKLRHIWQLLGSPVVLTDAELVAEFAGLETLSGLPGIRVLSIEELLDTAADH 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  180 DWHQSSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDHVGGIGMLHLRDVYLGCQEIN 259
Cdd:cd05906    160 DLPQSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHVGGLVELHLRAVYLGCQQVH 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  260 VSSETILMEPLKWLDWIDHYRASVTWAPNFAFGLVTDFAEEIKDRKWDLSSMRYMLNGGEAMVAKVGRRILELLEPHGLP 339
Cdd:cd05906    240 VPTEEILADPLRWLDLIDRYRVTITWAPNFAFALLNDLLEEIEDGTWDLSSLRYLVNAGEAVVAKTIRRLLRLLEPYGLP 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  340 ADAIRPAWGMSETSSGVIFSHEFTRAGTSDDDHFVEIGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGYYQRPD 419
Cdd:cd05906    320 PDAIRPAFGMTETCSGVIYSRSFPTYDHSQALEFVSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPE 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  420 LNESVFTEDGWFETGDLGFLRNGRLTITGRTKDAIIINGINYYSHAIESAVEELSEIETSYTAACAVRLGQNSTDQLAIF 499
Cdd:cd05906    400 ANAEAFTEDGWFRTGDLGFLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPSFTAAFAVRDPGAETEELAIF 479
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1776025254  500 FVTSAKLNDeQMSQLLRNIQSHVSQVIGVTPEYLLPVQKEEIPKTAIGKIQRTQLKTSFENG 561
Cdd:cd05906    480 FVPEYDLQD-ALSETLRAIRSVVSREVGVSPAYLIPLPKEEIPKTSLGKIQRSKLKAAFEAG 540
PRK12467 PRK12467
peptide synthase; Provisional
185-1737 0e+00

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 845.21  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  185 SPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDI-----TFN-----WMPFDHVGGIGMLHLRDvylg 254
Cdd:PRK12467   654 DPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSmlmvsTFAfdlgvTELFGALASGATLHLLP---- 729
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  255 cqeinvssETILMEPLKWLDWIDHYRASVTWAPNFAFGLVTDFAEEIKDRkwdlsSMRYMLNGGEAMVAKVGRRILELLe 334
Cdd:PRK12467   730 --------PDCARDAEAFAALMADQGVTVLKIVPSHLQALLQASRVALPR-----PQRALVCGGEALQVDLLARVRALG- 795
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  335 phglPADAIRPAWGMSETSSGVIFsheFTRAGTSDDDHFVEIGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGY 414
Cdd:PRK12467   796 ----PGARLINHYGPTETTVGVST---YELSDEERDFGNVPIGQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGY 868
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  415 YQRPDLNESVFTEDGW-------FETGDLGFLR-NGRLTITGRTKDAIIINGINYyshaiesaveELSEIETSYTAACAV 486
Cdd:PRK12467   869 HRRPALTAERFVPDPFgadggrlYRTGDLARYRaDGVIEYLGRMDHQVKIRGFRI----------ELGEIEARLLAQPGV 938
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  487 R------LGQNSTDQLAIFFVTSAKLNDEQMSQLLRNIQSHVSQVIgvtPEYLLP---VQKEEIPKTAIGKIQRTQLKts 557
Cdd:PRK12467   939 ReavvlaQPGDAGLQLVAYLVPAAVADGAEHQATRDELKAQLRQVL---PDYMVPahlLLLDSLPLTPNGKLDRKALP-- 1013
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  558 fengefdhllhKPnrmnDAVQDEEMQQADhvkrvREEIQEHLLTCLTEELHVSRdwVEPNANIQSLGVNSIKMMKLIRSI 637
Cdd:PRK12467  1014 -----------KP----DASAVQATFVAP-----QTELEKRLAAIWADVLKVER--VGLTDNFFELGGHSLLATQVISRV 1071
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  638 EKNYHIKLTAREIHQYPTIERLASYLSehedlssssADKKGTDTYKTEPERSQAtfQPLSEVQKGLWTLQKMSPEKSAYH 717
Cdd:PRK12467  1072 RQRLGIQVPLRTLFEHQTLAGFAQAVA---------AQQQGAQPALPDVDRDQP--LPLSYAQERQWFLWQLEPGSAAYH 1140
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  718 VPLCFKFSSGLHLETLQQAFGLVLNQHPILKHVIQEKDGVPILKNEPALS--IEIKTENISSMKESDIPAFLRKKVKEPY 795
Cdd:PRK12467  1141 IPQALRLKGPLDIEALERSFDALVARHESLRTTFVQEDGRTRQVIHPVGSltLEEPLLLAADKDEAQLKVYVEAEARQPF 1220
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  796 VKENSPLVRVMSFSRSEQEHFLLVVIHHLIFDGVSSVTFIHSLFDTYQLLLKGQQPEIAVSPAIYHDFAAWEKNMLAGKD 875
Cdd:PRK12467  1221 DLEQGPLLRVGLLRLAADEHVLVLTLHHIVSDGWSMQVLVDELVALYAAYSQGQSLQLPALPIQYADYAVWQRQWMDAGE 1300
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  876 GVKHRTYWQKQLSGTLPNLQLP-KVSASSVSEFREDTYTRRLSSGFMNQVRMFAKEHSVNVTTVFLSCYMMLLGRYTGQK 954
Cdd:PRK12467  1301 RARQLAYWKAQLGGEQPVLELPtDRPRPAVQSHRGARLAFELPPALAEGLRALARREGVTLFMLLLASFQTLLHRYSGQD 1380
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  955 EQIVGMPAMVRPEERFDDAIGHFLNMLPIRSELNPADTFSSFISKLQLTILDGLDHAAYPFPKMVRDLNIPRSQAGSPVF 1034
Cdd:PRK12467  1381 DIRVGVPIANRNRAETEGLIGFFVNTQVLRAEVDGQASFQQLLQQVKQAALEAQAHQDLPFEQLVEALQPERSLSHSPLF 1460
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1035 QTAFFYQNFLQSGSYQsllsryADFFSVDYVEYIHQEGEYELVFELWETEEKMELNIKYNTGLFDAASISAMFDHFVYVT 1114
Cdd:PRK12467  1461 QVMFNHQRDDHQAQAQ------LPGLSVESLSWESQTAQFDLTLDTYESSEGLQASLTYATDLFEASTIERLAGHWLNLL 1534
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1115 EQAMLNPSQPLKEYSLLPEAEKQMILKTWNATGKTYPY-ITFHELFEQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAI 1193
Cdd:PRK12467  1535 QGLVADPERRLGELDLLDEAERRQILEGWNATHTGYPLaRLVHQLIEDQAAATPEAVALVFGEQELTYGELNRRANRLAH 1614
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1194 YLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLEDSEVFITLTTSELVNTL-SWNGVTTA 1272
Cdd:PRK12467  1615 RLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQSHLQARLpLPDGLRSL 1694
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1273 LLDQ--DWDEiAQTASDRKVltrTVTPENLAYVIYTSGSTGKPKGVMIPHKALTNFLVSMGETPGLTAEDKMLAVTTYCF 1350
Cdd:PRK12467  1695 VLDQedDWLE-GYSDSNPAV---NLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFAF 1770
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1351 DIAALELFLPLIKGAHCYICQTEHTKDVEKLKRDIRTIKPTVMQATPATWKMlFYSGWENEENV----KILCGGEALPET 1426
Cdd:PRK12467  1771 DVSVWELFWPLINGARLVIAPPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQ-LLQMDEQVEHPlslrRVVCGGEALEVE 1849
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1427 LKRYFL----DTGseAWNMFGPTETTI----WSAvqRINDECSRAT--IGRPIANTQIYITDSQLAPVPAGVPGELCIAG 1496
Cdd:PRK12467  1850 ALRPWLerlpDTG--LFNLYGPTETAVdvthWTC--RRKDLEGRDSvpIGQPIANLSTYILDASLNPVPIGVAGELYLGG 1925
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1497 DGVAKGYYKKEELTDSRFIDNPF-EPGSKLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILEC 1575
Cdd:PRK12467  1926 VGLARGYLNRPALTAERFVADPFgTVGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREA 2005
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1576 VVVA-DMDN---LAAYYTAKHA-------NASLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLKNIDLS 1644
Cdd:PRK12467  2006 VVIAqDGANgkqLVAYVVPTDPglvdddeAQVALRAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKALPAPDAS 2085
                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1645 geQLKQRQTSPKN-IQDTVFTIWQEVLKTSDIEWDDGFFDVGGDSLLAVTVADRIKHElSCEFSVTDLFEYSTIKNISQY 1723
Cdd:PRK12467  2086 --ELQQAYVAPQSeLEQRLAAIWQDVLGLEQVGLHDNFFELGGDSIISIQVVSRARQA-GIRFTPKDLFQHQTVQSLAAV 2162
                         1610
                   ....*....|....
gi 1776025254 1724 ITEQRMGNASDHMP 1737
Cdd:PRK12467  2163 AQEGDGTVSIDQGP 2176
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
3339-3881 0e+00

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 814.49  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3339 EPVAIVGISGRFPGAMDIDEFWKNLEEGKDSITEVPKDRWDWREHYGNPDTDVNKTDIKWGGFIDGVAEFDPLFFGISPR 3418
Cdd:COG3321      4 EPIAIIGMACRFPGADDPEEFWRNLRAGRDAITEVPADRWDADAYYDPDPDAPGKTYVRWGGFLDDVDEFDALFFGISPR 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3419 EADYVDPQQRLLMTYVWKALEDAGCPPQSLSGTGTGIFIGTGNTGYKDLFHRANLPIEGHAATGhMIPSVGPNRMSYFLN 3498
Cdd:COG3321     84 EAEAMDPQQRLLLEVAWEALEDAGYDPESLAGSRTGVFVGASSNDYALLLLADPEAIDAYALTG-NAKSVLAGRISYKLD 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3499 IHGPSEPVETACSSSLVAIHRAVTAMQNGDCEMAIAGGVNTILTEEAHISYSKAGMLSKDGRCKTFSADANGYVRGEGVG 3578
Cdd:COG3321    163 LRGPSVTVDTACSSSLVAVHLACQSLRSGECDLALAGGVNLMLTPESFILFSKGGMLSPDGRCRAFDADADGYVRGEGVG 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3579 MVMLKKLEDAERDGNHIYGVIRGTAENHGGRANTLTSPNPKAQADLLVRAYRQAGIDPSTVTYIEAHGTGTELGDPIEIN 3658
Cdd:COG3321    243 VVVLKRLSDALRDGDRIYAVIRGSAVNQDGRSNGLTAPNGPAQAAVIRRALADAGVDPATVDYVEAHGTGTPLGDPIEAA 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3659 GLKAAFKELsnmRGESQPdvpdhrCGIGSVKSNIGHLELAAGISGLIKVLLQMKHKTLVKSLHCETLNPYLQLTDSPFYI 3738
Cdd:COG3321    323 ALTAAFGQG---RPADQP------CAIGSVKSNIGHLEAAAGVAGLIKAVLALRHGVLPPTLHFETPNPHIDFENSPFYV 393
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3739 VQEKQEWKSvtdcdgNELPRRAGISSFGIGGVNAHIVIEEYMPKANSEHTATEQPNVIVLSAKNKSRLIDRASQLLEAIR 3818
Cdd:COG3321    394 NTELRPWPA------GGGPRRAGVSSFGFGGTNAHVVLEEAPAAAPAAAAAARPPQLLVLSAKTEEALRALAARLAAFLE 467
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1776025254 3819 NKkyTDQGLHRIAYTLQVGREEMDERLACVAGTMQELEEKLQAFVDGKEETDEFFRGQSHRNK 3881
Cdd:COG3321    468 AH--PDLDLADVAYTLATGRAHFEHRLAVVASSREELAAKLRALAAGEAAPGVVTGAAAAAPK 528
C_PKS-NRPS_PksJ-like cd20484
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
693-1121 0e+00

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs), similar to Bacillus subtilis PksJ; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily have the typical C-domain HHxxxD motif. PksJ is involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is important in secondary metabolism. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380472 [Multi-domain]  Cd Length: 430  Bit Score: 789.59  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  693 FQPLSEVQKGLWTLQKMSPEKSAYHVPLCFKFSSGLHLETLQQAFGLVLNQHPILKHVIQEKDGVPILKNEPALSIEIKT 772
Cdd:cd20484      1 RSPLSEGQKGLWMLQKMSPEMSAYNVPLCFRFSSKLDVEKFKQACQFVLEQHPILKSVIEEEDGVPFQKIEPSKPLSFQE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  773 ENISSMKESDIPAFLRKKVKEPYVKENSPLVRVMSFSRSEQEHFLLVVIHHLIFDGVSSVTFIHSLFDTYQLLLKGQQPE 852
Cdd:cd20484     81 EDISSLKESEIIAYLREKAKEPFVLENGPLMRVHLFSRSEQEHFVLITIHHIIFDGSSSLTLIHSLLDAYQALLQGKQPT 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  853 IAVSPAIYHDFAAWEKNMLAGKDGVKHRTYWQKQLSGTLPNLQLPKVSA-SSVSEFREDTYTRRLSSGFMNQVRMFAKEH 931
Cdd:cd20484    161 LASSPASYYDFVAWEQDMLAGAEGEEHRAYWKQQLSGTLPILELPADRPrSSAPSFEGQTYTRRLPSELSNQIKSFARSQ 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  932 SVNVTTVFLSCYMMLLGRYTGQKEQIVGMPAMVRPEERFDDAIGHFLNMLPIRSELNPADTFSSFISKLQLTILDGLDHA 1011
Cdd:cd20484    241 SINLSTVFLGIFKLLLHRYTGQEDIIVGMPTMGRPEERFDSLIGYFINMLPIRSRILGEETFSDFIRKLQLTVLDGLDHA 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1012 AYPFPKMVRDLNIPRSQAGSPVFQTAFFYQNFLQSGSYQSLLSRYADFFSVDYVEYIHQEGEYELVFELWETEEKMELNI 1091
Cdd:cd20484    321 AYPFPAMVRDLNIPRSQANSPVFQVAFFYQNFLQSTSLQQFLAEYQDVLSIEFVEGIHQEGEYELVLEVYEQEDRFTLNI 400
                          410       420       430
                   ....*....|....*....|....*....|
gi 1776025254 1092 KYNTGLFDAASISAMFDHFVYVTEQAMLNP 1121
Cdd:cd20484    401 KYNPDLFDASTIERMMEHYVKLAEELIANP 430
PKS cd00833
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ...
3339-3776 0e+00

polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different products, called polyketides, by successive decarboxylating Claisen condensations. PKSs can be divided into 2 groups, modular type I PKSs consisting of one or more large multifunctional proteins and iterative type II PKSs, complexes of several monofunctional subunits.


Pssm-ID: 238429 [Multi-domain]  Cd Length: 421  Bit Score: 663.87  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3339 EPVAIVGISGRFPGAMDIDEFWKNLEEGKDSITEVPKDRWDWREHYGNPDTDvNKTDIKWGGFIDGVAEFDPLFFGISPR 3418
Cdd:cd00833      1 EPIAIVGMACRFPGAADPDEFWENLLEGRDAISEIPEDRWDADGYYPDPGKP-GKTYTRRGGFLDDVDAFDAAFFGISPR 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3419 EADYVDPQQRLLMTYVWKALEDAGCPPQSLSGTGTGIFIGTGNTGYKDLFHRANLPIEGHAATGHMIpSVGPNRMSYFLN 3498
Cdd:cd00833     80 EAEAMDPQQRLLLEVAWEALEDAGYSPESLAGSRTGVFVGASSSDYLELLARDPDEIDAYAATGTSR-AFLANRISYFFD 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3499 IHGPSEPVETACSSSLVAIHRAVTAMQNGDCEMAIAGGVNTILTEEAHISYSKAGMLSKDGRCKTFSADANGYVRGEGVG 3578
Cdd:cd00833    159 LRGPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLSPDGRCRPFDADADGYVRGEGVG 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3579 MVMLKKLEDAERDGNHIYGVIRGTAENHGGRANTLTSPNPKAQADLLVRAYRQAGIDPSTVTYIEAHGTGTELGDPIEIN 3658
Cdd:cd00833    239 VVVLKRLSDALRDGDRIYAVIRGSAVNQDGRTKGITAPSGEAQAALIRRAYARAGVDPSDIDYVEAHGTGTPLGDPIEVE 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3659 GLKAAFkelsnmrgeSQPDVPDHRCGIGSVKSNIGHLELAAGISGLIKVLLQMKHKTLVKSLHCETLNPYLQLTDSPFYI 3738
Cdd:cd00833    319 ALAKVF---------GGSRSADQPLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKIDFEESPLRV 389
                          410       420       430
                   ....*....|....*....|....*....|....*...
gi 1776025254 3739 VQEKQEWKSvtdcdgNELPRRAGISSFGIGGVNAHIVI 3776
Cdd:cd00833    390 PTEARPWPA------PAGPRRAGVSSFGFGGTNAHVIL 421
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
1759-2291 0e+00

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 644.62  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1759 DDSVAIIGISCEFPGAKNHDEFWENLRDGKESIAFFNKEEL--QRFGISKEIAENADYVPAKASIEGKDRFDPSFFQISP 1836
Cdd:COG3321      3 DEPIAIIGMACRFPGADDPEEFWRNLRAGRDAITEVPADRWdaDAYYDPDPDAPGKTYVRWGGFLDDVDEFDALFFGISP 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1837 KDAEFMDPQLRMLLTHSWKAIEDAGYAAGQIP--QTSVFMSASNNSYRALLPSDttesLETPDGYVSWVLAQSgTIPTMI 1914
Cdd:COG3321     83 REAEAMDPQQRLLLEVAWEALEDAGYDPESLAgsRTGVFVGASSNDYALLLLAD----PEAIDAYALTGNAKS-VLAGRI 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1915 SHKLGLRGPSYFVHANCSSSLIGLHSAYKSLLSAESDYALVGGATLHTESNIGYVHQPGLNFSSDGHIKAFDASADGMIG 1994
Cdd:COG3321    158 SYKLDLRGPSVTVDTACSSSLVAVHLACQSLRSGECDLALAGGVNLMLTPESFILFSKGGMLSPDGRCRAFDADADGYVR 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1995 GEGVAVVLLKKAADAVKDGDHIYALLRGIGVNNDGADKvGFYAPSVKGQADVVQQVMNQTKIHPESICYVEAHGTGTKLG 2074
Cdd:COG3321    238 GEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRSN-GLTAPNGPAQAAVIRRALADAGVDPATVDYVEAHGTGTPLG 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2075 DPIELAALTNVYRQYTNKTQFCGIGSVKTNIGHLDTAAGLAGCIKVVMSLYHQELAPSINYKEPNPNTDLASSPFYVVDQ 2154
Cdd:COG3321    317 DPIEAAALTAAFGQGRPADQPCAIGSVKSNIGHLEAAAGVAGLIKAVLALRHGVLPPTLHFETPNPHIDFENSPFYVNTE 396
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2155 KKTLSREIQTHRAALSSFGLGGTNTHAIFEQF--KRDSDKGKIDGTCIVPISAKNKERLQEYAEDILAYLERRGLENsqL 2232
Cdd:COG3321    397 LRPWPAGGGPRRAGVSSFGFGGTNAHVVLEEApaAAPAAAAAARPPQLLVLSAKTEEALRALAARLAAFLEAHPDLD--L 474
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1776025254 2233 PDFAYTLQVGREAMEHRVVFIADHVNELKQRLTDFINGKTAiEGCFQGSKHNAREVSWL 2291
Cdd:COG3321    475 ADVAYTLATGRAHFEHRLAVVASSREELAAKLRALAAGEAA-PGVVTGAAAAAPKVAFL 532
PKS cd00833
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ...
1760-2182 1.36e-171

polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different products, called polyketides, by successive decarboxylating Claisen condensations. PKSs can be divided into 2 groups, modular type I PKSs consisting of one or more large multifunctional proteins and iterative type II PKSs, complexes of several monofunctional subunits.


Pssm-ID: 238429 [Multi-domain]  Cd Length: 421  Bit Score: 535.99  E-value: 1.36e-171
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1760 DSVAIIGISCEFPGAKNHDEFWENLRDGKESIAFFNKEELQRFGI-SKEIAENADYVPAKASIEGKDRFDPSFFQISPKD 1838
Cdd:cd00833      1 EPIAIVGMACRFPGAADPDEFWENLLEGRDAISEIPEDRWDADGYyPDPGKPGKTYTRRGGFLDDVDAFDAAFFGISPRE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1839 AEFMDPQLRMLLTHSWKAIEDAGYAAGQIP--QTSVFMSASNNSYRALLPSDttesLETPDGYVSWVLAQSgTIPTMISH 1916
Cdd:cd00833     81 AEAMDPQQRLLLEVAWEALEDAGYSPESLAgsRTGVFVGASSSDYLELLARD----PDEIDAYAATGTSRA-FLANRISY 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1917 KLGLRGPSYFVHANCSSSLIGLHSAYKSLLSAESDYALVGGATLHTESNIGYVHQPGLNFSSDGHIKAFDASADGMIGGE 1996
Cdd:cd00833    156 FFDLRGPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLSPDGRCRPFDADADGYVRGE 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1997 GVAVVLLKKAADAVKDGDHIYALLRGIGVNNDGADKVGfYAPSVKGQADVVQQVMNQTKIHPESICYVEAHGTGTKLGDP 2076
Cdd:cd00833    236 GVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRTKGI-TAPSGEAQAALIRRAYARAGVDPSDIDYVEAHGTGTPLGDP 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2077 IELAALTNVYRQYTNKTQFCGIGSVKTNIGHLDTAAGLAGCIKVVMSLYHQELAPSINYKEPNPNTDLASSPFYVVDQKK 2156
Cdd:cd00833    315 IEVEALAKVFGGSRSADQPLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKIDFEESPLRVPTEAR 394
                          410       420
                   ....*....|....*....|....*.
gi 1776025254 2157 TLSREIQTHRAALSSFGLGGTNTHAI 2182
Cdd:cd00833    395 PWPAPAGPRRAGVSSFGFGGTNAHVI 420
PKS_KS smart00825
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ...
3341-3778 4.30e-157

Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the thiolase family and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.


Pssm-ID: 214836 [Multi-domain]  Cd Length: 298  Bit Score: 488.76  E-value: 4.30e-157
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  3341 VAIVGISGRFPGAMDIDEFWKNLEEGkdsitevpkdrwdwrehygnpdtdvnktdikwggfIDGVAEFDPLFFGISPREA 3420
Cdd:smart00825    1 IAIVGMSCRFPGADDPEEFWDLLLAG-----------------------------------LDDVDLFDAAFFGISPREA 45
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  3421 DYVDPQQRLLMTYVWKALEDAGCPPQSLSGTGTGIFIGTGNTGYkdlfhranlpieghaatghmipsvgpnrmsyflnih 3500
Cdd:smart00825   46 EAMDPQQRLLLEVAWEALEDAGIDPESLRGSRTGVFVGVSSSDY------------------------------------ 89
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  3501 gpSEPVETACSSSLVAIHRAVTAMQNGDCEMAIAGGVNTILTEEAHISYSKAGMLSKDGRCKTFSADANGYVRGEGVGMV 3580
Cdd:smart00825   90 --SVTVDTACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLSPDGRCKTFDASADGYVRGEGVGVV 167
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  3581 MLKKLEDAERDGNHIYGVIRGTAENHGGRANTLTSPNPKAQadllvrayrqagidpstvtyieahgtgtelgdpieingl 3660
Cdd:smart00825  168 VLKRLSDALRDGDPILAVIRGSAVNQDGRSNGITAPSGPAQ--------------------------------------- 208
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  3661 kaafkelsnmrgesqpdvpdhrCGIGSVKSNIGHLELAAGISGLIKVLLQMKHKTLVKSLHCETLNPYLQLTDSPFYIVQ 3740
Cdd:smart00825  209 ----------------------LLIGSVKSNIGHLEAAAGVAGLIKVVLALKHGVIPPTLHFETPNPHIDLEESPLRVPT 266
                           410       420       430
                    ....*....|....*....|....*....|....*...
gi 1776025254  3741 EKQEWksvtdcDGNELPRRAGISSFGIGGVNAHIVIEE 3778
Cdd:smart00825  267 ELTPW------PPPGRPRRAGVSSFGFGGTNAHVILEE 298
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
690-1140 8.04e-157

Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.


Pssm-ID: 395541 [Multi-domain]  Cd Length: 454  Bit Score: 494.93  E-value: 8.04e-157
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  690 QATFQPLSEVQKGLWTLQKMSPEKSAYHVPLCFKFSSGLHLETLQQAFGLVLNQHPILKHVIQEK-DGVPILKNEPALSI 768
Cdd:pfam00668    1 VQDEYPLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRQeNGEPVQVILEERPF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  769 EIKTENIS----SMKESDIPAFLRKKVKEPYVKENSPLVRVMSFSRSEQEHFLLVVIHHLIFDGVSSVTFIHSLFDTYQL 844
Cdd:pfam00668   81 ELEIIDISdlseSEEEEAIEAFIQRDLQSPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQQ 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  845 LLKGQQPEIAVSPAiYHDFAAWEKNMLAGKDGVKHRTYWQKQLSGTLPNLQLPKVSASS-VSEFREDTYTRRLSSGFMNQ 923
Cdd:pfam00668  161 LLKGEPLPLPPKTP-YKDYAEWLQQYLQSEDYQKDAAYWLEQLEGELPVLQLPKDYARPaDRSFKGDRLSFTLDEDTEEL 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  924 VRMFAKEHSVNVTTVFLSCYMMLLGRYTGQKEQIVGMPAMVRPEERFDDAIGHFLNMLPIRSELNPADTFSSFISKLQLT 1003
Cdd:pfam00668  240 LRKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSPDIERMVGMFVNTLPLRIDPKGGKTFSELIKRVQED 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1004 ILDGLDHAAYPFPKMVRDLNIPRSQAGSPVFQTAFFYQNFLQSGSYQSLLSRYADFFSVDYVeyIHQEGEYELVFELWET 1083
Cdd:pfam00668  320 LLSAEPHQGYPFGDLVNDLRLPRDLSRHPLFDPMFSFQNYLGQDSQEEEFQLSELDLSVSSV--IEEEAKYDLSLTASER 397
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1776025254 1084 EEKMELNIKYNTGLFDAASISAMFDHFVYVTEQAMLNPSQPLKEYSLLPEAEKQMIL 1140
Cdd:pfam00668  398 GGGLTIKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLSDAEKQKLL 454
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
1180-1577 3.66e-153

amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.


Pssm-ID: 273779 [Multi-domain]  Cd Length: 409  Bit Score: 482.54  E-value: 3.66e-153
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1180 TYRELDERSTQLAIYLQA-HGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLEDSEVFITLTTS 1258
Cdd:TIGR01733    1 TYRELDERANRLARHLRAaGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1259 ELVNTLSWNGVTTALLDQDWDEIAQTASDRKVLTRTVTPENLAYVIYTSGSTGKPKGVMIPHKALTNFLVSMGETPGLTA 1338
Cdd:TIGR01733   81 ALASRLAGLVLPVILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDP 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1339 EDKMLAVTTYCFDIAALELFLPLIKGAHCYICQTEHTKDVEKLKRD-IRTIKPTVMQATPATWKMLFYSGWENEENVKIL 1417
Cdd:TIGR01733  161 DDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLAAlIAEHPVTVLNLTPSLLALLAAALPPALASLRLV 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1418 C-GGEALPETLKRYFLDTGSEA--WNMFGPTETTIWSAVQRI----NDECSRATIGRPIANTQIYITDSQLAPVPAGVPG 1490
Cdd:TIGR01733  241 IlGGEALTPALVDRWRARGPGArlINLYGPTETTVWSTATLVdpddAPRESPVPIGRPLANTRLYVLDDDLRPVPVGVVG 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1491 ELCIAGDGVAKGYYKKEELTDSRFIDNPF--EPGSKLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSE 1568
Cdd:TIGR01733  321 ELYIGGPGVARGYLNRPELTAERFVPDPFagGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLR 400

                   ....*....
gi 1776025254 1569 HPGILECVV 1577
Cdd:TIGR01733  401 HPGVREAVV 409
PKS cd00833
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ...
4588-4989 4.14e-135

polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different products, called polyketides, by successive decarboxylating Claisen condensations. PKSs can be divided into 2 groups, modular type I PKSs consisting of one or more large multifunctional proteins and iterative type II PKSs, complexes of several monofunctional subunits.


Pssm-ID: 238429 [Multi-domain]  Cd Length: 421  Bit Score: 431.21  E-value: 4.14e-135
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4588 EGIAVVGLSCRFPGAETLESYWSLLSEGRSSIGPIPAERWGCKTPY------------YAGVIDGVSYFDPDFFLLHEED 4655
Cdd:cd00833      1 EPIAIVGMACRFPGAADPDEFWENLLEGRDAISEIPEDRWDADGYYpdpgkpgktytrRGGFLDDVDAFDAAFFGISPRE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4656 VRAMDPQALLVLEECLKLLYHAGYTPEEIKGKPVGVYIGGRS---QHKPDEDSLDHAKNPIVTVGQNYLAANLSQFFDVR 4732
Cdd:cd00833     81 AEAMDPQQRLLLEVAWEALEDAGYSPESLAGSRTGVFVGASSsdyLELLARDPDEIDAYAATGTSRAFLANRISYFFDLR 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4733 GPSVVVDTACSSALVGMNMAIQALRGGDIQSAIVGGVSLLSSDASHRLFDRRGILSKHSSFHVFDERADGVVLGEGVGMV 4812
Cdd:cd00833    161 GPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLSPDGRCRPFDADADGYVRGEGVGVV 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4813 MLKTVKQALEDGDTIYAVVKAASVNNDGRTAGPATPNLEAQKEVMKDALFKSGKKPEDISYLEANGSGSIVTDLLELKAI 4892
Cdd:cd00833    241 VLKRLSDALRDGDRIYAVIRGSAVNQDGRTKGITAPSGEAQAALIRRAYARAGVDPSDIDYVEAHGTGTPLGDPIEVEAL 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4893 QSVYRSGHS--SPLSLGSIKPNIGHPLCAEGIASFIKVVLMLKERRFVPFLSGEKEMAHFDQQKANITFSRALEKW-TDS 4969
Cdd:cd00833    321 AKVFGGSRSadQPLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKIDFEESPLRVPTEARPWpAPA 400
                          410       420
                   ....*....|....*....|.
gi 1776025254 4970 QP-TAAINCFADGGTNVHVIV 4989
Cdd:cd00833    401 GPrRAGVSSFGFGGTNAHVIL 421
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
2672-3082 9.55e-130

ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes both KR domains of the Bacillus subtilis Pks J,-L, and PksM, and all three KR domains of PksN, components of the megacomplex bacillaene synthase, which synthesizes the antibiotic bacillaene. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187656 [Multi-domain]  Cd Length: 436  Bit Score: 416.38  E-value: 9.55e-130
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2672 LEPVWEKQNEEREDEDLSYTEHIIVLFETERSVTDSIASHMKDARvitlneavghiaeryQCYMQNIFELLQ-SKVRELS 2750
Cdd:cd08953     36 LQPVWAPAALASAFLALAYEAALLGLAAAEAALLDALSALDPAAA---------------LQLLESLQRLLKaGLLAARA 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2751 AGRIIIQAIVPLEKEKQL------FAGVSGLLKTAEIEFSKLTAQVIEIEKPEEMID-LHLKLKDDSQRPFDKQIRYEAG 2823
Cdd:cd08953    101 SGRALLQVVTGLPGALGLdaldpaGAGLAGLLRTLAQEYPGLTCRLIDLDAGEASAEaLARELAAELAAPGAAEVRYRDG 180
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2824 HRFVKGWREMVLPSADTLHMPWRDEGVYLITGGAGSLGLLFAKEIANRTGRsTIVLTGRSVLSEDKENE---LEALRSIG 2900
Cdd:cd08953    181 LRYVQTLEPLPLPAGAAASAPLKPGGVYLVTGGAGGIGRALARALARRYGA-RLVLLGRSPLPPEEEWKaqtLAALEALG 259
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2901 AEVVYREADVSDQHAVHHLFEEIKERYGTLNGIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSGLLHVDECSKDFPLDFFI 2980
Cdd:cd08953    260 ARVLYISADVTDAAAVRRLLEKVRERYGAIDGVIHAAGVLRDALLAQKTAEDFEAVLAPKVDGLLNLAQALADEPLDFFV 339
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2981 FFSSVSGCLGNAGQADYAAANSFMDAFAEYRRSLAAskkrFGSTISFNWPLWEEGGMQVGAEDEkRMLKTTGMVPMPTDS 3060
Cdd:cd08953    340 LFSSVSAFFGGAGQADYAAANAFLDAFAAYLRQRGP----QGRVLSINWPAWREGGMAADLGAR-ELLARAGLLPIEPEE 414
                          410       420
                   ....*....|....*....|..
gi 1776025254 3061 GLKAFYQGIASDKPQVFVMEGQ 3082
Cdd:cd08953    415 GLQALEQALSSDLPQVLVSPGD 436
PKS_KS smart00825
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ...
1762-2185 1.13e-120

Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the thiolase family and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.


Pssm-ID: 214836 [Multi-domain]  Cd Length: 298  Bit Score: 384.37  E-value: 1.13e-120
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  1762 VAIIGISCEFPGAKNHDEFWENLRDGkesiaffnkeelqrfgiskeiaenadyvpakasIEGKDRFDPSFFQISPKDAEF 1841
Cdd:smart00825    1 IAIVGMSCRFPGADDPEEFWDLLLAG---------------------------------LDDVDLFDAAFFGISPREAEA 47
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  1842 MDPQLRMLLTHSWKAIEDAGYAAGQIP--QTSVFMSASNNSYrallpsdttesletpdgyvswvlaqsgtiptmishklg 1919
Cdd:smart00825   48 MDPQQRLLLEVAWEALEDAGIDPESLRgsRTGVFVGVSSSDY-------------------------------------- 89
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  1920 lrgpSYFVHANCSSSLIGLHSAYKSLLSAESDYALVGGATLHTESNIGYVHQPGLNFSSDGHIKAFDASADGMIGGEGVA 1999
Cdd:smart00825   90 ----SVTVDTACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLSPDGRCKTFDASADGYVRGEGVG 165
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  2000 VVLLKKAADAVKDGDHIYALLRGIGVNNDGADKvGFYAPSVKGQadvvqqvmnqtkihpesicyveahgtgtklgdpiel 2079
Cdd:smart00825  166 VVVLKRLSDALRDGDPILAVIRGSAVNQDGRSN-GITAPSGPAQ------------------------------------ 208
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  2080 aaltnvyrqytnktqfCGIGSVKTNIGHLDTAAGLAGCIKVVMSLYHQELAPSINYKEPNPNTDLASSPFYVVDQKKTLS 2159
Cdd:smart00825  209 ----------------LLIGSVKSNIGHLEAAAGVAGLIKVVLALKHGVIPPTLHFETPNPHIDLEESPLRVPTELTPWP 272
                           410       420
                    ....*....|....*....|....*.
gi 1776025254  2160 REIQTHRAALSSFGLGGTNTHAIFEQ 2185
Cdd:smart00825  273 PPGRPRRAGVSSFGFGGTNAHVILEE 298
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
4587-5010 1.38e-118

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 413.50  E-value: 1.38e-118
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4587 AEGIAVVGLSCRFPGAETLESYWSLLSEGRSSIGPIPAERWGCKTPY-------------YAGVIDGVSYFDPDFFLLHE 4653
Cdd:COG3321      3 DEPIAIIGMACRFPGADDPEEFWRNLRAGRDAITEVPADRWDADAYYdpdpdapgktyvrWGGFLDDVDEFDALFFGISP 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4654 EDVRAMDPQALLVLEECLKLLYHAGYTPEEIKGKPVGVYIGG-------RSQHKPDEDSLDHAknpiVTVGQNYLAANLS 4726
Cdd:COG3321     83 REAEAMDPQQRLLLEVAWEALEDAGYDPESLAGSRTGVFVGAssndyalLLLADPEAIDAYAL----TGNAKSVLAGRIS 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4727 QFFDVRGPSVVVDTACSSALVGMNMAIQALRGGDIQSAIVGGVSLLSSDASHRLFDRRGILSKHSSFHVFDERADGVVLG 4806
Cdd:COG3321    159 YKLDLRGPSVTVDTACSSSLVAVHLACQSLRSGECDLALAGGVNLMLTPESFILFSKGGMLSPDGRCRAFDADADGYVRG 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4807 EGVGMVMLKTVKQALEDGDTIYAVVKAASVNNDGRTAGPATPNLEAQKEVMKDALFKSGKKPEDISYLEANGSGSIVTDL 4886
Cdd:COG3321    239 EGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRSNGLTAPNGPAQAAVIRRALADAGVDPATVDYVEAHGTGTPLGDP 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4887 LELKAIQSVYRSGHS--SPLSLGSIKPNIGHPLCAEGIASFIKVVLMLKERRFVPFLsgekemaHFDQQKANITFS---- 4960
Cdd:COG3321    319 IEAAALTAAFGQGRPadQPCAIGSVKSNIGHLEAAAGVAGLIKAVLALRHGVLPPTL-------HFETPNPHIDFEnspf 391
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1776025254 4961 ---RALEKW-TDSQP-TAAINCFADGGTNVHVIVEAWEKDEKHAikRSPKSPPQL 5010
Cdd:COG3321    392 yvnTELRPWpAGGGPrRAGVSSFGFGGTNAHVVLEEAPAAAPAA--AAAARPPQL 444
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
4029-4401 1.70e-109

ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes both KR domains of the Bacillus subtilis Pks J,-L, and PksM, and all three KR domains of PksN, components of the megacomplex bacillaene synthase, which synthesizes the antibiotic bacillaene. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187656 [Multi-domain]  Cd Length: 436  Bit Score: 358.22  E-value: 1.70e-109
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4029 DWKEFDGLVDVIGCGWDDeGRLDWIEWVQRLVEF----GHKEGLRLLCVTKGLESFQNTS-VRMAGASRAGLYRMLQCEY 4103
Cdd:cd08953     61 LAAAEAALLDALSALDPA-AALQLLESLQRLLKAgllaARASGRALLQVVTGLPGALGLDaLDPAGAGLAGLLRTLAQEY 139
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4104 SHLISRHMDAEEVTDHP-RLAKLIADEfYSESYDAEVCYRDGLRYQSFLKAHPETGKATeQSAVFPKDHVLLITGGTRGI 4182
Cdd:cd08953    140 PGLTCRLIDLDAGEASAeALARELAAE-LAAPGAAEVRYRDGLRYVQTLEPLPLPAGAA-ASAPLKPGGVYLVTGGAGGI 217
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4183 GLLCARHFAECYGvKKLVLTGREQLPPREEWARfktsntslaekiQAVRELEAKGVQVEMLSLTLSDDAQVEQTLQHIKR 4262
Cdd:cd08953    218 GRALARALARRYG-ARLVLLGRSPLPPEEEWKA------------QTLAALEALGARVLYISADVTDAAAVRRLLEKVRE 284
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4263 TLGPIGGVIHCAGLTDMDTLafIRKTSDDIQRVMEPKVSGLTTLYRHVCNEPLQFFVLFSSVSAIIPelSAGQADYAMAN 4342
Cdd:cd08953    285 RYGAIDGVIHAAGVLRDALL--AQKTAEDFEAVLAPKVDGLLNLAQALADEPLDFFVLFSSVSAFFG--GAGQADYAAAN 360
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1776025254 4343 SYMDYFAEAHQK---HVPIISVQWPNWKETGMGEV--TNQAYRESGLFSITNSEGLRFLDQIVS 4401
Cdd:cd08953    361 AFLDAFAAYLRQrgpQGRVLSINWPAWREGGMAADlgARELLARAGLLPIEPEEGLQALEQALS 424
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
3339-3588 2.31e-108

Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains. The N-terminal domain contains most of the structures involved in dimer formation and also the active site cysteine.


Pssm-ID: 425468 [Multi-domain]  Cd Length: 251  Bit Score: 346.93  E-value: 2.31e-108
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3339 EPVAIVGISGRFPGAMDIDEFWKNLEEGKDSITEVPKDRWDWREHYGNPDTDVNKTDIKWGGfIDGVAEFDPLFFGISPR 3418
Cdd:pfam00109    1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIPADRWDPDKLYDPPSRIAGKIYTKWGG-LDDIFDFDPLFFGISPR 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3419 EADYVDPQQRLLMTYVWKALEDAGCPPQSLSGTGTGIFIGTGNTGYKDL--FHRANLPIEGHAATGHMIPSVGPNRMSYF 3496
Cdd:pfam00109   80 EAERMDPQQRLLLEAAWEALEDAGITPDSLDGSRTGVFIGSGIGDYAALllLDEDGGPRRGSPFAVGTMPSVIAGRISYF 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3497 LNIHGPSEPVETACSSSLVAIHRAVTAMQNGDCEMAIAGGVNTILTEEAHISYSKAGMLSKDGRCKTFSADANGYVRGEG 3576
Cdd:pfam00109  160 LGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSPDGPCKAFDPFADGFVRGEG 239
                          250
                   ....*....|..
gi 1776025254 3577 VGMVMLKKLEDA 3588
Cdd:pfam00109  240 VGAVVLKRLSDA 251
PKS_KS smart00825
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ...
4590-4991 5.41e-104

Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the thiolase family and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.


Pssm-ID: 214836 [Multi-domain]  Cd Length: 298  Bit Score: 336.61  E-value: 5.41e-104
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  4590 IAVVGLSCRFPGAETLESYWSLLSEGrssigpipaerwgcktpyyagvIDGVSYFDPDFFLLHEEDVRAMDPQALLVLEE 4669
Cdd:smart00825    1 IAIVGMSCRFPGADDPEEFWDLLLAG----------------------LDDVDLFDAAFFGISPREAEAMDPQQRLLLEV 58
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  4670 CLKLLYHAGYTPEEIKGKPVGVYIGGRSQHkpdedsldhaknpivtvgqnYlaanlsqffdvrgpSVVVDTACSSALVGM 4749
Cdd:smart00825   59 AWEALEDAGIDPESLRGSRTGVFVGVSSSD--------------------Y--------------SVTVDTACSSSLVAL 104
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  4750 NMAIQALRGGDIQSAIVGGVSLLSSDASHRLFDRRGILSKHSSFHVFDERADGVVLGEGVGMVMLKTVKQALEDGDTIYA 4829
Cdd:smart00825  105 HLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLSPDGRCKTFDASADGYVRGEGVGVVVLKRLSDALRDGDPILA 184
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  4830 VVKAASVNNDGRTAGPATPNLEAQkevmkdalfksgkkpedisyleangsgsivtdllelkaiqsvyrsghsspLSLGSI 4909
Cdd:smart00825  185 VIRGSAVNQDGRSNGITAPSGPAQ--------------------------------------------------LLIGSV 214
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  4910 KPNIGHPLCAEGIASFIKVVLMLKERRFVPFLSGEKEMAHFDQQKANITFSRALEKW--TDSQPTAAINCFADGGTNVHV 4987
Cdd:smart00825  215 KSNIGHLEAAAGVAGLIKVVLALKHGVIPPTLHFETPNPHIDLEESPLRVPTELTPWppPGRPRRAGVSSFGFGGTNAHV 294

                    ....
gi 1776025254  4988 IVEA 4991
Cdd:smart00825  295 ILEE 298
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
31-564 4.87e-91

O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440087 [Multi-domain]  Cd Length: 452  Bit Score: 305.58  E-value: 4.87e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254   31 IPEVLYRTAAELGDTKGIIYlqpDGTEVyqSYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNSQLLPAFWGCVLTGVV 110
Cdd:COG0318      1 LADLLRRAAARHPDRPALVF---GGRRL--TYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAV 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  111 PAPlaVPPTYAEsssgtQKLKDAWTLLDKPAVITdrgmhqemldwakeqglegfraiivedllsaeadtdwhqsspedlA 190
Cdd:COG0318     76 VVP--LNPRLTA-----EELAYILEDSGARALVT---------------------------------------------A 103
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  191 LLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDHVGGIGMLHLRDVYLGCQeinvsseTILME-- 268
Cdd:COG0318    104 LILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGAT-------LVLLPrf 176
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  269 -PLKWLDWIDHYRASV-TWAPNFAFGLvtdfAEEIKDRKWDLSSMRYMLNGGEAMVAKVGRRILELLEPhglpadAIRPA 346
Cdd:COG0318    177 dPERVLELIERERVTVlFGVPTMLARL----LRHPEFARYDLSSLRLVVSGGAPLPPELLERFEERFGV------RIVEG 246
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  347 WGMSETSSGVIFsheftRAGTSDDDHFVEIGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGYYQRPDLNESVFt 426
Cdd:COG0318    247 YGLTETSPVVTV-----NPEDPGERRPGSVGRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAF- 320
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  427 EDGWFETGDLGFLR-NGRLTITGRTKDAIIINGINYYSHAIESAVEELSEIetsytAACAV------RLGQnstdQLAIF 499
Cdd:COG0318    321 RDGWLRTGDLGRLDeDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGV-----AEAAVvgvpdeKWGE----RVVAF 391
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1776025254  500 FVTS--AKLNDEQMSQLLRniqSHVSQvIGVtPEYLLPVqkEEIPKTAIGKIQRTQLKTSFENGEFD 564
Cdd:COG0318    392 VVLRpgAELDAEELRAFLR---ERLAR-YKV-PRRVEFV--DELPRTASGKIDRRALRERYAAGALE 451
omega_3_PfaA TIGR02813
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ...
3340-3881 3.42e-85

polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this alignment are involved in omega-3 polyunsaturated fatty acid biosynthesis, such as the protein PfaA from the eicosapentaenoic acid biosynthesis operon in Photobacterium profundum strain SS9. PfaA is encoded together with PfaB, PfaC, and PfaD, and the functions of the individual polypeptides have not yet been described. More distant homologs of PfaA, also included with the reach of this model, appear to be involved in polyketide-like biosynthetic mechanisms of polyunsaturated fatty acid biosynthesis, an alternative to the more familiar iterated mechanism of chain extension and desaturation, and in most cases are encoded near genes for homologs of PfaB, PfaC, and/or PfaD.


Pssm-ID: 274311 [Multi-domain]  Cd Length: 2582  Bit Score: 315.02  E-value: 3.42e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3340 PVAIVGISGRFPGAMDIDEFWKNLEEGKDSITEVPKDRWDWREHYGNPDTDVNKTDIKWGGFIDGVaEFDPLFFGISPRE 3419
Cdd:TIGR02813    8 PIAIVGMASIFANSRYLNKFWDLIFEKIDAITDVPSDHWAKDDYYDSDKSEADKSYCKRGGFLPEV-DFNPMEFGLPPNI 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3420 ADYVDPQQRLLMTYVWKALEDAGCPpQSLSGTGTGIFIGTG-----------------------NTGYKDL--------F 3468
Cdd:TIGR02813   87 LELTDISQLLSLVVAKEVLNDAGLP-DGYDRDKIGITLGVGggqkqssslnarlqypvlkkvfkASGVEDEdsemlikkF 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3469 HRANLPIEGHAATGhMIPSVGPNRMSYFLNIHGPSEPVETACSSSLVAIHRAVTAMQNGDCEMAIAGGVNTILTEEAHIS 3548
Cdd:TIGR02813  166 QDQYIHWEENSFPG-SLGNVISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGGVCTDNSPFMYMS 244
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3549 YSKAGMLSKDGRCKTFSADANGYVRGEGVGMVMLKKLEDAERDGNHIYGVIRGTAENHGGRANTLTSPNPKAQADLLVRA 3628
Cdd:TIGR02813  245 FSKTPAFTTNEDIQPFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGKFKSIYAPRPEGQAKALKRA 324
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3629 YRQAGIDPSTVTYIEAHGTGTELGDPIEINGLKAAFkelsnmrgeSQPDVPDHRCGIGSVKSNIGHLELAAGISGLIKVL 3708
Cdd:TIGR02813  325 YDDAGFAPHTCGLIEAHGTGTAAGDVAEFGGLVSVF---------SQDNDQKQHIALGSVKSQIGHTKSTAGTAGMIKAV 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3709 LQMKHKTLVKSLHCETLNPYLQLTDSPFYIVQEKQEWKSVTDcdgnELPRRAGISSFGIGGVNAHIVIEEYMPKA--NSE 3786
Cdd:TIGR02813  396 LALHHKVLPPTINVDQPNPKLDIENSPFYLNTETRPWMQRED----GTPRRAGISSFGFGGTNFHMVLEEYSPKHqrDDQ 471
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3787 HTATEQPNVIVLSAKNKSRLIDRASQLLEAIrNKKYTDQGLHRIAYTLQVGREEMD---ERLACVAGTMQELEEKL-QAF 3862
Cdd:TIGR02813  472 YRQRAVAQTLLFTAANEKALVSSLKDWKNKL-SAKADDQPYAFNALAVENTLRTIAvalARLGFVAKNADELITMLeQAI 550
                          570       580
                   ....*....|....*....|..
gi 1776025254 3863 VDGKEETDEFFR---GQSHRNK 3881
Cdd:TIGR02813  551 TQLEAKSCEEWQlpsGISYRKS 572
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
4588-4820 7.44e-79

Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains. The N-terminal domain contains most of the structures involved in dimer formation and also the active site cysteine.


Pssm-ID: 425468 [Multi-domain]  Cd Length: 251  Bit Score: 262.57  E-value: 7.44e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4588 EGIAVVGLSCRFPGAETLESYWSLLSEGRSSIGPIPAERWGCKTPYY------------AGVIDGVSYFDPDFFLLHEED 4655
Cdd:pfam00109    1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIPADRWDPDKLYDppsriagkiytkWGGLDDIFDFDPLFFGISPRE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4656 VRAMDPQALLVLEECLKLLYHAGYTPEEIKGKPVGVYIGGRSQHKPDEDSLDHAKNP------IVTVGQNYLAANLSQFF 4729
Cdd:pfam00109   81 AERMDPQQRLLLEAAWEALEDAGITPDSLDGSRTGVFIGSGIGDYAALLLLDEDGGPrrgspfAVGTMPSVIAGRISYFL 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4730 DVRGPSVVVDTACSSALVGMNMAIQALRGGDIQSAIVGGVSLLSSDASHRLFDRRGILSKHSSFHVFDERADGVVLGEGV 4809
Cdd:pfam00109  161 GLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSPDGPCKAFDPFADGFVRGEGV 240
                          250
                   ....*....|.
gi 1776025254 4810 GMVMLKTVKQA 4820
Cdd:pfam00109  241 GAVVLKRLSDA 251
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
1760-2009 5.80e-77

Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains. The N-terminal domain contains most of the structures involved in dimer formation and also the active site cysteine.


Pssm-ID: 425468 [Multi-domain]  Cd Length: 251  Bit Score: 256.79  E-value: 5.80e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1760 DSVAIIGISCEFPGAKNHDEFWENLRDGKESIAFFNKE--ELQRFGISKEIAENADYVPAKAsIEGKDRFDPSFFQISPK 1837
Cdd:pfam00109    1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIPADrwDPDKLYDPPSRIAGKIYTKWGG-LDDIFDFDPLFFGISPR 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1838 DAEFMDPQLRMLLTHSWKAIEDAGYAAGQI--PQTSVFMSASNNSYRALLPSDTTESLEtpDGYVSWVLAQSGTIPTMIS 1915
Cdd:pfam00109   80 EAERMDPQQRLLLEAAWEALEDAGITPDSLdgSRTGVFIGSGIGDYAALLLLDEDGGPR--RGSPFAVGTMPSVIAGRIS 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1916 HKLGLRGPSYFVHANCSSSLIGLHSAYKSLLSAESDYALVGGATLHTESNIGYVHQPGLNFSSDGHIKAFDASADGMIGG 1995
Cdd:pfam00109  158 YFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSPDGPCKAFDPFADGFVRG 237
                          250
                   ....*....|....
gi 1776025254 1996 EGVAVVLLKKAADA 2009
Cdd:pfam00109  238 EGVGAVVLKRLSDA 251
PRK07768 PRK07768
long-chain-fatty-acid--CoA ligase; Validated
33-553 1.22e-73

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236091 [Multi-domain]  Cd Length: 545  Bit Score: 258.39  E-value: 1.22e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254   33 EVLYRTAAelGDTKGIIYLQPDGtEVYQSYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNSQLLPAFWGCVLTGVV-- 110
Cdd:PRK07768     6 EKMYANAR--TSPRGMVTGEPDA-PVRHTWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASlt 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  111 ----PAPLAVPPTYAESSsgtqklKDAWTLLDKPAVITDrgmhqEMLDWAKEQgLE--GFRAIIVEDLLSAEAdTDWHQS 184
Cdd:PRK07768    83 mlhqPTPRTDLAVWAEDT------LRVIGMIGAKAVVVG-----EPFLAAAPV-LEekGIRVLTVADLLAADP-IDPVET 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  185 SPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTRE-DITFNWMPFDH-VGGIGMLHLrDVYLGCQEINVSS 262
Cdd:PRK07768   150 GEDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVEtDVMVSWLPLFHdMGMVGFLTV-PMYFGAELVKVTP 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  263 ETILMEPLKWLDWIDHYRASVTWAPNFAFGLVTD-FAEEIKDRKWDLSSMRYMLNGGEAMVAKVGRRILELLEPHGLPAD 341
Cdd:PRK07768   229 MDFLRDPLLWAELISKYRGTMTAAPNFAYALLARrLRRQAKPGAFDLSSLRFALNGAEPIDPADVEDLLDAGARFGLRPE 308
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  342 AIRPAWGMSETSSGVIFSHEFT----------------RAGTSDDDH---FVEIGSPIPGFSMRIVNDHNELVEEGEIGR 402
Cdd:PRK07768   309 AILPAYGMAEATLAVSFSPCGAglvvdevdadllaalrRAVPATKGNtrrLATLGPPLPGLEVRVVDEDGQVLPPRGVGV 388
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  403 FQVSGLSVTSGYYQrPDLNESVFTEDGWFETGDLGFL-RNGRLTITGRTKDAIIINGINYYSHAIESAVEELSEIETSyt 481
Cdd:PRK07768   389 IELRGESVTPGYLT-MDGFIPAQDADGWLDTGDLGYLtEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVRPG-- 465
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1776025254  482 AACAVRL-GQNSTDQLAIFFVTSAKLNDEQMSQLLRNIQSHVSQVIGVTPEYLLPVQKEEIPKTAIGKIQRTQ 553
Cdd:PRK07768   466 NAVAVRLdAGHSREGFAVAVESNAFEDPAEVRRIRHQVAHEVVAEVGVRPRNVVVLGPGSIPKTPSGKLRRAN 538
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
2849-3034 6.18e-70

KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.


Pssm-ID: 430138 [Multi-domain]  Cd Length: 180  Bit Score: 233.99  E-value: 6.18e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2849 GVYLITGGAGSLGLLFAKEIANRtGRSTIVLTGRSVLS-EDKENELEALRSIGAEVVYREADVSDQHAVHHLFEEIKERY 2927
Cdd:pfam08659    1 GTYLITGGLGGLGRELARWLAER-GARHLVLLSRSAAPrPDAQALIAELEARGVEVVVVACDVSDPDAVAALLAEIKAEG 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2928 GTLNGIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSGLLHVDECSKDFPLDFFIFFSSVSGCLGNAGQADYAAANSFMDAF 3007
Cdd:pfam08659   80 PPIRGVIHAAGVLRDALLENMTDEDWRRVLAPKVTGTWNLHEATPDEPLDFFVLFSSIAGLLGSPGQANYAAANAFLDAL 159
                          170       180
                   ....*....|....*....|....*..
gi 1776025254 3008 AEYRRSLAAskkrfgSTISFNWPLWEE 3034
Cdd:pfam08659  160 AEYRRSQGL------PATSINWGPWAE 180
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
2849-3034 5.13e-69

This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.


Pssm-ID: 214833 [Multi-domain]  Cd Length: 180  Bit Score: 231.22  E-value: 5.13e-69
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  2849 GVYLITGGAGSLGLLFAKEIANRTGRsTIVLTGRSVLSEDKENEL-EALRSIGAEVVYREADVSDQHAVHHLFEEIKERY 2927
Cdd:smart00822    1 GTYLITGGLGGLGRALARWLAERGAR-RLVLLSRSGPDAPGAAALlAELEAAGARVTVVACDVADRDALAAVLAAIPAVE 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  2928 GTLNGIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSGLLHVDECSKDFPLDFFIFFSSVSGCLGNAGQADYAAANSFMDAF 3007
Cdd:smart00822   80 GPLTGVIHAAGVLDDGVLASLTPERFAAVLAPKAAGAWNLHELTADLPLDFFVLFSSIAGVLGSPGQANYAAANAFLDAL 159
                           170       180
                    ....*....|....*....|....*..
gi 1776025254  3008 AEYRRSLAaskkrfGSTISFNWPLWEE 3034
Cdd:smart00822  160 AEYRRARG------LPALSIAWGAWAE 180
PS-DH pfam14765
Polyketide synthase dehydratase; This is the dehydratase domain of polyketide synthases. ...
2373-2658 1.08e-61

Polyketide synthase dehydratase; This is the dehydratase domain of polyketide synthases. Structural analysis shows these DH domains are double hotdogs in which the active site contains a histidine from the N-terminal hotdog and an aspartate from the C-terminal hotdog. Studies have uncovered that a substrate tunnel formed between the DH domains may be essential for loading substrates and unloading products.


Pssm-ID: 434191  Cd Length: 296  Bit Score: 214.93  E-value: 1.08e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2373 HPLL-HQNTS-DFSEQKFSSVFTGDEF-FLRDHVVRGKPVLPGVAYLEMAYAAINQAAGSEIG---QDVRIRlnhtvwvQ 2446
Cdd:pfam14765    1 HPLLgSRVPSpSDLEPVWRNRLRLADLpWLRDHRVGGTVVLPGAGYLEMALEAARQLFGGSGAvalRDVSIL-------K 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2447 PVVVDRHSA-QVDISLFPEEDG---KITFDIYSTQEDGDDPVIHSQGSAELASAAETPVADLTEISRRC----GKGKMSP 2518
Cdd:pfam14765   74 ALVLPEDDPvEVQTSLTPEEDGadsWWEFEIFSRAGGGWEWTLHATGTVRLAPGEPAAPVDLESLPARCaqpaDPRSVSS 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2519 DQFYEEGRSRGMFHGPAFQGIKNVNIGNREVLAQLQLPEIVSGTNEQFVLHPSIMDSALQT-ATICIMQELTDQKLILPF 2597
Cdd:pfam14765  154 AEFYERLAARGLFYGPAFQGLRRIWRGDGEALAEARLPEAAAGGESPYLLHPALLDAALQLlGAALPAEAEHADQAYLPV 233
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1776025254 2598 ALEELEVIKG--CSSSMWAYARLSDSDHSGGVvqkADIDVIDESGSVCVRIKGFSTRVLEGEV 2658
Cdd:pfam14765  234 GIERLRIYRSlpPGEPLWVHARLERRGGRTIV---GDLTLVDEDGRVVARIEGLRLRRVEREA 293
AMP-binding pfam00501
AMP-binding enzyme;
35-456 5.94e-60

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 214.10  E-value: 5.94e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254   35 LYRTAAELGDTkgiIYLQPDGTEVYqSYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNSQLLPAFWGCVLTGVVPAPl 114
Cdd:pfam00501    1 LERQAARTPDK---TALEVGEGRRL-TYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVP- 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  115 aVPPTYAESSSGTQkLKDAwtllDKPAVITDRGMHQEMLDWAKEQGLEGFRAIIV--------EDLLSAEADTDWHQS-- 184
Cdd:pfam00501   76 -LNPRLPAEELAYI-LEDS----GAKVLITDDALKLEELLEALGKLEVVKLVLVLdrdpvlkeEPLPEEAKPADVPPPpp 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  185 ---SPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQ----GFTREDITFNWMPFDHVGGIGMLHLRDVYLGCQe 257
Cdd:pfam00501  150 pppDPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRprgfGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGAT- 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  258 INVSSETILMEPLKWLDWIDHYRASVTWAPNFAFGLVTDFAEEikdRKWDLSSMRYMLNGGEAMVAKVGRRILELLephg 337
Cdd:pfam00501  229 VVLPPGFPALDPAALLELIERYKVTVLYGVPTLLNMLLEAGAP---KRALLSSLRLVLSGGAPLPPELARRFRELF---- 301
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  338 lpADAIRPAWGMSETSSGVIFS----HEFTRAGTsdddhfveIGSPIPGFSMRIVNDH-NELVEEGEIGRFQVSGLSVTS 412
Cdd:pfam00501  302 --GGALVNGYGLTETTGVVTTPlpldEDLRSLGS--------VGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMK 371
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*
gi 1776025254  413 GYYQRPDLNESVFTEDGWFETGDLG-FLRNGRLTITGRTKDAIII 456
Cdd:pfam00501  372 GYLNDPELTAEAFDEDGWYRTGDLGrRDEDGYLEIVGRKKDQIKL 416
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
4172-4368 1.32e-57

This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.


Pssm-ID: 214833 [Multi-domain]  Cd Length: 180  Bit Score: 198.48  E-value: 1.32e-57
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  4172 VLLITGGTRGIGLLCARHFAECyGVKKLVLTGREQLPPREEWArfktsntslaekiqAVRELEAKGVQVEMLSLTLSDDA 4251
Cdd:smart00822    2 TYLITGGLGGLGRALARWLAER-GARRLVLLSRSGPDAPGAAA--------------LLAELEAAGARVTVVACDVADRD 66
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  4252 QVEQTLQHIKRTLGPIGGVIHCAGLTDMDTLAfiRKTSDDIQRVMEPKVSGLTTLYRHVCNEPLQFFVLFSSVSAIIPel 4331
Cdd:smart00822   67 ALAAVLAAIPAVEGPLTGVIHAAGVLDDGVLA--SLTPERFAAVLAPKAAGAWNLHELTADLPLDFFVLFSSIAGVLG-- 142
                           170       180       190
                    ....*....|....*....|....*....|....*...
gi 1776025254  4332 SAGQADYAMANSYMDYFAEAHQKHV-PIISVQWPNWKE 4368
Cdd:smart00822  143 SPGQANYAAANAFLDALAEYRRARGlPALSIAWGAWAE 180
omega_3_PfaA TIGR02813
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ...
1759-2193 5.13e-53

polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this alignment are involved in omega-3 polyunsaturated fatty acid biosynthesis, such as the protein PfaA from the eicosapentaenoic acid biosynthesis operon in Photobacterium profundum strain SS9. PfaA is encoded together with PfaB, PfaC, and PfaD, and the functions of the individual polypeptides have not yet been described. More distant homologs of PfaA, also included with the reach of this model, appear to be involved in polyketide-like biosynthetic mechanisms of polyunsaturated fatty acid biosynthesis, an alternative to the more familiar iterated mechanism of chain extension and desaturation, and in most cases are encoded near genes for homologs of PfaB, PfaC, and/or PfaD.


Pssm-ID: 274311 [Multi-domain]  Cd Length: 2582  Bit Score: 208.71  E-value: 5.13e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1759 DDSVAIIGISCEFPGAKNHDEFWENLRDGKESIaffnkeelqrfgisKEIAEN----ADYVPAKASIEGKD--------- 1825
Cdd:TIGR02813    6 DMPIAIVGMASIFANSRYLNKFWDLIFEKIDAI--------------TDVPSDhwakDDYYDSDKSEADKSyckrggflp 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1826 --RFDPSFFQISPKDAEFMDPQLRMLLTHSWKAIEDA---------------GYAAGQIPQTSVFMSASNNSYRALLPSD 1888
Cdd:TIGR02813   72 evDFNPMEFGLPPNILELTDISQLLSLVVAKEVLNDAglpdgydrdkigitlGVGGGQKQSSSLNARLQYPVLKKVFKAS 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1889 TTESLETP-------DGYVSWvlaQSGTIPTM--------ISHKLGLRGPSYFVHANCSSSLIGLHSAYKSLLSAESDYA 1953
Cdd:TIGR02813  152 GVEDEDSEmlikkfqDQYIHW---EENSFPGSlgnvisgrIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMM 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1954 LVGGATLHTESNIGYVHQPGLNFSSDGHIKAFDASADGMIGGEGVAVVLLKKAADAVKDGDHIYALLRGIGVNNDGADKv 2033
Cdd:TIGR02813  229 ITGGVCTDNSPFMYMSFSKTPAFTTNEDIQPFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGKFK- 307
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2034 GFYAPSVKGQADVVQQVMNQTKIHPESICYVEAHGTGTKLGDPIELAALTNVYRQYTNKTQFCGIGSVKTNIGHLDTAAG 2113
Cdd:TIGR02813  308 SIYAPRPEGQAKALKRAYDDAGFAPHTCGLIEAHGTGTAAGDVAEFGGLVSVFSQDNDQKQHIALGSVKSQIGHTKSTAG 387
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2114 LAGCIKVVMSLYHQELAPSINYKEPNPNTDLASSPFYVVDQKKT-LSREIQT-HRAALSSFGLGGTNTHAIFEQFKRDSD 2191
Cdd:TIGR02813  388 TAGMIKAVLALHHKVLPPTINVDQPNPKLDIENSPFYLNTETRPwMQREDGTpRRAGISSFGFGGTNFHMVLEEYSPKHQ 467

                   ..
gi 1776025254 2192 KG 2193
Cdd:TIGR02813  468 RD 469
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
4174-4368 8.60e-48

KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.


Pssm-ID: 430138 [Multi-domain]  Cd Length: 180  Bit Score: 170.44  E-value: 8.60e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4174 LITGGTRGIGLLCARHFAEcYGVKKLVLTGReqlppreewarfktSNTSLAEKIQAVRELEAKGVQVEMLSLTLSDDAQV 4253
Cdd:pfam08659    4 LITGGLGGLGRELARWLAE-RGARHLVLLSR--------------SAAPRPDAQALIAELEARGVEVVVVACDVSDPDAV 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4254 EQTLQHIKRTLGPIGGVIHCAGLTDmDTLaFIRKTSDDIQRVMEPKVSGLTTLYRHVCNEPLQFFVLFSSVSAIIPelSA 4333
Cdd:pfam08659   69 AALLAEIKAEGPPIRGVIHAAGVLR-DAL-LENMTDEDWRRVLAPKVTGTWNLHEATPDEPLDFFVLFSSIAGLLG--SP 144
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1776025254 4334 GQADYAMANSYMDYFAEA-HQKHVPIISVQWPNWKE 4368
Cdd:pfam08659  145 GQANYAAANAFLDALAEYrRSQGLPATSINWGPWAE 180
menE TIGR01923
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ...
61-554 9.50e-41

O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 162605 [Multi-domain]  Cd Length: 436  Bit Score: 158.77  E-value: 9.50e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254   61 SYRRLWDDGLRIVKGLRQSGLKaKQSVILQLGDNS-QLLPAFWGCVLTGVVPAPLAvpPTYAESSSGTQkLKDawtlLDK 139
Cdd:TIGR01923    1 TWQDLDCEAAHLAKALKAQGIR-SGSRVALVGQNSiEMVLLLHACLLLGAEIAMLN--TRLTENERTNQ-LED----LDV 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  140 PAVITDrgmhqEMLDwakeqgLEGFRAIIVEDL-LSAEADTDWHQSSP-EDLALLLLTSGSTGTPKAVMLNHRNIMSMVK 217
Cdd:TIGR01923   73 QLLLTD-----SLLE------EKDFQADSLDRIeAAGRYETSLSASFNmDQIATLMFTSGTTGKPKAVPHTFRNHYASAV 141
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  218 GIIQMQGFTREDitfNWM---PFDHVGGIGMLhLRDVYLGCQEINVSSETILMEPLKwldwidhyRASVTWApnfafGLV 294
Cdd:TIGR01923  142 GSKENLGFTEDD---NWLlslPLYHISGLSIL-FRWLIEGATLRIVDKFNQLLEMIA--------NERVTHI-----SLV 204
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  295 TDFAEEIKDRKWDLSSMRYMLNGGEAMVAKVGRRILELlephGLPadaIRPAWGMSETSSGVI-FSHEFTRAGTSdddhf 373
Cdd:TIGR01923  205 PTQLNRLLDEGGHNENLRKILLGGSAIPAPLIEEAQQY----GLP---IYLSYGMTETCSQVTtATPEMLHARPD----- 272
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  374 veIGSPIPGFSMRIVNDhnELVEEGEIgrfQVSGLSVTSGYYQRPDLNESVFtEDGWFETGDLGFLRN-GRLTITGRTKD 452
Cdd:TIGR01923  273 --VGRPLAGREIKIKVD--NKEGHGEI---MVKGANLMKGYLYQGELTPAFE-QQGWFNTGDIGELDGeGFLYVLGRRDD 344
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  453 AIIINGINYYSHAIESAVEELSEIETsytaaCAVRLGQNST-DQLAIFFVTSAklNDEQMSQLLRNIQSHVSQVigVTPE 531
Cdd:TIGR01923  345 LIISGGENIYPEEIETVLYQHPGIQE-----AVVVPKPDAEwGQVPVAYIVSE--SDISQAKLIAYLTEKLAKY--KVPI 415
                          490       500
                   ....*....|....*....|...
gi 1776025254  532 YLLPVQkeEIPKTAIGKIQRTQL 554
Cdd:TIGR01923  416 AFEKLD--ELPYNASGKILRNQL 436
omega_3_PfaA TIGR02813
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ...
4590-5009 4.06e-40

polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this alignment are involved in omega-3 polyunsaturated fatty acid biosynthesis, such as the protein PfaA from the eicosapentaenoic acid biosynthesis operon in Photobacterium profundum strain SS9. PfaA is encoded together with PfaB, PfaC, and PfaD, and the functions of the individual polypeptides have not yet been described. More distant homologs of PfaA, also included with the reach of this model, appear to be involved in polyketide-like biosynthetic mechanisms of polyunsaturated fatty acid biosynthesis, an alternative to the more familiar iterated mechanism of chain extension and desaturation, and in most cases are encoded near genes for homologs of PfaB, PfaC, and/or PfaD.


Pssm-ID: 274311 [Multi-domain]  Cd Length: 2582  Bit Score: 166.33  E-value: 4.06e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4590 IAVVGLSCRFPGAETLESYWSLLSEGRSSIGPIPAERWGcKTPYY--------------AGVIDGVSyFDPDFFLLHEED 4655
Cdd:TIGR02813    9 IAIVGMASIFANSRYLNKFWDLIFEKIDAITDVPSDHWA-KDDYYdsdkseadksyckrGGFLPEVD-FNPMEFGLPPNI 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4656 VRAMDPQALLVLEECLKLLYHAGyTPEEIKGKPVGVYIG---GRSQHKP--------------------DEDS------- 4705
Cdd:TIGR02813   87 LELTDISQLLSLVVAKEVLNDAG-LPDGYDRDKIGITLGvggGQKQSSSlnarlqypvlkkvfkasgveDEDSemlikkf 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4706 ----LDHAKNPIVTVGQNYLAANLSQFFDVRGPSVVVDTACSSALVGMNMAIQALRGGDIQSAIVGGVSLLSSDASHRLF 4781
Cdd:TIGR02813  166 qdqyIHWEENSFPGSLGNVISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGGVCTDNSPFMYMSF 245
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4782 DRRGILSKHSSFHVFDERADGVVLGEGVGMVMLKTVKQALEDGDTIYAVVKAASVNNDGRTAGPATPNLEAQKEVMKDAL 4861
Cdd:TIGR02813  246 SKTPAFTTNEDIQPFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGKFKSIYAPRPEGQAKALKRAY 325
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4862 FKSGKKPEDISYLEANGSGSIVTDLLELKAIQSVYRSGHSSP--LSLGSIKPNIGHPLCAEGIASFIKVVLMLKERRFVP 4939
Cdd:TIGR02813  326 DDAGFAPHTCGLIEAHGTGTAAGDVAEFGGLVSVFSQDNDQKqhIALGSVKSQIGHTKSTAGTAGMIKAVLALHHKVLPP 405
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1776025254 4940 FLSGEKEMAHFDQQKANITFSRALEKW---TDSQP-TAAINCFADGGTNVHVIVEAWEKDEKHAIKRSPKSPPQ 5009
Cdd:TIGR02813  406 TINVDQPNPKLDIENSPFYLNTETRPWmqrEDGTPrRAGISSFGFGGTNFHMVLEEYSPKHQRDDQYRQRAVAQ 479
PRK07314 PRK07314
beta-ketoacyl-ACP synthase II;
3351-3779 4.16e-37

beta-ketoacyl-ACP synthase II;


Pssm-ID: 235987 [Multi-domain]  Cd Length: 411  Bit Score: 147.24  E-value: 4.16e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3351 PGAMDIDEFWKNLEEGKDSItevpkdrwdwrehygNPDTDVNKTDI--KWGGFIDGvaeFDPLFFgISPREADYVDPQQR 3428
Cdd:PRK07314    14 PLGNDVESTWKNLLAGKSGI---------------GPITHFDTSDLavKIAGEVKD---FNPDDY-MSRKEARRMDRFIQ 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3429 LLMTYVWKALEDAGCPPQSLSGTGTGIFIGTGNTGYKdlfhranlPIEGHAATGH----------MIPSVGPNRMSYFLN 3498
Cdd:PRK07314    75 YGIAAAKQAVEDAGLEITEENADRIGVIIGSGIGGLE--------TIEEQHITLLekgprrvspfFVPMAIINMAAGHVS 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3499 IH----GPSEPVETACSSSLVAIHRAVTAMQNGDCEMAIAGGVntilteEAHIS------YSKAGMLSKD-----GRCKT 3563
Cdd:PRK07314   147 IRygakGPNHSIVTACATGAHAIGDAARLIAYGDADVMVAGGA------EAAITplgiagFAAARALSTRnddpeRASRP 220
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3564 FSADANGYVRGEGVGMVMLKKLEDAERDGNHIYGVIRGTAENhgGRANTLTSPNPK----AQAdlLVRAYRQAGIDPSTV 3639
Cdd:PRK07314   221 FDKDRDGFVMGEGAGILVLEELEHAKARGAKIYAEVVGYGMT--GDAYHMTAPAPDgegaARA--MKLALKDAGINPEDI 296
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3640 TYIEAHGTGTELGDPIEINGLKAAFkelsnmrGESQPDVPdhrcgIGSVKSNIGHLELAAGISGLIKVLLQMKHKTLVKS 3719
Cdd:PRK07314   297 DYINAHGTSTPAGDKAETQAIKRVF-------GEHAYKVA-----VSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPT 364
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1776025254 3720 LHCETLNPylqltdspfyivqekqewksvtDCDGNELP---RRAGI-----SSFGIGGVNAHIVIEEY 3779
Cdd:PRK07314   365 INLDNPDE----------------------ECDLDYVPneaRERKIdyalsNSFGFGGTNASLVFKRY 410
PKS_DH smart00826
Dehydratase domain in polyketide synthase (PKS) enzymes;
2373-2539 4.16e-34

Dehydratase domain in polyketide synthase (PKS) enzymes;


Pssm-ID: 214837  Cd Length: 167  Bit Score: 130.81  E-value: 4.16e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  2373 HPLLHQNTSDFSEQkfSSVFTG-----DEFFLRDHVVRGKPVLPGVAYLEMAYAAinqaaGSEIGQDVRIRLNHTVWVQP 2447
Cdd:smart00826    1 HPLLGARVELADGG--GVVLTGrlslrTHPWLADHRVGGTVVLPGAAYVELALAA-----ADEVGGGAPARLEELTLEAP 73
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  2448 VVVDRHSA-QVDISLF-PEEDGKITFDIYSTQEDGDDPVIHSQGSAELASAAETPVADLTEISRRCGKGKMSPDQFYEEG 2525
Cdd:smart00826   74 LVLPEDGAvRVQVVVGaPDEDGRRTFTVYSRPDGDGPWTRHATGTLRPAAAAPAAPAADLAAWPPAGAEPVDVDDLYERL 153
                           170
                    ....*....|....
gi 1776025254  2526 RSRGMFHGPAFQGI 2539
Cdd:smart00826  154 AARGLEYGPAFQGL 167
PTZ00050 PTZ00050
3-oxoacyl-acyl carrier protein synthase; Provisional
1778-2186 1.31e-33

3-oxoacyl-acyl carrier protein synthase; Provisional


Pssm-ID: 240245 [Multi-domain]  Cd Length: 421  Bit Score: 137.13  E-value: 1.31e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1778 DEFWENLRDGKESIAFFNKEELQRFGISKEIAENADYVPA-----KASIEGKDrFDPSFFQISPKDaefmDPQLRMLLTH 1852
Cdd:PTZ00050    10 ESTWEALIAGKSGIRKLTEFPKFLPDCIPEQKALENLVAAmpcqiAAEVDQSE-FDPSDFAPTKRE----SRATHFAMAA 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1853 SWKAIEDAG--YAAGQIP-QTSVFMSASNNSYRALLpsDTTESLETpDGY--VSWVLaqsgtIPTMISH--------KLG 1919
Cdd:PTZ00050    85 AREALADAKldILSEKDQeRIGVNIGSGIGSLADLT--DEMKTLYE-KGHsrVSPYF-----IPKILGNmaaglvaiKHK 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1920 LRGPSYFVHANC--SSSLIGlhSAYKSLLSAESDYALVGG--ATLHTESNIGYVHQPGL----NFSSDGHIKAFDASADG 1991
Cdd:PTZ00050   157 LKGPSGSAVTACatGAHCIG--EAFRWIKYGEADIMICGGteASITPVSFAGFSRMRALctkyNDDPQRASRPFDKDRAG 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1992 MIGGEGVAVVLLKKAADAVKDGDHIYALLRGIGVNNDGADkVGFYAPSVKGQADVVQQVMNQT-KIHPESICYVEAHGTG 2070
Cdd:PTZ00050   235 FVMGEGAGILVLEELEHALRRGAKIYAEIRGYGSSSDAHH-ITAPHPDGRGARRCMENALKDGaNININDVDYVNAHATS 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2071 TKLGDPIELAALTNVYRQYTNKTqfCGIGSVKTNIGHLDTAAGLAGCIKVVMSLYHQELAPSINYKEPNPNTDLasspfy 2150
Cdd:PTZ00050   314 TPIGDKIELKAIKKVFGDSGAPK--LYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINLENPDAECDL------ 385
                          410       420       430
                   ....*....|....*....|....*....|....*..
gi 1776025254 2151 vVDQKKTLSREIQTHRAALS-SFGLGGTNTHAIFEQF 2186
Cdd:PTZ00050   386 -NLVQGKTAHPLQSIDAVLStSFGFGGVNTALLFTKY 421
PRK07103 PRK07103
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
4590-4939 7.96e-26

polyketide beta-ketoacyl:acyl carrier protein synthase; Validated


Pssm-ID: 180839 [Multi-domain]  Cd Length: 410  Bit Score: 113.97  E-value: 7.96e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4590 IAVVGLSCRFPGAETLESYWSLLSEGRSSIG-------PIPAERWGCKT-PYYAGVIDGVSYFDP-DFFLLHEE--DVRA 4658
Cdd:PRK07103     4 VVVTGVGVVSAIGQGRPSFAAALLAGRHAFGvmrrpgrQVPDDAGAGLAsAFIGAELDSLALPERlDAKLLRRAslSAQA 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4659 mdpqALLVLEECLKllyHAGYTPEEikGKPVGVYIGG-----RSQHKPDEDSLDHAK--NP--IVTVGQNYLAANLSQFF 4729
Cdd:PRK07103    84 ----ALAAAREAWR---DAALGPVD--PDRIGLVVGGsnlqqREQALVHETYRDRPAflRPsyGLSFMDTDLVGLCSEQF 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4730 DVRGPSVVVDTACSSALVGMNMAIQALRGGDIQSAI-VGGVSLLSSDASHRLFDRRGILSKHSSFHV------FDERADG 4802
Cdd:PRK07103   155 GIRGEGFTVGGASASGQLAVIQAARLVQSGSVDACIaVGALMDLSYWECQALRSLGAMGSDRFADEPeaacrpFDQDRDG 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4803 VVLGEGVGMVMLKTVKQALEDGDTIYAVVKAASVNNDGrTAGPAtPNLEAQKEVMKDALFKSGKKPEDISYLEANGSGSI 4882
Cdd:PRK07103   235 FIYGEACGAVVLESAESARRRGARPYAKLLGWSMRLDA-NRGPD-PSLEGEMRVIRAALRRAGLGPEDIDYVNPHGTGSP 312
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1776025254 4883 VTDLLELKAIqsvYRSGHSSPLsLGSIKPNIGHPLCAEGIASFIKVVLMLKERRFVP 4939
Cdd:PRK07103   313 LGDETELAAL---FASGLAHAW-INATKSLTGHGLSAAGIVELIATLLQMRAGFLHP 365
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
2843-3078 4.45e-22

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 98.79  E-value: 4.45e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2843 MPWRDeGVYLITGGAGSLGLLFAKEIANRtGRsTIVLTGRSvlsEDKENEL-EALRSIGAEVVYREADVSDQHAVHHLFE 2921
Cdd:COG0300      1 MSLTG-KTVLITGASSGIGRALARALAAR-GA-RVVLVARD---AERLEALaAELRAAGARVEVVALDVTDPDAVAALAE 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2922 EIKERYGTLNGIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSGLLHvdeCSKDF-PL------DFFIFFSSVSGCLGNAGQ 2994
Cdd:COG0300     75 AVLARFGPIDVLVNNAGVGGGGPFEELDLEDLRRVFEVNVFGPVR---LTRALlPLmrargrGRIVNVSSVAGLRGLPGM 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2995 ADYAAANSFMDAFAEyrrSLAASKKRFG---STISFNW---PLWEEGGMQVGAEdekrmlkttgmvPMPTDSGLKAFYQG 3068
Cdd:COG0300    152 AAYAASKAALEGFSE---SLRAELAPTGvrvTAVCPGPvdtPFTARAGAPAGRP------------LLSPEEVARAILRA 216
                          250
                   ....*....|
gi 1776025254 3069 IASDKPQVFV 3078
Cdd:COG0300    217 LERGRAEVYV 226
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
4174-4373 5.64e-22

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 98.40  E-value: 5.64e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4174 LITGGTRGIGLLCARHFAECyGVKkLVLTGREqlppreewarfktsntslAEKIQAVR-ELEAKGVQVEMLSLTLSDDAQ 4252
Cdd:COG0300      9 LITGASSGIGRALARALAAR-GAR-VVLVARD------------------AERLEALAaELRAAGARVEVVALDVTDPDA 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4253 VEQTLQHIKRTLGPIGGVIHCAGLtdMDTLAFIRKTSDDIQRVMEPKVSGLTTLYRHVcnepLQFF--------VLFSSV 4324
Cdd:COG0300     69 VAALAEAVLARFGPIDVLVNNAGV--GGGGPFEELDLEDLRRVFEVNVFGPVRLTRAL----LPLMrargrgriVNVSSV 142
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1776025254 4325 SAIIPelSAGQADYAMANSYMDYFAEA-----HQKHVPIISVQwPNWKETGMGE 4373
Cdd:COG0300    143 AGLRG--LPGMAAYAASKAALEGFSESlraelAPTGVRVTAVC-PGPVDTPFTA 193
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
2850-3015 2.26e-17

3-ketoacyl-(acyl-carrier-protein) reductase; Validated


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 84.86  E-value: 2.26e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGLLFAKEIAnRTGrSTIVLTGRSvlSEDKENEL-EALRSIGAEVVYREADVSDQHAVHHLFEEIKERYG 2928
Cdd:PRK05557     7 VALVTGASRGIGRAIAERLA-AQG-ANVVINYAS--SEAGAEALvAEIGALGGKALAVQGDVSDAESVERAVDEAKAEFG 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2929 TLNGIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSGLLHvdeCSKDFPLDF-------FIFFSSVSGCLGNAGQADYAAAN 3001
Cdd:PRK05557    83 GVDILVNNAGITRDNLLMRMKEEDWDRVIDTNLTGVFN---LTKAVARPMmkqrsgrIINISSVVGLMGNPGQANYAASK 159
                          170
                   ....*....|....
gi 1776025254 3002 SFMDAFAeyrRSLA 3015
Cdd:PRK05557   160 AGVIGFT---KSLA 170
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
3111-3185 2.32e-13

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 68.43  E-value: 2.32e-13
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1776025254  3111 QTRKLEAALIQMVGAILKVNTDD-IDVNTELSEYGFDSVTFTVFTNKINEKFQLELTPTIFFEYGSVQSLAEYVVA 3185
Cdd:smart00823    9 RRRLLLDLVREQVAAVLGHAAAEaIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHLAA 84
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
3117-3178 3.22e-13

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.


Pssm-ID: 425746 [Multi-domain]  Cd Length: 62  Bit Score: 67.20  E-value: 3.22e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1776025254 3117 AALIQMVGAILKVNTDDIDVNTELSEYGFDSVTFTVFTNKINEKFQLELTPTIFFEYGSVQS 3178
Cdd:pfam00550    1 ERLRELLAEVLGVPAEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLAE 62
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
4172-4341 4.87e-13

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 72.11  E-value: 4.87e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4172 VLLITGGTRGIGLLCARHFAEcYGVKkLVLTGReqlppreewarfktsNTSLAEKIQAvrELEAKGVQVEMLSLTLSDDA 4251
Cdd:PRK05653     7 TALVTGASRGIGRAIALRLAA-DGAK-VVIYDS---------------NEEAAEALAA--ELRAAGGEARVLVFDVSDEA 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4252 QVEQTLQHIKRTLGPIGGVIHCAGLTDMDtlAFIRKTSDDIQRVMEpkVSgLTTLYrHVCNEPLQFF--------VLFSS 4323
Cdd:PRK05653    68 AVRALIEAAVEAFGALDILVNNAGITRDA--LLPRMSEEDWDRVID--VN-LTGTF-NVVRAALPPMikarygriVNISS 141
                          170
                   ....*....|....*...
gi 1776025254 4324 VSAIIPelSAGQADYAMA 4341
Cdd:PRK05653   142 VSGVTG--NPGQTNYSAA 157
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
3221-3281 1.28e-12

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 66.50  E-value: 1.28e-12
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1776025254  3221 VSAILKVNSED-IDVNTELSEYGFDSVTFTVFTNKINEEFQLELTPTIFFEYGSIHSLAEYL 3281
Cdd:smart00823   21 VAAVLGHAAAEaIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHL 82
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
3219-3274 4.50e-12

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.


Pssm-ID: 425746 [Multi-domain]  Cd Length: 62  Bit Score: 63.74  E-value: 4.50e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1776025254 3219 NMVSAILKVNSEDIDVNTELSEYGFDSVTFTVFTNKINEEFQLELTPTIFFEYGSI 3274
Cdd:pfam00550    5 ELLAEVLGVPAEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTL 60
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
592-666 5.73e-12

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 64.10  E-value: 5.73e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1776025254  592 REEIQEHLLTCLTEELHVSRDWVEPNAN-IQSLGVNSIKMMKLIRSIEKNYHIKLTAREIHQYPTIERLASYLSEH 666
Cdd:COG0236      3 REELEERLAEIIAEVLGVDPEEITPDDSfFEDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEEK 78
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
4465-4525 2.21e-11

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.


Pssm-ID: 425746 [Multi-domain]  Cd Length: 62  Bit Score: 61.81  E-value: 2.21e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1776025254 4465 SWLIDLFTEELRIDREDFEIDGLFQDYGVDSIILAQVLQRINRKLEAALDPSILYEYPTIQ 4525
Cdd:pfam00550    1 ERLRELLAEVLGVPAEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLA 61
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
3115-3186 2.04e-10

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 59.87  E-value: 2.04e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1776025254 3115 LEAALIQMVGAILKVNTDDIDVNTEL-SEYGFDSVTFTVFTNKINEKFQLELTPTIFFEYGSVQSLAEYVVAA 3186
Cdd:COG0236      6 LEERLAEIIAEVLGVDPEEITPDDSFfEDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEEK 78
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
4461-4531 3.63e-10

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 59.10  E-value: 3.63e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1776025254 4461 SETQSWLIDLFTEELRIDREDFEID-GLFQDYGVDSIILAQVLQRINRKLEAALDPSILYEYPTIQRFTDWL 4531
Cdd:COG0236      4 EELEERLAEIIAEVLGVDPEEITPDdSFFEDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYL 75
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
599-657 3.02e-09

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.


Pssm-ID: 425746 [Multi-domain]  Cd Length: 62  Bit Score: 56.03  E-value: 3.02e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1776025254  599 LLTCLTEELHVSRDWVEPNANIQSLGVNSIKMMKLIRSIEKNYHIKLTAREIHQYPTIE 657
Cdd:pfam00550    3 LRELLAEVLGVPAEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLA 61
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
3219-3281 8.26e-09

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 55.24  E-value: 8.26e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1776025254 3219 NMVSAILKVNSEDIDVNTEL-SEYGFDSVTFTVFTNKINEEFQLELTPTIFFEYGSIHSLAEYL 3281
Cdd:COG0236     12 EIIAEVLGVDPEEITPDDSFfEDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYL 75
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
1658-1727 1.90e-08

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 54.56  E-value: 1.90e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1776025254  1658 IQDTVFTIWQEVLKTSD---IEWDDGFFDVGGDSLLAVTVADRIKHELSCEFSVTDLFEYSTIKNISQYITEQ 1727
Cdd:smart00823   13 LLDLVREQVAAVLGHAAaeaIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHLAAE 85
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
592-665 1.02e-07

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 52.25  E-value: 1.02e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1776025254   592 REEIQEHLLTCLTEEL-HVSRDWVEPNANIQSLGVNSIKMMKLIRSIEKNYHIKLTAREIHQYPTIERLASYLSE 665
Cdd:smart00823   10 RRLLLDLVREQVAAVLgHAAAEAIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHLAA 84
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
4461-4533 1.96e-07

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 51.48  E-value: 1.96e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1776025254  4461 SETQSWLIDLFTEEL-----RIDREDFEIDGLFQDYGVDSIILAQVLQRINRKLEAALDPSILYEYPTIQRFTDWLIG 4533
Cdd:smart00823    7 AERRRLLLDLVREQVaavlgHAAAEAIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHLAA 84
E_NRPS cd19534
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
695-894 2.46e-07

Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Epimerization (E) domains of nonribosomal peptide synthetases (NRPS) flip the chirality of the end amino acid of a peptide being manufactured by the NRPS. E-domains are homologous to the Condensation (C) domains. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Specialized tailoring NRPS domains such as E-domains greatly increase the range of possible peptide products created by the NRPS machinery. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the E-domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380457 [Multi-domain]  Cd Length: 428  Bit Score: 56.88  E-value: 2.46e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  695 PLSEVQKglWTLQKMSPEKSAYHVPLCFKFSSGLHLETLQQAFGLVLNQHPILKHVIQEKDGVPILKNEPALSIEIKTEn 774
Cdd:cd19534      3 PLTPIQR--WFFEQNLAGRHHFNQSVLLRVPQGLDPDALRQALRALVEHHDALRMRFRREDGGWQQRIRGDVEELFRLE- 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  775 ISSMKESDIPAFLRKKVkEPYVK----ENSPLVRVMSFSRSEQEHFLLVVIHHLIFDGVSSVTFIHSLFDTYQLLLKGQQ 850
Cdd:cd19534     80 VVDLSSLAQAAAIEALA-AEAQSsldlEEGPLLAAALFDGTDGGDRLLLVIHHLVVDGVSWRILLEDLEAAYEQALAGEP 158
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1776025254  851 PEIAVSPAiYHDFAAWEKNMLAGKDGVKHRTYWQKQLSGTLPNL 894
Cdd:cd19534    159 IPLPSKTS-FQTWAELLAEYAQSPALLEELAYWRELPAADYWGL 201
PT_fungal_PKS TIGR04532
iterative type I PKS product template domain; Sequences found by this model are the so-called ...
2381-2580 3.99e-07

iterative type I PKS product template domain; Sequences found by this model are the so-called product template (PT) domain of various fungal iterative type I polyketide synthases. This domain resembles pfam14765, designated polyketide synthase dehydratase by Pfam, but members of that family are primarily bacterial, where type I PKS are predominantly modular, not iterative. The dehydratase active site residues well-conserved in pfam14765 (His in the first hot dog domain, Asp in the second hot dog domain) seem well conserved in this family also.


Pssm-ID: 275325  Cd Length: 324  Bit Score: 55.71  E-value: 3.99e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2381 SDFSEQKFSSVFTGdefflrdHVVRGKPVLPGVAYLEMAYAAIN----QAAGSEIGQDVRIRLNHTVWVQPVVVD----- 2451
Cdd:TIGR04532   23 SDLSDPDLLAAIQG-------HRVNGVPLCPSSVYADMALTAAKyllkRLRGSKDAADVGLDVRDMEVDKPLVADpsdsd 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2452 ----RHSAQVDISLfpeeDGKITFDIYSTQEDGDDPVIHSQGSAELASAAETPVAD----LTEISRRC---------GKG 2514
Cdd:TIGR04532   96 pqllRVTATADAST----SSRVSISFSSSSSSGKKTEEHATCTVRFGDPAAAWLAEwsrtAYLVKSRIdalrqsakeGSA 171
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1776025254 2515 -KMSPDQFYEegrsrgMF-----HGPAFQGIKNVNI--GNREVLAQLQLPEIVSGTNeqFVLHPSIMDSALQTA 2580
Cdd:TIGR04532  172 hRLSRRMAYK------LFsslvdYSPKYRGMQEVVLdsDGLEATATVKLPTDPPDGG--FTVSPYWIDSLLHLA 237
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
3909-4006 7.68e-07

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 56.03  E-value: 7.68e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3909 LADLWVKGVSIQWNTLYGETKPRLISLPSYPFAKDHYWVPAKEHSERDKKELVNAIEDRAACFLTKQWSLSPIGSAVPGT 3988
Cdd:COG3321    837 LAQLWVAGVPVDWSALYPGRGRRRVPLPTYPFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAA 916
                           90
                   ....*....|....*...
gi 1776025254 3989 RTVAILCCQETADLAAEV 4006
Cdd:COG3321    917 AALALAAAALAALLALVA 934
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
2313-2347 1.02e-06

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 55.65  E-value: 1.02e-06
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1776025254 2313 LAEMWSKGAHIDWMQLYKGERPNRMSLPTYPFAKE 2347
Cdd:COG3321    837 LAQLWVAGVPVDWSALYPGRGRRRVPLPTYPFQRE 871
KAsynt_C_assoc pfam16197
Ketoacyl-synthetase C-terminal extension; KAsynt_C_assoc represents the very C-terminus of a ...
4973-5010 2.77e-04

Ketoacyl-synthetase C-terminal extension; KAsynt_C_assoc represents the very C-terminus of a subset of proteins from the keto-acyl-synthetase 2 family. It is found in proteins ranging from bacteria to human.


Pssm-ID: 465059 [Multi-domain]  Cd Length: 111  Bit Score: 43.30  E-value: 2.77e-04
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1776025254 4973 AAINCFADGGTNVHVIVEAWEKdeKHAIKRSPKSPPQL 5010
Cdd:pfam16197   27 VGVNSFGFGGANAHVILKSNPK--PKIPPESPDNLPRL 62
PRK12449 PRK12449
acyl carrier protein; Provisional
592-666 1.02e-03

acyl carrier protein; Provisional


Pssm-ID: 183533 [Multi-domain]  Cd Length: 80  Bit Score: 40.84  E-value: 1.02e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1776025254  592 REEIQEHLLTCLTEELHVSRDWVEPNANIQS-LGVNSIKMMKLIRSIEKNYHIKLTAREIHQYPTIERLASYLSEH 666
Cdd:PRK12449     3 REEIFERLINLIQKQRSYLSLAITEQTHLKDdLAVDSIELVEFIINVEDEFHIAIPDEDVEDMVSMGDLLDYLVQR 78
 
Name Accession Description Interval E-value
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
801-1698 0e+00

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 963.55  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  801 PLVRVMSFSRSEQEHFLLVVIHHLIFDGVSSVTFIHSLFDTYQLLLKGQQPEIAVSPAIYHDFAAWEKNMLAGKDGVKHR 880
Cdd:COG1020    129 PLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLLLAELLRLYLAAYAGAPLPLPPLPIQYADYALWQREWLQGEELARQL 208
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  881 TYWQKQLSGTLPNLQLP-KVSASSVSEFREDTYTRRLSSGFMNQVRMFAKEHSVNVTTVFLSCYMMLLGRYTGQKEQIVG 959
Cdd:COG1020    209 AYWRQQLAGLPPLLELPtDRPRPAVQSYRGARVSFRLPAELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVG 288
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  960 MPAMVRPEERFDDAIGHFLNMLPIRSELNPADTFSSFISKLQLTILDGLDHAAYPFPKMVRDLNIPRSQAGSPVFQTAFF 1039
Cdd:COG1020    289 TPVAGRPRPELEGLVGFFVNTLPLRVDLSGDPSFAELLARVRETLLAAYAHQDLPFERLVEELQPERDLSRNPLFQVMFV 368
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1040 YQNFLQSGsyqsllsryADF--FSVDYVEYIHQEGEYELVFELWETEEKMELNIKYNTGLFDAASISAMFDHFVYVTEQA 1117
Cdd:COG1020    369 LQNAPADE---------LELpgLTLEPLELDSGTAKFDLTLTVVETGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEAL 439
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1118 MLNPSQPLKEYSLLPEAEKQMILKTWNATGKTYP-YITFHELFEQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQ 1196
Cdd:COG1020    440 AADPDQPLGDLPLLTAAERQQLLAEWNATAAPYPaDATLHELFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLR 519
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1197 AHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLEDSEVFITLTTSELVNTLSWNGVTTALLDQ 1276
Cdd:COG1020    520 ALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYMLEDAGARLVLTQSALAARLPELGVPVLALDA 599
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1277 dwDEIAQTASDRkvLTRTVTPENLAYVIYTSGSTGKPKGVMIPHKALTNFLVSMGETPGLTAEDKMLAVTTYCFDIAALE 1356
Cdd:COG1020    600 --LALAAEPATN--PPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFDASVWE 675
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1357 LFLPLIKGAHCYICQTEHTKDVEKLKRDIRTIKPTVMQATPATWKMLFYSGWENEENVK-ILCGGEALPETLKRYFLDTG 1435
Cdd:COG1020    676 IFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLLRALLDAAPEALPSLRlVLVGGEALPPELVRRWRARL 755
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1436 SEA--WNMFGPTETTIWSAVQRINDECSRA---TIGRPIANTQIYITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELT 1510
Cdd:COG1020    756 PGArlVNLYGPTETTVDSTYYEVTPPDADGgsvPIGRPIANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELT 835
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1511 DSRFIDNPF-EPGSKLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMDN-----L 1584
Cdd:COG1020    836 AERFVADPFgFPGARLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDApgdkrL 915
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1585 AAYYTAkHANASLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLKNIDLSGEQlkQRQTSPKNIQDTVFT 1664
Cdd:COG1020    916 VAYVVP-EAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAAAAAA--AAAAPPAEEEEEEAA 992
                          890       900       910
                   ....*....|....*....|....*....|....
gi 1776025254 1665 IWQEVLKTSDIEWDDGFFDVGGDSLLAVTVADRI 1698
Cdd:COG1020    993 LALLLLLVVVVGDDDFFFFGGGLGLLLLLALARA 1026
A_NRPS_TubE_like cd05906
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ...
20-561 0e+00

The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341232 [Multi-domain]  Cd Length: 540  Bit Score: 866.98  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254   20 PLHISEKQPATIPEVLYRtAAELGDTKGIIYLQPDGTEVYQSYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNSQLLP 99
Cdd:cd05906      1 PLHRPEGAPRTLLELLLR-AAERGPTKGITYIDADGSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  100 AFWGCVLTGVVPAPLAVPPTYAESSSGTQKLKDAWTLLDKPAVITDRGMHQEMLDWAKEQGLEGFRAIIVEDLLSAEADT 179
Cdd:cd05906     80 AFWACVLAGFVPAPLTVPPTYDEPNARLRKLRHIWQLLGSPVVLTDAELVAEFAGLETLSGLPGIRVLSIEELLDTAADH 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  180 DWHQSSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDHVGGIGMLHLRDVYLGCQEIN 259
Cdd:cd05906    160 DLPQSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHVGGLVELHLRAVYLGCQQVH 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  260 VSSETILMEPLKWLDWIDHYRASVTWAPNFAFGLVTDFAEEIKDRKWDLSSMRYMLNGGEAMVAKVGRRILELLEPHGLP 339
Cdd:cd05906    240 VPTEEILADPLRWLDLIDRYRVTITWAPNFAFALLNDLLEEIEDGTWDLSSLRYLVNAGEAVVAKTIRRLLRLLEPYGLP 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  340 ADAIRPAWGMSETSSGVIFSHEFTRAGTSDDDHFVEIGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGYYQRPD 419
Cdd:cd05906    320 PDAIRPAFGMTETCSGVIYSRSFPTYDHSQALEFVSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPE 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  420 LNESVFTEDGWFETGDLGFLRNGRLTITGRTKDAIIINGINYYSHAIESAVEELSEIETSYTAACAVRLGQNSTDQLAIF 499
Cdd:cd05906    400 ANAEAFTEDGWFRTGDLGFLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPSFTAAFAVRDPGAETEELAIF 479
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1776025254  500 FVTSAKLNDeQMSQLLRNIQSHVSQVIGVTPEYLLPVQKEEIPKTAIGKIQRTQLKTSFENG 561
Cdd:cd05906    480 FVPEYDLQD-ALSETLRAIRSVVSREVGVSPAYLIPLPKEEIPKTSLGKIQRSKLKAAFEAG 540
PRK12467 PRK12467
peptide synthase; Provisional
185-1737 0e+00

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 845.21  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  185 SPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDI-----TFN-----WMPFDHVGGIGMLHLRDvylg 254
Cdd:PRK12467   654 DPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSmlmvsTFAfdlgvTELFGALASGATLHLLP---- 729
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  255 cqeinvssETILMEPLKWLDWIDHYRASVTWAPNFAFGLVTDFAEEIKDRkwdlsSMRYMLNGGEAMVAKVGRRILELLe 334
Cdd:PRK12467   730 --------PDCARDAEAFAALMADQGVTVLKIVPSHLQALLQASRVALPR-----PQRALVCGGEALQVDLLARVRALG- 795
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  335 phglPADAIRPAWGMSETSSGVIFsheFTRAGTSDDDHFVEIGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGY 414
Cdd:PRK12467   796 ----PGARLINHYGPTETTVGVST---YELSDEERDFGNVPIGQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGY 868
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  415 YQRPDLNESVFTEDGW-------FETGDLGFLR-NGRLTITGRTKDAIIINGINYyshaiesaveELSEIETSYTAACAV 486
Cdd:PRK12467   869 HRRPALTAERFVPDPFgadggrlYRTGDLARYRaDGVIEYLGRMDHQVKIRGFRI----------ELGEIEARLLAQPGV 938
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  487 R------LGQNSTDQLAIFFVTSAKLNDEQMSQLLRNIQSHVSQVIgvtPEYLLP---VQKEEIPKTAIGKIQRTQLKts 557
Cdd:PRK12467   939 ReavvlaQPGDAGLQLVAYLVPAAVADGAEHQATRDELKAQLRQVL---PDYMVPahlLLLDSLPLTPNGKLDRKALP-- 1013
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  558 fengefdhllhKPnrmnDAVQDEEMQQADhvkrvREEIQEHLLTCLTEELHVSRdwVEPNANIQSLGVNSIKMMKLIRSI 637
Cdd:PRK12467  1014 -----------KP----DASAVQATFVAP-----QTELEKRLAAIWADVLKVER--VGLTDNFFELGGHSLLATQVISRV 1071
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  638 EKNYHIKLTAREIHQYPTIERLASYLSehedlssssADKKGTDTYKTEPERSQAtfQPLSEVQKGLWTLQKMSPEKSAYH 717
Cdd:PRK12467  1072 RQRLGIQVPLRTLFEHQTLAGFAQAVA---------AQQQGAQPALPDVDRDQP--LPLSYAQERQWFLWQLEPGSAAYH 1140
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  718 VPLCFKFSSGLHLETLQQAFGLVLNQHPILKHVIQEKDGVPILKNEPALS--IEIKTENISSMKESDIPAFLRKKVKEPY 795
Cdd:PRK12467  1141 IPQALRLKGPLDIEALERSFDALVARHESLRTTFVQEDGRTRQVIHPVGSltLEEPLLLAADKDEAQLKVYVEAEARQPF 1220
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  796 VKENSPLVRVMSFSRSEQEHFLLVVIHHLIFDGVSSVTFIHSLFDTYQLLLKGQQPEIAVSPAIYHDFAAWEKNMLAGKD 875
Cdd:PRK12467  1221 DLEQGPLLRVGLLRLAADEHVLVLTLHHIVSDGWSMQVLVDELVALYAAYSQGQSLQLPALPIQYADYAVWQRQWMDAGE 1300
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  876 GVKHRTYWQKQLSGTLPNLQLP-KVSASSVSEFREDTYTRRLSSGFMNQVRMFAKEHSVNVTTVFLSCYMMLLGRYTGQK 954
Cdd:PRK12467  1301 RARQLAYWKAQLGGEQPVLELPtDRPRPAVQSHRGARLAFELPPALAEGLRALARREGVTLFMLLLASFQTLLHRYSGQD 1380
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  955 EQIVGMPAMVRPEERFDDAIGHFLNMLPIRSELNPADTFSSFISKLQLTILDGLDHAAYPFPKMVRDLNIPRSQAGSPVF 1034
Cdd:PRK12467  1381 DIRVGVPIANRNRAETEGLIGFFVNTQVLRAEVDGQASFQQLLQQVKQAALEAQAHQDLPFEQLVEALQPERSLSHSPLF 1460
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1035 QTAFFYQNFLQSGSYQsllsryADFFSVDYVEYIHQEGEYELVFELWETEEKMELNIKYNTGLFDAASISAMFDHFVYVT 1114
Cdd:PRK12467  1461 QVMFNHQRDDHQAQAQ------LPGLSVESLSWESQTAQFDLTLDTYESSEGLQASLTYATDLFEASTIERLAGHWLNLL 1534
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1115 EQAMLNPSQPLKEYSLLPEAEKQMILKTWNATGKTYPY-ITFHELFEQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAI 1193
Cdd:PRK12467  1535 QGLVADPERRLGELDLLDEAERRQILEGWNATHTGYPLaRLVHQLIEDQAAATPEAVALVFGEQELTYGELNRRANRLAH 1614
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1194 YLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLEDSEVFITLTTSELVNTL-SWNGVTTA 1272
Cdd:PRK12467  1615 RLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQSHLQARLpLPDGLRSL 1694
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1273 LLDQ--DWDEiAQTASDRKVltrTVTPENLAYVIYTSGSTGKPKGVMIPHKALTNFLVSMGETPGLTAEDKMLAVTTYCF 1350
Cdd:PRK12467  1695 VLDQedDWLE-GYSDSNPAV---NLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFAF 1770
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1351 DIAALELFLPLIKGAHCYICQTEHTKDVEKLKRDIRTIKPTVMQATPATWKMlFYSGWENEENV----KILCGGEALPET 1426
Cdd:PRK12467  1771 DVSVWELFWPLINGARLVIAPPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQ-LLQMDEQVEHPlslrRVVCGGEALEVE 1849
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1427 LKRYFL----DTGseAWNMFGPTETTI----WSAvqRINDECSRAT--IGRPIANTQIYITDSQLAPVPAGVPGELCIAG 1496
Cdd:PRK12467  1850 ALRPWLerlpDTG--LFNLYGPTETAVdvthWTC--RRKDLEGRDSvpIGQPIANLSTYILDASLNPVPIGVAGELYLGG 1925
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1497 DGVAKGYYKKEELTDSRFIDNPF-EPGSKLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILEC 1575
Cdd:PRK12467  1926 VGLARGYLNRPALTAERFVADPFgTVGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREA 2005
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1576 VVVA-DMDN---LAAYYTAKHA-------NASLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLKNIDLS 1644
Cdd:PRK12467  2006 VVIAqDGANgkqLVAYVVPTDPglvdddeAQVALRAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKALPAPDAS 2085
                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1645 geQLKQRQTSPKN-IQDTVFTIWQEVLKTSDIEWDDGFFDVGGDSLLAVTVADRIKHElSCEFSVTDLFEYSTIKNISQY 1723
Cdd:PRK12467  2086 --ELQQAYVAPQSeLEQRLAAIWQDVLGLEQVGLHDNFFELGGDSIISIQVVSRARQA-GIRFTPKDLFQHQTVQSLAAV 2162
                         1610
                   ....*....|....
gi 1776025254 1724 ITEQRMGNASDHMP 1737
Cdd:PRK12467  2163 AQEGDGTVSIDQGP 2176
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
3339-3881 0e+00

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 814.49  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3339 EPVAIVGISGRFPGAMDIDEFWKNLEEGKDSITEVPKDRWDWREHYGNPDTDVNKTDIKWGGFIDGVAEFDPLFFGISPR 3418
Cdd:COG3321      4 EPIAIIGMACRFPGADDPEEFWRNLRAGRDAITEVPADRWDADAYYDPDPDAPGKTYVRWGGFLDDVDEFDALFFGISPR 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3419 EADYVDPQQRLLMTYVWKALEDAGCPPQSLSGTGTGIFIGTGNTGYKDLFHRANLPIEGHAATGhMIPSVGPNRMSYFLN 3498
Cdd:COG3321     84 EAEAMDPQQRLLLEVAWEALEDAGYDPESLAGSRTGVFVGASSNDYALLLLADPEAIDAYALTG-NAKSVLAGRISYKLD 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3499 IHGPSEPVETACSSSLVAIHRAVTAMQNGDCEMAIAGGVNTILTEEAHISYSKAGMLSKDGRCKTFSADANGYVRGEGVG 3578
Cdd:COG3321    163 LRGPSVTVDTACSSSLVAVHLACQSLRSGECDLALAGGVNLMLTPESFILFSKGGMLSPDGRCRAFDADADGYVRGEGVG 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3579 MVMLKKLEDAERDGNHIYGVIRGTAENHGGRANTLTSPNPKAQADLLVRAYRQAGIDPSTVTYIEAHGTGTELGDPIEIN 3658
Cdd:COG3321    243 VVVLKRLSDALRDGDRIYAVIRGSAVNQDGRSNGLTAPNGPAQAAVIRRALADAGVDPATVDYVEAHGTGTPLGDPIEAA 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3659 GLKAAFKELsnmRGESQPdvpdhrCGIGSVKSNIGHLELAAGISGLIKVLLQMKHKTLVKSLHCETLNPYLQLTDSPFYI 3738
Cdd:COG3321    323 ALTAAFGQG---RPADQP------CAIGSVKSNIGHLEAAAGVAGLIKAVLALRHGVLPPTLHFETPNPHIDFENSPFYV 393
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3739 VQEKQEWKSvtdcdgNELPRRAGISSFGIGGVNAHIVIEEYMPKANSEHTATEQPNVIVLSAKNKSRLIDRASQLLEAIR 3818
Cdd:COG3321    394 NTELRPWPA------GGGPRRAGVSSFGFGGTNAHVVLEEAPAAAPAAAAAARPPQLLVLSAKTEEALRALAARLAAFLE 467
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1776025254 3819 NKkyTDQGLHRIAYTLQVGREEMDERLACVAGTMQELEEKLQAFVDGKEETDEFFRGQSHRNK 3881
Cdd:COG3321    468 AH--PDLDLADVAYTLATGRAHFEHRLAVVASSREELAAKLRALAAGEAAPGVVTGAAAAAPK 528
PRK05691 PRK05691
peptide synthase; Validated
28-1715 0e+00

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 807.85  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254   28 PATIPEVLYRTAAELGDTKGIIYLQPDGTE-VYQSYRRLwDDGLRIVKGLRQSGLKAKQSVILQLGDNSQLLPAFWGCVL 106
Cdd:PRK05691     8 PLTLVQALQRRAAQTPDRLALRFLADDPGEgVVLSYRDL-DLRARTIAAALQARASFGDRAVLLFPSGPDYVAAFFGCLY 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  107 TGVVPAPlAVPPtyaESSSGTQK------LKDAWTLLdkpaVITDRGMHQEMldwakeQGLEGFRA------IIVEDLLS 174
Cdd:PRK05691    87 AGVIAVP-AYPP---ESARRHHQerllsiIADAEPRL----LLTVADLRDSL------LQMEELAAanapelLCVDTLDP 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  175 AEADtDWH--QSSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIiqMQGF----TREDITFNWMPFDH-VGGIGMLh 247
Cdd:PRK05691   153 ALAE-AWQepALQPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLI--RHGFgidlNPDDVIVSWLPLYHdMGLIGGL- 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  248 LRDVYLGCQEINVSSETILMEPLKWLDWIDHYRASVTWAPNFAFGLVTDFAEEIKDRKWDLSSMRYMLNGGEAMVAKVGR 327
Cdd:PRK05691   229 LQPIFSGVPCVLMSPAYFLERPLRWLEAISEYGGTISGGPDFAYRLCSERVSESALERLDLSRWRVAYSGSEPIRQDSLE 308
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  328 RILELLEPHGLPADAIRPAWGMSETSSGV--------IFSHEF-------TRAGTSDDDHFVEIGSPIPGFSMRIVN-DH 391
Cdd:PRK05691   309 RFAEKFAACGFDPDSFFASYGLAEATLFVsggrrgqgIPALELdaealarNRAEPGTGSVLMSCGRSQPGHAVLIVDpQS 388
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  392 NELVEEGEIGRFQVSGLSVTSGYYQRPDLNESVFTE-DG--WFETGDLGFLRNGRLTITGRTKDAIIINGINYYSHAIES 468
Cdd:PRK05691   389 LEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTFVEhDGrtWLRTGDLGFLRDGELFVTGRLKDMLIVRGHNLYPQDIEK 468
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  469 AVE-ELSEIETSYTAACAVRlgQNSTDQLAIFFVTSAKLNDEQMSQ-LLRNIQSHVSQVIGVTPEYLLPVQKEEIPKTAI 546
Cdd:PRK05691   469 TVErEVEVVRKGRVAAFAVN--HQGEEGIGIAAEISRSVQKILPPQaLIKSIRQAVAEACQEAPSVVLLLNPGALPKTSS 546
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  547 GKIQRTQLKTSFENGEFDHLLHKPNrmNDAVQDEEMQQADhvkrvrEEIQEHLLTCLTEELHVSRdwVEPNANIQSLGVN 626
Cdd:PRK05691   547 GKLQRSACRLRLADGSLDSYALFPA--LQAVEAAQTAASG------DELQARIAAIWCEQLKVEQ--VAADDHFFLLGGN 616
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  627 SIKMMKLIRSIEKNYHIKLTAREIHQYPTIERLASYLSEHEdlssssADKKGTDTYKTEPERSQATfqPLSEVQKGLWTL 706
Cdd:PRK05691   617 SIAATQVVARLRDELGIDLNLRQLFEAPTLAAFSAAVARQL------AGGGAAQAAIARLPRGQAL--PQSLAQNRLWLL 688
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  707 QKMSPEKSAYHVPlcfkfsSGLHL------ETLQQAFGLVLNQHPILKHVIQEKDGVPILKNEPALSIEIKTENISSMKE 780
Cdd:PRK05691   689 WQLDPQSAAYNIP------GGLHLrgeldeAALRASFQRLVERHESLRTRFYERDGVALQRIDAQGEFALQRIDLSDLPE 762
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  781 SDIPAFLRK----KVKEPYVKENSPLVRVMSFSRSEQEHFLLVVIHHLIFDGVSSVTFIHSLFDTYQLLLKGQQPEIAVS 856
Cdd:PRK05691   763 AEREARAAQireeEARQPFDLEKGPLLRVTLVRLDDEEHQLLVTLHHIVADGWSLNILLDEFSRLYAAACQGQTAELAPL 842
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  857 PAIYHDFAAWEKNMLAGKDGVKHRTYWQKQLSGTLPNLQLP-KVSASSVSEFREDTYTRRLSSGFMNQVRMFAKEHSVNV 935
Cdd:PRK05691   843 PLGYADYGAWQRQWLAQGEAARQLAYWKAQLGDEQPVLELAtDHPRSARQAHSAARYSLRVDASLSEALRGLAQAHQATL 922
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  936 TTVFLSCYMMLLGRYTGQKEQIVGMPAMVRPEERFDDAIGHFLNMLPIRSELNPADTFSSFISKLQLTILDGLDHAAYPF 1015
Cdd:PRK05691   923 FMVLLAAFQALLHRYSGQGDIRIGVPNANRPRLETQGLVGFFINTQVLRAQLDGRLPFTALLAQVRQATLGAQAHQDLPF 1002
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1016 PKMVRDLNIPRSQAgspVFQTAFFYQnflqsgsyQSLLS--RYADFFSVDYVEYIHQEGEYELvfELWETEE---KMELN 1090
Cdd:PRK05691  1003 EQLVEALPQAREQG---LFQVMFNHQ--------QRDLSalRRLPGLLAEELPWHSREAKFDL--QLHSEEDrngRLTLS 1069
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1091 IKYNTGLFDAASISAMFDHFVYVTEQAMLNPSQPLKEYSLLPEAEKQMiLKTWNATGKTYPYITFHELFEQQAKKTPDRA 1170
Cdd:PRK05691  1070 FDYAAELFDAATIERLAEHFLALLEQVCEDPQRALGDVQLLDAAERAQ-LAQWGQAPCAPAQAWLPELLNEQARQTPERI 1148
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1171 AVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLEDSE 1250
Cdd:PRK05691  1149 ALVWDGGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSG 1228
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1251 VFITLTTSELVNTL-SWNGVTTALLDQ-DWDEIAQTASdrkvlTRTVTPENLAYVIYTSGSTGKPKGVMIPHKALTNFLV 1328
Cdd:PRK05691  1229 VELLLTQSHLLERLpQAEGVSAIALDSlHLDSWPSQAP-----GLHLHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQ 1303
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1329 SMGETPGLTAEDKMLAVTTYCFDIAALELFLPLIKGAHCYICQTEHTKDVEKLKRDIRTIKPTVMQATPATWKMLFYSGW 1408
Cdd:PRK05691  1304 WMQATYALDDSDVLMQKAPISFDVSVWECFWPLITGCRLVLAGPGEHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEPL 1383
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1409 ENEENV--KILCGGEALPETLKRYFLDT--GSEAWNMFGPTETTI----WsavQRINDECSRATIGRPIANTQIYITDSQ 1480
Cdd:PRK05691  1384 AAACTSlrRLFSGGEALPAELRNRVLQRlpQVQLHNRYGPTETAInvthW---QCQAEDGERSPIGRPLGNVLCRVLDAE 1460
                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1481 LAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPF-EPGSKLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIEL 1559
Cdd:PRK05691  1461 LNLLPPGVAGELCIGGAGLARGYLGRPALTAERFVPDPLgEDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEP 1540
                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1560 GDIESRLSEHPGILECVVV----ADMDNLAAYYTAKhANASLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDR 1635
Cdd:PRK05691  1541 EEIQARLLAQPGVAQAAVLvregAAGAQLVGYYTGE-AGQEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDR 1619
                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1636 NSLKNidlsgEQLKQRQ-TSPKN-IQDTVFTIWQEVLKTSDIEWDDGFFDVGGDSLLAVTVADRIKHELSCEFSVTDLFE 1713
Cdd:PRK05691  1620 RALPE-----PVWQQREhVEPRTeLQQQIAAIWREVLGLPRVGLRDDFFALGGHSLLATQIVSRTRQACDVELPLRALFE 1694

                   ..
gi 1776025254 1714 YS 1715
Cdd:PRK05691  1695 AS 1696
PRK12316 PRK12316
peptide synthase; Provisional
61-1722 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 794.16  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254   61 SYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNSQLLPAFWGCVLTGVVPAPLavPPTYAesssgTQKLkdAWTLLDKP 140
Cdd:PRK12316  2030 SYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPL--DPNYP-----AERL--AYMLEDSG 2100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  141 A--VITDRGMHQEMLdwaKEQGLEgfraiivedLLSAEADTDWH---------QSSPEDLALLLLTSGSTGTPKAVMLNH 209
Cdd:PRK12316  2101 AalLLTQRHLLERLP---LPAGVA---------RLPLDRDAEWAdypdtapavQLAGENLAYVIYTSGSTGLPKGVAVSH 2168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  210 RNIMSMVKGIIQMQGFTREDITFNWMPFDHVGGI-----GMLHLRDVYLGCQEINVSSETI-LMEplkwldwidhyRASV 283
Cdd:PRK12316  2169 GALVAHCQAAGERYELSPADCELQFMSFSFDGAHeqwfhPLLNGARVLIRDDELWDPEQLYdEME-----------RHGV 2237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  284 TWApNFAFGLVTDFAEEIKDRKWDLSSMRYMLnGGEAMVAKVGRRILEllephGLPADAIRPAWGMSETSsgVIFSHEFT 363
Cdd:PRK12316  2238 TIL-DFPPVYLQQLAEHAERDGRPPAVRVYCF-GGEAVPAASLRLAWE-----ALRPVYLFNGYGPTEAV--VTPLLWKC 2308
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  364 RAGTSDDDHFVEIGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGYYQRPDLNESVFTEDGW-------FETGDL 436
Cdd:PRK12316  2309 RPQDPCGAAYVPIGRALGNRRAYILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFsasgerlYRTGDL 2388
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  437 GFLR-NGRLTITGRTKDAIIINGINYyshaiesaveELSEIETSYTAACAVR----LGQN--STDQLAIFFVTsaklnDE 509
Cdd:PRK12316  2389 ARYRaDGVVEYLGRIDHQVKIRGFRI----------ELGEIEARLQAHPAVReavvVAQDgaSGKQLVAYVVP-----DD 2453
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  510 QMSQLLRNIQSHVSQVIgvtPEYLLP---VQKEEIPKTAIGKIQRTQLKtsfengefdhllhkpnrmndAVQDEEMQQAD 586
Cdd:PRK12316  2454 AAEDLLAELRAWLAARL---PAYMVPahwVVLERLPLNPNGKLDRKALP--------------------KPDVSQLRQAY 2510
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  587 HVKRvrEEIQEHLLTCLTEELHVSRdwVEPNANIQSLGVNSIKMMKLIRSIEKNYHIKLTAREIHQYPTIERLAsylseh 666
Cdd:PRK12316  2511 VAPQ--EGLEQRLAAIWQAVLKVEQ--VGLDDHFFELGGHSLLATQVVSRVRQDLGLEVPLRILFERPTLAAFA------ 2580
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  667 edlssssADKKGTDTYKTEPERSQATFQPL--SEVQKGLWTLQKMSPEKSAYHVPLCFKFSSGLHLETLQQAFGLVLNQH 744
Cdd:PRK12316  2581 -------ASLESGQTSRAPVLQKVTRVQPLplSHAQQRQWFLWQLEPESAAYHLPSALHLRGVLDQAALEQAFDALVLRH 2653
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  745 PILKHVIQEKDGVPILKNEPALSIEIKTENISSMKESDIPAFLRKKVKEPYVKENSPLVRVMSFSRSEQEHFLLVVIHHL 824
Cdd:PRK12316  2654 ETLRTRFVEVGEQTRQVILPNMSLRIVLEDCAGVADAAIRQRVAEEIQRPFDLARGPLLRVRLLALDGQEHVLVITQHHI 2733
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  825 IFDGVSSVTFIHSLFDTYQLLLKGQQPEIAVSPAIYHDFAAWEKNMLAGKDGVKHRTYWQKQLSGTLPNLQLPKVSAS-S 903
Cdd:PRK12316  2734 VSDGWSMQVMVDELVQAYAGARRGEQPTLPPLPLQYADYAAWQRAWMDSGEGARQLDYWRERLGGEQPVLELPLDRPRpA 2813
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  904 VSEFREDTYTRRLSSGFMNQVRMFAKEHSVNVTTVFLSCYMMLLGRYTGQKEQIVGMPAMVRPEERFDDAIGHFLNMLPI 983
Cdd:PRK12316  2814 LQSHRGARLDVALDVALSRELLALARREGVTLFMLLLASFQVLLHRYSGQSDIRVGVPIANRNRAETERLIGFFVNTQVL 2893
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  984 RSELNPADTFSSFISKLQLTILDGLDHAAYPFPKMVRDLNIPRSQAGSPVFQTAFFYQNFLQSGSYQSLLsryaDFFSVD 1063
Cdd:PRK12316  2894 RAQVDAQLAFRDLLGQVKEQALGAQAHQDLPFEQLVEALQPERSLSHSPLFQVMYNHQSGERAAAQLPGL----HIESFA 2969
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1064 YVEYIHQegeYELVFELWETEEKMELNIKYNTGLFDAASISAMFDHFVYVTEQAMLNPSQPLKEYSLLPEAEKQMILKTW 1143
Cdd:PRK12316  2970 WDGAATQ---FDLALDTWESAEGLGASLTYATDLFDARTVERLARHWQNLLRGMVENPQRSVDELAMLDAEERGQLLEAW 3046
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1144 NATGKTYPY-ITFHELFEQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLA 1222
Cdd:PRK12316  3047 NATAAEYPLeRGVHRLFEEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLA 3126
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1223 ILKAGGAYVPLDPSYPAERLEYMLEDSEVFITLTTSELVNTLSwNGVTTALLDQDWDEIAQTASDRKVltrtvTPENLAY 1302
Cdd:PRK12316  3127 ILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQSHLRLPLA-QGVQVLDLDRGDENYAEANPAIRT-----MPENLAY 3200
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1303 VIYTSGSTGKPKGVMIPHKALTNFLVSMGETPGLTAEDKMLAVTTYCFDIAALELFLPLIKGAHCYICQTEHTKDVEKLK 1382
Cdd:PRK12316  3201 VIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDPALLV 3280
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1383 RDIRTIKPTVMQATPATWKMLFYSGWENEENV--KILCGGEALPETLKRYFLdTGSEAWNMFGPTETTIWSAVQRINDEC 1460
Cdd:PRK12316  3281 ELINSEGVDVLHAYPSMLQAFLEEEDAHRCTSlkRIVCGGEALPADLQQQVF-AGLPLYNLYGPTEATITVTHWQCVEEG 3359
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1461 -SRATIGRPIANTQIYITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPFEPGSKLYRTGDMARWLPGGR 1539
Cdd:PRK12316  3360 kDAVPIGRPIANRACYILDGSLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPFVPGERLYRTGDLARYRADGV 3439
                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1540 IEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMDNLAAYYTAKHANASLTARELRHFVKNALPAYMVPSYF 1619
Cdd:PRK12316  3440 IEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAVDGRQLVAYVVPEDEAGDLREALKAHLKASLPEYMVPAHL 3519
                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1620 IQLDHMPLTPNGKIDRNSLKNIDLSgeQLKQRQTSPKN-IQDTVFTIWQEVLKTSDIEWDDGFFDVGGDSLLAVTVADRI 1698
Cdd:PRK12316  3520 LFLERMPLTPNGKLDRKALPRPDAA--LLQQDYVAPVNeLERRLAAIWADVLKLEQVGLTDNFFELGGDSIISLQVVSRA 3597
                         1690      1700
                   ....*....|....*....|....
gi 1776025254 1699 KhELSCEFSVTDLFEYSTIKNISQ 1722
Cdd:PRK12316  3598 R-QAGIRFTPKDLFQHQTIQGLAR 3620
C_PKS-NRPS_PksJ-like cd20484
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
693-1121 0e+00

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs), similar to Bacillus subtilis PksJ; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily have the typical C-domain HHxxxD motif. PksJ is involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is important in secondary metabolism. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380472 [Multi-domain]  Cd Length: 430  Bit Score: 789.59  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  693 FQPLSEVQKGLWTLQKMSPEKSAYHVPLCFKFSSGLHLETLQQAFGLVLNQHPILKHVIQEKDGVPILKNEPALSIEIKT 772
Cdd:cd20484      1 RSPLSEGQKGLWMLQKMSPEMSAYNVPLCFRFSSKLDVEKFKQACQFVLEQHPILKSVIEEEDGVPFQKIEPSKPLSFQE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  773 ENISSMKESDIPAFLRKKVKEPYVKENSPLVRVMSFSRSEQEHFLLVVIHHLIFDGVSSVTFIHSLFDTYQLLLKGQQPE 852
Cdd:cd20484     81 EDISSLKESEIIAYLREKAKEPFVLENGPLMRVHLFSRSEQEHFVLITIHHIIFDGSSSLTLIHSLLDAYQALLQGKQPT 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  853 IAVSPAIYHDFAAWEKNMLAGKDGVKHRTYWQKQLSGTLPNLQLPKVSA-SSVSEFREDTYTRRLSSGFMNQVRMFAKEH 931
Cdd:cd20484    161 LASSPASYYDFVAWEQDMLAGAEGEEHRAYWKQQLSGTLPILELPADRPrSSAPSFEGQTYTRRLPSELSNQIKSFARSQ 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  932 SVNVTTVFLSCYMMLLGRYTGQKEQIVGMPAMVRPEERFDDAIGHFLNMLPIRSELNPADTFSSFISKLQLTILDGLDHA 1011
Cdd:cd20484    241 SINLSTVFLGIFKLLLHRYTGQEDIIVGMPTMGRPEERFDSLIGYFINMLPIRSRILGEETFSDFIRKLQLTVLDGLDHA 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1012 AYPFPKMVRDLNIPRSQAGSPVFQTAFFYQNFLQSGSYQSLLSRYADFFSVDYVEYIHQEGEYELVFELWETEEKMELNI 1091
Cdd:cd20484    321 AYPFPAMVRDLNIPRSQANSPVFQVAFFYQNFLQSTSLQQFLAEYQDVLSIEFVEGIHQEGEYELVLEVYEQEDRFTLNI 400
                          410       420       430
                   ....*....|....*....|....*....|
gi 1776025254 1092 KYNTGLFDAASISAMFDHFVYVTEQAMLNP 1121
Cdd:cd20484    401 KYNPDLFDASTIERMMEHYVKLAEELIANP 430
PRK12467 PRK12467
peptide synthase; Provisional
688-1733 0e+00

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 788.20  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  688 RSQATFQPLSEVQKGLWTLQKMSPEKSAYHVPLCFKFSSGLHLETLQQAFGLVLNQHPILKHVIQEKDGVPILKNEPALS 767
Cdd:PRK12467    44 RSAFERIPLSYAQERQWFLWQLDPDSAAYNIPTALRLRGELDVSALRRAFDALVARHESLRTRFVQDEEGFRQVIDASLS 123
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  768 IEIKTENISSM----KESDIPAFLRKKVKEPYVKENSPLVRVMSFSRSEQEHFLLVVIHHLIFDGVSSVTFIHSLFDTYQ 843
Cdd:PRK12467   124 LTIPLDDLANEqgraRESQIEAYINEEVARPFDLANGPLLRVRLLRLADDEHVLVVTLHHIISDGWSMRVLVEELVQLYS 203
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  844 LLLKGQQPEIAVSPAIYHDFAAWEKNMLAGKDGVKHRTYWQKQLSGTLPNLQLP-KVSASSVSEFREDTYTRRLSSGFMN 922
Cdd:PRK12467   204 AYSQGREPSLPALPIQYADYAIWQRSWLEAGERERQLAYWQEQLGGEHTVLELPtDRPRPAVPSYRGARLRVDLPQALSA 283
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  923 QVRMFAKEHSVNVTTVFLSCYMMLLGRYTGQKEQIVGMPAMVRPEERFDDAIGHFLNMLPIRSELNPADTFSSFISKLQL 1002
Cdd:PRK12467   284 GLKALAQREGVTLFMVLLASFQTLLHRYSGQSDIRIGVPNANRNRVETERLIGFFVNTQVLKAEVDPQASFLELLQQVKR 363
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1003 TILDGLDHAAYPFPKMVRDLNIPRSQAGSPVFQTAFFYQNfLQSGSYQSLLSRYADFfSVDYVEYIHQEGEYELVFELWE 1082
Cdd:PRK12467   364 TALGAQAHQDLPFEQLVEALQPERSLSHSPLFQVMFNHQN-TATGGRDREGAQLPGL-TVEELSWARHTAQFDLALDTYE 441
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1083 TEEKMELNIKYNTGLFDAASISAMFDHFVYVTEQAMLNPSQPLKEYSLLPEAEKQMILKTWNATGKTYPYITFHELFEQQ 1162
Cdd:PRK12467   442 SAQGLWAAFTYATDLFEATTIERLATHWRNLLEAIVAEPRRRLGELPLLDAEERARELVRWNAPATEYAPDCVHQLIEAQ 521
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1163 AKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERL 1242
Cdd:PRK12467   522 ARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRL 601
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1243 EYMLEDSEVFITLTTSELVNTLSW-NGVTTALLDQDWDEIAQTASDRKVLtrTVTPENLAYVIYTSGSTGKPKGVMIPHK 1321
Cdd:PRK12467   602 AYMLDDSGVRLLLTQSHLLAQLPVpAGLRSLCLDEPADLLCGYSGHNPEV--ALDPDNLAYVIYTSGSTGQPKGVAISHG 679
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1322 ALTNFLVSMGETPGLTAEDKMLAVTTYCFDIAALELFLPLIKGAHCYICQTEHTKDVEKLKRDIRTIKPTVMQATPATWK 1401
Cdd:PRK12467   680 ALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPDCARDAEAFAALMADQGVTVLKIVPSHLQ 759
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1402 MLFYSGWENE--ENVKILCGGEALPETLKRYFLDTGSEA--WNMFGPTETTIWSAVQRINDE---CSRATIGRPIANTQI 1474
Cdd:PRK12467   760 ALLQASRVALprPQRALVCGGEALQVDLLARVRALGPGArlINHYGPTETTVGVSTYELSDEerdFGNVPIGQPLANLGL 839
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1475 YITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPFEP-GSKLYRTGDMARWLPGGRIEYIGRIDNQVKIR 1553
Cdd:PRK12467   840 YILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDPFGAdGGRLYRTGDLARYRADGVIEYLGRMDHQVKIR 919
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1554 GFRIELGDIESRLSEHPGILECVVVA---DMDN-LAAY----YTAKHANASLTARELRHFVKNALPAYMVPSYFIQLDHM 1625
Cdd:PRK12467   920 GFRIELGEIEARLLAQPGVREAVVLAqpgDAGLqLVAYlvpaAVADGAEHQATRDELKAQLRQVLPDYMVPAHLLLLDSL 999
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1626 PLTPNGKIDRNSLKNIDLSgeQLKQRQTSPKN-IQDTVFTIWQEVLKTSDIEWDDGFFDVGGDSLLAVTVADRIKHELSC 1704
Cdd:PRK12467  1000 PLTPNGKLDRKALPKPDAS--AVQATFVAPQTeLEKRLAAIWADVLKVERVGLTDNFFELGGHSLLATQVISRVRQRLGI 1077
                         1050      1060
                   ....*....|....*....|....*....
gi 1776025254 1705 EFSVTDLFEYSTIKNISQYITEQRMGNAS 1733
Cdd:PRK12467  1078 QVPLRTLFEHQTLAGFAQAVAAQQQGAQP 1106
A_NRPS_Ta1_like cd12116
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ...
1167-1638 0e+00

The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.


Pssm-ID: 341281 [Multi-domain]  Cd Length: 470  Bit Score: 766.07  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1167 PDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYML 1246
Cdd:cd12116      1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1247 EDSEVFITLTTSELVNTLSWNGVTTALLdqdwdeIAQTASDRKVLTRTVTPENLAYVIYTSGSTGKPKGVMIPHKALTNF 1326
Cdd:cd12116     81 EDAEPALVLTDDALPDRLPAGLPVLLLA------LAAAAAAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNF 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1327 LVSMGETPGLTAEDKMLAVTTYCFDIAALELFLPLIKGAHCYICQTEHTKDVEKLKRDIRTIKPTVMQATPATWKMLFYS 1406
Cdd:cd12116    155 LHSMRERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSITVMQATPATWRMLLDA 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1407 GWENEENVKILCGGEALPETLKRYFLDTGSEAWNMFGPTETTIWSAVQRINDECSRATIGRPIANTQIYITDSQLAPVPA 1486
Cdd:cd12116    235 GWQGRAGLTALCGGEALPPDLAARLLSRVGSLWNLYGPTETTIWSTAARVTAAAGPIPIGRPLANTQVYVLDAALRPVPP 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1487 GVPGELCIAGDGVAKGYYKKEELTDSRFIDNPF-EPGSKLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESR 1565
Cdd:cd12116    315 GVPGELYIGGDGVAQGYLGRPALTAERFVPDPFaGPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAA 394
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1776025254 1566 LSEHPGILECVVVADMDN----LAAYYTAKHAnASLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSL 1638
Cdd:cd12116    395 LAAHPGVAQAAVVVREDGgdrrLVAYVVLKAG-AAPDAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
PRK12316 PRK12316
peptide synthase; Provisional
686-1740 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 732.53  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  686 PERSQATFQPLSEVQKGLWTLQKMSPEKSAYHVPLCFKFSSGLHLETLQQAFGLVLNQHPILKHVIQEKDGVPILKNEPA 765
Cdd:PRK12316    42 AGVSSAERDRLSYAQQRMWFLWQLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADDSLAQVPLD 121
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  766 LSIEIKTENISSMKESDIPAFLRKKVK----EPYVKENSPLVRVMSFSRSEQEHFLLVVIHHLIFDGVSSVTFIHSLFDT 841
Cdd:PRK12316   122 RPLEVEFEDCSGLPEAEQEARLRDEAQreslQPFDLCEGPLLRVRLLRLGEEEHVLLLTLHHIVSDGWSMNVLIEEFSRF 201
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  842 YQLLLKGQQPEIAVSPAIYHDFAAWEKNMLAGKDGVKHRTYWQKQLSGTLPNLQLP-KVSASSVSEFREDTYTRRLSSGF 920
Cdd:PRK12316   202 YSAYATGAEPGLPALPIQYADYALWQRSWLEAGEQERQLEYWRAQLGEEHPVLELPtDHPRPAVPSYRGSRYEFSIDPAL 281
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  921 MNQVRMFAKEHSVNVTTVFLSCYMMLLGRYTGQKEQIVGMPAMVRPEERFDDAIGHFLNMLPIRSELNPADTFSSFISKL 1000
Cdd:PRK12316   282 AEALRGTARRQGLTLFMLLLGAFNVLLHRYSGQTDIRVGVPIANRNRAEVEGLIGFFVNTQVLRSVFDGRTRVATLLAGV 361
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1001 QLTILDGLDHAAYPFPKMVRDLNIPRSQAGSPVFQTAFFYQNFLQSGSYQSLLSRyadfFSVDYVEYIHQEGEYELVFEL 1080
Cdd:PRK12316   362 KDTVLGAQAHQDLPFERLVEALKVERSLSHSPLFQVMYNHQPLVADIEALDTVAG----LEFGQLEWKSRTTQFDLTLDT 437
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1081 WETEEKMELNIKYNTGLFDAASISAMFDHFVYVTEQAMLNPSQPLKEYSLLPEAEKQMILKTWNATGKTYPYIT-FHELF 1159
Cdd:PRK12316   438 YEKGGRLHAALTYATDLFEARTVERMARHWQNLLRGMVENPQARVDELPMLDAEERGQLVEGWNATAAEYPLQRgVHRLF 517
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1160 EQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPA 1239
Cdd:PRK12316   518 EEQVERTPEAPALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPA 597
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1240 ERLEYMLEDSEVFITLTTSELVNTLSWN-GVTTALLDQDWDEIAqTASDRKVLTRtVTPENLAYVIYTSGSTGKPKGVMI 1318
Cdd:PRK12316   598 ERLAYMLEDSGVQLLLSQSHLGRKLPLAaGVQVLDLDRPAAWLE-GYSEENPGTE-LNPENLAYVIYTSGSTGKPKGAGN 675
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1319 PHKALTNFLVSMGETPGLTAEDKMLAVTTYCFDIAALELFLPLIKGAHCYICQTEHTKDVEKLKRDIRTIKPTVMQATPA 1398
Cdd:PRK12316   676 RHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPS 755
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1399 twkMLfySGWENEENV-------KILCGGEALPETLKR--YFLDTGSEAWNMFGPTETTI----WSAVQRINDECSratI 1465
Cdd:PRK12316   756 ---ML--QAFLQDEDVasctslrRIVCSGEALPADAQEqvFAKLPQAGLYNLYGPTEAAIdvthWTCVEEGGDSVP---I 827
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1466 GRPIANTQIYITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPFEPGSKLYRTGDMARWLPGGRIEYIGR 1545
Cdd:PRK12316   828 GRPIANLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFVPSPFVAGERMYRTGDLARYRADGVIEYAGR 907
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1546 IDNQVKIRGFRIELGDIESRLSEHPGILECVVVA-DMDNLAAYYTAKHANASLtaRE-LRHFVKNALPAYMVPSYFIQLD 1623
Cdd:PRK12316   908 IDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAvDGKQLVGYVVLESEGGDW--REaLKAHLAASLPEYMVPAQWLALE 985
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1624 HMPLTPNGKIDRNSLKNIDLSGEQlkQRQTSPKN-IQDTVFTIWQEVLKTSDIEWDDGFFDVGGDSLLAVTVADRIKHEl 1702
Cdd:PRK12316   986 RLPLTPNGKLDRKALPAPEASVAQ--QGYVAPRNaLERTLAAIWQDVLGVERVGLDDNFFELGGDSIVSIQVVSRARQA- 1062
                         1050      1060      1070      1080
                   ....*....|....*....|....*....|....*....|...
gi 1776025254 1703 SCEFSVTDLFEYSTIKNISQYI-----TEQRMGNASDHMPTDP 1740
Cdd:PRK12316  1063 GIQLSPRDLFQHQTIRSLALVAkagqaTAADQGPASGEVALAP 1105
PRK12316 PRK12316
peptide synthase; Provisional
647-1736 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 711.73  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  647 AREIHQYPTIERLA-SYLSE------------HEDLSSSSADKKGTDTYKTE----PERSQATFQPLSEVQKGLWTLQKM 709
Cdd:PRK12316  4039 SREMFEEATIQRLAdDYAAEltalvehccdaeRHGVTPSDFPLAGLDQARLDalplPLGEIEDIYPLSPMQQGMLFHSLY 4118
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  710 SPEKSAYHVPLCFKFSsGLHLETLQQAFGLVLNQHPILKH--VIQEKDGVPILKNEPALSIEIKTENISSMK--ESDIPA 785
Cdd:PRK12316  4119 EQEAGDYINQMRVDVQ-GLDVERFRAAWQAALDRHDVLRSgfVWQGELGRPLQVVHKQVSLPFAELDWRGRAdlQAALDA 4197
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  786 FLRKKVKEPYVKENSPLVRVMSFSRSEQEHFLLVVIHHLIFDGVSSVTFIHSLFDTYqlllKGQQPeiAVSPAIYHDFAA 865
Cdd:PRK12316  4198 LAAAERERGFDLQRAPLLRLVLVRTAEGRHHLIYTNHHILMDGWSNSQLLGEVLERY----SGRPP--AQPGGRYRDYIA 4271
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  866 WeknmLAGKDGVKHRTYWQKQLSgtlpNLQLPKVSASSVSEFREDT------YTRRLSSGFMNQVRMFAKEHSVNVTTVF 939
Cdd:PRK12316  4272 W----LQRQDAAASEAFWREQLA----ALDEPTRLAQAIARADLRSangygeHVRELDATATARLREFARTQRVTLNTLV 4343
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  940 LSCYMMLLGRYTGQKEQIVGMPAMVRPEER--FDDAIGHFLNMLPIRSELNPADTFSSFISKLQLTILDGLDHAAYPFPK 1017
Cdd:PRK12316  4344 QAAWLLLLQRYTGQDTVAFGATVAGRPAELpgIEGQIGLFINTLPVIATPRAQQSVVEWLQQVQRQNLALREHEHTPLYE 4423
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1018 MVRDlnipRSQAGSPVFQTAFFYQNF-----LQSGSYQSLlsRYADFFSvdyveyiHQEGEYELVFELwETEEKMELNIK 1092
Cdd:PRK12316  4424 IQRW----AGQGGEALFDSLLVFENYpvseaLQQGAPGGL--RFGEVTN-------HEQTNYPLTLAV-GLGETLSLQFS 4489
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1093 YNTGLFDAASISAMFDHFVYVTEQAMLNPSQPLKEYSLLPEAEKQMILKTWNATGKTYPY-ITFHELFEQQAKKTPDRAA 1171
Cdd:PRK12316  4490 YDRGHFDAATIERLARHLTNLLEAMAEDPQRRLGELQLLEKAEQQRIVALWNRTDAGYPAtRCVHQLVAERARMTPDAVA 4569
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1172 VSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLEDSEV 1251
Cdd:PRK12316  4570 VVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGA 4649
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1252 FITLTTSELVNTL-SWNGVTTALLDQ--DWDEIAQTASDRKvltrtVTPENLAYVIYTSGSTGKPKGVMIPHKALTNFLV 1328
Cdd:PRK12316  4650 ALLLTQSHLLQRLpIPDGLASLALDRdeDWEGFPAHDPAVR-----LHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLH 4724
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1329 SMGETPGLTAEDKMLAVTTYCFDIAALELFLPLIKGAHCYICQTEHTkDVEKLKRDIRTIKPTVMQATPATWKMLFySGW 1408
Cdd:PRK12316  4725 ATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVIRDDSLW-DPERLYAEIHEHRVTVLVFPPVYLQQLA-EHA 4802
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1409 ENEENV----KILCGGEALPETLKRYFLDTGSEA--WNMFGPTETTIWSAVQRI--NDECSRAT--IGRPIANTQIYITD 1478
Cdd:PRK12316  4803 ERDGEPpslrVYCFGGEAVAQASYDLAWRALKPVylFNGYGPTETTVTVLLWKArdGDACGAAYmpIGTPLGNRSGYVLD 4882
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1479 SQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPF-EPGSKLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRI 1557
Cdd:PRK12316  4883 GQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgAPGGRLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRI 4962
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1558 ELGDIESRLSEHPGILECVVVAD----MDNLAAYY---TAKHANASLTARELRHFVKNAL----PAYMVPSYFIQLDHMP 1626
Cdd:PRK12316  4963 ELGEIEARLREHPAVREAVVIAQegavGKQLVGYVvpqDPALADADEAQAELRDELKAALrerlPEYMVPAHLVFLARMP 5042
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1627 LTPNGKIDRNSLKNIDLSgeQLKQRQTSPKN-IQDTVFTIWQEVLKTSDIEWDDGFFDVGGDSLLAVTVADRIKHELSCE 1705
Cdd:PRK12316  5043 LTPNGKLDRKALPQPDAS--LLQQAYVAPRSeLEQQVAAIWAEVLQLERVGLDDNFFELGGHSLLAIQVTSRIQLELGLE 5120
                         1130      1140      1150
                   ....*....|....*....|....*....|.
gi 1776025254 1706 FSVTDLFEYSTIKNISQYITEQRMGNASDHM 1736
Cdd:PRK12316  5121 LPLRELFQTPTLAAFVELAAAAGSGDDEKFD 5151
PKS cd00833
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ...
3339-3776 0e+00

polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different products, called polyketides, by successive decarboxylating Claisen condensations. PKSs can be divided into 2 groups, modular type I PKSs consisting of one or more large multifunctional proteins and iterative type II PKSs, complexes of several monofunctional subunits.


Pssm-ID: 238429 [Multi-domain]  Cd Length: 421  Bit Score: 663.87  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3339 EPVAIVGISGRFPGAMDIDEFWKNLEEGKDSITEVPKDRWDWREHYGNPDTDvNKTDIKWGGFIDGVAEFDPLFFGISPR 3418
Cdd:cd00833      1 EPIAIVGMACRFPGAADPDEFWENLLEGRDAISEIPEDRWDADGYYPDPGKP-GKTYTRRGGFLDDVDAFDAAFFGISPR 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3419 EADYVDPQQRLLMTYVWKALEDAGCPPQSLSGTGTGIFIGTGNTGYKDLFHRANLPIEGHAATGHMIpSVGPNRMSYFLN 3498
Cdd:cd00833     80 EAEAMDPQQRLLLEVAWEALEDAGYSPESLAGSRTGVFVGASSSDYLELLARDPDEIDAYAATGTSR-AFLANRISYFFD 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3499 IHGPSEPVETACSSSLVAIHRAVTAMQNGDCEMAIAGGVNTILTEEAHISYSKAGMLSKDGRCKTFSADANGYVRGEGVG 3578
Cdd:cd00833    159 LRGPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLSPDGRCRPFDADADGYVRGEGVG 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3579 MVMLKKLEDAERDGNHIYGVIRGTAENHGGRANTLTSPNPKAQADLLVRAYRQAGIDPSTVTYIEAHGTGTELGDPIEIN 3658
Cdd:cd00833    239 VVVLKRLSDALRDGDRIYAVIRGSAVNQDGRTKGITAPSGEAQAALIRRAYARAGVDPSDIDYVEAHGTGTPLGDPIEVE 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3659 GLKAAFkelsnmrgeSQPDVPDHRCGIGSVKSNIGHLELAAGISGLIKVLLQMKHKTLVKSLHCETLNPYLQLTDSPFYI 3738
Cdd:cd00833    319 ALAKVF---------GGSRSADQPLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKIDFEESPLRV 389
                          410       420       430
                   ....*....|....*....|....*....|....*...
gi 1776025254 3739 VQEKQEWKSvtdcdgNELPRRAGISSFGIGGVNAHIVI 3776
Cdd:cd00833    390 PTEARPWPA------PAGPRRAGVSSFGFGGTNAHVIL 421
PRK05691 PRK05691
peptide synthase; Validated
160-1725 0e+00

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 658.78  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  160 GLEGFRAIIVEDLLSAEADTdWHQSSP------EDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFN 233
Cdd:PRK05691  1241 RLPQAEGVSAIALDSLHLDS-WPSQAPglhlhgDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQ 1319
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  234 WMP--FDhvggigmLHLRDVYL----GCQEInVSSETILMEPLKWLDWIDHYRASVTwapNFAFGLVTDFAEEikDRKWD 307
Cdd:PRK05691  1320 KAPisFD-------VSVWECFWplitGCRLV-LAGPGEHRDPQRIAELVQQYGVTTL---HFVPPLLQLFIDE--PLAAA 1386
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  308 LSSMRYMLNGGEAMVAKVGRRILELLephglPADAIRPAWGMSETSSGVifSHEFTRAgtsDDDHFVEIGSPIPGFSMRI 387
Cdd:PRK05691  1387 CTSLRRLFSGGEALPAELRNRVLQRL-----PQVQLHNRYGPTETAINV--THWQCQA---EDGERSPIGRPLGNVLCRV 1456
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  388 VNDHNELVEEGEIGRFQVSGLSVTSGYYQRPDLNESVFT-----EDG--WFETGDLG-FLRNGRLTITGRTKDAIIINGI 459
Cdd:PRK05691  1457 LDAELNLLPPGVAGELCIGGAGLARGYLGRPALTAERFVpdplgEDGarLYRTGDRArWNADGALEYLGRLDQQVKLRGF 1536
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  460 NYYSHAIESAVEELSEIETsytAACAVRLGQNSTdQLaIFFVTSAKLNDEQMSQLLRNIQSHVsqvigvtPEYLLPVQ-- 537
Cdd:PRK05691  1537 RVEPEEIQARLLAQPGVAQ---AAVLVREGAAGA-QL-VGYYTGEAGQEAEAERLKAALAAEL-------PEYMVPAQli 1604
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  538 -KEEIPKTAIGKIQRTqlktsfengefdhllhkpnrmndAVQDEEMQQADHVKRvREEIQEHLLTCLTEELHVSRdwVEP 616
Cdd:PRK05691  1605 rLDQMPLGPSGKLDRR-----------------------ALPEPVWQQREHVEP-RTELQQQIAAIWREVLGLPR--VGL 1658
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  617 NANIQSLGVNSIKMMKLIRSIEKNYHIKLTAREIHQYptiERLASYLSEHEDLSSSSADKKGTDTYKTEpeRSQATfqPL 696
Cdd:PRK05691  1659 RDDFFALGGHSLLATQIVSRTRQACDVELPLRALFEA---SELGAFAEQVARIQAAGERNSQGAIARVD--RSQPV--PL 1731
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  697 SEVQKGLWTLQKMSPEKSAYHVPLCFKFSSGLHLETLQQAFGLVLNQHPILKHVIQEKDGVPILKNEPALSIEIKTENIS 776
Cdd:PRK05691  1732 SYSQQRMWFLWQMEPDSPAYNVGGMARLSGVLDVDRFEAALQALILRHETLRTTFPSVDGVPVQQVAEDSGLRMDWQDFS 1811
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  777 SM----KESDIPAFLRKKVKEPYVKENSPLVRVMSFSRSEQEHFLLVVIHHLIFDGVSSVTFIHSLFDTYQLLLKGQQPE 852
Cdd:PRK05691  1812 ALpadaRQQRLQQLADSEAHQPFDLERGPLLRACLVKAAEREHYFVLTLHHIVTEGWAMDIFARELGALYEAFLDDRESP 1891
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  853 IAVSPAIYHDFAAWEKNMLAGKDGVKHRTYWQKQLSGTLPNLQLP-KVSASSVSEFREDTYTRRLSSGFMNQVRMFAKEH 931
Cdd:PRK05691  1892 LEPLPVQYLDYSVWQRQWLESGERQRQLDYWKAQLGNEHPLLELPaDRPRPPVQSHRGELYRFDLSPELAARVRAFNAQR 1971
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  932 SVNVTTVFLSCYMMLLGRYTGQKEQIVGMPAM--VRPEErfDDAIGHFLNMLPIRSELNPADTFSSFISKLQLTILDGLD 1009
Cdd:PRK05691  1972 GLTLFMTMTATLAALLYRYSGQRDLRIGAPVAnrIRPES--EGLIGAFLNTQVLRCQLDGQMSVSELLEQVRQTVIEGQS 2049
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1010 HAAYPFPKMVRDLNIPRSQAGSPVFQTAFFYQNFlqsgSYQSllSRYADFFSVDYVEYIHQEGEYELVFELWETEEKMEL 1089
Cdd:PRK05691  2050 HQDLPFDHLVEALQPPRSAAYNPLFQVMCNVQRW----EFQQ--SRQLAGMTVEYLVNDARATKFDLNLEVTDLDGRLGC 2123
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1090 NIKYNTGLFDAASISAMFDHFVYVTEQAMLNPSQPLKEYSLLPEAEKQMILKTWNAT-GKTYPYITFHELFEQQAKKTPD 1168
Cdd:PRK05691  2124 CLTYSRDLFDEPRIARMAEHWQNLLEALLGDPQQRLAELPLLAAAEQQQLLDSLAGEaGEARLDQTLHGLFAAQAARTPQ 2203
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1169 RAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLED 1248
Cdd:PRK05691  2204 APALTFAGQTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIED 2283
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1249 SEVFITLTTSELVNTLSW--NGVTTALLDQDWDEIAQTASDRkvLTRTVTPENLAYVIYTSGSTGKPKGVMIPHKALTNF 1326
Cdd:PRK05691  2284 SGIGLLLSDRALFEALGElpAGVARWCLEDDAAALAAYSDAP--LPFLSLPQHQAYLIYTSGSTGKPKGVVVSHGEIAMH 2361
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1327 LVSMGETPGLTAEDKMLAVTTYCFDIAALELFLPLIKGAHCyICQTEHTKDVEKLKRDIRTIKPTVMQATPATWKMLF-Y 1405
Cdd:PRK05691  2362 CQAVIERFGMRADDCELHFYSINFDAASERLLVPLLCGARV-VLRAQGQWGAEEICQLIREQQVSILGFTPSYGSQLAqW 2440
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1406 SGWENEENVKILC--GGEAL-PETLKRYFLDTGSEA-WNMFGPTETTIWS----AVQRINDECSRATIGRPIANTQIYIT 1477
Cdd:PRK05691  2441 LAGQGEQLPVRMCitGGEALtGEHLQRIRQAFAPQLfFNAYGPTETVVMPlaclAPEQLEEGAASVPIGRVVGARVAYIL 2520
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1478 DSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPFEP-GSKLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFR 1556
Cdd:PRK05691  2521 DADLALVPQGATGELYVGGAGLAQGYHDRPGLTAERFVADPFAAdGGRLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFR 2600
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1557 IELGDIESRLSEHPGILECVVVAdMDN-----LAAYYTAKHANASLTA----RE-LRHFVKNALPAYMVPSYFIQLDHMP 1626
Cdd:PRK05691  2601 IELGEIESRLLEHPAVREAVVLA-LDTpsgkqLAGYLVSAVAGQDDEAqaalREaLKAHLKQQLPDYMVPAHLILLDSLP 2679
                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1627 LTPNGKIDRNSLKNIDLsgEQLKQRQTSPKN-IQDTVFTIWQEVLKTSDIEWDDGFFDVGGDSLLAVTVADRIKhELSCE 1705
Cdd:PRK05691  2680 LTANGKLDRRALPAPDP--ELNRQAYQAPRSeLEQQLAQIWREVLNVERVGLGDNFFELGGDSILSIQVVSRAR-QLGIH 2756
                         1610      1620
                   ....*....|....*....|
gi 1776025254 1706 FSVTDLFEYSTIKNISQYIT 1725
Cdd:PRK05691  2757 FSPRDLFQHQTVQTLAAVAT 2776
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
1759-2291 0e+00

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 644.62  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1759 DDSVAIIGISCEFPGAKNHDEFWENLRDGKESIAFFNKEEL--QRFGISKEIAENADYVPAKASIEGKDRFDPSFFQISP 1836
Cdd:COG3321      3 DEPIAIIGMACRFPGADDPEEFWRNLRAGRDAITEVPADRWdaDAYYDPDPDAPGKTYVRWGGFLDDVDEFDALFFGISP 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1837 KDAEFMDPQLRMLLTHSWKAIEDAGYAAGQIP--QTSVFMSASNNSYRALLPSDttesLETPDGYVSWVLAQSgTIPTMI 1914
Cdd:COG3321     83 REAEAMDPQQRLLLEVAWEALEDAGYDPESLAgsRTGVFVGASSNDYALLLLAD----PEAIDAYALTGNAKS-VLAGRI 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1915 SHKLGLRGPSYFVHANCSSSLIGLHSAYKSLLSAESDYALVGGATLHTESNIGYVHQPGLNFSSDGHIKAFDASADGMIG 1994
Cdd:COG3321    158 SYKLDLRGPSVTVDTACSSSLVAVHLACQSLRSGECDLALAGGVNLMLTPESFILFSKGGMLSPDGRCRAFDADADGYVR 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1995 GEGVAVVLLKKAADAVKDGDHIYALLRGIGVNNDGADKvGFYAPSVKGQADVVQQVMNQTKIHPESICYVEAHGTGTKLG 2074
Cdd:COG3321    238 GEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRSN-GLTAPNGPAQAAVIRRALADAGVDPATVDYVEAHGTGTPLG 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2075 DPIELAALTNVYRQYTNKTQFCGIGSVKTNIGHLDTAAGLAGCIKVVMSLYHQELAPSINYKEPNPNTDLASSPFYVVDQ 2154
Cdd:COG3321    317 DPIEAAALTAAFGQGRPADQPCAIGSVKSNIGHLEAAAGVAGLIKAVLALRHGVLPPTLHFETPNPHIDFENSPFYVNTE 396
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2155 KKTLSREIQTHRAALSSFGLGGTNTHAIFEQF--KRDSDKGKIDGTCIVPISAKNKERLQEYAEDILAYLERRGLENsqL 2232
Cdd:COG3321    397 LRPWPAGGGPRRAGVSSFGFGGTNAHVVLEEApaAAPAAAAAARPPQLLVLSAKTEEALRALAARLAAFLEAHPDLD--L 474
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1776025254 2233 PDFAYTLQVGREAMEHRVVFIADHVNELKQRLTDFINGKTAiEGCFQGSKHNAREVSWL 2291
Cdd:COG3321    475 ADVAYTLATGRAHFEHRLAVVASSREELAAKLRALAAGEAA-PGVVTGAAAAAPKVAFL 532
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
1167-1638 0e+00

The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341253 [Multi-domain]  Cd Length: 444  Bit Score: 599.90  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1167 PDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYML 1246
Cdd:cd05930      1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1247 EDSEVFITLTTselvntlswngvttalldqdwdeiaqtasdrkvltrtvtPENLAYVIYTSGSTGKPKGVMIPHKALTNF 1326
Cdd:cd05930     81 EDSGAKLVLTD---------------------------------------PDDLAYVIYTSGSTGKPKGVMVEHRGLVNL 121
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1327 LVSMGETPGLTAEDKMLAVTTYCFDIAALELFLPLIKGAHCYICQTEHTKDVEKLKRDIRTIKPTVMQATPATWKMLF-Y 1405
Cdd:cd05930    122 LLWMQEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLRLLLqE 201
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1406 SGWENEENVKIL-CGGEALPETLKRYFLDTGSEA--WNMFGPTETTIWSAVQRINDEC---SRATIGRPIANTQIYITDS 1479
Cdd:cd05930    202 LELAALPSLRLVlVGGEALPPDLVRRWRELLPGArlVNLYGPTEATVDATYYRVPPDDeedGRVPIGRPIPNTRVYVLDE 281
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1480 QLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPFEPGSKLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIEL 1559
Cdd:cd05930    282 NLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIEL 361
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1560 GDIESRLSEHPGILECVVVADMDN-----LAAYYTAKHANAsLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKID 1634
Cdd:cd05930    362 GEIEAALLAHPGVREAAVVAREDGdgekrLVAYVVPDEGGE-LDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVD 440

                   ....
gi 1776025254 1635 RNSL 1638
Cdd:cd05930    441 RKAL 444
A_NRPS_Bac cd17655
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...
1157-1638 1.27e-178

bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341310 [Multi-domain]  Cd Length: 490  Bit Score: 559.25  E-value: 1.27e-178
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1157 ELFEQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPS 1236
Cdd:cd17655      1 ELFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1237 YPAERLEYMLEDSEVFITLTTSELVNTLSWNGVTTALLDQDWDEiaQTASDrkvLTRTVTPENLAYVIYTSGSTGKPKGV 1316
Cdd:cd17655     81 YPEERIQYILEDSGADILLTQSHLQPPIAFIGLIDLLDEDTIYH--EESEN---LEPVSKSDDLAYVIYTSGSTGKPKGV 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1317 MIPHKALTNFLVSMGETPGLTAEDKMLAVTTYCFDIAALELFLPLIKGAHCYICQTEHTKDVEKLKRDIRTIKPTVMQAT 1396
Cdd:cd17655    156 MIEHRGVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQALTQYIRQNRITIIDLT 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1397 PATWKMLFYSGWENEENVK-ILCGGEALPETLKRYFLD---TGSEAWNMFGPTETTIWSAVQRINDECSRAT---IGRPI 1469
Cdd:cd17655    236 PAHLKLLDAADDSEGLSLKhLIVGGEALSTELAKKIIElfgTNPTITNAYGPTETTVDASIYQYEPETDQQVsvpIGKPL 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1470 ANTQIYITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPFEPGSKLYRTGDMARWLPGGRIEYIGRIDNQ 1549
Cdd:cd17655    316 GNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVPGERMYRTGDLARWLPDGNIEFLGRIDHQ 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1550 VKIRGFRIELGDIESRLSEHPGILECVVVA--DMDN---LAAYYTakhANASLTARELRHFVKNALPAYMVPSYFIQLDH 1624
Cdd:cd17655    396 VKIRGYRIELGEIEARLLQHPDIKEAVVIArkDEQGqnyLCAYIV---SEKELPVAQLREFLARELPDYMIPSYFIKLDE 472
                          490
                   ....*....|....
gi 1776025254 1625 MPLTPNGKIDRNSL 1638
Cdd:cd17655    473 IPLTPNGKVDRKAL 486
A_NRPS_Srf_like cd12117
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...
1157-1638 5.54e-178

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.


Pssm-ID: 341282 [Multi-domain]  Cd Length: 483  Bit Score: 557.20  E-value: 5.54e-178
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1157 ELFEQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPS 1236
Cdd:cd12117      1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1237 YPAERLEYMLEDSEVFITLTTSELVNTLSwNGVTTALLDQDWDeiaqtASDRKVLTRTVTPENLAYVIYTSGSTGKPKGV 1316
Cdd:cd12117     81 LPAERLAFMLADAGAKVLLTDRSLAGRAG-GLEVAVVIDEALD-----AGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGV 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1317 MIPHKALTNfLVSMGETPGLTAEDKMLAVTTYCFDIAALELFLPLIKGAHCYICQTEHTKDVEKLKRDIRTIKPTVMQAT 1396
Cdd:cd12117    155 AVTHRGVVR-LVKNTNYVTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPDALGALIAEEGVTVLWLT 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1397 PATWKMLFysgwenEENV-------KILCGGEALPETLKRYFLDT--GSEAWNMFGPTETTIWSAVQRINDECSRAT--- 1464
Cdd:cd12117    234 AALFNQLA------DEDPecfaglrELLTGGEVVSPPHVRRVLAAcpGLRLVNGYGPTENTTFTTSHVVTELDEVAGsip 307
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1465 IGRPIANTQIYITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPFEPGSKLYRTGDMARWLPGGRIEYIG 1544
Cdd:cd12117    308 IGRPIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFGPGERLYRTGDLARWLPDGRLEFLG 387
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1545 RIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMDN-----LAAYYTAKHAnasLTARELRHFVKNALPAYMVPSYF 1619
Cdd:cd12117    388 RIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAggdkrLVAYVVAEGA---LDAAELRAFLRERLPAYMVPAAF 464
                          490
                   ....*....|....*....
gi 1776025254 1620 IQLDHMPLTPNGKIDRNSL 1638
Cdd:cd12117    465 VVLDELPLTANGKVDRRAL 483
PKS cd00833
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ...
1760-2182 1.36e-171

polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different products, called polyketides, by successive decarboxylating Claisen condensations. PKSs can be divided into 2 groups, modular type I PKSs consisting of one or more large multifunctional proteins and iterative type II PKSs, complexes of several monofunctional subunits.


Pssm-ID: 238429 [Multi-domain]  Cd Length: 421  Bit Score: 535.99  E-value: 1.36e-171
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1760 DSVAIIGISCEFPGAKNHDEFWENLRDGKESIAFFNKEELQRFGI-SKEIAENADYVPAKASIEGKDRFDPSFFQISPKD 1838
Cdd:cd00833      1 EPIAIVGMACRFPGAADPDEFWENLLEGRDAISEIPEDRWDADGYyPDPGKPGKTYTRRGGFLDDVDAFDAAFFGISPRE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1839 AEFMDPQLRMLLTHSWKAIEDAGYAAGQIP--QTSVFMSASNNSYRALLPSDttesLETPDGYVSWVLAQSgTIPTMISH 1916
Cdd:cd00833     81 AEAMDPQQRLLLEVAWEALEDAGYSPESLAgsRTGVFVGASSSDYLELLARD----PDEIDAYAATGTSRA-FLANRISY 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1917 KLGLRGPSYFVHANCSSSLIGLHSAYKSLLSAESDYALVGGATLHTESNIGYVHQPGLNFSSDGHIKAFDASADGMIGGE 1996
Cdd:cd00833    156 FFDLRGPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLSPDGRCRPFDADADGYVRGE 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1997 GVAVVLLKKAADAVKDGDHIYALLRGIGVNNDGADKVGfYAPSVKGQADVVQQVMNQTKIHPESICYVEAHGTGTKLGDP 2076
Cdd:cd00833    236 GVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRTKGI-TAPSGEAQAALIRRAYARAGVDPSDIDYVEAHGTGTPLGDP 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2077 IELAALTNVYRQYTNKTQFCGIGSVKTNIGHLDTAAGLAGCIKVVMSLYHQELAPSINYKEPNPNTDLASSPFYVVDQKK 2156
Cdd:cd00833    315 IEVEALAKVFGGSRSADQPLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKIDFEESPLRVPTEAR 394
                          410       420
                   ....*....|....*....|....*.
gi 1776025254 2157 TLSREIQTHRAALSSFGLGGTNTHAI 2182
Cdd:cd00833    395 PWPAPAGPRRAGVSSFGFGGTNAHVI 420
PRK12316 PRK12316
peptide synthase; Provisional
695-1739 1.53e-171

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 601.18  E-value: 1.53e-171
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  695 PLSEVQKGLWTLQKMSPEKSAY----HVPLCfkfssGLHLETLQQAFGLVLNQHPILKHVIQEKDGVP----ILKNEPAL 766
Cdd:PRK12316  1558 PLSPMQQGMLFHSLYEQEAGDYinqlRVDVQ-----GLDPDRFRAAWQATVDRHEILRSGFLWQDGLEqplqVIHKQVEL 1632
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  767 SIEIKTENISSMKESDIPAFLRKKVKEPYVKENSPLVRVMSFSRSEQEHFLLVVIHHLIFDGVSSVTFIHSLFDTYqlll 846
Cdd:PRK12316  1633 PFAELDWRGREDLGQALDALAQAERQKGFDLTRAPLLRLVLVRTGEGRHHLIYTNHHILMDGWSNAQLLGEVLQRY---- 1708
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  847 KGQQPEIAVSPaiYHDFAAWeknmLAGKDGVKHRTYWQKQLSGTLPNLQLPKVSASSVSEFREDTYTRRLSSGFMNQVRM 926
Cdd:PRK12316  1709 AGQPVAAPGGR--YRDYIAW----LQRQDAAASEAFWKEQLAALEEPTRLAQAARTEDGQVGYGDHQQLLDPAQTRALAE 1782
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  927 FAKEHSVNVTTVFLSCYMMLLGRYTGQKEQIVGMPAMVRPEER--FDDAIGHFLNMLPIRSELNPADTFSSFISKLQLTI 1004
Cdd:PRK12316  1783 FARAQKVTLNTLVQAAWLLLLQRYTGQETVAFGATVAGRPAELpgIEQQIGLFINTLPVIAAPRPDQSVADWLQEVQALN 1862
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1005 LDGLDHAAYPFpkmvrdLNIPR--SQAGSPVFQTAFFYQNF-----LQSGSYQSL-LSRYADffsvdyveyiHQEGEYEL 1076
Cdd:PRK12316  1863 LALREHEHTPL------YDIQRwaGQGGEALFDSLLVFENYpvaeaLKQGAPAGLvFGRVSN----------HEQTNYPL 1926
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1077 VFELwETEEKMELNIKYNTGLFDAASISAMFDHFVYVTEQAMLNPSQPLKEYSLLPEAEKQMILKTWNATGKTYPY-ITF 1155
Cdd:PRK12316  1927 TLAV-TLGETLSLQYSYDRGHFDAAAIERLDRHLLHLLEQMAEDAQAALGELALLDAGERQRILADWDRTPEAYPRgPGV 2005
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1156 HELFEQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDP 1235
Cdd:PRK12316  2006 HQRIAEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDP 2085
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1236 SYPAERLEYMLEDSEVFITLTTSELVNTLSW-NGVTTALLDQ--DWDEIAQTASDRKvltrtVTPENLAYVIYTSGSTGK 1312
Cdd:PRK12316  2086 NYPAERLAYMLEDSGAALLLTQRHLLERLPLpAGVARLPLDRdaEWADYPDTAPAVQ-----LAGENLAYVIYTSGSTGL 2160
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1313 PKGVMIPHKALTNFLVSMGETPGLTAEDKMLAVTTYCFDIAALELFLPLIKGAHCYICQTEHtKDVEKLKRDIRTIKPTV 1392
Cdd:PRK12316  2161 PKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAHEQWFHPLLNGARVLIRDDEL-WDPEQLYDEMERHGVTI 2239
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1393 MQATPATWKMLFysgwENEE------NVKILC-GGEALP-ETLKRYFLDTGSEAW-NMFGPTETTI----WSAvqRINDE 1459
Cdd:PRK12316  2240 LDFPPVYLQQLA----EHAErdgrppAVRVYCfGGEAVPaASLRLAWEALRPVYLfNGYGPTEAVVtpllWKC--RPQDP 2313
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1460 CSRAT--IGRPIANTQIYITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPFE-PGSKLYRTGDMARWLP 1536
Cdd:PRK12316  2314 CGAAYvpIGRALGNRRAYILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFSaSGERLYRTGDLARYRA 2393
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1537 GGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADM----DNLAAYYTAKHAnASLTARELRHFVKNALPA 1612
Cdd:PRK12316  2394 DGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQDgasgKQLVAYVVPDDA-AEDLLAELRAWLAARLPA 2472
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1613 YMVPSYFIQLDHMPLTPNGKIDRNSLKNIDLSgeQLKQRQTSPKN-IQDTVFTIWQEVLKTSDIEWDDGFFDVGGDSLLA 1691
Cdd:PRK12316  2473 YMVPAHWVVLERLPLNPNGKLDRKALPKPDVS--QLRQAYVAPQEgLEQRLAAIWQAVLKVEQVGLDDHFFELGGHSLLA 2550
                         1050      1060      1070      1080
                   ....*....|....*....|....*....|....*....|....*...
gi 1776025254 1692 VTVADRIKHELSCEFSVTDLFEYSTIKNISQYITEQRMGNASDHMPTD 1739
Cdd:PRK12316  2551 TQVVSRVRQDLGLEVPLRILFERPTLAAFAASLESGQTSRAPVLQKVT 2598
PRK12467 PRK12467
peptide synthase; Provisional
727-1724 2.66e-170

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 596.37  E-value: 2.66e-170
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  727 GLHLETLQQAFGLVLNQHPILK-------------HVIQEKDGVPIL----KNEPALSIEIKTENISSMKESdipaflrk 789
Cdd:PRK12467  2679 GLDVERFRTAWQAVIDRHEILRsgflwdgeleeplQVVYKQARLPFSrldwRDRADLEQALDALAAADRQQG-------- 2750
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  790 kvkepYVKENSPLVRVMSFSRSEQEHFLLVVIHHLIFDGVSSVTFIHSLFDTYqlllKGQQPeiAVSPAIYHDFAAWekn 869
Cdd:PRK12467  2751 -----FDLLSAPLLRLTLVRTGEDRHHLIYTNHHILMDGWSGSQLLGEVLQRY----FGQPP--PAREGRYRDYIAW--- 2816
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  870 mLAGKDGVKHRTYWQKQLSgtlpNLQLPKVSASSVS-------EFREDTYtRRLSSGFMNQVRMFAKEHSVNVTTVFLSC 942
Cdd:PRK12467  2817 -LQAQDAEASEAFWKEQLA----ALEEPTRLARALYpapaeavAGHGAHY-LHLDATQTRQLIEFARRHRVTLNTLVQGA 2890
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  943 YMMLLGRYTGQKEQIVGMPAMVRPEER--FDDAIGHFLNMLPIRSELNPADTFSSFISKLQLTILDGLDHAAYPFpkmvr 1020
Cdd:PRK12467  2891 WLLLLQRFTGQDTVCFGATVAGRPAQLrgAEQQLGLFINTLPVIASPRAEQTVSDWLQQVQAQNLALREFEHTPL----- 2965
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1021 dLNIPR--SQAGSPVFQTAFFYQNF-----LQSGSYQSLlsRYADFFSVDYVEYihqegEYELVFELWETeekMELNIKY 1093
Cdd:PRK12467  2966 -ADIQRwaGQGGEALFDSILVFENYpiseaLKQGAPSGL--RFGAVSSREQTNY-----PLTLAVGLGDT---LELEFSY 3034
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1094 NTGLFDAASISAMFDHFVYVTEQAMLNPSQPLKEYSLLPEAEKQMILKTWNATGKTYP-YITFHELFEQQAKKTPDRAAV 1172
Cdd:PRK12467  3035 DRQHFDAAAIERLAESFDRLLQAMLNNPAARLGELPTLAAHERRQVLHAWNATAAAYPsERLVHQLIEAQVARTPEAPAL 3114
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1173 SYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLEDSEVF 1252
Cdd:PRK12467  3115 VFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVK 3194
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1253 ITLTTSELVNTLSW-NGVTTALLDQD--WDEiaqtaSDRKVLTRtVTPENLAYVIYTSGSTGKPKGVMIPHKALTNFLVS 1329
Cdd:PRK12467  3195 LLLTQAHLLEQLPApAGDTALTLDRLdlNGY-----SENNPSTR-VMGENLAYVIYTSGSTGKPKGVGVRHGALANHLCW 3268
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1330 MGETPGLTAEDKMLAVTTYCFDIAALELFLPLIKGAhCYICQTEHTKDVEKLKRDIRTIKPTVMQATPATWKML--FYSG 1407
Cdd:PRK12467  3269 IAEAYELDANDRVLLFMSFSFDGAQERFLWTLICGG-CLVVRDNDLWDPEELWQAIHAHRISIACFPPAYLQQFaeDAGG 3347
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1408 WENEENVKILCGGEALP----ETLKRYFLDTGseAWNMFGPTETTI----WSAVQRINDECSRATIGRPIANTQIYITDS 1479
Cdd:PRK12467  3348 ADCASLDIYVFGGEAVPpaafEQVKRKLKPRG--LTNGYGPTEAVVtvtlWKCGGDAVCEAPYAPIGRPVAGRSIYVLDG 3425
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1480 QLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPFE-PGSKLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIE 1558
Cdd:PRK12467  3426 QLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVADPFSgSGGRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIE 3505
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1559 LGDIESRLSEHPGILECVVVA-DMDN---LAAYYTAKHANASLtARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKID 1634
Cdd:PRK12467  3506 LGEIEARLLQHPSVREAVVLArDGAGgkqLVAYVVPADPQGDW-RETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVD 3584
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1635 RNSLKNIDLsgeQLKQRQTSPKN-IQDTVFTIWQEVLKTSDIEWDDGFFDVGGDSLLAVTVADRIKHELSCEFSVTDLFE 1713
Cdd:PRK12467  3585 RKALPDPDA---KGSREYVAPRSeVEQQLAAIWADVLGVEQVGVTDNFFELGGDSLLALQVLSRIRQSLGLKLSLRDLMS 3661
                         1050
                   ....*....|.
gi 1776025254 1714 YSTIKNISQYI 1724
Cdd:PRK12467  3662 APTIAELAGYS 3672
A_NRPS_AB3403-like cd17646
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ...
1156-1638 2.72e-169

Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341301 [Multi-domain]  Cd Length: 488  Bit Score: 532.24  E-value: 2.72e-169
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1156 HELFEQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDP 1235
Cdd:cd17646      1 HALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1236 SYPAERLEYMLEDSEVFITLTTSELVNTLSwnGVTTALLDQDWDEIAQTASDRKVLTRtvtPENLAYVIYTSGSTGKPKG 1315
Cdd:cd17646     81 GYPADRLAYMLADAGPAVVLTTADLAARLP--AGGDVALLGDEALAAPPATPPLVPPR---PDNLAYVIYTSGSTGRPKG 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1316 VMIPHKALTNFLVSMGETPGLTAEDKMLAVTTYCFDIAALELFLPLIKGAHCYICQTEHTKDVEKLKRDIRTIKPTVMQA 1395
Cdd:cd17646    156 VMVTHAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDPAYLAALIREHGVTTCHF 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1396 TPAtwkML--FY-----SGWENEENVkiLCGGEALP-ETLKRYFLDTGSEAWNMFGPTETTI----WSAvqRINDECSRA 1463
Cdd:cd17646    236 VPS---MLrvFLaepaaGSCASLRRV--FCSGEALPpELAARFLALPGAELHNLYGPTEAAIdvthWPV--RGPAETPSV 308
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1464 TIGRPIANTQIYITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPFEPGSKLYRTGDMARWLPGGRIEYI 1543
Cdd:cd17646    309 PIGRPVPNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFGPGSRMYRTGDLARWRPDGALEFL 388
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1544 GRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMDN-----LAAYYTAKHANASLTARELRHFVKNALPAYMVPSY 1618
Cdd:cd17646    389 GRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPagaarLVGYVVPAAGAAGPDTAALRAHLAERLPEYMVPAA 468
                          490       500
                   ....*....|....*....|
gi 1776025254 1619 FIQLDHMPLTPNGKIDRNSL 1638
Cdd:cd17646    469 FVVLDALPLTANGKLDRAAL 488
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
695-1727 1.29e-165

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 551.57  E-value: 1.29e-165
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  695 PLSEVQKGLWTLQKMSPEKSAYHVPLCFKFSSGLHLETLQQAFGLVLNQHPILKHVIQEKDGVPILKNEPALSIEikTEN 774
Cdd:PRK10252     9 PLVAAQPGIWMAEKLSPLPSAWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFTEDNGEVWQWVDPALTFP--LPE 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  775 ISSMKESDIP-----AFLRKKVKEPY-VKENSPLVRVMSFSRSEQEHFLLVVIHHLIFDGVSSVTFIHSLFDTYQLLLKG 848
Cdd:PRK10252    87 IIDLRTQPDPhaaaqALMQADLQQDLrVDSGKPLVFHQLIQLGDNRWYWYQRYHHLLVDGFSFPAITRRIAAIYCAWLRG 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  849 QQ-PEIAVSP--AIYHDFAAWEKNMLAGKDGvkhrTYWQKQLSGTLPNLQL---PKVSASSVSEFREDTytRRLSSGFMn 922
Cdd:PRK10252   167 EPtPASPFTPfaDVVEEYQRYRASEAWQRDA----AFWAEQRRQLPPPASLspaPLPGRSASADILRLK--LEFTDGAF- 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  923 qVRMFAKEHSVNVTTVFLSCYMMLLGRYTGQKEQIVGMPAMVRPEERFDDAIGHFLNMLPIRSELNPADTFSSFISKLQL 1002
Cdd:PRK10252   240 -RQLAAQASGVQRPDLALALVALWLGRLCGRMDYAAGFIFMRRLGSAALTATGPVLNVLPLRVHIAAQETLPELATRLAA 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1003 TILDGLDHAAYPFPKMVRDLNipRSQAGSPVFQTAFFYQNFlqsgSYQsllsryADFFSVDYVEYIHQEG---EYELVFE 1079
Cdd:PRK10252   319 QLKKMRRHQRYDAEQIVRDSG--RAAGDEPLFGPVLNIKVF----DYQ------LDFPGVQAQTHTLATGpvnDLELALF 386
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1080 LwETEEKMELNIKYNTGLFDAASISAMFDHFVYVTEQAMLNPSQPLKEYSLLPEAEKQMiLKTWNATGKTYPYITFHELF 1159
Cdd:PRK10252   387 P-DEHGGLSIEILANPQRYDEATLIAHAERLKALIAQFAADPALLCGDVDILLPGEYAQ-LAQVNATAVEIPETTLSALV 464
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1160 EQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPA 1239
Cdd:PRK10252   465 AQQAAKTPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPD 544
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1240 ERLEYMLEDSEVFITLTTSELVNTLSWNGVTTALLDQDWdeiaQTASDRKVLTRTvTPENLAYVIYTSGSTGKPKGVMIP 1319
Cdd:PRK10252   545 DRLKMMLEDARPSLLITTADQLPRFADVPDLTSLCYNAP----LAPQGAAPLQLS-QPHHTAYIIFTSGSTGRPKGVMVG 619
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1320 HKALTNFLVSMGETPGLTAEDKMLAVTTYCFDIAALELFLPLIKGAHCYICQTEHTKDVEKLKRDIRTIKPTVMQATPAt 1399
Cdd:PRK10252   620 QTAIVNRLLWMQNHYPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTTHFVPS- 698
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1400 wkML--FYSGWENEENVK-------ILCGGEALPETLKRYFLD-TGSEAWNMFGPTET----TIWSAVQRINDECSRAT- 1464
Cdd:PRK10252   699 --MLaaFVASLTPEGARQscaslrqVFCSGEALPADLCREWQQlTGAPLHNLYGPTEAavdvSWYPAFGEELAAVRGSSv 776
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1465 -IGRPIANTQIYITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPFEPGSKLYRTGDMARWLPGGRIEYI 1543
Cdd:PRK10252   777 pIGYPVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPGERMYRTGDVARWLDDGAVEYL 856
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1544 GRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVA-----------DMDNLAAYYTAkHANASLTARELRHFVKNALPA 1612
Cdd:PRK10252   857 GRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVTHAcvinqaaatggDARQLVGYLVS-QSGLPLDTSALQAQLRERLPP 935
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1613 YMVPSYFIQLDHMPLTPNGKIDRNSLKNIDLSGeQLKQRqtSPKNIQDT-VFTIWQEVLKTSDIEWDDGFFDVGGDSLLA 1691
Cdd:PRK10252   936 HMVPVVLLQLDQLPLSANGKLDRKALPLPELKA-QVPGR--APKTGTETiIAAAFSSLLGCDVVDADADFFALGGHSLLA 1012
                         1050      1060      1070
                   ....*....|....*....|....*....|....*.
gi 1776025254 1692 VTVADRIKHELSCEFSVTDLFEYSTIKNISQYITEQ 1727
Cdd:PRK10252  1013 MKLAAQLSRQFARQVTPGQVMVASTVAKLATLLDAE 1048
A_NRPS_ApnA-like cd17644
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ...
1154-1638 3.94e-159

similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341299 [Multi-domain]  Cd Length: 465  Bit Score: 502.35  E-value: 3.94e-159
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1154 TFHELFEQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPL 1233
Cdd:cd17644      1 CIHQLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1234 DPSYPAERLEYMLEDSEVFITLTTselvntlswngvttalldqdwdeiaqtasdrkvltrtvtPENLAYVIYTSGSTGKP 1313
Cdd:cd17644     81 DPNYPQERLTYILEDAQISVLLTQ---------------------------------------PENLAYVIYTSGSTGKP 121
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1314 KGVMIPHKALTNFLVSMGETPGLTAEDKMLAVTTYCFDIAALELFLPLIKGAHCYICQTEHTKDVEKLKRDIRTIKPTVM 1393
Cdd:cd17644    122 KGVMIEHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEDFVQYIQQWQLTVL 201
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1394 QATPATWKMLFYSGWENEENV-----KILCGGEA-LPETLKRYFLDTGS--EAWNMFGPTETTIWSAVQRINDECSRA-- 1463
Cdd:cd17644    202 SLPPAYWHLLVLELLLSTIDLpsslrLVIVGGEAvQPELVRQWQKNVGNfiQLINVYGPTEATIAATVCRLTQLTERNit 281
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1464 --TIGRPIANTQIYITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPFE--PGSKLYRTGDMARWLPGGR 1539
Cdd:cd17644    282 svPIGRPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNssESERLYKTGDLARYLPDGN 361
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1540 IEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMDN-----LAAYYTAkHANASLTARELRHFVKNALPAYM 1614
Cdd:cd17644    362 IEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQpgnkrLVAYIVP-HYEESPSTVELRQFLKAKLPDYM 440
                          490       500
                   ....*....|....*....|....
gi 1776025254 1615 VPSYFIQLDHMPLTPNGKIDRNSL 1638
Cdd:cd17644    441 IPSAFVVLEELPLTPNGKIDRRAL 464
PKS_KS smart00825
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ...
3341-3778 4.30e-157

Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the thiolase family and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.


Pssm-ID: 214836 [Multi-domain]  Cd Length: 298  Bit Score: 488.76  E-value: 4.30e-157
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  3341 VAIVGISGRFPGAMDIDEFWKNLEEGkdsitevpkdrwdwrehygnpdtdvnktdikwggfIDGVAEFDPLFFGISPREA 3420
Cdd:smart00825    1 IAIVGMSCRFPGADDPEEFWDLLLAG-----------------------------------LDDVDLFDAAFFGISPREA 45
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  3421 DYVDPQQRLLMTYVWKALEDAGCPPQSLSGTGTGIFIGTGNTGYkdlfhranlpieghaatghmipsvgpnrmsyflnih 3500
Cdd:smart00825   46 EAMDPQQRLLLEVAWEALEDAGIDPESLRGSRTGVFVGVSSSDY------------------------------------ 89
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  3501 gpSEPVETACSSSLVAIHRAVTAMQNGDCEMAIAGGVNTILTEEAHISYSKAGMLSKDGRCKTFSADANGYVRGEGVGMV 3580
Cdd:smart00825   90 --SVTVDTACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLSPDGRCKTFDASADGYVRGEGVGVV 167
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  3581 MLKKLEDAERDGNHIYGVIRGTAENHGGRANTLTSPNPKAQadllvrayrqagidpstvtyieahgtgtelgdpieingl 3660
Cdd:smart00825  168 VLKRLSDALRDGDPILAVIRGSAVNQDGRSNGITAPSGPAQ--------------------------------------- 208
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  3661 kaafkelsnmrgesqpdvpdhrCGIGSVKSNIGHLELAAGISGLIKVLLQMKHKTLVKSLHCETLNPYLQLTDSPFYIVQ 3740
Cdd:smart00825  209 ----------------------LLIGSVKSNIGHLEAAAGVAGLIKVVLALKHGVIPPTLHFETPNPHIDLEESPLRVPT 266
                           410       420       430
                    ....*....|....*....|....*....|....*...
gi 1776025254  3741 EKQEWksvtdcDGNELPRRAGISSFGIGGVNAHIVIEE 3778
Cdd:smart00825  267 ELTPW------PPPGRPRRAGVSSFGFGGTNAHVILEE 298
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
690-1140 8.04e-157

Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.


Pssm-ID: 395541 [Multi-domain]  Cd Length: 454  Bit Score: 494.93  E-value: 8.04e-157
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  690 QATFQPLSEVQKGLWTLQKMSPEKSAYHVPLCFKFSSGLHLETLQQAFGLVLNQHPILKHVIQEK-DGVPILKNEPALSI 768
Cdd:pfam00668    1 VQDEYPLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRQeNGEPVQVILEERPF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  769 EIKTENIS----SMKESDIPAFLRKKVKEPYVKENSPLVRVMSFSRSEQEHFLLVVIHHLIFDGVSSVTFIHSLFDTYQL 844
Cdd:pfam00668   81 ELEIIDISdlseSEEEEAIEAFIQRDLQSPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQQ 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  845 LLKGQQPEIAVSPAiYHDFAAWEKNMLAGKDGVKHRTYWQKQLSGTLPNLQLPKVSASS-VSEFREDTYTRRLSSGFMNQ 923
Cdd:pfam00668  161 LLKGEPLPLPPKTP-YKDYAEWLQQYLQSEDYQKDAAYWLEQLEGELPVLQLPKDYARPaDRSFKGDRLSFTLDEDTEEL 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  924 VRMFAKEHSVNVTTVFLSCYMMLLGRYTGQKEQIVGMPAMVRPEERFDDAIGHFLNMLPIRSELNPADTFSSFISKLQLT 1003
Cdd:pfam00668  240 LRKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSPDIERMVGMFVNTLPLRIDPKGGKTFSELIKRVQED 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1004 ILDGLDHAAYPFPKMVRDLNIPRSQAGSPVFQTAFFYQNFLQSGSYQSLLSRYADFFSVDYVeyIHQEGEYELVFELWET 1083
Cdd:pfam00668  320 LLSAEPHQGYPFGDLVNDLRLPRDLSRHPLFDPMFSFQNYLGQDSQEEEFQLSELDLSVSSV--IEEEAKYDLSLTASER 397
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1776025254 1084 EEKMELNIKYNTGLFDAASISAMFDHFVYVTEQAMLNPSQPLKEYSLLPEAEKQMIL 1140
Cdd:pfam00668  398 GGGLTIKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLSDAEKQKLL 454
A_NRPS_VisG_like cd17651
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ...
1159-1638 1.04e-153

similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341306 [Multi-domain]  Cd Length: 491  Bit Score: 487.62  E-value: 1.04e-153
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1159 FEQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYP 1238
Cdd:cd17651      1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1239 AERLEYMLEDSEVFITLTTSELVNTLSwnGVTTALLDQDWDEIAQTASDRkvLTRTVTPENLAYVIYTSGSTGKPKGVMI 1318
Cdd:cd17651     81 AERLAFMLADAGPVLVLTHPALAGELA--VELVAVTLLDQPGAAAGADAE--PDPALDADDLAYVIYTSGSTGRPKGVVM 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1319 PHKALTNFLVSMGETPGLTAEDKMLAVTTYCFDIAALELFLPLIKGAhCYICQTEHTK-DVEKLKRDIRTIKPTVMQATP 1397
Cdd:cd17651    157 PHRSLANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGA-TLVLPPEEVRtDPPALAAWLDEQRISRVFLPT 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1398 ATWKMLFYSGWENEENV----KILCGGEALP--ETLKRYFLDTGSEAW-NMFGPTETTIWSAVQRINDEC---SRATIGR 1467
Cdd:cd17651    236 VALRALAEHGRPLGVRLaalrYLLTGGEQLVltEDLREFCAGLPGLRLhNHYGPTETHVVTALSLPGDPAawpAPPPIGR 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1468 PIANTQIYITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPFEPGSKLYRTGDMARWLPGGRIEYIGRID 1547
Cdd:cd17651    316 PIDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVPGARMYRTGDLARWLPDGELEFLGRAD 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1548 NQVKIRGFRIELGDIESRLSEHPGILECVVVADMDN-----LAAYYTAkHANASLTARELRHFVKNALPAYMVPSYFIQL 1622
Cdd:cd17651    396 DQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRpgekrLVAYVVG-DPEAPVDAAELRAALATHLPEYMVPSAFVLL 474
                          490
                   ....*....|....*.
gi 1776025254 1623 DHMPLTPNGKIDRNSL 1638
Cdd:cd17651    475 DALPLTPNGKLDRRAL 490
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
1180-1577 3.66e-153

amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.


Pssm-ID: 273779 [Multi-domain]  Cd Length: 409  Bit Score: 482.54  E-value: 3.66e-153
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1180 TYRELDERSTQLAIYLQA-HGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLEDSEVFITLTTS 1258
Cdd:TIGR01733    1 TYRELDERANRLARHLRAaGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1259 ELVNTLSWNGVTTALLDQDWDEIAQTASDRKVLTRTVTPENLAYVIYTSGSTGKPKGVMIPHKALTNFLVSMGETPGLTA 1338
Cdd:TIGR01733   81 ALASRLAGLVLPVILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDP 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1339 EDKMLAVTTYCFDIAALELFLPLIKGAHCYICQTEHTKDVEKLKRD-IRTIKPTVMQATPATWKMLFYSGWENEENVKIL 1417
Cdd:TIGR01733  161 DDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLAAlIAEHPVTVLNLTPSLLALLAAALPPALASLRLV 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1418 C-GGEALPETLKRYFLDTGSEA--WNMFGPTETTIWSAVQRI----NDECSRATIGRPIANTQIYITDSQLAPVPAGVPG 1490
Cdd:TIGR01733  241 IlGGEALTPALVDRWRARGPGArlINLYGPTETTVWSTATLVdpddAPRESPVPIGRPLANTRLYVLDDDLRPVPVGVVG 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1491 ELCIAGDGVAKGYYKKEELTDSRFIDNPF--EPGSKLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSE 1568
Cdd:TIGR01733  321 ELYIGGPGVARGYLNRPELTAERFVPDPFagGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLR 400

                   ....*....
gi 1776025254 1569 HPGILECVV 1577
Cdd:TIGR01733  401 HPGVREAVV 409
A_NRPS_CmdD_like cd17652
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ...
1167-1638 7.65e-149

similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).


Pssm-ID: 341307 [Multi-domain]  Cd Length: 436  Bit Score: 471.35  E-value: 7.65e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1167 PDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYML 1246
Cdd:cd17652      1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1247 EDSEVFITLTTselvntlswngvttalldqdwdeiaqtasdrkvltrtvtPENLAYVIYTSGSTGKPKGVMIPHKALTNF 1326
Cdd:cd17652     81 ADARPALLLTT---------------------------------------PDNLAYVIYTSGSTGRPKGVVVTHRGLANL 121
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1327 LVSMGETPGLTAEDKMLAVTTYCFDIAALELFLPLIKGAHCYICQTEHTKDVEKLKRDIRTIKPTVMQATPATWKMLfyS 1406
Cdd:cd17652    122 AAAQIAAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREHRITHVTLPPAALAAL--P 199
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1407 GWENEENVKILCGGEALP-ETLKRYflDTGSEAWNMFGPTETTIWSAVQRINDECSRATIGRPIANTQIYITDSQLAPVP 1485
Cdd:cd17652    200 PDDLPDLRTLVVAGEACPaELVDRW--APGRRMINAYGPTETTVCATMAGPLPGGGVPPIGRPVPGTRVYVLDARLRPVP 277
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1486 AGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPF-EPGSKLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIES 1564
Cdd:cd17652    278 PGVPGELYIAGAGLARGYLNRPGLTAERFVADPFgAPGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEA 357
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1776025254 1565 RLSEHPGILECVVVADMDN-----LAAYYTAKhANASLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSL 1638
Cdd:cd17652    358 ALTEHPGVAEAVVVVRDDRpgdkrLVAYVVPA-PGAAPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
A_NRPS_PvdJ-like cd17649
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ...
1167-1639 1.92e-147

non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341304 [Multi-domain]  Cd Length: 450  Bit Score: 468.00  E-value: 1.92e-147
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1167 PDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYML 1246
Cdd:cd17649      1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1247 EDSEVFITLTTselvntlswngvttalldqdwdeiaqtasdrkvltrtvTPENLAYVIYTSGSTGKPKGVMIPHKALTNF 1326
Cdd:cd17649     81 EDSGAGLLLTH--------------------------------------HPRQLAYVIYTSGSTGTPKGVAVSHGPLAAH 122
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1327 LVSMGETPGLTAEDKMLAVTTYCFDIAALELFLPLIKGAHCYICQTEHTKDVEKLKRDIRTIKPTVMQATPATWKMLF-- 1404
Cdd:cd17649    123 CQATAERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVTVLDLPPAYLQQLAee 202
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1405 --YSGWENEENVKILC-GGEAL-PETLKRYFldTGSEAW-NMFGPTETTI----WSAVQRINDECSRATIGRPIANTQIY 1475
Cdd:cd17649    203 adRTGDGRPPSLRLYIfGGEALsPELLRRWL--KAPVRLfNAYGPTEATVtplvWKCEAGAARAGASMPIGRPLGGRSAY 280
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1476 ITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPF-EPGSKLYRTGDMARWLPGGRIEYIGRIDNQVKIRG 1554
Cdd:cd17649    281 ILDADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFgAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRG 360
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1555 FRIELGDIESRLSEHPGILECVVVA-DMD---NLAAYYTAKHANA-SLTARELRHFVKNALPAYMVPSYFIQLDHMPLTP 1629
Cdd:cd17649    361 FRIELGEIEAALLEHPGVREAAVVAlDGAggkQLVAYVVLRAAAAqPELRAQLRTALRASLPDYMVPAHLVFLARLPLTP 440
                          490
                   ....*....|
gi 1776025254 1630 NGKIDRNSLK 1639
Cdd:cd17649    441 NGKLDRKALP 450
A_NRPS_Sfm_like cd12115
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ...
1156-1638 9.31e-147

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.


Pssm-ID: 341280 [Multi-domain]  Cd Length: 447  Bit Score: 465.64  E-value: 9.31e-147
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1156 HELFEQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDP 1235
Cdd:cd12115      2 HDLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDP 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1236 SYPAERLEYMLEDSEVFITLTTselvntlswngvttalldqdwdeiaqtasdrkvltrtvtPENLAYVIYTSGSTGKPKG 1315
Cdd:cd12115     82 AYPPERLRFILEDAQARLVLTD---------------------------------------PDDLAYVIYTSGSTGRPKG 122
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1316 VMIPHKALTNFLVSMGETpgLTAED--KMLAVTTYCFDIAALELFLPLIKGAHCYICQT-EHTKDVEKLKRD--IRTIkP 1390
Cdd:cd12115    123 VAIEHRNAAAFLQWAAAA--FSAEElaGVLASTSICFDLSVFELFGPLATGGKVVLADNvLALPDLPAAAEVtlINTV-P 199
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1391 TVMQ------ATPATWKMLfysgweneeNVkilcGGEALPETLKR--YFLDTGSEAWNMFGPTETTIWSAVQRINDECSR 1462
Cdd:cd12115    200 SAAAellrhdALPASVRVV---------NL----AGEPLPRDLVQrlYARLQVERVVNLYGPSEDTTYSTVAPVPPGASG 266
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1463 A-TIGRPIANTQIYITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPFEPGSKLYRTGDMARWLPGGRIE 1541
Cdd:cd12115    267 EvSIGRPLANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGPGARLYRTGDLVRWRPDGLLE 346
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1542 YIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMD-----NLAAYYTAKHANASLTArELRHFVKNALPAYMVP 1616
Cdd:cd12115    347 FLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDaagerRLVAYIVAEPGAAGLVE-DLRRHLGTRLPAYMVP 425
                          490       500
                   ....*....|....*....|..
gi 1776025254 1617 SYFIQLDHMPLTPNGKIDRNSL 1638
Cdd:cd12115    426 SRFVRLDALPLTPNGKIDRSAL 447
A_NRPS_Cytc1-like cd17643
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...
1167-1638 8.04e-145

similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341298 [Multi-domain]  Cd Length: 450  Bit Score: 460.24  E-value: 8.04e-145
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1167 PDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYML 1246
Cdd:cd17643      1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1247 EDSEVFITLTTselvntlswngvttalldqdwdeiaqtasdrkvltrtvtPENLAYVIYTSGSTGKPKGVMIPHKALTNF 1326
Cdd:cd17643     81 ADSGPSLLLTD---------------------------------------PDDLAYVIYTSGSTGRPKGVVVSHANVLAL 121
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1327 LVSMGETPGLTAEDKMLAVTTYCFDIAALELFLPLIKGAHCYICQTEHTKDVEKLKRDIRTIKPTVMQATPATWKMLFYS 1406
Cdd:cd17643    122 FAATQRWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGVTVLNQTPSAFYQLVEA 201
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1407 GWENEENVK----ILCGGEAL-PETLKRY---FLDTGSEAWNMFGPTETTIWSAVQRIN----DECSRATIGRPIANTQI 1474
Cdd:cd17643    202 ADRDGRDPLalryVIFGGEALeAAMLRPWagrFGLDRPQLVNMYGITETTVHVTFRPLDaadlPAAAASPIGRPLPGLRV 281
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1475 YITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPF-EPGSKLYRTGDMARWLPGGRIEYIGRIDNQVKIR 1553
Cdd:cd17643    282 YVLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFgGPGSRMYRTGDLARRLPDGELEYLGRADEQVKIR 361
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1554 GFRIELGDIESRLSEHPGILECVVVADMDN-----LAAYYTAKhANASLTARELRHFVKNALPAYMVPSYFIQLDHMPLT 1628
Cdd:cd17643    362 GFRIELGEIEAALATHPSVRDAAVIVREDEpgdtrLVAYVVAD-DGAAADIAELRALLKELLPDYMVPARYVPLDALPLT 440
                          490
                   ....*....|
gi 1776025254 1629 PNGKIDRNSL 1638
Cdd:cd17643    441 VNGKLDRAAL 450
A_NRPS_ProA cd17656
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ...
1166-1638 1.74e-141

gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341311 [Multi-domain]  Cd Length: 479  Bit Score: 451.93  E-value: 1.74e-141
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1166 TPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYM 1245
Cdd:cd17656      1 TPDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1246 LEDSEVFITLTTSELVNTLSWNGVTTALldqDWDEIAQtaSDRKVLTRTVTPENLAYVIYTSGSTGKPKGVMIPHKALTN 1325
Cdd:cd17656     81 MLDSGVRVVLTQRHLKSKLSFNKSTILL---EDPSISQ--EDTSNIDYINNSDDLLYIIYTSGTTGKPKGVQLEHKNMVN 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1326 FLVSMGETPGLTAEDKMLAVTTYCFDIAALELFLPLIKGAHCYICQTEHTKDVEKLKRDIRTIKPTVMQATPATWKMLFY 1405
Cdd:cd17656    156 LLHFEREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNIEVVFLPVAFLKFIFS 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1406 S-GWENE--ENVK-ILCGGEAL--PETLKRYFLDTGSEAWNMFGPTETTIWSAVqRINDECSRAT---IGRPIANTQIYI 1476
Cdd:cd17656    236 ErEFINRfpTCVKhIITAGEQLviTNEFKEMLHEHNVHLHNHYGPSETHVVTTY-TINPEAEIPElppIGKPISNTWIYI 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1477 TDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPFEPGSKLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFR 1556
Cdd:cd17656    315 LDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYR 394
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1557 IELGDIESRLSEHPGILECVVVADMDN-----LAAYYTAKHAnasLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNG 1631
Cdd:cd17656    395 IELGEIEAQLLNHPGVSEAVVLDKADDkgekyLCAYFVMEQE---LNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNG 471

                   ....*..
gi 1776025254 1632 KIDRNSL 1638
Cdd:cd17656    472 KVDRKAL 478
PKS cd00833
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ...
4588-4989 4.14e-135

polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different products, called polyketides, by successive decarboxylating Claisen condensations. PKSs can be divided into 2 groups, modular type I PKSs consisting of one or more large multifunctional proteins and iterative type II PKSs, complexes of several monofunctional subunits.


Pssm-ID: 238429 [Multi-domain]  Cd Length: 421  Bit Score: 431.21  E-value: 4.14e-135
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4588 EGIAVVGLSCRFPGAETLESYWSLLSEGRSSIGPIPAERWGCKTPY------------YAGVIDGVSYFDPDFFLLHEED 4655
Cdd:cd00833      1 EPIAIVGMACRFPGAADPDEFWENLLEGRDAISEIPEDRWDADGYYpdpgkpgktytrRGGFLDDVDAFDAAFFGISPRE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4656 VRAMDPQALLVLEECLKLLYHAGYTPEEIKGKPVGVYIGGRS---QHKPDEDSLDHAKNPIVTVGQNYLAANLSQFFDVR 4732
Cdd:cd00833     81 AEAMDPQQRLLLEVAWEALEDAGYSPESLAGSRTGVFVGASSsdyLELLARDPDEIDAYAATGTSRAFLANRISYFFDLR 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4733 GPSVVVDTACSSALVGMNMAIQALRGGDIQSAIVGGVSLLSSDASHRLFDRRGILSKHSSFHVFDERADGVVLGEGVGMV 4812
Cdd:cd00833    161 GPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLSPDGRCRPFDADADGYVRGEGVGVV 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4813 MLKTVKQALEDGDTIYAVVKAASVNNDGRTAGPATPNLEAQKEVMKDALFKSGKKPEDISYLEANGSGSIVTDLLELKAI 4892
Cdd:cd00833    241 VLKRLSDALRDGDRIYAVIRGSAVNQDGRTKGITAPSGEAQAALIRRAYARAGVDPSDIDYVEAHGTGTPLGDPIEVEAL 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4893 QSVYRSGHS--SPLSLGSIKPNIGHPLCAEGIASFIKVVLMLKERRFVPFLSGEKEMAHFDQQKANITFSRALEKW-TDS 4969
Cdd:cd00833    321 AKVFGGSRSadQPLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKIDFEESPLRVPTEARPWpAPA 400
                          410       420
                   ....*....|....*....|.
gi 1776025254 4970 QP-TAAINCFADGGTNVHVIV 4989
Cdd:cd00833    401 GPrRAGVSSFGFGGTNAHVIL 421
A_NRPS_LgrA-like cd17645
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ...
1156-1638 7.74e-135

adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.


Pssm-ID: 341300 [Multi-domain]  Cd Length: 440  Bit Score: 431.21  E-value: 7.74e-135
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1156 HELFEQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDP 1235
Cdd:cd17645      1 HQLFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1236 SYPAERLEYMLEDSEVFITLTTselvntlswngvttalldqdwdeiaqtasdrkvltrtvtPENLAYVIYTSGSTGKPKG 1315
Cdd:cd17645     81 DYPGERIAYMLADSSAKILLTN---------------------------------------PDDLAYVIYTSGSTGLPKG 121
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1316 VMIPHKALTNFLVSMGETPGLTAEDKMLAVTTYCFDIAALELFLPLIKGAHCYICQTEHTKDVEKLKRDIRTIKPTV-MQ 1394
Cdd:cd17645    122 VMIEHHNLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDLDALNDYFNQEGITIsFL 201
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1395 ATPATWKmlfYSGWENEENVKILCGGEALpetlkRYFLDTGSEAWNMFGPTETTIWSAVQRINDECSRATIGRPIANTQI 1474
Cdd:cd17645    202 PTGAAEQ---FMQLDNQSLRVLLTGGDKL-----KKIERKGYKLVNNYGPTENTVVATSFEIDKPYANIPIGKPIDNTRV 273
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1475 YITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPFEPGSKLYRTGDMARWLPGGRIEYIGRIDNQVKIRG 1554
Cdd:cd17645    274 YILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRG 353
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1555 FRIELGDIESRLSEHPGILECVVVADMDN-----LAAYYTAKhanASLTARELRHFVKNALPAYMVPSYFIQLDHMPLTP 1629
Cdd:cd17645    354 YRIEPGEIEPFLMNHPLIELAAVLAKEDAdgrkyLVAYVTAP---EEIPHEELREWLKNDLPDYMIPTYFVHLKALPLTA 430

                   ....*....
gi 1776025254 1630 NGKIDRNSL 1638
Cdd:cd17645    431 NGKVDRKAL 439
A_NRPS_PpsD_like cd17650
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ...
1167-1638 6.83e-134

similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341305 [Multi-domain]  Cd Length: 447  Bit Score: 428.81  E-value: 6.83e-134
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1167 PDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYML 1246
Cdd:cd17650      1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1247 EDSEVFITLTTselvntlswngvttalldqdwdeiaqtasdrkvltrtvtPENLAYVIYTSGSTGKPKGVMIPHKALTNF 1326
Cdd:cd17650     81 EDSGAKLLLTQ---------------------------------------PEDLAYVIYTSGTTGKPKGVMVEHRNVAHA 121
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1327 LVSMGETPGLTAED-KMLAVTTYCFDIAALELFLPLIKGAHCYICQTEHTKDVEKLKRDIRTIKPTVMQATPATWKMLF- 1404
Cdd:cd17650    122 AHAWRREYELDSFPvRLLQMASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRITLMESTPALIRPVMa 201
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1405 YSGWENE--ENVKILCGGEAL-----PETLKRYFLdTGSEAWNMFGPTETTIWSAVQRIND--ECSRAT--IGRPIANTQ 1473
Cdd:cd17650    202 YVYRNGLdlSAMRLLIVGSDGckaqdFKTLAARFG-QGMRIINSYGVTEATIDSTYYEEGRdpLGDSANvpIGRPLPNTA 280
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1474 IYITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPFEPGSKLYRTGDMARWLPGGRIEYIGRIDNQVKIR 1553
Cdd:cd17650    281 MYVLDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIR 360
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1554 GFRIELGDIESRLSEHPGILECVVVADMDN-----LAAYYTAKHanaSLTARELRHFVKNALPAYMVPSYFIQLDHMPLT 1628
Cdd:cd17650    361 GFRIELGEIESQLARHPAIDEAVVAVREDKggearLCAYVVAAA---TLNTAELRAFLAKELPSYMIPSYYVQLDALPLT 437
                          490
                   ....*....|
gi 1776025254 1629 PNGKIDRNSL 1638
Cdd:cd17650    438 PNGKVDRRAL 447
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
2672-3082 9.55e-130

ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes both KR domains of the Bacillus subtilis Pks J,-L, and PksM, and all three KR domains of PksN, components of the megacomplex bacillaene synthase, which synthesizes the antibiotic bacillaene. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187656 [Multi-domain]  Cd Length: 436  Bit Score: 416.38  E-value: 9.55e-130
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2672 LEPVWEKQNEEREDEDLSYTEHIIVLFETERSVTDSIASHMKDARvitlneavghiaeryQCYMQNIFELLQ-SKVRELS 2750
Cdd:cd08953     36 LQPVWAPAALASAFLALAYEAALLGLAAAEAALLDALSALDPAAA---------------LQLLESLQRLLKaGLLAARA 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2751 AGRIIIQAIVPLEKEKQL------FAGVSGLLKTAEIEFSKLTAQVIEIEKPEEMID-LHLKLKDDSQRPFDKQIRYEAG 2823
Cdd:cd08953    101 SGRALLQVVTGLPGALGLdaldpaGAGLAGLLRTLAQEYPGLTCRLIDLDAGEASAEaLARELAAELAAPGAAEVRYRDG 180
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2824 HRFVKGWREMVLPSADTLHMPWRDEGVYLITGGAGSLGLLFAKEIANRTGRsTIVLTGRSVLSEDKENE---LEALRSIG 2900
Cdd:cd08953    181 LRYVQTLEPLPLPAGAAASAPLKPGGVYLVTGGAGGIGRALARALARRYGA-RLVLLGRSPLPPEEEWKaqtLAALEALG 259
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2901 AEVVYREADVSDQHAVHHLFEEIKERYGTLNGIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSGLLHVDECSKDFPLDFFI 2980
Cdd:cd08953    260 ARVLYISADVTDAAAVRRLLEKVRERYGAIDGVIHAAGVLRDALLAQKTAEDFEAVLAPKVDGLLNLAQALADEPLDFFV 339
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2981 FFSSVSGCLGNAGQADYAAANSFMDAFAEYRRSLAAskkrFGSTISFNWPLWEEGGMQVGAEDEkRMLKTTGMVPMPTDS 3060
Cdd:cd08953    340 LFSSVSAFFGGAGQADYAAANAFLDAFAAYLRQRGP----QGRVLSINWPAWREGGMAADLGAR-ELLARAGLLPIEPEE 414
                          410       420
                   ....*....|....*....|..
gi 1776025254 3061 GLKAFYQGIASDKPQVFVMEGQ 3082
Cdd:cd08953    415 GLQALEQALSSDLPQVLVSPGD 436
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
1156-1641 9.14e-129

The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341242 [Multi-domain]  Cd Length: 481  Bit Score: 415.40  E-value: 9.14e-129
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1156 HELFEQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDP 1235
Cdd:cd05918      2 HDLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLDP 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1236 SYPAERLEYMLEDSEVFITLTTselvntlswngvttalldqdwdeiaqtasdrkvltrtvTPENLAYVIYTSGSTGKPKG 1315
Cdd:cd05918     82 SHPLQRLQEILQDTGAKVVLTS--------------------------------------SPSDAAYVIFTSGSTGKPKG 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1316 VMIPHKALTNFLVSMGETPGLTAEDKMLAVTTYCFDIAALELFLPLIKGAhCyIC-QTEHTKdVEKLKRDIRTIKPTVMQ 1394
Cdd:cd05918    124 VVIEHRALSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGG-C-LCiPSEEDR-LNDLAGFINRLRVTWAF 200
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1395 ATPATWKMLfysGWENEENVKILC-GGEALPETLKRYFLDtGSEAWNMFGPTETTIWSAVQRINDECSRATIGRPIANTq 1473
Cdd:cd05918    201 LTPSVARLL---DPEDVPSLRTLVlGGEALTQSDVDTWAD-RVRLINAYGPAECTIAATVSPVVPSTDPRNIGRPLGAT- 275
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1474 IYITD--SQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNP-------FEPGSKLYRTGDMARWLPGGRIEYIG 1544
Cdd:cd05918    276 CWVVDpdNHDRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPawlkqegSGRGRRLYRTGDLVRYNPDGSLEYVG 355
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1545 RIDNQVKIRGFRIELGDIESRLSEH-PGILECVVVA-------DMDNLAAYYTAK----------------HANASLTAR 1600
Cdd:cd05918    356 RKDTQVKIRGQRVELGEIEHHLRQSlPGAKEVVVEVvkpkdgsSSPQLVAFVVLDgsssgsgdgdslflepSDEFRALVA 435
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|.
gi 1776025254 1601 ELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLKNI 1641
Cdd:cd05918    436 ELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRALREL 476
A_NRPS_TlmIV_like cd12114
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ...
1167-1635 8.87e-128

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.


Pssm-ID: 341279 [Multi-domain]  Cd Length: 477  Bit Score: 412.43  E-value: 8.87e-128
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1167 PDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYML 1246
Cdd:cd12114      1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1247 EDSEVFITLTTSELVNTLSWNGVTTALLDQdwdeiAQTASDRkVLTRTVTPENLAYVIYTSGSTGKPKGVMIPHKALTNF 1326
Cdd:cd12114     81 ADAGARLVLTDGPDAQLDVAVFDVLILDLD-----ALAAPAP-PPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNT 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1327 LVSMGETPGLTAEDKMLAVTTYCFDIAALELFLPLIKGAHCYICQTEHTKDVEKLKRDIRTIKPTVMQATPATWKMLF-Y 1405
Cdd:cd12114    155 ILDINRRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDPAHWAELIERHGVTLWNSVPALLEMLLdV 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1406 SGWENEENVK---ILCGGE----ALPETLKRYFldTGSEAWNMFGPTETTIWSAVQRIND-ECSRATI--GRPIANTQIY 1475
Cdd:cd12114    235 LEAAQALLPSlrlVLLSGDwiplDLPARLRALA--PDARLISLGGATEASIWSIYHPIDEvPPDWRSIpyGRPLANQRYR 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1476 ITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPfePGSKLYRTGDMARWLPGGRIEYIGRIDNQVKIRGF 1555
Cdd:cd12114    313 VLDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHP--DGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGY 390
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1556 RIELGDIESRLSEHPGILECVVVADMD----NLAAYYTAKHANASLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNG 1631
Cdd:cd12114    391 RIELGEIEAALQAHPGVARAVVVVLGDpggkRLAAFVVPDNDGTPIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANG 470

                   ....
gi 1776025254 1632 KIDR 1635
Cdd:cd12114    471 KVDR 474
A_NRPS_GliP_like cd17653
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ...
1157-1640 3.53e-125

nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341308 [Multi-domain]  Cd Length: 433  Bit Score: 403.23  E-value: 3.53e-125
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1157 ELFEQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPS 1236
Cdd:cd17653      1 DAFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1237 YPAERLEYMLEDSEVFITLTTSelvntlswngvttalldqdwdeiaqtasdrkvltrtvTPENLAYVIYTSGSTGKPKGV 1316
Cdd:cd17653     81 LPSARIQAILRTSGATLLLTTD-------------------------------------SPDDLAYIIFTSGSTGIPKGV 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1317 MIPHKALTNFLVSMGETPGLTAEDKMLAVTTYCFDIAALELFLPLIKGAHcyICQTEHTKDVEKLKR--DIRTIKPTVMQ 1394
Cdd:cd17653    124 MVPHRGVLNYVSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGT--LVLADPSDPFAHVARtvDALMSTPSILS 201
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1395 ATPATwkmlfysgweNEENVK-ILCGGEALPETLKRYFLDtGSEAWNMFGPTETTIWSAVQRINDEcSRATIGRPIANTQ 1473
Cdd:cd17653    202 TLSPQ----------DFPNLKtIFLGGEAVPPSLLDRWSP-GRRLYNAYGPTECTISSTMTELLPG-QPVTIGKPIPNST 269
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1474 IYITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPFEPGSKLYRTGDMARWLPGGRIEYIGRIDNQVKIR 1553
Cdd:cd17653    270 CYILDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFWPGSRMYRTGDYGRWTEDGGLEFLGREDNQVKVR 349
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1554 GFRIELGDIESR-LSEHPGILECVVVADMDNLAAYYTAkhanASLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGK 1632
Cdd:cd17653    350 GFRINLEEIEEVvLQSQPEVTQAAAIVVNGRLVAFVTP----ETVDVDGLRSELAKHLPSYAVPDRIIALDSFPLTANGK 425

                   ....*...
gi 1776025254 1633 IDRNSLKN 1640
Cdd:cd17653    426 VDRKALRE 433
PRK05691 PRK05691
peptide synthase; Validated
695-1736 7.57e-123

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 439.99  E-value: 7.57e-123
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  695 PLSEVQKGLWTLQKMSPEKSAYHVPLCFKFSSGLHLETLQQAFGLVLNQHPILK------------HVI----------Q 752
Cdd:PRK05691  3259 PLTPMQEGLLLHTLLEPGTGLYYMQDRYRINSALDPERFAQAWQAVVARHEALRasfswnagetmlQVIhkpgrtpidyL 3338
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  753 EKDGVPILKNEPALSIEIKTENISSMKESDIPAF-LRkkvkepyvkenspLVRVmsfsrSEQEHFLLVVIHHLIFDGVSS 831
Cdd:PRK05691  3339 DWRGLPEDGQEQRLQALHKQEREAGFDLLNQPPFhLR-------------LIRV-----DEARYWFMMSNHHILIDAWCR 3400
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  832 VTFIHSLFDTYQLLLKGQQPEIAVSPAiYHDFAAWeknmLAGKDGVKHRTYWQKQLSGtlpnLQLPKVSASSVSEFRE-- 909
Cdd:PRK05691  3401 SLLMNDFFEIYTALGEGREAQLPVPPR-YRDYIGW----LQRQDLAQARQWWQDNLRG----FERPTPIPSDRPFLREha 3471
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  910 ---------DTYTRrLSSGFMNQVRMFAKEHSVNVTTVFLSCYMMLLGRYTGQKEQI---------VGMPAMVRpeerfd 971
Cdd:PRK05691  3472 gdsggmvvgDCYTR-LDAADGARLRELAQAHQLTVNTFAQAAWALVLRRYSGDRDVLfgvtvagrpVSMPQMQR------ 3544
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  972 dAIGHFLNMLPIRSELnPAD----TFSSFISKLQLTILDGLDHAAYPFPKMVRDLNIPRsqaGSPVFQTAFFYQNF---- 1043
Cdd:PRK05691  3545 -TVGLFINSIALRVQL-PAAgqrcSVRQWLQGLLDSNMELREYEYLPLVAIQECSELPK---GQPLFDSLFVFENApvev 3619
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1044 -----LQSGSYQSLLSRYADFFSVDYVEYihqegeyelvfelweTEEKMELNIKYNTGLFDAASISAMFDHFVYVTEQAM 1118
Cdd:PRK05691  3620 svldrAQSLNASSDSGRTHTNFPLTAVCY---------------PGDDLGLHLSYDQRYFDAPTVERLLGEFKRLLLALV 3684
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1119 LNPSQPLKEYSLLPEAEKQMILKTWNATGKTYP----YItfhELFEQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIY 1194
Cdd:PRK05691  3685 QGFHGDLSELPLLGEQERDFLLDGCNRSERDYPleqsYV---RLFEAQVAAHPQRIAASCLDQQWSYAELNRAANRLGHA 3761
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1195 LQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLEDSEvfitltTSELVNTLSWNGVTTALL 1274
Cdd:PRK05691  3762 LRAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGLPAQRLQRIIELSR------TPVLVCSAACREQARALL 3835
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1275 DQ----------DWDEIAQTASDRKVLTRTVTPENLAYVIYTSGSTGKPKGVMIPHKALTNFLVSMGETPGLTAEDKMLA 1344
Cdd:PRK05691  3836 DElgcanrprllVWEEVQAGEVASHNPGIYSGPDNLAYVIYTSGSTGLPKGVMVEQRGMLNNQLSKVPYLALSEADVIAQ 3915
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1345 VTTYCFDIAALElFL--PLIkGAHCYICQTEHTKDVEKLKRDIRTIKPTVMQATPATWKMLFYSGWENEENVK-ILCGGE 1421
Cdd:PRK05691  3916 TASQSFDISVWQ-FLaaPLF-GARVEIVPNAIAHDPQGLLAHVQAQGITVLESVPSLIQGMLAEDRQALDGLRwMLPTGE 3993
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1422 ALPETLKRYFLDTGSEAW--NMFGPTETTIWSAVQRINDECSRAT---IGRPIANTQIYITDSQLAPVPAGVPGELCIAG 1496
Cdd:PRK05691  3994 AMPPELARQWLQRYPQIGlvNAYGPAECSDDVAFFRVDLASTRGSylpIGSPTDNNRLYLLDEALELVPLGAVGELCVAG 4073
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1497 DGVAKGYYKKEELTDSRFIDNPF-EPGSKLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILEC 1575
Cdd:PRK05691  4074 TGVGRGYVGDPLRTALAFVPHPFgAPGERLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREA 4153
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1576 VVV----ADMDNLAAYYTAKHANASLTAR--ELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLKNIDLSGEQlK 1649
Cdd:PRK05691  4154 AVAvqegVNGKHLVGYLVPHQTVLAQGALleRIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKALPALDIGQLQ-S 4232
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1650 QRQTSPKN-IQDTVFTIWQEVLKTSDIEWDDGFFDVGGDSLLAVTVADRIKHELSCEFSVTDLFEYSTIKNISQYI---- 1724
Cdd:PRK05691  4233 QAYLAPRNeLEQTLATIWADVLKVERVGVHDNFFELGGHSLLATQIASRVQKALQRNVPLRAMFECSTVEELAEYIegla 4312
                         1130
                   ....*....|....*.
gi 1776025254 1725 ----TEQRMGNASDHM 1736
Cdd:PRK05691  4313 gsaiDEQKVDRLSDLM 4328
PKS_KS smart00825
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ...
1762-2185 1.13e-120

Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the thiolase family and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.


Pssm-ID: 214836 [Multi-domain]  Cd Length: 298  Bit Score: 384.37  E-value: 1.13e-120
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  1762 VAIIGISCEFPGAKNHDEFWENLRDGkesiaffnkeelqrfgiskeiaenadyvpakasIEGKDRFDPSFFQISPKDAEF 1841
Cdd:smart00825    1 IAIVGMSCRFPGADDPEEFWDLLLAG---------------------------------LDDVDLFDAAFFGISPREAEA 47
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  1842 MDPQLRMLLTHSWKAIEDAGYAAGQIP--QTSVFMSASNNSYrallpsdttesletpdgyvswvlaqsgtiptmishklg 1919
Cdd:smart00825   48 MDPQQRLLLEVAWEALEDAGIDPESLRgsRTGVFVGVSSSDY-------------------------------------- 89
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  1920 lrgpSYFVHANCSSSLIGLHSAYKSLLSAESDYALVGGATLHTESNIGYVHQPGLNFSSDGHIKAFDASADGMIGGEGVA 1999
Cdd:smart00825   90 ----SVTVDTACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLSPDGRCKTFDASADGYVRGEGVG 165
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  2000 VVLLKKAADAVKDGDHIYALLRGIGVNNDGADKvGFYAPSVKGQadvvqqvmnqtkihpesicyveahgtgtklgdpiel 2079
Cdd:smart00825  166 VVVLKRLSDALRDGDPILAVIRGSAVNQDGRSN-GITAPSGPAQ------------------------------------ 208
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  2080 aaltnvyrqytnktqfCGIGSVKTNIGHLDTAAGLAGCIKVVMSLYHQELAPSINYKEPNPNTDLASSPFYVVDQKKTLS 2159
Cdd:smart00825  209 ----------------LLIGSVKSNIGHLEAAAGVAGLIKVVLALKHGVIPPTLHFETPNPHIDLEESPLRVPTELTPWP 272
                           410       420
                    ....*....|....*....|....*.
gi 1776025254  2160 REIQTHRAALSSFGLGGTNTHAIFEQ 2185
Cdd:smart00825  273 PPGRPRRAGVSSFGFGGTNAHVILEE 298
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
4587-5010 1.38e-118

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 413.50  E-value: 1.38e-118
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4587 AEGIAVVGLSCRFPGAETLESYWSLLSEGRSSIGPIPAERWGCKTPY-------------YAGVIDGVSYFDPDFFLLHE 4653
Cdd:COG3321      3 DEPIAIIGMACRFPGADDPEEFWRNLRAGRDAITEVPADRWDADAYYdpdpdapgktyvrWGGFLDDVDEFDALFFGISP 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4654 EDVRAMDPQALLVLEECLKLLYHAGYTPEEIKGKPVGVYIGG-------RSQHKPDEDSLDHAknpiVTVGQNYLAANLS 4726
Cdd:COG3321     83 REAEAMDPQQRLLLEVAWEALEDAGYDPESLAGSRTGVFVGAssndyalLLLADPEAIDAYAL----TGNAKSVLAGRIS 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4727 QFFDVRGPSVVVDTACSSALVGMNMAIQALRGGDIQSAIVGGVSLLSSDASHRLFDRRGILSKHSSFHVFDERADGVVLG 4806
Cdd:COG3321    159 YKLDLRGPSVTVDTACSSSLVAVHLACQSLRSGECDLALAGGVNLMLTPESFILFSKGGMLSPDGRCRAFDADADGYVRG 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4807 EGVGMVMLKTVKQALEDGDTIYAVVKAASVNNDGRTAGPATPNLEAQKEVMKDALFKSGKKPEDISYLEANGSGSIVTDL 4886
Cdd:COG3321    239 EGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRSNGLTAPNGPAQAAVIRRALADAGVDPATVDYVEAHGTGTPLGDP 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4887 LELKAIQSVYRSGHS--SPLSLGSIKPNIGHPLCAEGIASFIKVVLMLKERRFVPFLsgekemaHFDQQKANITFS---- 4960
Cdd:COG3321    319 IEAAALTAAFGQGRPadQPCAIGSVKSNIGHLEAAAGVAGLIKAVLALRHGVLPPTL-------HFETPNPHIDFEnspf 391
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1776025254 4961 ---RALEKW-TDSQP-TAAINCFADGGTNVHVIVEAWEKDEKHAikRSPKSPPQL 5010
Cdd:COG3321    392 yvnTELRPWpAGGGPrRAGVSSFGFGGTNAHVVLEEAPAAAPAA--AAAARPPQL 444
A_NRPS_ACVS-like cd17648
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ...
1167-1638 8.02e-115

N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.


Pssm-ID: 341303 [Multi-domain]  Cd Length: 453  Bit Score: 374.04  E-value: 8.02e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1167 PDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVG-PDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYM 1245
Cdd:cd17648      1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAEIrPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1246 LEDSEVFITLTTselvntlswngvttalldqdwdeiaqtasdrkvltrtvtPENLAYVIYTSGSTGKPKGVMIPHKALTN 1325
Cdd:cd17648     81 LEDTGARVVITN---------------------------------------STDLAYAIYTSGTTGKPKGVLVEHGSVVN 121
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1326 FLVSMGETPGLTAED--KMLAVTTYCFDIAALELFLPLIKGAHCYICQTEHTKDVEKLKRDIRTIKPTVMQATPATWKML 1403
Cdd:cd17648    122 LRTSLSERYFGRDNGdeAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPDRFYAYINREKVTYLSGTPSVLQQY 201
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1404 FYSGWENEEnvKILCGGEALP----ETLKRYFldtGSEAWNMFGPTETTIWSAVQRI-NDECSRATIGRPIANTQIYITD 1478
Cdd:cd17648    202 DLARLPHLK--RVDAAGEEFTapvfEKLRSRF---AGLIINAYGPTETTVTNHKRFFpGDQRFDKSLGRPVRNTKCYVLN 276
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1479 SQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPFEP--------GSKLYRTGDMARWLPGGRIEYIGRIDNQV 1550
Cdd:cd17648    277 DAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFQTeqerargrNARLYKTGDLVRWLPSGELEYLGRNDFQV 356
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1551 KIRGFRIELGDIESRLSEHPGILECVVVADMDN----------LAAYYTAkhANASLTARELRHFVKNALPAYMVPSYFI 1620
Cdd:cd17648    357 KIRGQRIEPGEVEAALASYPGVRECAVVAKEDAsqaqsriqkyLVGYYLP--EPGHVPESDLLSFLRAKLPRYMVPARLV 434
                          490
                   ....*....|....*...
gi 1776025254 1621 QLDHMPLTPNGKIDRNSL 1638
Cdd:cd17648    435 RLEGIPVTINGKLDVRAL 452
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
1155-1639 2.38e-114

O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440087 [Multi-domain]  Cd Length: 452  Bit Score: 372.61  E-value: 2.38e-114
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1155 FHELFEQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLD 1234
Cdd:COG0318      1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1235 PSYPAERLEYMLEDSEVfitlttselvntlswngvttalldqdwdeiaqtasdrKVLtrtVTpenlAYVIYTSGSTGKPK 1314
Cdd:COG0318     81 PRLTAEELAYILEDSGA-------------------------------------RAL---VT----ALILYTSGTTGRPK 116
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1315 GVMIPHKALTNFLVSMGETPGLTAEDKMLAVTTYCFDIA-ALELFLPLIKGAHCYIcqteHTK-DVEKLKRDIRTIKPTV 1392
Cdd:COG0318    117 GVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGlTVGLLAPLLAGATLVL----LPRfDPERVLELIERERVTV 192
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1393 MQATPATWKMLFYSGWENEENVK----ILCGGEALPETLKRYFLD-TGSEAWNMFGPTETTIWSAVQRINDECSR-ATIG 1466
Cdd:COG0318    193 LFGVPTMLARLLRHPEFARYDLSslrlVVSGGAPLPPELLERFEErFGVRIVEGYGLTETSPVVTVNPEDPGERRpGSVG 272
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1467 RPIANTQIYITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNpfepgskLYRTGDMARWLPGGRIEYIGRI 1546
Cdd:COG0318    273 RPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFRDG-------WLRTGDLGRLDEDGYLYIVGRK 345
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1547 DNQVKIRGFRIELGDIESRLSEHPGILECVVVADMDN-----LAAYYTAKhANASLTARELRHFVKNALPAYMVPSYFIQ 1621
Cdd:COG0318    346 KDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEkwgerVVAFVVLR-PGAELDAEELRAFLRERLARYKVPRRVEF 424
                          490
                   ....*....|....*...
gi 1776025254 1622 LDHMPLTPNGKIDRNSLK 1639
Cdd:COG0318    425 VDELPRTASGKIDRRALR 442
DltA cd05945
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ...
1163-1638 3.41e-114

D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341267 [Multi-domain]  Cd Length: 449  Bit Score: 372.35  E-value: 3.41e-114
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1163 AKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERL 1242
Cdd:cd05945      1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1243 EYMLEDSEVfitlttselvntlswngvtTALLdqdwdeiaqtasdrkvltrtVTPENLAYVIYTSGSTGKPKGVMIPHKA 1322
Cdd:cd05945     81 REILDAAKP-------------------ALLI--------------------ADGDDNAYIIFTSGSTGRPKGVQISHDN 121
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1323 LTNFLVSMGETPGLTAEDKMLAVTTYCFDIAALELFLPLIKGAHCYICQTEHTKDVEKLKRDIRTIKPTVMQATPATWKM 1402
Cdd:cd05945    122 LVSFTNWMLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADPKQLFRFLAEHGITVWVSTPSFAAM 201
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1403 LFYSGWENEENVK-----ILCGgEALP----ETLKRYFldTGSEAWNMFGPTETTIWSAVQRINDECS----RATIGRPI 1469
Cdd:cd05945    202 CLLSPTFTPESLPslrhfLFCG-EVLPhktaRALQQRF--PDARIYNTYGPTEATVAVTYIEVTPEVLdgydRLPIGYAK 278
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1470 ANTQIYITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPFEPGsklYRTGDMARWLPGGRIEYIGRIDNQ 1549
Cdd:cd05945    279 PGAKLVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDEGQRA---YRTGDLVRLEADGLLFYRGRLDFQ 355
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1550 VKIRGFRIELGDIESRLSEHPGILECVVVADMDN-----LAAYYTAKHANASLTARELRHFVKNALPAYMVPSYFIQLDH 1624
Cdd:cd05945    356 VKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGekvteLIAFVVPKPGAEAGLTKAIKAELAERLPPYMIPRRFVYLDE 435
                          490
                   ....*....|....
gi 1776025254 1625 MPLTPNGKIDRNSL 1638
Cdd:cd05945    436 LPLNANGKIDRKAL 449
AMP-binding pfam00501
AMP-binding enzyme;
1159-1553 4.72e-114

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 370.49  E-value: 4.72e-114
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1159 FEQQAKKTPDRAAVS-YEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSY 1237
Cdd:pfam00501    1 LERQAARTPDKTALEvGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1238 PAERLEYMLEDSE--VFITLTTSELVNTLSW-----NGVTTALLDQDW-------DEIAQTASDRKVLTRTVTPENLAYV 1303
Cdd:pfam00501   81 PAEELAYILEDSGakVLITDDALKLEELLEAlgkleVVKLVLVLDRDPvlkeeplPEEAKPADVPPPPPPPPDPDDLAYI 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1304 IYTSGSTGKPKGVMIPHKALTNFLVSMGETP----GLTAEDKMLAVTTYCFDIA-ALELFLPLIKGAHCYICQTEHTKDV 1378
Cdd:pfam00501  161 IYTSGTTGKPKGVMLTHRNLVANVLSIKRVRprgfGLGPDDRVLSTLPLFHDFGlSLGLLGPLLAGATVVLPPGFPALDP 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1379 EKLKRDIRTIKPTVMQATPATWKMLFYSGWENEENVK----ILCGGEALPETLKRYFLD-TGSEAWNMFGPTETTIWSA- 1452
Cdd:pfam00501  241 AALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSslrlVLSGGAPLPPELARRFRElFGGALVNGYGLTETTGVVTt 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1453 -VQRINDECSRATIGRPIANTQIYITD-SQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPFepgsklYRTGD 1530
Cdd:pfam00501  321 pLPLDEDLRSLGSVGRPLPGTEVKIVDdETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDEDGW------YRTGD 394
                          410       420
                   ....*....|....*....|...
gi 1776025254 1531 MARWLPGGRIEYIGRIDNQVKIR 1553
Cdd:pfam00501  395 LGRRDEDGYLEIVGRKKDQIKLG 417
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
4029-4401 1.70e-109

ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes both KR domains of the Bacillus subtilis Pks J,-L, and PksM, and all three KR domains of PksN, components of the megacomplex bacillaene synthase, which synthesizes the antibiotic bacillaene. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187656 [Multi-domain]  Cd Length: 436  Bit Score: 358.22  E-value: 1.70e-109
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4029 DWKEFDGLVDVIGCGWDDeGRLDWIEWVQRLVEF----GHKEGLRLLCVTKGLESFQNTS-VRMAGASRAGLYRMLQCEY 4103
Cdd:cd08953     61 LAAAEAALLDALSALDPA-AALQLLESLQRLLKAgllaARASGRALLQVVTGLPGALGLDaLDPAGAGLAGLLRTLAQEY 139
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4104 SHLISRHMDAEEVTDHP-RLAKLIADEfYSESYDAEVCYRDGLRYQSFLKAHPETGKATeQSAVFPKDHVLLITGGTRGI 4182
Cdd:cd08953    140 PGLTCRLIDLDAGEASAeALARELAAE-LAAPGAAEVRYRDGLRYVQTLEPLPLPAGAA-ASAPLKPGGVYLVTGGAGGI 217
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4183 GLLCARHFAECYGvKKLVLTGREQLPPREEWARfktsntslaekiQAVRELEAKGVQVEMLSLTLSDDAQVEQTLQHIKR 4262
Cdd:cd08953    218 GRALARALARRYG-ARLVLLGRSPLPPEEEWKA------------QTLAALEALGARVLYISADVTDAAAVRRLLEKVRE 284
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4263 TLGPIGGVIHCAGLTDMDTLafIRKTSDDIQRVMEPKVSGLTTLYRHVCNEPLQFFVLFSSVSAIIPelSAGQADYAMAN 4342
Cdd:cd08953    285 RYGAIDGVIHAAGVLRDALL--AQKTAEDFEAVLAPKVDGLLNLAQALADEPLDFFVLFSSVSAFFG--GAGQADYAAAN 360
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1776025254 4343 SYMDYFAEAHQK---HVPIISVQWPNWKETGMGEV--TNQAYRESGLFSITNSEGLRFLDQIVS 4401
Cdd:cd08953    361 AFLDAFAAYLRQrgpQGRVLSINWPAWREGGMAADlgARELLARAGLLPIEPEEGLQALEQALS 424
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
3339-3588 2.31e-108

Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains. The N-terminal domain contains most of the structures involved in dimer formation and also the active site cysteine.


Pssm-ID: 425468 [Multi-domain]  Cd Length: 251  Bit Score: 346.93  E-value: 2.31e-108
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3339 EPVAIVGISGRFPGAMDIDEFWKNLEEGKDSITEVPKDRWDWREHYGNPDTDVNKTDIKWGGfIDGVAEFDPLFFGISPR 3418
Cdd:pfam00109    1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIPADRWDPDKLYDPPSRIAGKIYTKWGG-LDDIFDFDPLFFGISPR 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3419 EADYVDPQQRLLMTYVWKALEDAGCPPQSLSGTGTGIFIGTGNTGYKDL--FHRANLPIEGHAATGHMIPSVGPNRMSYF 3496
Cdd:pfam00109   80 EAERMDPQQRLLLEAAWEALEDAGITPDSLDGSRTGVFIGSGIGDYAALllLDEDGGPRRGSPFAVGTMPSVIAGRISYF 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3497 LNIHGPSEPVETACSSSLVAIHRAVTAMQNGDCEMAIAGGVNTILTEEAHISYSKAGMLSKDGRCKTFSADANGYVRGEG 3576
Cdd:pfam00109  160 LGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSPDGPCKAFDPFADGFVRGEG 239
                          250
                   ....*....|..
gi 1776025254 3577 VGMVMLKKLEDA 3588
Cdd:pfam00109  240 VGAVVLKRLSDA 251
A_NRPS_MycA_like cd05908
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ...
46-563 4.76e-105

The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341234 [Multi-domain]  Cd Length: 499  Bit Score: 347.94  E-value: 4.76e-105
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254   46 KGIIYLQPDGTEVYQSYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNSQLLPAFWGCVLTGVVPaplaVPPTYAESSS 125
Cdd:cd05908      2 EGIIFILGDKKEKFVSYRHLREEALGYLGALQELGIKPGQEVVFQITHNNKFLYLFWACLLGGMIA----VPVSIGSNEE 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  126 GTQKLKDAWTLLDKPAVITDRGMHQEMldwakeqglegfraiivedllsaeadtdwhqssPEDLALLLLTSGSTGTPKAV 205
Cdd:cd05908     78 HKLKLNKVWNTLKNPYLITEEEVLCEL---------------------------------ADELAFIQFSSGSTGDPKGV 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  206 MLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDHVGGIGMLHLRDVYLGCQEINVSSETILMEPLKWLDWIDHYRASVTW 285
Cdd:cd05908    125 MLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMPTRLFIRRPILWLKKASEHKATIVS 204
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  286 APNFAFGLVTDFAEEIKDRKWDLSSMRYMLNGGEAMVAKVGRRILELLEPHGLPADAIRPAWGMSETSSGVIFS------ 359
Cdd:cd05908    205 SPNFGYKYFLKTLKPEKANDWDLSSIRMILNGAEPIDYELCHEFLDHMSKYGLKRNAILPVYGLAEASVGASLPkaqspf 284
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  360 ------HEFTRAG-----TSDDDH----FVEIGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGYYQRPDLNESV 424
Cdd:cd05908    285 ktitlgRRHVTHGepepeVDKKDSecltFVEVGKPIDETDIRICDEDNKILPDGYIGHIQIRGKNVTPGYYNNPEATAKV 364
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  425 FTEDGWFETGDLGFLRNGRLTITGRTKDAIIINGINYYSHAIESAVEELSEIETSYTAACAVRLGQNSTDQLAIFFVTSA 504
Cdd:cd05908    365 FTDDGWLKTGDLGFIRNGRLVITGREKDIIFVNGQNVYPHDIERIAEELEGVELGRVVACGVNNSNTRNEEIFCFIEHRK 444
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1776025254  505 KLNDeqMSQLLRNIQSHVSQVIGVTPEYLLPVQKeeIPKTAIGKIQRTQLKTSFENGEF 563
Cdd:cd05908    445 SEDD--FYPLGKKIKKHLNKRGGWQINEVLPIRR--IPKTTSGKVKRYELAQRYQSGEF 499
PKS_KS smart00825
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ...
4590-4991 5.41e-104

Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the thiolase family and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.


Pssm-ID: 214836 [Multi-domain]  Cd Length: 298  Bit Score: 336.61  E-value: 5.41e-104
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  4590 IAVVGLSCRFPGAETLESYWSLLSEGrssigpipaerwgcktpyyagvIDGVSYFDPDFFLLHEEDVRAMDPQALLVLEE 4669
Cdd:smart00825    1 IAIVGMSCRFPGADDPEEFWDLLLAG----------------------LDDVDLFDAAFFGISPREAEAMDPQQRLLLEV 58
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  4670 CLKLLYHAGYTPEEIKGKPVGVYIGGRSQHkpdedsldhaknpivtvgqnYlaanlsqffdvrgpSVVVDTACSSALVGM 4749
Cdd:smart00825   59 AWEALEDAGIDPESLRGSRTGVFVGVSSSD--------------------Y--------------SVTVDTACSSSLVAL 104
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  4750 NMAIQALRGGDIQSAIVGGVSLLSSDASHRLFDRRGILSKHSSFHVFDERADGVVLGEGVGMVMLKTVKQALEDGDTIYA 4829
Cdd:smart00825  105 HLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLSPDGRCKTFDASADGYVRGEGVGVVVLKRLSDALRDGDPILA 184
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  4830 VVKAASVNNDGRTAGPATPNLEAQkevmkdalfksgkkpedisyleangsgsivtdllelkaiqsvyrsghsspLSLGSI 4909
Cdd:smart00825  185 VIRGSAVNQDGRSNGITAPSGPAQ--------------------------------------------------LLIGSV 214
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  4910 KPNIGHPLCAEGIASFIKVVLMLKERRFVPFLSGEKEMAHFDQQKANITFSRALEKW--TDSQPTAAINCFADGGTNVHV 4987
Cdd:smart00825  215 KSNIGHLEAAAGVAGLIKVVLALKHGVIPPTLHFETPNPHIDLEESPLRVPTELTPWppPGRPRRAGVSSFGFGGTNAHV 294

                    ....
gi 1776025254  4988 IVEA 4991
Cdd:smart00825  295 ILEE 298
FAAL cd05931
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...
37-560 6.09e-97

Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.


Pssm-ID: 341254 [Multi-domain]  Cd Length: 547  Bit Score: 326.12  E-value: 6.09e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254   37 RTAAELGDTKGIIYL-QPDGTEVYQSYRRLWDDGLRIVKGLRQSGlKAKQSVILQLGDNSQLLPAFWGCVLTGVVPAPLA 115
Cdd:cd05931      1 RRAAARPDRPAYTFLdDEGGREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  116 VPptyaESSSGTQKLKDAwtLLD-KP-AVITDRGMHQEMLDWAKEQGLEGFRAIIVEDLLSAEADTDWH--QSSPEDLAL 191
Cdd:cd05931     80 PP----TPGRHAERLAAI--LADaGPrVVLTTAAALAAVRAFAASRPAAGTPRLLVVDLLPDTSAADWPppSPDPDDIAY 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  192 LLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDH-VGGIGMLhLRDVYLGCQEINVSSETILMEPL 270
Cdd:cd05931    154 LQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHdMGLIGGL-LTPLYSGGPSVLMSPAAFLRRPL 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  271 KWLDWIDHYRASVTWAPNFAFGLVTDFAEEIKDRKWDLSSMRYMLNGGEAMVAKVGRRILELLEPHGLPADAIRPAWGMS 350
Cdd:cd05931    233 RWLRLISRYRATISAAPNFAYDLCVRRVRDEDLEGLDLSSWRVALNGAEPVRPATLRRFAEAFAPFGFRPEAFRPSYGLA 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  351 ETSSGVIFS---------------HEFTRAGTSDDDH----FVEIGSPIPGFSMRIVN-DHNELVEEGEIGRFQVSGLSV 410
Cdd:cd05931    313 EATLFVSGGppgtgpvvlrvdrdaLAGRAVAVAADDPaareLVSCGRPLPDQEVRIVDpETGRELPDGEVGEIWVRGPSV 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  411 TSGYYQRPDLNESVF------TEDGWFETGDLGFLRNGRLTITGRTKDAIIINGINYYSHAIESAVEELSE-IETSYTAA 483
Cdd:cd05931    393 ASGYWGRPEATAETFgalaatDEGGWLRTGDLGFLHDGELYITGRLKDLIIVRGRNHYPQDIEATAEEAHPaLRPGCVAA 472
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1776025254  484 CAVrlGQNSTDQLAIFFVTSAKLNDEQMSQLLRNIQSHVSQVIGVTPEYLLPVQKEEIPKTAIGKIQRTQLKTSFEN 560
Cdd:cd05931    473 FSV--PDDGEERLVVVAEVERGADPADLAAIAAAIRAAVAREHGVAPADVVLVRPGSIPRTSSGKIQRRACRAAYLD 547
LCL_NRPS-like cd19531
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ...
695-1121 3.83e-92

LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380454 [Multi-domain]  Cd Length: 427  Bit Score: 307.74  E-value: 3.83e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  695 PLSEVQKGLWTLQKMSPEKSAYHVPLCFKFSSGLHLETLQQAFGLVLNQHPILKHVIQEKDGVPILKNEPALSIEIKTEN 774
Cdd:cd19531      3 PLSFAQQRLWFLDQLEPGSAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFVEVDGEPVQVILPPLPLPLPVVD 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  775 ISSM----KESDIPAFLRKKVKEPYVKENSPLVRVMSFSRSEQEHFLLVVIHHLIFDGVSSVTFIHSLFDTYQLLLKGQQ 850
Cdd:cd19531     83 LSGLpeaeREAEAQRLAREEARRPFDLARGPLLRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYAAFLAGRP 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  851 PEIAVSPAIYHDFAAWEKNMLAGKDGVKHRTYWQKQLSGTLPNLQLPkvsA----SSVSEFREDTYTRRLSSGFMNQVRM 926
Cdd:cd19531    163 SPLPPLPIQYADYAVWQREWLQGEVLERQLAYWREQLAGAPPVLELP---TdrprPAVQSFRGARVRFTLPAELTAALRA 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  927 FAKEHsvNVT--TVFLSCYMMLLGRYTGQKEQIVGMPAMVRPEERFDDAIGHFLNMLPIRSELNPADTFSSFISKLQLTI 1004
Cdd:cd19531    240 LARRE--GATlfMTLLAAFQVLLHRYSGQDDIVVGTPVAGRNRAELEGLIGFFVNTLVLRTDLSGDPTFRELLARVRETA 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1005 LDGLDHAAYPFPKMVRDLNIPRSQAGSPVFQTAFFYQNFLQSGSYQSLLsryadffSVDYVEYIHQEGEYELVFELWETE 1084
Cdd:cd19531    318 LEAYAHQDLPFEKLVEALQPERDLSRSPLFQVMFVLQNAPAAALELPGL-------TVEPLEVDSGTAKFDLTLSLTETD 390
                          410       420       430
                   ....*....|....*....|....*....|....*..
gi 1776025254 1085 EKMELNIKYNTGLFDAASISAMFDHFVYVTEQAMLNP 1121
Cdd:cd19531    391 GGLRGSLEYNTDLFDAATIERMAGHFQTLLEAIVADP 427
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
31-564 4.87e-91

O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440087 [Multi-domain]  Cd Length: 452  Bit Score: 305.58  E-value: 4.87e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254   31 IPEVLYRTAAELGDTKGIIYlqpDGTEVyqSYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNSQLLPAFWGCVLTGVV 110
Cdd:COG0318      1 LADLLRRAAARHPDRPALVF---GGRRL--TYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAV 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  111 PAPlaVPPTYAEsssgtQKLKDAWTLLDKPAVITdrgmhqemldwakeqglegfraiivedllsaeadtdwhqsspedlA 190
Cdd:COG0318     76 VVP--LNPRLTA-----EELAYILEDSGARALVT---------------------------------------------A 103
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  191 LLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDHVGGIGMLHLRDVYLGCQeinvsseTILME-- 268
Cdd:COG0318    104 LILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGAT-------LVLLPrf 176
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  269 -PLKWLDWIDHYRASV-TWAPNFAFGLvtdfAEEIKDRKWDLSSMRYMLNGGEAMVAKVGRRILELLEPhglpadAIRPA 346
Cdd:COG0318    177 dPERVLELIERERVTVlFGVPTMLARL----LRHPEFARYDLSSLRLVVSGGAPLPPELLERFEERFGV------RIVEG 246
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  347 WGMSETSSGVIFsheftRAGTSDDDHFVEIGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGYYQRPDLNESVFt 426
Cdd:COG0318    247 YGLTETSPVVTV-----NPEDPGERRPGSVGRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAF- 320
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  427 EDGWFETGDLGFLR-NGRLTITGRTKDAIIINGINYYSHAIESAVEELSEIetsytAACAV------RLGQnstdQLAIF 499
Cdd:COG0318    321 RDGWLRTGDLGRLDeDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGV-----AEAAVvgvpdeKWGE----RVVAF 391
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1776025254  500 FVTS--AKLNDEQMSQLLRniqSHVSQvIGVtPEYLLPVqkEEIPKTAIGKIQRTQLKTSFENGEFD 564
Cdd:COG0318    392 VVLRpgAELDAEELRAFLR---ERLAR-YKV-PRRVEFV--DELPRTASGKIDRRALRERYAAGALE 451
PRK04813 PRK04813
D-alanine--poly(phosphoribitol) ligase subunit DltA;
1157-1640 3.38e-86

D-alanine--poly(phosphoribitol) ligase subunit DltA;


Pssm-ID: 235313 [Multi-domain]  Cd Length: 503  Bit Score: 293.34  E-value: 3.38e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1157 ELFEQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPS 1236
Cdd:PRK04813     6 ETIEEFAQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVDVS 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1237 YPAERLEYMLEDSEVFITLTTSELVNTLSwnGVTTALLDQDWDEIAQTASdrKVLTRTVTPENLAYVIYTSGSTGKPKGV 1316
Cdd:PRK04813    86 SPAERIEMIIEVAKPSLIIATEELPLEIL--GIPVITLDELKDIFATGNP--YDFDHAVKGDDNYYIIFTSGTTGKPKGV 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1317 MIPHKAL---TNFLVSMGETPgltAEDKMLAVTTYCFDIAALELFLPLIKGAHCYICQTEHTKDVEKLKRDIRTIKPTVM 1393
Cdd:PRK04813   162 QISHDNLvsfTNWMLEDFALP---EGPQFLNQAPYSFDLSVMDLYPTLASGGTLVALPKDMTANFKQLFETLPQLPINVW 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1394 QATPATWKMLFYSGWENEEN-----VKILCGgEALP----ETLKRYFLDtgSEAWNMFGPTETTIwsAV------QRIND 1458
Cdd:PRK04813   239 VSTPSFADMCLLDPSFNEEHlpnltHFLFCG-EELPhktaKKLLERFPS--ATIYNTYGPTEATV--AVtsieitDEMLD 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1459 ECSRATIGRPIANTQIYITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDnpfEPGSKLYRTGDMARwLPGG 1538
Cdd:PRK04813   314 QYKRLPIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFFT---FDGQPAYHTGDAGY-LEDG 389
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1539 RIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADM-----DNLAAYYTAKH----ANASLTaRELRHFVKNA 1609
Cdd:PRK04813   390 LLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYNkdhkvQYLIAYVVPKEedfeREFELT-KAIKKELKER 468
                          490       500       510
                   ....*....|....*....|....*....|.
gi 1776025254 1610 LPAYMVPSYFIQLDHMPLTPNGKIDRNSLKN 1640
Cdd:PRK04813   469 LMEYMIPRKFIYRDSLPLTPNGKIDRKALIE 499
omega_3_PfaA TIGR02813
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ...
3340-3881 3.42e-85

polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this alignment are involved in omega-3 polyunsaturated fatty acid biosynthesis, such as the protein PfaA from the eicosapentaenoic acid biosynthesis operon in Photobacterium profundum strain SS9. PfaA is encoded together with PfaB, PfaC, and PfaD, and the functions of the individual polypeptides have not yet been described. More distant homologs of PfaA, also included with the reach of this model, appear to be involved in polyketide-like biosynthetic mechanisms of polyunsaturated fatty acid biosynthesis, an alternative to the more familiar iterated mechanism of chain extension and desaturation, and in most cases are encoded near genes for homologs of PfaB, PfaC, and/or PfaD.


Pssm-ID: 274311 [Multi-domain]  Cd Length: 2582  Bit Score: 315.02  E-value: 3.42e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3340 PVAIVGISGRFPGAMDIDEFWKNLEEGKDSITEVPKDRWDWREHYGNPDTDVNKTDIKWGGFIDGVaEFDPLFFGISPRE 3419
Cdd:TIGR02813    8 PIAIVGMASIFANSRYLNKFWDLIFEKIDAITDVPSDHWAKDDYYDSDKSEADKSYCKRGGFLPEV-DFNPMEFGLPPNI 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3420 ADYVDPQQRLLMTYVWKALEDAGCPpQSLSGTGTGIFIGTG-----------------------NTGYKDL--------F 3468
Cdd:TIGR02813   87 LELTDISQLLSLVVAKEVLNDAGLP-DGYDRDKIGITLGVGggqkqssslnarlqypvlkkvfkASGVEDEdsemlikkF 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3469 HRANLPIEGHAATGhMIPSVGPNRMSYFLNIHGPSEPVETACSSSLVAIHRAVTAMQNGDCEMAIAGGVNTILTEEAHIS 3548
Cdd:TIGR02813  166 QDQYIHWEENSFPG-SLGNVISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGGVCTDNSPFMYMS 244
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3549 YSKAGMLSKDGRCKTFSADANGYVRGEGVGMVMLKKLEDAERDGNHIYGVIRGTAENHGGRANTLTSPNPKAQADLLVRA 3628
Cdd:TIGR02813  245 FSKTPAFTTNEDIQPFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGKFKSIYAPRPEGQAKALKRA 324
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3629 YRQAGIDPSTVTYIEAHGTGTELGDPIEINGLKAAFkelsnmrgeSQPDVPDHRCGIGSVKSNIGHLELAAGISGLIKVL 3708
Cdd:TIGR02813  325 YDDAGFAPHTCGLIEAHGTGTAAGDVAEFGGLVSVF---------SQDNDQKQHIALGSVKSQIGHTKSTAGTAGMIKAV 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3709 LQMKHKTLVKSLHCETLNPYLQLTDSPFYIVQEKQEWKSVTDcdgnELPRRAGISSFGIGGVNAHIVIEEYMPKA--NSE 3786
Cdd:TIGR02813  396 LALHHKVLPPTINVDQPNPKLDIENSPFYLNTETRPWMQRED----GTPRRAGISSFGFGGTNFHMVLEEYSPKHqrDDQ 471
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3787 HTATEQPNVIVLSAKNKSRLIDRASQLLEAIrNKKYTDQGLHRIAYTLQVGREEMD---ERLACVAGTMQELEEKL-QAF 3862
Cdd:TIGR02813  472 YRQRAVAQTLLFTAANEKALVSSLKDWKNKL-SAKADDQPYAFNALAVENTLRTIAvalARLGFVAKNADELITMLeQAI 550
                          570       580
                   ....*....|....*....|..
gi 1776025254 3863 VDGKEETDEFFR---GQSHRNK 3881
Cdd:TIGR02813  551 TQLEAKSCEEWQlpsGISYRKS 572
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
4588-4820 7.44e-79

Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains. The N-terminal domain contains most of the structures involved in dimer formation and also the active site cysteine.


Pssm-ID: 425468 [Multi-domain]  Cd Length: 251  Bit Score: 262.57  E-value: 7.44e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4588 EGIAVVGLSCRFPGAETLESYWSLLSEGRSSIGPIPAERWGCKTPYY------------AGVIDGVSYFDPDFFLLHEED 4655
Cdd:pfam00109    1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIPADRWDPDKLYDppsriagkiytkWGGLDDIFDFDPLFFGISPRE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4656 VRAMDPQALLVLEECLKLLYHAGYTPEEIKGKPVGVYIGGRSQHKPDEDSLDHAKNP------IVTVGQNYLAANLSQFF 4729
Cdd:pfam00109   81 AERMDPQQRLLLEAAWEALEDAGITPDSLDGSRTGVFIGSGIGDYAALLLLDEDGGPrrgspfAVGTMPSVIAGRISYFL 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4730 DVRGPSVVVDTACSSALVGMNMAIQALRGGDIQSAIVGGVSLLSSDASHRLFDRRGILSKHSSFHVFDERADGVVLGEGV 4809
Cdd:pfam00109  161 GLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSPDGPCKAFDPFADGFVRGEGV 240
                          250
                   ....*....|.
gi 1776025254 4810 GMVMLKTVKQA 4820
Cdd:pfam00109  241 GAVVLKRLSDA 251
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
1760-2009 5.80e-77

Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains. The N-terminal domain contains most of the structures involved in dimer formation and also the active site cysteine.


Pssm-ID: 425468 [Multi-domain]  Cd Length: 251  Bit Score: 256.79  E-value: 5.80e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1760 DSVAIIGISCEFPGAKNHDEFWENLRDGKESIAFFNKE--ELQRFGISKEIAENADYVPAKAsIEGKDRFDPSFFQISPK 1837
Cdd:pfam00109    1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIPADrwDPDKLYDPPSRIAGKIYTKWGG-LDDIFDFDPLFFGISPR 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1838 DAEFMDPQLRMLLTHSWKAIEDAGYAAGQI--PQTSVFMSASNNSYRALLPSDTTESLEtpDGYVSWVLAQSGTIPTMIS 1915
Cdd:pfam00109   80 EAERMDPQQRLLLEAAWEALEDAGITPDSLdgSRTGVFIGSGIGDYAALLLLDEDGGPR--RGSPFAVGTMPSVIAGRIS 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1916 HKLGLRGPSYFVHANCSSSLIGLHSAYKSLLSAESDYALVGGATLHTESNIGYVHQPGLNFSSDGHIKAFDASADGMIGG 1995
Cdd:pfam00109  158 YFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSPDGPCKAFDPFADGFVRG 237
                          250
                   ....*....|....
gi 1776025254 1996 EGVAVVLLKKAADA 2009
Cdd:pfam00109  238 EGVGAVVLKRLSDA 251
AFD_class_I cd04433
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ...
188-550 6.52e-75

Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341228 [Multi-domain]  Cd Length: 336  Bit Score: 254.52  E-value: 6.52e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  188 DLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDHVGGIGmLHLRDVYLGCQeinvsseTILM 267
Cdd:cd04433      1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLF-GLLGALLAGGT-------VVLL 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  268 E---PLKWLDWIDHYRASVTWAPNFAFGLVTDFAEEikdRKWDLSSMRYMLNGGEAMVAKVGRRILELLEPhglpadAIR 344
Cdd:cd04433     73 PkfdPEAALELIEREKVTILLGVPTLLARLLKAPES---AGYDLSSLRALVSGGAPLPPELLERFEEAPGI------KLV 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  345 PAWGMSETSSGVIFSheftrAGTSDDDHFVEIGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGYYQRPDLNESV 424
Cdd:cd04433    144 NGYGLTETGGTVATG-----PPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAV 218
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  425 FtEDGWFETGDLGFLR-NGRLTITGRTKDAIIINGINYYSHAIESAVEELSEIetsytAACAV------RLGQnstdQLA 497
Cdd:cd04433    219 D-EDGWYRTGDLGRLDeDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGV-----AEAAVvgvpdpEWGE----RVV 288
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1776025254  498 IFFVTsaklnDEQMSQLLRNIQSHVSQVIG--VTPEYLLPVqkEEIPKTAIGKIQ 550
Cdd:cd04433    289 AVVVL-----RPGADLDAEELRAHVRERLApyKVPRRVVFV--DALPRTASGKID 336
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
909-1775 8.90e-74

L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.


Pssm-ID: 274582 [Multi-domain]  Cd Length: 1389  Bit Score: 274.63  E-value: 8.90e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  909 EDTYTRRLSSgfmnqvRMFAKEHSVNVTTVFLSCYMMLLGRYTGQKEQIVGmpamVRPEERFDDAIghflnmlpIRSELN 988
Cdd:TIGR03443   28 EATYSLQLPS------AEVTAGGGSTPFIILLAAFAALVYRLTGDEDIVLG----TSSNKSGRPFV--------LRLNIT 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  989 PADTFSSFISKLQLTILDGLDHAAYPFPKMVRDLNIP-RSQAGSPVFQTAFFYQNFLQSgsyqsllSRYADFFSVDYVEY 1067
Cdd:TIGR03443   90 PELSFLQLYAKVSEEEKEGASDIGVPFDELSEHIQAAkKLERTPPLFRLAFQDAPDNQQ-------TTYSTGSTTDLTVF 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1068 IHQEGEyelvfelweteeKMELNIKYNTGLFDAASISAMFDHFVYVTEQAMLNPSQPLKEYSLLPEAEKQMI------LK 1141
Cdd:TIGR03443  163 LTPSSP------------ELELSIYYNSLLFSSDRITIVADQLAQLLSAASSNPDEPIGKVSLITPSQKSLLpdptkdLD 230
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1142 TWNATGktypyiTFHELFEQQAKKTPDRAAV---------SYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDR 1212
Cdd:TIGR03443  231 WSGFRG------AIHDIFADNAEKHPDRTCVvetpsfldpSSKTRSFTYKQINEASNILAHYLLKTGIKRGDVVMIYAYR 304
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1213 SLDMLVGLLAILKAGGAYVPLDPSYPAER--------------------------LEYMLEDSEVFITLTTSELVNTLSw 1266
Cdd:TIGR03443  305 GVDLVVAVMGVLKAGATFSVIDPAYPPARqtiylsvakpraliviekagtldqlvRDYIDKELELRTEIPALALQDDGS- 383
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1267 ngVTTALLDQDWDEIAQTASDRKVlTRT---VTPENLAYVIYTSGSTGKPKGVMIPHKALTNFLVSMGETPGLTAEDKML 1343
Cdd:TIGR03443  384 --LVGGSLEGGETDVLAPYQALKD-TPTgvvVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFGLSENDKFT 460
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1344 AVTTYCFDIAALELFLPLIKGAHCYICQTEHTKDVEKLKRDIRTIKPTVMQATPATWKML--------------FYSGwe 1409
Cdd:TIGR03443  461 MLSGIAHDPIQRDMFTPLFLGAQLLVPTADDIGTPGRLAEWMAKYGATVTHLTPAMGQLLsaqattpipslhhaFFVG-- 538
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1410 neenvKILcggealpetLKRYFLDTGSEA-----WNMFGPTETTiwSAVQ------RINDECSRATI------GRPIANT 1472
Cdd:TIGR03443  539 -----DIL---------TKRDCLRLQTLAenvciVNMYGTTETQ--RAVSyfeipsRSSDSTFLKNLkdvmpaGKGMKNV 602
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1473 QIYITD----SQLAPVpaGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPF-EPGS---------------------KLY 1526
Cdd:TIGR03443  603 QLLVVNrndrTQTCGV--GEVGEIYVRAGGLAEGYLGLPELNAEKFVNNWFvDPSHwidldkennkperefwlgprdRLY 680
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1527 RTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECV--VVADMDN---LAAYYTAKHANASLTA-- 1599
Cdd:TIGR03443  681 RTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVtlVRRDKDEeptLVSYIVPQDKSDELEEfk 760
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1600 -----------------------RELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLKNIDLSGEQLKQRQTSPk 1656
Cdd:TIGR03443  761 sevddeessdpvvkglikyrkliKDIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKPALPFPDTAQLAAVAKNRSA- 839
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1657 NIQDTVFT--------IWQEVL--KTSDIEWDDGFFDVGGDSLLAVTVADRIKHELSCEFSVTDLFEYSTIKNISQYITE 1726
Cdd:TIGR03443  840 SAADEEFTetereirdLWLELLpnRPATISPDDSFFDLGGHSILATRMIFELRKKLNVELPLGLIFKSPTIKGFAKEVDR 919
                          970       980       990      1000      1010
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1776025254 1727 -QRMGNASDHMPTdppahIEDQSTEMSDLpDYYDDSVAII-GISCEFPGAK 1775
Cdd:TIGR03443  920 lKKGEELADEGDS-----EIEEEETVLEL-DYAKDAKTLVdSLPKSYPSRK 964
PRK07768 PRK07768
long-chain-fatty-acid--CoA ligase; Validated
33-553 1.22e-73

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236091 [Multi-domain]  Cd Length: 545  Bit Score: 258.39  E-value: 1.22e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254   33 EVLYRTAAelGDTKGIIYLQPDGtEVYQSYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNSQLLPAFWGCVLTGVV-- 110
Cdd:PRK07768     6 EKMYANAR--TSPRGMVTGEPDA-PVRHTWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASlt 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  111 ----PAPLAVPPTYAESSsgtqklKDAWTLLDKPAVITDrgmhqEMLDWAKEQgLE--GFRAIIVEDLLSAEAdTDWHQS 184
Cdd:PRK07768    83 mlhqPTPRTDLAVWAEDT------LRVIGMIGAKAVVVG-----EPFLAAAPV-LEekGIRVLTVADLLAADP-IDPVET 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  185 SPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTRE-DITFNWMPFDH-VGGIGMLHLrDVYLGCQEINVSS 262
Cdd:PRK07768   150 GEDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVEtDVMVSWLPLFHdMGMVGFLTV-PMYFGAELVKVTP 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  263 ETILMEPLKWLDWIDHYRASVTWAPNFAFGLVTD-FAEEIKDRKWDLSSMRYMLNGGEAMVAKVGRRILELLEPHGLPAD 341
Cdd:PRK07768   229 MDFLRDPLLWAELISKYRGTMTAAPNFAYALLARrLRRQAKPGAFDLSSLRFALNGAEPIDPADVEDLLDAGARFGLRPE 308
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  342 AIRPAWGMSETSSGVIFSHEFT----------------RAGTSDDDH---FVEIGSPIPGFSMRIVNDHNELVEEGEIGR 402
Cdd:PRK07768   309 AILPAYGMAEATLAVSFSPCGAglvvdevdadllaalrRAVPATKGNtrrLATLGPPLPGLEVRVVDEDGQVLPPRGVGV 388
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  403 FQVSGLSVTSGYYQrPDLNESVFTEDGWFETGDLGFL-RNGRLTITGRTKDAIIINGINYYSHAIESAVEELSEIETSyt 481
Cdd:PRK07768   389 IELRGESVTPGYLT-MDGFIPAQDADGWLDTGDLGYLtEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVRPG-- 465
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1776025254  482 AACAVRL-GQNSTDQLAIFFVTSAKLNDEQMSQLLRNIQSHVSQVIGVTPEYLLPVQKEEIPKTAIGKIQRTQ 553
Cdd:PRK07768   466 NAVAVRLdAGHSREGFAVAVESNAFEDPAEVRRIRHQVAHEVVAEVGVRPRNVVVLGPGSIPKTPSGKLRRAN 538
FC-FACS_FadD_like cd05936
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ...
1157-1639 8.95e-72

Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341259 [Multi-domain]  Cd Length: 468  Bit Score: 250.17  E-value: 8.95e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1157 ELFEQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGP-DRLAgIYVDRSLDMLVGLLAILKAGGAYVPLDP 1235
Cdd:cd05936      3 DLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPgDRVA-LMLPNCPQFPIAYFGALKAGAVVVPLNP 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1236 SYPAERLEYMLEDSevfitlttselvntlswnGVTTALLDQDWDEIAQTASdRKVLTRTVTPENLAYVIYTSGSTGKPKG 1315
Cdd:cd05936     82 LYTPRELEHILNDS------------------GAKALIVAVSFTDLLAAGA-PLGERVALTPEDVAVLQYTSGTTGVPKG 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1316 VMIPHKALT-NFLVSMG-ETPGLTAEDKMLAVT----TYCFDIAaleLFLPLIKGAHCYIcqtEHTKDVEKLKRDIRTIK 1389
Cdd:cd05936    143 AMLTHRNLVaNALQIKAwLEDLLEGDDVVLAALplfhVFGLTVA---LLLPLALGATIVL---IPRFRPIGVLKEIRKHR 216
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1390 PTVMQATPATWKMLFYSGWENEENVK----ILCGGEALPETLKRYFLD-TGSEAWNMFGPTETTIWSAVQRINDECSRAT 1464
Cdd:cd05936    217 VTIFPGVPTMYIALLNAPEFKKRDFSslrlCISGGAPLPVEVAERFEElTGVPIVEGYGLTETSPVVAVNPLDGPRKPGS 296
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1465 IGRPIANTQIYITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPFepgsklyRTGDMARWLPGGRIEYIG 1544
Cdd:cd05936    297 IGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVDGWL-------RTGDIGYMDEDGYFFIVD 369
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1545 RIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMDNLA-----AYYTAKHaNASLTARELRHFVKNALPAYMVPSYF 1619
Cdd:cd05936    370 RKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSgeavkAFVVLKE-GASLTEEEIIAFCREQLAGYKVPRQV 448
                          490       500
                   ....*....|....*....|
gi 1776025254 1620 IQLDHMPLTPNGKIDRNSLK 1639
Cdd:cd05936    449 EFRDELPKSAVGKILRRELR 468
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
2849-3034 6.18e-70

KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.


Pssm-ID: 430138 [Multi-domain]  Cd Length: 180  Bit Score: 233.99  E-value: 6.18e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2849 GVYLITGGAGSLGLLFAKEIANRtGRSTIVLTGRSVLS-EDKENELEALRSIGAEVVYREADVSDQHAVHHLFEEIKERY 2927
Cdd:pfam08659    1 GTYLITGGLGGLGRELARWLAER-GARHLVLLSRSAAPrPDAQALIAELEARGVEVVVVACDVSDPDAVAALLAEIKAEG 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2928 GTLNGIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSGLLHVDECSKDFPLDFFIFFSSVSGCLGNAGQADYAAANSFMDAF 3007
Cdd:pfam08659   80 PPIRGVIHAAGVLRDALLENMTDEDWRRVLAPKVTGTWNLHEATPDEPLDFFVLFSSIAGLLGSPGQANYAAANAFLDAL 159
                          170       180
                   ....*....|....*....|....*..
gi 1776025254 3008 AEYRRSLAAskkrfgSTISFNWPLWEE 3034
Cdd:pfam08659  160 AEYRRSQGL------PATSINWGPWAE 180
A_NRPS_acs4 cd17654
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ...
1167-1638 1.44e-69

acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341309 [Multi-domain]  Cd Length: 449  Bit Score: 243.15  E-value: 1.44e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1167 PDRAAVS-YEGQ---TLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERL 1242
Cdd:cd17654      1 PDRPALIiDQTTsdtTVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1243 EYMLEDSEVFITLTTSELVNTlswngvttalldqdwdeiAQTASDRKVLTRTVTPENLAYVIYTSGSTGKPKGVMIPHKA 1322
Cdd:cd17654     81 LTVMKKCHVSYLLQNKELDNA------------------PLSFTPEHRHFNIRTDECLAYVIHTSGTTGTPKIVAVPHKC 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1323 LTNFLVSMGETPGLTAEDKMLAVTTYCFDIAALELFLPLIKGAHCYICQTEHTKDVEKLKRDIRTI-KPTVMQATPATWK 1401
Cdd:cd17654    143 ILPNIQHFRSLFNITSEDILFLTSPLTFDPSVVEIFLSLSSGATLLIVPTSVKVLPSKLADILFKRhRITVLQATPTLFR 222
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1402 MLFYSGWENE-----ENVKILC-GGEALP-----ETLKRYFLDTgsEAWNMFGPTETTIWSAVQRINDECSRATIGRPIA 1470
Cdd:cd17654    223 RFGSQSIKSTvlsatSSLRVLAlGGEPFPslvilSSWRGKGNRT--RIFNIYGITEVSCWALAYKVPEEDSPVQLGSPLL 300
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1471 NTQIYITDSQlapvPAGVPGELciAGDGVAKGYYKKEELTdsrfidnpfEPGSKLYRTGDMARwLPGGRIEYIGRIDNQV 1550
Cdd:cd17654    301 GTVIEVRDQN----GSEGTGQV--FLGGLNRVCILDDEVT---------VPKGTMRATGDFVT-VKDGELFFLGRKDSQI 364
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1551 KIRGFRIELGDIESRLSEHPGILECVV-VADMDNLAAYYTAKhanaSLTARELRHFVKNALPAYMVPSYFIQLDHMPLTP 1629
Cdd:cd17654    365 KRRGKRINLDLIQQVIESCLGVESCAVtLSDQQRLIAFIVGE----SSSSRIHKELQLTLLSSHAIPDTFVQIDKLPLTS 440

                   ....*....
gi 1776025254 1630 NGKIDRNSL 1638
Cdd:cd17654    441 HGKVDKSEL 449
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
2849-3034 5.13e-69

This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.


Pssm-ID: 214833 [Multi-domain]  Cd Length: 180  Bit Score: 231.22  E-value: 5.13e-69
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  2849 GVYLITGGAGSLGLLFAKEIANRTGRsTIVLTGRSVLSEDKENEL-EALRSIGAEVVYREADVSDQHAVHHLFEEIKERY 2927
Cdd:smart00822    1 GTYLITGGLGGLGRALARWLAERGAR-RLVLLSRSGPDAPGAAALlAELEAAGARVTVVACDVADRDALAAVLAAIPAVE 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  2928 GTLNGIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSGLLHVDECSKDFPLDFFIFFSSVSGCLGNAGQADYAAANSFMDAF 3007
Cdd:smart00822   80 GPLTGVIHAAGVLDDGVLASLTPERFAAVLAPKAAGAWNLHELTADLPLDFFVLFSSIAGVLGSPGQANYAAANAFLDAL 159
                           170       180
                    ....*....|....*....|....*..
gi 1776025254  3008 AEYRRSLAaskkrfGSTISFNWPLWEE 3034
Cdd:smart00822  160 AEYRRARG------LPALSIAWGAWAE 180
AFD_class_I cd04433
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ...
1300-1634 3.01e-68

Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341228 [Multi-domain]  Cd Length: 336  Bit Score: 235.26  E-value: 3.01e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1300 LAYVIYTSGSTGKPKGVMIPHKALTNFLVSMGETPGLTAEDKMLAVTTYCFDIAALELFLPLIKGAHCYIcqtEHTKDVE 1379
Cdd:cd04433      2 PALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVL---LPKFDPE 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1380 KLKRDIRTIKPTVMQATPATWKMLFYSGWENEEN----VKILCGGEALPETLKRYFLD-TGSEAWNMFGPTETTIWSAVQ 1454
Cdd:cd04433     79 AALELIEREKVTILLGVPTLLARLLKAPESAGYDlsslRALVSGGAPLPPELLERFEEaPGIKLVNGYGLTETGGTVATG 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1455 RINDECSRA-TIGRPIANTQIYITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNpfepgskLYRTGDMAR 1533
Cdd:cd04433    159 PPDDDARKPgSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVDEDG-------WYRTGDLGR 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1534 WLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVA----DMDNLAAYYTAKHANASLTARELRHFVKNA 1609
Cdd:cd04433    232 LDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGvpdpEWGERVVAVVVLRPGADLDAEELRAHVRER 311
                          330       340
                   ....*....|....*....|....*
gi 1776025254 1610 LPAYMVPSYFIQLDHMPLTPNGKID 1634
Cdd:cd04433    312 LAPYKVPRRVVFVDALPRTASGKID 336
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
3340-3776 5.20e-63

Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible for the elongation steps in fatty acid biosynthesis. KASIII catalyses the initial condensation and KAS I and II catalyze further elongation steps by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP.


Pssm-ID: 238430 [Multi-domain]  Cd Length: 406  Bit Score: 222.80  E-value: 5.20e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3340 PVAIVGISGRFPGAMDIDEFWKNLEEGKDSITEVPKDrwdwrehygnpdtDVNKTDIKWGGFIDGVAEFDPlffgISPRE 3419
Cdd:cd00834      2 RVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRF-------------DASGFPSRIAGEVPDFDPEDY----LDRKE 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3420 ADYVDPQQRLLMTYVWKALEDAGCPPQSLSGTGTGIFIGTGNTGYKDL--FHRANLPIEGHAATGHMIPSVGPNRMSYF- 3496
Cdd:cd00834     65 LRRMDRFAQFALAAAEEALADAGLDPEELDPERIGVVIGSGIGGLATIeeAYRALLEKGPRRVSPFFVPMALPNMAAGQv 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3497 ---LNIHGPSEPVETACSSSLVAIHRAVTAMQNGDCEMAIAGGVNTILTEEAHISYSKAGMLSKDG-----RCKTFSADA 3568
Cdd:cd00834    145 airLGLRGPNYTVSTACASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALRALSTRNddpekASRPFDKDR 224
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3569 NGYVRGEGVGMVMLKKLEDAERDGNHIYGVIRGTAENhgGRANTLTSPNPKAQADLLV--RAYRQAGIDPSTVTYIEAHG 3646
Cdd:cd00834    225 DGFVLGEGAGVLVLESLEHAKARGAKIYAEILGYGAS--SDAYHITAPDPDGEGAARAmrAALADAGLSPEDIDYINAHG 302
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3647 TGTELGDPIEINGLKAAFkelsnmrGESQPDVPdhrcgIGSVKSNIGHLELAAGISGLIKVLLQMKHKTLVKSLHCETLN 3726
Cdd:cd00834    303 TSTPLNDAAESKAIKRVF-------GEHAKKVP-----VSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPD 370
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1776025254 3727 PYLQLTdspfYIVQEKQEWksvtdcdgnelPRRAGIS-SFGIGGVNAHIVI 3776
Cdd:cd00834    371 PECDLD----YVPNEAREA-----------PIRYALSnSFGFGGHNASLVF 406
PRK06187 PRK06187
long-chain-fatty-acid--CoA ligase; Validated
1150-1639 6.19e-63

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235730 [Multi-domain]  Cd Length: 521  Bit Score: 226.22  E-value: 6.19e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1150 YPYITFHELFEQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGP-DRLAgiYVDR-SLDMLVGLLAILKAG 1227
Cdd:PRK06187     3 DYPLTIGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKgDRVA--VFDWnSHEYLEAYFAVPKIG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1228 GAYVPLDPSYPAERLEYMLEDSEVFITLTTSELVNTLS-----------------WNGVTTALLDQDWDEIAQTASDRKV 1290
Cdd:PRK06187    81 AVLHPINIRLKPEEIAYILNDAEDRVVLVDSEFVPLLAailpqlptvrtvivegdGPAAPLAPEVGEYEELLAAASDTFD 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1291 lTRTVTPENLAYVIYTSGSTGKPKGVMIPHKALTNFLVSMGETPGLTAEDKMLAVTTyCFDIAALEL-FLPLIKGA---- 1365
Cdd:PRK06187   161 -FPDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVP-MFHVHAWGLpYLALMAGAkqvi 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1366 -HCYicqtehtkDVEKLKRDIRTIKPTVMQATPATWKMLF---------YSGWEneenvKILCGGEALPETLKRYFLDTG 1435
Cdd:PRK06187   239 pRRF--------DPENLLDLIETERVTFFFAVPTIWQMLLkaprayfvdFSSLR-----LVIYGGAALPPALLREFKEKF 305
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1436 S----EAWNMfgpTETTIWSAVQRINDECS-----RATIGRPIANTQIYITDSQLAPVPA--GVPGELCIAGDGVAKGYY 1504
Cdd:PRK06187   306 GidlvQGYGM---TETSPVVSVLPPEDQLPgqwtkRRSAGRPLPGVEARIVDDDGDELPPdgGEVGEIIVRGPWLMQGYW 382
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1505 KKEELTDSRFIDNpfepgskLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMDNL 1584
Cdd:PRK06187   383 NRPEATAETIDGG-------WLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEK 455
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1585 A-----AYYTAKhANASLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLK 1639
Cdd:PRK06187   456 WgerpvAVVVLK-PGATLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLR 514
FACL_FadD13-like cd17631
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ...
1159-1635 2.13e-62

fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.


Pssm-ID: 341286 [Multi-domain]  Cd Length: 435  Bit Score: 222.10  E-value: 2.13e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1159 FEQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGP-DRLAgIYVDRSLDMLVGLLAILKAGGAYVPLDPSY 1237
Cdd:cd17631      1 LRRRARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKgDRVA-VLSKNSPEFLELLFAAARLGAVFVPLNFRL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1238 PAERLEYMLEDSEvfitlttselvntlswngvTTALLDQdwdeiaqtasdrkvltrtvtpenLAYVIYTSGSTGKPKGVM 1317
Cdd:cd17631     80 TPPEVAYILADSG-------------------AKVLFDD-----------------------LALLMYTSGTTGRPKGAM 117
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1318 IPHKALTNFLVSMGETPGLTAEDKMLAVTTYcFDIAALELFLP--LIKGAHCYICqteHTKDVEKLKRDIRTIKPTVMQA 1395
Cdd:cd17631    118 LTHRNLLWNAVNALAALDLGPDDVLLVVAPL-FHIGGLGVFTLptLLRGGTVVIL---RKFDPETVLDLIERHRVTSFFL 193
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1396 TPATWKMLFYSGWENEENV----KILCGGEALPETLKRYFLDTGSEAWNMFGPTETTIWSAVQRINDECSRA-TIGRPIA 1470
Cdd:cd17631    194 VPTMIQALLQHPRFATTDLsslrAVIYGGAPMPERLLRALQARGVKFVQGYGMTETSPGVTFLSPEDHRRKLgSAGRPVF 273
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1471 NTQIYITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPFepgsklyRTGDMARWLPGGRIEYIGRIDNQV 1550
Cdd:cd17631    274 FVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFRDGWF-------HTGDLGRLDEDGYLYIVDRKKDMI 346
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1551 KIRGFRIELGDIESRLSEHPGILECVVVADMDNL-----AAYYTAKhANASLTARELRHFVKNALPAYMVPSYFIQLDHM 1625
Cdd:cd17631    347 ISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKwgeavVAVVVPR-PGAELDEDELIAHCRERLARYKIPKSVEFVDAL 425
                          490
                   ....*....|
gi 1776025254 1626 PLTPNGKIDR 1635
Cdd:cd17631    426 PRNATGKILK 435
FabB COG0304
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...
3341-3779 9.93e-62

3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism]; 3-oxoacyl-(acyl-carrier-protein) synthase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440073 [Multi-domain]  Cd Length: 409  Bit Score: 219.20  E-value: 9.93e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3341 VAIVGISGRFPGAMDIDEFWKNLEEGKDSITEVPKDrwdwrehygnpdtDVNKTDIKWGGFIDGvaeFDPLFFgISPREA 3420
Cdd:COG0304      3 VVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITRF-------------DASGLPVRIAGEVKD---FDPEEY-LDRKEL 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3421 DYVDPQQRLLMTYVWKALEDAGCPPQSLSGTGTGIFIGTGNTG-------YKDLFHRANLPIEGHAATGhMIPSVGPNRM 3493
Cdd:COG0304     66 RRMDRFTQYALAAAREALADAGLDLDEVDPDRTGVIIGSGIGGldtleeaYRALLEKGPRRVSPFFVPM-MMPNMAAGHV 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3494 SYFLNIHGPSEPVETACSSSLVAIHRAVTAMQNGDCEMAIAGGVNTILTEEAHISYSKAGMLSK-----DGRCKTFSADA 3568
Cdd:COG0304    145 SIRFGLKGPNYTVSTACASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLAGFDALGALSTrnddpEKASRPFDKDR 224
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3569 NGYVRGEGVGMVMLKKLEDAERDGNHIYGVIRGTAENHGGRANTLTSPNPKAQADLLVRAYRQAGIDPSTVTYIEAHGTG 3648
Cdd:COG0304    225 DGFVLGEGAGVLVLEELEHAKARGAKIYAEVVGYGASSDAYHITAPAPDGEGAARAMRAALKDAGLSPEDIDYINAHGTS 304
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3649 TELGDPIEINGLKAAFkelsnmrGESQPDVPdhrcgIGSVKSNIGHLELAAGISGLIKVLLQMKHKTLVKSLHCETLNPY 3728
Cdd:COG0304    305 TPLGDAAETKAIKRVF-------GDHAYKVP-----VSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPE 372
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1776025254 3729 LQLTdspfYIVQEKQewksvtdcdgnELPRRAGIS-SFGIGGVNAHIVIEEY 3779
Cdd:COG0304    373 CDLD----YVPNEAR-----------EAKIDYALSnSFGFGGHNASLVFKRY 409
PS-DH pfam14765
Polyketide synthase dehydratase; This is the dehydratase domain of polyketide synthases. ...
2373-2658 1.08e-61

Polyketide synthase dehydratase; This is the dehydratase domain of polyketide synthases. Structural analysis shows these DH domains are double hotdogs in which the active site contains a histidine from the N-terminal hotdog and an aspartate from the C-terminal hotdog. Studies have uncovered that a substrate tunnel formed between the DH domains may be essential for loading substrates and unloading products.


Pssm-ID: 434191  Cd Length: 296  Bit Score: 214.93  E-value: 1.08e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2373 HPLL-HQNTS-DFSEQKFSSVFTGDEF-FLRDHVVRGKPVLPGVAYLEMAYAAINQAAGSEIG---QDVRIRlnhtvwvQ 2446
Cdd:pfam14765    1 HPLLgSRVPSpSDLEPVWRNRLRLADLpWLRDHRVGGTVVLPGAGYLEMALEAARQLFGGSGAvalRDVSIL-------K 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2447 PVVVDRHSA-QVDISLFPEEDG---KITFDIYSTQEDGDDPVIHSQGSAELASAAETPVADLTEISRRC----GKGKMSP 2518
Cdd:pfam14765   74 ALVLPEDDPvEVQTSLTPEEDGadsWWEFEIFSRAGGGWEWTLHATGTVRLAPGEPAAPVDLESLPARCaqpaDPRSVSS 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2519 DQFYEEGRSRGMFHGPAFQGIKNVNIGNREVLAQLQLPEIVSGTNEQFVLHPSIMDSALQT-ATICIMQELTDQKLILPF 2597
Cdd:pfam14765  154 AEFYERLAARGLFYGPAFQGLRRIWRGDGEALAEARLPEAAAGGESPYLLHPALLDAALQLlGAALPAEAEHADQAYLPV 233
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1776025254 2598 ALEELEVIKG--CSSSMWAYARLSDSDHSGGVvqkADIDVIDESGSVCVRIKGFSTRVLEGEV 2658
Cdd:pfam14765  234 GIERLRIYRSlpPGEPLWVHARLERRGGRTIV---GDLTLVDEDGRVVARIEGLRLRRVEREA 293
KR_2_FAS_SDR_x cd08955
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 2, complex (x); ...
2817-3079 1.36e-60

beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 2, complex (x); Ketoreductase, a module of the multidomain polyketide synthase, has 2 subdomains, each corresponding to a short-chain dehydrogenases/reductase (SDR) family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerizes but is composed of 2 subdomains, each resembling an SDR monomer. In some instances, as in porcine FAS, an enoyl reductase (a Rossman fold NAD binding domain of the MDR family) module is inserted between the sub-domains. The active site resembles that of typical SDRs, except that the usual positions of the catalytic asparagine and tyrosine are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular polyketide synthases are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) fatty acid synthase. In some instances, such as porcine FAS , an enoyl reductase module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consists of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthesis uses dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-ketoacyl reductase (KR), forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-enoyl reductase (ER). Polyketide syntheses also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes the KR domain of the Lyngbya majuscule Jam J, -K, and #L which are encoded on the jam gene cluster and are involved in the synthesis of the Jamaicamides (neurotoxins); Lyngbya majuscule Jam P belongs to a different KR_FAS_SDR_x subfamily. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187658 [Multi-domain]  Cd Length: 376  Bit Score: 214.84  E-value: 1.36e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2817 QIRYEAGHRFV---KGWRemvlpsadtlHMPWRDEGVYLITGGAGSLGLLFAKEIANRtGRSTIVLTGRSVLSEDKENEL 2893
Cdd:cd08955    125 QVALRGGARYVarlVRAP----------ARPLRPDATYLITGGLGGLGLLVAEWLVER-GARHLVLTGRRAPSAAARQAI 193
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2894 EALRSIGAEVVYREADVSDQHAVHHLFEEIKERYGTLNGIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSGLLHVDECSKD 2973
Cdd:cd08955    194 AALEEAGAEVVVLAADVSDRDALAAALAQIRASLPPLRGVIHAAGVLDDGVLANQDWERFRKVLAPKVQGAWNLHQLTQD 273
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2974 FPLDFFIFFSSVSGCLGNAGQADYAAANSFMDAFAEYRRS--LAAskkrfgstISFNWPLWEEGGMQVGAEDEKRmLKTT 3051
Cdd:cd08955    274 LPLDFFVLFSSVASLLGSPGQANYAAANAFLDALAHYRRArgLPA--------LSINWGPWAEVGMAASLARQAR-LEAR 344
                          250       260
                   ....*....|....*....|....*...
gi 1776025254 3052 GMVPMPTDSGLKAFYQGIASDKPQVFVM 3079
Cdd:cd08955    345 GVGAISPAAGLQALGQLLRTGSTQVGVA 372
AMP-binding pfam00501
AMP-binding enzyme;
35-456 5.94e-60

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 214.10  E-value: 5.94e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254   35 LYRTAAELGDTkgiIYLQPDGTEVYqSYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNSQLLPAFWGCVLTGVVPAPl 114
Cdd:pfam00501    1 LERQAARTPDK---TALEVGEGRRL-TYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVP- 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  115 aVPPTYAESSSGTQkLKDAwtllDKPAVITDRGMHQEMLDWAKEQGLEGFRAIIV--------EDLLSAEADTDWHQS-- 184
Cdd:pfam00501   76 -LNPRLPAEELAYI-LEDS----GAKVLITDDALKLEELLEALGKLEVVKLVLVLdrdpvlkeEPLPEEAKPADVPPPpp 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  185 ---SPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQ----GFTREDITFNWMPFDHVGGIGMLHLRDVYLGCQe 257
Cdd:pfam00501  150 pppDPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRprgfGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGAT- 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  258 INVSSETILMEPLKWLDWIDHYRASVTWAPNFAFGLVTDFAEEikdRKWDLSSMRYMLNGGEAMVAKVGRRILELLephg 337
Cdd:pfam00501  229 VVLPPGFPALDPAALLELIERYKVTVLYGVPTLLNMLLEAGAP---KRALLSSLRLVLSGGAPLPPELARRFRELF---- 301
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  338 lpADAIRPAWGMSETSSGVIFS----HEFTRAGTsdddhfveIGSPIPGFSMRIVNDH-NELVEEGEIGRFQVSGLSVTS 412
Cdd:pfam00501  302 --GGALVNGYGLTETTGVVTTPlpldEDLRSLGS--------VGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMK 371
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*
gi 1776025254  413 GYYQRPDLNESVFTEDGWFETGDLG-FLRNGRLTITGRTKDAIII 456
Cdd:pfam00501  372 GYLNDPELTAEAFDEDGWYRTGDLGrRDEDGYLEIVGRKKDQIKL 416
PRK07656 PRK07656
long-chain-fatty-acid--CoA ligase; Validated
1157-1639 3.82e-59

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236072 [Multi-domain]  Cd Length: 513  Bit Score: 215.15  E-value: 3.82e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1157 ELFEQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGP-DRLAgIYVDRSLDMLVGLLAILKAGGAYVPLDP 1235
Cdd:PRK07656     9 ELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKgDRVA-IWAPNSPHWVIAALGALKAGAVVVPLNT 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1236 SYPAERLEYMLEDSEVFITLTTSEL-----------------VNTLSWNGVTTALLDQDWDEIAQTASDRKVlTRTVTPE 1298
Cdd:PRK07656    88 RYTADEAAYILARGDAKALFVLGLFlgvdysattrlpalehvVICETEEDDPHTEKMKTFTDFLAAGDPAER-APEVDPD 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1299 NLAYVIYTSGSTGKPKGVMIPHKALTNFLVSMGETPGLTAEDKMLAVT----TYCFDIAALElflPLIKGAHCYIcqtEH 1374
Cdd:PRK07656   167 DVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAANpffhVFGYKAGVNA---PLMRGATILP---LP 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1375 TKDVEKLKRDIRTIKPTVMQATPATWKMLFYSGWENEENVKILC----GGEALPETLKRYF-----LDTGSEAwnmFGPT 1445
Cdd:PRK07656   241 VFDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRlavtGAASMPVALLERFeselgVDIVLTG---YGLS 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1446 ETTIWSAVQRIND--ECSRATIGRPIANTQIYITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTdSRFIDnpfePGS 1523
Cdd:PRK07656   318 EASGVTTFNRLDDdrKTVAGTIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEAT-AAAID----ADG 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1524 KLYrTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVV--VADmDNLA----AYYTAKHAnASL 1597
Cdd:PRK07656   393 WLH-TGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVigVPD-ERLGevgkAYVVLKPG-AEL 469
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|..
gi 1776025254 1598 TARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLK 1639
Cdd:PRK07656   470 TEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRALR 511
KR_FAS_SDR_x cd05274
ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of ...
2770-3079 6.42e-59

ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. In some instances, such as porcine FAS, an enoyl reductase (ER) module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consist of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthase uses a dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-KR, forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-ER. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187582 [Multi-domain]  Cd Length: 375  Bit Score: 209.93  E-value: 6.42e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2770 AGVSGLLKTAEIEFSKLTAQVIEIEKPEEMIDLHLKLKDDSQRPFDKQIRYEAGHRFVKGWREMVLPSADTLHMPWRDEG 2849
Cdd:cd05274     72 AALWGLLRVLALEHPELWGGLVDLDAADAADEAAALAALLAGAPGEDELALRGGQRLVPRLVRAPAAALELAAAPGGLDG 151
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGLLFAKEIANRTGRsTIVLTGRSVLSEDKENELEALRSIGAEVVYREADVSDQHAVHHLFEEIkERYGT 2929
Cdd:cd05274    152 TYLITGGLGGLGLLVARWLAARGAR-HLVLLSRRGPAPRAAARAALLRAGGARVSVVRCDVTDPAALAALLAEL-AAGGP 229
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2930 LNGIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSGLLHVDECSKDFPLDFFIFFSSVSGCLGNAGQADYAAANSFMDAFAE 3009
Cdd:cd05274    230 LAGVIHAAGVLRDALLAELTPAAFAAVLAAKVAGALNLHELTPDLPLDFFVLFSSVAALLGGAGQAAYAAANAFLDALAA 309
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3010 YRRSLAaskkrfGSTISFNWPLWEEGGMqVGAEDEKRMLKTTGMVPMPTDSGLKAFYQGIASDKPQVFVM 3079
Cdd:cd05274    310 QRRRRG------LPATSVQWGAWAGGGM-AAAAALRARLARSGLGPLAPAEALEALEALLASDAPQAVVA 372
Acs COG0365
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
1156-1653 1.30e-58

Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];


Pssm-ID: 440134 [Multi-domain]  Cd Length: 565  Bit Score: 214.98  E-value: 1.30e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1156 HELFEQQAKKTPDRAAVSYEG-----QTLTYRELDERSTQLAIYLQAHGVGP-DRLAgIYVDRSLDMLVGLLAILKAGGA 1229
Cdd:COG0365     12 YNCLDRHAEGRGDKVALIWEGedgeeRTLTYAELRREVNRFANALRALGVKKgDRVA-IYLPNIPEAVIAMLACARIGAV 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1230 YVPLDPSYPAERLEYMLEDSE--VFIT---------------------LTTSELVNTLSWNGVTTALL---DQDWDEIAQ 1283
Cdd:COG0365     91 HSPVFPGFGAEALADRIEDAEakVLITadgglrggkvidlkekvdealEELPSLEHVIVVGRTGADVPmegDLDWDELLA 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1284 TASDrkvltrTVTPENL-----AYVIYTSGSTGKPKGVMIPHKA-LTNFLVSMGETPGLTAEDKMLAVTT--------YC 1349
Cdd:COG0365    171 AASA------EFEPEPTdaddpLFILYTSGTTGKPKGVVHTHGGyLVHAATTAKYVLDLKPGDVFWCTADigwatghsYI 244
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1350 fdiaaleLFLPLIKGAHCYICQ-TEHTKDVEKLKRDIRTIKPTVMQATPATWKMLFYSGwenEENVK---------ILCG 1419
Cdd:COG0365    245 -------VYGPLLNGATVVLYEgRPDFPDPGRLWELIEKYGVTVFFTAPTAIRALMKAG---DEPLKkydlsslrlLGSA 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1420 GEAL-PETLKRYFLDTGSEAWNMFGPTETT-IWSAVQRInDECSRATIGRPIANTQIYITDSQLAPVPAGVPGELCIAGD 1497
Cdd:COG0365    315 GEPLnPEVWEWWYEAVGVPIVDGWGQTETGgIFISNLPG-LPVKPGSMGKPVPGYDVAVVDEDGNPVPPGEEGELVIKGP 393
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1498 --GVAKGYYKKEEltdsRFIDNPFEPGSKLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILEC 1575
Cdd:COG0365    394 wpGMFRGYWNDPE----RYRETYFGRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEA 469
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1576 VVVA--DMDNLA---AYYTAK---HANASLtARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLKNIDLsGEQ 1647
Cdd:COG0365    470 AVVGvpDEIRGQvvkAFVVLKpgvEPSDEL-AKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKIAE-GRP 547

                   ....*.
gi 1776025254 1648 LKQRQT 1653
Cdd:COG0365    548 LGDTST 553
PRK09192 PRK09192
fatty acyl-AMP ligase;
56-563 2.26e-58

fatty acyl-AMP ligase;


Pssm-ID: 236403 [Multi-domain]  Cd Length: 579  Bit Score: 214.48  E-value: 2.26e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254   56 TEVYqSYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNSQLLPAFWGCVLTGVVPAPLAVPPTYAESSSGTQKLKDAWT 135
Cdd:PRK09192    47 EEAL-PYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPLPMGFGGRESYIAQLRGMLA 125
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  136 LLDKPAVITDrgmhQEMLDWAKE--QGLEGFRAIIVEDL-LSAEADTDWHQSSPEDLALLLLTSGSTGTPKAVMLNHRNI 212
Cdd:PRK09192   126 SAQPAAIITP----DELLPWVNEatHGNPLLHVLSHAWFkALPEADVALPRPTPDDIAYLQYSSGSTRFPRGVIITHRAL 201
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  213 MSMVKGIIQMQGFTRE-DITFNWMPFDH-VGGIGMLHlrdVYLGCQeINV---SSETILMEPLKWLDWIDHYRASVTWAP 287
Cdd:PRK09192   202 MANLRAISHDGLKVRPgDRCVSWLPFYHdMGLVGFLL---TPVATQ-LSVdylPTRDFARRPLQWLDLISRNRGTISYSP 277
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  288 NFAFGLVTDFAEEIKDRKWDLSSMRYMLNGGEAMVAKVGRRILELLEPHGLPADAIRPAWGMSETSSGVIFS-------- 359
Cdd:PRK09192   278 PFGYELCARRVNSKDLAELDLSCWRVAGIGADMIRPDVLHQFAEAFAPAGFDDKAFMPSYGLAEATLAVSFSplgsgivv 357
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  360 HEFTRAGTSDDDH-------------FVEIGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGYYQRPDlNESVFT 426
Cdd:PRK09192   358 EEVDRDRLEYQGKavapgaetrrvrtFVNCGKALPGHEIEIRNEAGMPLPERVVGHICVRGPSLMSGYFRDEE-SQDVLA 436
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  427 EDGWFETGDLGFLRNGRLTITGRTKDAIIINGINYYSHAIESAVEELSEIETSYTAACAVrlgqNSTDQLAIFFVTSAKL 506
Cdd:PRK09192   437 ADGWLDTGDLGYLLDGYLYITGRAKDLIIINGRNIWPQDIEWIAEQEPELRSGDAAAFSI----AQENGEKIVLLVQCRI 512
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1776025254  507 NDEQMSQLLRN-IQSHVSQVIGVTPEYLLpVQKEEIPKTAIGKIQRTQLKTSFENGEF 563
Cdd:PRK09192   513 SDEERRGQLIHaLAALVRSEFGVEAAVEL-VPPHSLPRTSSGKLSRAKAKKRYLSGAF 569
ligase_PEP_1 TIGR03098
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ...
1154-1639 2.34e-58

acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.


Pssm-ID: 211788 [Multi-domain]  Cd Length: 517  Bit Score: 212.72  E-value: 2.34e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1154 TFHELFEQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPL 1233
Cdd:TIGR03098    1 LLHHLLEDAAARLPDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1234 DPSYPAERLEYMLEDSEVFITLTTSELVNTLSWNGVTTALLDQ--------------------DWDEiAQTASDRKVLTR 1293
Cdd:TIGR03098   81 NPLLKAEQVAHILADCNVRLLVTSSERLDLLHPALPGCHDLRTliivgdpahaseghpgeepaSWPK-LLALGDADPPHP 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1294 tVTPENLAYVIYTSGSTGKPKGVMIPHKALTNFLVSMGETPGLTAEDKMLAVTTYCFDIAALELFLPLIKGAHCYICQTE 1373
Cdd:TIGR03098  160 -VIDSDMAAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPLSFDYGFNQLTTAFYVGATVVLHDYL 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1374 HTKDVEKL--KRDIrtikpTVMQATPATWKMLFYSGWENE--ENVKILC--GGEALPET---LKRYFLDTgsEAWNMFGP 1444
Cdd:TIGR03098  239 LPRDVLKAleKHGI-----TGLAAVPPLWAQLAQLDWPESaaPSLRYLTnsGGAMPRATlsrLRSFLPNA--RLFLMYGL 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1445 TE----TTIWSA-VQRINDecsraTIGRPIANTQIYITD---SQLAPvpaGVPGELCIAGDGVAKGYYKKEELTDSRFID 1516
Cdd:TIGR03098  312 TEafrsTYLPPEeVDRRPD-----SIGKAIPNAEVLVLRedgSECAP---GEEGELVHRGALVAMGYWNDPEKTAERFRP 383
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1517 NP-FEPGSKLYRT----GDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMD-----NLAA 1586
Cdd:TIGR03098  384 LPpFPGELHLPELavwsGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAFGVPDptlgqAIVL 463
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1776025254 1587 YYTAKhANASLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLK 1639
Cdd:TIGR03098  464 VVTPP-GGEELDRAALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKALA 515
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
4172-4368 1.32e-57

This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.


Pssm-ID: 214833 [Multi-domain]  Cd Length: 180  Bit Score: 198.48  E-value: 1.32e-57
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  4172 VLLITGGTRGIGLLCARHFAECyGVKKLVLTGREQLPPREEWArfktsntslaekiqAVRELEAKGVQVEMLSLTLSDDA 4251
Cdd:smart00822    2 TYLITGGLGGLGRALARWLAER-GARRLVLLSRSGPDAPGAAA--------------LLAELEAAGARVTVVACDVADRD 66
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  4252 QVEQTLQHIKRTLGPIGGVIHCAGLTDMDTLAfiRKTSDDIQRVMEPKVSGLTTLYRHVCNEPLQFFVLFSSVSAIIPel 4331
Cdd:smart00822   67 ALAAVLAAIPAVEGPLTGVIHAAGVLDDGVLA--SLTPERFAAVLAPKAAGAWNLHELTADLPLDFFVLFSSIAGVLG-- 142
                           170       180       190
                    ....*....|....*....|....*....|....*...
gi 1776025254  4332 SAGQADYAMANSYMDYFAEAHQKHV-PIISVQWPNWKE 4368
Cdd:smart00822  143 SPGQANYAAANAFLDALAEYRRARGlPALSIAWGAWAE 180
KR_FAS_SDR_x cd05274
ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of ...
4056-4411 3.01e-56

ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. In some instances, such as porcine FAS, an enoyl reductase (ER) module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consist of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthase uses a dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-KR, forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-ER. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187582 [Multi-domain]  Cd Length: 375  Bit Score: 202.23  E-value: 3.01e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4056 VQRLVEFGHKEGLRLLCVTKGLESFQNTSVRMAGASR-AGLYRMLQCEYSHLISRHMDAEEVTDHPRLAKLiADEFYSES 4134
Cdd:cd05274     37 VAALLAAYASTGPPLWLVTRGAEAVSADDVAALAQAAlWGLLRVLALEHPELWGGLVDLDAADAADEAAAL-AALLAGAP 115
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4135 YDAEVCYRDGLRYQSFLKAHPETGkATEQSAVFPKDHVLLITGGTRGIGLLCARHFAECyGVKKLVLTGREQLPPREEWA 4214
Cdd:cd05274    116 GEDELALRGGQRLVPRLVRAPAAA-LELAAAPGGLDGTYLITGGLGGLGLLVARWLAAR-GARHLVLLSRRGPAPRAAAR 193
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4215 rfktsntslaekiqaVRELEAKGVQVEMLSLTLSDDAQVEQTLQHIkRTLGPIGGVIHCAGLTDMDTLAFIrkTSDDIQR 4294
Cdd:cd05274    194 ---------------AALLRAGGARVSVVRCDVTDPAALAALLAEL-AAGGPLAGVIHAAGVLRDALLAEL--TPAAFAA 255
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4295 VMEPKVSGLTTLYRHVCNEPLQFFVLFSSVSAIIpeLSAGQADYAMANSYMDYFAEA-HQKHVPIISVQWPNWKETGMG- 4372
Cdd:cd05274    256 VLAAKVAGALNLHELTPDLPLDFFVLFSSVAALL--GGAGQAAYAAANAFLDALAAQrRRRGLPATSVQWGAWAGGGMAa 333
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 1776025254 4373 -EVTNQAYRESGLFSITNSEGLRFLDQIVSKMFG-PVVLPA 4411
Cdd:cd05274    334 aAALRARLARSGLGPLAPAEALEALEALLASDAPqAVVASV 374
C_PKS-NRPS cd20483
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
695-1111 9.56e-56

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHXXXD motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380471 [Multi-domain]  Cd Length: 430  Bit Score: 202.49  E-value: 9.56e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  695 PLSEVQKGLWTLQKMSPEKSAYHVPLCFKFSSGLHLETLQQAFGLVLNQHPILKHVIQEKDGVPILKNEPALSIEIKTEN 774
Cdd:cd20483      3 PMSTFQRRLWFLHNFLEDKTFLNLLLVCHIKGKPDVNLLQKALSELVRRHEVLRTAYFEGDDFGEQQVLDDPSFHLIVID 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  775 ISSMK--ESDIPAFLRKKVKEPYVKENSPLVRVMSFSRSEQEHFLLVVIHHLIFDGVSSVTFIHSLFDTYQLLLKgQQPE 852
Cdd:cd20483     83 LSEAAdpEAALDQLVRNLRRQELDIEEGEVIRGWLVKLPDEEFALVLASHHIAWDRGSSKSIFEQFTALYDALRA-GRDL 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  853 IAVSP--AIYHDFAAWEKNMLAGKDGVKHRTYWQKQLSG---TLPNLQLPKVSASSVSEFREDTYTRRLSSGFMNQVRMF 927
Cdd:cd20483    162 ATVPPppVQYIDFTLWHNALLQSPLVQPLLDFWKEKLEGipdASKLLPFAKAERPPVKDYERSTVEATLDKELLARMKRI 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  928 AKEHSVnvtTVF---LSCYMMLLGRYTGQKEQIVGMPAMVRPEERFDDAIGHFLNMLPIRSELNPADTFSSFISKLQLTI 1004
Cdd:cd20483    242 CAQHAV---TPFmflLAAFRAFLYRYTEDEDLTIGMVDGDRPHPDFDDLVGFFVNMLPIRCRMDCDMSFDDLLESTKTTC 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1005 LDGLDHAAYPFPKMVRDLNIPRSQAGSPVFQTAFFYQnflQSGSYQSllSRYADFfsvDYVEYIHQEGE--YELVFELWE 1082
Cdd:cd20483    319 LEAYEHSAVPFDYIVDALDVPRSTSHFPIGQIAVNYQ---VHGKFPE--YDTGDF---KFTDYDHYDIPtaCDIALEAEE 390
                          410       420       430
                   ....*....|....*....|....*....|
gi 1776025254 1083 TEEK-MELNIKYNTGLFDAASISAMFDHFV 1111
Cdd:cd20483    391 DPDGgLDLRLEFSTTLYDSADMERFLDNFV 420
FC-FACS_FadD_like cd05936
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ...
31-555 8.75e-55

Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341259 [Multi-domain]  Cd Length: 468  Bit Score: 200.87  E-value: 8.75e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254   31 IPEVLYRTAAELGDTKGIIylqpdGTEVYQSYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNSQLLPAFWGCVLTGVV 110
Cdd:cd05936      1 LADLLEEAARRFPDKTALI-----FMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAV 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  111 PAPLAvpPTYaesssgtqklkdawtlldkpaviTDRGMHQEMLDwakeqglEGFRAIIV----EDLLSAEADTD-WHQSS 185
Cdd:cd05936     76 VVPLN--PLY-----------------------TPRELEHILND-------SGAKALIVavsfTDLLAAGAPLGeRVALT 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  186 PEDLALLLLTSGSTGTPKAVMLNHRNIMS---MVKGIIQmQGFTREDITFNWMPFDHVGGIGMLHLRDVYLGCQEINVSS 262
Cdd:cd05936    124 PEDVAVLQYTSGTTGVPKGAMLTHRNLVAnalQIKAWLE-DLLEGDDVVLAALPLFHVFGLTVALLLPLALGATIVLIPR 202
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  263 etilMEPLKWLDWIDHYRASV-TWAPNFAFGLVTDFAeeikDRKWDLSSMRYMLNGGEAMVAKVGRRILELLephGLPad 341
Cdd:cd05936    203 ----FRPIGVLKEIRKHRVTIfPGVPTMYIALLNAPE----FKKRDFSSLRLCISGGAPLPVEVAERFEELT---GVP-- 269
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  342 aIRPAWGMSETSSGVIFSH--EFTRAGTsdddhfveIGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGYYQRPD 419
Cdd:cd05936    270 -IVEGYGLTETSPVVAVNPldGPRKPGS--------IGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPE 340
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  420 LNESVFTeDGWFETGDLGFL-RNGRLTITGRTKDAIIINGINYYSHAIESAVEELSEIetsytAACAVrLG---QNSTDQ 495
Cdd:cd05936    341 ETAEAFV-DGWLRTGDIGYMdEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAV-----AEAAV-VGvpdPYSGEA 413
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1776025254  496 LAIFFV--TSAKLNDEQMSQLLRniqSHVsqvigvtPEYLLPVQ---KEEIPKTAIGKIQRTQLK 555
Cdd:cd05936    414 VKAFVVlkEGASLTEEEIIAFCR---EQL-------AGYKVPRQvefRDELPKSAVGKILRRELR 468
Firefly_Luc_like cd05911
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ...
61-550 4.64e-54

Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341237 [Multi-domain]  Cd Length: 486  Bit Score: 199.36  E-value: 4.64e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254   61 SYRRLWDDGLRIVKGLRQSGLKaKQSVILQLGDNS-QLLPAFWGCVLTGVVPAPLAvpPTYAESSSGTQkLKDAwtlldK 139
Cdd:cd05911     12 TYAQLRTLSRRLAAGLRKLGLK-KGDVVGIISPNStYYPPVFLGCLFAGGIFSAAN--PIYTADELAHQ-LKIS-----K 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  140 P-AVITDRGMHQEMLDWAKEQG---------LEGFRAIIVEDLLSAEA-DTDWHQ-----SSPEDLALLLLTSGSTGTPK 203
Cdd:cd05911     83 PkVIFTDPDGLEKVKEAAKELGpkdkiivldDKPDGVLSIEDLLSPTLgEEDEDLppplkDGKDDTAAILYSSGTTGLPK 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  204 AVMLNHRNIMSMvkgIIQMQGFT-----REDITFNWMPFDHVGGIGMLHLRdVYLGCqeinvssETILM---EPLKWLDW 275
Cdd:cd05911    163 GVCLSHRNLIAN---LSQVQTFLygndgSNDVILGFLPLYHIYGLFTTLAS-LLNGA-------TVIIMpkfDSELFLDL 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  276 IDHYRASVTWA--PNFAFglvtdFAEEIKDRKWDLSSMRYMLNGGeamvAKVGRRILELLEPHgLPADAIRPAWGMSETS 353
Cdd:cd05911    232 IEKYKITFLYLvpPIAAA-----LAKSPLLDKYDLSSLRVILSGG----APLSKELQELLAKR-FPNATIKQGYGMTETG 301
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  354 SGVIFSHEFtragtsdDDHFVEIGSPIPGFSMRIVNDH-NELVEEGEIGRFQVSGLSVTSGYYQRPDLNESVFTEDGWFE 432
Cdd:cd05911    302 GILTVNPDG-------DDKPGSVGRLLPNVEAKIVDDDgKDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGWLH 374
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  433 TGDLGFLR-NGRLTITGRTKDAIIINGINYYSHAIESAVEELSEIETsytaACAVRLGQNSTDQLAIFFVTSAKlnDEQM 511
Cdd:cd05911    375 TGDIGYFDeDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVAD----AAVIGIPDEVSGELPRAYVVRKP--GEKL 448
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*...
gi 1776025254  512 S--QLLRNIQSHVSQ-------VIGVtpeyllpvqkEEIPKTAIGKIQ 550
Cdd:cd05911    449 TekEVKDYVAKKVASykqlrggVVFV----------DEIPKSASGKIL 486
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
1762-2183 9.95e-54

Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible for the elongation steps in fatty acid biosynthesis. KASIII catalyses the initial condensation and KAS I and II catalyze further elongation steps by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP.


Pssm-ID: 238430 [Multi-domain]  Cd Length: 406  Bit Score: 195.84  E-value: 9.95e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1762 VAIIGISCEFPGAKNHDEFWENLRDGKESIAffnkeELQRFGISKEIAENADYVPAkasiegkdrFDPSFFqISPKDAEF 1841
Cdd:cd00834      3 VVITGLGAVTPLGNGVEEFWEALLAGRSGIR-----PITRFDASGFPSRIAGEVPD---------FDPEDY-LDRKELRR 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1842 MDPQLRMLLTHSWKAIEDAGYAAGQIPQ--TSVFMSASNNSYRALLPSDTTeSLETPDGYVSWVL---AQSGTIPTMISH 1916
Cdd:cd00834     68 MDRFAQFALAAAEEALADAGLDPEELDPerIGVVIGSGIGGLATIEEAYRA-LLEKGPRRVSPFFvpmALPNMAAGQVAI 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1917 KLGLRGPSYFVHANCSSSLIGLHSAYKSLLSAESDYALVGGA-TLHTESNIGyvhqpglNFSS--------DGHIKA--- 1984
Cdd:cd00834    147 RLGLRGPNYTVSTACASGAHAIGDAARLIRLGRADVVIAGGAeALITPLTLA-------GFAAlralstrnDDPEKAsrp 219
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1985 FDASADGMIGGEGVAVVLLKKAADAVKDGDHIYALLRGIGVNNDGADKVgfyAPSV--KGQADVVQQVMNQTKIHPESIC 2062
Cdd:cd00834    220 FDKDRDGFVLGEGAGVLVLESLEHAKARGAKIYAEILGYGASSDAYHIT---APDPdgEGAARAMRAALADAGLSPEDID 296
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2063 YVEAHGTGTKLGDPIELAALTNVYRQYTNKTQFCgigSVKTNIGHLDTAAGLAGCIKVVMSLYHQELAPSINYKEPNPNT 2142
Cdd:cd00834    297 YINAHGTSTPLNDAAESKAIKRVFGEHAKKVPVS---STKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPEC 373
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|..
gi 1776025254 2143 DLAsspfYVVDQkktlSREIQThRAALS-SFGLGGTNTHAIF 2183
Cdd:cd00834    374 DLD----YVPNE----AREAPI-RYALSnSFGFGGHNASLVF 406
LCL_NRPS cd19538
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ...
695-1121 2.66e-53

LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380461 [Multi-domain]  Cd Length: 432  Bit Score: 195.56  E-value: 2.66e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  695 PLSEVQKGLWTLQKMSPEKSAYHVPLCFKFSSGLHLETLQQAFGLVLNQHPILKHVIQEKDGVP---ILkNEPALSIEIK 771
Cdd:cd19538      3 PLSFAQRRLWFLHQLEGPSATYNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVFPEEDGVPyqlIL-EEDEATPKLE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  772 TENISsmkESDIPAFLRKKVKEPYVKENSPLVRVMSFSRSEQEHFLLVVIHHLIFDGVSSVTFIHSLFDTYQLLLKGQQP 851
Cdd:cd19538     82 IKEVD---EEELESEINEAVRYPFDLSEEPPFRATLFELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYRARCKGEAP 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  852 EIAVSPAIYHDFAAWEKNMLAGKDGVKHR-----TYWQKQLSGtLPN-LQLPK-VSASSVSEFREDTYTRRLSSGFMNQV 924
Cdd:cd19538    159 ELAPLPVQYADYALWQQELLGDESDPDSLiarqlAYWKKQLAG-LPDeIELPTdYPRPAESSYEGGTLTFEIDSELHQQL 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  925 RMFAKEHSVNVTTVFLSCYMMLLGRYTGQKEQIVGMPAMVRPEERFDDAIGHFLNMLPIRSEL--NPadTFSSFISKLQL 1002
Cdd:cd19538    238 LQLAKDNNVTLFMVLQAGFAALLTRLGAGTDIPIGSPVAGRNDDSLEDLVGFFVNTLVLRTDTsgNP--SFRELLERVKE 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1003 TILDGLDHAAYPFPKMVRDLNIPRSQAGSPVFQTAFFYQNFLQSgsyqSLlsryaDFFSVDYVEYIHQEG--EYELVFEL 1080
Cdd:cd19538    316 TNLEAYEHQDIPFERLVEALNPTRSRSRHPLFQIMLALQNTPQP----SL-----DLPGLEAKLELRTVGsaKFDLTFEL 386
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*.
gi 1776025254 1081 WE-----TEEKMELNIKYNTGLFDAASISAMFDHFVYVTEQAMLNP 1121
Cdd:cd19538    387 REqyndgTPNGIEGFIEYRTDLFDHETIEALAQRYLLLLESAVENP 432
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
696-939 2.78e-53

Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 188.71  E-value: 2.78e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  696 LSEVQKGLWtlqKMSPEKSAYHVPLCFKFSSGLHLETLQQAFGLVLNQHPILKHVIQEKDGVPILKNEPALSIEIKTENI 775
Cdd:COG4908      1 LSPAQKRFL---FLEPGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEEDGEPVQRIDPDADLPLEVVDL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  776 SSM----KESDIPAFLRKKVKEPYVKENSPLVRVMSFSRSEQEHFLLVVIHHLIFDGVSSVTFIHSLFDTYQLLLKGQQP 851
Cdd:COG4908     78 SALpepeREAELEELVAEEASRPFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALLEGEPP 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  852 EIAVSPAIYHDFAAWEKNMLAGKDGVKHRTYWQKQLSGTLPNLQLPK-VSASSVSEFREDTYTRRLSSGFMNQVRMFAKE 930
Cdd:COG4908    158 PLPELPIQYADYAAWQRAWLQSEALEKQLEYWRQQLAGAPPVLELPTdRPRPAVQTFRGATLSFTLPAELTEALKALAKA 237

                   ....*....
gi 1776025254  931 HSvnvTTVF 939
Cdd:COG4908    238 HG---ATVN 243
omega_3_PfaA TIGR02813
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ...
1759-2193 5.13e-53

polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this alignment are involved in omega-3 polyunsaturated fatty acid biosynthesis, such as the protein PfaA from the eicosapentaenoic acid biosynthesis operon in Photobacterium profundum strain SS9. PfaA is encoded together with PfaB, PfaC, and PfaD, and the functions of the individual polypeptides have not yet been described. More distant homologs of PfaA, also included with the reach of this model, appear to be involved in polyketide-like biosynthetic mechanisms of polyunsaturated fatty acid biosynthesis, an alternative to the more familiar iterated mechanism of chain extension and desaturation, and in most cases are encoded near genes for homologs of PfaB, PfaC, and/or PfaD.


Pssm-ID: 274311 [Multi-domain]  Cd Length: 2582  Bit Score: 208.71  E-value: 5.13e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1759 DDSVAIIGISCEFPGAKNHDEFWENLRDGKESIaffnkeelqrfgisKEIAEN----ADYVPAKASIEGKD--------- 1825
Cdd:TIGR02813    6 DMPIAIVGMASIFANSRYLNKFWDLIFEKIDAI--------------TDVPSDhwakDDYYDSDKSEADKSyckrggflp 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1826 --RFDPSFFQISPKDAEFMDPQLRMLLTHSWKAIEDA---------------GYAAGQIPQTSVFMSASNNSYRALLPSD 1888
Cdd:TIGR02813   72 evDFNPMEFGLPPNILELTDISQLLSLVVAKEVLNDAglpdgydrdkigitlGVGGGQKQSSSLNARLQYPVLKKVFKAS 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1889 TTESLETP-------DGYVSWvlaQSGTIPTM--------ISHKLGLRGPSYFVHANCSSSLIGLHSAYKSLLSAESDYA 1953
Cdd:TIGR02813  152 GVEDEDSEmlikkfqDQYIHW---EENSFPGSlgnvisgrIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMM 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1954 LVGGATLHTESNIGYVHQPGLNFSSDGHIKAFDASADGMIGGEGVAVVLLKKAADAVKDGDHIYALLRGIGVNNDGADKv 2033
Cdd:TIGR02813  229 ITGGVCTDNSPFMYMSFSKTPAFTTNEDIQPFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGKFK- 307
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2034 GFYAPSVKGQADVVQQVMNQTKIHPESICYVEAHGTGTKLGDPIELAALTNVYRQYTNKTQFCGIGSVKTNIGHLDTAAG 2113
Cdd:TIGR02813  308 SIYAPRPEGQAKALKRAYDDAGFAPHTCGLIEAHGTGTAAGDVAEFGGLVSVFSQDNDQKQHIALGSVKSQIGHTKSTAG 387
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2114 LAGCIKVVMSLYHQELAPSINYKEPNPNTDLASSPFYVVDQKKT-LSREIQT-HRAALSSFGLGGTNTHAIFEQFKRDSD 2191
Cdd:TIGR02813  388 TAGMIKAVLALHHKVLPPTINVDQPNPKLDIENSPFYLNTETRPwMQREDGTpRRAGISSFGFGGTNFHMVLEEYSPKHQ 467

                   ..
gi 1776025254 2192 KG 2193
Cdd:TIGR02813  468 RD 469
FabB COG0304
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...
1762-2186 1.21e-52

3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism]; 3-oxoacyl-(acyl-carrier-protein) synthase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440073 [Multi-domain]  Cd Length: 409  Bit Score: 192.62  E-value: 1.21e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1762 VAIIGISCEFPGAKNHDEFWENLRDGKESIAFfnkeeLQRFGISKeiaenadyVPAKASIEGKDrFDPSFFqISPKDAEF 1841
Cdd:COG0304      3 VVITGLGAVSPLGNGVEEFWEALLAGRSGIRP-----ITRFDASG--------LPVRIAGEVKD-FDPEEY-LDRKELRR 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1842 MDPQLRMLLTHSWKAIEDAGYAAGQI--PQTSVFMSASNNSYRALLPSDTTESLETPDgYVS--WVLAQ-SGTIPTMISH 1916
Cdd:COG0304     68 MDRFTQYALAAAREALADAGLDLDEVdpDRTGVIIGSGIGGLDTLEEAYRALLEKGPR-RVSpfFVPMMmPNMAAGHVSI 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1917 KLGLRGPSYFVHANCSSSLIGLHSAYKSLLSAESDYALVGGAtlhtESNIgyvHQPGLN-FSSdghIKA----------- 1984
Cdd:COG0304    147 RFGLKGPNYTVSTACASGAHAIGEAYRLIRRGRADVMIAGGA----EAAI---TPLGLAgFDA---LGAlstrnddpeka 216
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1985 ---FDASADGMIGGEGVAVVLLKKAADAVKDGDHIYALLRGIGVNNDGADKVGfYAPSVKGQADVVQQVMNQTKIHPESI 2061
Cdd:COG0304    217 srpFDKDRDGFVLGEGAGVLVLEELEHAKARGAKIYAEVVGYGASSDAYHITA-PAPDGEGAARAMRAALKDAGLSPEDI 295
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2062 CYVEAHGTGTKLGDPIELAALTNVYRQYTNKTQfcgIGSVKTNIGHLDTAAGLAGCIKVVMSLYHQELAPSINYKEPNPN 2141
Cdd:COG0304    296 DYINAHGTSTPLGDAAETKAIKRVFGDHAYKVP---VSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPE 372
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*.
gi 1776025254 2142 TDLAsspfYVVDQkktlSREIQThRAALS-SFGLGGTNTHAIFEQF 2186
Cdd:COG0304    373 CDLD----YVPNE----AREAKI-DYALSnSFGFGGHNASLVFKRY 409
decarbox_cond_enzymes cd00825
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ...
3426-3776 3.17e-52

decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new carbon-carbon bond by a decarboxylating Claisen-like condensation reaction. Members are involved in the synthesis of fatty acids and polyketides, a diverse group of natural products. Both pathways are an iterative series of additions of small carbon units, usually acetate, to a nascent acyl group. There are 2 classes of decarboxylating condensing enzymes, which can be distinguished by sequence similarity, type of active site residues and type of primer units (acetyl CoA or acyl carrier protein (ACP) linked units).


Pssm-ID: 238421 [Multi-domain]  Cd Length: 332  Bit Score: 189.00  E-value: 3.17e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3426 QQRLLMTYVWKALEDAGCPPQSLSGTGTGIFIGTGNTGYKDLFHRAN--LPIEGHAATGHMIPSVGpNRMSYFLNIHGPS 3503
Cdd:cd00825     11 VSILGFEAAERAIADAGLSREYQKNPIVGVVVGTGGGSPRFQVFGADamRAVGPYVVTKAMFPGAS-GQIATPLGIHGPA 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3504 EPVETACSSSLVAIHRAVTAMQNGDCEMAIAGGVNTILTEEAHISYSKAGMLSKDGRCKTFSADANGYVRGEGVGMVMLK 3583
Cdd:cd00825     90 YDVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAPMDCEFDAMGALSTPEKASRTFDAAADGFVFGDGAGALVVE 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3584 KLEDAERDGNHIYGVIRGTAENHGGRANTLTSPNPKAQADLLVRAYRQAGIDPSTVTYIEAHGTGTELGDPIEINGLKAA 3663
Cdd:cd00825    170 ELEHALARGAHIYAEIVGTAATIDGAGMGAFAPSAEGLARAAKEALAVAGLTVWDIDYLVAHGTGTPIGDVKELKLLRSE 249
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3664 FKelsnmrgesqpdvpDHRCGIGSVKSNIGHLELAAGISGLIKVLLQMKHKTLVKSLHCETLNPYLQLTdspfyivqekq 3743
Cdd:cd00825    250 FG--------------DKSPAVSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPPSIHIEELDEAGLNI----------- 304
                          330       340       350
                   ....*....|....*....|....*....|...
gi 1776025254 3744 ewksVTDCDGNElPRRAGISSFGIGGVNAHIVI 3776
Cdd:cd00825    305 ----VTETTPRE-LRTALLNGFGLGGTNATLVL 332
A_NRPS_alphaAR cd17647
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ...
1167-1638 3.44e-52

Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.


Pssm-ID: 341302 [Multi-domain]  Cd Length: 520  Bit Score: 194.66  E-value: 3.44e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1167 PDRAAV-------SYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPA 1239
Cdd:cd17647      2 PERTCVvetpslnSSKTRSFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPP 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1240 ERleymledSEVFITLTTSELVNTLSWNGVTtalldqdwdeiaqtasdrkvltrtVTPENLAYVIYTSGSTGKPKGVMIP 1319
Cdd:cd17647     82 AR-------QNIYLGVAKPRGLIVIRAAGVV------------------------VGPDSNPTLSFTSGSEGIPKGVLGR 130
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1320 HKALTNFLVSMGETPGLTAEDKMLAVTTYCFDIAALELFLPLIKGAHCYICQTEHTKDVEKLKRDIRTIKPTVMQATPAT 1399
Cdd:cd17647    131 HFSLAYYFPWMAKRFNLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTQDDIGTPGRLAEWMAKYGATVTHLTPAM 210
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1400 WKMLfySGWENEENVKILCG---GEALpetLKRYFLDTGSEA-----WNMFGPTET----TIWSAVQRINDEC----SRA 1463
Cdd:cd17647    211 GQLL--TAQATTPFPKLHHAffvGDIL---TKRDCLRLQTLAenvriVNMYGTTETqravSYFEVPSRSSDPTflknLKD 285
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1464 TI--GRPIANTQIYITD----SQLAPVpaGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPF-EPG-------------- 1522
Cdd:cd17647    286 VMpaGRGMLNVQLLVVNrndrTQICGI--GEVGEIYVRAGGLAEGYRGLPELNKEKFVNNWFvEPDhwnyldkdnnepwr 363
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1523 -------SKLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECV--VVADMDN---LAAYYTA 1590
Cdd:cd17647    364 qfwlgprDRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENItlVRRDKDEeptLVSYIVP 443
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1776025254 1591 KHANASLTA----------------------RELRH----FVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSL 1638
Cdd:cd17647    444 RFDKPDDESfaqedvpkevstdpivkgligyRKLIKdireFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKL 517
FAA1 COG1022
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
1154-1580 5.43e-52

Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];


Pssm-ID: 440645 [Multi-domain]  Cd Length: 603  Bit Score: 196.09  E-value: 5.43e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1154 TFHELFEQQAKKTPDRAAVSY----EGQTLTYRELDERSTQLAIYLQAHGVGP-DRLAgIYVDRSLDMLVGLLAILKAGG 1228
Cdd:COG1022     12 TLPDLLRRRAARFPDRVALREkedgIWQSLTWAEFAERVRALAAGLLALGVKPgDRVA-ILSDNRPEWVIADLAILAAGA 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1229 AYVPLDPSYPAERLEYMLEDSEV-FITLTTSELVNTLSwngvttALLDQ----------------------DWDEI---- 1281
Cdd:COG1022     91 VTVPIYPTSSAEEVAYILNDSGAkVLFVEDQEQLDKLL------EVRDElpslrhivvldprglrddprllSLDELlalg 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1282 AQTASDRKVLTR--TVTPENLAYVIYTSGSTGKPKGVMIPHKALTNFLVSMGETPGLTAEDKMLavttycfdiaaleLFL 1359
Cdd:COG1022    165 REVADPAELEARraAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTL-------------SFL 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1360 PLikgAH------CYIC-----QTEHTKDVEKLKRDIRTIKPTVMQATPATW------------------KMLFYS---- 1406
Cdd:COG1022    232 PL---AHvfertvSYYAlaagaTVAFAESPDTLAEDLREVKPTFMLAVPRVWekvyagiqakaeeagglkRKLFRWalav 308
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1407 GWENEE---------------------------------NVKIL-CGGEALPETLKRYFLDTG---SEAWnmfGPTETTI 1449
Cdd:COG1022    309 GRRYARarlagkspslllrlkhaladklvfsklrealggRLRFAvSGGAALGPELARFFRALGipvLEGY---GLTETSP 385
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1450 WSAVQRiNDECSRATIGRPIANTQIYITDSqlapvpagvpGELCIAGDGVAKGYYKKEELTDSRFIDNPFepgsklYRTG 1529
Cdd:COG1022    386 VITVNR-PGDNRIGTVGPPLPGVEVKIAED----------GEILVRGPNVMKGYYKNPEATAEAFDADGW------LHTG 448
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1776025254 1530 DMARWLPGGRIEYIGRIDNQVKIR-GFRIELGDIESRLSEHPGILECVVVAD 1580
Cdd:COG1022    449 DIGELDEDGFLRITGRKKDLIVTSgGKNVAPQPIENALKASPLIEQAVVVGD 500
BCL_like cd05919
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ...
1169-1639 6.73e-51

Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.


Pssm-ID: 341243 [Multi-domain]  Cd Length: 436  Bit Score: 188.44  E-value: 6.73e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1169 RAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLED 1248
Cdd:cd05919      1 KTAFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1249 SEvfitlttselvntlswngvtTALLDQDWDEIAqtasdrkvltrtvtpenlaYVIYTSGSTGKPKGVMIPHKALTNFLV 1328
Cdd:cd05919     81 CE--------------------ARLVVTSADDIA-------------------YLLYSSGTTGPPKGVMHAHRDPLLFAD 121
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1329 SMG-ETPGLTAEDKMLAVTTYCFDIA-ALELFLPLIKGAHCYICQTehTKDVEKLKRDIRTIKPTVMQATPATWKMLFYS 1406
Cdd:cd05919    122 AMArEALGLTPGDRVFSSAKMFFGYGlGNSLWFPLAVGASAVLNPG--WPTAERVLATLARFRPTVLYGVPTFYANLLDS 199
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1407 G-WENEENVKILC---GGEALPETLKRYFLDT-GSEAWNMFGPTETTIWSAVQRInDECSRATIGRPIANTQIYITDSQL 1481
Cdd:cd05919    200 CaGSPDALRSLRLcvsAGEALPRGLGERWMEHfGGPILDGIGATEVGHIFLSNRP-GAWRLGSTGRPVPGYEIRLVDEEG 278
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1482 APVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNpfepgskLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGD 1561
Cdd:cd05919    279 HTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFNGG-------WYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVE 351
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1562 IESRLSEHPGILECVVVA-----DMDNLAAYYTAK--HANASLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKID 1634
Cdd:cd05919    352 VESLIIQHPAVAEAAVVAvpestGLSRLTAFVVLKspAAPQESLARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQ 431

                   ....*
gi 1776025254 1635 RNSLK 1639
Cdd:cd05919    432 RFKLR 436
Ketoacyl-synt_C pfam02801
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ...
3596-3723 8.28e-51

Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.


Pssm-ID: 426989  Cd Length: 118  Bit Score: 176.60  E-value: 8.28e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3596 YGVIRGTAENHGGRANTLTSPNPKAQADLLVRAYRQAGIDPSTVTYIEAHGTGTELGDPIEINGLKAAFkelsnmrgesQ 3675
Cdd:pfam02801    1 YAVIKGSAVNHDGRHNGLTAPNGEGQARAIRRALADAGVDPEDVDYVEAHGTGTPLGDPIEAEALKRVF----------G 70
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1776025254 3676 PDVPDHRCGIGSVKSNIGHLELAAGISGLIKVLLQMKHKTLVKSLHCE 3723
Cdd:pfam02801   71 SGARKQPLAIGSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLNLE 118
PRK06187 PRK06187
long-chain-fatty-acid--CoA ligase; Validated
27-562 9.25e-51

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235730 [Multi-domain]  Cd Length: 521  Bit Score: 190.40  E-value: 9.25e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254   27 QPATIPEVLYRTAAELGDTKgIIYlqPDGTEVyqSYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNSQLLPAFWGCVL 106
Cdd:PRK06187     4 YPLTIGRILRHGARKHPDKE-AVY--FDGRRT--TYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPK 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  107 TGVVPAPLAVpptyaesssgtqKLKD---AWTLLDKPA--VITDRGmHQEMLDWAKEQgLEGFRAIIV------------ 169
Cdd:PRK06187    79 IGAVLHPINI------------RLKPeeiAYILNDAEDrvVLVDSE-FVPLLAAILPQ-LPTVRTVIVegdgpaaplape 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  170 ----EDLLSAEADT-DWHQSSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDHVGGIG 244
Cdd:PRK06187   145 vgeyEELLAAASDTfDFPDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPMFHVHAWG 224
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  245 MLHLRdVYLGCQEINVSSetilMEPLKWLDWIDHYRasVTwapnFAFG---LVTDFAEEIKDRKWDLSSMRYMLNGG--- 318
Cdd:PRK06187   225 LPYLA-LMAGAKQVIPRR----FDPENLLDLIETER--VT----FFFAvptIWQMLLKAPRAYFVDFSSLRLVIYGGaal 293
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  319 -----EAMVAKVGRRILEllephglpadairpAWGMSETSSGVIFSH-------EFTRAGTSdddhfveiGSPIPGFSMR 386
Cdd:PRK06187   294 ppallREFKEKFGIDLVQ--------------GYGMTETSPVVSVLPpedqlpgQWTKRRSA--------GRPLPGVEAR 351
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  387 IVNDH-NEL-VEEGEIGRFQVSGLSVTSGYYQRPDLNESVFtEDGWFETGDLGFL-RNGRLTITGRTKDAIIINGINYYS 463
Cdd:PRK06187   352 IVDDDgDELpPDGGEVGEIIVRGPWLMQGYWNRPEATAETI-DGGWLHTGDVGYIdEDGYLYITDRIKDVIISGGENIYP 430
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  464 HAIESAVEELSEIetsytAACAVrLGQnsTDQ------LAifFVTSAKlnDEQMSQllRNIQSHVSQVIgvtPEYLLPVQ 537
Cdd:PRK06187   431 RELEDALYGHPAV-----AEVAV-IGV--PDEkwgerpVA--VVVLKP--GATLDA--KELRAFLRGRL---AKFKLPKR 493
                          570       580
                   ....*....|....*....|....*...
gi 1776025254  538 ---KEEIPKTAIGKIQRTQLKTSFENGE 562
Cdd:PRK06187   494 iafVDELPRTSVGKILKRVLREQYAEGK 521
MCS cd05941
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ...
1168-1640 1.94e-50

Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.


Pssm-ID: 341264 [Multi-domain]  Cd Length: 442  Bit Score: 187.50  E-value: 1.94e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1168 DRAAVSYEGQTLTYRELDERSTQLAIYLQAHG-VGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYML 1246
Cdd:cd05941      1 DRIAIVDDGDSITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1247 EDSEVfitlttselvntlswngvtTALLDqdwdeiaqtasdrkvltrtvtpenLAYVIYTSGSTGKPKGVMIPHKALTNF 1326
Cdd:cd05941     81 TDSEP-------------------SLVLD------------------------PALILYTSGTTGRPKGVVLTHANLAAN 117
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1327 LVSMGETPGLTAEDKMLAVttycfdiaaLELF----------LPLIKGAHCyICQTEHTKDVEKLKRDIRTIK-----PT 1391
Cdd:cd05941    118 VRALVDAWRWTEDDVLLHV---------LPLHhvhglvnallCPLFAGASV-EFLPKFDPKEVAISRLMPSITvfmgvPT 187
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1392 V----MQATPATWKMLFYSGWENEENVKIL-CGGEALPE-TLKRYFLDTGSEAWNMFGPTETTIwSAVQRINDECSRATI 1465
Cdd:cd05941    188 IytrlLQYYEAHFTDPQFARAAAAERLRLMvSGSAALPVpTLEEWEAITGHTLLERYGMTEIGM-ALSNPLDGERRPGTV 266
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1466 GRPIANTQIYITDSQLA-PVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPFepgsklYRTGDMARWLPGGRIEYIG 1544
Cdd:cd05941    267 GMPLPGVQARIVDEETGePLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGW------FKTGDLGVVDEDGYYWILG 340
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1545 RI-DNQVKIRGFRIELGDIESRLSEHPGILECVVV--ADMD---NLAAYYTAKHANASLTARELRHFVKNALPAYMVPSY 1618
Cdd:cd05941    341 RSsVDIIKSGGYKVSALEIERVLLAHPGVSECAVIgvPDPDwgeRVVAVVVLRAGAAALSLEELKEWAKQRLAPYKRPRR 420
                          490       500
                   ....*....|....*....|..
gi 1776025254 1619 FIQLDHMPLTPNGKIDRNSLKN 1640
Cdd:cd05941    421 LILVDELPRNAMGKVNKKELRK 442
C_NRPS-like cd19066
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
695-1121 2.68e-50

Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long, with various activities such as antibiotic, antifungal, antitumor and immunosuppression. There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380453 [Multi-domain]  Cd Length: 427  Bit Score: 186.46  E-value: 2.68e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  695 PLSEVQKGLWTLQKMSPEKSAYHVPLCFKFSSGLHLETLQQAFGLVLNQHPILKHVIQEKDGVP---ILKNEPALSIEIK 771
Cdd:cd19066      3 PLSPMQRGMWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEEAGRYeqvVLDKTVRFRIEII 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  772 TENISSMKESDIPAFLRKKVKEPYVKENSPLVRVMSFSRSEQEHFLLVVIHHLIFDGVSSVTFIHSLFDTYQLLLKgQQP 851
Cdd:cd19066     83 DLRNLADPEARLLELIDQIQQTIYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDAAER-QKP 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  852 EIAVSPAIYHDFAAWEKNMLAGKDGVKHRTYWQKQLSGTLPNLQLPKVSASSvsefREDTYTRR-----LSSGFMNQVRM 926
Cdd:cd19066    162 TLPPPVGSYADYAAWLEKQLESEAAQADLAYWTSYLHGLPPPLPLPKAKRPS----QVASYEVLtleffLRSEETKRLRE 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  927 FAKEHSVNVTTVFLSCYMMLLGRYTGQKEQIVGMPAMVRPEERFDDAIGHFLNMLPIRSELNPADTFSSFISKLQLTILD 1006
Cdd:cd19066    238 VARESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDEAVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKEQSRE 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1007 GLDHAAYPFPKMVRDLNIPRSQAGSPVFQTAF-FYQNFLQSGSYQSllsryadfFSVDYVEYIHQEG-EYELVFELWETE 1084
Cdd:cd19066    318 AIEHQRVPFIELVRHLGVVPEAPKHPLFEPVFtFKNNQQQLGKTGG--------FIFTTPVYTSSEGtVFDLDLEASEDP 389
                          410       420       430
                   ....*....|....*....|....*....|....*...
gi 1776025254 1085 EK-MELNIKYNTGLFDAASISAMFDHFVYVTEQAMLNP 1121
Cdd:cd19066    390 DGdLLLRLEYSRGVYDERTIDRFAERYMTALRQLIENP 427
FACL_DitJ_like cd05934
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
1176-1639 4.60e-50

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.


Pssm-ID: 341257 [Multi-domain]  Cd Length: 422  Bit Score: 185.57  E-value: 4.60e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1176 GQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLEDSEVFITL 1255
Cdd:cd05934      1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1256 TTselvntlswngvttalldqdwdeiaqtasdrkvltrtvtpenLAYVIYTSGSTGKPKGVMIPHKALTNFLVSMGETPG 1335
Cdd:cd05934     81 VD------------------------------------------PASILYTSGTTGPPKGVVITHANLTFAGYYSARRFG 118
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1336 LTAEDKMLAVTTYcFDIAALEL-FLP-LIKGAHCYICQTEHTKdveKLKRDIRTIKPTVMQATPATWKMLfYSGWENEEN 1413
Cdd:cd05934    119 LGEDDVYLTVLPL-FHINAQAVsVLAaLSVGATLVLLPRFSAS---RFWSDVRRYGATVTNYLGAMLSYL-LAQPPSPDD 193
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1414 ----VKILCGGEALPETLKRYFLDTGSEAWNMFGPTETTIwsAVQRINDECSRA-TIGRPIANTQIYITDSQLAPVPAGV 1488
Cdd:cd05934    194 rahrLRAAYGAPNPPELHEEFEERFGVRLLEGYGMTETIV--GVIGPRDEPRRPgSIGRPAPGYEVRIVDDDGQELPAGE 271
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1489 PGELCI---AGDGVAKGYYKKEELTDSRFIDNpfepgskLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESR 1565
Cdd:cd05934    272 PGELVIrglRGWGFFKGYYNMPEATAEAMRNG-------WFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERA 344
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1776025254 1566 LSEHPGILECVVVADMDNL-----AAYYTAKHAnASLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLK 1639
Cdd:cd05934    345 ILRHPAVREAAVVAVPDEVgedevKAVVVLRPG-ETLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
Firefly_Luc_like cd05911
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ...
1175-1633 5.24e-50

Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341237 [Multi-domain]  Cd Length: 486  Bit Score: 187.42  E-value: 5.24e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1175 EGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLEDSEVFIT 1254
Cdd:cd05911      7 TGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVI 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1255 LTTSEL----------------VNTLSWNGVTTALLDQDWDEIAQTASDRKVLTRTVTPENLAYVIYTSGSTGKPKGVMI 1318
Cdd:cd05911     87 FTDPDGlekvkeaakelgpkdkIIVLDDKPDGVLSIEDLLSPTLGEEDEDLPPPLKDGKDDTAAILYSSGTTGLPKGVCL 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1319 PHKALTN--FLVSMGETPGLTAEDKMLAVTT----YCFDIAaleLFLPLiKGAHCYICqtehTK-DVEKLKRDIRTIKPT 1391
Cdd:cd05911    167 SHRNLIAnlSQVQTFLYGNDGSNDVILGFLPlyhiYGLFTT---LASLL-NGATVIIM----PKfDSELFLDLIEKYKIT 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1392 VMQATPATWKMLFYSGWENEENVK----ILCGG----EALPETLKRYFLDTG-SEAWNMfgpTETTIWSAVQRINDEcSR 1462
Cdd:cd05911    239 FLYLVPPIAAALAKSPLLDKYDLSslrvILSGGaplsKELQELLAKRFPNATiKQGYGM---TETGGILTVNPDGDD-KP 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1463 ATIGRPIANTQIYI----TDSQLAPvpaGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPFepgsklYRTGDMARWLPGG 1538
Cdd:cd05911    315 GSVGRLLPNVEAKIvdddGKDSLGP---NEPGEICVRGPQVMKGYYNNPEATKETFDEDGW------LHTGDIGYFDEDG 385
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1539 RIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVV----ADMDNLAAYYTAKHANASLTARELRHFVKNALPAYM 1614
Cdd:cd05911    386 YLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIgipdEVSGELPRAYVVRKPGEKLTEKEVKDYVAKKVASYK 465
                          490       500
                   ....*....|....*....|....
gi 1776025254 1615 -----VpsYFIqlDHMPLTPNGKI 1633
Cdd:cd05911    466 qlrggV--VFV--DEIPKSASGKI 485
SgcC5_NRPS-like cd19539
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ...
695-1121 8.55e-50

SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- bond forming activity and similar C-domains of modular NRPSs; SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. This subfamily also includes similar C-domains of modular NRPSs such as Penicillium chrysogenum N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase PCBAB. Condensation (C) domains of NRPSs normally catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380462 [Multi-domain]  Cd Length: 427  Bit Score: 184.89  E-value: 8.55e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  695 PLSEVQKGLWTLQKMSPEKSAYHVPLCFKFSSGLHLETLQQAFGLVLNQHPILKHVIQEKDG-----VPILKNEPAL-SI 768
Cdd:cd19539      3 PLSFAQERLWFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDGgvprqEILPPGPAPLeVR 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  769 EIKTENisSMKESDIPAFLRKKVKEPYVKENSPLVRVMSFSRSEQEHFLLVVIHHLIFDGVSSVTFIHSLFDTYQLLLKG 848
Cdd:cd19539     83 DLSDPD--SDRERRLEELLRERESRGFDLDEEPPIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAARRKG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  849 QQPEIAVSPAIYHDFAAWEKNMLAGKDGVKHRTYWQKQLSGTLPnLQLP-KVSASSVSEFREDTYTRRLSSGFMNQVRMF 927
Cdd:cd19539    161 PAAPLPELRQQYKEYAAWQREALAAPRAAELLDFWRRRLRGAEP-TALPtDRPRPAGFPYPGADLRFELDAELVAALREL 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  928 AKEHSVNVTTVFLSCYMMLLGRYTGQKEQIVGMPAMVRPEERFDDAIGHFLNMLPIRSELNPADTFSSFISKLQLTILDG 1007
Cdd:cd19539    240 AKRARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNHPRFESTVGFFVNLLPLRVDVSDCATFRDLIARVRKALVDA 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1008 LDHAAYPFPKMVRDLNIPRSQAGSPVFQTAFFYQNFLQSGsyqsllSRYADFFSVDYVEYIHQEGEYELVFELWETEEKM 1087
Cdd:cd19539    320 QRHQELPFQQLVAELPVDRDAGRHPLVQIVFQVTNAPAGE------LELAGGLSYTEGSDIPDGAKFDLNLTVTEEGTGL 393
                          410       420       430
                   ....*....|....*....|....*....|....
gi 1776025254 1088 ELNIKYNTGLFDAASISAMFDHFVYVTEQAMLNP 1121
Cdd:cd19539    394 RGSLGYATSLFDEETIQGFLADYLQVLRQLLANP 427
C_PKS-NRPS cd19532
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
695-1040 6.40e-49

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHxxxD motif, a few such as Monascus pilosus lovastatin nonaketide synthase MokA have a non-canonical HRxxxD motif in the C-domain and are unable to catalyze amide-bond formation. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380455 [Multi-domain]  Cd Length: 421  Bit Score: 182.27  E-value: 6.40e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  695 PLSEVQKGLWTLQKMSPEKSAYHVPLCFKFSSGLHLETLQQAFGLVLNQHPILK--HVIQEKDGVP---ILKnEPALSIE 769
Cdd:cd19532      3 PMSFGQSRFWFLQQYLEDPTTFNVTFSYRLTGPLDVARLERAVRAVGQRHEALRtcFFTDPEDGEPmqgVLA-SSPLRLE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  770 IKTenISSmkESDIPAFLRKKVKEPYVKENSPLVRVMSFSRSEQEHFLLVVIHHLIFDGVSSVTFIHSLFDTYQlllkGQ 849
Cdd:cd19532     82 HVQ--ISD--EAEVEEEFERLKNHVYDLESGETMRIVLLSLSPTEHYLIFGYHHIAMDGVSFQIFLRDLERAYN----GQ 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  850 QPeiavSPAI--YHDFAAWEKNMLAGKDGVKHRTYWQKQLSG---TLPNLQLPKVSA-SSVSEFREDTYTRRLSSGFMNQ 923
Cdd:cd19532    154 PL----LPPPlqYLDFAARQRQDYESGALDEDLAYWKSEFSTlpePLPLLPFAKVKSrPPLTRYDTHTAERRLDAALAAR 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  924 VRMFAKEHSVNVTTVFLSCYMMLLGRYTGQKEQIVGMPAMVRPEERFDDAIGHFLNMLPIRSELNPADTFSSFISKLQLT 1003
Cdd:cd19532    230 IKEASRKLRVTPFHFYLAALQVLLARLLDVDDICIGIADANRTDEDFMETIGFFLNLLPLRFRRDPSQTFADVLKETRDK 309
                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 1776025254 1004 ILDGLDHAAYPFPKMVRDLNIPRSQAGSPVFQTAFFY 1040
Cdd:cd19532    310 AYAALAHSRVPFDVLLDELGVPRSATHSPLFQVFINY 346
FACL_FadD13-like cd17631
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ...
187-486 6.78e-49

fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.


Pssm-ID: 341286 [Multi-domain]  Cd Length: 435  Bit Score: 182.81  E-value: 6.78e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  187 EDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDHVGGIGMLHLRDVYLGcqeinvsSETIL 266
Cdd:cd17631     98 DDLALLMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRG-------GTVVI 170
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  267 M---EPLKWLDWIDHYRASVTWA-PNFAFGLVT--DFAEeikdrkWDLSSMRYMLNGGEAMVAkvgrRILELLEPHGLpa 340
Cdd:cd17631    171 LrkfDPETVLDLIERHRVTSFFLvPTMIQALLQhpRFAT------TDLSSLRAVIYGGAPMPE----RLLRALQARGV-- 238
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  341 dAIRPAWGMSETSSGVIF-SHEFTRAgtsdddHFVEIGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGYYQRPD 419
Cdd:cd17631    239 -KFVQGYGMTETSPGVTFlSPEDHRR------KLGSAGRPVFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPE 311
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1776025254  420 LNESVFtEDGWFETGDLGFL-RNGRLTITGRTKDAIIINGINYYSHAIESAVEELSEIetsytAACAV 486
Cdd:cd17631    312 ATAAAF-RDGWFHTGDLGRLdEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAV-----AEVAV 373
PRK05851 PRK05851
long-chain-fatty acid--ACP ligase MbtM;
166-561 2.06e-48

long-chain-fatty acid--ACP ligase MbtM;


Pssm-ID: 180289 [Multi-domain]  Cd Length: 525  Bit Score: 183.81  E-value: 2.06e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  166 AIIVEDLLSAEA---DTDWHQSSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTR-EDITFNWMPFDHVG 241
Cdd:PRK05851   128 SVTVHDLATAAHtnrSASLTPPDSGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVGLDAaTDVGCSWLPLYHDM 207
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  242 GIGMLhLRDVYLGCQEINVSSETILMEPLKWLDWIDHYRASVTWAPNFAFGLVTDFAEEIKDrkWDLSSMRYMLNGGEAM 321
Cdd:PRK05851   208 GLAFL-LTAALAGAPLWLAPTTAFSASPFRWLSWLSDSRATLTAAPNFAYNLIGKYARRVSD--VDLGALRVALNGGEPV 284
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  322 VAKVGRRILELLEPHGLPADAIRPAWGMSETS---------SGVIFSHEFTRAGTSDDDHFVeIGSPIPGFSMRIV-NDH 391
Cdd:PRK05851   285 DCDGFERFATAMAPFGFDAGAAAPSYGLAESTcavtvpvpgIGLRVDEVTTDDGSGARRHAV-LGNPIPGMEVRISpGDG 363
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  392 NELVEEGEIGRFQVSGLSVTSGYyqrpdLNESVFTEDGWFETGDLGFLRNGRLTITGRTKDAIIINGINYYSHAIESAVE 471
Cdd:PRK05851   364 AAGVAGREIGEIEIRGASMMSGY-----LGQAPIDPDDWFPTGDLGYLVDGGLVVCGRAKELITVAGRNIFPTEIERVAA 438
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  472 ELSEIETSytAACAVRLGQNSTDQ---LAIFFVTSaklnDEQMSQllRNIQSHVSQVIGVTPEYLLPVQKEEIPKTAIGK 548
Cdd:PRK05851   439 QVRGVREG--AVVAVGTGEGSARPglvIAAEFRGP----DEAGAR--SEVVQRVASECGVVPSDVVFVAPGSLPRTSSGK 510
                          410
                   ....*....|...
gi 1776025254  549 IQRTQLKTSFENG 561
Cdd:PRK05851   511 LRRLAVKRSLEAA 523
KR_2_FAS_SDR_x cd08955
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 2, complex (x); ...
4056-4418 4.61e-48

beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 2, complex (x); Ketoreductase, a module of the multidomain polyketide synthase, has 2 subdomains, each corresponding to a short-chain dehydrogenases/reductase (SDR) family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerizes but is composed of 2 subdomains, each resembling an SDR monomer. In some instances, as in porcine FAS, an enoyl reductase (a Rossman fold NAD binding domain of the MDR family) module is inserted between the sub-domains. The active site resembles that of typical SDRs, except that the usual positions of the catalytic asparagine and tyrosine are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular polyketide synthases are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) fatty acid synthase. In some instances, such as porcine FAS , an enoyl reductase module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consists of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthesis uses dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-ketoacyl reductase (KR), forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-enoyl reductase (ER). Polyketide syntheses also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes the KR domain of the Lyngbya majuscule Jam J, -K, and #L which are encoded on the jam gene cluster and are involved in the synthesis of the Jamaicamides (neurotoxins); Lyngbya majuscule Jam P belongs to a different KR_FAS_SDR_x subfamily. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187658 [Multi-domain]  Cd Length: 376  Bit Score: 178.25  E-value: 4.61e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4056 VQRLVEFGHKEGLRLLCVTKGLESF--QNTSVRMAGASRAGLYRMLQCEYSHLISRHMDAEEVTDHPRLAKLIADEFYSE 4133
Cdd:cd08955     41 VQALSKAGLRRAPRLWLVTRGAQSVlaDGEPVSPAQAPLWGLGRVIALEHPELRCGLVDLDPEATAAEEAEALLAELLAA 120
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4134 SYDAEVCYRDGLRYQSFLKAHPetgkATEQSAvfpkDHVLLITGGTRGIGLLCARHFAEcYGVKKLVLTGREQLPpreew 4213
Cdd:cd08955    121 DAEDQVALRGGARYVARLVRAP----ARPLRP----DATYLITGGLGGLGLLVAEWLVE-RGARHLVLTGRRAPS----- 186
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4214 arfktsntslAEKIQAVRELEAKGVQVEMLSLTLSDDAQVEQTLQHIKRTLGPIGGVIHCAGLTDMDTLAfiRKTSDDIQ 4293
Cdd:cd08955    187 ----------AAARQAIAALEEAGAEVVVLAADVSDRDALAAALAQIRASLPPLRGVIHAAGVLDDGVLA--NQDWERFR 254
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4294 RVMEPKVSGLTTLYRHVCNEPLQFFVLFSSVSAIIPelSAGQADYAMANSYMDYFAEAHQ-KHVPIISVQWPNWKETGM- 4371
Cdd:cd08955    255 KVLAPKVQGAWNLHQLTQDLPLDFFVLFSSVASLLG--SPGQANYAAANAFLDALAHYRRaRGLPALSINWGPWAEVGMa 332
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*...
gi 1776025254 4372 GEVTNQAY-RESGLFSITNSEGLRFLDQIVSKmfGPVVLPAManQTNW 4418
Cdd:cd08955    333 ASLARQARlEARGVGAISPAAGLQALGQLLRT--GSTQVGVA--PVDW 376
Ketoacyl-synt_C pfam02801
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ...
2017-2136 4.70e-48

Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.


Pssm-ID: 426989  Cd Length: 118  Bit Score: 168.52  E-value: 4.70e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2017 YALLRGIGVNNDGADkVGFYAPSVKGQADVVQQVMNQTKIHPESICYVEAHGTGTKLGDPIELAALTNVYRQYTNKtQFC 2096
Cdd:pfam02801    1 YAVIKGSAVNHDGRH-NGLTAPNGEGQARAIRRALADAGVDPEDVDYVEAHGTGTPLGDPIEAEALKRVFGSGARK-QPL 78
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1776025254 2097 GIGSVKTNIGHLDTAAGLAGCIKVVMSLYHQELAPSINYK 2136
Cdd:pfam02801   79 AIGSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLNLE 118
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
4174-4368 8.60e-48

KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.


Pssm-ID: 430138 [Multi-domain]  Cd Length: 180  Bit Score: 170.44  E-value: 8.60e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4174 LITGGTRGIGLLCARHFAEcYGVKKLVLTGReqlppreewarfktSNTSLAEKIQAVRELEAKGVQVEMLSLTLSDDAQV 4253
Cdd:pfam08659    4 LITGGLGGLGRELARWLAE-RGARHLVLLSR--------------SAAPRPDAQALIAELEARGVEVVVVACDVSDPDAV 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4254 EQTLQHIKRTLGPIGGVIHCAGLTDmDTLaFIRKTSDDIQRVMEPKVSGLTTLYRHVCNEPLQFFVLFSSVSAIIPelSA 4333
Cdd:pfam08659   69 AALLAEIKAEGPPIRGVIHAAGVLR-DAL-LENMTDEDWRRVLAPKVTGTWNLHEATPDEPLDFFVLFSSIAGLLG--SP 144
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1776025254 4334 GQADYAMANSYMDYFAEA-HQKHVPIISVQWPNWKE 4368
Cdd:pfam08659  145 GQANYAAANAFLDALAEYrRSQGLPATSINWGPWAE 180
decarbox_cond_enzymes cd00825
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ...
1847-2182 1.10e-47

decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new carbon-carbon bond by a decarboxylating Claisen-like condensation reaction. Members are involved in the synthesis of fatty acids and polyketides, a diverse group of natural products. Both pathways are an iterative series of additions of small carbon units, usually acetate, to a nascent acyl group. There are 2 classes of decarboxylating condensing enzymes, which can be distinguished by sequence similarity, type of active site residues and type of primer units (acetyl CoA or acyl carrier protein (ACP) linked units).


Pssm-ID: 238421 [Multi-domain]  Cd Length: 332  Bit Score: 175.90  E-value: 1.10e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1847 RMLLTHSWKAIEDAGYAAGQI--PQTSVFMSASNNSYRALLPSDTTESLETPDGYVSWVLAQSGTiptMISHKLGLRGPS 1924
Cdd:cd00825     13 ILGFEAAERAIADAGLSREYQknPIVGVVVGTGGGSPRFQVFGADAMRAVGPYVVTKAMFPGASG---QIATPLGIHGPA 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1925 YFVHANCSSSLIGLHSAYKSLLSAESDYALVGGATLHTESNIGYVHQPGLNFSSDGHIKAFDASADGMIGGEGVAVVLLK 2004
Cdd:cd00825     90 YDVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAPMDCEFDAMGALSTPEKASRTFDAAADGFVFGDGAGALVVE 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2005 KAADAVKDGDHIYALLRGIGVNNDGADKVGFyAPSVKGQADVVQQVMNQTKIHPESICYVEAHGTGTKLGDPIELAALTN 2084
Cdd:cd00825    170 ELEHALARGAHIYAEIVGTAATIDGAGMGAF-APSAEGLARAAKEALAVAGLTVWDIDYLVAHGTGTPIGDVKELKLLRS 248
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2085 VYrqytnKTQFCGIGSVKTNIGHLDTAAGLAGCIKVVMSLYHQELAPSINYKEPNPNTDLASSpfyvvdqkKTLSREIQT 2164
Cdd:cd00825    249 EF-----GDKSPAVSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPPSIHIEELDEAGLNIVT--------ETTPRELRT 315
                          330
                   ....*....|....*...
gi 1776025254 2165 hrAALSSFGLGGTNTHAI 2182
Cdd:cd00825    316 --ALLNGFGLGGTNATLV 331
FabB COG0304
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...
4590-4992 3.56e-47

3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism]; 3-oxoacyl-(acyl-carrier-protein) synthase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440073 [Multi-domain]  Cd Length: 409  Bit Score: 176.82  E-value: 3.56e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4590 IAVVGLSCRFPGAETLESYWSLLSEGRSSIGPIP---AERWGCKtpyYAGVIDGvsyFDPDFFLlHEEDVRAMDPQ---A 4663
Cdd:COG0304      3 VVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITrfdASGLPVR---IAGEVKD---FDPEEYL-DRKELRRMDRFtqyA 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4664 LLVLEECLKllyHAGYTPEEIKGKPVGVYIG-GRSQHKPDEDSLD--HAKNP-------IVTVGQNYLAANLSQFFDVRG 4733
Cdd:COG0304     76 LAAAREALA---DAGLDLDEVDPDRTGVIIGsGIGGLDTLEEAYRalLEKGPrrvspffVPMMMPNMAAGHVSIRFGLKG 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4734 PSVVVDTACSSALVGMNMAIQALRGGDIQSAIVGGVSLLSSDASHRLFDRRGILS------KHSSfHVFDERADGVVLGE 4807
Cdd:COG0304    153 PNYTVSTACASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLAGFDALGALStrnddpEKAS-RPFDKDRDGFVLGE 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4808 GVGMVMLKTVKQALEDGDTIYAVVKAASVNNDG-RTAGPAtPNLEAQKEVMKDALFKSGKKPEDISYLEANGSGSIVTDL 4886
Cdd:COG0304    232 GAGVLVLEELEHAKARGAKIYAEVVGYGASSDAyHITAPA-PDGEGAARAMRAALKDAGLSPEDIDYINAHGTSTPLGDA 310
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4887 LELKAIQSVYrSGHSSPLSLGSIKPNIGHPLCA----EGIASfikvVLMLKERRFVPflsgekeMAHFDQQ----KANIT 4958
Cdd:COG0304    311 AETKAIKRVF-GDHAYKVPVSSTKSMTGHLLGAagaiEAIAS----VLALRDGVIPP-------TINLENPdpecDLDYV 378
                          410       420       430
                   ....*....|....*....|....*....|....
gi 1776025254 4959 FSRALEKwtdSQPTAAINCFADGGTNVHVIVEAW 4992
Cdd:COG0304    379 PNEAREA---KIDYALSNSFGFGGHNASLVFKRY 409
VL_LC_FACS_like cd05907
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ...
1177-1580 1.16e-45

Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341233 [Multi-domain]  Cd Length: 452  Bit Score: 173.55  E-value: 1.16e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1177 QTLTYRELDERSTQLAIYLQAHGVGP-DRLAgIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLEDSEVfitl 1255
Cdd:cd05907      4 QPITWAEFAEEVRALAKGLIALGVEPgDRVA-ILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEA---- 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1256 ttselvntlswngvtTALLdqdwdeiaqtasdrkvltrTVTPENLAYVIYTSGSTGKPKGVMIPHKALTNFLVSMGETPG 1335
Cdd:cd05907     79 ---------------KALF-------------------VEDPDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLP 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1336 LTAEDKMLavttycfdiaaleLFLPLikgAHC-------YIC-----QTEHTKDVEKLKRDIRTIKPTVMQATPATWKML 1403
Cdd:cd05907    125 ATEGDRHL-------------SFLPL---AHVferraglYVPllagaRIYFASSAETLLDDLSEVRPTVFLAVPRVWEKV 188
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1404 fYSG---------------WENEENVK-ILCGGEALPETLKRYFLDTGSEAWNMFGPTETTIWSAVQRINDEcSRATIGR 1467
Cdd:cd05907    189 -YAAikvkavpglkrklfdLAVGGRLRfAASGGAPLPAELLHFFRALGIPVYEGYGLTETSAVVTLNPPGDN-RIGTVGK 266
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1468 PIANTQIYITDSqlapvpagvpGELCIAGDGVAKGYYKKEELTDSRFIDNPFepgsklYRTGDMARWLPGGRIEYIGRID 1547
Cdd:cd05907    267 PLPGVEVRIADD----------GEILVRGPNVMLGYYKNPEATAEALDADGW------LHTGDLGEIDEDGFLHITGRKK 330
                          410       420       430
                   ....*....|....*....|....*....|....
gi 1776025254 1548 N-QVKIRGFRIELGDIESRLSEHPGILECVVVAD 1580
Cdd:cd05907    331 DlIITSGGKNISPEPIENALKASPLISQAVVIGD 364
MACS_like_4 cd05969
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ...
1179-1643 1.16e-45

Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.


Pssm-ID: 341273 [Multi-domain]  Cd Length: 442  Bit Score: 173.46  E-value: 1.16e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1179 LTYRELDERSTQLAIYLQAHGVGP-DRLAgIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLEDSEVFITLTT 1257
Cdd:cd05969      1 YTFAQLKVLSARFANVLKSLGVGKgDRVF-VLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITT 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1258 SELVntlswngvttalldqdwdeiaqtasdrkvltRTVTPENLAYVIYTSGSTGKPKGVMIPHKALTNFLVSMGETPGLT 1337
Cdd:cd05969     80 EELY-------------------------------ERTDPEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLH 128
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1338 AEDKM--------LAVTTYcfdiaalELFLPLIKGAHCYICQTEHtkDVEKLKRDIRTIKPTVMQATPATWKMLFYSGWE 1409
Cdd:cd05969    129 PDDIYwctadpgwVTGTVY-------GIWAPWLNGVTNVVYEGRF--DAESWYGIIERVKVTVWYTAPTAIRMLMKEGDE 199
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1410 -----NEENVKILC-GGEAL-PETLKryfldTGSEAWNM-----FGPTETtiwSAVQRINDECSRA---TIGRPIANTQI 1474
Cdd:cd05969    200 larkyDLSSLRFIHsVGEPLnPEAIR-----WGMEVFGVpihdtWWQTET---GSIMIANYPCMPIkpgSMGKPLPGVKA 271
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1475 YITDSQLAPVPAGVPGELCIAGD--GVAKGYYKKEELTDSRFIDNpfepgskLYRTGDMARWLPGGRIEYIGRIDNQVKI 1552
Cdd:cd05969    272 AVVDENGNELPPGTKGILALKPGwpSMFRGIWNDEERYKNSFIDG-------WYLTGDLAYRDEDGYFWFVGRADDIIKT 344
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1553 RGFRIELGDIESRLSEHPGILECVVVADMDNL-----AAYYTAK--HANASLTARELRHFVKNALPAYMVPSYFIQLDHM 1625
Cdd:cd05969    345 SGHRVGPFEVESALMEHPAVAEAGVIGKPDPLrgeiiKAFISLKegFEPSDELKEEIINFVRQKLGAHVAPREIEFVDNL 424
                          490
                   ....*....|....*...
gi 1776025254 1626 PLTPNGKIDRNSLKNIDL 1643
Cdd:cd05969    425 PKTRSGKIMRRVLKAKEL 442
FAA1 COG1022
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
27-477 1.23e-45

Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];


Pssm-ID: 440645 [Multi-domain]  Cd Length: 603  Bit Score: 177.21  E-value: 1.23e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254   27 QPATIPEVLYRTAAELGDTKGIIYLQpDGTEVYQSYRRLWDDGLRIVKGLRQSGLKAKQSVILqLGDNS-QLLPAFWGCV 105
Cdd:COG1022      9 PADTLPDLLRRRAARFPDRVALREKE-DGIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAI-LSDNRpEWVIADLAIL 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  106 LTGVVPAPLavpptYAESS----------SGT-----------QKLKDAW---TLLDKPAVITDRGMHQE--MLDWAK-- 157
Cdd:COG1022     87 AAGAVTVPI-----YPTSSaeevayilndSGAkvlfvedqeqlDKLLEVRdelPSLRHIVVLDPRGLRDDprLLSLDEll 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  158 EQGlegfRAIIVEDLLSAEadtdWHQSSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPF 237
Cdd:COG1022    162 ALG----REVADPAELEAR----RAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFLPL 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  238 DHVGG-IGMLHLrdVYLGCQeINV--SSETIL----------------------------MEPLKWL-----DW-----I 276
Cdd:COG1022    234 AHVFErTVSYYA--LAAGAT-VAFaeSPDTLAedlrevkptfmlavprvwekvyagiqakAEEAGGLkrklfRWalavgR 310
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  277 DHYRASVT-WAPNFAFGLVTDFAEEIKDRKW-DL--SSMRYMLNGGEAMvakvGRRILELLEPHGLPadaIRPAWGMSET 352
Cdd:COG1022    311 RYARARLAgKSPSLLLRLKHALADKLVFSKLrEAlgGRLRFAVSGGAAL----GPELARFFRALGIP---VLEGYGLTET 383
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  353 SsGVIFSHEF--TRAGTsdddhfveIGSPIPGFSMRIVndhnelvEEGEIgrfQVSGLSVTSGYYQRPDLNESVFTEDGW 430
Cdd:COG1022    384 S-PVITVNRPgdNRIGT--------VGPPLPGVEVKIA-------EDGEI---LVRGPNVMKGYYKNPEATAEAFDADGW 444
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|
gi 1776025254  431 FETGDLGFLR-NGRLTITGRTKDaIII--NGINYYSHAIESAVEELSEIE 477
Cdd:COG1022    445 LHTGDIGELDeDGFLRITGRKKD-LIVtsGGKNVAPQPIENALKASPLIE 493
BCL_4HBCL cd05959
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ...
1157-1639 1.87e-45

Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.


Pssm-ID: 341269 [Multi-domain]  Cd Length: 508  Bit Score: 174.48  E-value: 1.87e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1157 ELFEQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGP-DRLAGIYVDrSLDMLVGLLAILKAGGAYVPLDP 1235
Cdd:cd05959      8 LVDLNLNEGRGDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKReERVLLIMLD-TVDFPTAFLGAIRAGIVPVPVNT 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1236 SYPAERLEYMLEDSEVFITLTTSELVNTL--SWNGVTTALLDQDWDEIAQTASDRKVLTRTVT------------PENLA 1301
Cdd:cd05959     87 LLTPDDYAYYLEDSRARVVVVSGELAPVLaaALTKSEHTLVVLIVSGGAGPEAGALLLAELVAaeaeqlkpaathADDPA 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1302 YVIYTSGSTGKPKGVMIPHKALTNFLVSMGE-TPGLTAEDKmlavttyCFDIAAL--------ELFLPLIKGAHCyICQT 1372
Cdd:cd05959    167 FWLYSSGSTGRPKGVVHLHADIYWTAELYARnVLGIREDDV-------CFSAAKLffayglgnSLTFPLSVGATT-VLMP 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1373 EHTKDVEKLKRdIRTIKPTVMQATPATW-KMLFYSGWENEENVKI-LC--GGEALPETLKRYFLD-TGSEAWNMFGPTET 1447
Cdd:cd05959    239 ERPTPAAVFKR-IRRYRPTVFFGVPTLYaAMLAAPNLPSRDLSSLrLCvsAGEALPAEVGERWKArFGLDILDGIGSTEM 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1448 T---IWSAVQRINDECSratiGRPIANTQIYITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIdnpfepGSk 1524
Cdd:cd05959    318 LhifLSNRPGRVRYGTT----GKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQ------GE- 386
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1525 LYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVA--DMDNL---AAYYTAK---HANAS 1596
Cdd:cd05959    387 WTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGveDEDGLtkpKAFVVLRpgyEDSEA 466
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|...
gi 1776025254 1597 LtARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLK 1639
Cdd:cd05959    467 L-EEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
FACL_like_6 cd05922
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
1186-1639 8.96e-45

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341246 [Multi-domain]  Cd Length: 457  Bit Score: 171.08  E-value: 8.96e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1186 ERSTQLAIYLQAHG-VGPDRLAgIYVDRSLDMLVGLLAILKAGGA----YVPLDPSYPAERLEYMLEDSEVFITLTTSEL 1260
Cdd:cd05922      1 LGVSAAASALLEAGgVRGERVV-LILPNRFTYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRIVLADAGA 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1261 VNTLSWNGVTTALLDQDWDEIAQTASDRKVLTRTVTPENLAYVIYTSGSTGKPKGVMIPHKALTNFLVSMGETPGLTAED 1340
Cdd:cd05922     80 ADRLRDALPASPDPGTVLDADGIRAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADD 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1341 KMLAVTTYCFDIAALELFLPLIKGAHCYIcqTEHTKDVEKLKRDIRTIKPTVMQATPATWKMLFYSGWENEE--NVKIL- 1417
Cdd:cd05922    160 RALTVLPLSYDYGLSVLNTHLLRGATLVL--TNDGVLDDAFWEDLREHGATGLAGVPSTYAMLTRLGFDPAKlpSLRYLt 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1418 -CGGEALPETLKRYF-LDTGSEAWNMFGPTETTIWSAV---QRINDECSraTIGRPIANTQIYITDSQLAPVPAGVPGEL 1492
Cdd:cd05922    238 qAGGRLPQETIARLReLLPGAQVYVMYGQTEATRRMTYlppERILEKPG--SIGLAIPGGEFEILDDDGTPTPPGEPGEI 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1493 CIAGDGVAKGYYKkeeltDSRFIDNPFEPGSKLYrTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGI 1572
Cdd:cd05922    316 VHRGPNVMKGYWN-----DPPYRRKEGRGGGVLH-TGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLI 389
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1776025254 1573 LECVVVAD----MDNLAAYYTAKhanASLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLK 1639
Cdd:cd05922    390 IEAAAVGLpdplGEKLALFVTAP---DKIDPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
elong_cond_enzymes cd00828
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ...
3339-3776 2.96e-44

"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, including beta-ketoacyl [ACP] synthase, type I and II and polyketide synthases.They are characterized by the utlization of acyl carrier protein (ACP) thioesters as primer substrates, as well as the nature of their active site residues.


Pssm-ID: 238424 [Multi-domain]  Cd Length: 407  Bit Score: 168.39  E-value: 2.96e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3339 EPVAIVGISGRFP---GAMDIDEFWKNLEEGKDSITEVPKDRWDWREHY-GNPDTdvnktdikwgGFIDGvaefdplffG 3414
Cdd:cd00828      1 SRVVITGIGVVSPhgeGCDEVEEFWEALREGRSGIAPVARLKSRFDRGVaGQIPT----------GDIPG---------W 61
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3415 ISPREADyVDPQQRLLMTYVWKALEDAGC-PPQSLSGTGTGIFIGTGnTGYKDLFHRANLP----IEGHAATGHM--IPS 3487
Cdd:cd00828     62 DAKRTGI-VDRTTLLALVATEEALADAGItDPYEVHPSEVGVVVGSG-MGGLRFLRRGGKLdaraVNPYVSPKWMlsPNT 139
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3488 VGPNRMSYFLNIHGPSEPVETACSSSLVAIHRAVTAMQNGDCEMAIAGGVNTILTEEAhISYSKAGMLSKD-----GRCK 3562
Cdd:cd00828    140 VAGWVNILLLSSHGPIKTPVGACATALEALDLAVEAIRSGKADIVVVGGVEDPLEEGL-SGFANMGALSTAeeepeEMSR 218
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3563 TFSADANGYVRGEGVGMVMLKKLEDAERDGNHIYGVIRGTAENHGGRANTLTSPNPkAQADLLVRAYRQAGIDPSTVTYI 3642
Cdd:cd00828    219 PFDETRDGFVEAEGAGVLVLERAELALARGAPIYGRVAGTASTTDGAGRSVPAGGK-GIARAIRTALAKAGLSLDDLDVI 297
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3643 EAHGTGTELGDPIEINGLKAAFKELsnmrGESQPdvpdhrcgIGSVKSNIGHLELAAGISGLIKVLLQMKHKTLVKSLHC 3722
Cdd:cd00828    298 SAHGTSTPANDVAESRAIAEVAGAL----GAPLP--------VTAQKALFGHSKGAAGALQLIGALQSLEHGLIPPTANL 365
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1776025254 3723 ETLNPYLQLTdspfYIVQEKQEWksvtdcdgNELPRRAGISSFGIGGVNAHIVI 3776
Cdd:cd00828    366 DDVDPDVEHL----SVVGLSRDL--------NLKVRAALVNAFGFGGSNAALVL 407
CHC_CoA_lg cd05903
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ...
61-556 1.06e-43

Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.


Pssm-ID: 341229 [Multi-domain]  Cd Length: 437  Bit Score: 167.56  E-value: 1.06e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254   61 SYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNSQLLPAFWGCVLTGVVPAPlaVPPTYAEsssgtQKLkdAWTLLDKP 140
Cdd:cd05903      3 TYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNP--ILPFFRE-----HEL--AFILRRAK 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  141 A---VITDRgmhqemldwakeqgLEGFRaiivedllsaeadtdwHQSSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVK 217
Cdd:cd05903     74 AkvfVVPER--------------FRQFD----------------PAAMPDAVALLLFTSGTTGEPKGVMHSHNTLSASIR 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  218 GIIQMQGFTREDItfNWM--PFDHVGGIGMLHLRDVYLGcqeinvsSETILME---PLKWLDWIDHYRASVTW-APNFAF 291
Cdd:cd05903    124 QYAERLGLGPGDV--FLVasPMAHQTGFVYGFTLPLLLG-------APVVLQDiwdPDKALALMREHGVTFMMgATPFLT 194
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  292 GLVTdfAEEIKDRkwDLSSMRYMLNGGEAMVAKVGRRILELLEPHglpadaIRPAWGMSETSS--GVIFSHEFTRAGTSD 369
Cdd:cd05903    195 DLLN--AVEEAGE--PLSRLRTFVCGGATVPRSLARRAAELLGAK------VCSAYGSTECPGavTSITPAPEDRRLYTD 264
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  370 ddhfveiGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGYYQRPDLNeSVFTEDGWFETGDLGFL-RNGRLTITG 448
Cdd:cd05903    265 -------GRPLPGVEIKVVDDTGATLAPGVEGELLSRGPSVFLGYLDRPDLT-ADAAPEGWFRTGDLARLdEDGYLRITG 336
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  449 RTKDAIIINGINYYSHAIESA-VEELSEIETSYTAACAVRLGQNStdqlAIFFVTS--AKLNDEQMSQLLRNiQSHVSQV 525
Cdd:cd05903    337 RSKDIIIRGGENIPVLEVEDLlLGHPGVIEAAVVALPDERLGERA----CAVVVTKsgALLTFDELVAYLDR-QGVAKQY 411
                          490       500       510
                   ....*....|....*....|....*....|.
gi 1776025254  526 IgvtPEYLlpVQKEEIPKTAIGKIQRTQLKT 556
Cdd:cd05903    412 W---PERL--VHVDDLPRTPSGKVQKFRLRE 437
VL_LC_FACS_like cd05907
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ...
61-470 5.06e-43

Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341233 [Multi-domain]  Cd Length: 452  Bit Score: 165.85  E-value: 5.06e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254   61 SYRRLWDDGLRIVKGLRQSGLKaKQSVILQLGDNSqllPAFW----GCVLTGVVPAPLavpptYAESSSGTQklkdAWTL 136
Cdd:cd05907      7 TWAEFAEEVRALAKGLIALGVE-PGDRVAILSRNR---PEWTiadlAILAIGAVPVPI-----YPTSSAEQI----AYIL 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  137 LDKPAvitdrgmhqemldwakeqglegfRAIIVEDllsaeadtdwhqssPEDLALLLLTSGSTGTPKAVMLNHRNIMSMV 216
Cdd:cd05907     74 NDSEA-----------------------KALFVED--------------PDDLATIIYTSGTTGRPKGVMLSHRNILSNA 116
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  217 KGIIQMQGFTREDITFNWMPFDHVGGIGMLHLRDVYLGCQEINVSSETILMEPLKWLDwiDHYRASV--TWAPNFAFGLV 294
Cdd:cd05907    117 LALAERLPATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFASSAETLLDDLSEVR--PTVFLAVprVWEKVYAAIKV 194
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  295 TDfAEEIKDRKWDL---SSMRYMLNGGeamvAKVGRRILELLEPHGLPadaIRPAWGMSETSSGVIFSHEFT-RAGTsdd 370
Cdd:cd05907    195 KA-VPGLKRKLFDLavgGRLRFAASGG----APLPAELLHFFRALGIP---VYEGYGLTETSAVVTLNPPGDnRIGT--- 263
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  371 dhfveIGSPIPGFSMRIVNDhnelveeGEIgrfQVSGLSVTSGYYQRPDLNESVFTEDGWFETGDLG-FLRNGRLTITGR 449
Cdd:cd05907    264 -----VGKPLPGVEVRIADD-------GEI---LVRGPNVMLGYYKNPEATAEALDADGWLHTGDLGeIDEDGFLHITGR 328
                          410       420
                   ....*....|....*....|...
gi 1776025254  450 TKDaIIIN--GINYYSHAIESAV 470
Cdd:cd05907    329 KKD-LIITsgGKNISPEPIENAL 350
PRK13295 PRK13295
cyclohexanecarboxylate-CoA ligase; Reviewed
30-557 1.21e-42

cyclohexanecarboxylate-CoA ligase; Reviewed


Pssm-ID: 171961 [Multi-domain]  Cd Length: 547  Bit Score: 167.15  E-value: 1.21e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254   30 TIPEVLYRTAAELGDTKGIIYLQPDGTEVYQ-SYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNSQLLPAFWGCVLTG 108
Cdd:PRK13295    25 TINDDLDACVASCPDKTAVTAVRLGTGAPRRfTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIG 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  109 VVPAPLavPPTYAESS-SGTQKLKDAwTLLDKPAVItdRGM-HQEML-----DWAKEQ--------GLEGFRAIIVEDLL 173
Cdd:PRK13295   105 AVLNPL--MPIFRERElSFMLKHAES-KVLVVPKTF--RGFdHAAMArrlrpELPALRhvvvvggdGADSFEALLITPAW 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  174 SAEADT----DWHQSSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDHVGGIGMLHLR 249
Cdd:PRK13295   180 EQEPDApailARLRPGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPMAHQTGFMYGLMM 259
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  250 DVYLGcqeinvsSETILM---EPLKWLDWIDHYRASVTWApnfAFGLVTDFAEEIKDRKWDLSSMRYMLNGGEAMVAKVG 326
Cdd:PRK13295   260 PVMLG-------ATAVLQdiwDPARAAELIRTEGVTFTMA---STPFLTDLTRAVKESGRPVSSLRTFLCAGAPIPGALV 329
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  327 RRILELLEPHglpadaIRPAWGMSETS--SGVIFSHEFTRAGTSDddhfveiGSPIPGFSMRIVNDHNELVEEGEIGRFQ 404
Cdd:PRK13295   330 ERARAALGAK------IVSAWGMTENGavTLTKLDDPDERASTTD-------GCPLPGVEVRVVDADGAPLPAGQIGRLQ 396
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  405 VSGLSVTSGYYQRPDLNESVFteDGWFETGDLGFL-RNGRLTITGRTKDAIIINGINYYSHAIESAVEELSEIETsyTAA 483
Cdd:PRK13295   397 VRGCSNFGGYLKRPQLNGTDA--DGWFDTGDLARIdADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQ--VAI 472
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  484 CAV---RLGQNstdqlAIFFVT---SAKLNDEQMSQLLRNiQSHVSQVIgvtPEYLlpVQKEEIPKTAIGKIQ----RTQ 553
Cdd:PRK13295   473 VAYpdeRLGER-----ACAFVVprpGQSLDFEEMVEFLKA-QKVAKQYI---PERL--VVRDALPRTPSGKIQkfrlREM 541

                   ....
gi 1776025254  554 LKTS 557
Cdd:PRK13295   542 LRGE 545
PRK05850 PRK05850
acyl-CoA synthetase; Validated
100-566 1.23e-42

acyl-CoA synthetase; Validated


Pssm-ID: 235624 [Multi-domain]  Cd Length: 578  Bit Score: 167.81  E-value: 1.23e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  100 AFWGCVLTGVVPAPLAVPPTYAESSSGTQKLKDAwtlldKPAVI-TDRGMHQEMLDWAKEQGLEGFRAIIVEDLL--SAE 176
Cdd:PRK05850    75 AFLGALQAGLIAVPLSVPQGGAHDERVSAVLRDT-----SPSVVlTTSAVVDDVTEYVAPQPGQSAPPVIEVDLLdlDSP 149
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  177 ADTDWHQSSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIiqMQGFTRE-------DITF-NWMPFDHVGGIgMLHL 248
Cdd:PRK05850   150 RGSDARPRDLPSTAYLQYTSGSTRTPAGVMVSHRNVIANFEQL--MSDYFGDtggvpppDTTVvSWLPFYHDMGL-VLGV 226
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  249 -RDVYLGCQEINVSSETILMEPLKWLDWIDHYRASVTWAPNFAFGLVTdfaeeikdRK--------WDLSSMRYMLNGGE 319
Cdd:PRK05850   227 cAPILGGCPAVLTSPVAFLQRPARWMQLLASNPHAFSAAPNFAFELAV--------RKtsdddmagLDLGGVLGIISGSE 298
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  320 AMVAKVGRRILELLEPHGLPADAIRPAWGMSE------------TSSGVIFSHEF----------TRAGTSdddhFVEIG 377
Cdd:PRK05850   299 RVHPATLKRFADRFAPFNLRETAIRPSYGLAEatvyvatrepgqPPESVRFDYEKlsaghakrceTGGGTP----LVSYG 374
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  378 SPIPGfSMRIVnDHNELVE--EGEIGRFQVSGLSVTSGYYQRPDLNESVF----------TEDG-WFETGDLGFLRNGRL 444
Cdd:PRK05850   375 SPRSP-TVRIV-DPDTCIEcpAGTVGEIWVHGDNVAAGYWQKPEETERTFgatlvdpspgTPEGpWLRTGDLGFISEGEL 452
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  445 TITGRTKDAIIINGINYYSHAIESAVEelsEIETSYTAACAVrlGQNSTDQLaiffVTSAKLN-----DEQMSQLL---- 515
Cdd:PRK05850   453 FIVGRIKDLLIVDGRNHYPDDIEATIQ---EITGGRVAAISV--PDDGTEKL----VAIIELKkrgdsDEEAMDRLrtvk 523
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1776025254  516 RNIQSHVSQVIGVTPEYLLPVQKEEIPKTAIGKIQRTQLKTSFENGEFDHL 566
Cdd:PRK05850   524 REVTSAISKSHGLSVADLVLVAPGSIPITTSGKIRRAACVEQYRQDEFTRL 574
MACS_like cd05972
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ...
1179-1639 1.82e-42

Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.


Pssm-ID: 341276 [Multi-domain]  Cd Length: 428  Bit Score: 163.66  E-value: 1.82e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1179 LTYRELDERSTQLAIYLQAHGVGP-DRLAGIyVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLEDSEVFITLTT 1257
Cdd:cd05972      1 WSFRELKRESAKAANVLAKLGLRKgDRVAVL-LPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTD 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1258 SElvntlswngvttalldqdwdeiaqtasdrkvltrtvtpeNLAYVIYTSGSTGKPKGVMIPHKALTNFLVSMGETPGLT 1337
Cdd:cd05972     80 AE---------------------------------------DPALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLR 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1338 AEDKMLAVTTYCFDIAAL-ELFLPLIKGAHCYICqTEHTKDVEKLKRDIRTIKPTVMQATPATWKMLFYSGWE--NEENV 1414
Cdd:cd05972    121 PDDIHWNIADPGWAKGAWsSFFGPWLLGATVFVY-EGPRFDAERILELLERYGVTSFCGPPTAYRMLIKQDLSsyKFSHL 199
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1415 KIL-CGGEAL-PETLKRYFLDTGSEAWNMFGPTETTIWSAVQRINDeCSRATIGRPIANTQIYITDSQLAPVPAGVPGEL 1492
Cdd:cd05972    200 RLVvSAGEPLnPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMP-VKPGSMGRPTPGYDVAIIDDDGRELPPGEEGDI 278
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1493 CI--AGDGVAKGYYKKEELTDSRFIDNpfepgskLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHP 1570
Cdd:cd05972    279 AIklPPPGLFLGYVGDPEKTEASIRGD-------YYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHP 351
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1776025254 1571 GILECVVVADMDNL------AAYYTAKHANAS-LTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLK 1639
Cdd:cd05972    352 AVAEAAVVGSPDPVrgevvkAFVVLTSGYEPSeELAEELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRVELR 427
starter-C_NRPS cd19533
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ...
693-1121 2.17e-42

Starter Condensation domains, found in the first module of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. While standard C-domains catalyze peptide bond formation between two amino acids, an initial, ('starter') C-domain may instead acylate an amino acid with a fatty acid. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380456 [Multi-domain]  Cd Length: 419  Bit Score: 162.92  E-value: 2.17e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  693 FQPLSEVQKGLWTLQKMSPEKSAYHVPLCFKFSSGLHLETLQQAFGLVLNQHPILKHVIQEKDGVPILKNEPALSIEIKT 772
Cdd:cd19533      1 RLPLTSAQRGVWFAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEEEGEPYQWIDPYTPVPIRH 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  773 ENISSMK--ESDIPAFLRKKVKEPYVKENSPLVRVMSFSRSEQEHFLLVVIHHLIFDGVSSVTFIHSLFDTYQLLLKGQQ 850
Cdd:cd19533     81 IDLSGDPdpEGAAQQWMQEDLRKPLPLDNDPLFRHALFTLGDNRHFWYQRVHHIVMDGFSFALFGQRVAEIYTALLKGRP 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  851 PeiavSPAIYHDFAAW---EKNMLAGKDGVKHRTYWQKQLSGTLPNLQL-PKVSASSVSEFREdtyTRRLSSGFMNQVRM 926
Cdd:cd19533    161 A----PPAPFGSFLDLveeEQAYRQSERFERDRAFWTEQFEDLPEPVSLaRRAPGRSLAFLRR---TAELPPELTRTLLE 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  927 FAKEHSVNVTTVFLSCYMMLLGRYTGQKEQIVGMPAMVRPEERFDDAIGHFLNMLPIRSELNPADTFSSFISKLQLTILD 1006
Cdd:cd19533    234 AAEAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRLGAAARQTPGMVANTLPLRLTVDPQQTFAELVAQVSRELRS 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1007 GLDHAAYPFPKMVRDLNipRSQAGSPVFQTAFFYQNFlqsgSYQsllsryADFFSVDYVEYIHQEG---EYEL-VFELWe 1082
Cdd:cd19533    314 LLRHQRYRYEDLRRDLG--LTGELHPLFGPTVNYMPF----DYG------LDFGGVVGLTHNLSSGptnDLSIfVYDRD- 380
                          410       420       430
                   ....*....|....*....|....*....|....*....
gi 1776025254 1083 TEEKMELNIKYNTGLFDAASISAMFDHFVYVTEQAMLNP 1121
Cdd:cd19533    381 DESGLRIDFDANPALYSGEDLARHQERLLRLLEEAAADP 419
PRK08316 PRK08316
acyl-CoA synthetase; Validated
1163-1633 2.43e-42

acyl-CoA synthetase; Validated


Pssm-ID: 181381 [Multi-domain]  Cd Length: 523  Bit Score: 165.49  E-value: 2.43e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1163 AKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGP-DRLAgIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAER 1241
Cdd:PRK08316    21 ARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKgDRVA-ALGHNSDAYALLWLACARAGAVHVPVNFMLTGEE 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1242 LEYMLEDSEVFITLTTSELVNT----------------LSWNGVTTALLDQDWDEIAQTASDRKVLTRtVTPENLAYVIY 1305
Cdd:PRK08316   100 LAYILDHSGARAFLVDPALAPTaeaalallpvdtlilsLVLGGREAPGGWLDFADWAEAGSVAEPDVE-LADDDLAQILY 178
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1306 TSGSTGKPKGVMIPHKALTNFLVSMGETPGLTAEDKML-AVTTY-CfdiAALELFLplikGAHCYICQTEH---TKDVEK 1380
Cdd:PRK08316   179 TSGTESLPKGAMLTHRALIAEYVSCIVAGDMSADDIPLhALPLYhC---AQLDVFL----GPYLYVGATNVildAPDPEL 251
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1381 LKRDIRTIKPTVMQATPATWKMLFYSGWENEENVKILCGG---------EALPETLKRYfldTGSEAWNMFGPTETTIWS 1451
Cdd:PRK08316   252 ILRTIEAERITSFFAPPTVWISLLRHPDFDTRDLSSLRKGyygasimpvEVLKELRERL---PGLRFYNCYGQTEIAPLA 328
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1452 AVQRINDECSRA-TIGRPIANTQIYITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPFepgsklyRTGD 1530
Cdd:PRK08316   329 TVLGPEEHLRRPgSAGRPVLNVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAFRGGWF-------HSGD 401
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1531 MARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMDN-----LAAYYTAKhANASLTARELRHF 1605
Cdd:PRK08316   402 LGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPkwieaVTAVVVPK-AGATVTEDELIAH 480
                          490       500
                   ....*....|....*....|....*...
gi 1776025254 1606 VKNALPAYMVPSYFIQLDHMPLTPNGKI 1633
Cdd:PRK08316   481 CRARLAGFKVPKRVIFVDELPRNPSGKI 508
ttLC_FACS_AlkK_like cd12119
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
1158-1640 6.04e-42

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.


Pssm-ID: 341284 [Multi-domain]  Cd Length: 518  Bit Score: 164.34  E-value: 6.04e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1158 LFEQQAKKTPDRAAVSYEGQ----TLTYRELDERSTQLAIYLQAHGVGP-DRLAgiyvdrSLDM-----LVGLLAILKAG 1227
Cdd:cd12119      1 LLEHAARLHGDREIVSRTHEgevhRYTYAEVAERARRLANALRRLGVKPgDRVA------TLAWnthrhLELYYAVPGMG 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1228 GAYVPLDPSYPAERLEYMLEDSE---VFI-------------TLTTSELVNTLSWNG---VTTALLDQDWDEIAQTASDR 1288
Cdd:cd12119     75 AVLHTINPRLFPEQIAYIINHAEdrvVFVdrdflplleaiapRLPTVEHVVVMTDDAampEPAGVGVLAYEELLAAESPE 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1289 KVLTrtVTPENLAYVI-YTSGSTGKPKGVMIPHKALtnFLVSMG----ETPGLTAEDKMLAVT------TYCFDIAAL-- 1355
Cdd:cd12119    155 YDWP--DFDENTAAAIcYTSGTTGNPKGVVYSHRSL--VLHAMAalltDGLGLSESDVVLPVVpmfhvnAWGLPYAAAmv 230
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1356 --ELFLPlikGAHcyicqtehtKDVEKLKRDIRTIKPTVMQATPATWKMLFYSGWENEENV----KILCGGEALPETLKR 1429
Cdd:cd12119    231 gaKLVLP---GPY---------LDPASLAELIEREGVTFAAGVPTVWQGLLDHLEANGRDLsslrRVVIGGSAVPRSLIE 298
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1430 YFLDTGSE---AWNMfgpTETTIWSAVQRINDECS----------RATIGRPIANTQIYITDSQLAPVPA-GVP-GELCI 1494
Cdd:cd12119    299 AFEERGVRvihAWGM---TETSPLGTVARPPSEHSnlsedeqlalRAKQGRPVPGVELRIVDDDGRELPWdGKAvGELQV 375
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1495 AGDGVAKGYYKKEELTDSRFIDNPFepgsklyRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILE 1574
Cdd:cd12119    376 RGPWVTKSYYKNDEESEALTEDGWL-------RTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAE 448
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1776025254 1575 CVVVADMDN------LAayYTAKHANASLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLKN 1640
Cdd:cd12119    449 AAVIGVPHPkwgerpLA--VVVLKEGATVTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
PRK12316 PRK12316
peptide synthase; Provisional
3-1040 6.08e-42

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 172.45  E-value: 6.08e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254    3 NNDNIRILANPSVSHGEPLHISEKQPATIPEVLYRTAAELGDTKGIIYL-------QPDGTEVY-----QSYRRLWDDGL 70
Cdd:PRK12316  3014 QNLLRGMVENPQRSVDELAMLDAEERGQLLEAWNATAAEYPLERGVHRLfeeqverTPDAVALAfgeqrLSYAELNRRAN 3093
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254   71 RIVKGLRQSGLKAKQSVILQLGDNSQLLPAFWGCVLTGVVPAPLavPPTYAESssgtqklKDAWTLLDKPAvitDRGMHQ 150
Cdd:PRK12316  3094 RLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPL--DPEYPEE-------RLAYMLEDSGA---QLLLSQ 3161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  151 EMLDWAKEQGLEGFrAIIVEDLLSAEADTDWHqSSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDI 230
Cdd:PRK12316  3162 SHLRLPLAQGVQVL-DLDRGDENYAEANPAIR-TMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDR 3239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  231 TFNWMPFDHVGGIGMLHLrdvylgcqEINVSSETILMEPLKWLD---WIDHYRASVTWAPNFAFGLVTDFAEEIKDRkwD 307
Cdd:PRK12316  3240 VLQFTTFSFDVFVEELFW--------PLMSGARVVLAGPEDWRDpalLVELINSEGVDVLHAYPSMLQAFLEEEDAH--R 3309
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  308 LSSMRYMLNGGEAMVAKVGRRILellephglpadAIRPAWGMSETSSGVIFSHEFTRAGTSDDDHFveIGSPIPGFSMRI 387
Cdd:PRK12316  3310 CTSLKRIVCGGEALPADLQQQVF-----------AGLPLYNLYGPTEATITVTHWQCVEEGKDAVP--IGRPIANRACYI 3376
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  388 VNDHNELVEEGEIGRFQVSGLSVTSGYYQRPDLNESVFTEDGW------FETGDLGFLR-NGRLTITGRTKDAIIINGIN 460
Cdd:PRK12316  3377 LDGSLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPFvpgerlYRTGDLARYRaDGVIEYIGRVDHQVKIRGFR 3456
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  461 YyshaiesaveELSEIETSYTAACAVR---LGQNSTDQLAIFFVTSAKLNDeqmsqLLRNIQSHVSQVIgvtPEYLLPVQ 537
Cdd:PRK12316  3457 I----------ELGEIEARLLEHPWVReavVLAVDGRQLVAYVVPEDEAGD-----LREALKAHLKASL---PEYMVPAH 3518
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  538 ---KEEIPKTAIGKIQRtqlktsfengefdHLLHKPnrmndavqDEEMQQADHVKRVrEEIQEHLLTCLTEELHVSRdwV 614
Cdd:PRK12316  3519 llfLERMPLTPNGKLDR-------------KALPRP--------DAALLQQDYVAPV-NELERRLAAIWADVLKLEQ--V 3574
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  615 EPNANIQSLGVNSIKMMKLIrSIEKNYHIKLTAREIHQYPTIERLAsylsehedlsssSADKKGTDTYKTEPERSQATfq 694
Cdd:PRK12316  3575 GLTDNFFELGGDSIISLQVV-SRARQAGIRFTPKDLFQHQTIQGLA------------RVARVGGGVAVDQGPVSGET-- 3639
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  695 PLSEVQKGLwtLQKMSPEKSAYHVPLCFKFSSGLHLETLQQAFGLVLNQHPILKHVIQEKDGVPILKNEPAL---SIEIK 771
Cdd:PRK12316  3640 LLLPIQQQF--FEEPVPERHHWNQSLLLKPREALDAAALEAALQALVEHHDALRLRFVEDAGGWTAEHLPVElggALLWR 3717
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  772 TENIS-SMKESdipafLRKKVKEPYVKENSPLVRVMSFSRSEQEHFLLVVIHHLIFDGVSSVTFIHSLFDTYQLLLKGQQ 850
Cdd:PRK12316  3718 AELDDaEELER-----LGEEAQRSLDLADGPLLRALLATLADGSQRLLLVIHHLVVDGVSWRILLEDLQQAYQQLLQGEA 3792
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  851 PEIAVSPAIYHDFAAWEKNMLAGKDGVKHRTYWQKQLSGTLPNL-------QLPKVSASSVSEFREDTYTRRLssgfmnq 923
Cdd:PRK12316  3793 PRLPAKTSSFKAWAERLQEHARGEALKAELAYWQEQLQGVSSELpcdhpqgALQNRHAASVQTRLDRELTRRL------- 3865
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  924 VRMFAKEHSVNVTTVFLSCYMMLLGRYTGQKEQIVGMPAMVRpEERFDD-----AIGHFLNMLPIRseLNPADTFSSFIS 998
Cdd:PRK12316  3866 LQQAPAAYRTQVNDLLLTALARVVCRWTGEASALVQLEGHGR-EDLFADidlsrTVGWFTSLFPVR--LSPVEDLGASIK 3942
                         1050      1060      1070      1080
                   ....*....|....*....|....*....|....*....|....
gi 1776025254  999 --KLQLTILDGlDHAAYPFPKMVRDLNIPRSQAGSPVFQTAFFY 1040
Cdd:PRK12316  3943 aiKEQLRAIPN-KGIGFGLLRYLGDEESRRTLAGLPVPRITFNY 3985
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
4590-4989 6.60e-42

Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible for the elongation steps in fatty acid biosynthesis. KASIII catalyses the initial condensation and KAS I and II catalyze further elongation steps by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP.


Pssm-ID: 238430 [Multi-domain]  Cd Length: 406  Bit Score: 161.17  E-value: 6.60e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4590 IAVVGLSCRFPGAETLESYWSLLSEGRSSIGPIPAERWGCKTPYYAGVIDGvsyFDPDFFLLhEEDVRAMDPQALLVL-- 4667
Cdd:cd00834      3 VVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRFDASGFPSRIAGEVPD---FDPEDYLD-RKELRRMDRFAQFALaa 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4668 -EECLKllyHAGYTPEEIKGKPVGVYIGG--------RSQHKPDEDSLDHAKNP--IVTVGQNYLAANLSQFFDVRGPSV 4736
Cdd:cd00834     79 aEEALA---DAGLDPEELDPERIGVVIGSgigglatiEEAYRALLEKGPRRVSPffVPMALPNMAAGQVAIRLGLRGPNY 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4737 VVDTACSSALVGMNMAIQALRGGDIQSAIVGGVSLLSSDASHRLFDRRGILSKHSSFHV-----FDERADGVVLGEGVGM 4811
Cdd:cd00834    156 TVSTACASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALRALSTRNDDPEkasrpFDKDRDGFVLGEGAGV 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4812 VMLKTVKQALEDGDTIYAVVKAASVNNDGR--TAgPAtPNLEAQKEVMKDALFKSGKKPEDISYLEANGSGSIVTDLLEL 4889
Cdd:cd00834    236 LVLESLEHAKARGAKIYAEILGYGASSDAYhiTA-PD-PDGEGAARAMRAALADAGLSPEDIDYINAHGTSTPLNDAAES 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4890 KAIQSVYrSGHSSPLSLGSIKPNIGHPLCAEGIASFIKVVLMLKERRFVPflsgekeMAHFDQQKA----NITFSRAlek 4965
Cdd:cd00834    314 KAIKRVF-GEHAKKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPP-------TINLEEPDPecdlDYVPNEA--- 382
                          410       420
                   ....*....|....*....|....*
gi 1776025254 4966 wTDSQPTAAINC-FADGGTNVHVIV 4989
Cdd:cd00834    383 -REAPIRYALSNsFGFGGHNASLVF 406
FACL_fum10p_like cd05926
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ...
1167-1640 8.25e-42

Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.


Pssm-ID: 341249 [Multi-domain]  Cd Length: 493  Bit Score: 163.25  E-value: 8.25e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1167 PDRAAVSYEGQT--LTYRELDERSTQLAIYLQAHGVGP-DRLAgIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLE 1243
Cdd:cd05926      1 PDAPALVVPGSTpaLTYADLAELVDDLARQLAALGIKKgDRVA-IALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1244 YMLEDSEVFITLTTSELVNTLSWNGVTT--ALLDQDWD-----------EIAQTASDRKVLTRT--VTPENLAYVIYTSG 1308
Cdd:cd05926     80 FYLADLGSKLVLTPKGELGPASRAASKLglAILELALDvgvlirapsaeSLSNLLADKKNAKSEgvPLPDDLALILHTSG 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1309 STGKPKGVMIPHkalTNFLVSM---GETPGLTAEDKMLAVTTYcFDIAAL--ELFLPLIKGAhCYICQteHTKDVEKLKR 1383
Cdd:cd05926    160 TTGRPKGVPLTH---RNLAASAtniTNTYKLTPDDRTLVVMPL-FHVHGLvaSLLSTLAAGG-SVVLP--PRFSASTFWP 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1384 DIRTIKPTVMQATPATWKMLFYSGWENEENVK-----ILCGGEALPET----LKRYFLDTGSEAWNMfgpTETTIWSAVQ 1454
Cdd:cd05926    233 DVRDYNATWYTAVPTIHQILLNRPEPNPESPPpklrfIRSCSASLPPAvleaLEATFGAPVLEAYGM---TEAAHQMTSN 309
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1455 RINDECSRA-TIGRPiANTQIYITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPFepgsklYRTGDMAR 1533
Cdd:cd05926    310 PLPPGPRKPgSVGKP-VGVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGW------FRTGDLGY 382
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1534 WLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMD-----NLAAYYTAKhANASLTARELRHFVKN 1608
Cdd:cd05926    383 LDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDekygeEVAAAVVLR-EGASVTEEELRAFCRK 461
                          490       500       510
                   ....*....|....*....|....*....|..
gi 1776025254 1609 ALPAYMVPSYFIQLDHMPLTPNGKIDRNSLKN 1640
Cdd:cd05926    462 HLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
MACS_like_3 cd05971
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
1180-1639 1.03e-41

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341275 [Multi-domain]  Cd Length: 439  Bit Score: 161.83  E-value: 1.03e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1180 TYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLEDSEvfitlttse 1259
Cdd:cd05971      8 TFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSG--------- 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1260 lvntlswngvTTALLdqdwdeiaqtasdrkvltrTVTPENLAYVIYTSGSTGKPKGVMIPHKALtnflvsMGETPGLTAE 1339
Cdd:cd05971     79 ----------ASALV-------------------TDGSDDPALIIYTSGTTGPPKGALHAHRVL------LGHLPGVQFP 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1340 DKMLAVTTYCFDIAA--------LELFLP-LIKGAHCYICQTEHTkDVEKLKRDIRTIKPTVMQATPATWKMLFYSGWEN 1410
Cdd:cd05971    124 FNLFPRDGDLYWTPAdwawigglLDVLLPsLYFGVPVLAHRMTKF-DPKAALDLMSRYGVTTAFLPPTALKMMRQQGEQL 202
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1411 EE---NVK-ILCGGEALPETL----KRYFLDTGSEAwnmFGPTETTIW----SAVQRINDecsrATIGRPIANTQIYITD 1478
Cdd:cd05971    203 KHaqvKLRaIATGGESLGEELlgwaREQFGVEVNEF---YGQTECNLVigncSALFPIKP----GSMGKPIPGHRVAIVD 275
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1479 SQLAPVPAGVPGELCIA-GDGVAK-GYYKKEELTDSRFIdnpfepgSKLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFR 1556
Cdd:cd05971    276 DNGTPLPPGEVGEIAVElPDPVAFlGYWNNPSATEKKMA-------GDWLLTGDLGRKDSDGYFWYVGRDDDVITSSGYR 348
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1557 IELGDIESRLSEHPGILECVVVADMDN-----LAAYYtakHANASLT-----ARELRHFVKNALPAYMVPSYFIQLDHMP 1626
Cdd:cd05971    349 IGPAEIEECLLKHPAVLMAAVVGIPDPirgeiVKAFV---VLNPGETpsdalAREIQELVKTRLAAHEYPREIEFVNELP 425
                          490
                   ....*....|...
gi 1776025254 1627 LTPNGKIDRNSLK 1639
Cdd:cd05971    426 RTATGKIRRRELR 438
LCL_NRPS-like cd19540
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ...
695-1117 1.58e-41

LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380463 [Multi-domain]  Cd Length: 433  Bit Score: 161.05  E-value: 1.58e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  695 PLSEVQKGLWTLQKMSPEKSAYHVPLCFKFSSGLHLETLQQAFGLVLNQHPILKHVIQEKDGVP---ILKNEPAlSIEIK 771
Cdd:cd19540      3 PLSFAQQRLWFLNRLDGPSAAYNIPLALRLTGALDVDALRAALADVVARHESLRTVFPEDDGGPyqvVLPAAEA-RPDLT 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  772 TENISsmkESDIPAFLRKKVKEPY-VKENSPLvRVMSFSRSEQEHFLLVVIHHLIFDGVSSVTFIHSLFDTYQLLLKGQQ 850
Cdd:cd19540     82 VVDVT---EDELAARLAEAARRGFdLTAELPL-RARLFRLGPDEHVLVLVVHHIAADGWSMAPLARDLATAYAARRAGRA 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  851 PEIAVSPAIYHDFAAWEKNMLAGKD---GVKHR--TYWQKQLSGtLPN-LQLPkvsA----SSVSEFREDTYTRRLSSGF 920
Cdd:cd19540    158 PDWAPLPVQYADYALWQRELLGDEDdpdSLAARqlAYWRETLAG-LPEeLELP---TdrprPAVASYRGGTVEFTIDAEL 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  921 MNQVRMFAKEHSVNVTTVFLSCYMMLLGRYTGQKEQIVGMPAMVRPEERFDDAIGHFLNMLPIRSELNPADTFSSFISKL 1000
Cdd:cd19540    234 HARLAALAREHGATLFMVLHAALAVLLSRLGAGDDIPIGTPVAGRGDEALDDLVGMFVNTLVLRTDVSGDPTFAELLARV 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1001 QLTILDGLDHAAYPFPKMVRDLNIPRSQAGSPVFQTAFFYQNFLQSGsyqsllsryADF--FSVDYVEYIHQEGEYELVF 1078
Cdd:cd19540    314 RETDLAAFAHQDVPFERLVEALNPPRSTARHPLFQVMLAFQNTAAAT---------LELpgLTVEPVPVDTGVAKFDLSF 384
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*
gi 1776025254 1079 ELWETEEK------MELNIKYNTGLFDAASISAMFDHFVYVTEQA 1117
Cdd:cd19540    385 TLTERRDAdgapagLTGELEYATDLFDRSTAERLADRFVRVLEAV 429
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
186-554 2.51e-41

The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341253 [Multi-domain]  Cd Length: 444  Bit Score: 160.77  E-value: 2.51e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  186 PEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMP--FDhvggigmLHLRDVYL-----GCQEI 258
Cdd:cd05930     92 PDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAYPLTPGDRVLQFTSfsFD-------VSVWEIFGallagATLVV 164
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  259 nVSSETILmEPLKWLDWIDHYRASVTWAPNFAFGLVTDFAEEikdrkWDLSSMRYMLNGGEAMVAKVGRRILELLEPHgl 338
Cdd:cd05930    165 -LPEEVRK-DPEALADLLAEEGITVLHLTPSLLRLLLQELEL-----AALPSLRLVLVGGEALPPDLVRRWRELLPGA-- 235
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  339 padAIRPAWGMSETSsgvIFSHEFTRAGTSDDDHFVEIGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGYYQRP 418
Cdd:cd05930    236 ---RLVNLYGPTEAT---VDATYYRVPPDDEEDGRVPIGRPIPNTRVYVLDENLRPVPPGVPGELYIGGAGLARGYLNRP 309
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  419 DLNESVFTEDGWFE------TGDLG-FLRNGRLTITGRTKDAIIINGinyysH-----AIESAVEELSEIEtsyTAACAV 486
Cdd:cd05930    310 ELTAERFVPNPFGPgermyrTGDLVrWLPDGNLEFLGRIDDQVKIRG-----YrielgEIEAALLAHPGVR---EAAVVA 381
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1776025254  487 RLGQNSTDQLAIFFVTsaklnDEQMSQLLRNIQSHVSQVIgvtPEYLLP---VQKEEIPKTAIGKIQRTQL 554
Cdd:cd05930    382 REDGDGEKRLVAYVVP-----DEGGELDEEELRAHLAERL---PDYMVPsafVVLDALPLTPNGKVDRKAL 444
LC_FACS_like cd17640
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ...
1177-1586 4.04e-41

Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341295 [Multi-domain]  Cd Length: 468  Bit Score: 160.60  E-value: 4.04e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1177 QTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLEDSEVfitlt 1256
Cdd:cd17640      4 KRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSES----- 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1257 tselvntlswngvTTALLDQDwdeiaqtasdrkvltrtvtPENLAYVIYTSGSTGKPKGVMIPHKALTNFLVSMGETPGL 1336
Cdd:cd17640     79 -------------VALVVEND-------------------SDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPP 126
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1337 TAEDKMLAVTT--YCFDIAAlELFLpLIKGAhcyicqTEHTKDVEKLKRDIRTIKPTVMQATPATWKMLfYSGWENE--- 1411
Cdd:cd17640    127 QPGDRFLSILPiwHSYERSA-EYFI-FACGC------SQAYTSIRTLKDDLKRVKPHYIVSVPRLWESL-YSGIQKQvsk 197
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1412 ---------------ENVKI-LCGGEALPETLKRYFLDTGSEAWNMFGPTETTIWSAVQRInDECSRATIGRPIANTQIY 1475
Cdd:cd17640    198 sspikqflflfflsgGIFKFgISGGGALPPHVDTFFEAIGIEVLNGYGLTETSPVVSARRL-KCNVRGSVGRPLPGTEIK 276
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1476 ITDSQL-APVPAGVPGELCIAGDGVAKGYYKKEELTdSRFIDNpfepgSKLYRTGDMARWLPGGRIEYIGRI-DNQVKIR 1553
Cdd:cd17640    277 IVDPEGnVVLPPGEKGIVWVRGPQVMKGYYKNPEAT-SKVLDS-----DGWFNTGDLGWLTCGGELVLTGRAkDTIVLSN 350
                          410       420       430
                   ....*....|....*....|....*....|....
gi 1776025254 1554 GFRIELGDIESRLSEHPGILECVVVA-DMDNLAA 1586
Cdd:cd17640    351 GENVEPQPIEEALMRSPFIEQIMVVGqDQKRLGA 384
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
695-1121 4.13e-41

DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor; The DCL-type Condensation (C) domain catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. This domain is D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains in addition to the LCL- and DCL-types such as starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380465 [Multi-domain]  Cd Length: 423  Bit Score: 159.29  E-value: 4.13e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  695 PLSEVQKGLWTLQKMSPEKSAYHVPLCFKFSSGLHLETLQQAFGLVLNQHPILK-HVIQEKDGVP---ILKNEPalsIEI 770
Cdd:cd19543      3 PLSPMQEGMLFHSLLDPGSGAYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRtSFVWEGLGEPlqvVLKDRK---LPW 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  771 KTENISSM----KESDIPAFLRKKVKEPYVKENSPLVRVMSFSRSEQEHFLLVVIHHLIFDGVSSVTFIHSLFDTYQLLL 846
Cdd:cd19543     80 RELDLSHLseaeQEAELEALAEEDRERGFDLARAPLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAALG 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  847 KGQQPEIAVSPAiYHDFAAWeknmLAGKDGVKHRTYWQKQLSG-----TLPNLQLpkvsASSVSEFREDTYTRRLSSGFM 921
Cdd:cd19543    160 EGQPPSLPPVRP-YRDYIAW----LQRQDKEAAEAYWREYLAGfeeptPLPKELP----ADADGSYEPGEVSFELSAELT 230
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  922 NQVRMFAKEHSVNVTTVFLSCYMMLLGRYTGQKEQIVGMPAMVRPEER--FDDAIGHFLNMLPIRSELNPADTFSSFISK 999
Cdd:cd19543    231 ARLQELARQHGVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGRPAELpgIETMVGLFINTLPVRVRLDPDQTVLELLKD 310
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1000 LQLTILDGLDHAAYPFPKMVRdlnipRSQAGSPVFQTAFFYQNFLQSGSyqSLLSRYADFFSVDYVEyIHQEGEYELVFE 1079
Cdd:cd19543    311 LQAQQLELREHEYVPLYEIQA-----WSEGKQALFDHLLVFENYPVDES--LEEEQDEDGLRITDVS-AEEQTNYPLTVV 382
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|..
gi 1776025254 1080 LWETEEkMELNIKYNTGLFDAASISAMFDHFVYVTEQAMLNP 1121
Cdd:cd19543    383 AIPGEE-LTIKLSYDAEVFDEATIERLLGHLRRVLEQVAANP 423
KR_3_FAS_SDR_x cd08956
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 3, complex (x); ...
2836-3076 6.83e-41

beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 3, complex (x); Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. In some instances, such as porcine FAS, an enoyl reductase (ER) module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consists of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthesis uses a dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-KR, forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta- ER. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes KR domains found in many multidomain PKSs, including six of seven Sorangium cellulosum PKSs (encoded by spiDEFGHIJ) which participate in the synthesis of the polyketide scaffold of the cytotoxic spiroketal polyketide spirangien. These seven PKSs have either a single PKS module (SpiF), two PKR modules (SpiD,-E,-I,-J), or three PKS modules (SpiG,-H). This subfamily includes the second KR domains of SpiE,-G, I, and -J, both KR domains of SpiD, and the third KR domain of SpiH. The single KR domain of SpiF, the first and second KR domains of SpiH, the first KR domains of SpiE,-G,- I, and -J, and the third KR domain of SpiG, belong to a different KR_FAS_SDR subfamily. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187659 [Multi-domain]  Cd Length: 448  Bit Score: 159.35  E-value: 6.83e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2836 PSADTLHMPWRDEGVYLITGGAGSLGLLFAKEIANRTGRSTIVLTGRSVLSEDKENELEA-LRSIGAEVVYREADVSDQH 2914
Cdd:cd08956    181 ATLPPVPRPLDPDGTVLITGGTGTLGALLARHLVTEHGVRHLLLVSRRGPDAPGAAELVAeLAALGAEVTVAACDVADRA 260
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2915 AVHHLFEEI-KERygTLNGIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSGLLHVDECSKDFPLDFFIFFSSVSGCLGNAG 2993
Cdd:cd08956    261 ALAALLAAVpADH--PLTAVVHAAGVLDDGVLTSLTPERLDAVLRPKVDAAWHLHELTRDLDLAAFVLFSSAAGVLGSPG 338
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2994 QADYAAANSFMDAFAEYRRS--LAASkkrfgstiSFNWPLWEEGGM---QVGAEDEKRMlKTTGMVPMPTDSGLKAFYQG 3068
Cdd:cd08956    339 QANYAAANAFLDALAQHRRArgLPAT--------SLAWGLWAQASGmtaHLSDADLARL-ARGGLRPLSAEEGLALFDAA 409

                   ....*...
gi 1776025254 3069 IASDKPQV 3076
Cdd:cd08956    410 LAADEPVL 417
menE TIGR01923
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ...
61-554 9.50e-41

O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 162605 [Multi-domain]  Cd Length: 436  Bit Score: 158.77  E-value: 9.50e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254   61 SYRRLWDDGLRIVKGLRQSGLKaKQSVILQLGDNS-QLLPAFWGCVLTGVVPAPLAvpPTYAESSSGTQkLKDawtlLDK 139
Cdd:TIGR01923    1 TWQDLDCEAAHLAKALKAQGIR-SGSRVALVGQNSiEMVLLLHACLLLGAEIAMLN--TRLTENERTNQ-LED----LDV 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  140 PAVITDrgmhqEMLDwakeqgLEGFRAIIVEDL-LSAEADTDWHQSSP-EDLALLLLTSGSTGTPKAVMLNHRNIMSMVK 217
Cdd:TIGR01923   73 QLLLTD-----SLLE------EKDFQADSLDRIeAAGRYETSLSASFNmDQIATLMFTSGTTGKPKAVPHTFRNHYASAV 141
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  218 GIIQMQGFTREDitfNWM---PFDHVGGIGMLhLRDVYLGCQEINVSSETILMEPLKwldwidhyRASVTWApnfafGLV 294
Cdd:TIGR01923  142 GSKENLGFTEDD---NWLlslPLYHISGLSIL-FRWLIEGATLRIVDKFNQLLEMIA--------NERVTHI-----SLV 204
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  295 TDFAEEIKDRKWDLSSMRYMLNGGEAMVAKVGRRILELlephGLPadaIRPAWGMSETSSGVI-FSHEFTRAGTSdddhf 373
Cdd:TIGR01923  205 PTQLNRLLDEGGHNENLRKILLGGSAIPAPLIEEAQQY----GLP---IYLSYGMTETCSQVTtATPEMLHARPD----- 272
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  374 veIGSPIPGFSMRIVNDhnELVEEGEIgrfQVSGLSVTSGYYQRPDLNESVFtEDGWFETGDLGFLRN-GRLTITGRTKD 452
Cdd:TIGR01923  273 --VGRPLAGREIKIKVD--NKEGHGEI---MVKGANLMKGYLYQGELTPAFE-QQGWFNTGDIGELDGeGFLYVLGRRDD 344
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  453 AIIINGINYYSHAIESAVEELSEIETsytaaCAVRLGQNST-DQLAIFFVTSAklNDEQMSQLLRNIQSHVSQVigVTPE 531
Cdd:TIGR01923  345 LIISGGENIYPEEIETVLYQHPGIQE-----AVVVPKPDAEwGQVPVAYIVSE--SDISQAKLIAYLTEKLAKY--KVPI 415
                          490       500
                   ....*....|....*....|...
gi 1776025254  532 YLLPVQkeEIPKTAIGKIQRTQL 554
Cdd:TIGR01923  416 AFEKLD--ELPYNASGKILRNQL 436
Ketoacyl-synt_C pfam02801
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ...
4828-4944 3.33e-40

Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.


Pssm-ID: 426989  Cd Length: 118  Bit Score: 146.17  E-value: 3.33e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4828 YAVVKAASVNNDGRTAGPATPNLEAQKEVMKDALFKSGKKPEDISYLEANGSGSIVTDLLELKAIQSVYRSGH-SSPLSL 4906
Cdd:pfam02801    1 YAVIKGSAVNHDGRHNGLTAPNGEGQARAIRRALADAGVDPEDVDYVEAHGTGTPLGDPIEAEALKRVFGSGArKQPLAI 80
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1776025254 4907 GSIKPNIGHPLCAEGIASFIKVVLMLKERRFVPFLSGE 4944
Cdd:pfam02801   81 GSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLNLE 118
omega_3_PfaA TIGR02813
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ...
4590-5009 4.06e-40

polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this alignment are involved in omega-3 polyunsaturated fatty acid biosynthesis, such as the protein PfaA from the eicosapentaenoic acid biosynthesis operon in Photobacterium profundum strain SS9. PfaA is encoded together with PfaB, PfaC, and PfaD, and the functions of the individual polypeptides have not yet been described. More distant homologs of PfaA, also included with the reach of this model, appear to be involved in polyketide-like biosynthetic mechanisms of polyunsaturated fatty acid biosynthesis, an alternative to the more familiar iterated mechanism of chain extension and desaturation, and in most cases are encoded near genes for homologs of PfaB, PfaC, and/or PfaD.


Pssm-ID: 274311 [Multi-domain]  Cd Length: 2582  Bit Score: 166.33  E-value: 4.06e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4590 IAVVGLSCRFPGAETLESYWSLLSEGRSSIGPIPAERWGcKTPYY--------------AGVIDGVSyFDPDFFLLHEED 4655
Cdd:TIGR02813    9 IAIVGMASIFANSRYLNKFWDLIFEKIDAITDVPSDHWA-KDDYYdsdkseadksyckrGGFLPEVD-FNPMEFGLPPNI 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4656 VRAMDPQALLVLEECLKLLYHAGyTPEEIKGKPVGVYIG---GRSQHKP--------------------DEDS------- 4705
Cdd:TIGR02813   87 LELTDISQLLSLVVAKEVLNDAG-LPDGYDRDKIGITLGvggGQKQSSSlnarlqypvlkkvfkasgveDEDSemlikkf 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4706 ----LDHAKNPIVTVGQNYLAANLSQFFDVRGPSVVVDTACSSALVGMNMAIQALRGGDIQSAIVGGVSLLSSDASHRLF 4781
Cdd:TIGR02813  166 qdqyIHWEENSFPGSLGNVISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGGVCTDNSPFMYMSF 245
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4782 DRRGILSKHSSFHVFDERADGVVLGEGVGMVMLKTVKQALEDGDTIYAVVKAASVNNDGRTAGPATPNLEAQKEVMKDAL 4861
Cdd:TIGR02813  246 SKTPAFTTNEDIQPFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGKFKSIYAPRPEGQAKALKRAY 325
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4862 FKSGKKPEDISYLEANGSGSIVTDLLELKAIQSVYRSGHSSP--LSLGSIKPNIGHPLCAEGIASFIKVVLMLKERRFVP 4939
Cdd:TIGR02813  326 DDAGFAPHTCGLIEAHGTGTAAGDVAEFGGLVSVFSQDNDQKqhIALGSVKSQIGHTKSTAGTAGMIKAVLALHHKVLPP 405
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1776025254 4940 FLSGEKEMAHFDQQKANITFSRALEKW---TDSQP-TAAINCFADGGTNVHVIVEAWEKDEKHAIKRSPKSPPQ 5009
Cdd:TIGR02813  406 TINVDQPNPKLDIENSPFYLNTETRPWmqrEDGTPrRAGISSFGFGGTNFHMVLEEYSPKHQRDDQYRQRAVAQ 479
KR_1_SDR_x cd08952
ketoreductase (KR), subgroup 1, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
2836-3078 4.80e-40

ketoreductase (KR), subgroup 1, complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes KR domains found in many multidomain PKSs, including six of seven Sorangium cellulosum PKSs (encoded by spiDEFGHIJ) which participate in the synthesis of the polyketide scaffold of the cytotoxic spiroketal polyketide spirangien. These seven PKSs have either a single PKS module (SpiF), two PKR modules (SpiD,-E,-I,-J), or three PKS modules (SpiG,-H). This subfamily includes the single KR domain of SpiF, the first KR domains of SpiE,-G,H,-I,and #J, the third KR domain of SpiG, and the second KR domain of SpiH. The second KR domains of SpiE,-G, I, and #J, and the KR domains of SpiD, belong to a different KR_FAS_SDR subfamily. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187655 [Multi-domain]  Cd Length: 480  Bit Score: 157.72  E-value: 4.80e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2836 PSADTLHMPWRDEGVYLITGGAGSLGLLFAKEIAnRTGRSTIVLTGRSVLSEDKENELEA-LRSIGAEVVYREADVSDQH 2914
Cdd:cd08952    218 PAPAPAARPWRPRGTVLVTGGTGALGAHVARWLA-RRGAEHLVLTSRRGPDAPGAAELVAeLTALGARVTVAACDVADRD 296
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2915 AVHHLFEEIKERYgTLNGIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSGLLHVDECSKDFPLDFFIFFSSVSGCLGNAGQ 2994
Cdd:cd08952    297 ALAALLAALPAGH-PLTAVVHAAGVLDDGPLDDLTPERLAEVLRAKVAGARHLDELTRDRDLDAFVLFSSIAGVWGSGGQ 375
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2995 ADYAAANSFMDAFAEYRRS--LAASkkrfgstiSFNWPLWEEGGMqVGAEDEKRmLKTTGMVPMPTDSGLKAFYQGIASD 3072
Cdd:cd08952    376 GAYAAANAYLDALAERRRArgLPAT--------SVAWGPWAGGGM-AAGAAAER-LRRRGLRPMDPELALAALRRALDHD 445

                   ....*.
gi 1776025254 3073 KPQVFV 3078
Cdd:cd08952    446 ETAVVV 451
DltA cd05945
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ...
54-554 1.01e-39

D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341267 [Multi-domain]  Cd Length: 449  Bit Score: 155.87  E-value: 1.01e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254   54 DGTEVYQSYRRLWDDGLRIVKGLRQSGLKAKQSVILqLGDNSQL-LPAFWGCVLTG--VVPAPLAVPPtyaessSGTQKL 130
Cdd:cd05945     11 VEGGRTLTYRELKERADALAAALASLGLDAGDPVVV-YGHKSPDaIAAFLAALKAGhaYVPLDASSPA------ERIREI 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  131 KDAwtllDKPAVItdrgmhqemldwakeqglegfraIIVEDllsaeadtdwhqsspeDLALLLLTSGSTGTPKAVMLNHR 210
Cdd:cd05945     84 LDA----AKPALL-----------------------IADGD----------------DNAYIIFTSGSTGRPKGVQISHD 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  211 NIMSMVKGIIQMQGFTREDITFNWMP--FDhvggigmLHLRDVYL-----GCqeINVSSETILMEPLKWLDWIDHYRASV 283
Cdd:cd05945    121 NLVSFTNWMLSDFPLGPGDVFLNQAPfsFD-------LSVMDLYPalasgAT--LVPVPRDATADPKQLFRFLAEHGITV 191
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  284 tW--APNFAFGLVTD--FAEEikdrkwDLSSMRYMLNGGEAMVAKVGRRILELLephglPADAIRPAWGMSETSSGVIfS 359
Cdd:cd05945    192 -WvsTPSFAAMCLLSptFTPE------SLPSLRHFLFCGEVLPHKTARALQQRF-----PDARIYNTYGPTEATVAVT-Y 258
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  360 HEFTRAGTSDDDHfVEIGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGYYQRPDLNESVFTED---GWFETGDL 436
Cdd:cd05945    259 IEVTPEVLDGYDR-LPIGYAKPGAKLVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDegqRAYRTGDL 337
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  437 GFLRN-GRLTITGRTKDAIIINGINYYSHAIESAVEELSEIEtsytAACAVRLGQNSTDQLAIFFVTsakLNDEQMSQLL 515
Cdd:cd05945    338 VRLEAdGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVK----EAVVVPKYKGEKVTELIAFVV---PKPGAEAGLT 410
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|..
gi 1776025254  516 RNIQSHVSQVIgvtPEYLLP---VQKEEIPKTAIGKIQRTQL 554
Cdd:cd05945    411 KAIKAELAERL---PPYMIPrrfVYLDELPLNANGKIDRKAL 449
CHC_CoA_lg cd05903
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ...
1178-1633 1.41e-39

Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.


Pssm-ID: 341229 [Multi-domain]  Cd Length: 437  Bit Score: 155.23  E-value: 1.41e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1178 TLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLEDSEVFITLTT 1257
Cdd:cd05903      1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1258 SElvntlsWNGVTTALLdqdwdeiaqtasdrkvltrtvtPENLAYVIYTSGSTGKPKGVMIPHKALTNFLVSMGETPGLT 1337
Cdd:cd05903     81 ER------FRQFDPAAM----------------------PDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLG 132
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1338 AEDKMLAVTTYCFDIAALELF-LPLIKGAHCYICQTEHTKDVEKLkrdIRTIKPTVMQATPATWKMLFYSGWENEENV-- 1414
Cdd:cd05903    133 PGDVFLVASPMAHQTGFVYGFtLPLLLGAPVVLQDIWDPDKALAL---MREHGVTFMMGATPFLTDLLNAVEEAGEPLsr 209
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1415 --KILCGGEALPETLKRYFLDTG----SEAWNMfgpTETTiwSAVQRINDECSRA---TIGRPIANTQIYITDSQLAPVP 1485
Cdd:cd05903    210 lrTFVCGGATVPRSLARRAAELLgakvCSAYGS---TECP--GAVTSITPAPEDRrlyTDGRPLPGVEIKVVDDTGATLA 284
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1486 AGVPGELCIAGDGVAKGYYKKEELTdSRFIDNPFepgsklYRTGDMARWLPGGRIEYIGRIDNqVKIR-GFRIELGDIES 1564
Cdd:cd05903    285 PGVEGELLSRGPSVFLGYLDRPDLT-ADAAPEGW------FRTGDLARLDEDGYLRITGRSKD-IIIRgGENIPVLEVED 356
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1776025254 1565 RLSEHPGILECVVVADMD-----NLAAYYTAKhANASLTARELR-HFVKNALPAYMVPSYFIQLDHMPLTPNGKI 1633
Cdd:cd05903    357 LLLGHPGVIEAAVVALPDerlgeRACAVVVTK-SGALLTFDELVaYLDRQGVAKQYWPERLVHVDDLPRTPSGKV 430
PRK06178 PRK06178
acyl-CoA synthetase; Validated
1163-1638 1.66e-39

acyl-CoA synthetase; Validated


Pssm-ID: 235724 [Multi-domain]  Cd Length: 567  Bit Score: 157.90  E-value: 1.66e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1163 AKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGP-DRLAgIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAER 1241
Cdd:PRK06178    43 ARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAgDRVA-VFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHE 121
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1242 LEYMLEDS--EVFITL-------------TTSELVNTLSWNGVTTA--------------LLDQDWDEI--AQTASDRKV 1290
Cdd:PRK06178   122 LSYELNDAgaEVLLALdqlapvveqvraeTSLRHVIVTSLADVLPAeptlplpdslraprLAAAGAIDLlpALRACTAPV 201
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1291 LTRTVTPENLAYVIYTSGSTGKPKGVMIPHK-----ALTNFLVSMGETPGltaeDKMLAVTTYcFDIAA--LELFLPLIK 1363
Cdd:PRK06178   202 PLPPPALDALAALNYTGGTTGMPKGCEHTQRdmvytAAAAYAVAVVGGED----SVFLSFLPE-FWIAGenFGLLFPLFS 276
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1364 GA------------------HCYICQTEHTKD--VEKL------KRDIRTikptvMQATPAtwkMLFysgweneenVKIL 1417
Cdd:PRK06178   277 GAtlvllarwdavafmaaveRYRVTRTVMLVDnaVELMdhprfaEYDLSS-----LRQVRV---VSF---------VKKL 339
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1418 CggealPETLKRYFLDTGS----EAWNMfgpTET----TIWSAVQRIN-DECSRAT-IGRPIANTQIYITDSQL-APVPA 1486
Cdd:PRK06178   340 N-----PDYRQRWRALTGSvlaeAAWGM---TEThtcdTFTAGFQDDDfDLLSQPVfVGLPVPGTEFKICDFETgELLPL 411
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1487 GVPGELCIAGDGVAKGYYKKEELTDSRFIDNpfepgskLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRL 1566
Cdd:PRK06178   412 GAEGEIVVRTPSLLKGYWNKPEATAEALRDG-------WLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALL 484
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1776025254 1567 SEHPGILECVVVADMDN-----LAAYYTAKhANASLTARELRHFVKNALPAYMVPSYFIqLDHMPLTPNGKIDRNSL 1638
Cdd:PRK06178   485 GQHPAVLGSAVVGRPDPdkgqvPVAFVQLK-PGADLTAAALQAWCRENMAVYKVPEIRI-VDALPMTATGKVRKQDL 559
BCL_4HBCL cd05959
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ...
31-555 2.46e-39

Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.


Pssm-ID: 341269 [Multi-domain]  Cd Length: 508  Bit Score: 156.37  E-value: 2.46e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254   31 IPEVLYRTAAELGDTKGIIYlqPDGTevyQSYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNSQLLPAFWGCVLTGVV 110
Cdd:cd05959      6 ATLVDLNLNEGRGDKTAFID--DAGS---LTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  111 PAP---LAVPPTYAE--SSSGTQKLKDAWTLLDK-PAVITDRGMHQEMLDWAKEQGLEGFRAIIVEDLLSAEADTDWHQS 184
Cdd:cd05959     81 PVPvntLLTPDDYAYylEDSRARVVVVSGELAPVlAAALTKSEHTLVVLIVSGGAGPEAGALLLAELVAAEAEQLKPAAT 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  185 SPEDLALLLLTSGSTGTPKAVMLNHRNIMSM----VKGIIqmqGFTREDITFNWMPFDHVGGIGmlhlRDVYLgcqEINV 260
Cdd:cd05959    161 HADDPAFWLYSSGSTGRPKGVVHLHADIYWTaelyARNVL---GIREDDVCFSAAKLFFAYGLG----NSLTF---PLSV 230
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  261 SSETILM----EPLKWLDWIDHYRasvtwaPNFAFGLVTDFAEEIKDRKW---DLSSMRYMLNGGEAMVAKVGRRI---- 329
Cdd:cd05959    231 GATTVLMperpTPAAVFKRIRRYR------PTVFFGVPTLYAAMLAAPNLpsrDLSSLRLCVSAGEALPAEVGERWkarf 304
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  330 -LELLEphglpadairpawGMSETSSGVIFSHEFTRA---GTSdddhfveiGSPIPGFSMRIVNDHNELVEEGEIGRFQV 405
Cdd:cd05959    305 gLDILD-------------GIGSTEMLHIFLSNRPGRvryGTT--------GKPVPGYEVELRDEDGGDVADGEPGELYV 363
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  406 SGLSVTSGYYQRPDLNESVFtEDGWFETGDlGFLRN--GRLTITGRTKDAIIINGINYYSHAIESAVEELSEIetsytAA 483
Cdd:cd05959    364 RGPSSATMYWNNRDKTRDTF-QGEWTRTGD-KYVRDddGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAV-----LE 436
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  484 CAVrLGQNSTDQL---AIFFVtsakLNDEQMSQ--LLRNIQSHVSQVIgvtPEYLLPVQKE---EIPKTAIGKIQRTQLK 555
Cdd:cd05959    437 AAV-VGVEDEDGLtkpKAFVV----LRPGYEDSeaLEEELKEFVKDRL---APYKYPRWIVfvdELPKTATGKIQRFKLR 508
PRK07769 PRK07769
long-chain-fatty-acid--CoA ligase; Validated
167-561 4.17e-39

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 181109 [Multi-domain]  Cd Length: 631  Bit Score: 157.97  E-value: 4.17e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  167 IIVEDLLSAEADTDWHQSSP--EDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDHvgGIG 244
Cdd:PRK07769   158 VIAVDAVPDEVGATWVPPEAneDTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEGQEGDRGVSWLPFFH--DMG 235
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  245 MLHLRDVYLGCQEINV-SSETILMEPLKWLDWI----DHYRASVTWAPNFAF------GLVTDfaeeiKDRKWDLSSMRY 313
Cdd:PRK07769   236 LITVLLPALLGHYITFmSPAAFVRRPGRWIRELarkpGGTGGTFSAAPNFAFehaaarGLPKD-----GEPPLDLSNVKG 310
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  314 MLNGGEAMVAKVGRRILELLEPHGLPADAIRPAWGMSETSSGV--IFSHEFTRAGTSDDD-----HFVEIGSPIP----- 381
Cdd:PRK07769   311 LLNGSEPVSPASMRKFNEAFAPYGLPPTAIKPSYGMAEATLFVstTPMDEEPTVIYVDRDelnagRFVEVPADAPnavaq 390
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  382 ---GFSMR-----IVnDHNELVE--EGEIGRFQVSGLSVTSGYYQRPDLNESVF----------------TEDG-WFETG 434
Cdd:PRK07769   391 vsaGKVGVsewavIV-DPETASElpDGQIGEIWLHGNNIGTGYWGKPEETAATFqnilksrlseshaegaPDDAlWVRTG 469
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  435 DLGFLRNGRLTITGRTKDAIIINGINYYSHAIESAVEELSE-IETSYTAACAVRLGQ------------------NSTDQ 495
Cdd:PRK07769   470 DYGVYFDGELYITGRVKDLVIIDGRNHYPQDLEYTAQEATKaLRTGYVAAFSVPANQlpqvvfddshaglkfdpeDTSEQ 549
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1776025254  496 LAIFFVTSAKLNDEQMSQLLRNIQSHVSQVIGVTPEYLLPVQKEEIPKTAIGKIQRTQLKTSFENG 561
Cdd:PRK07769   550 LVIVAERAPGAHKLDPQPIADDIRAAIAVRHGVTVRDVLLVPAGSIPRTSSGKIARRACRAAYLDG 615
MACS_like_2 cd05973
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
1179-1640 5.20e-39

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341277 [Multi-domain]  Cd Length: 437  Bit Score: 153.83  E-value: 5.20e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1179 LTYRELDERSTQLAIYLQAHGVGP-DRLAGIyVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLEDSEVFITLTt 1257
Cdd:cd05973      1 LTFGELRALSARFANALQELGVGPgDVVAGL-LPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVT- 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1258 selvntlswngvttalldqDWDEIAQTASDRKVLtrtvtpenlayvIYTSGSTGKPKGVMIPHKALTNFLVSMGETPGLT 1337
Cdd:cd05973     79 -------------------DAANRHKLDSDPFVM------------MFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLR 127
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1338 AEDKMlavttycFDIA----ALELFL----PLIKGAHCYICQTEHTkdVEKLKRDIRTIKPTVMQATPATWKMLFYSGWE 1409
Cdd:cd05973    128 PEDSF-------WNAAdpgwAYGLYYaitgPLALGHPTILLEGGFS--VESTWRVIERLGVTNLAGSPTAYRLLMAAGAE 198
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1410 NEENVK-----ILCGGEALPETLKRYFLDT-GSEAWNMFGPTETTIWSAVQR-INDECSRATIGRPIANTQIYITDSQLA 1482
Cdd:cd05973    199 VPARPKgrlrrVSSAGEPLTPEVIRWFDAAlGVPIHDHYGQTELGMVLANHHaLEHPVHAGSAGRAMPGWRVAVLDDDGD 278
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1483 PVPAGVPGELCIAGDGVA----KGYYKKEELTdsrfidnpfePGSKLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIE 1558
Cdd:cd05973    279 ELGPGEPGRLAIDIANSPlmwfRGYQLPDTPA----------IDGGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIG 348
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1559 LGDIESRLSEHPGILECVVVADMDN-----LAAY--YTAKHANASLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNG 1631
Cdd:cd05973    349 PFDVESALIEHPAVAEAAVIGVPDPertevVKAFvvLRGGHEGTPALADELQLHVKKRLSAHAYPRTIHFVDELPKTPSG 428

                   ....*....
gi 1776025254 1632 KIDRNSLKN 1640
Cdd:cd05973    429 KIQRFLLRR 437
A_NRPS_Srf_like cd12117
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...
33-554 2.17e-38

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.


Pssm-ID: 341282 [Multi-domain]  Cd Length: 483  Bit Score: 152.74  E-value: 2.17e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254   33 EVLYRTAAELGDTKGIIYlqpDGTEVyqSYRRLWDDGLRIVKGLRQSGLkAKQSVILQLGDNS-QLLPAFWGCVLTG--V 109
Cdd:cd12117      1 ELFEEQAARTPDAVAVVY---GDRSL--TYAELNERANRLARRLRAAGV-GPGDVVGVLAERSpELVVALLAVLKAGaaY 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  110 VPAPLAVPPTYAESSsgtqkLKDAwtllDKPAVITDRGMhqemldwAKEQGLEGFRAIIVEDLLSAEADTDWHQSSPEDL 189
Cdd:cd12117     75 VPLDPELPAERLAFM-----LADA----GAKVLLTDRSL-------AGRAGGLEVAVVIDEALDAGPAGNPAVPVSPDDL 138
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  190 ALLLLTSGSTGTPKAVMLNHRNIMSMVKGiiqmQGFTRED----------ITFNWMPFDHVGGI---GMLHLrdvylgcq 256
Cdd:cd12117    139 AYVMYTSGSTGRPKGVAVTHRGVVRLVKN----TNYVTLGpddrvlqtspLAFDASTFEIWGALlngARLVL-------- 206
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  257 einVSSETILmEPLKWLDWIDHYRASVTWAPNFAFGLVTDFAEEIkdrkwdLSSMRYMLNGGEAMVAKVGRRILElleph 336
Cdd:cd12117    207 ---APKGTLL-DPDALGALIAEEGVTVLWLTAALFNQLADEDPEC------FAGLRELLTGGEVVSPPHVRRVLA----- 271
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  337 GLPADAIRPAWGMSETSsgvIFSHEFTRAGTSDDDHFVEIGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGYYQ 416
Cdd:cd12117    272 ACPGLRLVNGYGPTENT---TFTTSHVVTELDEVAGSIPIGRPIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLN 348
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  417 RPDLNESVFTEDGW------FETGDL-GFLRNGRLTITGRTKDAIIINGINYYSHAIESAVEELSEIEtsyTAACAVRLG 489
Cdd:cd12117    349 RPALTAERFVADPFgpgerlYRTGDLaRWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVR---EAVVVVRED 425
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1776025254  490 QNSTDQLAIFFVTSAKLNDEQmsqllrnIQSHVSQVIgvtPEYLLP---VQKEEIPKTAIGKIQRTQL 554
Cdd:cd12117    426 AGGDKRLVAYVVAEGALDAAE-------LRAFLRERL---PAYMVPaafVVLDELPLTANGKVDRRAL 483
PRK08314 PRK08314
long-chain-fatty-acid--CoA ligase; Validated
1149-1633 2.19e-38

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236235 [Multi-domain]  Cd Length: 546  Bit Score: 154.35  E-value: 2.19e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1149 TYPYITFHELFEQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAH-GVGP-DRLAgIYVDRSLDMLVGLLAILKA 1226
Cdd:PRK08314     6 TLPETSLFHNLEVSARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQQEcGVRKgDRVL-LYMQNSPQFVIAYYAILRA 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1227 GGAYVPLDPSYPAERLEYMLEDSEVFITLTTSELVN---------TLSWNGVTT---ALLDQ------DWDEIA---QTA 1285
Cdd:PRK08314    85 NAVVVPVNPMNREEELAHYVTDSGARVAIVGSELAPkvapavgnlRLRHVIVAQysdYLPAEpeiavpAWLRAEpplQAL 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1286 SDRKVLT-------------RTVTPENLAYVIYTSGSTGKPKGVMIPHKALTNFLVSMGETPGLTAEDKMLAVTTYcFDI 1352
Cdd:PRK08314   165 APGGVVAwkealaaglapppHTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPL-FHV 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1353 AALELFL--PLIKGAHCYICqtehTK-DVEKLKRDIRTIKPTVMQATPATWKMLFYSGWENEENVKILC----GGEALPE 1425
Cdd:PRK08314   244 TGMVHSMnaPIYAGATVVLM----PRwDREAAARLIERYRVTHWTNIPTMVVDFLASPGLAERDLSSLRyiggGGAAMPE 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1426 TLKRYFLD-TGSEAWNMFGPTET---TIWSAVQRINDECsratIGRPIANTQIYITDSQ-LAPVPAGVPGELCIAGDGVA 1500
Cdd:PRK08314   320 AVAERLKElTGLDYVEGYGLTETmaqTHSNPPDRPKLQC----LGIPTFGVDARVIDPEtLEELPPGEVGEIVVHGPQVF 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1501 KGYYKKEELTDSRFIDnpFEpGSKLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVAD 1580
Cdd:PRK08314   396 KGYWNRPEATAEAFIE--ID-GKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIAT 472
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1776025254 1581 MDnlaAYY--TAK-------HANASLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKI 1633
Cdd:PRK08314   473 PD---PRRgeTVKavvvlrpEARGKTTEEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKI 531
PRK07656 PRK07656
long-chain-fatty-acid--CoA ligase; Validated
28-556 2.73e-38

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236072 [Multi-domain]  Cd Length: 513  Bit Score: 153.14  E-value: 2.73e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254   28 PATIPEVLYRTAAELGDTKGIIYlqpDGTEVyqSYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNSQLLPAFWGCVLT 107
Cdd:PRK07656     4 WMTLPELLARAARRFGDKEAYVF---GDQRL--TYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKA 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  108 G--VVPaplaVPPTY--AESS-----SGTQKLKDAWTLL--DKPA--------------VITDRGMHQEMLDWAK--EQG 160
Cdd:PRK07656    79 GavVVP----LNTRYtaDEAAyilarGDAKALFVLGLFLgvDYSAttrlpalehvviceTEEDDPHTEKMKTFTDflAAG 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  161 LEGFRAIIVedllsaeadtdwhqsSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDHV 240
Cdd:PRK07656   155 DPAERAPEV---------------DPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAANPFFHV 219
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  241 GGigmlhLRDVYLGCQeinVSSETILME----PLKWLDWIDHYRASVTWAP----NFAFGLVtdfaeeiKDRKWDLSSMR 312
Cdd:PRK07656   220 FG-----YKAGVNAPL---MRGATILPLpvfdPDEVFRLIETERITVLPGPptmyNSLLQHP-------DRSAEDLSSLR 284
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  313 YMLNGGEAM-VAKVgRRILELLephglPADAIRPAWGMSEtSSGVIfshEFTRAGTSDDDHFVEIGSPIPGFSMRIVNDH 391
Cdd:PRK07656   285 LAVTGAASMpVALL-ERFESEL-----GVDIVLTGYGLSE-ASGVT---TFNRLDDDRKTVAGTIGTAIAGVENKIVNEL 354
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  392 NELVEEGEIGRFQVSGLSVTSGYYQRPDLNESVFTEDGWFETGDLGFL-RNGRLTITGRTKDAIIINGINYYSHAIESAV 470
Cdd:PRK07656   355 GEEVPVGEVGELLVRGPNVMKGYYDDPEATAAAIDADGWLHTGDLGRLdEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVL 434
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  471 EELSEIetsytAACAV------RLGqnstdQLAIFFVT---SAKLNDEqmsQLLRNIQSH-----VSQVIgvtpEYLlpv 536
Cdd:PRK07656   435 YEHPAV-----AEAAVigvpdeRLG-----EVGKAYVVlkpGAELTEE---ELIAYCREHlakykVPRSI----EFL--- 494
                          570       580
                   ....*....|....*....|
gi 1776025254  537 qkEEIPKTAIGKIQRTQLKT 556
Cdd:PRK07656   495 --DELPKNATGKVLKRALRE 512
elong_cond_enzymes cd00828
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ...
4588-4989 2.74e-38

"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, including beta-ketoacyl [ACP] synthase, type I and II and polyketide synthases.They are characterized by the utlization of acyl carrier protein (ACP) thioesters as primer substrates, as well as the nature of their active site residues.


Pssm-ID: 238424 [Multi-domain]  Cd Length: 407  Bit Score: 150.67  E-value: 2.74e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4588 EGIAVVGLSCRFP---GAETLESYWSLLSEGRSSIGPIPAErwgcKTPYYAGVIDGVSYFDPDffllhEEDVRA---MDP 4661
Cdd:cd00828      1 SRVVITGIGVVSPhgeGCDEVEEFWEALREGRSGIAPVARL----KSRFDRGVAGQIPTGDIP-----GWDAKRtgiVDR 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4662 QALLVLEECLKLLYHAGYT-PEEIKGKPVGVYIG-----GRSQH---KPDEDSLDHAKNPIVTVGQNYLAANLSQFFDV- 4731
Cdd:cd00828     72 TTLLALVATEEALADAGITdPYEVHPSEVGVVVGsgmggLRFLRrggKLDARAVNPYVSPKWMLSPNTVAGWVNILLLSs 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4732 RGPSVVVDTACSSALVGMNMAIQALRGGDIQSAIVGGVSLLSSDASH------RLFDRRGILSKHSSFhvFDERADGVVL 4805
Cdd:cd00828    152 HGPIKTPVGACATALEALDLAVEAIRSGKADIVVVGGVEDPLEEGLSgfanmgALSTAEEEPEEMSRP--FDETRDGFVE 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4806 GEGVGMVMLKTVKQALEDGDTIYAVVKAASVNNDGRTAGpATPNLEAQKEVMKDALFKSGKKPEDISYLEANGSGSIVTD 4885
Cdd:cd00828    230 AEGAGVLVLERAELALARGAPIYGRVAGTASTTDGAGRS-VPAGGKGIARAIRTALAKAGLSLDDLDVISAHGTSTPAND 308
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4886 LLELKAIQSVYRsGHSSPLSLGSIKPNIGHPLCAEGIASFIKVVLMLkERRFVPflsGEKEMAHFDQQKANITFSRALEK 4965
Cdd:cd00828    309 VAESRAIAEVAG-ALGAPLPVTAQKALFGHSKGAAGALQLIGALQSL-EHGLIP---PTANLDDVDPDVEHLSVVGLSRD 383
                          410       420
                   ....*....|....*....|....
gi 1776025254 4966 WTDSQPTAAINCFADGGTNVHVIV 4989
Cdd:cd00828    384 LNLKVRAALVNAFGFGGSNAALVL 407
PRK06087 PRK06087
medium-chain fatty-acid--CoA ligase;
1161-1655 4.77e-38

medium-chain fatty-acid--CoA ligase;


Pssm-ID: 180393 [Multi-domain]  Cd Length: 547  Bit Score: 153.36  E-value: 4.77e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1161 QQAKKTPDRAAVSYE-GQTLTYRELDERSTQLAIYLQAHGVGP-DRLAgIYVDRSLDMLVGLLAILKAGGAYVPLDPSYP 1238
Cdd:PRK06087    31 QTARAMPDKIAVVDNhGASYTYSALDHAASRLANWLLAKGIEPgDRVA-FQLPGWCEFTIIYLACLKVGAVSVPLLPSWR 109
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1239 AERLEYMLE--DSEVFITLTTSELVNTLSW-----NGVTT----ALLDQ-----DWDEIAQTASDRKVLTR--TVTPENL 1300
Cdd:PRK06087   110 EAELVWVLNkcQAKMFFAPTLFKQTRPVDLilplqNQLPQlqqiVGVDKlapatSSLSLSQIIADYEPLTTaiTTHGDEL 189
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1301 AYVIYTSGSTGKPKGVMIPHkalTNFLVS---MGETPGLTAEDKM-----LAVTTYCFDiaalELFLPLIKGAHCYICQT 1372
Cdd:PRK06087   190 AAVLFTSGTEGLPKGVMLTH---NNILASeraYCARLNLTWQDVFmmpapLGHATGFLH----GVTAPFLIGARSVLLDI 262
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1373 -EHTKDVEKLKRDIRTikpTVMQATPATWKML--------------FYsgweneenvkiLCGGEALPETLKRYFLDTGSE 1437
Cdd:PRK06087   263 fTPDACLALLEQQRCT---CMLGATPFIYDLLnllekqpadlsalrFF-----------LCGGTTIPKKVARECQQRGIK 328
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1438 AWNMFGPTETtIWSAVQRINDECSR--ATIGRPIANTQIYITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDsRFI 1515
Cdd:PRK06087   329 LLSVYGSTES-SPHAVVNLDDPLSRfmHTDGYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTA-RAL 406
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1516 DNpfepgSKLYRTGDMARWLPGGRIEYIGRiDNQVKIRGFR-IELGDIESRLSEHPGILECVVVADMDN-----LAAYYT 1589
Cdd:PRK06087   407 DE-----EGWYYSGDLCRMDEAGYIKITGR-KKDIIVRGGEnISSREVEDILLQHPKIHDACVVAMPDErlgerSCAYVV 480
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1776025254 1590 AKHANASLTAREL-RHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLKNiDLSgEQLKQRQTSP 1655
Cdd:PRK06087   481 LKAPHHSLTLEEVvAFFSRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRK-DIM-RRLTQDVCEE 545
MCS cd05941
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ...
61-555 4.91e-38

Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.


Pssm-ID: 341264 [Multi-domain]  Cd Length: 442  Bit Score: 150.90  E-value: 4.91e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254   61 SYRRLWDDGLRIVKGLRQSGLKAK-QSVILQLGDNSQLLPAFWGCVLTGVVPAPLAVPPTYAESSSgtqklkdawtlldk 139
Cdd:cd05941     13 TYADLVARAARLANRLLALGKDLRgDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEY-------------- 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  140 paVITDRGMhqemldwakeqglegfrAIIVedllsaeadtdwhqsspeDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGI 219
Cdd:cd05941     79 --VITDSEP-----------------SLVL------------------DPALILYTSGTTGRPKGVVLTHANLAANVRAL 121
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  220 IQMQGFTREDITFNWMPFDHVGGIGMLHLRDVYLGcqeinvsSETILM---EPLKWLDWIDHYRASVTWA-PNFAFGLV- 294
Cdd:cd05941    122 VDAWRWTEDDVLLHVLPLHHVHGLVNALLCPLFAG-------ASVEFLpkfDPKEVAISRLMPSITVFMGvPTIYTRLLq 194
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  295 ---TDFAEEIKDRKWDLSSMRYMLNGGEAM--------VAKVGRRILEllephglpadaiRpaWGMSETssGVIFS---H 360
Cdd:cd05941    195 yyeAHFTDPQFARAAAAERLRLMVSGSAALpvptleewEAITGHTLLE------------R--YGMTEI--GMALSnplD 258
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  361 EFTRAGTsdddhfveIGSPIPGFSMRIV-NDHNELVEEGEIGRFQVSGLSVTSGYYQRPDLNESVFTEDGWFETGDLGFL 439
Cdd:cd05941    259 GERRPGT--------VGMPLPGVQARIVdEETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGWFKTGDLGVV 330
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  440 R-NGRLTITGRTKDAII-INGINYYSHAIESAVEELSEIetsytAACAV------RLGQNstdqlaiffVTSA-KLNDEQ 510
Cdd:cd05941    331 DeDGYYWILGRSSVDIIkSGGYKVSALEIERVLLAHPGV-----SECAVigvpdpDWGER---------VVAVvVLRAGA 396
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*..
gi 1776025254  511 MSQLLRNIQSHVSQVIGVT--PEYLLPVqkEEIPKTAIGKIQRTQLK 555
Cdd:cd05941    397 AALSLEELKEWAKQRLAPYkrPRRLILV--DELPRNAMGKVNKKELR 441
LC_FACS_like cd05935
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ...
1179-1638 5.32e-38

Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.


Pssm-ID: 341258 [Multi-domain]  Cd Length: 430  Bit Score: 150.32  E-value: 5.32e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1179 LTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLEDSEVFITLTTS 1258
Cdd:cd05935      2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGS 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1259 ELvntlswngvttalldqdwdeiaqtasdrkvltrtvtpENLAYVIYTSGSTGKPKGVMIPHKALTNFLVSMGETPGLTA 1338
Cdd:cd05935     82 EL-------------------------------------DDLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTP 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1339 EDKMLAVTTYcFDIAALE--LFLPLIKGAHcYICQTEHtkDVEKLKRDIRTIKPTVMQATPaTWKMLFYSGWENEE---- 1412
Cdd:cd05935    125 SDVILACLPL-FHVTGFVgsLNTAVYVGGT-YVLMARW--DRETALELIEKYKVTFWTNIP-TMLVDLLATPEFKTrdls 199
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1413 NVKILCGGEA-LPETLKRYFLD-TGSEAWNMFGPTETTIWSAV---QRINDECsratIGRPIANTQIYITD-SQLAPVPA 1486
Cdd:cd05935    200 SLKVLTGGGApMPPAVAEKLLKlTGLRFVEGYGLTETMSQTHTnppLRPKLQC----LGIP*FGVDARVIDiETGRELPP 275
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1487 GVPGELCIAGDGVAKGYYKKEELTDSRFIDnpfEPGSKLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRL 1566
Cdd:cd05935    276 NEVGEIVVRGPQIFKGYWNRPEETEESFIE---IKGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKL 352
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1776025254 1567 SEHPGILECVVVADMDNLA-----AYYTAKHA-NASLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSL 1638
Cdd:cd05935    353 YKHPAI*EVCVISVPDERVgeevkAFIVLRPEyRGKVTEEDIIEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
PRK06839 PRK06839
o-succinylbenzoate--CoA ligase;
1160-1641 7.83e-38

o-succinylbenzoate--CoA ligase;


Pssm-ID: 168698 [Multi-domain]  Cd Length: 496  Bit Score: 151.55  E-value: 7.83e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1160 EQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAH-GVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYP 1238
Cdd:PRK06839     9 EKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLT 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1239 AERLEYMLEDSEVFITLTTSELVNTLSWNGVTTALLDQDWDEIAQTASDRKVLTRTVTPENLAYVI-YTSGSTGKPKGVM 1317
Cdd:PRK06839    89 ENELIFQLKDSGTTVLFVEKTFQNMALSMQKVSYVQRVISITSLKEIEDRKIDNFVEKNESASFIIcYTSGTTGKPKGAV 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1318 IPHK-----ALTNFLvsmgeTPGLTAEDKMLaVTTYCFDIAALELF-LP-LIKGAHCYICQtehTKDVEKLKRDIRTIKP 1390
Cdd:PRK06839   169 LTQEnmfwnALNNTF-----AIDLTMHDRSI-VLLPLFHIGGIGLFaFPtLFAGGVIIVPR---KFEPTKALSMIEKHKV 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1391 TVMQATPATWKMLFYS---GWENEENVKIL-CGGEALPETLKRYFLDTGSEAWNMFGPTETTiwSAVQRINDECSR---A 1463
Cdd:PRK06839   240 TVVMGVPTIHQALINCskfETTNLQSVRWFyNGGAPCPEELMREFIDRGFLFGQGFGMTETS--PTVFMLSEEDARrkvG 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1464 TIGRPIANTQIYITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPFepgsklyRTGDMARWLPGGRIEYI 1543
Cdd:PRK06839   318 SIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETIQDGWL-------CTGDLARVDEDGFVYIV 390
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1544 GRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMD----NLAAYYTAKHANASLTARELRHFVKNALPAYMVPSYF 1619
Cdd:PRK06839   391 GRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHvkwgEIPIAFIVKKSSSVLIEKDVIEHCRLFLAKYKIPKEI 470
                          490       500
                   ....*....|....*....|..
gi 1776025254 1620 IQLDHMPLTPNGKIDRNSLKNI 1641
Cdd:PRK06839   471 VFLKELPKNATGKIQKAQLVNQ 492
decarbox_cond_enzymes cd00825
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ...
4662-4989 1.38e-37

decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new carbon-carbon bond by a decarboxylating Claisen-like condensation reaction. Members are involved in the synthesis of fatty acids and polyketides, a diverse group of natural products. Both pathways are an iterative series of additions of small carbon units, usually acetate, to a nascent acyl group. There are 2 classes of decarboxylating condensing enzymes, which can be distinguished by sequence similarity, type of active site residues and type of primer units (acetyl CoA or acyl carrier protein (ACP) linked units).


Pssm-ID: 238421 [Multi-domain]  Cd Length: 332  Bit Score: 146.63  E-value: 1.38e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4662 QALLVLEECLKLLYHAGYTPEEIKGKPVGVYIG-----GRSQHKpDEDSLDHAkNPIVTVGQNY--LAANLSQFFDVRGP 4734
Cdd:cd00825     11 VSILGFEAAERAIADAGLSREYQKNPIVGVVVGtgggsPRFQVF-GADAMRAV-GPYVVTKAMFpgASGQIATPLGIHGP 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4735 SVVVDTACSSALVGMNMAIQALRGGDIQSAIVGGVSLLSsDASHRLFDRRGILSKHS-SFHVFDERADGVVLGEGVGMVM 4813
Cdd:cd00825     89 AYDVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEELA-APMDCEFDAMGALSTPEkASRTFDAAADGFVFGDGAGALV 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4814 LKTVKQALEDGDTIYAVVKAASVNNDGRTAGPATPNLEAQKEVMKDALFKSGKKPEDISYLEANGSGSIVTDLLELKAIQ 4893
Cdd:cd00825    168 VEELEHALARGAHIYAEIVGTAATIDGAGMGAFAPSAEGLARAAKEALAVAGLTVWDIDYLVAHGTGTPIGDVKELKLLR 247
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4894 SVYRsghSSPLSLGSIKPNIGHPLCAEGIASFIKVVLMLKerrfVPFLSGEKEMAHFDQQKANITfsralEKWTDSQP-T 4972
Cdd:cd00825    248 SEFG---DKSPAVSATKAMTGNLSSAAVVLAVDEAVLMLE----HGFIPPSIHIEELDEAGLNIV-----TETTPRELrT 315
                          330
                   ....*....|....*..
gi 1776025254 4973 AAINCFADGGTNVHVIV 4989
Cdd:cd00825    316 ALLNGFGLGGTNATLVL 332
PRK12476 PRK12476
putative fatty-acid--CoA ligase; Provisional
30-564 3.01e-37

putative fatty-acid--CoA ligase; Provisional


Pssm-ID: 171527 [Multi-domain]  Cd Length: 612  Bit Score: 152.20  E-value: 3.01e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254   30 TIPEVLYRTAAELGDTKGIIYLQ----PDGTEVYQSYRRLwddglrivkGLRQSGLKAKQSVILQLGDNSQLLP------ 99
Cdd:PRK12476    35 TLISLIERNIANVGDTVAYRYLDhshsAAGCAVELTWTQL---------GVRLRAVGARLQQVAGPGDRVAILApqgidy 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  100 --AFWGCVLTGVVPAPLAVP--PTYAESSSGTqkLKDAwtlldKPAVITDRGmhqemldwAKEQGLEGF----------R 165
Cdd:PRK12476   106 vaGFFAAIKAGTIAVPLFAPelPGHAERLDTA--LRDA-----EPTVVLTTT--------AAAEAVEGFlrnlprlrrpR 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  166 AIIV--------EDLLSAEADTDwhqsspeDLALLLLTSGSTGTPKAVMLNHRNIMS-MVKGIIQMQGFTREDITFNWMP 236
Cdd:PRK12476   171 VIAIdaipdsagESFVPVELDTD-------DVSHLQYTSGSTRPPVGVEITHRAVGTnLVQMILSIDLLDRNTHGVSWLP 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  237 FDHVGGIGMLHLRDVYLGcqeinvssETILMEPLKWLD----WID------HYRASVTWAPNFAF------GLVTDfAEE 300
Cdd:PRK12476   244 LYHDMGLSMIGFPAVYGG--------HSTLMSPTAFVRrpqrWIKalsegsRTGRVVTAAPNFAYewaaqrGLPAE-GDD 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  301 IkdrkwDLSSMrYMLNGGEAMVAKVGRRILELLEPHGLPADAIRPAWGMSETS------------SGVIFSHEFTRAGTS 368
Cdd:PRK12476   315 I-----DLSNV-VLIIGSEPVSIDAVTTFNKAFAPYGLPRTAFKPSYGIAEATlfvatiapdaepSVVYLDREQLGAGRA 388
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  369 ---DDDH-----FVEIGSPIPGFSMRIVNDH--NELvEEGEIGRFQVSGLSVTSGYYQRPDLNESVF------------- 425
Cdd:PRK12476   389 vrvAADApnavaHVSCGQVARSQWAVIVDPDtgAEL-PDGEVGEIWLHGDNIGRGYWGRPEETERTFgaklqsrlaegsh 467
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  426 ---TEDG--WFETGDLGFLRNGRLTITGRTKDAIIINGINYYSHAIESAVEELSEI-ETSYTAACAVRLGQNstDQLAIF 499
Cdd:PRK12476   468 adgAADDgtWLRTGDLGVYLDGELYITGRIADLIVIDGRNHYPQDIEATVAEASPMvRRGYVTAFTVPAEDN--ERLVIV 545
                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1776025254  500 FVTSAKLNDEQMSQLLRNIQSHVSQVIGVTPEYLLPVQKEEIPKTAIGKIQRTQLKTSFENGEFD 564
Cdd:PRK12476   546 AERAAGTSRADPAPAIDAIRAAVSRRHGLAVADVRLVPAGAIPRTTSGKLARRACRAQYLDGRLG 610
PRK07314 PRK07314
beta-ketoacyl-ACP synthase II;
3351-3779 4.16e-37

beta-ketoacyl-ACP synthase II;


Pssm-ID: 235987 [Multi-domain]  Cd Length: 411  Bit Score: 147.24  E-value: 4.16e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3351 PGAMDIDEFWKNLEEGKDSItevpkdrwdwrehygNPDTDVNKTDI--KWGGFIDGvaeFDPLFFgISPREADYVDPQQR 3428
Cdd:PRK07314    14 PLGNDVESTWKNLLAGKSGI---------------GPITHFDTSDLavKIAGEVKD---FNPDDY-MSRKEARRMDRFIQ 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3429 LLMTYVWKALEDAGCPPQSLSGTGTGIFIGTGNTGYKdlfhranlPIEGHAATGH----------MIPSVGPNRMSYFLN 3498
Cdd:PRK07314    75 YGIAAAKQAVEDAGLEITEENADRIGVIIGSGIGGLE--------TIEEQHITLLekgprrvspfFVPMAIINMAAGHVS 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3499 IH----GPSEPVETACSSSLVAIHRAVTAMQNGDCEMAIAGGVntilteEAHIS------YSKAGMLSKD-----GRCKT 3563
Cdd:PRK07314   147 IRygakGPNHSIVTACATGAHAIGDAARLIAYGDADVMVAGGA------EAAITplgiagFAAARALSTRnddpeRASRP 220
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3564 FSADANGYVRGEGVGMVMLKKLEDAERDGNHIYGVIRGTAENhgGRANTLTSPNPK----AQAdlLVRAYRQAGIDPSTV 3639
Cdd:PRK07314   221 FDKDRDGFVMGEGAGILVLEELEHAKARGAKIYAEVVGYGMT--GDAYHMTAPAPDgegaARA--MKLALKDAGINPEDI 296
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3640 TYIEAHGTGTELGDPIEINGLKAAFkelsnmrGESQPDVPdhrcgIGSVKSNIGHLELAAGISGLIKVLLQMKHKTLVKS 3719
Cdd:PRK07314   297 DYINAHGTSTPAGDKAETQAIKRVF-------GEHAYKVA-----VSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPT 364
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1776025254 3720 LHCETLNPylqltdspfyivqekqewksvtDCDGNELP---RRAGI-----SSFGIGGVNAHIVIEEY 3779
Cdd:PRK07314   365 INLDNPDE----------------------ECDLDYVPneaRERKIdyalsNSFGFGGTNASLVFKRY 410
PTZ00050 PTZ00050
3-oxoacyl-acyl carrier protein synthase; Provisional
3351-3772 7.62e-37

3-oxoacyl-acyl carrier protein synthase; Provisional


Pssm-ID: 240245 [Multi-domain]  Cd Length: 421  Bit Score: 146.76  E-value: 7.62e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3351 PGAMDIDEFWKNLEEGK---DSITEVPKDRWDWREHYGNPDTDVNKTDIKWGGFIDGVaEFDPLFFGISPREADYVdpqq 3427
Cdd:PTZ00050     4 PLGVGAESTWEALIAGKsgiRKLTEFPKFLPDCIPEQKALENLVAAMPCQIAAEVDQS-EFDPSDFAPTKRESRAT---- 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3428 RLLMTYVWKALEDAGCPPQS-LSGTGTGIFIGTGNTGYKDLFH-RANLPIEGHAATGHM-IPSVGPNRMSYFL----NIH 3500
Cdd:PTZ00050    79 HFAMAAAREALADAKLDILSeKDQERIGVNIGSGIGSLADLTDeMKTLYEKGHSRVSPYfIPKILGNMAAGLVaikhKLK 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3501 GPSEPVETACSSSLVAIHRAVTAMQNGDCEMAIAGGVNTILTEEAHISYSKAGMLSK------DGRCKTFSADANGYVRG 3574
Cdd:PTZ00050   159 GPSGSAVTACATGAHCIGEAFRWIKYGEADIMICGGTEASITPVSFAGFSRMRALCTkynddpQRASRPFDKDRAGFVMG 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3575 EGVGMVMLKKLEDAERDGNHIYGVIRGTAENhgGRANTLTSPNPKAQAdlLVRAYRQA-----GIDPSTVTYIEAHGTGT 3649
Cdd:PTZ00050   239 EGAGILVLEELEHALRRGAKIYAEIRGYGSS--SDAHHITAPHPDGRG--ARRCMENAlkdgaNININDVDYVNAHATST 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3650 ELGDPIEINGLKAAFKelsnmrgesqpDVPDHRCGIGSVKSNIGHLELAAGISGLIKVLLQMKHKTLVKSLHCETLNPYL 3729
Cdd:PTZ00050   315 PIGDKIELKAIKKVFG-----------DSGAPKLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINLENPDAEC 383
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....
gi 1776025254 3730 QLTdspfyIVQEKQEwKSVTDCDgnelprrAGIS-SFGIGGVNA 3772
Cdd:PTZ00050   384 DLN-----LVQGKTA-HPLQSID-------AVLStSFGFGGVNT 414
OSB_CoA_lg cd05912
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ...
1178-1639 9.30e-37

O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.


Pssm-ID: 341238 [Multi-domain]  Cd Length: 411  Bit Score: 146.34  E-value: 9.30e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1178 TLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLEDSEVfitltt 1257
Cdd:cd05912      1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDV------ 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1258 selvntlswngvttalldqDWDEIAQtasdrkvltrtvtpenlayVIYTSGSTGKPKGVMIPHKALTNFLVSMGETPGLT 1337
Cdd:cd05912     75 -------------------KLDDIAT-------------------IMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLT 116
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1338 AEDKMLAVTTYcFDIAALELFL-PLIKGAHCYIcqteHTK-DVEKLKRDIRTIKPTVMQATPA--TWKMLFYSGWENEEN 1413
Cdd:cd05912    117 EDDNWLCALPL-FHISGLSILMrSVIYGMTVYL----VDKfDAEQVLHLINSGKVTIISVVPTmlQRLLEILGEGYPNNL 191
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1414 VKILCGGEALPETLKRYFLDTGSEAWNMFGPTETTIWSAVQRINDECSR-ATIGRPIANTQIYITDsqlAPVPAGVPGEL 1492
Cdd:cd05912    192 RCILLGGGPAPKPLLEQCKEKGIPVYQSYGMTETCSQIVTLSPEDALNKiGSAGKPLFPVELKIED---DGQPPYEVGEI 268
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1493 CIAGDGVAKGYYKKEELTDSRFIDNPFEpgsklyrTGDmarwlpggrieyIGRIDNQ----VKIR--------GFRIELG 1560
Cdd:cd05912    269 LLKGPNVTKGYLNRPDATEESFENGWFK-------TGD------------IGYLDEEgflyVLDRrsdliisgGENIYPA 329
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1561 DIESRLSEHPGILECVVVADMDNL-----AAYYTakhANASLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDR 1635
Cdd:cd05912    330 EIEEVLLSHPAIKEAGVVGIPDDKwgqvpVAFVV---SERPISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLR 406

                   ....
gi 1776025254 1636 NSLK 1639
Cdd:cd05912    407 HELK 410
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
61-478 1.08e-36

amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.


Pssm-ID: 273779 [Multi-domain]  Cd Length: 409  Bit Score: 146.26  E-value: 1.08e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254   61 SYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNS-QLLPAFWGCVLTGVVPAPLAvpPTYAESSsgTQK-LKDAwtllD 138
Cdd:TIGR01733    1 TYRELDERANRLARHLRAAGGVGPGDRVAVLLERSaELVVAILAVLKAGAAYVPLD--PAYPAER--LAFiLEDA----G 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  139 KPAVITDRGMHQEMLDWAKEQGLEgfrAIIVEDLLSAEADTDWHQ--SSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMV 216
Cdd:TIGR01733   73 ARLLLTDSALASRLAGLVLPVILL---DPLELAALDDAPAPPPPDapSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLL 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  217 KGIIQMQGFTREDITFNWMP--FDhvggigmLHLRDVYL----GCQEINVSSETILMEPLKWLDWIDHYRASVTWAPNFA 290
Cdd:TIGR01733  150 AWLARRYGLDPDDRVLQFASlsFD-------ASVEEIFGallaGATLVVPPEDEERDDAALLAALIAEHPVTVLNLTPSL 222
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  291 FGLVTDFAEEikdrkwDLSSMRYMLNGGEAMVAKVGRRILELlephgLPADAIRPAWGMSETSsgvIFSHEFTRAGTSDD 370
Cdd:TIGR01733  223 LALLAAALPP------ALASLRLVILGGEALTPALVDRWRAR-----GPGARLINLYGPTETT---VWSTATLVDPDDAP 288
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  371 DHF-VEIGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGYYQRPDLNESVFTEDG--------WFETGDLGFLR- 440
Cdd:TIGR01733  289 RESpVPIGRPLANTRLYVLDDDLRPVPVGVVGELYIGGPGVARGYLNRPELTAERFVPDPfaggdgarLYRTGDLVRYLp 368
                          410       420       430
                   ....*....|....*....|....*....|....*...
gi 1776025254  441 NGRLTITGRTKDAIIINGinyysHAIesaveELSEIET 478
Cdd:TIGR01733  369 DGNLEFLGRIDDQVKIRG-----YRI-----ELGEIEA 396
PRK03640 PRK03640
o-succinylbenzoate--CoA ligase;
1161-1641 1.22e-36

o-succinylbenzoate--CoA ligase;


Pssm-ID: 235146 [Multi-domain]  Cd Length: 483  Bit Score: 147.80  E-value: 1.22e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1161 QQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAE 1240
Cdd:PRK03640    10 QRAFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSRE 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1241 RLEYMLEDSEVFITLTTSELVNTLswngvtTALLDQDWDEIAQTASDRKVLTRTVTPENLAYVIYTSGSTGKPKGVMIPH 1320
Cdd:PRK03640    90 ELLWQLDDAEVKCLITDDDFEAKL------IPGISVKFAELMNGPKEEAEIQEEFDLDEVATIMYTSGTTGKPKGVIQTY 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1321 KaltNFL---VSMGETPGLTAEDKMLAVTTYcFDIAALE-LFLPLIKGAHCYIcqteHTK-DVEKLKRDIRTIKPTVMQA 1395
Cdd:PRK03640   164 G---NHWwsaVGSALNLGLTEDDCWLAAVPI-FHISGLSiLMRSVIYGMRVVL----VEKfDAEKINKLLQTGGVTIISV 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1396 TPATWKMLF--YSGWENEENVK--ILCGGEALPETLKRyfldtgSEAWNM-----FGPTETTiwSAVQRINDECSRATI- 1465
Cdd:PRK03640   236 VSTMLQRLLerLGEGTYPSSFRcmLLGGGPAPKPLLEQ------CKEKGIpvyqsYGMTETA--SQIVTLSPEDALTKLg 307
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1466 --GRPIANTQIYITDsQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPFepgsklyRTGDmarwlpggrieyI 1543
Cdd:PRK03640   308 saGKPLFPCELKIEK-DGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQDGWF-------KTGD------------I 367
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1544 GRIDNQ----VKIR--------GFRIELGDIESRLSEHPGILECVVVADMDNL-----AAYYTAkhaNASLTARELRHFV 1606
Cdd:PRK03640   368 GYLDEEgflyVLDRrsdliisgGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKwgqvpVAFVVK---SGEVTEEELRHFC 444
                          490       500       510
                   ....*....|....*....|....*....|....*
gi 1776025254 1607 KNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLKNI 1641
Cdd:PRK03640   445 EEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQL 479
Acs COG0365
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
33-555 2.38e-36

Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];


Pssm-ID: 440134 [Multi-domain]  Cd Length: 565  Bit Score: 148.34  E-value: 2.38e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254   33 EVLYRTAAELGDTKGIIYLQPDGTEVYQSYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNSQLLPAFWGCVLTGVVPA 112
Cdd:COG0365     13 NCLDRHAEGRGDKVALIWEGEDGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHS 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  113 PLAV---PPTYAEsssgtqKLKDAwtlldKP-AVITDRG--------MHQEMLDWAKEQgLEGFRAIIV----EDLLSAE 176
Cdd:COG0365     93 PVFPgfgAEALAD------RIEDA-----EAkVLITADGglrggkviDLKEKVDEALEE-LPSLEHVIVvgrtGADVPME 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  177 ADTDWH-----QSSP--------EDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQM-QGFTREDITFN-----WMpF 237
Cdd:COG0365    161 GDLDWDellaaASAEfepeptdaDDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYvLDLKPGDVFWCtadigWA-T 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  238 DHVGGI--GMLHlrdvylGCqeinvsseTILM--------EPLKWLDWIDHYRASVTWAPNFAFGLVTDFAEEIKdRKWD 307
Cdd:COG0365    240 GHSYIVygPLLN------GA--------TVVLyegrpdfpDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPL-KKYD 304
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  308 LSSMRYMLNGGEAMVAKVGRRILELLephGLPadaIRPAWGMSETSSGVIFSHEFT--RAGtsdddhfvEIGSPIPGFSM 385
Cdd:COG0365    305 LSSLRLLGSAGEPLNPEVWEWWYEAV---GVP---IVDGWGQTETGGIFISNLPGLpvKPG--------SMGKPVPGYDV 370
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  386 RIVNDHNELVEEGEIGRFQVSG--LSVTSGYYQRPDLNESVF--TEDGWFETGDLGFL-RNGRLTITGRTKDAIIINGIN 460
Cdd:COG0365    371 AVVDEDGNPVPPGEEGELVIKGpwPGMFRGYWNDPERYRETYfgRFPGWYRTGDGARRdEDGYFWILGRSDDVINVSGHR 450
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  461 YYSHAIESAVEELSEIetsytAACAVrLGQNS--TDQLAIFFVT---SAKLNDEqmsqLLRNIQSHVSQVIGvtpEYLLP 535
Cdd:COG0365    451 IGTAEIESALVSHPAV-----AEAAV-VGVPDeiRGQVVKAFVVlkpGVEPSDE----LAKELQAHVREELG---PYAYP 517
                          570       580
                   ....*....|....*....|...
gi 1776025254  536 ---VQKEEIPKTAIGKIQRTQLK 555
Cdd:COG0365    518 reiEFVDELPKTRSGKIMRRLLR 540
FAAL cd05931
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...
1161-1579 3.54e-36

Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.


Pssm-ID: 341254 [Multi-domain]  Cd Length: 547  Bit Score: 147.77  E-value: 3.54e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1161 QQAKKTPDRAAVSY------EGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYvDRSLDMLVGLLAILKAGGAYVPL- 1233
Cdd:cd05931      1 RRAAARPDRPAYTFlddeggREETLTYAELDRRARAIAARLQAVGKPGDRVLLLA-PPGLDFVAAFLGCLYAGAIAVPLp 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1234 --DPSYPAERLEYMLEDSEVFITLTTSELVNTLSWNGVTTALLDQDW----DEIAQTASDRkVLTRTVTPENLAYVIYTS 1307
Cdd:cd05931     80 ppTPGRHAERLAAILADAGPRVVLTTAAALAAVRAFAASRPAAGTPRllvvDLLPDTSAAD-WPPPSPDPDDIAYLQYTS 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1308 GSTGKPKGVMIPHKALTNFLVSMGETPGLTAEDKMlaVT---TYcFD---IAAleLFLPLIKGAHCYICQTEHTkdVEKL 1381
Cdd:cd05931    159 GSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVV--VSwlpLY-HDmglIGG--LLTPLYSGGPSVLMSPAAF--LRRP 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1382 KRDIRTI---KPTVMQA------------TPATWKMLFYSGWENeenvkILCGGEAL-PETLKRyFLDTGSEA---WNMF 1442
Cdd:cd05931    232 LRWLRLIsryRATISAApnfaydlcvrrvRDEDLEGLDLSSWRV-----ALNGAEPVrPATLRR-FAEAFAPFgfrPEAF 305
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1443 GPT----ETTIWSAVQRINDE-------------------------CSRATIGRPIANTQIYITDSQ-LAPVPAGVPGEL 1492
Cdd:cd05931    306 RPSyglaEATLFVSGGPPGTGpvvlrvdrdalagravavaaddpaaRELVSCGRPLPDQEVRIVDPEtGRELPDGEVGEI 385
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1493 CIAGDGVAKGYYKKEELTDSRFIDNPFEPGSKLYRTGDMARwLPGGRIeYI-GRIDNQVKIRGFRIELGDIESRLSE-HP 1570
Cdd:cd05931    386 WVRGPSVASGYWGRPEATAETFGALAATDEGGWLRTGDLGF-LHDGEL-YItGRLKDLIIVRGRNHYPQDIEATAEEaHP 463

                   ....*....
gi 1776025254 1571 GILECVVVA 1579
Cdd:cd05931    464 ALRPGCVAA 472
PRK12583 PRK12583
acyl-CoA synthetase; Provisional
1154-1649 1.42e-35

acyl-CoA synthetase; Provisional


Pssm-ID: 237145 [Multi-domain]  Cd Length: 558  Bit Score: 146.07  E-value: 1.42e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1154 TFHELFEQQAKKTPDRAAVSY--EGQTLTYRELDERSTQLAIYLQAHGVGP-DRLaGIYVDRSLDMLVGLLAILKAGGAY 1230
Cdd:PRK12583    19 TIGDAFDATVARFPDREALVVrhQALRYTWRQLADAVDRLARGLLALGVQPgDRV-GIWAPNCAEWLLTQFATARIGAIL 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1231 VPLDPSYPAERLEYMLEDSEVFITLT-----TSELVNTLS------WNGVTTALLDQD--------------------WD 1279
Cdd:PRK12583    98 VNINPAYRASELEYALGQSGVRWVICadafkTSDYHAMLQellpglAEGQPGALACERlpelrgvvslapapppgflaWH 177
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1280 EI---AQTASDRKVLTRT--VTPENLAYVIYTSGSTGKPKGVMIPHKALTNFLVSMGETPGLTAEDKMLA-VTTY-CFDI 1352
Cdd:PRK12583   178 ELqarGETVSREALAERQasLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVpVPLYhCFGM 257
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1353 AaLELFLPLIKGAhCYICQTEHTKDVEKLkRDIRTIKPTVMQATPAtwkmLFYSGWENEE---------NVKILCGGEAL 1423
Cdd:PRK12583   258 V-LANLGCMTVGA-CLVYPNEAFDPLATL-QAVEEERCTALYGVPT----MFIAELDHPQrgnfdlsslRTGIMAGAPCP 330
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1424 PETLKRYFLDTG-SEAWNMFGPTETTIWSAVQRINDECSR--ATIGRPIANTQIYITDSQLAPVPAGVPGELCIAGDGVA 1500
Cdd:PRK12583   331 IEVMRRVMDEMHmAEVQIAYGMTETSPVSLQTTAADDLERrvETVGRTQPHLEVKVVDPDGATVPRGEIGELCTRGYSVM 410
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1501 KGYYKKEELTdSRFIDnpfepGSKLYRTGDMARWLPGGRIEYIGRIDNQVkIRGFR-IELGDIESRLSEHPGILECVVVA 1579
Cdd:PRK12583   411 KGYWNNPEAT-AESID-----EDGWMHTGDLATMDEQGYVRIVGRSKDMI-IRGGEnIYPREIEEFLFTHPAVADVQVFG 483
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1776025254 1580 DMDNlaaYYTAK-------HANASLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLKniDLSGEQLK 1649
Cdd:PRK12583   484 VPDE---KYGEEivawvrlHPGHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMR--EISIEELA 555
OSB_CoA_lg cd05912
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ...
172-556 1.43e-35

O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.


Pssm-ID: 341238 [Multi-domain]  Cd Length: 411  Bit Score: 142.87  E-value: 1.43e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  172 LLSAEADTDwhqsspeDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDitfNW---MPFDHVGGIGMLhL 248
Cdd:cd05912     69 LKDSDVKLD-------DIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLTEDD---NWlcaLPLFHISGLSIL-M 137
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  249 RDVYLGCQeinvsseTILME---PLKWLDWIDHYRASVtwapnfaFGLVTDFAEEIKDR--KWDLSSMRYMLNGGeamvA 323
Cdd:cd05912    138 RSVIYGMT-------VYLVDkfdAEQVLHLINSGKVTI-------ISVVPTMLQRLLEIlgEGYPNNLRCILLGG----G 199
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  324 KVGRRILELLEPHGLPadaIRPAWGMSETSSGVI-FSHEF--TRAGTSdddhfveiGSPIPGFSMRIVNDHNELVEEGEI 400
Cdd:cd05912    200 PAPKPLLEQCKEKGIP---VYQSYGMTETCSQIVtLSPEDalNKIGSA--------GKPLFPVELKIEDDGQPPYEVGEI 268
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  401 grfQVSGLSVTSGYYQRPDLNESVFtEDGWFETGDLGFLRN-GRLTITGRTKDAIIINGINYYSHAIESAVEELSEIets 479
Cdd:cd05912    269 ---LLKGPNVTKGYLNRPDATEESF-ENGWFKTGDIGYLDEeGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAI--- 341
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  480 ytAACAVrLGQnsTD----QLAI-FFVTSAKLNDEQMSQLLrniQSHVSQvigvtpeYLLPVQ---KEEIPKTAIGKIQR 551
Cdd:cd05912    342 --KEAGV-VGI--PDdkwgQVPVaFVVSERPISEEELIAYC---SEKLAK-------YKVPKKiyfVDELPRTASGKLLR 406

                   ....*
gi 1776025254  552 TQLKT 556
Cdd:cd05912    407 HELKQ 411
LC_FACL_like cd05914
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ...
184-551 1.57e-35

Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341240 [Multi-domain]  Cd Length: 463  Bit Score: 144.12  E-value: 1.57e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  184 SSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDHVGGIGMLHLRDVYLGCQEI---NV 260
Cdd:cd05914     86 SDEDDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVfldKI 165
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  261 SSETILME-----------PLKWLdwIDHYRASVTWAPNFAFGLVTDFAEEIKDRKwdLSSM-------------RYMLN 316
Cdd:cd05914    166 PSAKIIALafaqvtptlgvPVPLV--IEKIFKMDIIPKLTLKKFKFKLAKKINNRK--IRKLafkkvheafggniKEFVI 241
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  317 GGeamvAKVGRRILELLEPHGLPAdAIrpAWGMSETSSGVIFSH-EFTRAGTSdddhfveiGSPIPGFSMRIvNDHNELV 395
Cdd:cd05914    242 GG----AKINPDVEEFLRTIGFPY-TI--GYGMTETAPIISYSPpNRIRLGSA--------GKVIDGVEVRI-DSPDPAT 305
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  396 EEGEIgrfQVSGLSVTSGYYQRPDLNESVFTEDGWFETGDLG-FLRNGRLTITGRTKDAIII-NGINYYSHAIESAVEEL 473
Cdd:cd05914    306 GEGEI---IVRGPNVMKGYYKNPEATAEAFDKDGWFHTGDLGkIDAEGYLYIRGRKKEMIVLsSGKNIYPEEIEAKINNM 382
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  474 SEIETSYTAAcavrlgQNSTDQLAI-----FFVTSAKLNDEQMSQLLRNIQSHVSQvigVTPEYL----LPVQKEEIPKT 544
Cdd:cd05914    383 PFVLESLVVV------QEKKLVALAyidpdFLDVKALKQRNIIDAIKWEVRDKVNQ---KVPNYKkiskVKIVKEEFEKT 453

                   ....*..
gi 1776025254  545 AIGKIQR 551
Cdd:cd05914    454 PKGKIKR 460
PRK06188 PRK06188
acyl-CoA synthetase; Validated
1164-1639 3.25e-35

acyl-CoA synthetase; Validated


Pssm-ID: 235731 [Multi-domain]  Cd Length: 524  Bit Score: 144.36  E-value: 3.25e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1164 KKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGP-DRLAGIYVDRSlDMLVGLLAILKAGGAYVPLDPSYPAERL 1242
Cdd:PRK06188    23 KRYPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTgDAVALLSLNRP-EVLMAIGAAQLAGLRRTALHPLGSLDDH 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1243 EYMLEDSEVfitltTSELVNTLSWNGVTTALLDQ-----------------DWDEIAQTASDRKVLTRTVTPEnLAYVIY 1305
Cdd:PRK06188   102 AYVLEDAGI-----STLIVDPAPFVERALALLARvpslkhvltlgpvpdgvDLLAAAAKFGPAPLVAAALPPD-IAGLAY 175
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1306 TSGSTGKPKGVMIPHKALTNFLVSMGETPGLTAEDKMLAVTTYCFdiAALELFLP-LIKGAHCYICQTEHTKDVeklkrd 1384
Cdd:PRK06188   176 TGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSH--AGGAFFLPtLLRGGTVIVLAKFDPAEV------ 247
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1385 IRTIKPTVMQATPATWKMLF------------YSGWENeenvkILCGGEAL-PETLKryfldtgsEAWNMFGP------- 1444
Cdd:PRK06188   248 LRAIEEQRITATFLVPTMIYalldhpdlrtrdLSSLET-----VYYGASPMsPVRLA--------EAIERFGPifaqyyg 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1445 -TETTIWSAVQRINDECSR-----ATIGRPIANTQIYITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNp 1518
Cdd:PRK06188   315 qTEAPMVITYLRKRDHDPDdpkrlTSCGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAFRDG- 393
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1519 fepgskLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMDN-----LAAYYTAKhA 1593
Cdd:PRK06188   394 ------WLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEkwgeaVTAVVVLR-P 466
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*.
gi 1776025254 1594 NASLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLK 1639
Cdd:PRK06188   467 GAAVDAAELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALR 512
PRK07798 PRK07798
acyl-CoA synthetase; Validated
1154-1634 3.94e-35

acyl-CoA synthetase; Validated


Pssm-ID: 236100 [Multi-domain]  Cd Length: 533  Bit Score: 144.26  E-value: 3.94e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1154 TFHELFEQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPL 1233
Cdd:PRK07798     4 NIADLFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNV 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1234 DPSYPAERLEYMLEDSEVfitlttSELVNTLSWNGVTTALLDQ-----------------------DWDEI-AQTASDRK 1289
Cdd:PRK07798    84 NYRYVEDELRYLLDDSDA------VALVYEREFAPRVAEVLPRlpklrtlvvvedgsgndllpgavDYEDAlAAGSPERD 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1290 VLTRtvTPENLaYVIYTSGSTGKPKGVMIPHKALtnFLVSMGETPGLTAEDKM--LAVTTYCFDIAALELFL--PLIKGA 1365
Cdd:PRK07798   158 FGER--SPDDL-YLLYTGGTTGMPKGVMWRQEDI--FRVLLGGRDFATGEPIEdeEELAKRAAAGPGMRRFPapPLMHGA 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1366 ------------HCYICQTEHTKDVEKLKRDIRTIKPTVMQ------ATPATWKMLFYSGWENEENVKILCGGEALPETL 1427
Cdd:PRK07798   233 gqwaafaalfsgQTVVLLPDVRFDADEVWRTIEREKVNVITivgdamARPLLDALEARGPYDLSSLFAIASGGALFSPSV 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1428 KRYFLD-------TGSeawnmFGPTET----TIWSAVQRINDECSRATIGRPIAntqiyITDSQLAPVPAGVPGELCIAG 1496
Cdd:PRK07798   313 KEALLEllpnvvlTDS-----IGSSETgfggSGTVAKGAVHTGGPRFTIGPRTV-----VLDEDGNPVEPGSGEIGWIAR 382
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1497 DG-VAKGYYKKEELTDSRF--IDnpfepGSKLYRTGDMARWLPGGRIEYIGRiDNQV------KIrgFRIElgdIESRLS 1567
Cdd:PRK07798   383 RGhIPLGYYKDPEKTAETFptID-----GVRYAIPGDRARVEADGTITLLGR-GSVCintggeKV--FPEE---VEEALK 451
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1776025254 1568 EHPGILECVVVADMDN-----LAAyYTAKHANASLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKID 1634
Cdd:PRK07798   452 AHPDVADALVVGVPDErwgqeVVA-VVQLREGARPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGKAD 522
PRK13295 PRK13295
cyclohexanecarboxylate-CoA ligase; Reviewed
1154-1652 5.92e-35

cyclohexanecarboxylate-CoA ligase; Reviewed


Pssm-ID: 171961 [Multi-domain]  Cd Length: 547  Bit Score: 144.04  E-value: 5.92e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1154 TFHELFEQQAKKTPDRAAV------SYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAG 1227
Cdd:PRK13295    25 TINDDLDACVASCPDKTAVtavrlgTGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIG 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1228 GAYVPLDPSYPAERLEYMLE--DSEVFITLTT------SELVNTL--SW--------------NGVTTALLDQDWDeiaQ 1283
Cdd:PRK13295   105 AVLNPLMPIFRERELSFMLKhaESKVLVVPKTfrgfdhAAMARRLrpELpalrhvvvvggdgaDSFEALLITPAWE---Q 181
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1284 TASDRKVLTRTVT-PENLAYVIYTSGSTGKPKGVMIPHKALTNFLVSMGETPGLTAEDKMLAVTTycfdIAALELF---- 1358
Cdd:PRK13295   182 EPDAPAILARLRPgPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASP----MAHQTGFmygl 257
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1359 -LPLIKGAHCYIcqtEHTKDVEKLKRDIRTIKPT-VMQATPatwkmlFYSGW-----ENEENV----KILCGGEALPETL 1427
Cdd:PRK13295   258 mMPVMLGATAVL---QDIWDPARAAELIRTEGVTfTMASTP------FLTDLtravkESGRPVsslrTFLCAGAPIPGAL 328
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1428 KRyfldtgsEAWNMFGPTETTIW-----SAVQRIN----DECSRATIGRPIANTQIYITDSQLAPVPAGVPGELCIAGDG 1498
Cdd:PRK13295   329 VE-------RARAALGAKIVSAWgmtenGAVTLTKlddpDERASTTDGCPLPGVEVRVVDADGAPLPAGQIGRLQVRGCS 401
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1499 VAKGYYKKEELTDSRFiDNPFEpgsklyrTGDMARWLPGGRIEYIGRiDNQVKIRGFR-IELGDIESRLSEHPGILECVV 1577
Cdd:PRK13295   402 NFGGYLKRPQLNGTDA-DGWFD-------TGDLARIDADGYIRISGR-SKDVIIRGGEnIPVVEIEALLYRHPAIAQVAI 472
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1578 VADMD-----NLAAYYTAKhANASLTARELRHFVKN---ALPAYmvPSYFIQLDHMPLTPNGKIDRNSLKnidlsgEQLK 1649
Cdd:PRK13295   473 VAYPDerlgeRACAFVVPR-PGQSLDFEEMVEFLKAqkvAKQYI--PERLVVRDALPRTPSGKIQKFRLR------EMLR 543

                   ...
gi 1776025254 1650 QRQ 1652
Cdd:PRK13295   544 GED 546
FACL_like_2 cd05917
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
1305-1639 9.92e-35

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341241 [Multi-domain]  Cd Length: 349  Bit Score: 138.56  E-value: 9.92e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1305 YTSGSTGKPKGVMIPHKALTNFLVSMGETPGLTAEDKM-LAVTTY-CFDIAaLELFLPLIKGAHCYIcqTEHTKDVEKLK 1382
Cdd:cd05917      9 FTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLcIPVPLFhCFGSV-LGVLACLTHGATMVF--PSPSFDPLAVL 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1383 RDIRTIKPTVMQATPATWKMLFYSGWENEENVKILCGG-----EALPETLKRYFldtgsEAWNM------FGPTETTIWS 1451
Cdd:cd05917     86 EAIEKEKCTALHGVPTMFIAELEHPDFDKFDLSSLRTGimagaPCPPELMKRVI-----EVMNMkdvtiaYGMTETSPVS 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1452 AVQRINDECSR--ATIGRPIANTQIYITDSQLAPVPA-GVPGELCIAGDGVAKGYYKKEELTdSRFIDnpfepGSKLYRT 1528
Cdd:cd05917    161 TQTRTDDSIEKrvNTVGRIMPHTEAKIVDPEGGIVPPvGVPGELCIRGYSVMKGYWNDPEKT-AEAID-----GDGWLHT 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1529 GDMARWLPGGRIEYIGRIDNQVkIRGFR-IELGDIESRLSEHPGILECVVVADMD-----NLAAYyTAKHANASLTAREL 1602
Cdd:cd05917    235 GDLAVMDEDGYCRIVGRIKDMI-IRGGEnIYPREIEEFLHTHPKVSDVQVVGVPDerygeEVCAW-IRLKEGAELTEEDI 312
                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 1776025254 1603 RHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLK 1639
Cdd:cd05917    313 KAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
FACL_fum10p_like cd05926
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ...
53-555 1.07e-34

Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.


Pssm-ID: 341249 [Multi-domain]  Cd Length: 493  Bit Score: 142.07  E-value: 1.07e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254   53 PDGTEVYqSYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNSQLLPAFWGCVLTGVVPAPLAvpPTYAEsssgtQKLKD 132
Cdd:cd05926      9 PGSTPAL-TYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLN--PAYKK-----AEFEF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  133 AWTLLDKPAVITDRGMHQEMLDWAK-------EQGLEGFRAIIV---EDLLSAEADTDWHQSS----PEDLALLLLTSGS 198
Cdd:cd05926     81 YLADLGSKLVLTPKGELGPASRAASklglailELALDVGVLIRApsaESLSNLLADKKNAKSEgvplPDDLALILHTSGT 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  199 TGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDHVGG-IGMLhLRDVYLGcqeinvSSETILM--EPLKWLDW 275
Cdd:cd05926    161 TGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLVVMPLFHVHGlVASL-LSTLAAG------GSVVLPPrfSASTFWPD 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  276 IDHYRAsvTW---APNFAFGLVTDFAEEIKDRKwdlSSMRYMLNGGEAMVAKVGRRILE-----LLEphglpadairpAW 347
Cdd:cd05926    234 VRDYNA--TWytaVPTIHQILLNRPEPNPESPP---PKLRFIRSCSASLPPAVLEALEAtfgapVLE-----------AY 297
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  348 GMSETSSGViFSHEFtragtsdDDHFVEIGS-PIP-GFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGYYQRPDLNESVF 425
Cdd:cd05926    298 GMTEAAHQM-TSNPL-------PPGPRKPGSvGKPvGVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAA 369
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  426 TEDGWFETGDLGFL-RNGRLTITGRTKDAIIINGinyyshaiesavEELS--EIEtsytaacAVRLGQNSTDQLAIFFVT 502
Cdd:cd05926    370 FKDGWFRTGDLGYLdADGYLFLTGRIKELINRGG------------EKISplEVD-------GVLLSHPAVLEAVAFGVP 430
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1776025254  503 SAKLNDEQMSQLLRNIQSHVS--QVIGVTPEYLLP--VQKE-----EIPKTAIGKIQRTQLK 555
Cdd:cd05926    431 DEKYGEEVAAAVVLREGASVTeeELRAFCRKHLAAfkVPKKvyfvdELPKTATGKIQRRKVA 492
PRK05691 PRK05691
peptide synthase; Validated
184-990 2.31e-34

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 147.24  E-value: 2.31e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  184 SSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTRED-------ITFN------WMPFdhVGGIGMLhLR- 249
Cdd:PRK05691  2330 SLPQHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDcelhfysINFDaaserlLVPL--LCGARVV-LRa 2406
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  250 ----DVYLGCQEINVSSETILmeplkwldwidhyrasvTWAPNFAFGLVTDFAEEikdrkWDLSSMRYMLNGGEAMVAKV 325
Cdd:PRK05691  2407 qgqwGAEEICQLIREQQVSIL-----------------GFTPSYGSQLAQWLAGQ-----GEQLPVRMCITGGEALTGEH 2464
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  326 GRRILELLEPhglpaDAIRPAWGMSETssgVIF-----SHEFTRAGTSDddhfVEIGSPIPGFSMRIVNDHNELVEEGEI 400
Cdd:PRK05691  2465 LQRIRQAFAP-----QLFFNAYGPTET---VVMplaclAPEQLEEGAAS----VPIGRVVGARVAYILDADLALVPQGAT 2532
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  401 GRFQVSGLSVTSGYYQRPDLNESVFTEDGW-------FETGDLGFLR-NGRLTITGRTKDAIIINGINYyshaiesaveE 472
Cdd:PRK05691  2533 GELYVGGAGLAQGYHDRPGLTAERFVADPFaadggrlYRTGDLVRLRaDGLVEYVGRIDHQVKIRGFRI----------E 2602
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  473 LSEIETSYTAACAVR------LGQNSTDQLAIFFVTS-AKLNDEQMSQLLRNIQSHVSQVIgvtPEYLLPVQ---KEEIP 542
Cdd:PRK05691  2603 LGEIESRLLEHPAVReavvlaLDTPSGKQLAGYLVSAvAGQDDEAQAALREALKAHLKQQL---PDYMVPAHlilLDSLP 2679
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  543 KTAIGKIQRTQLKTSfengefdhllhkpnrmnDAVQDEEMQQADhvkrvREEIQEHLLTCLTEELHVSRdwVEPNANIQS 622
Cdd:PRK05691  2680 LTANGKLDRRALPAP-----------------DPELNRQAYQAP-----RSELEQQLAQIWREVLNVER--VGLGDNFFE 2735
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  623 LGVNSIKMMKLIrSIEKNYHIKLTAREIHQYPTIERLASYLSEHEDLSSSSADKKGTdtyktepersqatfQPLSEVQKg 702
Cdd:PRK05691  2736 LGGDSILSIQVV-SRARQLGIHFSPRDLFQHQTVQTLAAVATHSEAAQAEQGPLQGA--------------SGLTPIQH- 2799
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  703 lWTLQKMSPEKSAYHVPLCFKFSSGLHLETLQQAFGLVLNQHPILKHVIQEKDGVPILKNEPALSIEI-KTENISSMKES 781
Cdd:PRK05691  2800 -WFFDSPVPQPQHWNQALLLEPRQALDPALLEQALQALVEHHDALRLRFSQADGRWQAEYRAVTAQELlWQVTVADFAEC 2878
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  782 dipAFLRKKVKEPYVKENSPLVRVMSFSRSEQEHFLLVVIHHLIFDGVSSVTFIHSLFDTYQLLLKGQQPEIAVSPAIYH 861
Cdd:PRK05691  2879 ---AALFADAQRSLDLQQGPLLRALLVDGPQGQQRLLLAIHHLVVDGVSWRVLLEDLQALYRQLSAGAEPALPAKTSAFR 2955
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  862 DFAA-WEKnmLAGKDGVKHR-TYWQKQLSGtlPNLQLPKVSASSVSEFRE-DTYTRRLSSGFMNQVRMFA-KEHSVNVTT 937
Cdd:PRK05691  2956 DWAArLQA--YAGSESLREElGWWQAQLGG--PRAELPCDRPQGGNLNRHaQTVSVRLDAERTRQLLQQApAAYRTQVND 3031
                          810       820       830       840       850
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1776025254  938 VFLSCYMMLLGRYTGQKEQIVGMPAMVRpEERFDD-----AIGHFLNMLPIRseLNPA 990
Cdd:PRK05691  3032 LLLTALARVLCRWSGQPSVLVQLEGHGR-EALFDDidltrSVGWFTSAYPLR--LTPA 3086
OSB_MenE-like cd17630
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ...
188-558 3.72e-34

O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.


Pssm-ID: 341285 [Multi-domain]  Cd Length: 325  Bit Score: 136.31  E-value: 3.72e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  188 DLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDHVGGIGMLHlRDVYLGcqeinvsSETILM 267
Cdd:cd17630      1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLAILV-RSLLAG-------AELVLL 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  268 EPlKWLDWIDHYRASVTWA----PNFAFGLVTDFAEEikdrkwDLSSMRYMLNGGEAMVAKVGRRILELlephGLPadaI 343
Cdd:cd17630     73 ER-NQALAEDLAPPGVTHVslvpTQLQRLLDSGQGPA------ALKSLRAVLLGGAPIPPELLERAADR----GIP---L 138
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  344 RPAWGMSETSSGVIfsheftrAGTSDDDHFVEIGSPIPGFSMRIVNDhnelveegeiGRFQVSGLSVTSGYYQRPDLNEs 423
Cdd:cd17630    139 YTTYGMTETASQVA-------TKRPDGFGRGGVGVLLPGRELRIVED----------GEIWVGGASLAMGYLRGQLVPE- 200
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  424 vFTEDGWFETGDLGFLR-NGRLTITGRTKDAIIINGINYYSHAIESAVEELSEIEtsytAACAV-----RLGQnstdQLA 497
Cdd:cd17630    201 -FNEDGWFTTKDLGELHaDGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVR----DAFVVgvpdeELGQ----RPV 271
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1776025254  498 IFFVTSAKLNDEQMSQllrniqsHVSQVIGV--TPEYLLPVQkeEIPKTAIGKIQRTQLKTSF 558
Cdd:cd17630    272 AVIVGRGPADPAELRA-------WLKDKLARfkLPKRIYPVP--ELPRTGGGKVDRRALRAWL 325
PKS_DH smart00826
Dehydratase domain in polyketide synthase (PKS) enzymes;
2373-2539 4.16e-34

Dehydratase domain in polyketide synthase (PKS) enzymes;


Pssm-ID: 214837  Cd Length: 167  Bit Score: 130.81  E-value: 4.16e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  2373 HPLLHQNTSDFSEQkfSSVFTG-----DEFFLRDHVVRGKPVLPGVAYLEMAYAAinqaaGSEIGQDVRIRLNHTVWVQP 2447
Cdd:smart00826    1 HPLLGARVELADGG--GVVLTGrlslrTHPWLADHRVGGTVVLPGAAYVELALAA-----ADEVGGGAPARLEELTLEAP 73
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  2448 VVVDRHSA-QVDISLF-PEEDGKITFDIYSTQEDGDDPVIHSQGSAELASAAETPVADLTEISRRCGKGKMSPDQFYEEG 2525
Cdd:smart00826   74 LVLPEDGAvRVQVVVGaPDEDGRRTFTVYSRPDGDGPWTRHATGTLRPAAAAPAAPAADLAAWPPAGAEPVDVDDLYERL 153
                           170
                    ....*....|....
gi 1776025254  2526 RSRGMFHGPAFQGI 2539
Cdd:smart00826  154 AARGLEYGPAFQGL 167
PRK05677 PRK05677
long-chain-fatty-acid--CoA ligase; Validated
1151-1652 4.22e-34

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 168170 [Multi-domain]  Cd Length: 562  Bit Score: 141.44  E-value: 4.22e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1151 PYITFHELFEQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAH-GVGP-DRLAgIYVDRSLDMLVGLLAILKAGG 1228
Cdd:PRK05677    22 EYPNIQAVLKQSCQRFADKPAFSNLGKTLTYGELYKLSGAFAAWLQQHtDLKPgDRIA-VQLPNVLQYPVAVFGAMRAGL 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1229 AYVPLDPSYPAERLEYMLEDS--EVFITLTT--SELVNTLSWNGVTTALLDQDWD------------------------E 1280
Cdd:PRK05677   101 IVVNTNPLYTAREMEHQFNDSgaKALVCLANmaHLAEKVLPKTGVKHVIVTEVADmlpplkrllinavvkhvkkmvpayH 180
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1281 IAQTASDRKVLTR---------TVTPENLAYVIYTSGSTGKPKGVMIPHKaltNFLVSMGETPGLTAEDKMLAVTTYcfd 1351
Cdd:PRK05677   181 LPQAVKFNDALAKgagqpvteaNPQADDVAVLQYTGGTTGVAKGAMLTHR---NLVANMLQCRALMGSNLNEGCEIL--- 254
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1352 IAALELFLPLIKGAHCYICQT--EHT------KDVEKLKRDIRTIKPTVMQATpatwKMLFYSGWENEENVKI------- 1416
Cdd:PRK05677   255 IAPLPLYHIYAFTFHCMAMMLigNHNilisnpRDLPAMVKELGKWKFSGFVGL----NTLFVALCNNEAFRKLdfsalkl 330
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1417 -LCGGEALP-ETLKRYFLDTGSEAWNMFGPTETtiwSAVQRIN--DECSRATIGRPIANTQIYITDSQLAPVPAGVPGEL 1492
Cdd:PRK05677   331 tLSGGMALQlATAERWKEVTGCAICEGYGMTET---SPVVSVNpsQAIQVGTIGIPVPSTLCKVIDDDGNELPLGEVGEL 407
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1493 CIAGDGVAKGYYKKEELTDSRFIDNPFepgsklYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGI 1572
Cdd:PRK05677   408 CVKGPQVMKGYWQRPEATDEILDSDGW------LKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGV 481
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1573 LECVVVADMDNLAA----YYTAKHANASLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLKNidlsgEQL 1648
Cdd:PRK05677   482 LQCAAIGVPDEKSGeaikVFVVVKPGETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRRELRD-----EEL 556

                   ....
gi 1776025254 1649 KQRQ 1652
Cdd:PRK05677   557 KKAG 560
elong_cond_enzymes cd00828
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ...
1761-2181 5.70e-34

"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, including beta-ketoacyl [ACP] synthase, type I and II and polyketide synthases.They are characterized by the utlization of acyl carrier protein (ACP) thioesters as primer substrates, as well as the nature of their active site residues.


Pssm-ID: 238424 [Multi-domain]  Cd Length: 407  Bit Score: 137.96  E-value: 5.70e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1761 SVAIIGISCEFP---GAKNHDEFWENLRDGKESIAFFN--KEELQRFGiskeiaenADYVPaKASIEGKDrfdpsffqis 1835
Cdd:cd00828      2 RVVITGIGVVSPhgeGCDEVEEFWEALREGRSGIAPVArlKSRFDRGV--------AGQIP-TGDIPGWD---------- 62
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1836 PKDAEFMDPQLRMLLTHSWKAIEDAGYAAGQI---PQTSVFMSASNNSYRALLPSDTTESLETPDGYVSWVLAQSGTIP- 1911
Cdd:cd00828     63 AKRTGIVDRTTLLALVATEEALADAGITDPYEvhpSEVGVVVGSGMGGLRFLRRGGKLDARAVNPYVSPKWMLSPNTVAg 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1912 TMISHKLGLRGPSYFVHANCSSSLIGLHSAYKSLLSAESDYALVGGA-TLHTESNIGYVHQPGL---NFSSDGHIKAFDA 1987
Cdd:cd00828    143 WVNILLLSSHGPIKTPVGACATALEALDLAVEAIRSGKADIVVVGGVeDPLEEGLSGFANMGALstaEEEPEEMSRPFDE 222
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1988 SADGMIGGEGVAVVLLKKAADAVKDGDHIYALLRGIGVNNDGADKvgFYAPSVKGQADVVQQVMNQTKIHPESICYVEAH 2067
Cdd:cd00828    223 TRDGFVEAEGAGVLVLERAELALARGAPIYGRVAGTASTTDGAGR--SVPAGGKGIARAIRTALAKAGLSLDDLDVISAH 300
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2068 GTGTKLGDPIELAALTnvyRQYTNKTQFCGIGSVKTNIGHLDTAAGLAGCIKVVMSLYHQELAPSINYKEPNPNTDLASS 2147
Cdd:cd00828    301 GTSTPANDVAESRAIA---EVAGALGAPLPVTAQKALFGHSKGAAGALQLIGALQSLEHGLIPPTANLDDVDPDVEHLSV 377
                          410       420       430
                   ....*....|....*....|....*....|....*.
gi 1776025254 2148 PfyvvdqkkTLSREIQ-THRAALS-SFGLGGTNTHA 2181
Cdd:cd00828    378 V--------GLSRDLNlKVRAALVnAFGFGGSNAAL 405
CT_NRPS-like cd19542
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ...
695-1111 7.71e-34

Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike bacterial NRPS, which typically have specialized terminal thioesterase (TE) domains to cyclize peptide products, many fungal NRPSs employ a terminal condensation-like (CT) domain to produce macrocyclic peptidyl products (e.g. cyclosporine and echinocandin). Domains in this subfamily (which includes both terminal and non-terminal domains) typically have a non-canonical conserved [SN]HxxxDx(14)Y motif at their active site compared to the standard Condensation (C) domain active site motif (HHxxxD). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380464 [Multi-domain]  Cd Length: 401  Bit Score: 137.44  E-value: 7.71e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  695 PLSEVQKGLWTLQKMSPekSAYHVPLCFKFSSGLHLETLQQAFGLVLNQHPILKHVIQEKDGVP-----ILKNePALSIE 769
Cdd:cd19542      3 PCTPMQEGMLLSQLRSP--GLYFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFVESSAEGtflqvVLKS-LDPPIE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  770 IKTENissmkESDIPAFLRKKVKEPyVKENSPLVRVMSFSRSEQEHFLLVVIHHLIFDGVSsvtfIHSLFDTYQLLLKGQ 849
Cdd:cd19542     80 EVETD-----EDSLDALTRDLLDDP-TLFGQPPHRLTLLETSSGEVYLVLRISHALYDGVS----LPIILRDLAAAYNGQ 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  850 QPEIAVSpaiYHDFAAweknMLAGKDGVKHRTYWQKQLSGTLPNLQlPkvsassvSEFREDTYTRRLSSGFMNQ--VRMF 927
Cdd:cd19542    150 LLPPAPP---FSDYIS----YLQSQSQEESLQYWRKYLQGASPCAF-P-------SLSPKRPAERSLSSTRRSLakLEAF 214
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  928 AKEHSVNVTTVFLSCYMMLLGRYTGQKEQIVGMpaMVR----PEERFDDAIGHFLNMLPIRSELNPADTFSSFISKLQLT 1003
Cdd:cd19542    215 CASLGVTLASLFQAAWALVLARYTGSRDVVFGY--VVSgrdlPVPGIDDIVGPCINTLPVRVKLDPDWTVLDLLRQLQQQ 292
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1004 ILDGLDHAAYPFPKMVRDLNIPRSQagsPVFQTAFFYQNFLQSGSYQSLLSRYadfFSVDYVEYIHqegEYELVFELWET 1083
Cdd:cd19542    293 YLRSLPHQHLSLREIQRALGLWPSG---TLFNTLVSYQNFEASPESELSGSSV---FELSAAEDPT---EYPVAVEVEPS 363
                          410       420       430
                   ....*....|....*....|....*....|.
gi 1776025254 1084 EEKMELNIKYNTGLFD---AASISAMFDHFV 1111
Cdd:cd19542    364 GDSLKVSLAYSTSVLSeeqAEELLEQFDDIL 394
PTZ00050 PTZ00050
3-oxoacyl-acyl carrier protein synthase; Provisional
1778-2186 1.31e-33

3-oxoacyl-acyl carrier protein synthase; Provisional


Pssm-ID: 240245 [Multi-domain]  Cd Length: 421  Bit Score: 137.13  E-value: 1.31e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1778 DEFWENLRDGKESIAFFNKEELQRFGISKEIAENADYVPA-----KASIEGKDrFDPSFFQISPKDaefmDPQLRMLLTH 1852
Cdd:PTZ00050    10 ESTWEALIAGKSGIRKLTEFPKFLPDCIPEQKALENLVAAmpcqiAAEVDQSE-FDPSDFAPTKRE----SRATHFAMAA 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1853 SWKAIEDAG--YAAGQIP-QTSVFMSASNNSYRALLpsDTTESLETpDGY--VSWVLaqsgtIPTMISH--------KLG 1919
Cdd:PTZ00050    85 AREALADAKldILSEKDQeRIGVNIGSGIGSLADLT--DEMKTLYE-KGHsrVSPYF-----IPKILGNmaaglvaiKHK 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1920 LRGPSYFVHANC--SSSLIGlhSAYKSLLSAESDYALVGG--ATLHTESNIGYVHQPGL----NFSSDGHIKAFDASADG 1991
Cdd:PTZ00050   157 LKGPSGSAVTACatGAHCIG--EAFRWIKYGEADIMICGGteASITPVSFAGFSRMRALctkyNDDPQRASRPFDKDRAG 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1992 MIGGEGVAVVLLKKAADAVKDGDHIYALLRGIGVNNDGADkVGFYAPSVKGQADVVQQVMNQT-KIHPESICYVEAHGTG 2070
Cdd:PTZ00050   235 FVMGEGAGILVLEELEHALRRGAKIYAEIRGYGSSSDAHH-ITAPHPDGRGARRCMENALKDGaNININDVDYVNAHATS 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2071 TKLGDPIELAALTNVYRQYTNKTqfCGIGSVKTNIGHLDTAAGLAGCIKVVMSLYHQELAPSINYKEPNPNTDLasspfy 2150
Cdd:PTZ00050   314 TPIGDKIELKAIKKVFGDSGAPK--LYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINLENPDAECDL------ 385
                          410       420       430
                   ....*....|....*....|....*....|....*..
gi 1776025254 2151 vVDQKKTLSREIQTHRAALS-SFGLGGTNTHAIFEQF 2186
Cdd:PTZ00050   386 -NLVQGKTAHPLQSIDAVLStSFGFGGVNTALLFTKY 421
FACL_like_6 cd05922
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
75-555 1.46e-33

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341246 [Multi-domain]  Cd Length: 457  Bit Score: 137.96  E-value: 1.46e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254   75 GLRQSGLKAKQSVILQLGDNSQLLPAFWGCVLTGVVPAPLAVP--PTYAESSsgtqkLKDAWTLLDKPAVITDRGMHQEM 152
Cdd:cd05922      9 ALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRLGLVFVPlnPTLKESV-----LRYLVADAGGRIVLADAGAADRL 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  153 LDWAKEQGLEGFrAIIVEDLLSAEADTDWHQSSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITF 232
Cdd:cd05922     84 RDALPASPDPGT-VLDADGIRAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDRAL 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  233 NWMPFDHVGGIGMLHlrdVYLGCQEINVSSETILMEPLKWLDWIDHYRASVTWAPNFAfglvtdfaeEIKDR-KWD---L 308
Cdd:cd05922    163 TVLPLSYDYGLSVLN---THLLRGATLVLTNDGVLDDAFWEDLREHGATGLAGVPSTY---------AMLTRlGFDpakL 230
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  309 SSMRYMLNGGEAMVAKVGRRILELlephgLPADAIRPAWGMSETSSGVIF--SHEFTRAGTSdddhfveIGSPIPGFSMR 386
Cdd:cd05922    231 PSLRYLTQAGGRLPQETIARLREL-----LPGAQVYVMYGQTEATRRMTYlpPERILEKPGS-------IGLAIPGGEFE 298
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  387 IVNDHNELVEEGEIGRFQVSGLSVTSGYYQRPDLNESVFTEDGWFETGDLGFLR-NGRLTITGRTKDAIIINGINYYSHA 465
Cdd:cd05922    299 ILDDDGTPTPPGEPGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDeDGFLFIVGRRDRMIKLFGNRISPTE 378
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  466 IESAVEELSEIETsytaACAVRLGQNSTDQLAIFFVTSAKLNDEQMSQLLRNiqshvsqvigVTPEYLLPVQK---EEIP 542
Cdd:cd05922    379 IEAAARSIGLIIE----AAAVGLPDPLGEKLALFVTAPDKIDPKDVLRSLAE----------RLPPYKVPATVrvvDELP 444
                          490
                   ....*....|...
gi 1776025254  543 KTAIGKIQRTQLK 555
Cdd:cd05922    445 LTASGKVDYAALR 457
23DHB-AMP_lg cd05920
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ...
27-554 2.09e-33

2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.


Pssm-ID: 341244 [Multi-domain]  Cd Length: 482  Bit Score: 137.84  E-value: 2.09e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254   27 QPATIPEVLYRTAAELGDTKGIIylqpDGtEVYQSYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNSQLLPAFWGCVL 106
Cdd:cd05920     13 QDEPLGDLLARSAARHPDRIAVV----DG-DRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLR 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  107 TGVVPApLAVPPTYAESSSGTQKLKDAwtlldkPAVITDRgmhqemldwakEQGLEGFRAIIVEdLLSAEADTdwhqssp 186
Cdd:cd05920     88 LGAVPV-LALPSHRRSELSAFCAHAEA------VAYIVPD-----------RHAGFDHRALARE-LAESIPEV------- 141
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  187 edlALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDH------VGGIGMLHLRdvylGCQEINV 260
Cdd:cd05920    142 ---ALFLLSGGTTGTPKLIPRTHNDYAYNVRASAEVCGLDQDTVYLAVLPAAHnfplacPGVLGTLLAG----GRVVLAP 214
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  261 SSEtilmePLKWLDWIDHYRASVTWA-PnfafGLVTDFAEEIKDRKWDLSSMRYMLNGGEAMVAKVGRRILELLEPhglp 339
Cdd:cd05920    215 DPS-----PDAAFPLIEREGVTVTALvP----ALVSLWLDAAASRRADLSSLRLLQVGGARLSPALARRVPPVLGC---- 281
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  340 adAIRPAWGMSEtssGVIfshEFTRAGTSDDDHFVEIGSPI-PGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGYYQRP 418
Cdd:cd05920    282 --TLQQVFGMAE---GLL---NYTRLDDPDEVIIHTQGRPMsPDDEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAP 353
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  419 DLNESVFTEDGWFETGDLGFL-RNGRLTITGRTKDAIIINGINYYSHAIESAVEELSEIEtsYTAACAV---RLGQNSTd 494
Cdd:cd05920    354 EHNARAFTPDGFYRTGDLVRRtPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVH--DAAVVAMpdeLLGERSC- 430
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  495 qlAIFFVTSAKLNDEQMSQLLRNIQSHVSQVigvtPEYLLPVqkEEIPKTAIGKIQRTQL 554
Cdd:cd05920    431 --AFVVLRDPPPSAAQLRRFLRERGLAAYKL----PDRIEFV--DSLPLTAVGKIDKKAL 482
LC_FACL_like cd05914
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ...
1172-1635 3.82e-33

Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341240 [Multi-domain]  Cd Length: 463  Bit Score: 136.80  E-value: 3.82e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1172 VSYEGQTLTYRELDERSTQLAIYLQAHGVGP-DRLAgIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLEDSE 1250
Cdd:cd05914      1 LYYGGEPLTYKDLADNIAKFALLLKINGVGTgDRVA-LMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1251 VFITLTTSElvntlswngvttalldqdwdeiaqtasdrkvltrtvtpENLAYVIYTSGSTGKPKGVMIPHKALTNFLVSM 1330
Cdd:cd05914     80 AKAIFVSDE--------------------------------------DDVALINYTSGTTGNSKGVMLTYRNIVSNVDGV 121
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1331 GETPGLTAEDKMLAVTTY------CFDiaaleLFLPLIKGAHCYICQTEHTKDVEKLKRDirTIKPTVMQATP------- 1397
Cdd:cd05914    122 KEVVLLGKGDKILSILPLhhiyplTFT-----LLLPLLNGAHVVFLDKIPSAKIIALAFA--QVTPTLGVPVPlviekif 194
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1398 ----------ATWKMLFYSGWENEE---------------NVKILC-GGEALPETLKRYFLDTGSEAWNMFGPTETTIWS 1451
Cdd:cd05914    195 kmdiipkltlKKFKFKLAKKINNRKirklafkkvheafggNIKEFViGGAKINPDVEEFLRTIGFPYTIGYGMTETAPII 274
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1452 AVQRINDECSrATIGRPIANTQIYITDsqlaPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPFepgsklYRTGDM 1531
Cdd:cd05914    275 SYSPPNRIRL-GSAGKVIDGVEVRIDS----PDPATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDGW------FHTGDL 343
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1532 ARWLPGGRIEYIGRIDNQ-VKIRGFRIELGDIESRLSEHPGILECVVVADMDNLAA----YYTAKHANASLTAR------ 1600
Cdd:cd05914    344 GKIDAEGYLYIRGRKKEMiVLSSGKNIYPEEIEAKINNMPFVLESLVVVQEKKLVAlayiDPDFLDVKALKQRNiidaik 423
                          490       500       510
                   ....*....|....*....|....*....|....*..
gi 1776025254 1601 -ELRHFVKNALPAY-MVPSYFIQLDHMPLTPNGKIDR 1635
Cdd:cd05914    424 wEVRDKVNQKVPNYkKISKVKIVKEEFEKTPKGKIKR 460
EntE COG1021
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ...
1154-1639 4.70e-33

EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440644 [Multi-domain]  Cd Length: 533  Bit Score: 137.97  E-value: 4.70e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1154 TFHELFEQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDrlagiyvDR-------SLDMLVGLLAILKA 1226
Cdd:COG1021     26 TLGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPG-------DRvvvqlpnVAEFVIVFFALFRA 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1227 GGayVPLDpSYPAER---LEYMLEDSE--VFITLTTS------ELVNTL--SWNGVTTALLD------QDWDEIAQTASD 1287
Cdd:COG1021     99 GA--IPVF-ALPAHRraeISHFAEQSEavAYIIPDRHrgfdyrALARELqaEVPSLRHVLVVgdagefTSLDALLAAPAD 175
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1288 RKVltRTVTPENLAYVIYTSGSTGKPKgvMIP--HKA-LTNFLVSmGETPGLTAEDKMLAV----------------TTY 1348
Cdd:COG1021    176 LSE--PRPDPDDVAFFQLSGGTTGLPK--LIPrtHDDyLYSVRAS-AEICGLDADTVYLAAlpaahnfplsspgvlgVLY 250
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1349 -------CFDIAALELFlPLIkgahcyicqtehtkdvEKLKRDIRTIKPTV----MQATPATWKMLfySGWEneenvKIL 1417
Cdd:COG1021    251 aggtvvlAPDPSPDTAF-PLI----------------ERERVTVTALVPPLallwLDAAERSRYDL--SSLR-----VLQ 306
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1418 CGGEALPETLKRYFLDT-GSEAWNMFGPTE----TTiwsavqRIND--ECSRATIGRPI-ANTQIYITDSQLAPVPAGVP 1489
Cdd:COG1021    307 VGGAKLSPELARRVRPAlGCTLQQVFGMAEglvnYT------RLDDpeEVILTTQGRPIsPDDEVRIVDEDGNPVPPGEV 380
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1490 GELCIAGDGVAKGYYKKEELTDSRFIDNPFepgsklYRTGDMARWLPGGRIEYIGRIDNQVkIRGfrielG------DIE 1563
Cdd:COG1021    381 GELLTRGPYTIRGYYRAPEHNARAFTPDGF------YRTGDLVRRTPDGYLVVEGRAKDQI-NRG-----GekiaaeEVE 448
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1564 SRLSEHPGILECVVVADMDNL-----AAYYTAKhaNASLTARELRHFVKNA-LPAYMVPSYFIQLDHMPLTPNGKIDRNS 1637
Cdd:COG1021    449 NLLLAHPAVHDAAVVAMPDEYlgersCAFVVPR--GEPLTLAELRRFLRERgLAAFKLPDRLEFVDALPLTAVGKIDKKA 526

                   ..
gi 1776025254 1638 LK 1639
Cdd:COG1021    527 LR 528
PRK05605 PRK05605
long-chain-fatty-acid--CoA ligase; Validated
1142-1647 9.06e-33

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235531 [Multi-domain]  Cd Length: 573  Bit Score: 137.82  E-value: 9.06e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1142 TWNATGKTYPYITFHELFEQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGP-DRLAgIYVDRSLDMLVGL 1220
Cdd:PRK05605    21 PWTPHDLDYGDTTLVDLYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPgDRVA-IVLPNCPQHIVAF 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1221 LAILKAGGAYVPLDPSYPAERLEYMLED--SEVFITL-----TTSELVNTLSWNGV-----TTA--LLDQ---------- 1276
Cdd:PRK05605   100 YAVLRLGAVVVEHNPLYTAHELEHPFEDhgARVAIVWdkvapTVERLRRTTPLETIvsvnmIAAmpLLQRlalrlpipal 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1277 ---------------DWDEIAQTA---SDRKVLTRTVTPENLAYVIYTSGSTGKPKGVMIPHKAL-TNflVSMGET--PG 1335
Cdd:PRK05605   180 rkaraaltgpapgtvPWETLVDAAiggDGSDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLfAN--AAQGKAwvPG 257
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1336 LTAED-KMLAVTTYcFDIAALEL---FLPLIKGAHCYIcqteHTKDVEKLKRDIRTIKPTVMQATPATWKMLFYSGweNE 1411
Cdd:PRK05605   258 LGDGPeRVLAALPM-FHAYGLTLcltLAVSIGGELVLL----PAPDIDLILDAMKKHPPTWLPGVPPLYEKIAEAA--EE 330
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1412 ENVKI------LCGGEALP-ETLKRYFLDTGSEAWNMFGPTETTIWSAVQRINDECSRATIGRPIANTQIYITDsqlaP- 1483
Cdd:PRK05605   331 RGVDLsgvrnaFSGAMALPvSTVELWEKLTGGLLVEGYGLTETSPIIVGNPMSDDRRPGYVGVPFPDTEVRIVD----Pe 406
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1484 -----VPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNpfepgskLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIE 1558
Cdd:PRK05605   407 dpdetMPDGEEGELLVRGPQVFKGYWNRPEETAKSFLDG-------WFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVY 479
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1559 LGDIESRLSEHPGILECVVV------ADMDNLAAYYTAKHanASLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGK 1632
Cdd:PRK05605   480 PAEVEEVLREHPGVEDAAVVglpredGSEEVVAAVVLEPG--AALDPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGK 557
                          570
                   ....*....|....*
gi 1776025254 1633 IDRNSLKNIDLSGEQ 1647
Cdd:PRK05605   558 VRRREVREELLEKLG 572
DCL_NRPS-like cd19536
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ...
695-1110 1.82e-32

DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal fungal CT domains and Dual Epimerization/Condensation (E/C) domains; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type [D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L))], which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380459 [Multi-domain]  Cd Length: 419  Bit Score: 133.73  E-value: 1.82e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  695 PLSEVQKGLWTLQKMSPEKSAYHVPLCFKFSSGLHLETLQQAFGLVLNQHPILKHV-IQEKDGVPILKNEPALSIEIKTE 773
Cdd:cd19536      3 PLSSLQEGMLFHSLLNPGGSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSfIEDGLGQPVQVVHRQAQVPVTEL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  774 NISSMKESDIPafLRKKVKEPYVKE----NSPLVRVMSFSRSEQEHFLLVV-IHHLIFDGVSsvtfIHSLFDTYQLLLKG 848
Cdd:cd19536     83 DLTPLEEQLDP--LRAYKEETKIRRfdlgRAPLVRAALVRKDERERFLLVIsDHHSILDGWS----LYLLVKEILAVYNQ 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  849 Q--QPEIAVSPAI-YHDFAAWEKnmlAGKDGVKHRTYWQKQLSG-TLPNlqLPKVSASSVSEFREDTYTrRLSSGFMNQV 924
Cdd:cd19536    157 LleYKPLSLPPAQpYRDFVAHER---ASIQQAASERYWREYLAGaTLAT--LPALSEAVGGGPEQDSEL-LVSVPLPVRS 230
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  925 RMFAKEHSVNVTTVFLSCYMMLLGRYTGQKEQIVGMPAMVRPEErFDDA---IGHFLNMLPIRSELnPADTFSSFISKLQ 1001
Cdd:cd19536    231 RSLAKRSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEE-TTGAerlLGLFLNTLPLRVTL-SEETVEDLLKRAQ 308
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1002 LTILDGLDHAAYPFPkmvrdlNIPRSQAGSPVFQTAFFYQNFLQsgsYQSLLSRYADFFSVDYVEYIHQEGEYELVFELW 1081
Cdd:cd19536    309 EQELESLSHEQVPLA------DIQRCSEGEPLFDSIVNFRHFDL---DFGLPEWGSDEGMRRGLLFSEFKSNYDVNLSVL 379
                          410       420
                   ....*....|....*....|....*....
gi 1776025254 1082 ETEEKMELNIKYNTGLFDAASISAMFDHF 1110
Cdd:cd19536    380 PKQDRLELKLAYNSQVLDEEQAQRLAAYY 408
PRK06333 PRK06333
beta-ketoacyl-ACP synthase;
3351-3781 1.94e-32

beta-ketoacyl-ACP synthase;


Pssm-ID: 235781 [Multi-domain]  Cd Length: 424  Bit Score: 133.97  E-value: 1.94e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3351 PGAMDIDEFWKNLEEGKDSITEVPKDrwdwrehygnpdtDVNKTDIKWGGFI-----DGVAEFDPLFFgISPREADYVDP 3425
Cdd:PRK06333    16 PLGCGVETFWQRLLAGQSGIRTLTDF-------------PVGDLATKIGGQVpdlaeDAEAGFDPDRY-LDPKDQRKMDR 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3426 QQRLLMTYVWKALEDAGCPPQSLSGT-GTGIFIGTGNTGykdlfhranLPIEGHAATghMIPSVGPNRMS-----YFL-N 3498
Cdd:PRK06333    82 FILFAMAAAKEALAQAGWDPDTLEDReRTATIIGSGVGG---------FPAIAEAVR--TLDSRGPRRLSpftipSFLtN 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3499 I-----------HGPSEPVETACSSSLVAIHRAVTAMQNGDCEMAIAGGvntilTEEAHISYSKAGM-----LSKDGR-- 3560
Cdd:PRK06333   151 MaaghvsirygfKGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGG-----TEAAIDRVSLAGFaaaraLSTRFNda 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3561 ----CKTFSADANGYVRGEGVGMVMLKKLEDAERDGNHIYGVIRG---TAEnhggrANTLTSPNP--KAQADLLVRAYRQ 3631
Cdd:PRK06333   226 peqaSRPFDRDRDGFVMGEGAGILVIETLEHALARGAPPLAELVGygtSAD-----AYHMTAGPEdgEGARRAMLIALRQ 300
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3632 AGIDPSTVTYIEAHGTGTELGDPIEINGLKAAFKELSNMRgesqpdvpdhrcgIGSVKSNIGHLELAAGISGLIKVLLQM 3711
Cdd:PRK06333   301 AGIPPEEVQHLNAHATSTPVGDLGEVAAIKKVFGHVSGLA-------------VSSTKSATGHLLGAAGGVEAIFTILAL 367
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1776025254 3712 KHKTLVKSLHCETLNPYLQLTDspfYIVQEKQEWksvtdcdgnelPRRAGIS-SFGIGGVNAHIVIEEYMP 3781
Cdd:PRK06333   368 RDQIAPPTLNLENPDPAAEGLD---VVANKARPM-----------DMDYALSnGFGFGGVNASILFRRWEP 424
AAS_C cd05909
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ...
1175-1639 2.40e-32

C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.


Pssm-ID: 341235 [Multi-domain]  Cd Length: 490  Bit Score: 135.15  E-value: 2.40e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1175 EGQTLTYRELDERSTQLAIYLQAhGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLEDSEVFIT 1254
Cdd:cd05909      4 LGTSLTYRKLLTGAIALARKLAK-MTKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTV 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1255 LTTSELVNTLSWNGVTTALLDQDW---DE------------------IAQTASDRKVLTRTVTPENLAYVIYTSGSTGKP 1313
Cdd:cd05909     83 LTSKQFIEKLKLHHLFDVEYDARIvylEDlrakiskadkckaflagkFPPKWLLRIFGVAPVQPDDPAVILFTSGSEGLP 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1314 KGVMIPHKALTNFLVSMGETPGLTAEDKMLAVTT--YCFDIAAlELFLPLIKGAHcyICQTEHTKDVEKLKRDIRTIKPT 1391
Cdd:cd05909    163 KGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPffHSFGLTG-CLWLPLLSGIK--VVFHPNPLDYKKIPELIYDKKAT 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1392 VMQATPaTWKMLFYSGWENEENVK---ILCGGEALPETLKRYFLDT-GSEAWNMFGPTETtiwSAVQRINDECSRA---T 1464
Cdd:cd05909    240 ILLGTP-TFLRGYARAAHPEDFSSlrlVVAGAEKLKDTLRQEFQEKfGIRILEGYGTTEC---SPVISVNTPQSPNkegT 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1465 IGRPIANTQIYITDSQ-LAPVPAGVPGELCIAGDGVAKGYYKKEELTDsrfidnpFEPGSKLYRTGDMARWLPGGRIEYI 1543
Cdd:cd05909    316 VGRPLPGMEVKIVSVEtHEEVPIGEGGLLLVRGPNVMLGYLNEPELTS-------FAFGDGWYDTGDIGKIDGEGFLTIT 388
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1544 GRIDNQVKIRGFRIELGDIESRLSEH-PGILECVVVADMDN-----LAAYYTAKHANASltarELRHFVKNA-LPAYMVP 1616
Cdd:cd05909    389 GRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDGrkgekIVLLTTTTDTDPS----SLNDILKNAgISNLAKP 464
                          490       500
                   ....*....|....*....|...
gi 1776025254 1617 SYFIQLDHMPLTPNGKIDRNSLK 1639
Cdd:cd05909    465 SYIHQVEEIPLLGTGKPDYVTLK 487
KR_1_FAS_SDR_x cd08954
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 1, complex (x) SDRs; ...
2851-3063 2.72e-32

beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 1, complex (x) SDRs; NADP-dependent KR domain of the multidomain type I FAS, a complex SDR family. This subfamily also includes proteins identified as polyketide synthase (PKS), a protein with related modular protein architecture and similar function. It includes the KR domains of mammalian and chicken FAS, and Dictyostelium discoideum putative polyketide synthases (PKSs). These KR domains contain two subdomains, each of which is related to SDR Rossmann fold domains. However, while the C-terminal subdomain has an active site similar to the other SDRs and a NADP-binding capability, the N-terminal SDR-like subdomain is truncated and lacks these functions, serving a supportive structural role. In some instances, such as porcine FAS, an enoyl reductase (a Rossman fold NAD-binding domain of the medium-chain dehydrogenase/reductase, MDR family) module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consists of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthesis uses a dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-ketoacyl reductase (KR), forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-enoyl reductase (ER); this KR and ER are members of the SDR family. This KR subfamily has an active site tetrad with a similar 3D orientation compared to archetypical SDRs, but the active site Lys and Asn residue positions are swapped. The characteristic NADP-binding is typical of the multidomain complex SDRs, with a GGXGXXG NADP binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187657 [Multi-domain]  Cd Length: 452  Bit Score: 134.11  E-value: 2.72e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2851 YLITGGAGSLGLLFAKEIANRTGRSTIVLTGRSVLSEDKENELEALRSIGAEVVYREADVSDQHAVHHLFEEIKERY--G 2928
Cdd:cd08954    221 YLITGGSGGLGLEILKWLVKRGAVENIIILSRSGMKWELELLIREWKSQNIKFHFVSVDVSDVSSLEKAINLILNAPkiG 300
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2929 TLNGIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSGLLHVDECS--KDFPLDFFIFFSSVSGCLGNAGQADYAAANSFMDA 3006
Cdd:cd08954    301 PIGGIFHLAFVLIDKVLEIDTESLFISVNKAKVMGAINLHNQSikRCWKLDYFVLFSSVSSIRGSAGQCNYVCANSVLDS 380
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1776025254 3007 FAEYRRSLAAskkrfgSTISFNWPLWEEGGMQVGAEDEKRMLKTTGMVPMPTDSGLK 3063
Cdd:cd08954    381 LSRYRKSIGL------PSIAINWGAIGDVGFVSRNESVDTLLGGQGLLPQSINSCLG 431
FACL_like_2 cd05917
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
195-555 3.31e-32

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341241 [Multi-domain]  Cd Length: 349  Bit Score: 131.25  E-value: 3.31e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  195 TSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDHVGGIGMLHLRDVYLGCQEINVSSEtilMEPLKWLD 274
Cdd:cd05917     10 TSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPVPLFHCFGSVLGVLACLTHGATMVFPSPS---FDPLAVLE 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  275 WIDHYRASvtwapnFAFGLVTDFAEEI---KDRKWDLSSMRYMLNGGEAMVAKVGRRILELLephGLPADAIrpAWGMSE 351
Cdd:cd05917     87 AIEKEKCT------ALHGVPTMFIAELehpDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVM---NMKDVTI--AYGMTE 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  352 TSSgVIFShefTRAGTSDDDHFVEIGSPIPGFSMRIVN-DHNELVEEGEIGRFQVSGLSVTSGYYQRPDLNESVFTEDGW 430
Cdd:cd05917    156 TSP-VSTQ---TRTDDSIEKRVNTVGRIMPHTEAKIVDpEGGIVPPVGVPGELCIRGYSVMKGYWNDPEKTAEAIDGDGW 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  431 FETGDLGFL-RNGRLTITGRTKDAIIINGINYYSHAIES------AVEELSEI----ETSYTAACA-VRLGQNstdqlai 498
Cdd:cd05917    232 LHTGDLAVMdEDGYCRIVGRIKDMIIRGGENIYPREIEEflhthpKVSDVQVVgvpdERYGEEVCAwIRLKEG------- 304
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1776025254  499 ffvtsAKLNDEQMSQLLRNIQSHVSqvigvTPEYLLPVqkEEIPKTAIGKIQRTQLK 555
Cdd:cd05917    305 -----AELTEEDIKAYCKGKIAHYK-----VPRYVFFV--DEFPLTVSGKIQKFKLR 349
A_NRPS_Cytc1-like cd17643
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...
186-554 5.40e-32

similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341298 [Multi-domain]  Cd Length: 450  Bit Score: 133.20  E-value: 5.40e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  186 PEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDI--TFNWMPFD-HVGGI--GMLHlrdvylGCQEINV 260
Cdd:cd17643     92 PDDLAYVIYTSGSTGRPKGVVVSHANVLALFAATQRWFGFNEDDVwtLFHSYAFDfSVWEIwgALLH------GGRLVVV 165
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  261 SSETiLMEPLKWLDWIDHYRASVTWAPNFAFGlvtDFAEEIKDRKWDLSSMRYMLNGGEAMVAKVGRRileLLEPHGLPA 340
Cdd:cd17643    166 PYEV-ARSPEDFARLLRDEGVTVLNQTPSAFY---QLVEAADRDGRDPLALRYVIFGGEALEAAMLRP---WAGRFGLDR 238
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  341 DAIRPAWGMSETSSGVIFsHEFTRAGTSDDDHFVeIGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGYYQRPDL 420
Cdd:cd17643    239 PQLVNMYGITETTVHVTF-RPLDAADLPAAAASP-IGRPLPGLRVYVLDADGRPVPPGVVGELYVSGAGVARGYLGRPEL 316
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  421 NESVFTEDGW-------FETGDLG-FLRNGRLTITGRTKDAIIINGinyysHAIesaveELSEIETSYT-------AACA 485
Cdd:cd17643    317 TAERFVANPFggpgsrmYRTGDLArRLPDGELEYLGRADEQVKIRG-----FRI-----ELGEIEAALAthpsvrdAAVI 386
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1776025254  486 VRLGQNSTDQLAIFFVTsaklnDEQMSQLLRNIQSHVSQVIgvtPEYLLP---VQKEEIPKTAIGKIQRTQL 554
Cdd:cd17643    387 VREDEPGDTRLVAYVVA-----DDGAAADIAELRALLKELL---PDYMVParyVPLDALPLTVNGKLDRAAL 450
PRK07788 PRK07788
acyl-CoA synthetase; Validated
1152-1642 1.07e-31

acyl-CoA synthetase; Validated


Pssm-ID: 236097 [Multi-domain]  Cd Length: 549  Bit Score: 133.90  E-value: 1.07e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1152 YITFHELFEQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYV 1231
Cdd:PRK07788    48 YGPFAGLVAHAARRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARII 127
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1232 PLDPSYPAERLEYMLE---------DSEvFITLTT---SELVNTLSWNGVTTAL-----LDQDWDEIAQTASDRKVLTrt 1294
Cdd:PRK07788   128 LLNTGFSGPQLAEVAAregvkalvyDDE-FTDLLSalpPDLGRLRAWGGNPDDDepsgsTDETLDDLIAGSSTAPLPK-- 204
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1295 vTPENLAYVIYTSGSTGKPKGVMIPH-KALTNF--LVS-----MGETPGLTAedKMLAVTTYcfdiAALELFLPLikGAH 1366
Cdd:PRK07788   205 -PPKPGGIVILTSGTTGTPKGAPRPEpSPLAPLagLLSrvpfrAGETTLLPA--PMFHATGW----AHLTLAMAL--GST 275
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1367 CYIcqteHTK-DVEKLKRDIRTIKPTVMQATPATWKMLFysgwENEENVK----------ILCGGEALPETLKRYFLDT- 1434
Cdd:PRK07788   276 VVL----RRRfDPEATLEDIAKHKATALVVVPVMLSRIL----DLGPEVLakydtsslkiIFVSGSALSPELATRALEAf 347
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1435 GSEAWNMFGPTETTiWSAVQRIND-ECSRATIGRPIANTQIYITDSQLAPVPAGVPGELCIAGDGVAKGYykkeelTDSR 1513
Cdd:PRK07788   348 GPVLYNLYGSTEVA-FATIATPEDlAEAPGTVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGY------TDGR 420
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1514 fiDNPFEPGskLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMDN-----LAAYy 1588
Cdd:PRK07788   421 --DKQIIDG--LLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEefgqrLRAF- 495
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1776025254 1589 TAKHANASLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLKNID 1642
Cdd:PRK07788   496 VVKAPGAALDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELREMD 549
PRK07059 PRK07059
Long-chain-fatty-acid--CoA ligase; Validated
1151-1640 1.24e-31

Long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235923 [Multi-domain]  Cd Length: 557  Bit Score: 133.99  E-value: 1.24e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1151 PYITFHELFEQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGP-DRLAgIYVDRSLDMLVGLLAILKAGGA 1229
Cdd:PRK07059    21 QYPSLADLLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKgARVA-IMMPNVLQYPVAIAAVLRAGYV 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1230 YVPLDPSYPAERLEYMLEDS--EVFITL----TTSELV--NTLSWNGVTTALLDQ--------------------DW--- 1278
Cdd:PRK07059   100 VVNVNPLYTPRELEHQLKDSgaEAIVVLenfaTTVQQVlaKTAVKHVVVASMGDLlgfkghivnfvvrrvkkmvpAWslp 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1279 ------DEIAQTAsdRKVLTR-TVTPENLAYVIYTSGSTGKPKGVMIPHKaltNFLVSMGET-----PGLTAEDKMLAVT 1346
Cdd:PRK07059   180 ghvrfnDALAEGA--RQTFKPvKLGPDDVAFLQYTGGTTGVSKGATLLHR---NIVANVLQMeawlqPAFEKKPRPDQLN 254
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1347 TYC----FDIAALEL--FLPLIKGAHCYIcqTEHTKDVEKLKRDIRTIKPTVMqatPATwKMLFYSGWENEENVKI---- 1416
Cdd:PRK07059   255 FVCalplYHIFALTVcgLLGMRTGGRNIL--IPNPRDIPGFIKELKKYQVHIF---PAV-NTLYNALLNNPDFDKLdfsk 328
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1417 ----LCGGEALPETL-KRYFLDTGSEAWNMFGPTETTIWSAVQRINDECSRATIGRPIANTQIYITDSQLAPVPAGVPGE 1491
Cdd:PRK07059   329 livaNGGGMAVQRPVaERWLEMTGCPITEGYGLSETSPVATCNPVDATEFSGTIGLPLPSTEVSIRDDDGNDLPLGEPGE 408
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1492 LCIAGDGVAKGYYKKEELTDSRFIDNPFepgsklYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPG 1571
Cdd:PRK07059   409 ICIRGPQVMAGYWNRPDETAKVMTADGF------FRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPG 482
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1776025254 1572 ILECVVVADMDN-----LAAYYTAKhaNASLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLKN 1640
Cdd:PRK07059   483 VLEVAAVGVPDEhsgeaVKLFVVKK--DPALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRRELRD 554
PLN02836 PLN02836
3-oxoacyl-[acyl-carrier-protein] synthase
3436-3775 1.86e-31

3-oxoacyl-[acyl-carrier-protein] synthase


Pssm-ID: 215449 [Multi-domain]  Cd Length: 437  Bit Score: 131.07  E-value: 1.86e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3436 KALEDAGCPPQSLSGTG-TGIFIGTGNTGYKDLFHRANLPIEGHA--ATGHMIPSVGPNRMSYFLNI----HGPSEPVET 3508
Cdd:PLN02836   103 EALSDARWLPSEDEAKErTGVSIGGGIGSITDILEAAQLICEKRLrrLSPFFVPRILINMAAGHVSIrygfQGPNHAAVT 182
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3509 ACSSSLVAIHRAVTAMQNGDCEMAIAGGVNTILTEEAHISYSKAGMLS-KDGRCKT-----FSADANGYVRGEGVGMVML 3582
Cdd:PLN02836   183 ACATGAHSIGDAFRMIQFGDADVMVAGGTESSIDALSIAGFSRSRALStKFNSCPTeasrpFDCDRDGFVIGEGAGVLVL 262
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3583 KKLEDAERDGNHIYGVIRGTAENhgGRANTLTSPNPKAQADLLV--RAYRQAGIDPSTVTYIEAHGTGTELGDPIEINGL 3660
Cdd:PLN02836   263 EELEHAKRRGAKIYAEVRGYGMS--GDAHHITQPHEDGRGAVLAmtRALQQSGLHPNQVDYVNAHATSTPLGDAVEARAI 340
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3661 KAAFKElsnmrgesqpDVPDHRCGIGSVKSNIGHLELAAGISGLIKVLLQMKHKTLVKSLHCETLNP-----YLQLTDSP 3735
Cdd:PLN02836   341 KTVFSE----------HATSGGLAFSSTKGATGHLLGAAGAVEAIFSVLAIHHGIAPPTLNLERPDPifddgFVPLTASK 410
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 1776025254 3736 fyivqekqewksvtdcdgnELPRRAGIS-SFGIGGVNAHIV 3775
Cdd:PLN02836   411 -------------------AMLIRAALSnSFGFGGTNASLL 432
CBAL cd05923
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ...
1154-1638 1.96e-31

4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.


Pssm-ID: 341247 [Multi-domain]  Cd Length: 493  Bit Score: 132.25  E-value: 1.96e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1154 TFHELFEQQAKKTPDRAA-VSYEGQT-LTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYV 1231
Cdd:cd05923      2 TVFEMLRRAASRAPDACAiADPARGLrLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPA 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1232 PLDPSYPAERLEYMLEDSE---VFITLTTSELVNTLSWNGVTTALLDQDWDEIAQTASDrKVLTRTVTPENLAYVIYTSG 1308
Cdd:cd05923     82 LINPRLKAAELAELIERGEmtaAVIAVDAQVMDAIFQSGVRVLALSDLVGLGEPESAGP-LIEDPPREPEQPAFVFYTSG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1309 STGKPKGVMIPHKALTNFLVSMGETPGLT--AEDKMLAVTTYCFDIAALELFLPLIKGAHCYiCQTEHTKDVEKLKRdIR 1386
Cdd:cd05923    161 TTGLPKGAVIPQRAAESRVLFMSTQAGLRhgRHNVVLGLMPLYHVIGFFAVLVAALALDGTY-VVVEEFDPADALKL-IE 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1387 TIKPTVMQATPATWKMLFYSGWENEENVKIL----CGGEALPET-LKRYFLDTGSEAWNMFGPTETTiwsaVQRINDECS 1461
Cdd:cd05923    239 QERVTSLFATPTHLDALAAAAEFAGLKLSSLrhvtFAGATMPDAvLERVNQHLPGEKVNIYGTTEAM----NSLYMRDAR 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1462 RATIGRPIANTQIYIT---DSQLAPVPAGVPGELCIA--GDGVAKGYYKKEELTDSRFIDNpfepgskLYRTGDMARWLP 1536
Cdd:cd05923    315 TGTEMRPGFFSEVRIVrigGSPDEALANGEEGELIVAaaADAAFTGYLNQPEATAKKLQDG-------WYRTGDVGYVDP 387
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1537 GGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMDN-----LAAYYTAKHANasLTARELRHFVK-NAL 1610
Cdd:cd05923    388 SGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADErwgqsVTACVVPREGT--LSADELDQFCRaSEL 465
                          490       500
                   ....*....|....*....|....*...
gi 1776025254 1611 PAYMVPSYFIQLDHMPLTPNGKIDRNSL 1638
Cdd:cd05923    466 ADFKRPRRYFFLDELPKNAMNKVLRRQL 493
PRK06155 PRK06155
crotonobetaine/carnitine-CoA ligase; Provisional
1158-1646 2.69e-31

crotonobetaine/carnitine-CoA ligase; Provisional


Pssm-ID: 235719 [Multi-domain]  Cd Length: 542  Bit Score: 132.57  E-value: 2.69e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1158 LFEQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGP-DRLAGIYVDRS--LDMLVGLLAIlkaGGAYVPLD 1234
Cdd:PRK06155    26 MLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRgDRVALMCGNRIefLDVFLGCAWL---GAIAVPIN 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1235 PSYPAERLEYMLEDSEVFITLTTSELVNTLS------------W--NGVTTALLDQDWDEIAQTASDRKVLTRTVTPENL 1300
Cdd:PRK06155   103 TALRGPQLEHILRNSGARLLVVEAALLAALEaadpgdlplpavWllDAPASVSVPAGWSTAPLPPLDAPAPAAAVQPGDT 182
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1301 AYVIYTSGSTGKPKGVMIPHKALTNFLVSMGETPGLTAEDkMLAVTTYCFDIAALELFLP-LIKGAHCYICQ-------- 1371
Cdd:PRK06155   183 AAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADD-VLYTTLPLFHTNALNAFFQaLLAGATYVLEPrfsasgfw 261
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1372 ---TEHTKDVEKLKRDIRTIkptvMQATPATWKmlfysgwENEENVKILCGGEALPETLKRYFLDTGSEAWNMFGPTETT 1448
Cdd:PRK06155   262 pavRRHGATVTYLLGAMVSI----LLSQPARES-------DRAHRVRVALGPGVPAALHAAFRERFGVDLLDGYGSTETN 330
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1449 IWSAVQRinDECSRATIGRPIANTQIYITDSQLAPVPAGVPGELCIAGD---GVAKGYYKKEELTDSRFIDNPFEPGSKL 1525
Cdd:PRK06155   331 FVIAVTH--GSQRPGSMGRLAPGFEARVVDEHDQELPDGEPGELLLRADepfAFATGYFGMPEKTVEAWRNLWFHTGDRV 408
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1526 YRTGDmarwlpgGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVA-----DMDNLAAYYTAKHANAsLTAR 1600
Cdd:PRK06155   409 VRDAD-------GWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPvpselGEDEVMAAVVLRDGTA-LEPV 480
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*.
gi 1776025254 1601 ELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLKNIDLSGE 1646
Cdd:PRK06155   481 ALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLREQGVTAD 526
23DHB-AMP_lg cd05920
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ...
1154-1638 2.95e-31

2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.


Pssm-ID: 341244 [Multi-domain]  Cd Length: 482  Bit Score: 131.68  E-value: 2.95e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1154 TFHELFEQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPL 1233
Cdd:cd05920     16 PLGDLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVLA 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1234 DPSYPAERLEYMLEDSEVfitlttselvntlswngvtTALLDQD-WDEIAQTASDRKVLTRTVTPenlAYVIYTSGSTGK 1312
Cdd:cd05920     96 LPSHRRSELSAFCAHAEA-------------------VAYIVPDrHAGFDHRALARELAESIPEV---ALFLLSGGTTGT 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1313 PKgvMIP--HKALTNFLVSMGETPGLTAEDKMLAV--TTYCFDIAALELFLPLIKGAHCYICQTEHTKDVEKLkrdIRTI 1388
Cdd:cd05920    154 PK--LIPrtHNDYAYNVRASAEVCGLDQDTVYLAVlpAAHNFPLACPGVLGTLLAGGRVVLAPDPSPDAAFPL---IERE 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1389 KPTVMQATPATWKM-LFYSGWENEE--NVKIL-CGGEALPETLKRYFLDT-GSEAWNMFGPTETTIwsAVQRIND--ECS 1461
Cdd:cd05920    229 GVTVTALVPALVSLwLDAAASRRADlsSLRLLqVGGARLSPALARRVPPVlGCTLQQVFGMAEGLL--NYTRLDDpdEVI 306
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1462 RATIGRPI-ANTQIYITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPFepgsklYRTGDMARWLPGGRI 1540
Cdd:cd05920    307 IHTQGRPMsPDDEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGF------YRTGDLVRRTPDGYL 380
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1541 EYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMDNL-----AAYYTAKhaNASLTARELRHFVKNA-LPAYM 1614
Cdd:cd05920    381 VVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELlgersCAFVVLR--DPPPSAAQLRRFLRERgLAAYK 458
                          490       500
                   ....*....|....*....|....
gi 1776025254 1615 VPSYFIQLDHMPLTPNGKIDRNSL 1638
Cdd:cd05920    459 LPDRIEFVDSLPLTAVGKIDKKAL 482
PRK12467 PRK12467
peptide synthase; Provisional
162-1002 3.16e-31

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 136.83  E-value: 3.16e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  162 EGFRAIIVE---DLLSAEADTDWHQS-SPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPF 237
Cdd:PRK12467  1689 DGLRSLVLDqedDWLEGYSDSNPAVNlAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSF 1768
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  238 ----DHVGGIGMLhlrdvyLGCQEINVSSETILMEPLKWLDWIDHYRASVTWAPNFAFGLVTDFAEEIKDrkwdLSSMRY 313
Cdd:PRK12467  1769 afdvSVWELFWPL------INGARLVIAPPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQMDEQVEH----PLSLRR 1838
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  314 MLNGGEAMVAKVGRRILEllephGLPADAIRPAWGMSETSSGVifSHEFTRAGTSDDDHFVEIGSPIPGFSMRIVNDHNE 393
Cdd:PRK12467  1839 VVCGGEALEVEALRPWLE-----RLPDTGLFNLYGPTETAVDV--THWTCRRKDLEGRDSVPIGQPIANLSTYILDASLN 1911
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  394 LVEEGEIGRFQVSGLSVTSGYYQRPDLNESVFTEDGW-------FETGDLGFLR-NGRLTITGRTKDAIIINGINYYSHA 465
Cdd:PRK12467  1912 PVPIGVAGELYLGGVGLARGYLNRPALTAERFVADPFgtvgsrlYRTGDLARYRaDGVIEYLGRIDHQVKIRGFRIELGE 1991
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  466 IESAVEELSEIETSYTAACAVRLGQnstdQLAIFFVTSAKL---NDEQMSQLLRNIQSHVSQVIgvtPEYLLPVQ---KE 539
Cdd:PRK12467  1992 IEARLREQGGVREAVVIAQDGANGK----QLVAYVVPTDPGlvdDDEAQVALRAILKNHLKASL---PEYMVPAHlvfLA 2064
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  540 EIPKTAIGKIQRTQLKtsfengefdhllhKPnrmnDAVQdeeMQQAdhVKRVREEIQEHLLTCLTEELHVSRdwVEPNAN 619
Cdd:PRK12467  2065 RMPLTPNGKLDRKALP-------------AP----DASE---LQQA--YVAPQSELEQRLAAIWQDVLGLEQ--VGLHDN 2120
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  620 IQSLGVNSIKMMKLIrSIEKNYHIKLTAREIHQYPTIERLASYLSEHEDLSSSSADKKGTDTyktepersqatfqPLSEV 699
Cdd:PRK12467  2121 FFELGGDSIISIQVV-SRARQAGIRFTPKDLFQHQTVQSLAAVAQEGDGTVSIDQGPVTGDL-------------PLLPI 2186
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  700 QKGLWTLQkmSPEKSAYHVPLCFKFSSGLHLETLQQAFGLVLNQHPILKHVIQEKDG------VPILKNEPALSIEIKTE 773
Cdd:PRK12467  2187 QQMFFADD--IPERHHWNQSVLLEPREALDAELLEAALQALLVHHDALRLGFVQEDGgwsamhRAPEQERRPLLWQVVVA 2264
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  774 NISSMKEsdipafLRKKVKEPYVKENSPLVRVMSFSRSEQEHFLLVVIHHLIFDGVSSVTFIHSLFDTYQLLLKGQQpei 853
Cdd:PRK12467  2265 DKEELEA------LCEQAQRSLDLEEGPLLRAVLATLPDGSQRLLLVIHHLVVDGVSWRILLEDLQTAYRQLQGGQP--- 2335
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  854 AVSPAIYHDFAAWEKNM--LAGKDGVK-HRTYWQKQLSGT---LP------NLQLpKVSASSVSEFREDtYTRRLssgfm 921
Cdd:PRK12467  2336 VKLPAKTSAFKAWAERLqtYAASAALAdELGYWQAQLQGAsteLPcdhpqgGLQR-RHAASVTTHLDSE-WTRRL----- 2408
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  922 nqVRMFAKEHSVNVTTVFLSCYMMLLGRYTGQKEQIVGMPAMVRpEERFDD-----AIGHFLNMLPIRseLNPADTFSSF 996
Cdd:PRK12467  2409 --LQEAPAAYRTQVNDLLLTALARVIARWTGQASTLIQLEGHGR-EDLFDEidltrTVGWFTSLYPVK--LSPTASLATS 2483

                   ....*...
gi 1776025254  997 IS--KLQL 1002
Cdd:PRK12467  2484 IKtiKEQL 2491
PRK12583 PRK12583
acyl-CoA synthetase; Provisional
13-555 3.80e-31

acyl-CoA synthetase; Provisional


Pssm-ID: 237145 [Multi-domain]  Cd Length: 558  Bit Score: 132.59  E-value: 3.80e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254   13 PSVSHGEPLHISEKQpaTIPEVLYRTAAELGDTKGIIYLQpdgTEVYQSYRRLWDDGLRIVKGLRQSGLKAKQSVILQLG 92
Cdd:PRK12583     4 PSYYQGGGDKPLLTQ--TIGDAFDATVARFPDREALVVRH---QALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAP 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254   93 DN-----SQLLPAFWGCVLTGVVPAPLAVPPTYAESSSGTQKL--KDAWTLLDKPAVITD--RGMHQEMLDWAKEQGLEG 163
Cdd:PRK12583    79 NCaewllTQFATARIGAILVNINPAYRASELEYALGQSGVRWVicADAFKTSDYHAMLQEllPGLAEGQPGALACERLPE 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  164 FRAIIVEDLLSAEADTDWHQ-------SSPEDLAL------------LLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQG 224
Cdd:PRK12583   159 LRGVVSLAPAPPPGFLAWHElqargetVSREALAErqasldrddpinIQYTSGTTGFPKGATLSHHNILNNGYFVAESLG 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  225 FTREDITFNWMPFDHVGGIGMLHLrdvylGCqeinVSSETILMEPLKWLDWIDHYRASVTWAPNFAFGLVTDFAEEIK-- 302
Cdd:PRK12583   239 LTEHDRLCVPVPLYHCFGMVLANL-----GC----MTVGACLVYPNEAFDPLATLQAVEEERCTALYGVPTMFIAELDhp 309
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  303 DRK-WDLSSMRYMLNGGEAMVAKVGRRILEllEPHglpADAIRPAWGMSETSSgviFSHEFTRagTSDDDHFVE-IGSPI 380
Cdd:PRK12583   310 QRGnFDLSSLRTGIMAGAPCPIEVMRRVMD--EMH---MAEVQIAYGMTETSP---VSLQTTA--ADDLERRVEtVGRTQ 379
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  381 PGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGYYQRPDLNESVFTEDGWFETGDLGFL-RNGRLTITGRTKDAIIINGI 459
Cdd:PRK12583   380 PHLEVKVVDPDGATVPRGEIGELCTRGYSVMKGYWNNPEATAESIDEDGWMHTGDLATMdEQGYVRIVGRSKDMIIRGGE 459
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  460 NYYSHAIEsaveelsEIETSYTAACAVRL----GQNSTDQLAIFFV--TSAKLNDEQMSQLLRNIQSHVSqvigvTPEYL 533
Cdd:PRK12583   460 NIYPREIE-------EFLFTHPAVADVQVfgvpDEKYGEEIVAWVRlhPGHAASEEELREFCKARIAHFK-----VPRYF 527
                          570       580
                   ....*....|....*....|..
gi 1776025254  534 LPVqkEEIPKTAIGKIQRTQLK 555
Cdd:PRK12583   528 RFV--DEFPMTVTGKVQKFRMR 547
PRK09088 PRK09088
acyl-CoA synthetase; Validated
1162-1645 3.90e-31

acyl-CoA synthetase; Validated


Pssm-ID: 181644 [Multi-domain]  Cd Length: 488  Bit Score: 131.47  E-value: 3.90e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1162 QAKKTPDR-AAVSY-EGQTLTYRELDERSTQLAIYLQAHGVGP-DRLAgIYVDRSLDMLVGLLAILKAGGAYVPLDPSYP 1238
Cdd:PRK09088     4 HARLQPQRlAAVDLaLGRRWTYAELDALVGRLAAVLRRRGCVDgERLA-VLARNSVWLVALHFACARVGAIYVPLNWRLS 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1239 AERLEYMLEDSEVFITLTTSELVntlswnGVTTALLDQDwDEIAQTASDRKVLTRTVTPENLAYVIYTSGSTGKPKGVMI 1318
Cdd:PRK09088    83 ASELDALLQDAEPRLLLGDDAVA------AGRTDVEDLA-AFIASADALEPADTPSIPPERVSLILFTSGTSGQPKGVML 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1319 PHKALTNFLVSMGETPGLTAEDKMLaVTTYCFDIAAL--ELFLPLIKGAHCYICQT-EHTKDVEKLKRDIRTIK-----P 1390
Cdd:PRK09088   156 SERNLQQTAHNFGVLGRVDAHSSFL-CDAPMFHIIGLitSVRPVLAVGGSILVSNGfEPKRTLGRLGDPALGIThyfcvP 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1391 TVMQA-------TPATWKMLfysgweneenVKILCGGEALPETLKRYFLDTG---------SEAWNMFG-PTETTIwsav 1453
Cdd:PRK09088   235 QMAQAfraqpgfDAAALRHL----------TALFTGGAPHAAEDILGWLDDGipmvdgfgmSEAGTVFGmSVDCDV---- 300
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1454 qrINDECSRATIGRPIANTQIyiTDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFidnpfePGSKLYRTGDMAR 1533
Cdd:PRK09088   301 --IRAKAGAAGIPTPTVQTRV--VDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAF------TGDGWFRTGDIAR 370
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1534 WLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMD---NLAAYYTAKHANAS-LTARELRHFVKNA 1609
Cdd:PRK09088   371 RDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADaqwGEVGYLAIVPADGApLDLERIRSHLSTR 450
                          490       500       510
                   ....*....|....*....|....*....|....*.
gi 1776025254 1610 LPAYMVPSYFIQLDHMPLTPNGKIDRNSLKNIDLSG 1645
Cdd:PRK09088   451 LAKYKVPKHLRLVDALPRTASGKLQKARLRDALAAG 486
PRK07314 PRK07314
beta-ketoacyl-ACP synthase II;
1778-2187 5.69e-31

beta-ketoacyl-ACP synthase II;


Pssm-ID: 235987 [Multi-domain]  Cd Length: 411  Bit Score: 129.14  E-value: 5.69e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1778 DEFWENLRDGKESIAFfnkeeLQRFGISKEIAENADYVPAkasiegkdrFDPSFFqISPKDAEFMDPQLRMLLTHSWKAI 1857
Cdd:PRK07314    20 ESTWKNLLAGKSGIGP-----ITHFDTSDLAVKIAGEVKD---------FNPDDY-MSRKEARRMDRFIQYGIAAAKQAV 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1858 EDAGYAAGQI--PQTSVFMSASNNSYRALlpSDTTESLET--PDgYVSwVLAQSGTIPTMISH----KLGLRGPSYFVHA 1929
Cdd:PRK07314    85 EDAGLEITEEnaDRIGVIIGSGIGGLETI--EEQHITLLEkgPR-RVS-PFFVPMAIINMAAGhvsiRYGAKGPNHSIVT 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1930 NCSSsliGLHS---AYKSLLSAESDYALVGGAtlhtESNI------GYVHQPGLNFSSDGHIKA---FDASADGMIGGEG 1997
Cdd:PRK07314   161 ACAT---GAHAigdAARLIAYGDADVMVAGGA----EAAItplgiaGFAAARALSTRNDDPERAsrpFDKDRDGFVMGEG 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1998 VAVVLLKKAADAVKDGDHIYALLRGIGVNNDGadkvgfY---APSVKGQ--ADVVQQVMNQTKIHPESICYVEAHGTGTK 2072
Cdd:PRK07314   234 AGILVLEELEHAKARGAKIYAEVVGYGMTGDA------YhmtAPAPDGEgaARAMKLALKDAGINPEDIDYINAHGTSTP 307
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2073 LGDPIELAALTNVYRQYTNKTQfcgIGSVKTNIGHLDTAAGLAGCIKVVMSLYHQELAPSINYKEPNPNTDLAsspfYVV 2152
Cdd:PRK07314   308 AGDKAETQAIKRVFGEHAYKVA---VSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTINLDNPDEECDLD----YVP 380
                          410       420       430
                   ....*....|....*....|....*....|....*.
gi 1776025254 2153 DQKKtlSREIQthrAALS-SFGLGGTNTHAIFEQFK 2187
Cdd:PRK07314   381 NEAR--ERKID---YALSnSFGFGGTNASLVFKRYE 411
KR_3_FAS_SDR_x cd08956
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 3, complex (x); ...
4152-4411 5.71e-31

beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 3, complex (x); Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. In some instances, such as porcine FAS, an enoyl reductase (ER) module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consists of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthesis uses a dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-KR, forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta- ER. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes KR domains found in many multidomain PKSs, including six of seven Sorangium cellulosum PKSs (encoded by spiDEFGHIJ) which participate in the synthesis of the polyketide scaffold of the cytotoxic spiroketal polyketide spirangien. These seven PKSs have either a single PKS module (SpiF), two PKR modules (SpiD,-E,-I,-J), or three PKS modules (SpiG,-H). This subfamily includes the second KR domains of SpiE,-G, I, and -J, both KR domains of SpiD, and the third KR domain of SpiH. The single KR domain of SpiF, the first and second KR domains of SpiH, the first KR domains of SpiE,-G,- I, and -J, and the third KR domain of SpiG, belong to a different KR_FAS_SDR subfamily. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187659 [Multi-domain]  Cd Length: 448  Bit Score: 130.08  E-value: 5.71e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4152 KAHPETGKATEQSAVFPKDHVLlITGGTRGIGLLCARHFAECYGVKKLVLTGR--EQLPPREEWarfktsntslaekiqa 4229
Cdd:cd08956    176 RVAPAATLPPVPRPLDPDGTVL-ITGGTGTLGALLARHLVTEHGVRHLLLVSRrgPDAPGAAEL---------------- 238
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4230 VRELEAKGVQVEMLSLTLSDDAQVEQTLQHIKRTlGPIGGVIHCAGLTDMDTLAfiRKTSDDIQRVMEPKVSGLTTLYRH 4309
Cdd:cd08956    239 VAELAALGAEVTVAACDVADRAALAALLAAVPAD-HPLTAVVHAAGVLDDGVLT--SLTPERLDAVLRPKVDAAWHLHEL 315
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4310 VCNEPLQFFVLFSSVSAIIPelSAGQADYAMANSYMDyfAEAHQKH---VPIISVQWPNWKETGM-----GEVTNQAYRE 4381
Cdd:cd08956    316 TRDLDLAAFVLFSSAAGVLG--SPGQANYAAANAFLD--ALAQHRRargLPATSLAWGLWAQASGmtahlSDADLARLAR 391
                          250       260       270
                   ....*....|....*....|....*....|
gi 1776025254 4382 SGLFSITNSEGLRFLDQIVSkMFGPVVLPA 4411
Cdd:cd08956    392 GGLRPLSAEEGLALFDAALA-ADEPVLVPA 420
OSB_MenE-like cd17630
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ...
1300-1640 6.77e-31

O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.


Pssm-ID: 341285 [Multi-domain]  Cd Length: 325  Bit Score: 126.68  E-value: 6.77e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1300 LAYVIYTSGSTGKPKGVMIPHKALTNFLVSMGETPGLTAEDKMLaVTTYCFDIAALE-LFLPLIKGAHCYIcqTEHTKDV 1378
Cdd:cd17630      2 LATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWL-LSLPLYHVGGLAiLVRSLLAGAELVL--LERNQAL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1379 EKlkrDIRTIKPTVMQATPATWKMLFYSGWENE--ENVK-ILCGGEALPETLKRYFLDTGSEAWNMFGPTETTIWSAVQR 1455
Cdd:cd17630     79 AE---DLAPPGVTHVSLVPTQLQRLLDSGQGPAalKSLRaVLLGGAPIPPELLERAADRGIPLYTTYGMTETASQVATKR 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1456 INDECsRATIGRPIANTQIYITDsqlapvpagvPGELCIAGDGVAKGYYKKEEltdsrfIDNPFEPGskLYRTGDMARWL 1535
Cdd:cd17630    156 PDGFG-RGGVGVLLPGRELRIVE----------DGEIWVGGASLAMGYLRGQL------VPEFNEDG--WFTTKDLGELH 216
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1536 PGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMDN-----LAAYYTakhANASLTARELRHFVKNAL 1610
Cdd:cd17630    217 ADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEelgqrPVAVIV---GRGPADPAELRAWLKDKL 293
                          330       340       350
                   ....*....|....*....|....*....|
gi 1776025254 1611 PAYMVPSYFIQLDHMPLTPNGKIDRNSLKN 1640
Cdd:cd17630    294 ARFKLPKRIYPVPELPRTGGGKVDRRALRA 323
EntE COG1021
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ...
27-555 9.18e-31

EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440644 [Multi-domain]  Cd Length: 533  Bit Score: 131.04  E-value: 9.18e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254   27 QPATIPEVLYRTAAELGDTKGIIylqpDGTEVYqSYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNSQLLPAFWGCVL 106
Cdd:COG1021     23 RGETLGDLLRRRAERHPDRIAVV----DGERRL-SYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFR 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  107 TGVVPApLAVPP-------TYAESSsgtqklkdawtlldKP-AVITDRGM----HQEMldwAKE--QGLEGFRAIIV--- 169
Cdd:COG1021     98 AGAIPV-FALPAhrraeisHFAEQS--------------EAvAYIIPDRHrgfdYRAL---ARElqAEVPSLRHVLVvgd 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  170 -------EDLLSAEADTDWHQSSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDH--- 239
Cdd:COG1021    160 ageftslDALLAAPADLSEPRPDPDDVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEICGLDADTVYLAALPAAHnfp 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  240 -----------VGGigmlhlrdvylgcqeinvsseTILM----EPLKWLDWIDHYRASVTwapnfafGLV----TDFAEE 300
Cdd:COG1021    240 lsspgvlgvlyAGG---------------------TVVLapdpSPDTAFPLIERERVTVT-------ALVpplaLLWLDA 291
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  301 IKDRKWDLSSMRYMLNGGeamvAKVGRRIlellephglpADAIRPAW--------GMSEtssGVIfshEFTRAGTSDDDH 372
Cdd:COG1021    292 AERSRYDLSSLRVLQVGG----AKLSPEL----------ARRVRPALgctlqqvfGMAE---GLV---NYTRLDDPEEVI 351
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  373 FVEIGSPI-PGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGYYQRPDLNESVFTEDGWFETGDL-GFLRNGRLTITGRT 450
Cdd:COG1021    352 LTTQGRPIsPDDEVRIVDEDGNPVPPGEVGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLvRRTPDGYLVVEGRA 431
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  451 KDAIIINGINYYSHAIESAVEELSEIetsyTAACAV-----RLGQNSTdqlAifFVTsakLNDEQMSqlLRNIQSHVSQV 525
Cdd:COG1021    432 KDQINRGGEKIAAEEVENLLLAHPAV----HDAAVVampdeYLGERSC---A--FVV---PRGEPLT--LAELRRFLRER 497
                          570       580       590
                   ....*....|....*....|....*....|...
gi 1776025254  526 iGVtPEYLLP---VQKEEIPKTAIGKIQRTQLK 555
Cdd:COG1021    498 -GL-AAFKLPdrlEFVDALPLTAVGKIDKKALR 528
LC-FACS_euk cd05927
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ...
1179-1592 1.29e-30

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.


Pssm-ID: 341250 [Multi-domain]  Cd Length: 545  Bit Score: 130.80  E-value: 1.29e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1179 LTYRELDERSTQLAIYLQAHGV--GPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLEDSEVFITLT 1256
Cdd:cd05927      6 ISYKEVAERADNIGSALRSLGGkpAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVFC 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1257 TselvntlswNGVTTALldqdWDEIAQTASDRKVLTRTVTPENLAYVIYTSGSTGKPKGVMIPHKALTNFLVSM----GE 1332
Cdd:cd05927     86 D---------AGVKVYS----LEEFEKLGKKNKVPPPPPKPEDLATICYTSGTTGNPKGVMLTHGNIVSNVAGVfkilEI 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1333 TPGLTAEDKMLAvttycfdiaalelFLPLikgAHCY----ICQTEH--------TKDVEKLKRDIRTIKPTV-------- 1392
Cdd:cd05927    153 LNKINPTDVYIS-------------YLPL---AHIFervvEALFLYhgakigfySGDIRLLLDDIKALKPTVfpgvprvl 216
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1393 ----------MQATPATWKMLFYSGWENEE----------------------------NVKILCGGEA--LPETLKryFL 1432
Cdd:cd05927    217 nriydkifnkVQAKGPLKRKLFNFALNYKLaelrsgvvraspfwdklvfnkikqalggNVRLMLTGSAplSPEVLE--FL 294
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1433 DT--GSEAWNMFGPTETTIWSAVQRINDECSrATIGRPIANTQIYITD------SQLAPVPAgvpGELCIAGDGVAKGYY 1504
Cdd:cd05927    295 RValGCPVLEGYGQTECTAGATLTLPGDTSV-GHVGGPLPCAEVKLVDvpemnyDAKDPNPR---GEVCIRGPNVFSGYY 370
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1505 KKEELTDSRFIDNPFepgsklYRTGDMARWLPGGRIEYIGRIDNQVKI-RGFRIELGDIESRLSEHPGI----------- 1572
Cdd:cd05927    371 KDPEKTAEALDEDGW------LHTGDIGEWLPNGTLKIIDRKKNIFKLsQGEYVAPEKIENIYARSPFVaqifvygdslk 444
                          490       500
                   ....*....|....*....|..
gi 1776025254 1573 --LECVVVADMDNLAAYYTAKH 1592
Cdd:cd05927    445 sfLVAIVVPDPDVLKEWAASKG 466
PRK08974 PRK08974
long-chain-fatty-acid--CoA ligase FadD;
1151-1654 1.94e-30

long-chain-fatty-acid--CoA ligase FadD;


Pssm-ID: 236359 [Multi-domain]  Cd Length: 560  Bit Score: 130.56  E-value: 1.94e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1151 PYITFHELFEQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQaHGVG---PDRLAgIYVDRSLDMLVGLLAILKAG 1227
Cdd:PRK08974    21 RYQSLVDMFEQAVARYADQPAFINMGEVMTFRKLEERSRAFAAYLQ-NGLGlkkGDRVA-LMMPNLLQYPIALFGILRAG 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1228 GAYVPLDPSYPAERLEYMLEDSEVFITLTTSELVNTLSW--------NGVTTALLDQ---------------------DW 1278
Cdd:PRK08974    99 MIVVNVNPLYTPRELEHQLNDSGAKAIVIVSNFAHTLEKvvfktpvkHVILTRMGDQlstakgtlvnfvvkyikrlvpKY 178
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1279 DeIAQTASDRKVLTR---------TVTPENLAYVIYTSGSTGKPKGVMIPHK-ALTNFLVSMGETPGLTAEDKMLAVTTY 1348
Cdd:PRK08974   179 H-LPDAISFRSALHKgrrmqyvkpELVPEDLAFLQYTGGTTGVAKGAMLTHRnMLANLEQAKAAYGPLLHPGKELVVTAL 257
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1349 -CFDIAALE----LFLPLikGAHCYIcqTEHTKDVEKLKRDIRTIKPTVMQATpatwKMLFySGWENEENVKIL------ 1417
Cdd:PRK08974   258 pLYHIFALTvnclLFIEL--GGQNLL--ITNPRDIPGFVKELKKYPFTAITGV----NTLF-NALLNNEEFQELdfsslk 328
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1418 ---CGGEALPETL-KRYFLDTGSEAWNMFGPTETTIWSAVQRINDECSRATIGRPIANTQIYITDSQLAPVPAGVPGELC 1493
Cdd:PRK08974   329 lsvGGGMAVQQAVaERWVKLTGQYLLEGYGLTECSPLVSVNPYDLDYYSGSIGLPVPSTEIKLVDDDGNEVPPGEPGELW 408
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1494 IAGDGVAKGYYKKEELTDSRFIDNpfepgskLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGIL 1573
Cdd:PRK08974   409 VKGPQVMLGYWQRPEATDEVIKDG-------WLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVL 481
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1574 ECVVV-----ADMDNLAAYYTAKhaNASLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLKNidlsgEQL 1648
Cdd:PRK08974   482 EVAAVgvpseVSGEAVKIFVVKK--DPSLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRD-----EAR 554

                   ....*.
gi 1776025254 1649 KQRQTS 1654
Cdd:PRK08974   555 AKVDNK 560
PRK07638 PRK07638
acyl-CoA synthetase; Validated
1163-1650 2.52e-30

acyl-CoA synthetase; Validated


Pssm-ID: 236071 [Multi-domain]  Cd Length: 487  Bit Score: 128.74  E-value: 2.52e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1163 AKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAgIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERL 1242
Cdd:PRK07638    11 ASLQPNKIAIKENDRVLTYKDWFESVCKVANWLNEKESKNKTIA-ILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDEL 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1243 EYMLEDSEVFITLTTSELVNTLSwnGVTTALLDQD-WDEIAQTASDRkvLTRTVTPENLA-YVIYTSGSTGKPKGVMIPH 1320
Cdd:PRK07638    90 KERLAISNADMIVTERYKLNDLP--DEEGRVIEIDeWKRMIEKYLPT--YAPIENVQNAPfYMGFTSGSTGKPKAFLRAQ 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1321 KALTNFLVSMGETPGLTAEDKMLAVTTYC---FDIAALE-LFLplikGAHCYICQTEHTKDVeklKRDIRTIKPTVMQAT 1396
Cdd:PRK07638   166 QSWLHSFDCNVHDFHMKREDSVLIAGTLVhslFLYGAIStLYV----GQTVHLMRKFIPNQV---LDKLETENISVMYTV 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1397 PAtwkML--FYSGWENEEN-VKILCGG--------EALPET---LKRYfldtgseawNMFGPTETTIWSAVQRINDECSR 1462
Cdd:PRK07638   239 PT---MLesLYKENRVIENkMKIISSGakweaeakEKIKNIfpyAKLY---------EFYGASELSFVTALVDEESERRP 306
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1463 ATIGRPIANTQIYITDSqlapvpagvPGELCIAGDgVAKGYYKkeelTDSRFIDnpFEPGSKLYRTGDMARWLPGGRIEY 1542
Cdd:PRK07638   307 NSVGRPFHNVQVRICNE---------AGEEVQKGE-IGTVYVK----SPQFFMG--YIIGGVLARELNADGWMTVRDVGY 370
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1543 I---------GRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMDnlaAYYTAK-----HANAslTARELRHFVKN 1608
Cdd:PRK07638   371 EdeegfiyivGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPD---SYWGEKpvaiiKGSA--TKQQLKSFCLQ 445
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|..
gi 1776025254 1609 ALPAYMVPSYFIQLDHMPLTPNGKIDRNSLKNIDLSGEQLKQ 1650
Cdd:PRK07638   446 RLSSFKIPKEWHFVDEIPYTNSGKIARMEAKSWIENQEKIYE 487
A_NRPS_Ta1_like cd12116
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ...
61-554 3.18e-30

The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.


Pssm-ID: 341281 [Multi-domain]  Cd Length: 470  Bit Score: 128.18  E-value: 3.18e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254   61 SYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNSQLLPAFWGCVLTGVVPAPLAvpPTY-AESSSGTqkLKDAwtlldK 139
Cdd:cd12116     14 SYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLD--PDYpADRLRYI--LEDA-----E 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  140 PAVI-TDRGMhqemldwakeqgLEGFRAIIVEDLLSAEADTD-----WHQSSPEDLALLLLTSGSTGTPKAVMLNHRNIM 213
Cdd:cd12116     85 PALVlTDDAL------------PDRLPAGLPVLLLALAAAAAapaapRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLV 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  214 SMVKGIIQMQGFTRED-----ITFNwmpFDhvggIGMLHLRDVYLGCQEINVSSETILMEPLKWLDWIDHYRASV----- 283
Cdd:cd12116    153 NFLHSMRERLGLGPGDrllavTTYA---FD----ISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSITVmqatp 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  284 -TWAPNFAFGlvtdfaeeikdrkW-DLSSMRyMLNGGEAMVAKVGRRILellephglpaDAIRPAWGM---SETSsgvIF 358
Cdd:cd12116    226 aTWRMLLDAG-------------WqGRAGLT-ALCGGEALPPDLAARLL----------SRVGSLWNLygpTETT---IW 278
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  359 ShefTRAGTSDDDHFVEIGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGYYQRPDLNESVFTEDG-------WF 431
Cdd:cd12116    279 S---TAARVTAAAGPIPIGRPLANTQVYVLDAALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPfagpgsrLY 355
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  432 ETGDLGFLR-NGRLTITGRTKDAIIINGinyysHAIesaveELSEIETSYT-----AACAVRLGQNSTDQLAIFFVTSAK 505
Cdd:cd12116    356 RTGDLVRRRaDGRLEYLGRADGQVKIRG-----HRI-----ELGEIEAALAahpgvAQAAVVVREDGGDRRLVAYVVLKA 425
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1776025254  506 LNDEQMSQLLRNIQSHVsqvigvtPEYLLP---VQKEEIPKTAIGKIQRTQL 554
Cdd:cd12116    426 GAAPDAAALRAHLRATL-------PAYMVPsafVRLDALPLTANGKLDRKAL 470
PRK06145 PRK06145
acyl-CoA synthetase; Validated
1152-1640 3.26e-30

acyl-CoA synthetase; Validated


Pssm-ID: 102207 [Multi-domain]  Cd Length: 497  Bit Score: 128.85  E-value: 3.26e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1152 YITFHelfeqqAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYV 1231
Cdd:PRK06145     7 SIAFH------ARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1232 PLDPSYPAERLEYMLEDSEVFITLTTSEL---VNTLSWNGVTTALLDQDWDEIAQTASDRKVLTrTVTPENLAYVIYTSG 1308
Cdd:PRK06145    81 PINYRLAADEVAYILGDAGAKLLLVDEEFdaiVALETPKIVIDAAAQADSRRLAQGGLEIPPQA-AVAPTDLVRLMYTSG 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1309 STGKPKGVMIPHKALTNFLVSMGETPGLTAEDKMLAVTTYcFDIAALElfLPLIK-----GAHCYICQTEHTKDVEKLKR 1383
Cdd:PRK06145   160 TTDRPKGVMHSYGNLHWKSIDHVIALGLTASERLLVVGPL-YHVGAFD--LPGIAvlwvgGTLRIHREFDPEAVLAAIER 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1384 DIRT------IKPTVMQATPATWKMLFYS-GWeneenvkILCGGEALPETLKRYF--LDTGSEAWNMFGPTETTIWSAVQ 1454
Cdd:PRK06145   237 HRLTcawmapVMLSRVLTVPDRDRFDLDSlAW-------CIGGGEKTPESRIRDFtrVFTRARYIDAYGLTETCSGDTLM 309
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1455 RINDECSR-ATIGRPIANTQIYITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPFepgsklyRTGDMAR 1533
Cdd:PRK06145   310 EAGREIEKiGSTGRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWF-------RSGDVGY 382
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1534 WLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMD-NLAAYYTAK---HANASLTARELRHFVKNA 1609
Cdd:PRK06145   383 LDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDdRWGERITAVvvlNPGATLTLEALDRHCRQR 462
                          490       500       510
                   ....*....|....*....|....*....|.
gi 1776025254 1610 LPAYMVPSYFIQLDHMPLTPNGKIDRNSLKN 1640
Cdd:PRK06145   463 LASFKVPRQLKVRDELPRNPSGKVLKRVLRD 493
ABCL cd05958
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ...
1169-1639 4.23e-30

2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.


Pssm-ID: 341268 [Multi-domain]  Cd Length: 439  Bit Score: 127.21  E-value: 4.23e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1169 RAAVSYEGQTLTYRELDERSTQLAIYLQAHGVgpDRLAGIYVDRSLD--MLVG-LLAILKAGGAYVPLDPSYPAERLEYM 1245
Cdd:cd05958      1 RTCLRSPEREWTYRDLLALANRIANVLVGELG--IVPGNRVLLRGSNspELVAcWFGIQKAGAIAVATMPLLRPKELAYI 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1246 LEDSEVfitlttselvntlswngvTTALLDQdwdeiAQTASDrkvltrtvtpeNLAYVIYTSGSTGKPKGVMIPHKALtn 1325
Cdd:cd05958     79 LDKARI------------------TVALCAH-----ALTASD-----------DICILAFTSGTTGAPKATMHFHRDP-- 122
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1326 FLVSMGETP---GLTAEDKMLAVTTYCFDIA-ALELFLPLIKGAHCyICQTEHTKDveKLKRDIRTIKPTVMQATPATWK 1401
Cdd:cd05958    123 LASADRYAVnvlRLREDDRFVGSPPLAFTFGlGGVLLFPFGVGASG-VLLEEATPD--LLLSAIARYKPTVLFTAPTAYR 199
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1402 MLFYSGWENEEN----VKILCGGEALP-ETLKRYFLDTGSEAWNMFGPTET--TIWSAVQrinDECSRATIGRPIANTQI 1474
Cdd:cd05958    200 AMLAHPDAAGPDlsslRKCVSAGEALPaALHRAWKEATGIPIIDGIGSTEMfhIFISARP---GDARPGATGKPVPGYEA 276
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1475 YITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRfidnpfepGSKLYrTGDMARWLPGGRIEYIGRIDNQVKIRG 1554
Cdd:cd05958    277 KVVDDEGNPVPDGTIGRLAVRGPTGCRYLADKRQRTYVQ--------GGWNI-TGDTYSRDPDGYFRHQGRSDDMIVSGG 347
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1555 FRIELGDIESRLSEHPGILECVVVA--DMDNLA---AYYTAK--HANASLTARELRHFVKNALPAYMVPSYFIQLDHMPL 1627
Cdd:cd05958    348 YNIAPPEVEDVLLQHPAVAECAVVGhpDESRGVvvkAFVVLRpgVIPGPVLARELQDHAKAHIAPYKYPRAIEFVTELPR 427
                          490
                   ....*....|..
gi 1776025254 1628 TPNGKIDRNSLK 1639
Cdd:cd05958    428 TATGKLQRFALR 439
PRK08314 PRK08314
long-chain-fatty-acid--CoA ligase; Validated
30-454 4.46e-30

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236235 [Multi-domain]  Cd Length: 546  Bit Score: 128.92  E-value: 4.46e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254   30 TIPEV-----LYRTAAELGDTKGIIYLqpdGTEVyqSYRRLWDDGLRIVKGLRQS-GLKAKQSVILQLGDNSQLLPAFWG 103
Cdd:PRK08314     6 TLPETslfhnLEVSARRYPDKTAIVFY---GRAI--SYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  104 CVLTG--VVPA-PLAVPPTYAE--SSSGTQKLKDAWTLLDK--PAVITDR------GMHQEML---------DWAKE--- 158
Cdd:PRK08314    81 ILRANavVVPVnPMNREEELAHyvTDSGARVAIVGSELAPKvaPAVGNLRlrhvivAQYSDYLpaepeiavpAWLRAepp 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  159 -QGLEGFRAIIVEDLLSAEADTDWHQSSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPF 237
Cdd:PRK08314   161 lQALAPGGVVAWKEALAAGLAPPPHTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPL 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  238 DHVGG-IGMLHlRDVYLGcqeinvssETILMEPlKW-----LDWIDHYRASVTWAPNfafGLVTDFAEEIKDRKWDLSSM 311
Cdd:PRK08314   241 FHVTGmVHSMN-APIYAG--------ATVVLMP-RWdreaaARLIERYRVTHWTNIP---TMVVDFLASPGLAERDLSSL 307
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  312 RYMLNGGEAMVAKVGRRILELLephGLPadaIRPAWGMSETSSgvifsheFTRAGTSDDDHFVEIGSPIPGFSMRIVN-D 390
Cdd:PRK08314   308 RYIGGGGAAMPEAVAERLKELT---GLD---YVEGYGLTETMA-------QTHSNPPDRPKLQCLGIPTFGVDARVIDpE 374
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1776025254  391 HNELVEEGEIGRFQVSGLSVTSGYYQRPDLNESVFTE-DG--WFETGDLGFL-RNGRLTITGRTKDAI 454
Cdd:PRK08314   375 TLEELPPGEVGEIVVHGPQVFKGYWNRPEATAEAFIEiDGkrFFRTGDLGRMdEEGYFFITDRLKRMI 442
AAS_C cd05909
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ...
185-549 7.94e-30

C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.


Pssm-ID: 341235 [Multi-domain]  Cd Length: 490  Bit Score: 127.45  E-value: 7.94e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  185 SPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDH----VGGIGMLHLRDVYLGCQEINV 260
Cdd:cd05909    145 QPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFFHsfglTGCLWLPLLSGIKVVFHPNPL 224
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  261 SSETILmeplkwlDWIDHYRASVTWA-PNFaFGLVTDFAEeikdrKWDLSSMRYMLNGGEAMVAKVGRRILELLephGLP 339
Cdd:cd05909    225 DYKKIP-------ELIYDKKATILLGtPTF-LRGYARAAH-----PEDFSSLRLVVAGAEKLKDTLRQEFQEKF---GIR 288
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  340 adaIRPAWGMSETSSGVIFSHEFT--RAGTsdddhfveIGSPIPGFSMRIVN-DHNELVEEGEIGRFQVSGLSVTSGYYQ 416
Cdd:cd05909    289 ---ILEGYGTTECSPVISVNTPQSpnKEGT--------VGRPLPGMEVKIVSvETHEEVPIGEGGLLLVRGPNVMLGYLN 357
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  417 RPDLNESVFtEDGWFETGDLGFL-RNGRLTITGRTKDAIIINGiNYYSHaieSAVEE-LSEIETSYTAACAVRLGQNSTD 494
Cdd:cd05909    358 EPELTSFAF-GDGWYDTGDIGKIdGEGFLTITGRLSRFAKIAG-EMVSL---EAIEDiLSEILPEDNEVAVVSVPDGRKG 432
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1776025254  495 QLAIFFVTSAKLNDEQMSQLLRNIQshvsqvigvTPEYLLP---VQKEEIPKTAIGKI 549
Cdd:cd05909    433 EKIVLLTTTTDTDPSSLNDILKNAG---------ISNLAKPsyiHQVEEIPLLGTGKP 481
PRK07529 PRK07529
AMP-binding domain protein; Validated
28-555 1.27e-29

AMP-binding domain protein; Validated


Pssm-ID: 236043 [Multi-domain]  Cd Length: 632  Bit Score: 128.53  E-value: 1.27e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254   28 PATIPEVLYRTAAELGDTKGIIYlQPDGTE----VYQSYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNSQLLPAFWG 103
Cdd:PRK07529    24 PASTYELLSRAAARHPDAPALSF-LLDADPldrpETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWG 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  104 CVLTGVVPA--PLAVPPTYAE--SSSGT---------------QKLKDA---------WTLLD-KPAVITDRGMHQEMLD 154
Cdd:PRK07529   103 GEAAGIANPinPLLEPEQIAEllRAAGAkvlvtlgpfpgtdiwQKVAEVlaalpelrtVVEVDlARYLPGPKRLAVPLIR 182
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  155 WAKEQGLEGFRAIIveDLLSAEADTDWHQSSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNW 234
Cdd:PRK07529   183 RKAHARILDFDAEL--ARQPGDRLFSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDTVFCG 260
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  235 MPFDHVGG---IGMLHLrdvylgcqeinvSS--ETILMEPLKWLD-------W--IDHYRasvtwaPNFAFGLVTDFAE- 299
Cdd:PRK07529   261 LPLFHVNAllvTGLAPL------------ARgaHVVLATPQGYRGpgvianfWkiVERYR------INFLSGVPTVYAAl 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  300 -EIKDRKWDLSSMRYMLNGGEAMVAKVGRRILELLephGLPadaIRPAWGMSETSSGVIFS---HEfTRAGTsdddhfve 375
Cdd:PRK07529   323 lQVPVDGHDISSLRYALCGAAPLPVEVFRRFEAAT---GVR---IVEGYGLTEATCVSSVNppdGE-RRIGS-------- 387
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  376 IGSPIPGFSMRIV---NDHNELVE--EGEIGRFQVSGLSVTSGYYQrPDLNESVFTEDGWFETGDLGFL-RNGRLTITGR 449
Cdd:PRK07529   388 VGLRLPYQRVRVVildDAGRYLRDcaVDEVGVLCIAGPNVFSGYLE-AAHNKGLWLEDGWLNTGDLGRIdADGYFWLTGR 466
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  450 TKDAIIINGINYYSHAIESAVEELSEIetsyTAACAVrlGQNST--DQLAIFFVTSAKLNDEQMSQLLRNIQSHVSQVIG 527
Cdd:PRK07529   467 AKDLIIRGGHNIDPAAIEEALLRHPAV----ALAAAV--GRPDAhaGELPVAYVQLKPGASATEAELLAFARDHIAERAA 540
                          570       580
                   ....*....|....*....|....*...
gi 1776025254  528 VtPEYLLPVqkEEIPKTAIGKIQRTQLK 555
Cdd:PRK07529   541 V-PKHVRIL--DALPKTAVGKIFKPALR 565
A_NRPS_TubE_like cd05906
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ...
1154-1639 1.98e-29

The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341232 [Multi-domain]  Cd Length: 540  Bit Score: 127.01  E-value: 1.98e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1154 TFHELFEQQAKKTPDRAAVSY----EGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGA 1229
Cdd:cd05906     11 TLLELLLRAAERGPTKGITYIdadgSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFV 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1230 YVPLDP----SYPAERLEYMLEDSEVF---ITLTTSELVNTLSwnGVTTALLDQDWDEIAQT---ASDRKVLTRTVTPEN 1299
Cdd:cd05906     91 PAPLTVpptyDEPNARLRKLRHIWQLLgspVVLTDAELVAEFA--GLETLSGLPGIRVLSIEellDTAADHDLPQSRPDD 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1300 LAYVIYTSGSTGKPKGVMIPHKALTNFLVSMGETPGLTAEDKMLAVTTycFD-IAAL-ELFL-PLIKGAHCYICQTEHT- 1375
Cdd:cd05906    169 LALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVP--LDhVGGLvELHLrAVYLGCQQVHVPTEEIl 246
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1376 KDVEKLKRDI------RTIKPTVMQA---------TPATW-----KMLFYSGwenEENVKILCggEALPETLKRYFL--D 1433
Cdd:cd05906    247 ADPLRWLDLIdryrvtITWAPNFAFAllndlleeiEDGTWdlsslRYLVNAG---EAVVAKTI--RRLLRLLEPYGLppD 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1434 TGSEAWNMfgpTET---TIWSAV---QRINDECSRATIGRPIANTQIYITDSQLAPVPAGVPGELCIAGDGVAKGYYKKE 1507
Cdd:cd05906    322 AIRPAFGM---TETcsgVIYSRSfptYDHSQALEFVSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNP 398
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1508 ELTDSRFIDNPFepgsklYRTGDMArWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVA-------- 1579
Cdd:cd05906    399 EANAEAFTEDGW------FRTGDLG-FLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPSFTAAfavrdpga 471
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1776025254 1580 DMDNLAAYY--TAKHANA-SLTARELRHFVKNAL---PAYMVPsyfIQLDHMPLTPNGKIDRNSLK 1639
Cdd:cd05906    472 ETEELAIFFvpEYDLQDAlSETLRAIRSVVSREVgvsPAYLIP---LPKEEIPKTSLGKIQRSKLK 534
PRK07514 PRK07514
malonyl-CoA synthase; Validated
185-473 3.97e-29

malonyl-CoA synthase; Validated


Pssm-ID: 181011 [Multi-domain]  Cd Length: 504  Bit Score: 125.37  E-value: 3.97e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  185 SPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDHVGGIgmlhlrdvylgcqeiNVSSET 264
Cdd:PRK07514   154 GADDLAAILYTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIHALPIFHTHGL---------------FVATNV 218
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  265 ILMEplkwldwidhyRASVTWAPNFAFGLVTDF------------------AEEIKDRKwDLSSMRYMLNGGEAMVA--- 323
Cdd:PRK07514   219 ALLA-----------GASMIFLPKFDPDAVLALmpratvmmgvptfytrllQEPRLTRE-AAAHMRLFISGSAPLLAeth 286
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  324 -----KVGRRILEllephglpadaiRpaWGMSETssGVIFSHEFT---RAGTsdddhfveIGSPIPGFSMRIVN-DHNEL 394
Cdd:PRK07514   287 refqeRTGHAILE------------R--YGMTET--NMNTSNPYDgerRAGT--------VGFPLPGVSLRVTDpETGAE 342
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  395 VEEGEIGRFQVSGLSVTSGYYQRPDLNESVFTEDGWFETGDLGFL-RNGRLTITGRTKDAIIINGINYYSHAIESAVEEL 473
Cdd:PRK07514   343 LPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGFFITGDLGKIdERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDEL 422
A_NRPS_PpsD_like cd17650
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ...
186-554 4.01e-29

similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341305 [Multi-domain]  Cd Length: 447  Bit Score: 124.50  E-value: 4.01e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  186 PEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKG---IIQMQGFTREDITFNWMPFDHVGGIgmlHLRDVYLGCQEINVSS 262
Cdd:cd17650     92 PEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAwrrEYELDSFPVRLLQMASFSFDVFAGD---FARSLLNGGTLVICPD 168
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  263 ETiLMEPLKWLDWIDHYRASVTWA-PNFAFGLVtdfaEEIKDRKWDLSSMRYMLNGGEAMVAKVGRRILELLEPHglpaD 341
Cdd:cd17650    169 EV-KLDPAALYDLILKSRITLMEStPALIRPVM----AYVYRNGLDLSAMRLLIVGSDGCKAQDFKTLAARFGQG----M 239
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  342 AIRPAWGMSETS--SGVifsHEFTRAGTSDDDhFVEIGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGYYQRPD 419
Cdd:cd17650    240 RIINSYGVTEATidSTY---YEEGRDPLGDSA-NVPIGRPLPNTAMYVLDERLQPQPVGVAGELYIGGAGVARGYLNRPE 315
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  420 LNESVFTEDGW------FETGDLG-FLRNGRLTITGRTKDAIIINGINYYSHAIESAVEELSEIEtsyTAACAVRLGQNS 492
Cdd:cd17650    316 LTAERFVENPFapgermYRTGDLArWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAID---EAVVAVREDKGG 392
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1776025254  493 TDQLAIFFVTSAKLNdeqmsqlLRNIQSHVSQVIgvtPEYLLP---VQKEEIPKTAIGKIQRTQL 554
Cdd:cd17650    393 EARLCAYVVAAATLN-------TAELRAFLAKEL---PSYMIPsyyVQLDALPLTPNGKVDRRAL 447
cond_enzymes cd00327
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ...
3426-3776 4.02e-29

Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) Claisen-like condensation reaction. Members are share strong structural similarity, and are involved in the synthesis and degradation of fatty acids, and the production of polyketides, a diverse group of natural products.


Pssm-ID: 238201 [Multi-domain]  Cd Length: 254  Bit Score: 119.47  E-value: 4.02e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3426 QQRLLMTYVWKALEDAGCPpqslSGTGTGIFIGTGNTGYkdlfhranlpiEGHAATGhmipsvgpnRMSYFLNI-HGPSE 3504
Cdd:cd00327      7 ASELGFEAAEQAIADAGLS----KGPIVGVIVGTTGGSG-----------EFSGAAG---------QLAYHLGIsGGPAY 62
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3505 PVETACSSSLVAIHRAVTAMQNGDCEMAIAGGVNTIlteeahisyskagmlskdgrcktfsadangyVRGEGVGMVMLKK 3584
Cdd:cd00327     63 SVNQACATGLTALALAVQQVQNGKADIVLAGGSEEF-------------------------------VFGDGAAAAVVES 111
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3585 LEDAERDGNHIYGVIRGTAENHGGrANTLTSPNPKAQADLLVRAYRQAGIDPSTVTYIEAHGTGTELGDPIEINGLKAAF 3664
Cdd:cd00327    112 EEHALRRGAHPQAEIVSTAATFDG-ASMVPAVSGEGLARAARKALEGAGLTPSDIDYVEAHGTGTPIGDAVELALGLDPD 190
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3665 KelsnmrgesqpdvpDHRCGIGSVKSNIGHLELAAGISGLIKVLLQMKHktlvkslhcetlnpylqltdspfyivqekqE 3744
Cdd:cd00327    191 G--------------VRSPAVSATLIMTGHPLGAAGLAILDELLLMLEH------------------------------E 226
                          330       340       350
                   ....*....|....*....|....*....|..
gi 1776025254 3745 WKSVTDcdgnELPRRAGISSFGIGGVNAHIVI 3776
Cdd:cd00327    227 FIPPTP----REPRTVLLLGFGLGGTNAAVVL 254
PRK08439 PRK08439
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
1816-2186 5.31e-29

3-oxoacyl-(acyl carrier protein) synthase II; Reviewed


Pssm-ID: 236265 [Multi-domain]  Cd Length: 406  Bit Score: 123.30  E-value: 5.31e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1816 PAKASIEGKDrFDPSFFqISPKDAEFMDPQLRMLLTHSWKAIEDAGYAAGQIPQTSvfMSASNNSYRALLPSDTTESLet 1895
Cdd:PRK08439    45 PVQIAGEITD-FDPTEV-MDPKEVKKADRFIQLGLKAAREAMKDAGFLPEELDAER--FGVSSASGIGGLPNIEKNSI-- 118
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1896 pdgyvswVLAQSGT-------IPT--------MISHKLGLRGPSYFVHANCSSSLIGLHSAYKSLLSAESDYALVGGAtl 1960
Cdd:PRK08439   119 -------ICFEKGPrkispffIPSalvnmlggFISIEHGLKGPNLSSVTACAAGTHAIIEAVKTIMLGGADKMLVVGA-- 189
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1961 htESNI------GYVHQPGLNFSSDGHIKA---FDASADGMIGGEGVAVVLLKKAADAVKDGDHIYALLRGIGvnnDGAD 2031
Cdd:PRK08439   190 --ESAIcpvgigGFAAMKALSTRNDDPKKAsrpFDKDRDGFVMGEGAGALVLEEYESAKKRGAKIYAEIIGFG---ESGD 264
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2032 KVGFYAPSVKGQADVVQQVMNQTKihPESICYVEAHGTGTKLGDPIELAALTNVyrqYTNKTQFCGIGSVKTNIGHLDTA 2111
Cdd:PRK08439   265 ANHITSPAPEGPLRAMKAALEMAG--NPKIDYINAHGTSTPYNDKNETAALKEL---FGSKEKVPPVSSTKGQIGHCLGA 339
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1776025254 2112 AGLAGCIKVVMSLYHQELAPSINYKEPNPNTDLASSPfyvvdqkkTLSREIQTHRAALSSFGLGGTNTHAIFEQF 2186
Cdd:PRK08439   340 AGAIEAVISIMAMRDGILPPTINQETPDPECDLDYIP--------NVARKAELNVVMSNSFGFGGTNGVVIFKKV 406
4CL cd05904
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ...
1176-1638 5.89e-29

4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.


Pssm-ID: 341230 [Multi-domain]  Cd Length: 505  Bit Score: 125.04  E-value: 5.89e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1176 GQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLEDSEVFITL 1255
Cdd:cd05904     30 GRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAF 109
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1256 TTSELVNTLSWNGVTTALLDQD-------WDEIAQTASDRKVLTRtVTPENLAYVIYTSGSTGKPKGVMIPHK---ALTN 1325
Cdd:cd05904    110 TTAELAEKLASLALPVVLLDSAefdslsfSDLLFEADEAEPPVVV-IKQDDVAALLYSSGTTGRSKGVMLTHRnliAMVA 188
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1326 FLVsMGETPGLTAEDKMLAVTTYcFDIAALELFL--PLIKGAHCYICQtehTKDVEKLKRDIRTIKPTVMQATPATWKML 1403
Cdd:cd05904    189 QFV-AGEGSNSDSEDVFLCVLPM-FHIYGLSSFAlgLLRLGATVVVMP---RFDLEELLAAIERYKVTHLPVVPPIVLAL 263
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1404 FYSGWENEENVK----ILCGGEALP----ETLKRYF----LDTGseawnmFGPTETTIWSAVQrINDECSRA---TIGRP 1468
Cdd:cd05904    264 VKSPIVDKYDLSslrqIMSGAAPLGkeliEAFRAKFpnvdLGQG------YGMTESTGVVAMC-FAPEKDRAkygSVGRL 336
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1469 IANTQIYITD-SQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSrfidnpfepgsklyrTGDMARWLPGGRIEYI---- 1543
Cdd:cd05904    337 VPNVEAKIVDpETGESLPPNQTGELWIRGPSIMKGYLNNPEATAA---------------TIDKEGWLHTGDLCYIdedg 401
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1544 -----GRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMDNLA----AYYTAKHANASLTARELRHFVknalpAYM 1614
Cdd:cd05904    402 ylfivDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAgevpMAFVVRKPGSSLTEDEIMDFV-----AKQ 476
                          490       500       510
                   ....*....|....*....|....*....|.
gi 1776025254 1615 VPSY-------FIqlDHMPLTPNGKIDRNSL 1638
Cdd:cd05904    477 VAPYkkvrkvaFV--DAIPKSPSGKILRKEL 505
A_NRPS_VisG_like cd17651
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ...
185-554 6.47e-29

similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341306 [Multi-domain]  Cd Length: 491  Bit Score: 124.76  E-value: 6.47e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  185 SPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMP--FDH---------VGGiGMLHLRdvyl 253
Cdd:cd17651    134 DADDLAYVIYTSGSTGRPKGVVMPHRSLANLVAWQARASSLGPGARTLQFAGlgFDVsvqeifstlCAG-ATLVLP---- 208
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  254 gcqeinvsSETILMEPLKWLDWIDHYRASVTWAPNFAFGLVtdfAEEIKDRKWDLSSMRYMLNGGEAMVakVGRRILELL 333
Cdd:cd17651    209 --------PEEVRTDPPALAAWLDEQRISRVFLPTVALRAL---AEHGRPLGVRLAALRYLLTGGEQLV--LTEDLREFC 275
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  334 EphGLPADAIRPAWGMSETSsgVIFSHEFTrAGTSDDDHFVEIGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSG 413
Cdd:cd17651    276 A--GLPGLRLHNHYGPTETH--VVTALSLP-GDPAAWPAPPPIGRPIDNTRVYVLDAALRPVPPGVPGELYIGGAGLARG 350
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  414 YYQRPDLNESVFTEDGW------FETGDLG-FLRNGRLTITGRTKDAIIINGinyysHAIesaveELSEIETS------- 479
Cdd:cd17651    351 YLNRPELTAERFVPDPFvpgarmYRTGDLArWLPDGELEFLGRADDQVKIRG-----FRI-----ELGEIEAAlarhpgv 420
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1776025254  480 YTAACAVRLGQNSTDQLAIFFVTsaklnDEQMSQLLRNIQSHVSQVIgvtPEYLLP---VQKEEIPKTAIGKIQRTQL 554
Cdd:cd17651    421 REAVVLAREDRPGEKRLVAYVVG-----DPEAPVDAAELRAALATHL---PEYMVPsafVLLDALPLTPNGKLDRRAL 490
ttLC_FACS_AlkK_like cd12119
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
34-554 8.74e-29

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.


Pssm-ID: 341284 [Multi-domain]  Cd Length: 518  Bit Score: 124.67  E-value: 8.74e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254   34 VLYRTAAELGDTKgIIYLQPDGTEVYQSYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNSQLLPAFWGCVLTGVV--P 111
Cdd:cd12119      1 LLEHAARLHGDRE-IVSRTHEGEVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVlhT 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  112 APLAVPP---TY----AEsssgtqklkDAWTLLDK---P--AVITDRGMHQE----MLDWAKEQGLEGFRAIIVEDLLSA 175
Cdd:cd12119     80 INPRLFPeqiAYiinhAE---------DRVVFVDRdflPllEAIAPRLPTVEhvvvMTDDAAMPEPAGVGVLAYEELLAA 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  176 EADT-DWHQSSPEDLALLLLTSGSTGTPKAVMLNHRNIM--SMVKGIIQMQGFTREDITFNWMPFDHVGGIGMLHLRdVY 252
Cdd:cd12119    151 ESPEyDWPDFDENTAAAICYTSGTTGNPKGVVYSHRSLVlhAMAALLTDGLGLSESDVVLPVVPMFHVNAWGLPYAA-AM 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  253 LGcqeinvsSETIL----MEPLKWLDWIDHYRasVTWA---PNFAFGLvtdfAEEIKDRKWDLSSMRYMLNGGEAMVAKV 325
Cdd:cd12119    230 VG-------AKLVLpgpyLDPASLAELIEREG--VTFAagvPTVWQGL----LDHLEANGRDLSSLRRVVIGGSAVPRSL 296
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  326 GRRILEllepHGLPadaIRPAWGMSETSSGVIFSHEFTRAGTSDDDHFVEI----GSPIPGFSMRIVNDH-NELVEEGE- 399
Cdd:cd12119    297 IEAFEE----RGVR---VIHAWGMTETSPLGTVARPPSEHSNLSEDEQLALrakqGRPVPGVELRIVDDDgRELPWDGKa 369
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  400 IGRFQVSGLSVTSGYYQRPDLNESvFTEDGWFETGDLGFL-RNGRLTITGRTKDAIIINGINYYSHAIESAveeLSEIET 478
Cdd:cd12119    370 VGELQVRGPWVTKSYYKNDEESEA-LTEDGWLRTGDVATIdEDGYLTITDRSKDVIKSGGEWISSVELENA---IMAHPA 445
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  479 SYTAAC--------------AVRLGQNSTdqlaiffVTSAKLNDeQMSQLLRNIQshvsqvigvTPEYLLPVqkEEIPKT 544
Cdd:cd12119    446 VAEAAVigvphpkwgerplaVVVLKEGAT-------VTAEELLE-FLADKVAKWW---------LPDDVVFV--DEIPKT 506
                          570
                   ....*....|
gi 1776025254  545 AIGKIQRTQL 554
Cdd:cd12119    507 STGKIDKKAL 516
ACS-like cd17634
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ...
1154-1633 9.18e-29

acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341289 [Multi-domain]  Cd Length: 587  Bit Score: 125.38  E-value: 9.18e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1154 TFHELFEQQAKKTPDRAAVSYEG------QTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAG 1227
Cdd:cd17634     54 LAANALDRHLRENGDRTAIIYEGddtsqsRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIG 133
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1228 GAYVPLDPSYPAERLEYMLEDSEVFITLTTSE------LVN---------TLSWNGVTTALL--------------DQDW 1278
Cdd:cd17634    134 AVHSVIFGGFAPEAVAGRIIDSSSRLLITADGgvragrSVPlkknvddalNPNVTSVEHVIVlkrtgsdidwqegrDLWW 213
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1279 DEIAQTASDRKVLTRtVTPENLAYVIYTSGSTGKPKGVMIPHKAltnFLVSMGETpgltaedkmlavTTYCFDIAALELF 1358
Cdd:cd17634    214 RDLIAKASPEHQPEA-MNAEDPLFILYTSGTTGKPKGVLHTTGG---YLVYAATT------------MKYVFDYGPGDIY 277
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1359 L-----------------PLIKGAHCYI-------------CQTehtkdVEKLKRDIRTIKPTVMQA-TPATWKMLfysG 1407
Cdd:cd17634    278 WctadvgwvtghsyllygPLACGATTLLyegvpnwptparmWQV-----VDKHGVNILYTAPTAIRAlMAAGDDAI---E 349
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1408 WENEENVKILCG-GEAL-PETLKRYFLDTGSEAW---NMFGPTETTiWSAVQ--RINDECSRATIGRPIANTQIYITDSQ 1480
Cdd:cd17634    350 GTDRSSLRILGSvGEPInPEAYEWYWKKIGKEKCpvvDTWWQTETG-GFMITplPGAIELKAGSATRPVFGVQPAVVDNE 428
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1481 LAPVPAGVPGELCIAGD--GVAKGYYKKEEltdsRFIDNPFEPGSKLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIE 1558
Cdd:cd17634    429 GHPQPGGTEGNLVITDPwpGQTRTLFGDHE----RFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLG 504
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1559 LGDIESRLSEHPGILECVVVADMDNL-----AAYYTAKHA--NASLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNG 1631
Cdd:cd17634    505 TAEIESVLVAHPKVAEAAVVGIPHAIkgqapYAYVVLNHGvePSPELYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSG 584

                   ..
gi 1776025254 1632 KI 1633
Cdd:cd17634    585 KI 586
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
140-551 1.49e-28

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 127.67  E-value: 1.49e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  140 PAVITDRGMHQEMLDWakeqgleGFRAIIVEDLLSAEADTDWHQS--SPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVK 217
Cdd:COG1020    575 RLVLTQSALAARLPEL-------GVPVLALDALALAAEPATNPPVpvTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLA 647
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  218 GIIQMQGFTRED-------ITFN------WMPFdhVGGiGMLHLRDvylgcqeinvssETILMEPLKWLDWIDHYRASVT 284
Cdd:COG1020    648 WMQRRYGLGPGDrvlqfasLSFDasvweiFGAL--LSG-ATLVLAP------------PEARRDPAALAELLARHRVTVL 712
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  285 WAPNFAFGLVTDFAEEikdrkwDLSSMRYMLNGGEAMVAKVGRRILELlephgLPADAIRPAWGMSETSsgvIFSHEFTR 364
Cdd:COG1020    713 NLTPSLLRALLDAAPE------ALPSLRLVLVGGEALPPELVRRWRAR-----LPGARLVNLYGPTETT---VDSTYYEV 778
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  365 AGTSDDDHFVEIGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGYYQRPDLNESVFTEDGWFE-------TGDLG 437
Cdd:COG1020    779 TPPDADGGSVPIGRPIANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFGFpgarlyrTGDLA 858
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  438 -FLRNGRLTITGRTKDAIIINGinyysHAIesaveELSEIET------SYTAACAVRLGQNSTDQLAIFFVTSAKLNDEQ 510
Cdd:COG1020    859 rWLPDGNLEFLGRADDQVKIRG-----FRI-----ELGEIEAallqhpGVREAVVVAREDAPGDKRLVAYVVPEAGAAAA 928
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|.
gi 1776025254  511 MSQLLRNIQSHVSQVigvtPEYLLPVQKEEIPKTAIGKIQR 551
Cdd:COG1020    929 AALLRLALALLLPPY----MVPAAVVLLLPLPLTGNGKLDR 965
PRK08315 PRK08315
AMP-binding domain protein; Validated
1157-1633 1.58e-28

AMP-binding domain protein; Validated


Pssm-ID: 236236 [Multi-domain]  Cd Length: 559  Bit Score: 124.54  E-value: 1.58e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1157 ELFEQQAKKTPDRAAVSYEGQTL--TYRELDERSTQLAIYLQAHGVGP-DRLaGIYVDRSLDMLVGLLAILKAGGAYVPL 1233
Cdd:PRK08315    20 QLLDRTAARYPDREALVYRDQGLrwTYREFNEEVDALAKGLLALGIEKgDRV-GIWAPNVPEWVLTQFATAKIGAILVTI 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1234 DPSYPAERLEYMLEDSEV-FITLTTS-------ELVNTL------SWNGV----------TTALLDQD-------WDEIA 1282
Cdd:PRK08315    99 NPAYRLSELEYALNQSGCkALIAADGfkdsdyvAMLYELapelatCEPGQlqsarlpelrRVIFLGDEkhpgmlnFDELL 178
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1283 QTASDrkvltrtVTPENLAY---------VI---YTSGSTGKPKGVMIPHKALTN--FLVsmGETPGLTAEDKM-LAVTT 1347
Cdd:PRK08315   179 ALGRA-------VDDAELAArqatldpddPIniqYTSGTTGFPKGATLTHRNILNngYFI--GEAMKLTEEDRLcIPVPL 249
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1348 Y-CFDI-----AAL----------ELFLPL-----IKGAHC---------YICQTEHtKDVEKLkrDIRTIKPTVMQATP 1397
Cdd:PRK08315   250 YhCFGMvlgnlACVthgatmvypgEGFDPLatlaaVEEERCtalygvptmFIAELDH-PDFARF--DLSSLRTGIMAGSP 326
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1398 atwkmlfysgweneenvkilCggealP-ETLKRYfldtgSEAWNM------FGPTETTIWSAVQRINDECSR--ATIGRP 1468
Cdd:PRK08315   327 --------------------C-----PiEVMKRV-----IDKMHMsevtiaYGMTETSPVSTQTRTDDPLEKrvTTVGRA 376
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1469 IANTQIYITDSQL-APVPAGVPGELCIAGDGVAKGYYKKEELTdSRFIDnpfePGSKLyRTGDMARWLPGGRIEYIGRID 1547
Cdd:PRK08315   377 LPHLEVKIVDPETgETVPRGEQGELCTRGYSVMKGYWNDPEKT-AEAID----ADGWM-HTGDLAVMDEEGYVNIVGRIK 450
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1548 NQVkIRGfrielG------DIESRLSEHPGILECVVVADMDN-----LAAYYTAKhANASLTARELRHFVKNALPAYMVP 1616
Cdd:PRK08315   451 DMI-IRG-----GeniyprEIEEFLYTHPKIQDVQVVGVPDEkygeeVCAWIILR-PGATLTEEDVRDFCRGKIAHYKIP 523
                          570
                   ....*....|....*..
gi 1776025254 1617 SYFIQLDHMPLTPNGKI 1633
Cdd:PRK08315   524 RYIRFVDEFPMTVTGKI 540
PRK08751 PRK08751
long-chain fatty acid--CoA ligase;
1152-1640 1.67e-28

long-chain fatty acid--CoA ligase;


Pssm-ID: 181546 [Multi-domain]  Cd Length: 560  Bit Score: 124.60  E-value: 1.67e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1152 YITFHELFEQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYL--QAHGVGPDRLAgIYVDRSLDMLVGLLAILKAGGA 1229
Cdd:PRK08751    24 FRTVAEVFATSVAKFADRPAYHSFGKTITYREADQLVEQFAAYLlgELQLKKGDRVA-LMMPNCLQYPIATFGVLRAGLT 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1230 YVPLDPSYPAERLEYMLEDSEV--------FITLTTSELVNTLSWNGVTTALLDQ------------------------- 1276
Cdd:PRK08751   103 VVNVNPLYTPRELKHQLIDSGAsvlvvidnFGTTVQQVIADTPVKQVITTGLGDMlgfpkaalvnfvvkyvkklvpeyri 182
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1277 ----DWDEIAQTASDRKVLTRTVTPENLAYVIYTSGSTGKPKGVMIPHKALTNFLVSMGE---TPGLTAEDKMLAVTT-- 1347
Cdd:PRK08751   183 ngaiRFREALALGRKHSMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQwlaGTGKLEEGCEVVITAlp 262
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1348 --YCFDIAALELFLPLIKGAHCYICQTEHTKD-VEKLKRDIRTIKPTV------MQATPATWKMLFYSgweneenVKILC 1418
Cdd:PRK08751   263 lyHIFALTANGLVFMKIGGCNHLISNPRDMPGfVKELKKTRFTAFTGVntlfngLLNTPGFDQIDFSS-------LKMTL 335
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1419 GG-----EALPETLKRYfldTGSEAWNMFGPTETTIWSAVQRINDECSRATIGRPIANTQIYITDSQLAPVPAGVPGELC 1493
Cdd:PRK08751   336 GGgmavqRSVAERWKQV---TGLTLVEAYGLTETSPAACINPLTLKEYNGSIGLPIPSTDACIKDDAGTVLAIGEIGELC 412
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1494 IAGDGVAKGYYKKEELTdSRFIDnpfepGSKLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGIL 1573
Cdd:PRK08751   413 IKGPQVMKGYWKRPEET-AKVMD-----ADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVL 486
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1776025254 1574 ECVVVADMDN-----LAAYYTAKHANasLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLKN 1640
Cdd:PRK08751   487 EVAAVGVPDEksgeiVKVVIVKKDPA--LTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRRELRD 556
A_NRPS_TlmIV_like cd12114
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ...
61-554 1.68e-28

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.


Pssm-ID: 341279 [Multi-domain]  Cd Length: 477  Bit Score: 123.15  E-value: 1.68e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254   61 SYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNSQLLPAFWGCVLTGV--VPAPLAVPPT-----YAESSSGTqklkda 133
Cdd:cd12114     14 TYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAayVPVDIDQPAArreaiLADAGARL------ 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  134 wtlldkpaVITDrgmhqemLDWAKeQGLEGFRAIIVE-DLLSAEADTDWHQSSPEDLALLLLTSGSTGTPKAVMLNHRNI 212
Cdd:cd12114     88 --------VLTD-------GPDAQ-LDVAVFDVLILDlDALAAPAPPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAA 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  213 MSMVKGIIQMQGFTREDITFNWMPFDH------------VGGigmlhlrdvylgcqEINVSSETILMEPLKWLDWIDHYR 280
Cdd:cd12114    152 LNTILDINRRFAVGPDDRVLALSSLSFdlsvydifgalsAGA--------------TLVLPDEARRRDPAHWAELIERHG 217
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  281 ASVtWapNFA---FGLVTDFAEEIKDRkwdLSSMRYMLNGGeamvakvgRRIlellePHGLPAdAIRPAW---------G 348
Cdd:cd12114    218 VTL-W--NSVpalLEMLLDVLEAAQAL---LPSLRLVLLSG--------DWI-----PLDLPA-RLRALApdarlislgG 277
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  349 MSETSsgvIFS--HEFTRAgtsdDDHFVEI--GSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGYYQRPDLNESV 424
Cdd:cd12114    278 ATEAS---IWSiyHPIDEV----PPDWRSIpyGRPLANQRYRVLDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAAR 350
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  425 FTEDG----WFETGDLGFLR-NGRLTITGRTKDAIIINGINYYSHAIESAVEELSEIetsyTAACAVRLGQNSTDQLAIF 499
Cdd:cd12114    351 FVTHPdgerLYRTGDLGRYRpDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGV----ARAVVVVLGDPGGKRLAAF 426
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1776025254  500 FVTSAKLN-------DEQMSQLLRN--IQSHVSQVigvtpeyllpvqkEEIPKTAIGKIQRTQL 554
Cdd:cd12114    427 VVPDNDGTpiapdalRAFLAQTLPAymIPSRVIAL-------------EALPLTANGKVDRAAL 477
PRK06087 PRK06087
medium-chain fatty-acid--CoA ligase;
187-555 1.90e-28

medium-chain fatty-acid--CoA ligase;


Pssm-ID: 180393 [Multi-domain]  Cd Length: 547  Bit Score: 124.09  E-value: 1.90e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  187 EDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDHvgGIGMLH-LRDVYLgcqeinVSSETI 265
Cdd:PRK06087   187 DELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGH--ATGFLHgVTAPFL------IGARSV 258
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  266 LME---PLKWLDWIDhyRASVTWAPNfAFGLVTDFAEEIKDRKWDLSSMRYMLNGGEAMVAKVGRRILEllepHGLPADA 342
Cdd:PRK06087   259 LLDiftPDACLALLE--QQRCTCMLG-ATPFIYDLLNLLEKQPADLSALRFFLCGGTTIPKKVARECQQ----RGIKLLS 331
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  343 IrpaWGMSETSsgvifSHEFTRAGTSDDDHFVEIGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGYYQRPDLNE 422
Cdd:PRK06087   332 V---YGSTESS-----PHAVVNLDDPLSRFMHTDGYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTA 403
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  423 SVFTEDGWFETGDLGFL-RNGRLTITGRTKDAIIINGINYYSHAIESAVEELSEIETSYTAACA-VRLGQNStdqlaiff 500
Cdd:PRK06087   404 RALDEEGWYYSGDLCRMdEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPdERLGERS-------- 475
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1776025254  501 VTSAKLNDEQMSQLLRNIQSHVSQviGVTPEYLLP---VQKEEIPKTAIGKIQRTQLK 555
Cdd:PRK06087   476 CAYVVLKAPHHSLTLEEVVAFFSR--KRVAKYKYPehiVVIDKLPRTASGKIQKFLLR 531
PRK05605 PRK05605
long-chain-fatty-acid--CoA ligase; Validated
185-555 1.94e-28

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235531 [Multi-domain]  Cd Length: 573  Bit Score: 124.34  E-value: 1.94e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  185 SPEDLALLLLTSGSTGTPKAVMLNHRNIMS-MVKGIIQMQGFTREDITF-NWMPFDHVGGIGMLHLRDVYLGcqeinvsS 262
Cdd:PRK05605   217 TPDDVALILYTSGTTGKPKGAQLTHRNLFAnAAQGKAWVPGLGDGPERVlAALPMFHAYGLTLCLTLAVSIG-------G 289
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  263 ETIL---------MEPLKwldwidhyRASVTWAPnfafGLVTDF---AEEIKDRKWDLSSMRYMLNGgeAMVAKVgrRIL 330
Cdd:PRK05605   290 ELVLlpapdidliLDAMK--------KHPPTWLP----GVPPLYekiAEAAEERGVDLSGVRNAFSG--AMALPV--STV 353
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  331 ELLEPH--GLpadaIRPAWGMSETSSgVIFSHEFT---RAGTsdddhfveIGSPIPGFSMRIVNDHN--ELVEEGEIGRF 403
Cdd:PRK05605   354 ELWEKLtgGL----LVEGYGLTETSP-IIVGNPMSddrRPGY--------VGVPFPDTEVRIVDPEDpdETMPDGEEGEL 420
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  404 QVSGLSVTSGYYQRPDLNESVFtEDGWFETGDLGFL-RNGRLTITGRTKDAIIINGINYYSHAIESAVEELSEIETsyta 482
Cdd:PRK05605   421 LVRGPQVFKGYWNRPEETAKSF-LDGWFRTGDVVVMeEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVED---- 495
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1776025254  483 ACAVRLGQNSTDQ---LAIFFVTSAKLNDEQMSQLLRniqSHVSQvigvtpeYLLP---VQKEEIPKTAIGKIQRTQLK 555
Cdd:PRK05605   496 AAVVGLPREDGSEevvAAVVLEPGAALDPEGLRAYCR---EHLTR-------YKVPrrfYHVDELPRDQLGKVRRREVR 564
PRK12492 PRK12492
long-chain-fatty-acid--CoA ligase; Provisional
1152-1641 2.60e-28

long-chain-fatty-acid--CoA ligase; Provisional


Pssm-ID: 171539 [Multi-domain]  Cd Length: 562  Bit Score: 123.78  E-value: 2.60e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1152 YITFHELFEQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHG--VGPDRLAgIYVDRSLDMLVGLLAILKAGGA 1229
Cdd:PRK12492    23 YKSVVEVFERSCKKFADRPAFSNLGVTLSYAELERHSAAFAAYLQQHTdlVPGDRIA-VQMPNVLQYPIAVFGALRAGLI 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1230 YVPLDPSYPAERLEYMLEDS------------------------EVFITLTTSELVNTLSWNGVTTAL-----------L 1274
Cdd:PRK12492   102 VVNTNPLYTAREMRHQFKDSgaralvylnmfgklvqevlpdtgiEYLIEAKMGDLLPAAKGWLVNTVVdkvkkmvpayhL 181
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1275 DQ--DWDEIAQTASDRKVLTRTVTPENLAYVIYTSGSTGKPKGVMIPHKAL-TNFLVSMGETPGLTAEDKMLAVTTYCFD 1351
Cdd:PRK12492   182 PQavPFKQALRQGRGLSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLvANMLQVRACLSQLGPDGQPLMKEGQEVM 261
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1352 IAALELFLPLIKGAHCYICQTEHTKDVekLKRDIRTIKPTVMQAtpATWKM--------LFYSGWENEE-------NVKI 1416
Cdd:PRK12492   262 IAPLPLYHIYAFTANCMCMMVSGNHNV--LITNPRDIPGFIKEL--GKWRFsallglntLFVALMDHPGfkdldfsALKL 337
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1417 L-CGGEALPE-TLKRYFLDTGSEAWNMFGPTETtiwSAVQRINDECSRA---TIGRPIANTQIYITDSQLAPVPAGVPGE 1491
Cdd:PRK12492   338 TnSGGTALVKaTAERWEQLTGCTIVEGYGLTET---SPVASTNPYGELArlgTVGIPVPGTALKVIDDDGNELPLGERGE 414
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1492 LCIAGDGVAKGYYKKEELTdSRFIDnpfepGSKLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPG 1571
Cdd:PRK12492   415 LCIKGPQVMKGYWQQPEAT-AEALD-----AEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPK 488
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1776025254 1572 ILECVVVADMDNLAA-----YYTAKhaNASLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLKNI 1641
Cdd:PRK12492   489 VANCAAIGVPDERSGeavklFVVAR--DPGLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELRDI 561
PRK06839 PRK06839
o-succinylbenzoate--CoA ligase;
50-554 2.78e-28

o-succinylbenzoate--CoA ligase;


Pssm-ID: 168698 [Multi-domain]  Cd Length: 496  Bit Score: 122.66  E-value: 2.78e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254   50 YLQPD-----GTEVYQSYRRLWDDGLRIVKGLRQS-GLKAKQSVILQLGDNSQLLPAFWGCVLTGVVPAPLAVPPTYAE- 122
Cdd:PRK06839    13 YLHPDriaiiTEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENEl 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  123 ----SSSGTQKLKDAWTLLDKPAVITDRGMHQEMLDWAKEQGLEGFRAIIVEDllsaeadtdwhqSSPEDLALLLLTSGS 198
Cdd:PRK06839    93 ifqlKDSGTTVLFVEKTFQNMALSMQKVSYVQRVISITSLKEIEDRKIDNFVE------------KNESASFIICYTSGT 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  199 TGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDHVGGIGMLHLRDVYLGCQEInVSSEtilMEPLKWLDWIDH 278
Cdd:PRK06839   161 TGKPKGAVLTQENMFWNALNNTFAIDLTMHDRSIVLLPLFHIGGIGLFAFPTLFAGGVII-VPRK---FEPTKALSMIEK 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  279 YRASVTwapnfaFGLVT---DFAEEIKDRKWDLSSMRYMLNGGEAMVAKVGRRILELLEPHGlpadairPAWGMSETSSG 355
Cdd:PRK06839   237 HKVTVV------MGVPTihqALINCSKFETTNLQSVRWFYNGGAPCPEELMREFIDRGFLFG-------QGFGMTETSPT 303
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  356 V--IFSHEFTRAGTSdddhfveIGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGYYQRPDLNESVFtEDGWFET 433
Cdd:PRK06839   304 VfmLSEEDARRKVGS-------IGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETI-QDGWLCT 375
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  434 GDLG-FLRNGRLTITGRTKDAIIINGINYYSHAIESAVEELSEI-ETSYTAACAVRLGQnsTDQLAIFFVTSAKLNDEQm 511
Cdd:PRK06839   376 GDLArVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVyEVAVVGRQHVKWGE--IPIAFIVKKSSSVLIEKD- 452
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*.
gi 1776025254  512 sqllrnIQSHVSQVIGvtpEYLLP---VQKEEIPKTAIGKIQRTQL 554
Cdd:PRK06839   453 ------VIEHCRLFLA---KYKIPkeiVFLKELPKNATGKIQKAQL 489
PRK05677 PRK05677
long-chain-fatty-acid--CoA ligase; Validated
185-555 3.48e-28

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 168170 [Multi-domain]  Cd Length: 562  Bit Score: 123.33  E-value: 3.48e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  185 SPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTRED---ITFNWMPFDHVGGIGMLHLRDVYLGCQEINVS 261
Cdd:PRK05677   205 QADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCRALMGSNLNEgceILIAPLPLYHIYAFTFHCMAMMLIGNHNILIS 284
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  262 S----ETILMEPLKWldwidHYRASVtwapnfafGLVTDFAEEIKD---RKWDLSSMRYMLNGGEAMVAKVGRRILELLe 334
Cdd:PRK05677   285 NprdlPAMVKELGKW-----KFSGFV--------GLNTLFVALCNNeafRKLDFSALKLTLSGGMALQLATAERWKEVT- 350
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  335 phGLPadaIRPAWGMSETSSGVIFS-HEFTRAGTsdddhfveIGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSG 413
Cdd:PRK05677   351 --GCA---ICEGYGMTETSPVVSVNpSQAIQVGT--------IGIPVPSTLCKVIDDDGNELPLGEVGELCVKGPQVMKG 417
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  414 YYQRPDLNESVFTEDGWFETGDLGFLR-NGRLTITGRTKDAIIINGINYYSHAIESAVEELSEIETsyTAACAVRlGQNS 492
Cdd:PRK05677   418 YWQRPEATDEILDSDGWLKTGDIALIQeDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQ--CAAIGVP-DEKS 494
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1776025254  493 TDQLAIFFV--TSAKLNDEQMSQLLRniqshvSQVIGvtpeYLLPVQ---KEEIPKTAIGKIQRTQLK 555
Cdd:PRK05677   495 GEAIKVFVVvkPGETLTKEQVMEHMR------ANLTG----YKVPKAvefRDELPTTNVGKILRRELR 552
PRK07514 PRK07514
malonyl-CoA synthase; Validated
1158-1639 5.86e-28

malonyl-CoA synthase; Validated


Pssm-ID: 181011 [Multi-domain]  Cd Length: 504  Bit Score: 121.91  E-value: 5.86e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1158 LFEQQAKKTPDRAAVSYE---GQTLTYRELDERSTQLAIYLQAHGVGP-DRLAgIYVDRSLDMLVGLLAILKAGGAYVPL 1233
Cdd:PRK07514     5 LFDALRAAFADRDAPFIEtpdGLRYTYGDLDAASARLANLLVALGVKPgDRVA-VQVEKSPEALALYLATLRAGAVFLPL 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1234 DPSYPAERLEYMLEDSE--VFIT-----LTTSELVNTLSWNGVTTalLDQDWD----EIAQTASDRKVlTRTVTPENLAY 1302
Cdd:PRK07514    84 NTAYTLAELDYFIGDAEpaLVVCdpanfAWLSKIAAAAGAPHVET--LDADGTgsllEAAAAAPDDFE-TVPRGADDLAA 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1303 VIYTSGSTGKPKGVMIPHKALTNFLVSMGETPGLTAEDKMlavttycfdIAALELF----------LPLIKGAHCYICQT 1372
Cdd:PRK07514   161 ILYTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVL---------IHALPIFhthglfvatnVALLAGASMIFLPK 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1373 EHTKDV-EKLKRdirtikPTVMQATPATWKMLFYSGWENEE---NVKILCGGEA--LPETLKRYFLDTGSEAWNMFGPTE 1446
Cdd:PRK07514   232 FDPDAVlALMPR------ATVMMGVPTFYTRLLQEPRLTREaaaHMRLFISGSAplLAETHREFQERTGHAILERYGMTE 305
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1447 TTIWSAvqriN--DECSRA-TIGRPIANTQIYITDSQL-APVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPFepg 1522
Cdd:PRK07514   306 TNMNTS----NpyDGERRAgTVGFPLPGVSLRVTDPETgAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGF--- 378
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1523 sklYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVV----ADMDNLAAYYTAKHANASLT 1598
Cdd:PRK07514   379 ---FITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIgvphPDFGEGVTAVVVPKPGAALD 455
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|.
gi 1776025254 1599 ARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLK 1639
Cdd:PRK07514   456 EAAILAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLLR 496
PRK03640 PRK03640
o-succinylbenzoate--CoA ligase;
133-556 5.91e-28

o-succinylbenzoate--CoA ligase;


Pssm-ID: 235146 [Multi-domain]  Cd Length: 483  Bit Score: 121.61  E-value: 5.91e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  133 AWTLLDKPA--VITDRGMHQEmldwakeqgLEGFRAIIVEDLL-SAEADTDWHQSSPED-LALLLLTSGSTGTPKAVMLN 208
Cdd:PRK03640    92 LWQLDDAEVkcLITDDDFEAK---------LIPGISVKFAELMnGPKEEAEIQEEFDLDeVATIMYTSGTTGKPKGVIQT 162
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  209 HRN-IMSMVKGIIQMqGFTREDitfNW---MPFDHVGGIGMLhLRDVYLGCQeinvsseTILME---PLKWLDWIDHYR- 280
Cdd:PRK03640   163 YGNhWWSAVGSALNL-GLTEDD---CWlaaVPIFHISGLSIL-MRSVIYGMR-------VVLVEkfdAEKINKLLQTGGv 230
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  281 --ASVTWApnfafgLVTDFAEEIKDRKWDlSSMRYMLNGGeamvAKVGRRILELLEPHGLPadaIRPAWGMSETSSGVif 358
Cdd:PRK03640   231 tiISVVST------MLQRLLERLGEGTYP-SSFRCMLLGG----GPAPKPLLEQCKEKGIP---VYQSYGMTETASQI-- 294
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  359 sheftrAGTSDDDHFVEIGS---PIPGFSMRIVNDHNEL--VEEGEIgrfQVSGLSVTSGYYQRPDLNESVFtEDGWFET 433
Cdd:PRK03640   295 ------VTLSPEDALTKLGSagkPLFPCELKIEKDGVVVppFEEGEI---VVKGPNVTKGYLNREDATRETF-QDGWFKT 364
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  434 GDLGFL-RNGRLTITGRTKDAIIINGINYYSHAIESAVEELSEIETsytaacAVRLGqnSTDQL-----AIFFVTSAKLN 507
Cdd:PRK03640   365 GDIGYLdEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAE------AGVVG--VPDDKwgqvpVAFVVKSGEVT 436
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1776025254  508 DEQMSQLLRNIQSHvsqvigvtpeYLLPVQ---KEEIPKTAIGKIQRTQLKT 556
Cdd:PRK03640   437 EEELRHFCEEKLAK----------YKVPKRfyfVEELPRNASGKLLRHELKQ 478
PLN02836 PLN02836
3-oxoacyl-[acyl-carrier-protein] synthase
1914-2183 7.92e-28

3-oxoacyl-[acyl-carrier-protein] synthase


Pssm-ID: 215449 [Multi-domain]  Cd Length: 437  Bit Score: 120.28  E-value: 7.92e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1914 ISHKLGLRGPSYFVHANCSSsliGLHS---AYKSLLSAESDYALVGGatlhTESNI------GYVHQPGL----NFSSDG 1980
Cdd:PLN02836   167 VSIRYGFQGPNHAAVTACAT---GAHSigdAFRMIQFGDADVMVAGG----TESSIdalsiaGFSRSRALstkfNSCPTE 239
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1981 HIKAFDASADGMIGGEGVAVVLLKKAADAVKDGDHIYALLRGIGVNNDGADkvgFYAPSVKGQADV--VQQVMNQTKIHP 2058
Cdd:PLN02836   240 ASRPFDCDRDGFVIGEGAGVLVLEELEHAKRRGAKIYAEVRGYGMSGDAHH---ITQPHEDGRGAVlaMTRALQQSGLHP 316
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2059 ESICYVEAHGTGTKLGDPIELAALTNVYRQYTNkTQFCGIGSVKTNIGHLDTAAGLAGCIKVVMSLYHQELAPSINYKEP 2138
Cdd:PLN02836   317 NQVDYVNAHATSTPLGDAVEARAIKTVFSEHAT-SGGLAFSSTKGATGHLLGAAGAVEAIFSVLAIHHGIAPPTLNLERP 395
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1776025254 2139 NPNTDLASSPFyvvdqkkTLSREIQThRAALS-SFGLGGTNTHAIF 2183
Cdd:PLN02836   396 DPIFDDGFVPL-------TASKAMLI-RAALSnSFGFGGTNASLLF 433
PRK12316 PRK12316
peptide synthase; Provisional
186-1002 9.00e-28

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 125.45  E-value: 9.00e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  186 PEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDHVGGIGMLHLrdVYLGCQEINVSSETI 265
Cdd:PRK12316   654 PENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFW--PLMSGARLVVAAPGD 731
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  266 LMEPLKWLDWIDHYRASVTwapNFAFGLVTDFAEEIKDRkwDLSSMRYMLNGGEAMVAKVGRRILELLephglPADAIRP 345
Cdd:PRK12316   732 HRDPAKLVELINREGVDTL---HFVPSMLQAFLQDEDVA--SCTSLRRIVCSGEALPADAQEQVFAKL-----PQAGLYN 801
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  346 AWGMSETSSGVIFSHEFTRAGTSdddhfVEIGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGYYQRPDLNESVF 425
Cdd:PRK12316   802 LYGPTEAAIDVTHWTCVEEGGDS-----VPIGRPIANLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERF 876
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  426 TEDGW------FETGDLGFLR-NGRLTITGRTKDAIIINGINYyshaiesaveELSEIETSYTAACAVR----LGQnSTD 494
Cdd:PRK12316   877 VPSPFvagermYRTGDLARYRaDGVIEYAGRIDHQVKLRGLRI----------ELGEIEARLLEHPWVReaavLAV-DGK 945
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  495 QLAIFFVTSAKLNDeqmsqLLRNIQSHVSQVIgvtPEYLLPVQ---KEEIPKTAIGKIQRTQLKtsfengefdhllhKPn 571
Cdd:PRK12316   946 QLVGYVVLESEGGD-----WREALKAHLAASL---PEYMVPAQwlaLERLPLTPNGKLDRKALP-------------AP- 1003
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  572 rmndavqDEEMQQADHVKRvREEIQEHLLTCLTEELHVSRdwVEPNANIQSLGVNSIKMMKLIrSIEKNYHIKLTAREIH 651
Cdd:PRK12316  1004 -------EASVAQQGYVAP-RNALERTLAAIWQDVLGVER--VGLDDNFFELGGDSIVSIQVV-SRARQAGIQLSPRDLF 1072
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  652 QYPTIERLAsylsehedlssSSADKKGTDTYKTEPERSQAtfqPLSEVQKglWTLQKMSPEKSAYHVPLCFKFSSGLHLE 731
Cdd:PRK12316  1073 QHQTIRSLA-----------LVAKAGQATAADQGPASGEV---ALAPVQR--WFFEQAIPQRQHWNQSLLLQARQPLDPD 1136
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  732 TLQQAFGLVLNQHPILKHVIQEKDGvpilKNEPALSIEIKTENI---SSMKESDIPAfLRKKVKEPYVKENSPLVRVMSF 808
Cdd:PRK12316  1137 RLGRALERLVAHHDALRLRFREEDG----GWQQAYAAPQAGEVLwqrQAASEEELLA-LCEEAQRSLDLEQGPLLRALLV 1211
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  809 SRSEQEHFLLVVIHHLIFDGVSSVTFIHSLFDTYQLLLkgqqpeiAVSPAIYHDFAAWEKNM--LAGKDGvKHRTYWQKQ 886
Cdd:PRK12316  1212 DMADGSQRLLLVIHHLVVDGVSWRILLEDLQRAYADLD-------ADLPARTSSYQAWARRLheHAGARA-EELDYWQAQ 1283
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  887 LSGTlpNLQLPKVSASSVSEFR-EDTYTRRLSSGFMNQVRMFA-KEHSVNVTTVFLSCYMMLLGRYTGQKEQIVGMPAMV 964
Cdd:PRK12316  1284 LEDA--PHELPCENPDGALENRhERKLELRLDAERTRQLLQEApAAYRTQVNDLLLTALARVTCRWSGQASVLVQLEGHG 1361
                          810       820       830       840
                   ....*....|....*....|....*....|....*....|....*
gi 1776025254  965 RpEERFDD-----AIGHFLNMLPIRseLNPADTFSSFIS--KLQL 1002
Cdd:PRK12316  1362 R-EDLFEDidlsrTVGWFTSLFPVR--LTPAADLGESIKaiKEQL 1403
PRK07103 PRK07103
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
1914-2179 9.10e-28

polyketide beta-ketoacyl:acyl carrier protein synthase; Validated


Pssm-ID: 180839 [Multi-domain]  Cd Length: 410  Bit Score: 119.75  E-value: 9.10e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1914 ISHKLGLRGPSYFVHANCSSSLIGLHSAYKSLLSAESDYALVGGATLHtesnIGYVHQPGL---------NFSSDGHI-- 1982
Cdd:PRK07103   150 CSEQFGIRGEGFTVGGASASGQLAVIQAARLVQSGSVDACIAVGALMD----LSYWECQALrslgamgsdRFADEPEAac 225
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1983 KAFDASADGMIGGEGVAVVLLKKAADAVKDGDHIYALLRGIGVNNDGADKVgfyAPSVKGQADVVQQVMNQTKIHPESIC 2062
Cdd:PRK07103   226 RPFDQDRDGFIYGEACGAVVLESAESARRRGARPYAKLLGWSMRLDANRGP---DPSLEGEMRVIRAALRRAGLGPEDID 302
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2063 YVEAHGTGTKLGDPIELAALTNVY--RQYTNKTqfcgigsvKTNIGHLDTAAGLAGCIKVVMSLYHQELAPSINYKEPNP 2140
Cdd:PRK07103   303 YVNPHGTGSPLGDETELAALFASGlaHAWINAT--------KSLTGHGLSAAGIVELIATLLQMRAGFLHPSRNLDEPID 374
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1776025254 2141 NTdlasspFYVVDQKktlSREIQTHRAALSSFGLGGTNT 2179
Cdd:PRK07103   375 ER------FRWVGST---AESARIRYALSLSFGFGGINT 404
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
184-560 9.91e-28

The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341242 [Multi-domain]  Cd Length: 481  Bit Score: 120.73  E-value: 9.91e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  184 SSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMP--FDhvggigmLHLRDVYL-----GCq 256
Cdd:cd05918    103 SSPSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGLTSESRVLQFASytFD-------VSILEIFTtlaagGC- 174
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  257 eINVSSETILMEPLkwLDWIDHYRasVTWA---PNFAFGLvtdfaeeikDRKwDLSSMRYMLNGGEAMVAKVgrrilelL 333
Cdd:cd05918    175 -LCIPSEEDRLNDL--AGFINRLR--VTWAfltPSVARLL---------DPE-DVPSLRTLVLGGEALTQSD-------V 232
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  334 EPHGLPADAIRpAWGMSETSsgvIFShefTRAGTSDDDHFVEIGSPIPGfSMRIVN--DHNELVEEGEIGRFQVSGLSVT 411
Cdd:cd05918    233 DTWADRVRLIN-AYGPAECT---IAA---TVSPVVPSTDPRNIGRPLGA-TCWVVDpdNHDRLVPIGAVGELLIEGPILA 304
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  412 SGYYQRPDLNESVFTED-GW------------FETGDLG-FLRNGRLTITGRTKDAIIINGINYYSHAIESAVEELSEIE 477
Cdd:cd05918    305 RGYLNDPEKTAAAFIEDpAWlkqegsgrgrrlYRTGDLVrYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGA 384
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  478 TSYTAACAVRLGQNSTDQLAIFFVTS------------AKLNDEQMSQLLRNIQSHVSQVIgvtPEY-----LLPVQkeE 540
Cdd:cd05918    385 KEVVVEVVKPKDGSSSPQLVAFVVLDgsssgsgdgdslFLEPSDEFRALVAELRSKLRQRL---PSYmvpsvFLPLS--H 459
                          410       420
                   ....*....|....*....|
gi 1776025254  541 IPKTAIGKIQRTQLKTSFEN 560
Cdd:cd05918    460 LPLTASGKIDRRALRELAES 479
cond_enzymes cd00327
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ...
1855-2182 1.32e-27

Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) Claisen-like condensation reaction. Members are share strong structural similarity, and are involved in the synthesis and degradation of fatty acids, and the production of polyketides, a diverse group of natural products.


Pssm-ID: 238201 [Multi-domain]  Cd Length: 254  Bit Score: 115.23  E-value: 1.32e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1855 KAIEDAGYAAGQIPQTSVfmsasnnsyrallpsdttesletpdGYVSWVLAQSGTIPTMISHKLGLRGPSYFVHANCSSS 1934
Cdd:cd00327     17 QAIADAGLSKGPIVGVIV-------------------------GTTGGSGEFSGAAGQLAYHLGISGGPAYSVNQACATG 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1935 LIGLHSAYKSLLSAESDYALVGGatlhtesnigyvhqpglnfssdghikaFDASadgmIGGEGVAVVLLKKAADAVKDGD 2014
Cdd:cd00327     72 LTALALAVQQVQNGKADIVLAGG---------------------------SEEF----VFGDGAAAAVVESEEHALRRGA 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2015 HIYALLRGIGVNNDGADKVgfYAPSVKGQADVVQQVMNQTKIHPESICYVEAHGTGTKLGDPIELAALTNVYRQytnktQ 2094
Cdd:cd00327    121 HPQAEIVSTAATFDGASMV--PAVSGEGLARAARKALEGAGLTPSDIDYVEAHGTGTPIGDAVELALGLDPDGV-----R 193
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2095 FCGIGSVKTNIGHLDTAAGLAGCIKVVMSLYHQElapsinykepnpntdlasspfyvvdqKKTLSREIQThrAALSSFGL 2174
Cdd:cd00327    194 SPAVSATLIMTGHPLGAAGLAILDELLLMLEHEF--------------------------IPPTPREPRT--VLLLGFGL 245

                   ....*...
gi 1776025254 2175 GGTNTHAI 2182
Cdd:cd00327    246 GGTNAAVV 253
PRK13383 PRK13383
acyl-CoA synthetase; Provisional
1118-1638 1.47e-27

acyl-CoA synthetase; Provisional


Pssm-ID: 139531 [Multi-domain]  Cd Length: 516  Bit Score: 120.87  E-value: 1.47e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1118 MLNPSQPLKEYSLLPEAEKqmilktwnatGKTYPYItfheLFEQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQA 1197
Cdd:PRK13383    14 LLNPPSPRAVLRLLREASR----------GGTNPYT----LLAVTAARWPGRTAIIDDDGALSYRELQRATESLARRLTR 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1198 HGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLEDSEVFITLTTSELVNTLSWNGVTTALLDqd 1277
Cdd:PRK13383    80 DGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAALRAHHISTVVADNEFAERIAGADDAVAVID-- 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1278 wdeiAQTASDRKVLTRTVTPENLAYVIYTSGSTGKPKGVmiPHK----ALTNFLVSMGETPGLTAEDKMLAVTTYCFDIA 1353
Cdd:PRK13383   158 ----PATAGAEESGGRPAVAAPGRIVLLTSGTTGKPKGV--PRApqlrSAVGVWVTILDRTRLRTGSRISVAMPMFHGLG 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1354 ALELFLPLIKG----------AHCYICQTE-HTKD----VEKLKRDIRTIKPTVMQATPATWKMLfysgweneenvkILC 1418
Cdd:PRK13383   232 LGMLMLTIALGgtvlthrhfdAEAALAQASlHRADaftaVPVVLARILELPPRVRARNPLPQLRV------------VMS 299
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1419 GGEALPETLKRYFLDT-GSEAWNMFGPTETTIWSAVQRINDECSRATIGRPIANTQIYITDSQLAPVPAGVPGELCIAGd 1497
Cdd:PRK13383   300 SGDRLDPTLGQRFMDTyGDILYNGYGSTEVGIGALATPADLRDAPETVGKPVAGCPVRILDRNNRPVGPRVTGRIFVGG- 378
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1498 gvakgyykkeELTDSRFIDNpfepGSK-----LYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGI 1572
Cdd:PRK13383   379 ----------ELAGTRYTDG----GGKavvdgMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAV 444
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1776025254 1573 LECVVVADMDN-----LAAYYTAkHANASLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSL 1638
Cdd:PRK13383   445 ADNAVIGVPDErfghrLAAFVVL-HPGSGVDAAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
PRK07103 PRK07103
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
3340-3777 2.45e-27

polyketide beta-ketoacyl:acyl carrier protein synthase; Validated


Pssm-ID: 180839 [Multi-domain]  Cd Length: 410  Bit Score: 118.21  E-value: 2.45e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3340 PVAIVGISGRFPGAMDIDEFWKNLEEGKDSITEVpkdrwdwrEHYGNPD---TDVNKTDIKWGGFIDGVAEFDPLFFGIS 3416
Cdd:PRK07103     3 EVVVTGVGVVSAIGQGRPSFAAALLAGRHAFGVM--------RRPGRQVpddAGAGLASAFIGAELDSLALPERLDAKLL 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3417 pREADYvdPQQRLLMTyVWKALEDAGCPPqsLSGTGTGIFIGTGNTGYKDLF--HRANlpiEGHAAtgHMIPSVGPNRM- 3493
Cdd:PRK07103    75 -RRASL--SAQAALAA-AREAWRDAALGP--VDPDRIGLVVGGSNLQQREQAlvHETY---RDRPA--FLRPSYGLSFMd 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3494 -------SYFLNIHGPSEPVETACSSSLVAIHRAVTAMQNGDCEMAIAGGVNTILTEEAHISYSKAGMLSKDGR------ 3560
Cdd:PRK07103   144 tdlvglcSEQFGIRGEGFTVGGASASGQLAVIQAARLVQSGSVDACIAVGALMDLSYWECQALRSLGAMGSDRFadepea 223
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3561 -CKTFSADANGYVRGEGVGMVMLKKLEDAERDGNHIYGVIRGTAENHGgrANTLTSPNPKAQADLLVRAYRQAGIDPSTV 3639
Cdd:PRK07103   224 aCRPFDQDRDGFIYGEACGAVVLESAESARRRGARPYAKLLGWSMRLD--ANRGPDPSLEGEMRVIRAALRRAGLGPEDI 301
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3640 TYIEAHGTGTELGDPIEINGLKAAfkelsnmrGESQPdvpdhrcGIGSVKSNIGHLELAAGISGLIKVLLQMKHktlvKS 3719
Cdd:PRK07103   302 DYVNPHGTGSPLGDETELAALFAS--------GLAHA-------WINATKSLTGHGLSAAGIVELIATLLQMRA----GF 362
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1776025254 3720 LHcetlnPYLQLT---DSPFYIVQEKQEWKSVtdcdgnelpRRAGISSFGIGGVNAHIVIE 3777
Cdd:PRK07103   363 LH-----PSRNLDepiDERFRWVGSTAESARI---------RYALSLSFGFGGINTALVLE 409
A_NRPS_AB3403-like cd17646
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ...
32-554 2.50e-27

Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341301 [Multi-domain]  Cd Length: 488  Bit Score: 119.69  E-value: 2.50e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254   32 PEVLYRTAAELGDTKGIIYlqpDGTEVyqSYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNSQLLPAFWGCVLTGVVP 111
Cdd:cd17646      1 HALVAEQAARTPDAPAVVD---EGRTL--TYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAY 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  112 APLavPPTYAEsssgtQKLkdAWTLLDKPA--VITDRGMhqemLDWAkeqGLEGFRAIIVEDLLSAEADTD-WHQSSPED 188
Cdd:cd17646     76 LPL--DPGYPA-----DRL--AYMLADAGPavVLTTADL----AARL---PAGGDVALLGDEALAAPPATPpLVPPRPDN 139
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  189 LALLLLTSGSTGTPKAVMLNHRNImsmVKGIIQMQ---GFTRED-------ITFN------WMPFDHVGGIGM----LHl 248
Cdd:cd17646    140 LAYVIYTSGSTGRPKGVMVTHAGI---VNRLLWMQdeyPLGPGDrvlqktpLSFDvsvwelFWPLVAGARLVVarpgGH- 215
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  249 RDV-YLgcqeinvssetilmeplkwLDWIDHYRASVTwapNFAFGLVTDFAEEIKDRKWDlsSMRYMLNGGEAMVAKVGR 327
Cdd:cd17646    216 RDPaYL-------------------AALIREHGVTTC---HFVPSMLRVFLAEPAAGSCA--SLRRVFCSGEALPPELAA 271
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  328 RILELL--EPHGLpadairpaWGMSETSSGVifSHEFTRAGTsdDDHFVEIGSPIPGFSMRIVNDHNELVEEGEIGRFQV 405
Cdd:cd17646    272 RFLALPgaELHNL--------YGPTEAAIDV--THWPVRGPA--ETPSVPIGRPVPNTRLYVLDDALRPVPVGVPGELYL 339
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  406 SGLSVTSGYYQRPDLNESVFTEDgWFE-------TGDLG-FLRNGRLTITGRTKDAIIINGinyysHAIesaveELSEIE 477
Cdd:cd17646    340 GGVQLARGYLGRPALTAERFVPD-PFGpgsrmyrTGDLArWRPDGALEFLGRSDDQVKIRG-----FRV-----EPGEIE 408
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  478 TSYTA------ACAVRLGQNSTDQLAIFFVTSAKLNDEQMSQLLRniqSHVSQVIgvtPEYLLP---VQKEEIPKTAIGK 548
Cdd:cd17646    409 AALAAhpavthAVVVARAAPAGAARLVGYVVPAAGAAGPDTAALR---AHLAERL---PEYMVPaafVVLDALPLTANGK 482

                   ....*.
gi 1776025254  549 IQRTQL 554
Cdd:cd17646    483 LDRAAL 488
PRK08633 PRK08633
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
156-449 2.82e-27

2-acyl-glycerophospho-ethanolamine acyltransferase; Validated


Pssm-ID: 236315 [Multi-domain]  Cd Length: 1146  Bit Score: 123.11  E-value: 2.82e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  156 AKEQGLEGFRAIIVEDLLSAEADTDW--HQSSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFN 233
Cdd:PRK08633   749 AKISKVDKLTALLAARLLPARLLKRLygPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILS 828
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  234 WMPFDHVGGIGMLHLRDVYLGCQEINVSSETilmEPLKWLDWIDHYRASVTWA-PNFaFGLvtdFAEEIKDRKWDLSSMR 312
Cdd:PRK08633   829 SLPFFHSFGLTVTLWLPLLEGIKVVYHPDPT---DALGIAKLVAKHRATILLGtPTF-LRL---YLRNKKLHPLMFASLR 901
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  313 YMLNGGE--------AMVAKVGRRILEllephglpadairpAWGMSETS-----------SGVIFSHEFTRAGTsdddhf 373
Cdd:PRK08633   902 LVVAGAEklkpevadAFEEKFGIRILE--------------GYGATETSpvasvnlpdvlAADFKRQTGSKEGS------ 961
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  374 veIGSPIPGFSMRIVN-DHNELVEEGEIGRFQVSGLSVTSGYYQRPDLNESVFTE---DGWFETGDLGFL-RNGRLTITG 448
Cdd:PRK08633   962 --VGMPLPGVAVRIVDpETFEELPPGEDGLILIGGPQVMKGYLGDPEKTAEVIKDidgIGWYVTGDKGHLdEDGFLTITD 1039

                   .
gi 1776025254  449 R 449
Cdd:PRK08633  1040 R 1040
PRK08633 PRK08633
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
1291-1641 3.75e-27

2-acyl-glycerophospho-ethanolamine acyltransferase; Validated


Pssm-ID: 236315 [Multi-domain]  Cd Length: 1146  Bit Score: 122.73  E-value: 3.75e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1291 LTRTVTPENLAYVIYTSGSTGKPKGVMIPHKALTNFLVSMGETPGLTAEDKMLAVTT--YCFDIAAlELFLPLIKGAHCy 1368
Cdd:PRK08633   775 YGPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLPffHSFGLTV-TLWLPLLEGIKV- 852
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1369 ICQTEHTkDVEKLKRDIRTIKPTVMQATPaTWKMLFysgwenEENVKI-----------LCGGEALPETLKRYFLDT-GS 1436
Cdd:PRK08633   853 VYHPDPT-DALGIAKLVAKHRATILLGTP-TFLRLY------LRNKKLhplmfaslrlvVAGAEKLKPEVADAFEEKfGI 924
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1437 EAWNMFGPTETTIWSAVQ----RINDE-----CSRATIGRPIANTQIYITD-SQLAPVPAGVPGELCIAGDGVAKGYYKK 1506
Cdd:PRK08633   925 RILEGYGATETSPVASVNlpdvLAADFkrqtgSKEGSVGMPLPGVAVRIVDpETFEELPPGEDGLILIGGPQVMKGYLGD 1004
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1507 EELTDS--RFIDnpfepGSKLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSE--HPGILECVVVADMD 1582
Cdd:PRK08633  1005 PEKTAEviKDID-----GIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKalGGEEVVFAVTAVPD 1079
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1776025254 1583 nlaayytAK--------HANASLTARELRHFVKNA-LPAYMVPSYFIQLDHMPLTPNGKIDRNSLKNI 1641
Cdd:PRK08633  1080 -------EKkgeklvvlHTCGAEDVEELKRAIKESgLPNLWKPSRYFKVEALPLLGSGKLDLKGLKEL 1140
BCL_like cd05919
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ...
50-555 4.01e-27

Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.


Pssm-ID: 341243 [Multi-domain]  Cd Length: 436  Bit Score: 118.33  E-value: 4.01e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254   50 YLQPDGTevyQSYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNSQLLPAFWGCVLTGVVPA---PLAVPPTYAESSSG 126
Cdd:cd05919      4 FYAADRS---VTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVvinPLLHPDDYAYIARD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  127 TQKlkdawtlldkpavitdrgmhqemldwakeqglegfRAIIVEDllsaeadtdwhqsspEDLALLLLTSGSTGTPKAVM 206
Cdd:cd05919     81 CEA-----------------------------------RLVVTSA---------------DDIAYLLYSSGTTGPPKGVM 110
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  207 LNHRNIMSMVKGI-IQMQGFTREDITFNW--MPFdhvgGIGMLHlrDVYLGCQeinVSSETILMEplkwlDWIDHYRASV 283
Cdd:cd05919    111 HAHRDPLLFADAMaREALGLTPGDRVFSSakMFF----GYGLGN--SLWFPLA---VGASAVLNP-----GWPTAERVLA 176
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  284 TWA---PNFAFGLVTDFAEEIKDRKW---DLSSMRYMLNGGEAMVAKVGRRileLLEPHGLP-ADAIrpawGMSETssGV 356
Cdd:cd05919    177 TLArfrPTVLYGVPTFYANLLDSCAGspdALRSLRLCVSAGEALPRGLGER---WMEHFGGPiLDGI----GATEV--GH 247
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  357 IF---SHEFTRAGTSdddhfveiGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGYYQRPDLNESVFtEDGWFET 433
Cdd:cd05919    248 IFlsnRPGAWRLGST--------GRPVPGYEIRLVDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATF-NGGWYRT 318
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  434 GDL-GFLRNGRLTITGRTKDAIIINGINYYSHAIESAVeelseIETSYTAACAVRLGQNSTD--QLAIFFVtsakLNDEQ 510
Cdd:cd05919    319 GDKfCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLI-----IQHPAVAEAAVVAVPESTGlsRLTAFVV----LKSPA 389
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|
gi 1776025254  511 MSQ--LLRNIQSHVSQVIgvtPEYLLPVQ---KEEIPKTAIGKIQRTQLK 555
Cdd:cd05919    390 APQesLARDIHRHLLERL---SAHKVPRRiafVDELPRTATGKLQRFKLR 436
MACS_AAE_MA_like cd05970
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ...
1163-1642 4.59e-27

Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.


Pssm-ID: 341274 [Multi-domain]  Cd Length: 537  Bit Score: 119.52  E-value: 4.59e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1163 AKKTPDRAAVSY-----EGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSY 1237
Cdd:cd05970     27 AKEYPDKLALVWcddagEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQL 106
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1238 PAERLEYMLEDSEVFITLTTSE---------------LVNTLSWNG--VTTALLDQDwDEIAQTASDRKVLTRTVTP--E 1298
Cdd:cd05970    107 TAKDIVYRIESADIKMIVAIAEdnipeeiekaapecpSKPKLVWVGdpVPEGWIDFR-KLIKNASPDFERPTANSYPcgE 185
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1299 NLAYVIYTSGSTGKPKgvMIPHkaltNFLVSMGETpgLTAE--------DKMLAVTTYCFDIAAL-ELFLPLIKGAHCYI 1369
Cdd:cd05970    186 DILLVYFSSGTTGMPK--MVEH----DFTYPLGHI--VTAKywqnvregGLHLTVADTGWGKAVWgKIYGQWIAGAAVFV 257
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1370 cqTEHTK-DVEKLKRDIRTIKPTVMQATPATWKMLFYSGWENEENVKI---LCGGEAL-PETLKRYFLDTGSEAWNMFGP 1444
Cdd:cd05970    258 --YDYDKfDPKALLEKLSKYGVTTFCAPPTIYRFLIREDLSRYDLSSLrycTTAGEALnPEVFNTFKEKTGIKLMEGFGQ 335
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1445 TETTIWSAVQRINdECSRATIGRPIANTQIYITDSQLAPVPAGVPGELCIAGD-----GVAKGYYKKEELTDSRFIDNpf 1519
Cdd:cd05970    336 TETTLTIATFPWM-EPKPGSMGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTSkgkpvGLFGGYYKDAEKTAEVWHDG-- 412
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1520 epgskLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMDN-----------LAAYY 1588
Cdd:cd05970    413 -----YYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPirgqvvkativLAKGY 487
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1776025254 1589 TAKHAnasLTaRELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLKNID 1642
Cdd:cd05970    488 EPSEE---LK-KELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEIRERD 537
PRK06333 PRK06333
beta-ketoacyl-ACP synthase;
1778-2187 5.60e-27

beta-ketoacyl-ACP synthase;


Pssm-ID: 235781 [Multi-domain]  Cd Length: 424  Bit Score: 117.41  E-value: 5.60e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1778 DEFWENLRDGKESIAFfnkeelqrfgISKEIAEN-----ADYVPAKASiEGKDRFDPSFFqISPKDAEFMDPQLRMLLTH 1852
Cdd:PRK06333    22 ETFWQRLLAGQSGIRT----------LTDFPVGDlatkiGGQVPDLAE-DAEAGFDPDRY-LDPKDQRKMDRFILFAMAA 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1853 SWKAIEDAGYAAGQIPQ---TSVFMSASNNSYRALlpsdtTESLETPDgyvswvlaQSG-------TIPTM--------I 1914
Cdd:PRK06333    90 AKEALAQAGWDPDTLEDrerTATIIGSGVGGFPAI-----AEAVRTLD--------SRGprrlspfTIPSFltnmaaghV 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1915 SHKLGLRGPSYFVHANCSSSLIGLHSAYKSLLSAESDYALVGGatlhTESNIGYVHQPGLN----FSS---DGHIKA--- 1984
Cdd:PRK06333   157 SIRYGFKGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGG----TEAAIDRVSLAGFAaaraLSTrfnDAPEQAsrp 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1985 FDASADGMIGGEGVAVVLLKKAADAVKDGDHIYALLRGIGVNNDgADKVGFYAPSVKGQADVVQQVMNQTKIHPESICYV 2064
Cdd:PRK06333   233 FDRDRDGFVMGEGAGILVIETLEHALARGAPPLAELVGYGTSAD-AYHMTAGPEDGEGARRAMLIALRQAGIPPEEVQHL 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2065 EAHGTGTKLGDPIELAALTNVYRQYTNktqfCGIGSVKTNIGHLDTAAGLAGCIKVVMSLYHQELAPSINYKEPNPNTDl 2144
Cdd:PRK06333   312 NAHATSTPVGDLGEVAAIKKVFGHVSG----LAVSSTKSATGHLLGAAGGVEAIFTILALRDQIAPPTLNLENPDPAAE- 386
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|...
gi 1776025254 2145 assPFYVVDQKktlSREIQTHRAALSSFGLGGTNTHAIFEQFK 2187
Cdd:PRK06333   387 ---GLDVVANK---ARPMDMDYALSNGFGFGGVNASILFRRWE 423
PRK05852 PRK05852
fatty acid--CoA ligase family protein;
1157-1639 7.47e-27

fatty acid--CoA ligase family protein;


Pssm-ID: 235625 [Multi-domain]  Cd Length: 534  Bit Score: 118.84  E-value: 7.47e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1157 ELFEQQAKKTPDRAA--VSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLD 1234
Cdd:PRK05852    20 DLVEVAATRLPEAPAlvVTADRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLD 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1235 PSYPAERLEYMLEDSEVFITLTTSELVN-----TLSWNGVTTALLDQDWDEIAQTASDRKVLT----RTVTPENL----A 1301
Cdd:PRK05852   100 PALPIAEQRVRSQAAGARVVLIDADGPHdraepTTRWWPLTVNVGGDSGPSGGTLSVHLDAATeptpATSTPEGLrpddA 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1302 YVIYTSGSTGKPKGVMIPHKALTNFLVSMGETPGLTAEDKMLAVTTYCFD---IAAL--------ELFLPlikgAHCYIc 1370
Cdd:PRK05852   180 MIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGhglIAALlatlasggAVLLP----ARGRF- 254
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1371 qTEHTkdvekLKRDIRTIKPTVMQATPATWKMLFYSGWENEENVKIL-------CGGEALPET---LKRYFLDTGSEAwn 1440
Cdd:PRK05852   255 -SAHT-----FWDDIKAVGATWYTAVPTIHQILLERAATEPSGRKPAalrfirsCSAPLTAETaqaLQTEFAAPVVCA-- 326
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1441 mFGPTETTIWSAVQRIN----DECSRATIGRPIANT--QIYITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRF 1514
Cdd:PRK05852   327 -FGMTEATHQVTTTQIEgigqTENPVVSTGLVGRSTgaQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANF 405
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1515 IDNPFepgsklyRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMDNL----AAYYTA 1590
Cdd:PRK05852   406 TDGWL-------RTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLygeaVAAVIV 478
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*....
gi 1776025254 1591 KHANASLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLK 1639
Cdd:PRK05852   479 PRESAPPTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAVA 527
LC_FACS_euk1 cd17639
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ...
1177-1583 7.65e-27

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.


Pssm-ID: 341294 [Multi-domain]  Cd Length: 507  Bit Score: 118.47  E-value: 7.65e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1177 QTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGgayvpldpsypaerleymledsevfITLT 1256
Cdd:cd17639      4 KYMSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQN-------------------------IPIV 58
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1257 TseLVNTLSWNGVTTALldqdwdeiAQTASdRKVLTrTVTPENLAYVIYTSGSTGKPKGVMIPHKALTNFLVSMGE--TP 1334
Cdd:cd17639     59 T--VYATLGEDALIHSL--------NETEC-SAIFT-DGKPDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDrvPE 126
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1335 GLTAEDKMLAvttycfdiaalelFLPLikgAH--------------CYIC----QTEHTKDVEKLKRDIRTIKPTVMQAT 1396
Cdd:cd17639    127 LLGPDDRYLA-------------YLPL---AHifelaaenvclyrgGTIGygspRTLTDKSKRGCKGDLTEFKPTLMVGV 190
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1397 PATW------------------KMLFYSGWENEEN------------------VK---------ILCGGEALPETLKRYF 1431
Cdd:cd17639    191 PAIWdtirkgvlaklnpmgglkRTLFWTAYQSKLKalkegpgtplldelvfkkVRaalggrlryMLSGGAPLSADTQEFL 270
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1432 LDTGSEAWNMFGPTETTIWSAVQRINDeCSRATIGRPIANTQI---------YITDsqlAPVPAGvpgELCIAGDGVAKG 1502
Cdd:cd17639    271 NIVLCPVIQGYGLTETCAGGTVQDPGD-LETGRVGPPLPCCEIklvdweeggYSTD---KPPPRG---EILIRGPNVFKG 343
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1503 YYKKEELTDSRFIDNPFepgsklYRTGDMARWLPGGRIEYIGRIDNQVKIR-GFRIELGDIESRLSEHPGILECVVVADM 1581
Cdd:cd17639    344 YYKNPEKTKEAFDGDGW------FHTGDIGEFHPDGTLKIIDRKKDLVKLQnGEYIALEKLESIYRSNPLVNNICVYADP 417

                   ..
gi 1776025254 1582 DN 1583
Cdd:cd17639    418 DK 419
X-Domain_NRPS cd19546
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ...
695-1121 7.99e-27

X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to the non-ribosomal peptide synthetase (NRPS); The X-domain is a catalytically inactive member of the Condensation (C) domain family of non-ribosomal peptide synthetase (NRPS). It has been shown to recruit oxygenases to the NRPS to perform side-chain crosslinking in the production of glycopeptide antibiotics. C-domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as this X-domain, the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, and dual E/C (epimerization and condensation) domains. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity; members of this X-domain subfamily lack the second H of this motif.


Pssm-ID: 380468 [Multi-domain]  Cd Length: 440  Bit Score: 117.58  E-value: 7.99e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  695 PLSEVQKGLWTLQKMSPEKSAYHVPLCFKFSSGLHLETLQQAFGLVLNQHPILK------------HVIQEKDGVPILKN 762
Cdd:cd19546      6 PATAGQLRTWLLARLDEETRGRHLSVALRLRGRLDRDALEAALGDVAARHEILRttfpgdggdvhqRILDADAARPELPV 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  763 EPAlsieiktenissmKESDIPAFLRKKVKEPYvkensPLVRVMS-----FSRSEQEHFLLVVIHHLIFDGVSSVTFIHS 837
Cdd:cd19546     86 VPA-------------TEEELPALLADRAAHLF-----DLTRETPwrctlFALSDTEHVLLLVVHRIAADDESLDVLVRD 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  838 LFDTYQLLLKGQQPEIAVSPAIYHDFAAWEKNMLAGKDGVK-----HRTYWQKQLSGTLPNLQLPKVSASSV-SEFREDT 911
Cdd:cd19546    148 LAAAYGARREGRAPERAPLPLQFADYALWERELLAGEDDRDsligdQIAYWRDALAGAPDELELPTDRPRPVlPSRRAGA 227
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  912 YTRRLSSGFMNQVRMFAKEHSVNVTTVFLSCYMMLLGRYTGQKEQIVGMpAMVRPEER--FDDAIGHFLNMLPIRSELNP 989
Cdd:cd19546    228 VPLRLDAEVHARLMEAAESAGATMFTVVQAALAMLLTRLGAGTDVTVGT-VLPRDDEEgdLEGMVGPFARPLALRTDLSG 306
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  990 ADTFSSFISKLQLTILDGLDHAAYPFPKMVRDLNIPRSQAGSPVFQTAFfyqnFLQSGSYQSLLSRYADFFSVDYVEYIH 1069
Cdd:cd19546    307 DPTFRELLGRVREAVREARRHQDVPFERLAELLALPPSADRHPVFQVAL----DVRDDDNDPWDAPELPGLRTSPVPLGT 382
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1776025254 1070 QEGEYELVFELWETE------EKMELNIKYNTGLFDAASISAMFDHFVYVTEQAMLNP 1121
Cdd:cd19546    383 EAMELDLSLALTERRnddgdpDGLDGSLRYAADLFDRATAAALARRLVRVLEQVAADP 440
LC_FACS_like cd17640
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ...
60-477 8.05e-27

Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341295 [Multi-domain]  Cd Length: 468  Bit Score: 117.85  E-value: 8.05e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254   60 QSYRRLWDDGLRIVKGLRQSGLKAKQSVILqLGDNS-QLLPAFWGCVLTGVVPAPLAvpptyaeSSSGTQKLkdawtlld 138
Cdd:cd17640      6 ITYKDLYQEILDFAAGLRSLGVKAGEKVAL-FADNSpRWLIADQGIMALGAVDVVRG-------SDSSVEEL-------- 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  139 kpavitdrgmhqemldwakeqglegfrAIIVEDllsAEADTDWHQSSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKG 218
Cdd:cd17640     70 ---------------------------LYILNH---SESVALVVENDSDDLATIIYTSGTTGNPKGVMLTHANLLHQIRS 119
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  219 IIQMQGFTREDITFNWMPFDHVggigMLHLRDVYL---GCQEINVSSETILmEPLKwlDWIDHYRASVtwaPNFAFGLVT 295
Cdd:cd17640    120 LSDIVPPQPGDRFLSILPIWHS----YERSAEYFIfacGCSQAYTSIRTLK-DDLK--RVKPHYIVSV---PRLWESLYS 189
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  296 DFAEEIKDRkwdlSSMRYML--------------NGGEAMVAKVGRrileLLEPHGLPadaIRPAWGMSETSsGVIFSHE 361
Cdd:cd17640    190 GIQKQVSKS----SPIKQFLflfflsggifkfgiSGGGALPPHVDT----FFEAIGIE---VLNGYGLTETS-PVVSARR 257
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  362 FTR--AGTsdddhfveIGSPIPGFSMRIVNDH-NELVEEGEIGRFQVSGLSVTSGYYQRPDLNESVFTEDGWFETGDLGF 438
Cdd:cd17640    258 LKCnvRGS--------VGRPLPGTEIKIVDPEgNVVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGWFNTGDLGW 329
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|.
gi 1776025254  439 L-RNGRLTITGRTKDAIII-NGINYYSHAIESAVEELSEIE 477
Cdd:cd17640    330 LtCGGELVLTGRAKDTIVLsNGENVEPQPIEEALMRSPFIE 370
FACL_DitJ_like cd05934
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
61-555 9.29e-27

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.


Pssm-ID: 341257 [Multi-domain]  Cd Length: 422  Bit Score: 117.01  E-value: 9.29e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254   61 SYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNSQLLPAFWGCVLTGVVPAPLAvpPTYAESSSgtqklkdawtlldkP 140
Cdd:cd05934      5 TYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPIN--TALRGDEL--------------A 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  141 AVITDRGMHqemldwakeqglegfrAIIVedllsaeadtdwhqsspeDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGII 220
Cdd:cd05934     69 YIIDHSGAQ----------------LVVV------------------DPASILYTSGTTGPPKGVVITHANLTFAGYYSA 114
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  221 QMQGFTREDITFNWMPFDHVGGIGMLHLRDVYLGCqeinvsseTILMEPL----KWLDWIDHYRASVTWAPNFAFGLVTD 296
Cdd:cd05934    115 RRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGA--------TLVLLPRfsasRFWSDVRRYGATVTNYLGAMLSYLLA 186
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  297 FAEEIKDRKWDLSsmrymlnggEAMVAKVGRRIL-ELLEPHGLPadaIRPAWGMSETSSGVIFSHEFTRAGTSdddhfve 375
Cdd:cd05934    187 QPPSPDDRAHRLR---------AAYGAPNPPELHeEFEERFGVR---LLEGYGMTETIVGVIGPRDEPRRPGS------- 247
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  376 IGSPIPGFSMRIVNDHNELVEEGEIGRFQV---SGLSVTSGYYQRPDLNESVFtEDGWFETGDLGFLR-NGRLTITGRTK 451
Cdd:cd05934    248 IGRPAPGYEVRIVDDDGQELPAGEPGELVIrglRGWGFFKGYYNMPEATAEAM-RNGWFHTGDLGYRDaDGFFYFVDRKK 326
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  452 DAIIINGINYYSHAIESAVEELSEIETSytAACAVRlGQNSTDQLAIFFVT--SAKLNDEQMSQLLRniqshvsqviGVT 529
Cdd:cd05934    327 DMIRRRGENISSAEVERAILRHPAVREA--AVVAVP-DEVGEDEVKAVVVLrpGETLDPEELFAFCE----------GQL 393
                          490       500
                   ....*....|....*....|....*....
gi 1776025254  530 PEYLLP--VQ-KEEIPKTAIGKIQRTQLK 555
Cdd:cd05934    394 AYFKVPryIRfVDDLPKTPTEKVAKAQLR 422
FADD10 cd17635
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ...
187-551 9.57e-27

adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.


Pssm-ID: 341290 [Multi-domain]  Cd Length: 340  Bit Score: 115.05  E-value: 9.57e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  187 EDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQ-GFTREDITFNWMPFDHVGgiGMLHLRDVYLGCQEINVSSETI 265
Cdd:cd17635      1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGlNWVVGDVTYLPLPATHIG--GLWWILTCLIHGGLCVTGGENT 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  266 LMEPLkwLDWIDHYRASVT-WAPNFAFGLVTDFAEEIKDRKwdlsSMRYMLNGGEAMVAKVGRRILellephGLPADAIR 344
Cdd:cd17635     79 TYKSL--FKILTTNAVTTTcLVPTLLSKLVSELKSANATVP----SLRLIGYGGSRAIAADVRFIE------ATGLTNTA 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  345 PAWGMSETSSGVIFSHEftragtSDDDHFVEIGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGYYQRPDLNESV 424
Cdd:cd17635    147 QVYGLSETGTALCLPTD------DDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEV 220
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  425 FTeDGWFETGDLGFLR-NGRLTITGRTKDAIIINGINYYSHAIESAVEELSEIEtsyTAACAvRLGQNSTDQLAIFFVTS 503
Cdd:cd17635    221 LI-DGWVNTGDLGERReDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQ---ECACY-EISDEEFGELVGLAVVA 295
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1776025254  504 AKLNDEQMsqllrnIQSHVSQVIGVTPEYLLP---VQKEEIPKTAIGKIQR 551
Cdd:cd17635    296 SAELDENA------IRALKHTIRRELEPYARPstiVIVTDIPRTQSGKVKR 340
PRK06501 PRK06501
beta-ketoacyl-ACP synthase;
3508-3776 1.25e-26

beta-ketoacyl-ACP synthase;


Pssm-ID: 235817 [Multi-domain]  Cd Length: 425  Bit Score: 116.65  E-value: 1.25e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3508 TACSSSLVAIHRAVTAMQNGDCEMAIAGGVNTILTEEAHISYSKAGMLSK-----DGRCKTFSADANGYVRGEGVGMVML 3582
Cdd:PRK06501   173 TACASGATAIQLGVEAIRRGETDRALCIATDGSVSAEALIRFSLLSALSTqndppEKASKPFSKDRDGFVMAEGAGALVL 252
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3583 KKLEDAERDGNHIYGVIRGTAENHGGRANTLTSPNPKAQADLLVRAYRQAGIDPSTVTYIEAHGTGTELGDPIEINGLKA 3662
Cdd:PRK06501   253 ESLESAVARGAKILGIVAGCGEKADSFHRTRSSPDGSPAIGAIRAALADAGLTPEQIDYINAHGTSTPENDKMEYLGLSA 332
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3663 AFkelsnmrGESQPDVPdhrcgIGSVKSNIGHLELAAGISGLIKVLLQMKHKTLVKSLHCETLNPYLqltdsPFYIVQEK 3742
Cdd:PRK06501   333 VF-------GERLASIP-----VSSNKSMIGHTLTAAGAVEAVFSLLTIQTGRLPPTINYDNPDPAI-----PLDVVPNV 395
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1776025254 3743 QEWKSVTDCDGNelprragisSFGIGGVNAHIVI 3776
Cdd:PRK06501   396 ARDARVTAVLSN---------SFGFGGQNASLVL 420
AFD_YhfT-like cd17633
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ...
1299-1635 2.90e-26

fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain


Pssm-ID: 341288 [Multi-domain]  Cd Length: 320  Bit Score: 112.88  E-value: 2.90e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1299 NLAYVIYTSGSTGKPKGVMIPHKAltnFLVSMGETPGL---TAEDKMLAVTTYCFDIAALELFLPLIKGAHCYICQTEHT 1375
Cdd:cd17633      1 NPFYIGFTSGTTGLPKAYYRSERS---WIESFVCNEDLfniSGEDAILAPGPLSHSLFLYGAISALYLGGTFIGQRKFNP 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1376 KdveKLKRDIRTIKPTVMQATPATWKMLfYSGWENEENVK-ILCGGEALPET----LKRYFLDtgSEAWNMFGPTETTI- 1449
Cdd:cd17633     78 K---SWIRKINQYNATVIYLVPTMLQAL-ARTLEPESKIKsIFSSGQKLFEStkkkLKNIFPK--ANLIEFYGTSELSFi 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1450 -WSAVQrinDECSRATIGRPIANTQIYITDSQlapvpAGVPGELCIAGDGVAKGYYKKEELtdsrfidNPFEPgsklYRT 1528
Cdd:cd17633    152 tYNFNQ---ESRPPNSVGRPFPNVEIEIRNAD-----GGEIGKIFVKSEMVFSGYVRGGFS-------NPDGW----MSV 212
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1529 GDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMDN-----LAAYYTAKhanaSLTARELR 1603
Cdd:cd17633    213 GDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDArfgeiAVALYSGD----KLTYKQLK 288
                          330       340       350
                   ....*....|....*....|....*....|..
gi 1776025254 1604 HFVKNALPAYMVPSYFIQLDHMPLTPNGKIDR 1635
Cdd:cd17633    289 RFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
ttLC_FACS_AEE21_like cd12118
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ...
1160-1640 3.55e-26

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.


Pssm-ID: 341283 [Multi-domain]  Cd Length: 486  Bit Score: 116.24  E-value: 3.55e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1160 EQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPA 1239
Cdd:cd12118     11 ERAAAVYPDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDA 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1240 ERLEYMLEDSEVFITLTTSELVntlswngvTTALLDQ--DWDEIAQTASDRKVLTrtvtpenlayVIYTSGSTGKPKGVM 1317
Cdd:cd12118     91 EEIAFILRHSEAKVLFVDREFE--------YEDLLAEgdPDFEWIPPADEWDPIA----------LNYTSGTTGRPKGVV 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1318 IPHK-----ALTNFLVS-MGETPGLTAEDKMLAVTTYCF--DIAAlelflplIKGAHcyICQteHTKDVEKLKRDIRTIK 1389
Cdd:cd12118    153 YHHRgaylnALANILEWeMKQHPVYLWTLPMFHCNGWCFpwTVAA-------VGGTN--VCL--RKVDAKAIYDLIEKHK 221
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1390 PTVMQATPATWKMLFYSGWENEEN----VKILCGGEALPETLKRYFLDTGSEAWNMFGPTETT------IWSAVQrinDE 1459
Cdd:cd12118    222 VTHFCGAPTVLNMLANAPPSDARPlphrVHVMTAGAPPPAAVLAKMEELGFDVTHVYGLTETYgpatvcAWKPEW---DE 298
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1460 CSRATIGRPIANTQI-YITDSQLA--------PVPA-GVP-GELCIAGDGVAKGYYKKEELTDSRFIDNPFepgsklyRT 1528
Cdd:cd12118    299 LPTEERARLKARQGVrYVGLEEVDvldpetmkPVPRdGKTiGEIVFRGNIVMKGYLKNPEATAEAFRGGWF-------HS 371
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1529 GDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMDN-----LAAYYTAKHAnASLTARELR 1603
Cdd:cd12118    372 GDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEkwgevPCAFVELKEG-AKVTEEEII 450
                          490       500       510
                   ....*....|....*....|....*....|....*..
gi 1776025254 1604 HFVKNALPAYMVPSYFIqLDHMPLTPNGKIDRNSLKN 1640
Cdd:cd12118    451 AFCREHLAGFMVPKTVV-FGELPKTSTGKIQKFVLRD 486
FCS cd05921
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ...
61-445 3.87e-26

Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.


Pssm-ID: 341245 [Multi-domain]  Cd Length: 561  Bit Score: 117.15  E-value: 3.87e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254   61 SYRRLWDDGLRIVKGLRQSGLKAKQSVILqLGDNS--QLLPAFwGCVLTGVVPAPlaVPPTYAESSSGTQKLKDAWTLLd 138
Cdd:cd05921     27 TYAEALRQVRAIAQGLLDLGLSAERPLLI-LSGNSieHALMAL-AAMYAGVPAAP--VSPAYSLMSQDLAKLKHLFELL- 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  139 KPAVI--TDRGMHQEMLDWAKEQGL---------EGFRAIIVEDLLS----AEADTDWHQSSPEDLALLLLTSGSTGTPK 203
Cdd:cd05921    102 KPGLVfaQDAAPFARALAAIFPLGTplvvsrnavAGRGAISFAELAAtpptAAVDAAFAAVGPDTVAKFLFTSGSTGLPK 181
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  204 AVMLNHRNIMSMVKGIIQMQGFTREDI--TFNWMPFDHV-GGIGMLHLRDVYLGCQEINVSSETILM--EPLKWLdwidh 278
Cdd:cd05921    182 AVINTQRMLCANQAMLEQTYPFFGEEPpvLVDWLPWNHTfGGNHNFNLVLYNGGTLYIDDGKPMPGGfeETLRNL----- 256
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  279 YRASVTWAPNFAFGLvTDFAEEIKD----RKWDLSSMRYMLNGGEAMVAKVGRRILELLEPHGLPADAIRPAWGMSETSS 354
Cdd:cd05921    257 REISPTVYFNVPAGW-EMLVAALEKdealRRRFFKRLKLMFYAGAGLSQDVWDRLQALAVATVGERIPMMAGLGATETAP 335
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  355 GVIFSHEFT-RAGTsdddhfveIGSPIPGFSMRivndhneLVEEGeiGRFQ--VSGLSVTSGYYQRPDLNESVFTEDGWF 431
Cdd:cd05921    336 TATFTHWPTeRSGL--------IGLPAPGTELK-------LVPSG--GKYEvrVKGPNVTPGYWRQPELTAQAFDEEGFY 398
                          410       420
                   ....*....|....*....|....*
gi 1776025254  432 ETGDL-----------GFLRNGRLT 445
Cdd:cd05921    399 CLGDAakladpddpakGLVFDGRVA 423
4CL cd05904
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ...
61-554 6.29e-26

4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.


Pssm-ID: 341230 [Multi-domain]  Cd Length: 505  Bit Score: 115.80  E-value: 6.29e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254   61 SYRRLWDDGLRIVKGLRQSGLKaKQSVILQLGDNSQLLP-AFWGCVLTGVV--PA-PLAVPPTYAE------------SS 124
Cdd:cd05904     34 TYAELERRVRRLAAGLAKRGGR-KGDVVLLLSPNSIEFPvAFLAVLSLGAVvtTAnPLSTPAEIAKqvkdsgaklaftTA 112
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  125 SGTQKLKDawtlLDKPAVITDRgmhqemldwAKEQGLEGFRAIIVEDllsaEADTDWHQSSPEDLALLLLTSGSTGTPKA 204
Cdd:cd05904    113 ELAEKLAS----LALPVVLLDS---------AEFDSLSFSDLLFEAD----EAEPPVVVIKQDDVAALLYSSGTTGRSKG 175
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  205 VMLNHRNIMSMVKGIIQMQG--FTREDITFNWMPFDHVGGIGMLHLRDVYLGcqeinvsSETILM---EPLKWLDWIDHY 279
Cdd:cd05904    176 VMLTHRNLIAMVAQFVAGEGsnSDSEDVFLCVLPMFHIYGLSSFALGLLRLG-------ATVVVMprfDLEELLAAIERY 248
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  280 RasVTWAPnFAFGLVTDFAEEIKDRKWDLSSMRYMLNGGeamvAKVGRRILELLEPHgLPADAIRPAWGMSEtSSGVIFS 359
Cdd:cd05904    249 K--VTHLP-VVPPIVLALVKSPIVDKYDLSSLRQIMSGA----APLGKELIEAFRAK-FPNVDLGQGYGMTE-STGVVAM 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  360 HeFTRAGtsDDDHFVEIGSPIPGFSMRIVN-DHNELVEEGEIGRFQVSGLSVTSGYYQRPDLNESVFTEDGWFETGDLGF 438
Cdd:cd05904    320 C-FAPEK--DRAKYGSVGRLVPNVEAKIVDpETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKEGWLHTGDLCY 396
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  439 LRN-GRLTITGRTKDAIIINGinyY------------SH-AIESAV------EELSEIetsyTAACAVR-LGQNSTDQLA 497
Cdd:cd05904    397 IDEdGYLFIVDRLKELIKYKG---FqvapaelealllSHpEILDAAvipypdEEAGEV----PMAFVVRkPGSSLTEDEI 469
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1776025254  498 IFFVtsAKlndeqmsqllrniqshvsQVIgvtpeyllPVQK-------EEIPKTAIGKIQRTQL 554
Cdd:cd05904    470 MDFV--AK------------------QVA--------PYKKvrkvafvDAIPKSPSGKILRKEL 505
PRK09088 PRK09088
acyl-CoA synthetase; Validated
168-555 6.70e-26

acyl-CoA synthetase; Validated


Pssm-ID: 181644 [Multi-domain]  Cd Length: 488  Bit Score: 115.29  E-value: 6.70e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  168 IVEDL--LSAEAD----TDWHQSSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDHVg 241
Cdd:PRK09088   110 DVEDLaaFIASADalepADTPSIPPERVSLILFTSGTSGQPKGVMLSERNLQQTAHNFGVLGRVDAHSSFLCDAPMFHI- 188
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  242 gIGML-HLRDVYLGCQEINVSSEtilMEPLKWLDW-------IDHYrasvtwapnfaFGlVTDFAEEIKDRK-WDLSSMR 312
Cdd:PRK09088   189 -IGLItSVRPVLAVGGSILVSNG---FEPKRTLGRlgdpalgITHY-----------FC-VPQMAQAFRAQPgFDAAALR 252
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  313 YM---LNGGEamvakvgrrilellePHglPADAIRpAW-----------GMSEtsSGVIFSHEF------TRAGTSdddh 372
Cdd:PRK09088   253 HLtalFTGGA---------------PH--AAEDIL-GWlddgipmvdgfGMSE--AGTVFGMSVdcdvirAKAGAA---- 308
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  373 fveiGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGYYQRPDLNESVFTEDGWFETGDLGfLRN--GRLTITGRT 450
Cdd:PRK09088   309 ----GIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDGWFRTGDIA-RRDadGFFWVVDRK 383
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  451 KDAIIINGINYYSHAIESAVEELSEIetsytAACAV------RLGqnstdQLAIFFVTSAklndEQMSQLLRNIQSHVSQ 524
Cdd:PRK09088   384 KDMFISGGENVYPAEIEAVLADHPGI-----RECAVvgmadaQWG-----EVGYLAIVPA----DGAPLDLERIRSHLST 449
                          410       420       430
                   ....*....|....*....|....*....|...
gi 1776025254  525 VIG--VTPEYLLPVqkEEIPKTAIGKIQRTQLK 555
Cdd:PRK09088   450 RLAkyKVPKHLRLV--DALPRTASGKLQKARLR 480
PRK07787 PRK07787
acyl-CoA synthetase; Validated
1158-1640 7.04e-26

acyl-CoA synthetase; Validated


Pssm-ID: 236096 [Multi-domain]  Cd Length: 471  Bit Score: 115.09  E-value: 7.04e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1158 LFEQQAKKTPDRA-AVSYEGQTLTYRELDERSTQLAiylqahgvgpDRLAGiyVDR-------SLDMLVGLLAILKAGGA 1229
Cdd:PRK07787     4 LNPAAVAAAADIAdAVRIGGRVLSRSDLAGAATAVA----------ERVAG--ARRvavlatpTLATVLAVVGALIAGVP 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1230 YVPLDP-SYPAERlEYMLEDSevfitlttselvntlswnGVTTALLDQDWDEIAQTASDRKVLTRT------VTPENLAY 1302
Cdd:PRK07787    72 VVPVPPdSGVAER-RHILADS------------------GAQAWLGPAPDDPAGLPHVPVRLHARSwhrypePDPDAPAL 132
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1303 VIYTSGSTGKPKGVMIPHKALTNFLVSMGETPGLTAEDKMlavttycfdIAALELFL----------PLIKGAhcyicqt 1372
Cdd:PRK07787   133 IVYTSGTTGPPKGVVLSRRAIAADLDALAEAWQWTADDVL---------VHGLPLFHvhglvlgvlgPLRIGN------- 196
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1373 ehtkdveklkRDIRTIKPT---VMQATPATWKMLFysG----W----ENEENVKIL-------CGGEALP----ETLKRY 1430
Cdd:PRK07787   197 ----------RFVHTGRPTpeaYAQALSEGGTLYF--GvptvWsriaADPEAARALrgarllvSGSAALPvpvfDRLAAL 264
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1431 fldTGSEAWNMFGPTETTIWSAVqRINDECSRATIGRPIANTQIYITDSQLAPVPAGVP--GELCIAGDGVAKGYYKKEE 1508
Cdd:PRK07787   265 ---TGHRPVERYGMTETLITLST-RADGERRPGWVGLPLAGVETRLVDEDGGPVPHDGEtvGELQVRGPTLFDGYLNRPD 340
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1509 LTDSRFIDNPFepgsklYRTGDMARWLPGGRIEYIGR--IDnQVKIRGFRIELGDIESRLSEHPGILECVVV--ADMD-- 1582
Cdd:PRK07787   341 ATAAAFTADGW------FRTGDVAVVDPDGMHRIVGResTD-LIKSGGYRIGAGEIETALLGHPGVREAAVVgvPDDDlg 413
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1776025254 1583 -NLAAYYTakhANASLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLKN 1640
Cdd:PRK07787   414 qRIVAYVV---GADDVAADELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLLS 469
PRK07103 PRK07103
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
4590-4939 7.96e-26

polyketide beta-ketoacyl:acyl carrier protein synthase; Validated


Pssm-ID: 180839 [Multi-domain]  Cd Length: 410  Bit Score: 113.97  E-value: 7.96e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4590 IAVVGLSCRFPGAETLESYWSLLSEGRSSIG-------PIPAERWGCKT-PYYAGVIDGVSYFDP-DFFLLHEE--DVRA 4658
Cdd:PRK07103     4 VVVTGVGVVSAIGQGRPSFAAALLAGRHAFGvmrrpgrQVPDDAGAGLAsAFIGAELDSLALPERlDAKLLRRAslSAQA 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4659 mdpqALLVLEECLKllyHAGYTPEEikGKPVGVYIGG-----RSQHKPDEDSLDHAK--NP--IVTVGQNYLAANLSQFF 4729
Cdd:PRK07103    84 ----ALAAAREAWR---DAALGPVD--PDRIGLVVGGsnlqqREQALVHETYRDRPAflRPsyGLSFMDTDLVGLCSEQF 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4730 DVRGPSVVVDTACSSALVGMNMAIQALRGGDIQSAI-VGGVSLLSSDASHRLFDRRGILSKHSSFHV------FDERADG 4802
Cdd:PRK07103   155 GIRGEGFTVGGASASGQLAVIQAARLVQSGSVDACIaVGALMDLSYWECQALRSLGAMGSDRFADEPeaacrpFDQDRDG 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4803 VVLGEGVGMVMLKTVKQALEDGDTIYAVVKAASVNNDGrTAGPAtPNLEAQKEVMKDALFKSGKKPEDISYLEANGSGSI 4882
Cdd:PRK07103   235 FIYGEACGAVVLESAESARRRGARPYAKLLGWSMRLDA-NRGPD-PSLEGEMRVIRAALRRAGLGPEDIDYVNPHGTGSP 312
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1776025254 4883 VTDLLELKAIqsvYRSGHSSPLsLGSIKPNIGHPLCAEGIASFIKVVLMLKERRFVP 4939
Cdd:PRK07103   313 LGDETELAAL---FASGLAHAW-INATKSLTGHGLSAAGIVELIATLLQMRAGFLHP 365
AACS_like cd05968
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ...
1156-1648 9.99e-26

Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.


Pssm-ID: 341272 [Multi-domain]  Cd Length: 610  Bit Score: 116.44  E-value: 9.99e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1156 HELFEQQAKKTPDRAAVSYEGQ-----TLTYRELDERSTQLAIYLQAHGVGP-DRLaGIYVDRSLDMLVGLLAILKAGGA 1229
Cdd:cd05968     64 EQLLDKWLADTRTRPALRWEGEdgtsrTLTYGELLYEVKRLANGLRALGVGKgDRV-GIYLPMIPEIVPAFLAVARIGGI 142
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1230 YVPLDPSYPAERLEYMLEDSEVFITLTTselvNTLSWNGVTTALLDQDWDEIAQTASDRKVLT-----RTVTPENLAY-- 1302
Cdd:cd05968    143 VVPIFSGFGKEAAATRLQDAEAKALITA----DGFTRRGREVNLKEEADKACAQCPTVEKVVVvrhlgNDFTPAKGRDls 218
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1303 ----------------------VIYTSGSTGKPKGVM-----IPHKALTNFLVSMGETPGltaeDKMLAVTTYCFDIAAL 1355
Cdd:cd05968    219 ydeeketagdgaertesedplmIIYTSGTTGKPKGTVhvhagFPLKAAQDMYFQFDLKPG----DLLTWFTDLGWMMGPW 294
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1356 ELFLPLIKGAHC--YICQTEHTKD------VEKLKRDIRTIKPTVMQATpatwkMLFYSGWENEENVKILcggealpetl 1427
Cdd:cd05968    295 LIFGGLILGATMvlYDGAPDHPKAdrlwrmVEDHEITHLGLSPTLIRAL-----KPRGDAPVNAHDLSSL---------- 359
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1428 kRYFLDTGS----EAWNMFgpTETTIWSAVQRIN----DECSRATIG----RPIA---------NTQIYITDSQLAPVPA 1486
Cdd:cd05968    360 -RVLGSTGEpwnpEPWNWL--FETVGKGRNPIINysggTEISGGILGnvliKPIKpssfngpvpGMKADVLDESGKPARP 436
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1487 GVpGELCIAGD--GVAKGYYKKEEltdsRFIDNPFEPGSKLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIES 1564
Cdd:cd05968    437 EV-GELVLLAPwpGMTRGFWRDED----RYLETYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIES 511
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1565 RLSEHPGILECVVVADMDNLAAyyTAKHANASL---------TARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDR 1635
Cdd:cd05968    512 VLNAHPAVLESAAIGVPHPVKG--EAIVCFVVLkpgvtpteaLAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMR 589
                          570
                   ....*....|...
gi 1776025254 1636 NSLKNIDLsGEQL 1648
Cdd:cd05968    590 RVIRAAYL-GKEL 601
FadD3 cd17638
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ...
188-490 1.13e-25

acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.


Pssm-ID: 341293 [Multi-domain]  Cd Length: 330  Bit Score: 111.44  E-value: 1.13e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  188 DLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDHVGGIGMlhlrdvylGCQEINVSSETIL- 266
Cdd:cd17638      1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFFHTFGYKA--------GIVACLLTGATVVp 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  267 ---MEPLKWLDWIDHYRASVTWAPNFAFGLVTDfaeEIKDRKWDLSSMRYMLNGGEAMVAKVGRRILEllephGLPADAI 343
Cdd:cd17638     73 vavFDVDAILEAIERERITVLPGPPTLFQSLLD---HPGRKKFDLSSLRAAVTGAATVPVELVRRMRS-----ELGFETV 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  344 RPAWGMSETSSGVIfshefTRAGTSDDDHFVEIGSPIPGFSMRIVNDhnelveeGEIgrfQVSGLSVTSGYYQRPDLNES 423
Cdd:cd17638    145 LTAYGLTEAGVATM-----CRPGDDAETVATTCGRACPGFEVRIADD-------GEV---LVRGYNVMQGYLDDPEATAE 209
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1776025254  424 VFTEDGWFETGDLGFL-RNGRLTITGRTKDAIIINGINYYSHAIESAVEELSEIetsytAACAV------RLGQ 490
Cdd:cd17638    210 AIDADGWLHTGDVGELdERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGV-----AQVAVigvpdeRMGE 278
PRK08316 PRK08316
acyl-CoA synthetase; Validated
30-564 1.55e-25

acyl-CoA synthetase; Validated


Pssm-ID: 181381 [Multi-domain]  Cd Length: 523  Bit Score: 114.64  E-value: 1.55e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254   30 TIPEVLYRTAAELGDTKGIIYlqpdGTEVYqSYRRLWDDGLRIVKGLRQSGLKAKQSVILqLGDNS-QLLPAFWGCVLTG 108
Cdd:PRK08316    12 TIGDILRRSARRYPDKTALVF----GDRSW-TYAELDAAVNRVAAALLDLGLKKGDRVAA-LGHNSdAYALLWLACARAG 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  109 VVpaplAVPPTYAESSsgtqklKDAWTLLDKP---AVITDRGMHQEMLDWAKEQGLEGFRAIIVEDLLSAEAD----TDW 181
Cdd:PRK08316    86 AV----HVPVNFMLTG------EELAYILDHSgarAFLVDPALAPTAEAALALLPVDTLILSLVLGGREAPGGwldfADW 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  182 HQSSP----------EDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDHVGGigmlhlRDV 251
Cdd:PRK08316   156 AEAGSvaepdveladDDLAQILYTSGTESLPKGAMLTHRALIAEYVSCIVAGDMSADDIPLHALPLYHCAQ------LDV 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  252 YLGCQeINVSSETILME---PLKWLDWIDHYRASVTWA-PNFAFGLVT--DFAeeikdrKWDLSSMRYMLNGGEAMVAKV 325
Cdd:PRK08316   230 FLGPY-LYVGATNVILDapdPELILRTIEAERITSFFApPTVWISLLRhpDFD------TRDLSSLRKGYYGASIMPVEV 302
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  326 GRRILEllephGLPADAIRPAWGMSETSS-GVIFSHEftragtsddDHFVEIGSP-IPGFSM--RIVNDHNELVEEGEIG 401
Cdd:PRK08316   303 LKELRE-----RLPGLRFYNCYGQTEIAPlATVLGPE---------EHLRRPGSAgRPVLNVetRVVDDDGNDVAPGEVG 368
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  402 RFQVSGLSVTSGYYQRPDLNESVFtEDGWFETGDLGFL-RNGRLTITGRTKDAIIINGINYYSHAIE------SAVEELS 474
Cdd:PRK08316   369 EIVHRSPQLMLGYWDDPEKTAEAF-RGGWFHSGDLGVMdEEGYITVVDRKKDMIKTGGENVASREVEealythPAVAEVA 447
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  475 EIETSY-------TAACAVRLGqnstdqlaiffvtsAKLNDEQmsqllrnIQSHVSQVIGV--TPEYLLPVqkEEIPKTA 545
Cdd:PRK08316   448 VIGLPDpkwieavTAVVVPKAG--------------ATVTEDE-------LIAHCRARLAGfkVPKRVIFV--DELPRNP 504
                          570
                   ....*....|....*....
gi 1776025254  546 IGKIQRTQLKTSFENGEFD 564
Cdd:PRK08316   505 SGKILKRELRERYAGAFTD 523
PRK06333 PRK06333
beta-ketoacyl-ACP synthase;
4590-4993 2.26e-25

beta-ketoacyl-ACP synthase;


Pssm-ID: 235781 [Multi-domain]  Cd Length: 424  Bit Score: 112.78  E-value: 2.26e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4590 IAVVGLSCRFPGAETLESYWSLLSEGRSSIGPIP---AERWGCKtpyYAGVI-----DGVSYFDPDFFLlHEEDVRAMDP 4661
Cdd:PRK06333     6 IVVTGMGAVSPLGCGVETFWQRLLAGQSGIRTLTdfpVGDLATK---IGGQVpdlaeDAEAGFDPDRYL-DPKDQRKMDR 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4662 QALLVLEECLKLLYHAGYTPEEIK-----GKPVGVYIGGRSqhkpdedSLDHAKNPIVTVGQ-------------NYLAA 4723
Cdd:PRK06333    82 FILFAMAAAKEALAQAGWDPDTLEdrertATIIGSGVGGFP-------AIAEAVRTLDSRGPrrlspftipsfltNMAAG 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4724 NLSQFFDVRGPSVVVDTACSSALVGMNMAIQALRGGDIQSAIVGG-------VSLLSSDASHRLFDRRGILSKHSSfHVF 4796
Cdd:PRK06333   155 HVSIRYGFKGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGteaaidrVSLAGFAAARALSTRFNDAPEQAS-RPF 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4797 DERADGVVLGEGVGMVMLKTVKQALEDGDTIYAVVKAASVNNDGR--TAGPatPNLEAQKEVMKDALFKSGKKPEDISYL 4874
Cdd:PRK06333   234 DRDRDGFVMGEGAGILVIETLEHALARGAPPLAELVGYGTSADAYhmTAGP--EDGEGARRAMLIALRQAGIPPEEVQHL 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4875 EANGSGSIVTDLLELKAIQSVYrsGHSSPLSLGSIKPNIGHPLCAEGIASFIKVVLMLKERRFVPFLSGEkemaHFDQQK 4954
Cdd:PRK06333   312 NAHATSTPVGDLGEVAAIKKVF--GHVSGLAVSSTKSATGHLLGAAGGVEAIFTILALRDQIAPPTLNLE----NPDPAA 385
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|...
gi 1776025254 4955 ANITFSRalekwTDSQPTA---AI-NCFADGGTNVHVIVEAWE 4993
Cdd:PRK06333   386 EGLDVVA-----NKARPMDmdyALsNGFGFGGVNASILFRRWE 423
PRK07786 PRK07786
long-chain-fatty-acid--CoA ligase; Validated
1160-1639 3.45e-25

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 169098 [Multi-domain]  Cd Length: 542  Bit Score: 114.10  E-value: 3.45e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1160 EQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVG-PDRLAGIYVDRSlDMLVGLLAILKAGGAYVPLDPSYP 1238
Cdd:PRK07786    24 ARHALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGfGDRVLILMLNRT-EFVESVLAANMLGAIAVPVNFRLT 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1239 AERLEYMLEDSEVFITLTTSELVN----------TLSWNGVTTALLDQDW----DEIAQTASDRKVLTrtvTPENL-AYV 1303
Cdd:PRK07786   103 PPEIAFLVSDCGAHVVVTEAALAPvatavrdivpLLSTVVVAGGSSDDSVlgyeDLLAEAGPAHAPVD---IPNDSpALI 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1304 IYTSGSTGKPKGVMIPHKALTNFLVSMGETPGLTAEDKMLAVTTYCFDIAALELFLP-LIKGAHCYICQT---EHTKDVE 1379
Cdd:PRK07786   180 MYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGADINSDVGFVGVPLFHIAGIGSMLPgLLLGAPTVIYPLgafDPGQLLD 259
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1380 KLKRDirtiKPTVMQATPATWKMLFYSGWENEENVK---ILCGGEALPETLKRYFLDTGSEAWNM--FGPTETTIWSAVQ 1454
Cdd:PRK07786   260 VLEAE----KVTGIFLVPAQWQAVCAEQQARPRDLAlrvLSWGAAPASDTLLRQMAATFPEAQILaaFGQTEMSPVTCML 335
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1455 RINDEC-SRATIGRPIANTQIYITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPFEpgsklyrTGDMAR 1533
Cdd:PRK07786   336 LGEDAIrKLGSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAGGWFH-------SGDLVR 408
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1534 WLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMDNL-----AAYYTAKHANASLTARELRHFVKN 1608
Cdd:PRK07786   409 QDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKwgevpVAVAAVRNDDAALTLEDLAEFLTD 488
                          490       500       510
                   ....*....|....*....|....*....|.
gi 1776025254 1609 ALPAYMVPSYFIQLDHMPLTPNGKIDRNSLK 1639
Cdd:PRK07786   489 RLARYKHPKALEIVDALPRNPAGKVLKTELR 519
PRK08180 PRK08180
feruloyl-CoA synthase; Reviewed
28-445 3.77e-25

feruloyl-CoA synthase; Reviewed


Pssm-ID: 236175 [Multi-domain]  Cd Length: 614  Bit Score: 114.59  E-value: 3.77e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254   28 PATIPEVLYRTAAELGDTkgiIYL---QPDGTEVYQSYRRLWDDGLRIVKGLRQSGLKAKQSVILqLGDNS--QLLPAFw 102
Cdd:PRK08180    38 PRRLTDRLVHWAQEAPDR---VFLaerGADGGWRRLTYAEALERVRAIAQALLDRGLSAERPLMI-LSGNSieHALLAL- 112
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  103 GCVLTGVVPAPlaVPPTYAESSSGTQKLKDAWTLLdKPAVI--TDRGMHQEMLDWAKEQGLE---------GFRAIIVED 171
Cdd:PRK08180   113 AAMYAGVPYAP--VSPAYSLVSQDFGKLRHVLELL-TPGLVfaDDGAAFARALAAVVPADVEvvavrgavpGRAATPFAA 189
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  172 LL----SAEADTDWHQSSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTRED--ITFNWMPFDHVGG--- 242
Cdd:PRK08180   190 LLatppTAAVDAAHAAVGPDTIAKFLFTSGSTGLPKAVINTHRMLCANQQMLAQTFPFLAEEppVLVDWLPWNHTFGgnh 269
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  243 -IGM-LH-----------------------LRDVylgcqeinvsSETI-LMEPLKWLDWIDHYRASVTWAPNFafglvtd 296
Cdd:PRK08180   270 nLGIvLYnggtlyiddgkptpggfdetlrnLREI----------SPTVyFNVPKGWEMLVPALERDAALRRRF------- 332
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  297 faeeikdrkwdLSSMRYMLNGGEAM------------VAKVGRRILellephglpadaIRPAWGMSETSSGVIFSHEFT- 363
Cdd:PRK08180   333 -----------FSRLKLLFYAGAALsqdvwdrldrvaEATCGERIR------------MMTGLGMTETAPSATFTTGPLs 389
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  364 RAGtsdddhfvEIGSPIPGFSMRivndhneLVEEGeiGRFQ--VSGLSVTSGYYQRPDLNESVFTEDGWFETGD------ 435
Cdd:PRK08180   390 RAG--------NIGLPAPGCEVK-------LVPVG--GKLEvrVKGPNVTPGYWRAPELTAEAFDEEGYYRSGDavrfvd 452
                          490
                   ....*....|....*
gi 1776025254  436 -----LGFLRNGRLT 445
Cdd:PRK08180   453 padpeRGLMFDGRIA 467
PRK04319 PRK04319
acetyl-CoA synthetase; Provisional
1168-1639 5.01e-25

acetyl-CoA synthetase; Provisional


Pssm-ID: 235279 [Multi-domain]  Cd Length: 570  Bit Score: 113.84  E-value: 5.01e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1168 DRAAVSYEG----QTLTYRELDERSTQLAIYLQAHGVGP-DRLAgIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERL 1242
Cdd:PRK04319    59 DKVALRYLDasrkEKYTYKELKELSNKFANVLKELGVEKgDRVF-IFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAV 137
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1243 EYMLEDSEVFITLTTSEL-----VNTLSwnGVTTALL----------DQDWDEIAQTASDRkVLTRTVTPENLAYVIYTS 1307
Cdd:PRK04319   138 RDRLEDSEAKVLITTPALlerkpADDLP--SLKHVLLvgedveegpgTLDFNALMEQASDE-FDIEWTDREDGAILHYTS 214
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1308 GSTGKPKGVMIPHKALTNFLVSmGET-----PG----LTAEDKMLAVTTYcfdiaalELFLPLIKGAHCYICQTEHtkDV 1378
Cdd:PRK04319   215 GSTGKPKGVLHVHNAMLQHYQT-GKYvldlhEDdvywCTADPGWVTGTSY-------GIFAPWLNGATNVIDGGRF--SP 284
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1379 EKLKRDIRTIKPTVMQATPATWKMLFYSGwenEENVK---------ILCGGEAL-PE-------TLKRYFLDTgseaWNM 1441
Cdd:PRK04319   285 ERWYRILEDYKVTVWYTAPTAIRMLMGAG---DDLVKkydlsslrhILSVGEPLnPEvvrwgmkVFGLPIHDN----WWM 357
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1442 fgpTETtiwsAVQRIndeCSRAT-------IGRPIANTQIYITDSQLAPVPAGVPGELCI-AG-DGVAKGYYKKEELTDS 1512
Cdd:PRK04319   358 ---TET----GGIMI---ANYPAmdikpgsMGKPLPGIEAAIVDDQGNELPPNRMGNLAIkKGwPSMMRGIWNNPEKYES 427
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1513 RFIDNpfepgskLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMDNLA-----AY 1587
Cdd:PRK04319   428 YFAGD-------WYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRgeiikAF 500
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1776025254 1588 YTAK--HANASLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLK 1639
Cdd:PRK04319   501 VALRpgYEPSEELKEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVLK 554
LC_FACS_like cd05935
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ...
184-554 6.20e-25

Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.


Pssm-ID: 341258 [Multi-domain]  Cd Length: 430  Bit Score: 111.42  E-value: 6.20e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  184 SSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDHVGGIGMLHLRDVYLGcqeinvsSE 263
Cdd:cd05935     81 SELDDLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVG-------GT 153
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  264 TILMEplKW-----LDWIDHYRASVTWApnfAFGLVTDFAEEIKDRKWDLSSMRYMLNGGEAMVAKVGRRILELLephgl 338
Cdd:cd05935    154 YVLMA--RWdretaLELIEKYKVTFWTN---IPTMLVDLLATPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLT----- 223
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  339 padAIR--PAWGMSETSSGVifsheftragTSDDDHFVE---IGSPIPGFSMRIVN-DHNELVEEGEIGRFQVSGLSVTS 412
Cdd:cd05935    224 ---GLRfvEGYGLTETMSQT----------HTNPPLRPKlqcLGIP*FGVDARVIDiETGRELPPNEVGEIVVRGPQIFK 290
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  413 GYYQRPDLNESVFTEDG---WFETGDLGFL-RNGRLTITGRTKDAIIINGINYYSHAIESAVEELSEIETsytaACAVRL 488
Cdd:cd05935    291 GYWNRPEETEESFIEIKgrrFFRTGDLGYMdEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*E----VCVISV 366
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1776025254  489 GQNSTDQLAIFFVT-----SAKLNDEQMSQLLRNIQSHVSQVIGVtpEYLlpvqkEEIPKTAIGKIQRTQL 554
Cdd:cd05935    367 PDERVGEEVKAFIVlrpeyRGKVTEEDIIEWAREQMAAYKYPREV--EFV-----DELPRSASGKILWRLL 430
ACLS-CaiC cd17637
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ...
1303-1635 6.70e-25

acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341292 [Multi-domain]  Cd Length: 333  Bit Score: 109.28  E-value: 6.70e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1303 VIYTSGSTGKPKGVMIPHKALTNFLVSMGETPGLTAEDKMLAVTTYcFDIAALELFLPLIKGAHCYICQTEHtkDVEKLK 1382
Cdd:cd17637      5 IIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPL-FHIAGLNLALATFHAGGANVVMEKF--DPAEAL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1383 RDIRTIKPTVMQATPATWKMLFYSGWENEENVKIL--CGGEALPETLKRYFLDTGSEAWNMFGPTETTIWSAVQRINDEC 1460
Cdd:cd17637     82 ELIEEEKVTLMGSFPPILSNLLDAAEKSGVDLSSLrhVLGLDAPETIQRFEETTGATFWSLYGQTETSGLVTLSPYRERP 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1461 SRAtiGRPIANTQIYITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNpfepgskLYRTGDMARWLPGGRI 1540
Cdd:cd17637    162 GSA--GRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTFRNG-------WHHTGDLGRFDEDGYL 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1541 EYIGRIDNQ--VKIRGFRIELGDIESRLSEHPGILECVV--VADmdnlaayytAK-----------HANASLTARELRHF 1605
Cdd:cd17637    233 WYAGRKPEKelIKPGGENVYPAEVEKVILEHPAIAEVCVigVPD---------PKwgegikavcvlKPGATLTADELIEF 303
                          330       340       350
                   ....*....|....*....|....*....|
gi 1776025254 1606 VKNALPAYMVPSYFIQLDHMPLTPNGKIDR 1635
Cdd:cd17637    304 VGSRIARYKKPRYVVFVEALPKTADGSIDR 333
A_NRPS_Bac cd17655
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...
168-554 6.84e-25

bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341310 [Multi-domain]  Cd Length: 490  Bit Score: 112.42  E-value: 6.84e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  168 IVEDLLSAEADTDWHQ-SSPEDLALLLLTSGSTGTPKAVMLNHRN----IMSMVKGIIQMQGFTRedITFNWMPFD-HVG 241
Cdd:cd17655    117 LDEDTIYHEESENLEPvSKSDDLAYVIYTSGSTGKPKGVMIEHRGvvnlVEWANKVIYQGEHLRV--ALFASISFDaSVT 194
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  242 GIGMLHLrdvyLGCQEINVSSETILMEPlKWLDWIDHYRASVTWAPNfafgLVTDFAEEIKDRKWdlSSMRYMLNGGEAM 321
Cdd:cd17655    195 EIFASLL----SGNTLYIVRKETVLDGQ-ALTQYIRQNRITIIDLTP----AHLKLLDAADDSEG--LSLKHLIVGGEAL 263
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  322 VAKVGRRILELLEPhglpADAIRPAWGMSETSSG-VIFSHEftraGTSDDDHFVEIGSPIPGFSMRIVNDHNELVEEGEI 400
Cdd:cd17655    264 STELAKKIIELFGT----NPTITNAYGPTETTVDaSIYQYE----PETDQQVSVPIGKPLGNTRIYILDQYGRPQPVGVA 335
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  401 GRFQVSGLSVTSGYYQRPDLNESVFTEDGW------FETGDLG-FLRNGRLTITGRTKDAIIINGinyysHAIesaveEL 473
Cdd:cd17655    336 GELYIGGEGVARGYLNRPELTAEKFVDDPFvpgermYRTGDLArWLPDGNIEFLGRIDHQVKIRG-----YRI-----EL 405
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  474 SEIETSYT-------AACAVRLGQNSTDQLAIFFVTSAKLNDEQMSQLLRNiqshvsqvigVTPEYLLP---VQKEEIPK 543
Cdd:cd17655    406 GEIEARLLqhpdikeAVVIARKDEQGQNYLCAYIVSEKELPVAQLREFLAR----------ELPDYMIPsyfIKLDEIPL 475
                          410
                   ....*....|.
gi 1776025254  544 TAIGKIQRTQL 554
Cdd:cd17655    476 TPNGKVDRKAL 486
PRK06164 PRK06164
acyl-CoA synthetase; Validated
1154-1639 1.25e-24

acyl-CoA synthetase; Validated


Pssm-ID: 235722 [Multi-domain]  Cd Length: 540  Bit Score: 112.14  E-value: 1.25e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1154 TFHELFEQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGP-DRLAGIYVDRSlDMLVGLLAILKAGGAYVP 1232
Cdd:PRK06164    11 TLASLLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRgDRVAVWLPNCI-EWVVLFLACARLGATVIA 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1233 LDPSYPAERLEYMLEDSEV--------FITLTTSELVNTLSWNGVTT----ALLDQDWDEI-AQTASDRKVL-----TRT 1294
Cdd:PRK06164    90 VNTRYRSHEVAHILGRGRArwlvvwpgFKGIDFAAILAAVPPDALPPlraiAVVDDAADATpAPAPGARVQLfalpdPAP 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1295 VT-------PENLAYVIYT-SGSTGKPKGVMIPHKALTNFLVSMGETPGLTAEDKMLAVTTYC--FDIAALELFL----P 1360
Cdd:PRK06164   170 PAaageraaDPDAGALLFTtSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCgvFGFSTLLGALaggaP 249
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1361 LIkgahcyicqTEHTKDVEKLKRDIRTIKPTVMQATPATWKMLFYSGWENEENVKI-LCG--------GEALPETLKRYF 1431
Cdd:PRK06164   250 LV---------CEPVFDAARTARALRRHRVTHTFGNDEMLRRILDTAGERADFPSArLFGfasfapalGELAALARARGV 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1432 LDTGseawnMFGPTETTIWSAVQRINDECS--RATIGRPI-ANTQIYITDSQLAPV-PAGVPGELCIAGDGVAKGYYKKE 1507
Cdd:PRK06164   321 PLTG-----LYGSSEVQALVALQPATDPVSvrIEGGGRPAsPEARVRARDPQDGALlPDGESGEIEIRAPSLMRGYLDNP 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1508 ELTDSRFIDNPFepgsklYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVA---DMDNL 1584
Cdd:PRK06164   396 DATARALTDDGY------FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGatrDGKTV 469
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1776025254 1585 AAYYTAKHANASLTARELRHFVKNALPAYMVPSYFIQLDHMPLT--PNG-KIDRNSLK 1639
Cdd:PRK06164   470 PVAFVIPTDGASPDEAGLMAACREALAGFKVPARVQVVEAFPVTesANGaKIQKHRLR 527
PRK08722 PRK08722
beta-ketoacyl-ACP synthase II;
1827-2186 1.30e-24

beta-ketoacyl-ACP synthase II;


Pssm-ID: 181539 [Multi-domain]  Cd Length: 414  Bit Score: 110.09  E-value: 1.30e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1827 FDPSFFqISPKDAEFMDPQLRMLLTHSWKAIEDAGYAAGQIPQTSVFMS-ASNNSYRALLPSDTTESLETPDGYVSWVLA 1905
Cdd:PRK08722    57 FNCEEY-MSKKDARKMDLFIQYGIAAGIQALDDSGLEVTEENAHRIGVAiGSGIGGLGLIEAGHQALVEKGPRKVSPFFV 135
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1906 QSgTIPTMISHKL----GLRGPSYFVHANCSSSLIGLHSAYKSLLSAESDYALVGGA-TLHTESNI-GYVHQPGLNFSSD 1979
Cdd:PRK08722   136 PS-TIVNMIAGNLsimrGLRGPNIAISTACTTGLHNIGHAARMIAYGDADAMVAGGAeKASTPLGMaGFGAAKALSTRND 214
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1980 GHIKA---FDASADGMIGGEGVAVVLLKKAADAVKDGDHIYALLRGIGVNNDgADKVGFYAPSVKGQADVVQQVMNQTKI 2056
Cdd:PRK08722   215 EPQKAsrpWDKDRDGFVLGDGAGMMVLEEYEHAKARGAKIYAELVGFGMSGD-AYHMTSPSEDGSGGALAMEAAMRDAGV 293
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2057 HPESICYVEAHGTGTKLGDPIELAALTNVYRQYTNKTQFcgIGSVKTNIGHLDTAAGLAGCIKVVMSLYHQELAPSINYK 2136
Cdd:PRK08722   294 TGEQIGYVNAHGTSTPAGDVAEIKGIKRALGEAGSKQVL--VSSTKSMTGHLLGAAGSVEAIITVMSLVDQIVPPTINLD 371
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1776025254 2137 EPNPNTDlasspfyvVDQKKTLSREIQTHRAAL-SSFGLGGTNTHAIFEQF 2186
Cdd:PRK08722   372 DPEEGLD--------IDLVPHTARKVESMEYAIcNSFGFGGTNGSLIFKKM 414
KR_1_SDR_x cd08952
ketoreductase (KR), subgroup 1, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
4174-4384 1.65e-24

ketoreductase (KR), subgroup 1, complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes KR domains found in many multidomain PKSs, including six of seven Sorangium cellulosum PKSs (encoded by spiDEFGHIJ) which participate in the synthesis of the polyketide scaffold of the cytotoxic spiroketal polyketide spirangien. These seven PKSs have either a single PKS module (SpiF), two PKR modules (SpiD,-E,-I,-J), or three PKS modules (SpiG,-H). This subfamily includes the single KR domain of SpiF, the first KR domains of SpiE,-G,H,-I,and #J, the third KR domain of SpiG, and the second KR domain of SpiH. The second KR domains of SpiE,-G, I, and #J, and the KR domains of SpiD, belong to a different KR_FAS_SDR subfamily. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187655 [Multi-domain]  Cd Length: 480  Bit Score: 111.11  E-value: 1.65e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4174 LITGGTRGIGLLCARHFAECyGVKKLVLTGR--EQLPPREEwarfktsntslaekiqAVRELEAKGVQVEMLSLTLSDDA 4251
Cdd:cd08952    234 LVTGGTGALGAHVARWLARR-GAEHLVLTSRrgPDAPGAAE----------------LVAELTALGARVTVAACDVADRD 296
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4252 QVEQTLQHIkRTLGPIGGVIHCAGLTDMDTLAfiRKTSDDIQRVMEPKVSGLTTLYRHVCNEPLQFFVLFSSVSAIIPel 4331
Cdd:cd08952    297 ALAALLAAL-PAGHPLTAVVHAAGVLDDGPLD--DLTPERLAEVLRAKVAGARHLDELTRDRDLDAFVLFSSIAGVWG-- 371
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1776025254 4332 SAGQADYAMANSYMDYFAEAHQKH-VPIISVQWPNWKETGMGEVTNQAY-RESGL 4384
Cdd:cd08952    372 SGGQGAYAAANAYLDALAERRRARgLPATSVAWGPWAGGGMAAGAAAERlRRRGL 426
PRK06710 PRK06710
long-chain-fatty-acid--CoA ligase; Validated
1149-1638 1.69e-24

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 180666 [Multi-domain]  Cd Length: 563  Bit Score: 112.05  E-value: 1.69e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1149 TYPYITFHELFEQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGG 1228
Cdd:PRK06710    20 SYDIQPLHKYVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGG 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1229 AYVPLDPSYPAERLEYMLEDSEV-------------------------------------------FITLTTSELVNTLS 1265
Cdd:PRK06710   100 IVVQTNPLYTERELEYQLHDSGAkvilcldlvfprvtnvqsatkiehvivtriadflpfpknllypFVQKKQSNLVVKVS 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1266 -------WNGVttallDQDWDEIAQTASDrkvltrtvtPEN-LAYVIYTSGSTGKPKGVMIPHKAL-TNFLVSMGETPG- 1335
Cdd:PRK06710   180 esetihlWNSV-----EKEVNTGVEVPCD---------PENdLALLQYTGGTTGFPKGVMLTHKNLvSNTLMGVQWLYNc 245
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1336 LTAEDKMLAVTTYcFDIAALE--LFLPLIKGahcYICQTEHTKDVEKLKRDIRTIKPTVMQATPATWKMLFYSGWENEEN 1413
Cdd:PRK06710   246 KEGEEVVLGVLPF-FHVYGMTavMNLSIMQG---YKMVLIPKFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYD 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1414 VK----ILCGGEALP-ETLKRYFLDTGSEAWNMFGPTETTIWSAVQRINDECSRATIGRPIANTQIYITDSQLAPV-PAG 1487
Cdd:PRK06710   322 ISsiraCISGSAPLPvEVQEKFETVTGGKLVEGYGLTESSPVTHSNFLWEKRVPGSIGVPWPDTEAMIMSLETGEAlPPG 401
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1488 VPGELCIAGDGVAKGYYKKEELTDSRFIDNpfepgskLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLS 1567
Cdd:PRK06710   402 EIGEIVVKGPQIMKGYWNKPEETAAVLQDG-------WLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLY 474
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1776025254 1568 EHPGILECVVVADMD-----NLAAYYTAKHaNASLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSL 1638
Cdd:PRK06710   475 EHEKVQEVVTIGVPDpyrgeTVKAFVVLKE-GTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
PRK13382 PRK13382
bile acid CoA ligase;
1153-1639 1.81e-24

bile acid CoA ligase;


Pssm-ID: 172019 [Multi-domain]  Cd Length: 537  Bit Score: 111.77  E-value: 1.81e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1153 ITFHELFEQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVP 1232
Cdd:PRK13382    43 MGPTSGFAIAAQRCPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILL 122
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1233 LDPSYPAERLEYMLEDSEVFITLTTSELVNTL--SWNGVTTALLDQDW-DEIAQTASDrkVLTRT-------VTPENLAY 1302
Cdd:PRK13382   123 LNTSFAGPALAEVVTREGVDTVIYDEEFSATVdrALADCPQATRIVAWtDEDHDLTVE--VLIAAhagqrpePTGRKGRV 200
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1303 VIYTSGSTGKPKGVMIPHKALTNFLVS-MGETPgLTAEDKMLAVT----TYCFDIAALELFLplikgaHCYICqTEHTKD 1377
Cdd:PRK13382   201 ILLTSGTTGTPKGARRSGPGGIGTLKAiLDRTP-WRAEEPTVIVApmfhAWGFSQLVLAASL------ACTIV-TRRRFD 272
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1378 VEKLKRDIRTIKPTVMQATPATWKMLF---------YSGweneENVKILCG-GEALPETLKRYFLDT-GSEAWNMFGPTE 1446
Cdd:PRK13382   273 PEATLDLIDRHRATGLAVVPVMFDRIMdlpaevrnrYSG----RSLRFAAAsGSRMRPDVVIAFMDQfGDVIYNNYNATE 348
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1447 TTiWSAVQRINDecSRA---TIGRPIANTQIYITDSQLAPVPAGVPGELCIAGDGVAKGYYKKeelTDSRFIDNpfepgs 1523
Cdd:PRK13382   349 AG-MIATATPAD--LRAapdTAGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGYTSG---STKDFHDG------ 416
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1524 kLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMDN-----LAAYYTAKhANASLT 1598
Cdd:PRK13382   417 -FMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEqygqrLAAFVVLK-PGASAT 494
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|.
gi 1776025254 1599 ARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLK 1639
Cdd:PRK13382   495 PETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQ 535
LC-FACS_euk cd05927
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ...
186-451 1.97e-24

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.


Pssm-ID: 341250 [Multi-domain]  Cd Length: 545  Bit Score: 111.54  E-value: 1.97e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  186 PEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQM----QGFTREDITFNWMPFDHV-------------GGIGMLH- 247
Cdd:cd05927    113 PEDLATICYTSGTTGNPKGVMLTHGNIVSNVAGVFKIleilNKINPTDVYISYLPLAHIfervvealflyhgAKIGFYSg 192
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  248 ----LRD-------------------VYLGCQEiNVSSETILmepLKWL-DWIDHYRASvtwapNFAFGLVTdfaeeiKD 303
Cdd:cd05927    193 dirlLLDdikalkptvfpgvprvlnrIYDKIFN-KVQAKGPL---KRKLfNFALNYKLA-----ELRSGVVR------AS 257
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  304 RKWD-----------LSSMRYMLNGGEAMVAKVGRRILELLephGLPadaIRPAWGMSETSSGVIFSHEF-TRAGTsddd 371
Cdd:cd05927    258 PFWDklvfnkikqalGGNVRLMLTGSAPLSPEVLEFLRVAL---GCP---VLEGYGQTECTAGATLTLPGdTSVGH---- 327
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  372 hfveIGSPIPGFSMRIVN------DHNELVEEGEIgrfQVSGLSVTSGYYQRPDLNESVFTEDGWFETGDLG-FLRNGRL 444
Cdd:cd05927    328 ----VGGPLPCAEVKLVDvpemnyDAKDPNPRGEV---CIRGPNVFSGYYKDPEKTAEALDEDGWLHTGDIGeWLPNGTL 400

                   ....*..
gi 1776025254  445 TITGRTK 451
Cdd:cd05927    401 KIIDRKK 407
PRK07967 PRK07967
beta-ketoacyl-ACP synthase I;
3437-3779 4.27e-24

beta-ketoacyl-ACP synthase I;


Pssm-ID: 181184 [Multi-domain]  Cd Length: 406  Bit Score: 108.60  E-value: 4.27e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3437 ALEDAGCPPQSLSGTGTGIFIGTGNTGYKDLFHRANLPIE--GHAATGhmiPSVGPNRMS--------YFLNIHGPSEPV 3506
Cdd:PRK07967    82 AIADAGLSEEQVSNPRTGLIAGSGGGSTRNQVEAADAMRGprGPKRVG---PYAVTKAMAstvsaclaTPFKIKGVNYSI 158
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3507 ETACSSSLVAIHRAVTAMQNGDCEMAIAGGvntilTEEAHISYS-----KAGMLSK-----DGRCKTFSADANGYVRGEG 3576
Cdd:PRK07967   159 SSACATSAHCIGNAVEQIQLGKQDIVFAGG-----GEELDWEMSclfdaMGALSTKyndtpEKASRAYDANRDGFVIAGG 233
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3577 VGMVMLKKLEDAERDGNHIYGVIRGTAENHGGrantltspnpkaqADLL-------VRAYRQA--GIDpSTVTYIEAHGT 3647
Cdd:PRK07967   234 GGVVVVEELEHALARGAKIYAEIVGYGATSDG-------------YDMVapsgegaVRCMQMAlaTVD-TPIDYINTHGT 299
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3648 GTELGDPIEINGLKAAFkelsnmrGESQPdvpdhrcGIGSVKSNIGHLELAAGISGLIKVLLQMKHKTLVKSLHCETLNP 3727
Cdd:PRK07967   300 STPVGDVKELGAIREVF-------GDKSP-------AISATKSLTGHSLGAAGVQEAIYSLLMMEHGFIAPSANIEELDP 365
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1776025254 3728 ylQLTDSPfyIVQEKQEWKSVTDCDGNelprragisSFGIGGVNAHIVIEEY 3779
Cdd:PRK07967   366 --QAAGMP--IVTETTDNAELTTVMSN---------SFGFGGTNATLVFRRY 404
PRK08974 PRK08974
long-chain-fatty-acid--CoA ligase FadD;
185-555 4.30e-24

long-chain-fatty-acid--CoA ligase FadD;


Pssm-ID: 236359 [Multi-domain]  Cd Length: 560  Bit Score: 110.53  E-value: 4.30e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  185 SPEDLALLLLTSGSTGTPKAVMLNHRNIMSMV---KGIIQMQGFTREDITFNWMPFDHVGGIGMLHLRDVYLGCQEINVS 261
Cdd:PRK08974   204 VPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLeqaKAAYGPLLHPGKELVVTALPLYHIFALTVNCLLFIELGGQNLLIT 283
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  262 SETILMEPLKWLDwidHYRASVTWAPNFAF-GLVTDfaEEIKdrKWDLSSMRYMLNGGEAM---VAK-----VGRRILEl 332
Cdd:PRK08974   284 NPRDIPGFVKELK---KYPFTAITGVNTLFnALLNN--EEFQ--ELDFSSLKLSVGGGMAVqqaVAErwvklTGQYLLE- 355
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  333 lephglpadairpAWGMSETSSGVifsheftrAGTSDD--DHFVEIGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSV 410
Cdd:PRK08974   356 -------------GYGLTECSPLV--------SVNPYDldYYSGSIGLPVPSTEIKLVDDDGNEVPPGEPGELWVKGPQV 414
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  411 TSGYYQRPDLNESVFtEDGWFETGDLGFL-RNGRLTITGRTKDAIIINGINYYSHAIESAVE---ELSEIetsytAACAV 486
Cdd:PRK08974   415 MLGYWQRPEATDEVI-KDGWLATGDIAVMdEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMlhpKVLEV-----AAVGV 488
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1776025254  487 RlGQNSTDQLAIFFVTsaklNDEQMS--QLLRNIQSHVSQvigvtpeYLLPVQ---KEEIPKTAIGKIQRTQLK 555
Cdd:PRK08974   489 P-SEVSGEAVKIFVVK----KDPSLTeeELITHCRRHLTG-------YKVPKLvefRDELPKSNVGKILRRELR 550
PRK07529 PRK07529
AMP-binding domain protein; Validated
1154-1639 4.35e-24

AMP-binding domain protein; Validated


Pssm-ID: 236043 [Multi-domain]  Cd Length: 632  Bit Score: 111.20  E-value: 4.35e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1154 TFHELFEQQAKKTPDRAAVSY--------EGQTLTYRELDERSTQLAIYLQAHGVGPD--------------------RL 1205
Cdd:PRK07529    26 STYELLSRAAARHPDAPALSFlldadpldRPETWTYAELLADVTRTANLLHSLGVGPGdvvafllpnlpethfalwggEA 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1206 AGIyVDRSLDMLVG--LLAILKAGGA--YVPLDPsYP----AERLEYMLEDSEVFITLTTSELVNTLSWNGVTTALLDQ- 1276
Cdd:PRK07529   106 AGI-ANPINPLLEPeqIAELLRAAGAkvLVTLGP-FPgtdiWQKVAEVLAALPELRTVVEVDLARYLPGPKRLAVPLIRr 183
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1277 -------DWD-EIAQTASDRKVLTRTVTPENLAYVIYTSGSTGKPKGVMIPHKALTNFLVSMGETPGLTAEDKMLAvtty 1348
Cdd:PRK07529   184 kaharilDFDaELARQPGDRLFSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDTVFC---- 259
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1349 cfdiaALELF----------LPLIKGAHCYICQTEHTKD----------VEKLKRDIRTIKPTVMQATpatwkMLFYSGW 1408
Cdd:PRK07529   260 -----GLPLFhvnallvtglAPLARGAHVVLATPQGYRGpgvianfwkiVERYRINFLSGVPTVYAAL-----LQVPVDG 329
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1409 ENEENVKI-LCGGEALPETLKRYFLD-TGSEAWNMFGPTETTIWSAVQRINDECSRATIGRPIANTQIYI-----TDSQL 1481
Cdd:PRK07529   330 HDISSLRYaLCGAAPLPVEVFRRFEAaTGVRIVEGYGLTEATCVSSVNPPDGERRIGSVGLRLPYQRVRVvilddAGRYL 409
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1482 APVPAGVPGELCIAGDGVAKGYykkeeLTDSRFIDNPFEPGskLYRTGDMAR-------WLPGGRIEYIgridnqvkIR- 1553
Cdd:PRK07529   410 RDCAVDEVGVLCIAGPNVFSGY-----LEAAHNKGLWLEDG--WLNTGDLGRidadgyfWLTGRAKDLI--------IRg 474
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1554 GFRIELGDIESRLSEHPGILECVVVADMDNLA-----AYYTAKhANASLTARELRHFVKNALP---AymVPSYFIQLDHM 1625
Cdd:PRK07529   475 GHNIDPAAIEEALLRHPAVALAAAVGRPDAHAgelpvAYVQLK-PGASATEAELLAFARDHIAeraA--VPKHVRILDAL 551
                          570
                   ....*....|....
gi 1776025254 1626 PLTPNGKIDRNSLK 1639
Cdd:PRK07529   552 PKTAVGKIFKPALR 565
PRK07470 PRK07470
acyl-CoA synthetase; Validated
1161-1651 4.94e-24

acyl-CoA synthetase; Validated


Pssm-ID: 180988 [Multi-domain]  Cd Length: 528  Bit Score: 110.13  E-value: 4.94e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1161 QQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGP-DRLAgIYVDRSLDMLVGLLAILKAGGAYVPLD-PSYP 1238
Cdd:PRK07470    15 QAARRFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKgDRIL-VHSRNCNQMFESMFAAFRLGAVWVPTNfRQTP 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1239 AErLEYMLEDSE--VFI------------TLTTSELVNTLSWNGVTTALldqDWDEIAQTASDRKVLTRTVTPENLAYVI 1304
Cdd:PRK07470    94 DE-VAYLAEASGarAMIchadfpehaaavRAASPDLTHVVAIGGARAGL---DYEALVARHLGARVANAAVDHDDPCWFF 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1305 YTSGSTGKPKGVMIPHKAL----TNFLVSMgeTPGLTAEDKMLAVTtycfdiaalelflPLIKGA--HcYICQTEHTK-- 1376
Cdd:PRK07470   170 FTSGTTGRPKAAVLTHGQMafviTNHLADL--MPGTTEQDASLVVA-------------PLSHGAgiH-QLCQVARGAat 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1377 --------DVEKLKRDIRTIKPTVMQATPATWKMLFysgwENEENVK---------ILCGGEALPETLKRYFLDTGSEAW 1439
Cdd:PRK07470   234 vllpserfDPAEVWALVERHRVTNLFTVPTILKMLV----EHPAVDRydhsslryvIYAGAPMYRADQKRALAKLGKVLV 309
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1440 NMFGPTETT-----IWSAVQRIND--ECSRATIGRPIANTQIYITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDS 1512
Cdd:PRK07470   310 QYFGLGEVTgnitvLPPALHDAEDgpDARIGTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAK 389
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1513 RFIDNPFepgsklyRTGDMARwLPGGRIEYI-GRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMDNL-----AA 1586
Cdd:PRK07470   390 AFRDGWF-------RTGDLGH-LDARGFLYItGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVwgevgVA 461
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1776025254 1587 YYTAKhANASLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLKnidlsgEQLKQR 1651
Cdd:PRK07470   462 VCVAR-DGAPVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVR------EELEER 519
FADD10 cd17635
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ...
1298-1635 5.32e-24

adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.


Pssm-ID: 341290 [Multi-domain]  Cd Length: 340  Bit Score: 106.96  E-value: 5.32e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1298 ENLAYVIYTSGSTGKPKGVMIPHKALtnFLVS---MGETPGLTAEDKMLAVTTYCFDIAALELFLPLIKGAHCYI-CQTE 1373
Cdd:cd17635      1 EDPLAVIFTSGTTGEPKAVLLANKTF--FAVPdilQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTgGENT 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1374 HTKDVEKLkrdIRTIKPTVMQATPATW-KMLFYSGWENEENVKILC---GGEALPETLKRYFLDTG-SEAWNMFGPTETT 1448
Cdd:cd17635     79 TYKSLFKI---LTTNAVTTTCLVPTLLsKLVSELKSANATVPSLRLigyGGSRAIAADVRFIEATGlTNTAQVYGLSETG 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1449 IWSAVQRINDECSRATIGRPIANTQIYITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPFepgsklyRT 1528
Cdd:cd17635    156 TALCLPTDDDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLIDGWV-------NT 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1529 GDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMDN-----LAAYYTAKHANASLTARELR 1603
Cdd:cd17635    229 GDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEefgelVGLAVVASAELDENAIRALK 308
                          330       340       350
                   ....*....|....*....|....*....|..
gi 1776025254 1604 HFVKNALPAYMVPSYFIQLDHMPLTPNGKIDR 1635
Cdd:cd17635    309 HTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
PRK07314 PRK07314
beta-ketoacyl-ACP synthase II;
4592-4934 8.66e-24

beta-ketoacyl-ACP synthase II;


Pssm-ID: 235987 [Multi-domain]  Cd Length: 411  Bit Score: 107.57  E-value: 8.66e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4592 VVGLSCRFPGAETLESYWSLLSEGRSSIGPIP---AERWGCKtpyYAGVIDGvsyFDPDFFLlHEEDVRAMDPQALLVLE 4668
Cdd:PRK07314     6 VTGLGAVSPLGNDVESTWKNLLAGKSGIGPIThfdTSDLAVK---IAGEVKD---FNPDDYM-SRKEARRMDRFIQYGIA 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4669 ECLKLLYHAGYTPEEIKGKPVGVYIG---GRSQHKPDEDSLDHAKNP-----------IVtvgqNYLAANLSQFFDVRGP 4734
Cdd:PRK07314    79 AAKQAVEDAGLEITEENADRIGVIIGsgiGGLETIEEQHITLLEKGPrrvspffvpmaII----NMAAGHVSIRYGAKGP 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4735 SVVVDTACSSALVGMNMAIQALRGGDIQSAIVGGVSllssDASHRLfdrrGI--------LS------KHSSfHVFDERA 4800
Cdd:PRK07314   155 NHSIVTACATGAHAIGDAARLIAYGDADVMVAGGAE----AAITPL----GIagfaaaraLStrnddpERAS-RPFDKDR 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4801 DGVVLGEGVGMVMLKTVKQALEDGDTIYAVVKAASVNNDGR--TAgPATPNLEAQKeVMKDALFKSGKKPEDISYLEANG 4878
Cdd:PRK07314   226 DGFVMGEGAGILVLEELEHAKARGAKIYAEVVGYGMTGDAYhmTA-PAPDGEGAAR-AMKLALKDAGINPEDIDYINAHG 303
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1776025254 4879 SGSIVTDLLELKAIQSVYrSGHSSPLSLGSIKPNIGHPLCAEGIASFIKVVLMLKE 4934
Cdd:PRK07314   304 TSTPAGDKAETQAIKRVF-GEHAYKVAVSSTKSMTGHLLGAAGAVEAIFSVLAIRD 358
A_NRPS_PvdJ-like cd17649
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ...
186-555 1.56e-23

non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341304 [Multi-domain]  Cd Length: 450  Bit Score: 107.45  E-value: 1.56e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  186 PEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDHVGGI-----GMLHLRDVYLGCQEINV 260
Cdd:cd17649     93 PRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAERYGLTPGDRELQFASFNFDGAHeqllpPLICGACVVLRPDELWA 172
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  261 SSETILMEplkwldwIDHYRASV-TWAPNFAFGLVTDFAEEIKDRKwdlSSMRYMLNGGEAMVAKVGRRILE----LLEP 335
Cdd:cd17649    173 SADELAEM-------VRELGVTVlDLPPAYLQQLAEEADRTGDGRP---PSLRLYIFGGEALSPELLRRWLKapvrLFNA 242
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  336 HGlPADAIRpawgmseTSSGVIFSHEFTRAGTSdddhfVEIGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGYY 415
Cdd:cd17649    243 YG-PTEATV-------TPLVWKCEAGAARAGAS-----MPIGRPLGGRSAYILDADLNPVPVGVTGELYIGGEGLARGYL 309
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  416 QRPDLNESVFTEDG-------WFETGDLGFLR-NGRLTITGRTKDAIIINGINYYSHAIESAVEELSEIEtsytAACAVR 487
Cdd:cd17649    310 GRPELTAERFVPDPfgapgsrLYRTGDLARWRdDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVR----EAAVVA 385
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1776025254  488 LGQNSTDQLAIFFVTSAklnDEQMSQLLRNIQSHVSQVIgvtPEYLLP---VQKEEIPKTAIGKIQRTQLK 555
Cdd:cd17649    386 LDGAGGKQLVAYVVLRA---AAAQPELRAQLRTALRASL---PDYMVPahlVFLARLPLTPNGKLDRKALP 450
PLN02787 PLN02787
3-oxoacyl-[acyl-carrier-protein] synthase II
1762-2187 1.60e-23

3-oxoacyl-[acyl-carrier-protein] synthase II


Pssm-ID: 215421 [Multi-domain]  Cd Length: 540  Bit Score: 108.91  E-value: 1.60e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1762 VAIIGISCEFPGAKNHDEFWENLRDGKESIAffnkeELQRFGISKeiaenadyVPAKASIEGKdrfdpSFFQ---ISPKD 1838
Cdd:PLN02787   131 VVVTGMGVVSPLGHDPDVFYNNLLEGVSGIS-----EIERFDCSQ--------FPTRIAGEIK-----SFSTdgwVAPKL 192
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1839 AEFMDPQLRMLLTHSWKAIEDAGYaagqipqTSVFMSASNNSYRALLP----------SDTTESLEtpdgyVSWVLAQSG 1908
Cdd:PLN02787   193 SKRMDKFMLYLLTAGKKALADGGI-------TEDVMKELDKTKCGVLIgsamggmkvfNDAIEALR-----ISYRKMNPF 260
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1909 TIP--------TMISHKLGLRGPSYFVHANCSSSLIGLHSAYKSLLSAESDYALVGG--ATLHTESNIGYVHQPGLNFSS 1978
Cdd:PLN02787   261 CVPfattnmgsAMLAMDLGWMGPNYSISTACATSNFCILNAANHIIRGEADVMLCGGsdAAIIPIGLGGFVACRALSQRN 340
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1979 DGHIKA---FDASADGMIGGEGVAVVLLKKAADAVKDGDHIYALLRGIGVNNDgADKVGFYAPSVKGQADVVQQVMNQTK 2055
Cdd:PLN02787   341 DDPTKAsrpWDMNRDGFVMGEGAGVLLLEELEHAKKRGANIYAEFLGGSFTCD-AYHMTEPHPEGAGVILCIEKALAQSG 419
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2056 IHPESICYVEAHGTGTKLGDPIELAALTNVYRQYTNktqfCGIGSVKTNIGHLDTAAGLAGCIKVVMSLYHQELAPSINY 2135
Cdd:PLN02787   420 VSKEDVNYINAHATSTKAGDLKEYQALMRCFGQNPE----LRVNSTKSMIGHLLGAAGAVEAIATVQAIRTGWVHPNINL 495
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1776025254 2136 KEPNPNTDLAsspFYVVDQKKTLsrEIqthRAALS-SFGLGGTNTHAIFEQFK 2187
Cdd:PLN02787   496 ENPESGVDTK---VLVGPKKERL--DI---KVALSnSFGFGGHNSSILFAPYK 540
PRK08279 PRK08279
long-chain-acyl-CoA synthetase; Validated
1159-1640 1.72e-23

long-chain-acyl-CoA synthetase; Validated


Pssm-ID: 236217 [Multi-domain]  Cd Length: 600  Bit Score: 109.19  E-value: 1.72e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1159 FEQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYP 1238
Cdd:PRK08279    43 FEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQR 122
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1239 AERLEYML------------EDSEVFIT----LTTSELVNTLSWNGVTTALLDQDWDEIAQTASDR-KVLTRTVTPENLA 1301
Cdd:PRK08279   123 GAVLAHSLnlvdakhlivgeELVEAFEEaradLARPPRLWVAGGDTLDDPEGYEDLAAAAAGAPTTnPASRSGVTAKDTA 202
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1302 YVIYTSGSTGKPKGVMIPHKALTNFLVSMGETPGLTAEDKMlavttYCfdiaalelFLPL-------------IKGAHCY 1368
Cdd:PRK08279   203 FYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDVL-----YC--------CLPLyhntggtvawssvLAAGATL 269
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1369 IcqtehtkdvekLKR---------DIRTIKPTVMQ----------ATPATWKmlfysgwENEENVKILCG----GEALPE 1425
Cdd:PRK08279   270 A-----------LRRkfsasrfwdDVRRYRATAFQyigelcryllNQPPKPT-------DRDHRLRLMIGnglrPDIWDE 331
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1426 TLKRYFLDTGSEAWnmfGPTETTIwsavQRINDECSRATIGR-------PIA------NTQIYITDSQ--LAPVPAGVPG 1490
Cdd:PRK08279   332 FQQRFGIPRILEFY---AASEGNV----GFINVFNFDGTVGRvplwlahPYAivkydvDTGEPVRDADgrCIKVKPGEVG 404
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1491 ELC--IAGDGVAKGYYKKEElTDSRFIDNPFEPGSKLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSE 1568
Cdd:PRK08279   405 LLIgrITDRGPFDGYTDPEA-SEKKILRDVFKKGDAWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENALSG 483
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1776025254 1569 HPGILECVV----VADMDNLA--AYYTAkHANASLTARELRHFVKNALPAYMVPsYFIQL-DHMPLTPNGKIDRNSLKN 1640
Cdd:PRK08279   484 FPGVEEAVVygveVPGTDGRAgmAAIVL-ADGAEFDLAALAAHLYERLPAYAVP-LFVRLvPELETTGTFKYRKVDLRK 560
AFD_YhfT-like cd17633
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ...
194-551 2.13e-23

fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain


Pssm-ID: 341288 [Multi-domain]  Cd Length: 320  Bit Score: 104.41  E-value: 2.13e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  194 LTSGSTGTPKAVMLNHRN-IMSMVKGIIQMQgFTREDITFNWMPFDHVGGIGMLhLRDVYLGcQEINVSSETIlmePLKW 272
Cdd:cd17633      7 FTSGTTGLPKAYYRSERSwIESFVCNEDLFN-ISGEDAILAPGPLSHSLFLYGA-ISALYLG-GTFIGQRKFN---PKSW 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  273 LDWIDHYRASVTW-APNFAFGLV-TDFAEeikdrkwdlSSMRYMLNGGEAMVAKVGRRIlellePHGLPADAIRPAWGMS 350
Cdd:cd17633     81 IRKINQYNATVIYlVPTMLQALArTLEPE---------SKIKSIFSSGQKLFESTKKKL-----KNIFPKANLIEFYGTS 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  351 ETS-SGVIFSHEFTRAGTsdddhfveIGSPIPGFSMRIVNDhnelvEEGEIGRFQVSGLSVTSGYyqrpdLNESVFTEDG 429
Cdd:cd17633    147 ELSfITYNFNQESRPPNS--------VGRPFPNVEIEIRNA-----DGGEIGKIFVKSEMVFSGY-----VRGGFSNPDG 208
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  430 WFETGDLGFL-RNGRLTITGRTKDAIIINGINYYSHAIESAVEELSEIETsytaacAVRLGQNST--DQLAIFFVTSAKL 506
Cdd:cd17633    209 WMSVGDIGYVdEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEE------AIVVGIPDArfGEIAVALYSGDKL 282
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 1776025254  507 NDEQMSQLLRniQSHVSQVIgvtPEYLLPVqkEEIPKTAIGKIQR 551
Cdd:cd17633    283 TYKQLKRFLK--QKLSRYEI---PKKIIFV--DSLPYTSSGKIAR 320
PRK08439 PRK08439
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
3405-3779 2.41e-23

3-oxoacyl-(acyl carrier protein) synthase II; Reviewed


Pssm-ID: 236265 [Multi-domain]  Cd Length: 406  Bit Score: 106.36  E-value: 2.41e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3405 VAEFDPLFFgISPREADYVDPQQRLLMTYVWKALEDAGCPPQSLSGTGTGIFIGTGNTGykdlfhranLP-IEGHAATgh 3483
Cdd:PRK08439    52 ITDFDPTEV-MDPKEVKKADRFIQLGLKAAREAMKDAGFLPEELDAERFGVSSASGIGG---------LPnIEKNSII-- 119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3484 mIPSVGPNRMSYFL-----------------NIHGPSEPVETACSSSLVAIHRAV-TAMQNGDCEMAIAGGVNTILTeeA 3545
Cdd:PRK08439   120 -CFEKGPRKISPFFipsalvnmlggfisiehGLKGPNLSSVTACAAGTHAIIEAVkTIMLGGADKMLVVGAESAICP--V 196
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3546 HISySKAGMLSKDGR-------CKTFSADANGYVRGEGVGMVMLKKLEDAERDGNHIYGVIRGTAENhgGRANTLTSPNP 3618
Cdd:PRK08439   197 GIG-GFAAMKALSTRnddpkkaSRPFDKDRDGFVMGEGAGALVLEEYESAKKRGAKIYAEIIGFGES--GDANHITSPAP 273
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3619 KAQADLLVRAYRQAGIDPstVTYIEAHGTGTELGDPIEINGLKAAFKelsnmrgeSQPDVPDhrcgIGSVKSNIGHLELA 3698
Cdd:PRK08439   274 EGPLRAMKAALEMAGNPK--IDYINAHGTSTPYNDKNETAALKELFG--------SKEKVPP----VSSTKGQIGHCLGA 339
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3699 AGISGLIKVLLQMKHKTLVKSLHCETLNPylqltdspfyivqekqewksvtDCDGNELP---RRAGI-----SSFGIGGV 3770
Cdd:PRK08439   340 AGAIEAVISIMAMRDGILPPTINQETPDP----------------------ECDLDYIPnvaRKAELnvvmsNSFGFGGT 397

                   ....*....
gi 1776025254 3771 NAHIVIEEY 3779
Cdd:PRK08439   398 NGVVIFKKV 406
FACL_like_4 cd05944
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
186-555 2.62e-23

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341266 [Multi-domain]  Cd Length: 359  Bit Score: 105.26  E-value: 2.62e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  186 PEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDHVGGIGMLHLRDVYLGcqeinvsSETI 265
Cdd:cd05944      1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASG-------AHVV 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  266 LMEPLKWLD-------W--IDHYRasvtwaPNFAFGLVTDFAEEIK---DRkwDLSSMRYMLNGGEAMVAKVGRRIlell 333
Cdd:cd05944     74 LAGPAGYRNpglfdnfWklVERYR------ITSLSTVPTVYAALLQvpvNA--DISSLRFAMSGAAPLPVELRARF---- 141
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  334 EPH-GLPadaIRPAWGMSETSSGVifshefTRAGTSDDDHFVEIGSPIPGFSMRIV---NDHNELVEEG--EIGRFQVSG 407
Cdd:cd05944    142 EDAtGLP---VVEGYGLTEATCLV------AVNPPDGPKRPGSVGLRLPYARVRIKvldGVGRLLRDCApdEVGEICVAG 212
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  408 LSVTSGYYQRpDLNESVFTEDGWFETGDLGFL-RNGRLTITGRTKDAIIINGinyysHAIESA-VEELSEIETSYTAACA 485
Cdd:cd05944    213 PGVFGGYLYT-EGNKNAFVADGWLNTGDLGRLdADGYLFITGRAKDLIIRGG-----HNIDPAlIEEALLRHPAVAFAGA 286
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  486 VRLGQNSTDQLAIFFVTSAKLNDEQMSQLLRNIQSHVSQVIGVtPEYLLPVqkEEIPKTAIGKIQRTQLK 555
Cdd:cd05944    287 VGQPDAHAGELPVAYVQLKPGAVVEEEELLAWARDHVPERAAV-PKHIEVL--EELPVTAVGKVFKPALR 353
PRK05691 PRK05691
peptide synthase; Validated
1161-1731 3.15e-23

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 110.64  E-value: 3.15e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1161 QQAKKTPDRAAVSY------EGQTLTYRELDERSTQLAIYLQAHGVGPDRlAGIYVDRSLDMLVGLLAILKAGGAYVPld 1234
Cdd:PRK05691    17 RRAAQTPDRLALRFladdpgEGVVLSYRDLDLRARTIAAALQARASFGDR-AVLLFPSGPDYVAAFFGCLYAGVIAVP-- 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1235 pSYPAE--------RLEYMLEDSEVFITLTTSELVNTL------------SWNGVTT--ALLDQDWDEIAqtasdrkvlt 1292
Cdd:PRK05691    94 -AYPPEsarrhhqeRLLSIIADAEPRLLLTVADLRDSLlqmeelaaanapELLCVDTldPALAEAWQEPA---------- 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1293 rtVTPENLAYVIYTSGSTGKPKGVMIPHKAL--TNFLVSMGETPGLTAEDKMLAVTTYCFDIAAL-ELFLPLIKGAHCYI 1369
Cdd:PRK05691   163 --LQPDDIAFLQYTSGSTALPKGVQVSHGNLvaNEQLIRHGFGIDLNPDDVIVSWLPLYHDMGLIgGLLQPIFSGVPCVL 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1370 CQTEHTkdvekLKRDIR----------TI--------KPTVMQATPATWKMLFYSGWEneenvKILCGGEALPE-TLKRY 1430
Cdd:PRK05691   241 MSPAYF-----LERPLRwleaiseyggTIsggpdfayRLCSERVSESALERLDLSRWR-----VAYSGSEPIRQdSLERF 310
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1431 ---FLDTGSEAWNMF---GPTETTIWSA---------VQRINDEC---SRA---------TIGRPIANTQIYITDSQ-LA 1482
Cdd:PRK05691   311 aekFAACGFDPDSFFasyGLAEATLFVSggrrgqgipALELDAEAlarNRAepgtgsvlmSCGRSQPGHAVLIVDPQsLE 390
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1483 PVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPfepGSKLYRTGDMArWLPGGRIEYIGRIDNQVKIRGFRIELGDI 1562
Cdd:PRK05691   391 VLGDNRVGEIWASGPSIAHGYWRNPEASAKTFVEHD---GRTWLRTGDLG-FLRDGELFVTGRLKDMLIVRGHNLYPQDI 466
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1563 ESRLSEhpgileCVVVADMDNLAAYYTAKHANASL-TARELRHFVKNALPA---------------YMVPSYFIQLD--H 1624
Cdd:PRK05691   467 EKTVER------EVEVVRKGRVAAFAVNHQGEEGIgIAAEISRSVQKILPPqaliksirqavaeacQEAPSVVLLLNpgA 540
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1625 MPLTPNGKIDRNSLKN------ID-------LSGEQLKQRQTSPKNIQDTVFTIWQEVLKTSDIEWDDGFFDVGGDSLLA 1691
Cdd:PRK05691   541 LPKTSSGKLQRSACRLrladgsLDsyalfpaLQAVEAAQTAASGDELQARIAAIWCEQLKVEQVAADDHFFLLGGNSIAA 620
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|
gi 1776025254 1692 VTVADRIKHELSCEFSVTDLFEYSTIKNISQYITEQRMGN 1731
Cdd:PRK05691   621 TQVVARLRDELGIDLNLRQLFEAPTLAAFSAAVARQLAGG 660
PRK12582 PRK12582
acyl-CoA synthetase; Provisional
28-437 3.67e-23

acyl-CoA synthetase; Provisional


Pssm-ID: 237144 [Multi-domain]  Cd Length: 624  Bit Score: 108.21  E-value: 3.67e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254   28 PATIPEVLYRTAAELGDTkgiIYL----QPDGTEVYQSYRrlwdDGLRIVKGLRQS----GLKAKQSVILqLGDNS--QL 97
Cdd:PRK12582    48 PRSIPHLLAKWAAEAPDR---PWLaqrePGHGQWRKVTYG----EAKRAVDALAQAlldlGLDPGRPVMI-LSGNSieHA 119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254   98 LPAFwGCVLTGVVPAPlaVPPTYAESSSGTQKLKDAWTLLdKPAVI--TDRGMHQEMLDWAKEQGL---------EGFRA 166
Cdd:PRK12582   120 LMTL-AAMQAGVPAAP--VSPAYSLMSHDHAKLKHLFDLV-KPRVVfaQSGAPFARALAALDLLDVtvvhvtgpgEGIAS 195
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  167 IIVEDLLS----AEADTDWHQSSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTRED---ITFNWMPFDH 239
Cdd:PRK12582   196 IAFADLAAtpptAAVAAAIAAITPDTVAKYLFTSGSTGMPKAVINTQRMMCANIAMQEQLRPREPDPpppVSLDWMPWNH 275
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  240 ------------VGGiGMLHLRDVYLGCQEInvsSETI--LMEPLKWldwidhYRASVtwaPnFAFGLVTDFAEEIKD-R 304
Cdd:PRK12582   276 tmggnanfngllWGG-GTLYIDDGKPLPGMF---EETIrnLREISPT------VYGNV---P-AGYAMLAEAMEKDDAlR 341
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  305 KWDLSSMRYMLNGGEAM------------VAKVGRRILellephglpadaIRPAWGMSETSSGVIFSHEFT-RAGtsddd 371
Cdd:PRK12582   342 RSFFKNLRLMAYGGATLsddlyermqalaVRTTGHRIP------------FYTGYGATETAPTTTGTHWDTeRVG----- 404
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1776025254  372 hfvEIGSPIPGFSMRivndhneLVEEGEIGRFQVSGLSVTSGYYQRPDLNESVFTEDGWFETGDLG 437
Cdd:PRK12582   405 ---LIGLPLPGVELK-------LAPVGDKYEVRVKGPNVTPGYHKDPELTAAAFDEEGFYRLGDAA 460
cond_enzymes cd00327
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ...
4733-4989 4.42e-23

Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) Claisen-like condensation reaction. Members are share strong structural similarity, and are involved in the synthesis and degradation of fatty acids, and the production of polyketides, a diverse group of natural products.


Pssm-ID: 238201 [Multi-domain]  Cd Length: 254  Bit Score: 101.75  E-value: 4.42e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4733 GPSVVVDTACSSALVGMNMAIQALRGGDIQSAIVGGVsllssdashrlfdrrgilskhssfhvfderaDGVVLGEGVGMV 4812
Cdd:cd00327     59 GPAYSVNQACATGLTALALAVQQVQNGKADIVLAGGS-------------------------------EEFVFGDGAAAA 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4813 MLKTVKQALEDGDTIYAVVKAASVNNDGRTAGPAtPNLEAQKEVMKDALFKSGKKPEDISYLEANGSGSIVTDLLELKAI 4892
Cdd:cd00327    108 VVESEEHALRRGAHPQAEIVSTAATFDGASMVPA-VSGEGLARAARKALEGAGLTPSDIDYVEAHGTGTPIGDAVELALG 186
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4893 QSVYRSGHSSPlslGSIKPNIGHPLCAEGIASFIKVVLMLKerrfvpflsgekemahfdqqkanitfsRALEKWTDSQPT 4972
Cdd:cd00327    187 LDPDGVRSPAV---SATLIMTGHPLGAAGLAILDELLLMLE---------------------------HEFIPPTPREPR 236
                          250
                   ....*....|....*...
gi 1776025254 4973 AA-INCFADGGTNVHVIV 4989
Cdd:cd00327    237 TVlLLGFGLGGTNAAVVL 254
PRK08722 PRK08722
beta-ketoacyl-ACP synthase II;
3341-3778 4.45e-23

beta-ketoacyl-ACP synthase II;


Pssm-ID: 181539 [Multi-domain]  Cd Length: 414  Bit Score: 105.47  E-value: 4.45e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3341 VAIVGISGRFPGAMDIDEFWKNLEEGKDSITEVpkdrwdwrEHYgnpdtDVNKTDIKWGGFIDGvaeFDPLFFgISPREA 3420
Cdd:PRK08722     6 VVVTGMGMLSPVGNTVESSWKALLAGQSGIVNI--------EHF-----DTTNFSTRFAGLVKD---FNCEEY-MSKKDA 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3421 DYVDPQQRLLMTYVWKALEDAGCPPQSLSGTGTGIFIGTG-------NTGYKDLFHRANLPIEGHAATGHMIPSVGPNrM 3493
Cdd:PRK08722    69 RKMDLFIQYGIAAGIQALDDSGLEVTEENAHRIGVAIGSGigglgliEAGHQALVEKGPRKVSPFFVPSTIVNMIAGN-L 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3494 SYFLNIHGPSEPVETACSSSLVAIHRAVTAMQNGDCEMAIAGGVNTILTEEAHISYSKAGMLSKDGR-----CKTFSADA 3568
Cdd:PRK08722   148 SIMRGLRGPNIAISTACTTGLHNIGHAARMIAYGDADAMVAGGAEKASTPLGMAGFGAAKALSTRNDepqkaSRPWDKDR 227
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3569 NGYVRGEGVGMVMLKKLEDAERDGNHIYGVIRGTAENhgGRANTLTSPNPKAQADLLVR--AYRQAGIDPSTVTYIEAHG 3646
Cdd:PRK08722   228 DGFVLGDGAGMMVLEEYEHAKARGAKIYAELVGFGMS--GDAYHMTSPSEDGSGGALAMeaAMRDAGVTGEQIGYVNAHG 305
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3647 TGTELGDPIEINGLKAAFKElsnmrgESQPDVPdhrcgIGSVKSNIGHLELAAG-ISGLIKVLlqmkhkTLVKSLHCETL 3725
Cdd:PRK08722   306 TSTPAGDVAEIKGIKRALGE------AGSKQVL-----VSSTKSMTGHLLGAAGsVEAIITVM------SLVDQIVPPTI 368
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1776025254 3726 NpylqlTDSPF------YIVQEKQEWKSVtdcdgnelpRRAGISSFGIGGVNAHIVIEE 3778
Cdd:PRK08722   369 N-----LDDPEegldidLVPHTARKVESM---------EYAICNSFGFGGTNGSLIFKK 413
Dip2 cd05905
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ...
48-566 4.95e-23

Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.


Pssm-ID: 341231 [Multi-domain]  Cd Length: 571  Bit Score: 107.43  E-value: 4.95e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254   48 IIYLQPDGTEVYQ-SYRRLWDDGLRIVKGLR-QSGLKAKQSVILQLGDNSQLLPAFWGCVLTGVVPAPLAVPPTYAESSS 125
Cdd:cd05905      2 YTLLDSKGKEATTlTWGKLLSRAEKIAAVLQkKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGF 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  126 --GTQKLKDAWTlldkpAVITDRGmHQEMLDWAKEQGL----EGFRAIIVEDLLS---AEADTDWHQSSP---EDLALLL 193
Cdd:cd05905     82 llGTCKVRVALT-----VEACLKG-LPKKLLKSKTAAEiakkKGWPKILDFVKIPkskRSKLKKWGPHPPtrdGDTAYIE 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  194 LTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWmpFDHVGGIGMLH--LRDVYLGCQEINVSSETILMEPLK 271
Cdd:cd05905    156 YSFSSDGSLSGVAVSHSSLLAHCRALKEACELYESRPLVTV--LDFKSGLGLWHgcLLSVYSGHHTILIPPELMKTNPLL 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  272 WLDWIDHYRASVTWAP----NFAFGLVTDFAEEIKDRKWDLSSMRyMLnggeaMVAKVGR-------RILELLEPHGLPA 340
Cdd:cd05905    234 WLQTLSQYKVRDAYVKlrtlHWCLKDLSSTLASLKNRDVNLSSLR-MC-----MVPCENRprisscdSFLKLFQTLGLSP 307
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  341 DAI----------RPAW-GMSETSSG-VIFS-----HEFTRAGTSDDDHFV---EIGSPIPGFSMRIVN-DHNELVEEGE 399
Cdd:cd05905    308 RAVstefgtrvnpFICWqGTSGPEPSrVYLDmralrHGVVRLDERDKPNSLplqDSGKVLPGAQVAIVNpETKGLCKDGE 387
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  400 IGRFQVSGLSVTSGYYQRPDLNESVF------------TEDGWFETGDLGFLRNGRLT-----------ITGRTKDAIII 456
Cdd:cd05905    388 IGEIWVNSPANASGYFLLDGETNDTFkvfpstrlstgiTNNSYARTGLLGFLRPTKCTdlnveehdllfVVGSIDETLEV 467
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  457 NGINYYSHAIESAVEELSeietSYTAACAVRlgqnSTDQLAIFFVTSAKLNDEQMSQLLRNIQSHVSQVIGVTPEYLLPV 536
Cdd:cd05905    468 RGLRHHPSDIEATVMRVH----PYRGRCAVF----SITGLVVVVAEQPPGSEEEALDLVPLVLNAILEEHQVIVDCVALV 539
                          570       580       590
                   ....*....|....*....|....*....|
gi 1776025254  537 QKEEIPKTAIGKIQRTQLKTSFENGEFDHL 566
Cdd:cd05905    540 PPGSLPKNPLGEKQRMEIRQAFLAGKLHPI 569
LC_FACS_euk1 cd17639
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ...
58-452 6.48e-23

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.


Pssm-ID: 341294 [Multi-domain]  Cd Length: 507  Bit Score: 106.53  E-value: 6.48e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254   58 VYQSYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNSQLLPAFWGCVLTGVVPAPLavpptYAEsssgtqklkdawtlL 137
Cdd:cd17639      4 KYMSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTV-----YAT--------------L 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  138 DKPAVITdrGMHQEmldwakeqgleGFRAIIvedllsaeadTDwhqSSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVK 217
Cdd:cd17639     65 GEDALIH--SLNET-----------ECSAIF----------TD---GKPDDLACIMYTSGSTGNPKGVMLTHGNLVAGIA 118
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  218 GIIQM--QGFTREDITFNWMPFDHV------------GG-IGMLHLR----DVYLGCQ-EINVSSETILME-PLKWldwi 276
Cdd:cd17639    119 GLGDRvpELLGPDDRYLAYLPLAHIfelaaenvclyrGGtIGYGSPRtltdKSKRGCKgDLTEFKPTLMVGvPAIW---- 194
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  277 DHYR----ASVTWAPNFAFGLVtDFAEEIKDR--KWDLSSM------------------RYMLNGGEAMVAKVGRRILEL 332
Cdd:cd17639    195 DTIRkgvlAKLNPMGGLKRTLF-WTAYQSKLKalKEGPGTPlldelvfkkvraalggrlRYMLSGGAPLSADTQEFLNIV 273
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  333 LEPhglpadaIRPAWGMSETSSGvifsheftrAGTSDDDHFV--EIGSPIPGFSMRIVNdhnelVEE-----------GE 399
Cdd:cd17639    274 LCP-------VIQGYGLTETCAG---------GTVQDPGDLEtgRVGPPLPCCEIKLVD-----WEEggystdkppprGE 332
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1776025254  400 IgrfQVSGLSVTSGYYQRPDLNESVFTEDGWFETGDLG-FLRNGRLTITGRTKD 452
Cdd:cd17639    333 I---LIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGeFHPDGTLKIIDRKKD 383
A_NRPS_GliP_like cd17653
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ...
184-555 7.84e-23

nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341308 [Multi-domain]  Cd Length: 433  Bit Score: 105.08  E-value: 7.84e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  184 SSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKgiiqmqgftreditfnWMPFD-HVG-GIGMLHLRDVYLGCQeINVS 261
Cdd:cd17653    102 DSPDDLAYIIFTSGSTGIPKGVMVPHRGVLNYVS----------------QPPARlDVGpGSRVAQVLSIAFDAC-IGEI 164
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  262 SETI-------LMEPLKwlDWIDHYRaSVTwapnfAFGLVTDFAEEIKDRkwDLSSMRYMLNGGEAMVAKV------GRR 328
Cdd:cd17653    165 FSTLcnggtlvLADPSD--PFAHVAR-TVD-----ALMSTPSILSTLSPQ--DFPNLKTIFLGGEAVPPSLldrwspGRR 234
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  329 ILEllephglpadairpAWGMSETSsgVIFSHEFTRAGTsdddhFVEIGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGL 408
Cdd:cd17653    235 LYN--------------AYGPTECT--ISSTMTELLPGQ-----PVTIGKPIPNSTCYILDADLQPVPEGVVGEICISGV 293
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  409 SVTSGYYQRPDLNESVFTEDGW------FETGDLGFL-RNGRLTITGRTKDAIIING--INYYshAIESAVEELSEIETS 479
Cdd:cd17653    294 QVARGYLGNPALTASKFVPDPFwpgsrmYRTGDYGRWtEDGGLEFLGREDNQVKVRGfrINLE--EIEEVVLQSQPEVTQ 371
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1776025254  480 YTAacavrlgQNSTDQLaIFFVTSAKLNDEQMSQLLRNI--QSHVSQVIgvtpeyllpVQKEEIPKTAIGKIQRTQLK 555
Cdd:cd17653    372 AAA-------IVVNGRL-VAFVTPETVDVDGLRSELAKHlpSYAVPDRI---------IALDSFPLTANGKVDRKALR 432
FACL_like_1 cd05910
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
1177-1578 8.60e-23

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341236 [Multi-domain]  Cd Length: 457  Bit Score: 105.62  E-value: 8.60e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1177 QTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLEDSE--VFIt 1254
Cdd:cd05910      1 SRLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAEpdAFI- 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1255 lttselvntlswnGVTTALLDqdwdeiaqtasdrkvltrtvtpenlAYVIYTSGSTGKPKGVMIPHKALTNFLVSMGETP 1334
Cdd:cd05910     80 -------------GIPKADEP-------------------------AAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLY 121
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1335 GLTAEDKMLAvttyCFDIAAleLFLPLIkGAHCYICQTEHTK----DVEKLKRDIRTIKPTVMQATPATWKMLFYSGWEN 1410
Cdd:cd05910    122 GIRPGEVDLA----TFPLFA--LFGPAL-GLTSVIPDMDPTRparaDPQKLVGAIRQYGVSIVFGSPALLERVARYCAQH 194
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1411 EENV----KILCGGEALP----ETLKRyFLDTGSEAWNMFGPTETTIWSAVQRINDECSRAT---------IGRPIANTQ 1473
Cdd:cd05910    195 GITLpslrRVLSAGAPVPialaARLRK-MLSDEAEILTPYGATEALPVSSIGSRELLATTTAatsggagtcVGRPIPGVR 273
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1474 ---IYITDSQLAP------VPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPFEpgSKLYRTGDMARWLPGGRIEYIG 1544
Cdd:cd05910    274 vriIEIDDEPIAEwddtleLPRGEIGEITVTGPTVTPTYVNRPVATALAKIDDNSE--GFWHRMGDLGYLDDEGRLWFCG 351
                          410       420       430
                   ....*....|....*....|....*....|....
gi 1776025254 1545 RIDNQVKIRGFRIELGDIESRLSEHPGILECVVV 1578
Cdd:cd05910    352 RKAHRVITTGGTLYTEPVERVFNTHPGVRRSALV 385
PRK06145 PRK06145
acyl-CoA synthetase; Validated
176-559 1.12e-22

acyl-CoA synthetase; Validated


Pssm-ID: 102207 [Multi-domain]  Cd Length: 497  Bit Score: 105.74  E-value: 1.12e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  176 EADTDWHQSSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDHVGGIGMLHLRDVYLG- 254
Cdd:PRK06145   138 LEIPPQAAVAPTDLVRLMYTSGTTDRPKGVMHSYGNLHWKSIDHVIALGLTASERLLVVGPLYHVGAFDLPGIAVLWVGg 217
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  255 --CQEINVSSETILMEplkwldwIDHYRASVTW-APNFAFGLVTdfaeeIKDR-KWDLSSMRYMLNGGEAMVAKVGRRIL 330
Cdd:PRK06145   218 tlRIHREFDPEAVLAA-------IERHRLTCAWmAPVMLSRVLT-----VPDRdRFDLDSLAWCIGGGEKTPESRIRDFT 285
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  331 ELLEpHGLPADairpAWGMSETSSGVIF---SHEFTRAGTSdddhfveiGSPIPGFSMRIVNDHNELVEEGEIGRFQVSG 407
Cdd:PRK06145   286 RVFT-RARYID----AYGLTETCSGDTLmeaGREIEKIGST--------GRALAHVEIRIADGAGRWLPPNMKGEICMRG 352
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  408 LSVTSGYYQRPDLNESVFTeDGWFETGDLGFL-RNGRLTITGRTKDAIIINGINYYSHAIESAVEELSEI-ETSYTAACA 485
Cdd:PRK06145   353 PKVTKGYWKDPEKTAEAFY-GDWFRSGDVGYLdEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVaEAAVIGVHD 431
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1776025254  486 VRLGQNstdqlaiffVTSAKLNDEQMSQLLRNIQSHVSQVIGV--TPEYLlpVQKEEIPKTAIGKIQRTQLKTSFE 559
Cdd:PRK06145   432 DRWGER---------ITAVVVLNPGATLTLEALDRHCRQRLASfkVPRQL--KVRDELPRNPSGKVLKRVLRDELN 496
PRK08722 PRK08722
beta-ketoacyl-ACP synthase II;
4590-4984 1.34e-22

beta-ketoacyl-ACP synthase II;


Pssm-ID: 181539 [Multi-domain]  Cd Length: 414  Bit Score: 104.31  E-value: 1.34e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4590 IAVVGLSCRFPGAETLESYWSLLSEGRSSIGPIPAERWGCKTPYYAGVIDGvsyFDPDFFLlHEEDVRAMDPQALLVLEE 4669
Cdd:PRK08722     6 VVVTGMGMLSPVGNTVESSWKALLAGQSGIVNIEHFDTTNFSTRFAGLVKD---FNCEEYM-SKKDARKMDLFIQYGIAA 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4670 CLKLLYHAGYTPEEIKGKPVGVYIGG--------RSQHK------PDEDSLDHAKNPIVtvgqNYLAANLSQFFDVRGPS 4735
Cdd:PRK08722    82 GIQALDDSGLEVTEENAHRIGVAIGSgigglgliEAGHQalvekgPRKVSPFFVPSTIV----NMIAGNLSIMRGLRGPN 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4736 VVVDTACSSALVGMNMAIQALRGGDIQSAIVGGVSLLSSDASHRLFDRRGILSK-----HSSFHVFDERADGVVLGEGVG 4810
Cdd:PRK08722   158 IAISTACTTGLHNIGHAARMIAYGDADAMVAGGAEKASTPLGMAGFGAAKALSTrndepQKASRPWDKDRDGFVLGDGAG 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4811 MVMLKTVKQALEDGDTIYAVVKAASVNNDGRTAGPATPNLEAQKEVMKDALFKSGKKPEDISYLEANGSGSIVTDLLELK 4890
Cdd:PRK08722   238 MMVLEEYEHAKARGAKIYAELVGFGMSGDAYHMTSPSEDGSGGALAMEAAMRDAGVTGEQIGYVNAHGTSTPAGDVAEIK 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4891 AIQSVYRSGHSSPLSLGSIKPNIGHPLCAEGIASFIKVVLMLKERRFVPFLSGEKEmahfdQQKANITFSRALEKWTDSQ 4970
Cdd:PRK08722   318 GIKRALGEAGSKQVLVSSTKSMTGHLLGAAGSVEAIITVMSLVDQIVPPTINLDDP-----EEGLDIDLVPHTARKVESM 392
                          410
                   ....*....|....
gi 1776025254 4971 PTAAINCFADGGTN 4984
Cdd:PRK08722   393 EYAICNSFGFGGTN 406
PRK08751 PRK08751
long-chain fatty acid--CoA ligase;
183-557 1.41e-22

long-chain fatty acid--CoA ligase;


Pssm-ID: 181546 [Multi-domain]  Cd Length: 560  Bit Score: 106.11  E-value: 1.41e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  183 QSSPEDLALLLLTSGSTGTPKAVMLNHRNI---MSMVKGIIQMQGFTRE--DITFNWMPFDHVGGI---GMLHLRdvYLG 254
Cdd:PRK08751   204 QIEPDDIAFLQYTGGTTGVAKGAMLTHRNLvanMQQAHQWLAGTGKLEEgcEVVITALPLYHIFALtanGLVFMK--IGG 281
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  255 CQEI--NVSSETILMEPLKwldwidHYRASVTWAPNFAFG--LVTDFAEEIkdrkwDLSSMRYMLNGGEAMVAKVGRRIL 330
Cdd:PRK08751   282 CNHLisNPRDMPGFVKELK------KTRFTAFTGVNTLFNglLNTPGFDQI-----DFSSLKMTLGGGMAVQRSVAERWK 350
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  331 ELLephGLPadaIRPAWGMSETSSGVIFSheftraGTSDDDHFVEIGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSV 410
Cdd:PRK08751   351 QVT---GLT---LVEAYGLTETSPAACIN------PLTLKEYNGSIGLPIPSTDACIKDDAGTVLAIGEIGELCIKGPQV 418
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  411 TSGYYQRPDLNESVFTEDGWFETGDLGFL-RNGRLTITGRTKDAIIINGINYYSHAIESAVEELSEIETsyTAACAVRLG 489
Cdd:PRK08751   419 MKGYWKRPEETAKVMDADGWLHTGDIARMdEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLE--VAAVGVPDE 496
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1776025254  490 QNSTDQLAIFFVTSAKLNDEQMSQLLRniqshvSQVIGVTPEYLLPVQKeEIPKTAIGKIQRTQLKTS 557
Cdd:PRK08751   497 KSGEIVKVVIVKKDPALTAEDVKAHAR------ANLTGYKQPRIIEFRK-ELPKTNVGKILRRELRDA 557
caiC PRK08008
putative crotonobetaine/carnitine-CoA ligase; Validated
1154-1639 1.75e-22

putative crotonobetaine/carnitine-CoA ligase; Validated


Pssm-ID: 181195 [Multi-domain]  Cd Length: 517  Bit Score: 105.15  E-value: 1.75e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1154 TFHELFEQQAKKTPDRAAVSYEG-----QTLTYRELDERSTQLAIYLQAHGVGP-DRLAgIYVDRSLDMLVGLLAILKAG 1227
Cdd:PRK08008     8 HLRQMWDDLADVYGHKTALIFESsggvvRRYSYLELNEEINRTANLFYSLGIRKgDKVA-LHLDNCPEFIFCWFGLAKIG 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1228 GAYVPLDPSYPAERLEYMLEDSEVFITLTTSELV-----------NTLSWNGVTTALLDQ-----DWDEIAQTASDRKVL 1291
Cdd:PRK08008    87 AIMVPINARLLREESAWILQNSQASLLVTSAQFYpmyrqiqqedaTPLRHICLTRVALPAddgvsSFTQLKAQQPATLCY 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1292 TRTVTPENLAYVIYTSGSTGKPKGVMIPHkalTNFLVSMGETP---GLTAEDKMLAVTTYC---FDIAALelfLPLIKGA 1365
Cdd:PRK08008   167 APPLSTDDTAEILFTSGTTSRPKGVVITH---YNLRFAGYYSAwqcALRDDDVYLTVMPAFhidCQCTAA---MAAFSAG 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1366 HCYICqtehtkdVEKLK-----RDIRTIKPTVMQATPATWKMLFY---SGWENEENVKILCGGEALPETLKRYFLDT-GS 1436
Cdd:PRK08008   241 ATFVL-------LEKYSarafwGQVCKYRATITECIPMMIRTLMVqppSANDRQHCLREVMFYLNLSDQEKDAFEERfGV 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1437 EAWNMFGPTETTIWSAVQRINDECSRATIGRPIANTQIYITDSQLAPVPAGVPGELCI---AGDGVAKGYYKKEELTDSr 1513
Cdd:PRK08008   314 RLLTSYGMTETIVGIIGDRPGDKRRWPSIGRPGFCYEAEIRDDHNRPLPAGEIGEICIkgvPGKTIFKEYYLDPKATAK- 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1514 fidnPFEPGSKLYrTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVV--VADM--DNLAAYYT 1589
Cdd:PRK08008   393 ----VLEADGWLH-TGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVvgIKDSirDEAIKAFV 467
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1590 AKHANASLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLK 1639
Cdd:PRK08008   468 VLNEGETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
Firefly_Luc cd17642
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ...
18-555 2.17e-22

insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341297 [Multi-domain]  Cd Length: 532  Bit Score: 105.30  E-value: 2.17e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254   18 GEPLHisEKQPATIPEVLYRTAAELGDTKGIIYLQPDGTEVYQSYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNSQL 97
Cdd:cd17642      5 PGPFY--PLEDGTAGEQLHKAMKRYASVPGTIAFTDAHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQF 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254   98 LPAFWGCVLTGVVPAPLAVppTYAE-----------------SSSGTQKL---KDAWTLLDKPAV---ITDRGMHQEMLD 154
Cdd:cd17642     83 FLPVIAGLFIGVGVAPTND--IYNEreldhslniskptivfcSKKGLQKVlnvQKKLKIIKTIIIldsKEDYKGYQCLYT 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  155 WAKEQGLEGFRaiiVEDLLSAEADTDwhqsspEDLALLLLTSGSTGTPKAVMLNHRNI---MSMVKGIIQMQGFTREDIT 231
Cdd:cd17642    161 FITQNLPPGFN---EYDFKPPSFDRD------EQVALIMNSSGSTGLPKGVQLTHKNIvarFSHARDPIFGNQIIPDTAI 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  232 FNWMPFDHvgGIGMLHLRDvYLGCqeinvSSETILM---EPLKWLDWIDHYRASVTW--APNFAFglvtdFAEEIKDRKW 306
Cdd:cd17642    232 LTVIPFHH--GFGMFTTLG-YLIC-----GFRVVLMykfEEELFLRSLQDYKVQSALlvPTLFAF-----FAKSTLVDKY 298
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  307 DLSSMRYMLNGGEAMVAKVGRRILELLephGLPadAIRPAWGMSETSSGVIFSHE-FTRAGTSdddhfveiGSPIPGFSM 385
Cdd:cd17642    299 DLSNLHEIASGGAPLSKEVGEAVAKRF---KLP--GIRQGYGLTETTSAILITPEgDDKPGAV--------GKVVPFFYA 365
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  386 RIVN-DHNELVEEGEIGRFQVSGLSVTSGYYQRPDLNESVFTEDGWFETGDLGFLRN-GRLTITGRTKDAIIINGINYYS 463
Cdd:cd17642    366 KVVDlDTGKTLGPNERGELCVKGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYDEdGHFFIVDRLKSLIKYKGYQVPP 445
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  464 HAIES-----------AVEELSEIETSYTAACAVRL--GQNSTDQLAIFFVTSAKLNdeqmSQLLRniqshvSQVIGVtp 530
Cdd:cd17642    446 AELESillqhpkifdaGVAGIPDEDAGELPAAVVVLeaGKTMTEKEVMDYVASQVST----AKRLR------GGVKFV-- 513
                          570       580
                   ....*....|....*....|....*
gi 1776025254  531 eyllpvqkEEIPKTAIGKIQRTQLK 555
Cdd:cd17642    514 --------DEVPKGLTGKIDRRKIR 530
PRK06178 PRK06178
acyl-CoA synthetase; Validated
171-559 2.64e-22

acyl-CoA synthetase; Validated


Pssm-ID: 235724 [Multi-domain]  Cd Length: 567  Bit Score: 105.12  E-value: 2.64e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  171 DLLSAEAD----TDWHQSSPEDLALLLLTSGSTGTPKAVMLNHRN-IMSMVKGIIQMQGFTREDITFNWMPFDHVGG--I 243
Cdd:PRK06178   189 DLLPALRActapVPLPPPALDALAALNYTGGTTGMPKGCEHTQRDmVYTAAAAYAVAVVGGEDSVFLSFLPEFWIAGenF 268
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  244 GMLHlrDVYLGCQeinvsseTILM---EPLKWLDWIDHYRASVTwapnfafGLVTDFAEEIKD----RKWDLSSMRymln 316
Cdd:PRK06178   269 GLLF--PLFSGAT-------LVLLarwDAVAFMAAVERYRVTRT-------VMLVDNAVELMDhprfAEYDLSSLR---- 328
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  317 ggEAMVAKVGRRilelLEP------HGLPADAIRPA-WGMSETSSgvifSHEFTrAGTSDDDH-------FVeiGSPIPG 382
Cdd:PRK06178   329 --QVRVVSFVKK----LNPdyrqrwRALTGSVLAEAaWGMTETHT----CDTFT-AGFQDDDFdllsqpvFV--GLPVPG 395
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  383 FSMRIVN-DHNELVEEGEIGRFQVSGLSVTSGYYQRPDLNESVFtEDGWFETGDLG-FLRNGRLTITGRTKDAIIINGIN 460
Cdd:PRK06178   396 TEFKICDfETGELLPLGAEGEIVVRTPSLLKGYWNKPEATAEAL-RDGWLHTGDIGkIDEQGFLHYLGRRKEMLKVNGMS 474
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  461 YYSHAIESAVEELSEIEtsytaACAVrLGQNSTD--QLAIFFVT---SAKLNDEQMSQLLRNiQSHVSQVigvtPE-YLL 534
Cdd:PRK06178   475 VFPSEVEALLGQHPAVL-----GSAV-VGRPDPDkgQVPVAFVQlkpGADLTAAALQAWCRE-NMAVYKV----PEiRIV 543
                          410       420
                   ....*....|....*....|....*
gi 1776025254  535 pvqkEEIPKTAIGKIQRTQLKTSFE 559
Cdd:PRK06178   544 ----DALPMTATGKVRKQDLQALAE 564
PRK07059 PRK07059
Long-chain-fatty-acid--CoA ligase; Validated
185-555 3.95e-22

Long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235923 [Multi-domain]  Cd Length: 557  Bit Score: 104.72  E-value: 3.95e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  185 SPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVkgiIQMQ-----GFTRED-----ITFNWMPFDHV-------------G 241
Cdd:PRK07059   202 GPDDVAFLQYTGGTTGVSKGATLLHRNIVANV---LQMEawlqpAFEKKPrpdqlNFVCALPLYHIfaltvcgllgmrtG 278
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  242 GIGML--HLRDVylgcqeinvsseTILMEPLKwldwidHYRASVTWAPNFAF-GLVT--DFaeeikdRKWDLSSMRYMLN 316
Cdd:PRK07059   279 GRNILipNPRDI------------PGFIKELK------KYQVHIFPAVNTLYnALLNnpDF------DKLDFSKLIVANG 334
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  317 GGEAMVAKVGRRILELLephGLPadaIRPAWGMSETSSGVIfsheftrAGTSDDDHFV-EIGSPIPGFSMRIVNDHNELV 395
Cdd:PRK07059   335 GGMAVQRPVAERWLEMT---GCP---ITEGYGLSETSPVAT-------CNPVDATEFSgTIGLPLPSTEVSIRDDDGNDL 401
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  396 EEGEIGRFQVSGLSVTSGYYQRPDLNESVFTEDGWFETGDLGFL-RNGRLTITGRTKDAIIINGINYYSHAIESAVEELS 474
Cdd:PRK07059   402 PLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMdERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHP 481
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  475 EI-EtsyTAACAVRlGQNSTDQLAIFFVTS-AKLNDEQmsqllrnIQSHV-SQVIGvtpeYLLPVQKE---EIPKTAIGK 548
Cdd:PRK07059   482 GVlE---VAAVGVP-DEHSGEAVKLFVVKKdPALTEED-------VKAFCkERLTN----YKRPKFVEfrtELPKTNVGK 546

                   ....*..
gi 1776025254  549 IQRTQLK 555
Cdd:PRK07059   547 ILRRELR 553
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
2843-3078 4.45e-22

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 98.79  E-value: 4.45e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2843 MPWRDeGVYLITGGAGSLGLLFAKEIANRtGRsTIVLTGRSvlsEDKENEL-EALRSIGAEVVYREADVSDQHAVHHLFE 2921
Cdd:COG0300      1 MSLTG-KTVLITGASSGIGRALARALAAR-GA-RVVLVARD---AERLEALaAELRAAGARVEVVALDVTDPDAVAALAE 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2922 EIKERYGTLNGIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSGLLHvdeCSKDF-PL------DFFIFFSSVSGCLGNAGQ 2994
Cdd:COG0300     75 AVLARFGPIDVLVNNAGVGGGGPFEELDLEDLRRVFEVNVFGPVR---LTRALlPLmrargrGRIVNVSSVAGLRGLPGM 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2995 ADYAAANSFMDAFAEyrrSLAASKKRFG---STISFNW---PLWEEGGMQVGAEdekrmlkttgmvPMPTDSGLKAFYQG 3068
Cdd:COG0300    152 AAYAASKAALEGFSE---SLRAELAPTGvrvTAVCPGPvdtPFTARAGAPAGRP------------LLSPEEVARAILRA 216
                          250
                   ....*....|
gi 1776025254 3069 IASDKPQVFV 3078
Cdd:COG0300    217 LERGRAEVYV 226
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
4174-4373 5.64e-22

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 98.40  E-value: 5.64e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4174 LITGGTRGIGLLCARHFAECyGVKkLVLTGREqlppreewarfktsntslAEKIQAVR-ELEAKGVQVEMLSLTLSDDAQ 4252
Cdd:COG0300      9 LITGASSGIGRALARALAAR-GAR-VVLVARD------------------AERLEALAaELRAAGARVEVVALDVTDPDA 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4253 VEQTLQHIKRTLGPIGGVIHCAGLtdMDTLAFIRKTSDDIQRVMEPKVSGLTTLYRHVcnepLQFF--------VLFSSV 4324
Cdd:COG0300     69 VAALAEAVLARFGPIDVLVNNAGV--GGGGPFEELDLEDLRRVFEVNVFGPVRLTRAL----LPLMrargrgriVNVSSV 142
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1776025254 4325 SAIIPelSAGQADYAMANSYMDYFAEA-----HQKHVPIISVQwPNWKETGMGE 4373
Cdd:COG0300    143 AGLRG--LPGMAAYAASKAALEGFSESlraelAPTGVRVTAVC-PGPVDTPFTA 193
PRK05952 PRK05952
beta-ketoacyl-ACP synthase;
3509-3776 6.65e-22

beta-ketoacyl-ACP synthase;


Pssm-ID: 235653 [Multi-domain]  Cd Length: 381  Bit Score: 101.28  E-value: 6.65e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3509 ACSSSLVAIHRAVTAMQNGDCEMAIAGGVNTILTEEAHISYSKAGMLSKDGrCKTFSADANGYVRGEGVGMVMLKKLEDA 3588
Cdd:PRK05952   145 ACATGLWAIAQGVELIQTGQCQRVIAGAVEAPITPLTLAGFQQMGALAKTG-AYPFDRQREGLVLGEGGAILVLESAELA 223
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3589 ERDGNHIYGVIRG---TAENHGGRAntlTSPNPKAQADLLVRAYRQAGIDPSTVTYIEAHGTGTELGDPIEINGLKAAFK 3665
Cdd:PRK05952   224 QKRGAKIYGQILGfglTCDAYHMSA---PEPDGKSAIAAIQQCLARSGLTPEDIDYIHAHGTATRLNDQREANLIQALFP 300
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3666 elsnmrgesqpdvpdHRCGIGSVKSNIGHLELAAGISGLIKVLLQMKHKTLVKSLHCETlnPYLQLTdspfyIVQEkqew 3745
Cdd:PRK05952   301 ---------------HRVAVSSTKGATGHTLGASGALGVAFSLLALRHQQLPPCVGLQE--PEFDLN-----FVRQ---- 354
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1776025254 3746 ksvtdcdgnelPRRAGIS-----SFGIGGVNAHIVI 3776
Cdd:PRK05952   355 -----------AQQSPLQnvlclSFGFGGQNAAIAL 379
PLN02787 PLN02787
3-oxoacyl-[acyl-carrier-protein] synthase II
3322-3779 8.33e-22

3-oxoacyl-[acyl-carrier-protein] synthase II


Pssm-ID: 215421 [Multi-domain]  Cd Length: 540  Bit Score: 103.52  E-value: 8.33e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3322 QPIiAKAERNKKQAADFEPVAIVGISGRFPGAMDIDEFWKNLEEGKDSITEVpkDRWDWREHYGNPDTDVNK--TDiKWg 3399
Cdd:PLN02787   113 QPE-KEVETKKKPLTKQRRVVVTGMGVVSPLGHDPDVFYNNLLEGVSGISEI--ERFDCSQFPTRIAGEIKSfsTD-GW- 187
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3400 gfidgvaefdplffgISPREADYVDPQQRLLMTYVWKALEDAGCPPQ---SLSGTGTGIFIGTGNTGYKdLFHRA--NLP 3474
Cdd:PLN02787   188 ---------------VAPKLSKRMDKFMLYLLTAGKKALADGGITEDvmkELDKTKCGVLIGSAMGGMK-VFNDAieALR 251
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3475 IEGHAATGHMIPSVGPNRMSYFLNIH----GPSEPVETACSSSLVAIHRAVTAMQNGDCEMAIAGGvntilTEEAHISYS 3550
Cdd:PLN02787   252 ISYRKMNPFCVPFATTNMGSAMLAMDlgwmGPNYSISTACATSNFCILNAANHIIRGEADVMLCGG-----SDAAIIPIG 326
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3551 KAGMLSkdgrCKTFS--------------ADANGYVRGEGVGMVMLKKLEDAERDGNHIYgvirgtAENHGGR----ANT 3612
Cdd:PLN02787   327 LGGFVA----CRALSqrnddptkasrpwdMNRDGFVMGEGAGVLLLEELEHAKKRGANIY------AEFLGGSftcdAYH 396
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3613 LTSPNPKAQADLLV--RAYRQAGIDPSTVTYIEAHGTGTELGDPIEINGLKAAFKELSNMRgesqpdvpdhrcgIGSVKS 3690
Cdd:PLN02787   397 MTEPHPEGAGVILCieKALAQSGVSKEDVNYINAHATSTKAGDLKEYQALMRCFGQNPELR-------------VNSTKS 463
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3691 NIGHLELAAGISGLIKVLLQMKHKTLVKSLHCEtlNPYlQLTDSPFYIVQEKQewksvtdcdgnELPRRAGIS-SFGIGG 3769
Cdd:PLN02787   464 MIGHLLGAAGAVEAIATVQAIRTGWVHPNINLE--NPE-SGVDTKVLVGPKKE-----------RLDIKVALSnSFGFGG 529
                          490
                   ....*....|
gi 1776025254 3770 VNAHIVIEEY 3779
Cdd:PLN02787   530 HNSSILFAPY 539
PRK07824 PRK07824
o-succinylbenzoate--CoA ligase;
187-558 9.26e-22

o-succinylbenzoate--CoA ligase;


Pssm-ID: 236108 [Multi-domain]  Cd Length: 358  Bit Score: 100.50  E-value: 9.26e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  187 EDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTReditfNW---MPFDHVGGIGMLhLRDVYLGCQ--EINVS 261
Cdd:PRK07824    35 DDVALVVATSGTTGTPKGAMLTAAALTASADATHDRLGGPG-----QWllaLPAHHIAGLQVL-VRSVIAGSEpvELDVS 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  262 SEtilMEPLKWLDWIDHYRASVTWApnfafGLV-TDFAEEIKDRKW--DLSSMRYMLNGGEAMVAKVGRRILELlephGL 338
Cdd:PRK07824   109 AG---FDPTALPRAVAELGGGRRYT-----SLVpMQLAKALDDPAAtaALAELDAVLVGGGPAPAPVLDAAAAA----GI 176
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  339 PadaIRPAWGMSETSSGVIFSheftragtsdddhfveiGSPIPGFSMRIVNdhnelveegeiGRFQVSGLSVTSGYYQRP 418
Cdd:PRK07824   177 N---VVRTYGMSETSGGCVYD-----------------GVPLDGVRVRVED-----------GRIALGGPTLAKGYRNPV 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  419 DlnESVFTEDGWFETGDLGFLRNGRLTITGRTKDAIIINGINYYSHAIESAVEELSEIetsytAACAV------RLGQNs 492
Cdd:PRK07824   226 D--PDPFAEPGWFRTDDLGALDDGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAV-----ADCAVfglpddRLGQR- 297
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1776025254  493 tdqlaiffVTSAKLNDEQMSQLLRNIQSHVSQVIGVT--PEYLLPVqkEEIPKTAIGKIQRTQLKTSF 558
Cdd:PRK07824   298 --------VVAAVVGDGGPAPTLEALRAHVARTLDRTaaPRELHVV--DELPRRGIGKVDRRALVRRF 355
PRK12316 PRK12316
peptide synthase; Provisional
173-676 9.49e-22

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 105.42  E-value: 9.49e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  173 LSAEADTDWHQSS---------PEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDHVG-G 242
Cdd:PRK12316  4671 LALDRDEDWEGFPahdpavrlhPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGsH 4750
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  243 IGMLHLrdvyLGCQEINVSSETILMEPLKWLDWIDHYRASVTWAPNFAFGLVTDFAEeikdRKWDLSSMRYMLNGGEAMV 322
Cdd:PRK12316  4751 EGLYHP----LINGASVVIRDDSLWDPERLYAEIHEHRVTVLVFPPVYLQQLAEHAE----RDGEPPSLRVYCFGGEAVA 4822
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  323 AKVGRRILELLEPhglpaDAIRPAWGMSETSsgVIFSHEFTRAGTSDDDHFVEIGSPIPGFSMRIVNDHNELVEEGEIGR 402
Cdd:PRK12316  4823 QASYDLAWRALKP-----VYLFNGYGPTETT--VTVLLWKARDGDACGAAYMPIGTPLGNRSGYVLDGQLNPLPVGVAGE 4895
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  403 FQVSGLSVTSGYYQRPDLNESVFTEDGW-------FETGDLGFLR-NGRLTITGRTKDAIIINGINYyshaiesaveELS 474
Cdd:PRK12316  4896 LYLGGEGVARGYLERPALTAERFVPDPFgapggrlYRTGDLARYRaDGVIDYLGRVDHQVKIRGFRI----------ELG 4965
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  475 EIETSYTAACAVR----LGQNST--DQLAIFFV--TSAKLNDEQMSQLLRN-IQSHVSQVIgvtPEYLLPVQ---KEEIP 542
Cdd:PRK12316  4966 EIEARLREHPAVReavvIAQEGAvgKQLVGYVVpqDPALADADEAQAELRDeLKAALRERL---PEYMVPAHlvfLARMP 5042
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  543 KTAIGKIQRTQLKtsfengefdhllhKPnrmnDAVQdeeMQQADHVKrvREEIQEHLLTCLTEELHVSRdwVEPNANIQS 622
Cdd:PRK12316  5043 LTPNGKLDRKALP-------------QP----DASL---LQQAYVAP--RSELEQQVAAIWAEVLQLER--VGLDDNFFE 5098
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1776025254  623 LGVNSIKMMKLIRSIEKNYHIKLTAREIHQYPTierLASYLSEHEDLSSSSADK 676
Cdd:PRK12316  5099 LGGHSLLAIQVTSRIQLELGLELPLRELFQTPT---LAAFVELAAAAGSGDDEK 5149
MACS_like cd05972
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ...
61-555 1.03e-21

Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.


Pssm-ID: 341276 [Multi-domain]  Cd Length: 428  Bit Score: 101.64  E-value: 1.03e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254   61 SYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNSQLLPAFWGCVLTGVVPAPLAvpptyaesssgtqklkdawTLLdKP 140
Cdd:cd05972      2 SFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLT-------------------TLL-GP 61
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  141 AVITDRGMHQemldwakeqgleGFRAIIVEDllsaeadtdwhqsspEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGII 220
Cdd:cd05972     62 KDIEYRLEAA------------GAKAIVTDA---------------EDPALIYFTSGTTGLPKGVLHTHSYPLGHIPTAA 114
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  221 QMQGFTREDITFN-----WMPFDHVGGIGMLhlrdvYLGCQeiNVSSETILMEPLKWLDWIDHYRASVTWAPNFAFGLVT 295
Cdd:cd05972    115 YWLGLRPDDIHWNiadpgWAKGAWSSFFGPW-----LLGAT--VFVYEGPRFDAERILELLERYGVTSFCGPPTAYRMLI 187
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  296 dfAEEIKDRkwDLSSMRYMLNGGEAM---VAKVGRRILellephGLPadaIRPAWGMSETSSgVIFSHEFT--RAGTsdd 370
Cdd:cd05972    188 --KQDLSSY--KFSHLRLVVSAGEPLnpeVIEWWRAAT------GLP---IRDGYGQTETGL-TVGNFPDMpvKPGS--- 250
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  371 dhfveIGSPIPGFSMRIVNDHNELVEEGEIGRFQV--SGLSVTSGYYQRPDLNESVFTEDgWFETGDLG-FLRNGRLTIT 447
Cdd:cd05972    251 -----MGRPTPGYDVAIIDDDGRELPPGEEGDIAIklPPPGLFLGYVGDPEKTEASIRGD-YYLTGDRAyRDEDGYFWFV 324
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  448 GRTKDAIIINGINYYSHAIESAVeelseIETSYTAACAVrlgQNSTD----QLAIFFVTSAKlnDEQMS-QLLRNIQSHV 522
Cdd:cd05972    325 GRADDIIKSSGYRIGPFEVESAL-----LEHPAVAEAAV---VGSPDpvrgEVVKAFVVLTS--GYEPSeELAEELQGHV 394
                          490       500       510
                   ....*....|....*....|....*....|....*.
gi 1776025254  523 SQVIGvtpEYLLPVQKE---EIPKTAIGKIQRTQLK 555
Cdd:cd05972    395 KKVLA---PYKYPREIEfveELPKTISGKIRRVELR 427
ABCL cd05958
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ...
184-555 1.04e-21

2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.


Pssm-ID: 341268 [Multi-domain]  Cd Length: 439  Bit Score: 101.79  E-value: 1.04e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  184 SSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGI-IQMQGFTREDITFNWMPFDHVGGIGMLHLRDVYLGcqeinvsS 262
Cdd:cd05958     94 TASDDICILAFTSGTTGAPKATMHFHRDPLASADRYaVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVG-------A 166
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  263 ETILME---PLKWLDWIDHYRASVTW-APNFAFGLVT--DFAEEikdrkwDLSSMRYMLNGGEAMVAKVGRRILELLeph 336
Cdd:cd05958    167 SGVLLEeatPDLLLSAIARYKPTVLFtAPTAYRAMLAhpDAAGP------DLSSLRKCVSAGEALPAALHRAWKEAT--- 237
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  337 GLP-ADAIrpawGMSETssgvifSHEFTRAgTSDDDHFVEIGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGlsvTSGYY 415
Cdd:cd05958    238 GIPiIDGI----GSTEM------FHIFISA-RPGDARPGATGKPVPGYEAKVVDDEGNPVPDGTIGRLAVRG---PTGCR 303
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  416 QRPDLNESVFTEDGWFETGDLgFLR--NGRLTITGRTKDAIIINGINYYSHAIESAVeelseIETSYTAACAVrLGQNST 493
Cdd:cd05958    304 YLADKRQRTYVQGGWNITGDT-YSRdpDGYFRHQGRSDDMIVSGGYNIAPPEVEDVL-----LQHPAVAECAV-VGHPDE 376
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1776025254  494 DQLAI---FFVTSAKLNDEQmsQLLRNIQSHVSQVIGvtpEYLLPVQKE---EIPKTAIGKIQRTQLK 555
Cdd:cd05958    377 SRGVVvkaFVVLRPGVIPGP--VLARELQDHAKAHIA---PYKYPRAIEfvtELPRTATGKLQRFALR 439
PRK06188 PRK06188
acyl-CoA synthetase; Validated
173-561 1.22e-21

acyl-CoA synthetase; Validated


Pssm-ID: 235731 [Multi-domain]  Cd Length: 524  Bit Score: 102.76  E-value: 1.22e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  173 LSAEADTDWHQ-----SSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVkgIIQMQGFT-REDITF-NWMPFDHVGGI-- 243
Cdd:PRK06188   149 LLAAAAKFGPAplvaaALPPDIAGLAYTGGTTGKPKGVMGTHRSIATMA--QIQLAEWEwPADPRFlMCTPLSHAGGAff 226
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  244 -------GMLHLRDVYlgcqeinvssetilmEPLKWLDWIDHYRASVTW-APNFAFGLVtdfaEEIKDRKWDLSSMRYML 315
Cdd:PRK06188   227 lptllrgGTVIVLAKF---------------DPAEVLRAIEEQRITATFlVPTMIYALL----DHPDLRTRDLSSLETVY 287
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  316 NGGEAMVAKvgrRILELLEPHGlPADAirPAWGMSETSSGVIF----SHEftragTSDDDHFVEIGSPIPGFSMRIVNDH 391
Cdd:PRK06188   288 YGASPMSPV---RLAEAIERFG-PIFA--QYYGQTEAPMVITYlrkrDHD-----PDDPKRLTSCGRPTPGLRVALLDED 356
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  392 NELVEEGEIGRFQVSGLSVTSGYYQRPDLNESVFtEDGWFETGDL------GFlrngrLTITGRTKDAIIINGINYYSHA 465
Cdd:PRK06188   357 GREVAQGEVGEICVRGPLVMDGYWNRPEETAEAF-RDGWLHTGDVarededGF-----YYIVDRKKDMIVTGGFNVFPRE 430
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  466 IESAVEELSEIetsytAACAV------RLGQNSTdqlAIFFVTSAKLNDEQmsqllrNIQSHVSQVIGV--TPEYLLPVq 537
Cdd:PRK06188   431 VEDVLAEHPAV-----AQVAVigvpdeKWGEAVT---AVVVLRPGAAVDAA------ELQAHVKERKGSvhAPKQVDFV- 495
                          410       420
                   ....*....|....*....|....
gi 1776025254  538 kEEIPKTAIGKIQRTQLKTSFENG 561
Cdd:PRK06188   496 -DSLPLTALGKPDKKALRARYWEG 518
ACS cd05966
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ...
1160-1648 1.41e-21

Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.


Pssm-ID: 341270 [Multi-domain]  Cd Length: 608  Bit Score: 103.02  E-value: 1.41e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1160 EQQAKKTPDRAAVSYEG------QTLTYRELDERSTQLAIYLQAHGVGP-DRLAgIYVDRSLDMLVGLLAILKAGGAYVP 1232
Cdd:cd05966     60 DRHLKERGDKVAIIWEGdepdqsRTITYRELLREVCRFANVLKSLGVKKgDRVA-IYMPMIPELVIAMLACARIGAVHSV 138
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1233 LDPSYPAERLEYMLEDSEVFITLTTSElvntlSWNG---------VTTAL------------------------LDQDWD 1279
Cdd:cd05966    139 VFAGFSAESLADRINDAQCKLVITADG-----GYRGgkviplkeiVDEALekcpsvekvlvvkrtggevpmtegRDLWWH 213
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1280 EIAQTASDRkVLTRTVTPENLAYVIYTSGSTGKPKGVMipHKaltnflvsmgeTPGLtaedkML--AVTT-YCFDIAALE 1356
Cdd:cd05966    214 DLMAKQSPE-CEPEWMDSEDPLFILYTSGSTGKPKGVV--HT-----------TGGY-----LLyaATTFkYVFDYHPDD 274
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1357 LFL-----------------PLIKGAHCYIcqTEHTKD----------VEKLKRDIRTIKPTVMQATpatwkMLFYSGWE 1409
Cdd:cd05966    275 IYWctadigwitghsyivygPLANGATTVM--FEGTPTypdpgrywdiVEKHKVTIFYTAPTAIRAL-----MKFGDEWV 347
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1410 NE---ENVKILcG--GEAL-PETLKRYF----------LDTgseaWNMfgpTET-----TIWSAVQRINDecsrATIGRP 1468
Cdd:cd05966    348 KKhdlSSLRVL-GsvGEPInPEAWMWYYevigkercpiVDT----WWQ---TETggimiTPLPGATPLKP----GSATRP 415
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1469 IANTQIYITDSQLAPVPAGVPGELCIAGD--GVAKGYYKKEEltdsRFIDNPFEPGSKLYRTGDMARWLPGGRIEYIGRI 1546
Cdd:cd05966    416 FFGIEPAILDEEGNEVEGEVEGYLVIKRPwpGMARTIYGDHE----RYEDTYFSKFPGYYFTGDGARRDEDGYYWITGRV 491
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1547 DNQVKIRGFRIELGDIESRLSEHPGILECVVVADMDNL-----AAYYTAK--HANASLTARELRHFVKNALPAYMVPSYF 1619
Cdd:cd05966    492 DDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIkgeaiYAFVTLKdgEEPSDELRKELRKHVRKEIGPIATPDKI 571
                          570       580
                   ....*....|....*....|....*....
gi 1776025254 1620 IQLDHMPLTPNGKIDRNSLKNIDLSGEQL 1648
Cdd:cd05966    572 QFVPGLPKTRSGKIMRRILRKIAAGEEEL 600
PRK06018 PRK06018
putative acyl-CoA synthetase; Provisional
1153-1649 1.66e-21

putative acyl-CoA synthetase; Provisional


Pssm-ID: 235673 [Multi-domain]  Cd Length: 542  Bit Score: 102.52  E-value: 1.66e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1153 ITFHELFEQQAKKTPDRAAV--SYEGQTL--TYRELDERSTQLAIYLQAHGVGP-DRLAGIY--VDRSLDMLVGLLAIlk 1225
Cdd:PRK06018    10 LLCHRIIDHAARIHGNREVVtrSVEGPIVrtTYAQIHDRALKVSQALDRDGIKLgDRVATIAwnTWRHLEAWYGIMGI-- 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1226 aGGAYVPLDPSYPAERLEYML---EDSEVFITLTTSELVNTLS--WNGVTTALLDQDWDEIAQT-------------ASD 1287
Cdd:PRK06018    88 -GAICHTVNPRLFPEQIAWIInhaEDRVVITDLTFVPILEKIAdkLPSVERYVVLTDAAHMPQTtlknavayeewiaEAD 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1288 RKVLTRTVTPENLAYVIYTSGSTGKPKGVMIPHKA--LTNFLVSMGETPGLTAEDKMLAV----------TTYCFDIAAL 1355
Cdd:PRK06018   167 GDFAWKTFDENTAAGMCYTSGTTGDPKGVLYSHRSnvLHALMANNGDALGTSAADTMLPVvplfhanswgIAFSAPSMGT 246
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1356 ELFLPLIK--GAHCYicqteHTKDVEKLkrdirtikpTVMQATPATWKMLFYSGWENEENV----KILCGGEALPETLKR 1429
Cdd:PRK06018   247 KLVMPGAKldGASVY-----ELLDTEKV---------TFTAGVPTVWLMLLQYMEKEGLKLphlkMVVCGGSAMPRSMIK 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1430 YFLDTGSEAWNMFGPTETTIWSAVQRINDECS----------RATIGRPIANTQIYITDSQLAPVP--AGVPGELCIAGD 1497
Cdd:PRK06018   313 AFEDMGVEVRHAWGMTEMSPLGTLAALKPPFSklpgdarldvLQKQGYPPFGVEMKITDDAGKELPwdGKTFGRLKVRGP 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1498 GVAKGYYK--KEELTDSRFIDnpfepgsklyrTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILEC 1575
Cdd:PRK06018   393 AVAAAYYRvdGEILDDDGFFD-----------TGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEA 461
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1776025254 1576 VVVA----DMDNLAAYYTAKHANASLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLKnidlsgEQLK 1649
Cdd:PRK06018   462 AVIGvyhpKWDERPLLIVQLKPGETATREEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALR------EQFK 533
MACS_euk cd05928
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ...
1180-1640 1.67e-21

Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.


Pssm-ID: 341251 [Multi-domain]  Cd Length: 530  Bit Score: 102.16  E-value: 1.67e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1180 TYRELDERSTQLA-IYLQAHGVGP-DRLAGIyVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLEDSEVFITLTT 1257
Cdd:cd05928     43 SFRELGSLSRKAAnVLSGACGLQRgDRVAVI-LPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTS 121
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1258 SEL---VNTLSWN--GVTTALL--DQDWD------EIAQTASDRKVLTRTVTPENLAyVIYTSGSTGKPKgvMIPHK--- 1321
Cdd:cd05928    122 DELapeVDSVASEcpSLKTKLLvsEKSRDgwlnfkELLNEASTEHHCVETGSQEPMA-IYFTSGTTGSPK--MAEHShss 198
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1322 ALTNFLVSMGETPGLTAEDKMLAVTTYCFDIAAL-ELFLPLIKGAhCYICQTEHTKDVEKLKRDIRTIKPTVMQATPATW 1400
Cdd:cd05928    199 LGLGLKVNGRYWLDLTASDIMWNTSDTGWIKSAWsSLFEPWIQGA-CVFVHHLPRFDPLVILKTLSSYPITTFCGAPTVY 277
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1401 KMLF---YSGWENEENVKILCGGEAL-PETLKRYFLDTGSEAWNMFGPTETTIWSAVQRiNDECSRATIGRPIANTQIYI 1476
Cdd:cd05928    278 RMLVqqdLSSYKFPSLQHCVTGGEPLnPEVLEKWKAQTGLDIYEGYGQTETGLICANFK-GMKIKPGSMGKASPPYDVQI 356
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1477 TDSQLAPVPAGVPGELCIAGDGVAKGYYKkeeltdSRFIDNPFEPGSKL----YRTGDMARWLPGGRIEYIGRIDNQVKI 1552
Cdd:cd05928    357 IDDNGNVLPPGTEGDIGIRVKPIRPFGLF------SGYVDNPEKTAATIrgdfYLTGDRGIMDEDGYFWFMGRADDVINS 430
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1553 RGFRIELGDIESRLSEHPGILECVVVADMDN-----------LAAYYTAkHANASLTaRELRHFVKNALPAYMVPSYFIQ 1621
Cdd:cd05928    431 SGYRIGPFEVESALIEHPAVVESAVVSSPDPirgevvkafvvLAPQFLS-HDPEQLT-KELQQHVKSVTAPYKYPRKVEF 508
                          490
                   ....*....|....*....
gi 1776025254 1622 LDHMPLTPNGKIDRNSLKN 1640
Cdd:cd05928    509 VQELPKTVTGKIQRNELRD 527
Firefly_Luc cd17642
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ...
1155-1641 1.82e-21

insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341297 [Multi-domain]  Cd Length: 532  Bit Score: 102.22  E-value: 1.82e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1155 FHELFEQQA-----------KKTPDRAAV--SYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLL 1221
Cdd:cd17642      8 FYPLEDGTAgeqlhkamkryASVPGTIAFtdAHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVI 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1222 AILKAGGAYVPLDPSYPAERLEYMLEDSE---VFIT-LTTSELVNTLSWNGV--TTALLDQDWDeIAQTASDRKVLTRTV 1295
Cdd:cd17642     88 AGLFIGVGVAPTNDIYNERELDHSLNISKptiVFCSkKGLQKVLNVQKKLKIikTIIILDSKED-YKGYQCLYTFITQNL 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1296 TP---------------ENLAYVIYTSGSTGKPKGVMIPHK-ALTNFLVSMGETPG--LTAEDKMLAVTTYCFDIAALEL 1357
Cdd:cd17642    167 PPgfneydfkppsfdrdEQVALIMNSSGSTGLPKGVQLTHKnIVARFSHARDPIFGnqIIPDTAILTVIPFHHGFGMFTT 246
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1358 FLPLIKGAHCYICQT--EHT--KDVEKLKRDIRTIKPTVMQATPatwKMLFYSGWENEENVKILCGG--------EALPE 1425
Cdd:cd17642    247 LGYLICGFRVVLMYKfeEELflRSLQDYKVQSALLVPTLFAFFA---KSTLVDKYDLSNLHEIASGGaplskevgEAVAK 323
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1426 TLKRYFLDTGseawnmFGPTETTiwSAVQRINDE-CSRATIGRPIANTQIYITDSQLAP-VPAGVPGELCIAGDGVAKGY 1503
Cdd:cd17642    324 RFKLPGIRQG------YGLTETT--SAILITPEGdDKPGAVGKVVPFFYAKVVDLDTGKtLGPNERGELCVKGPMIMKGY 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1504 YKKEELTDSRFIDNPFepgsklYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMD- 1582
Cdd:cd17642    396 VNNPEATKALIDKDGW------LHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDe 469
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1776025254 1583 ---NLAAYYTAKHANASLTARELRHFVK-NALPAYMVPSYFIQLDHMPLTPNGKIDRNSLKNI 1641
Cdd:cd17642    470 dagELPAAVVVLEAGKTMTEKEVMDYVAsQVSTAKRLRGGVKFVDEVPKGLTGKIDRRKIREI 532
PLN02860 PLN02860
o-succinylbenzoate-CoA ligase
60-555 2.22e-21

o-succinylbenzoate-CoA ligase


Pssm-ID: 215464 [Multi-domain]  Cd Length: 563  Bit Score: 102.18  E-value: 2.22e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254   60 QSYRRLWDDGLRIVKGLRQSGLKaKQSVILQLGDNSQL-LPAFWGCVLTGVVPAPLAVPPTYAESSSGTQKLKDAWTLLD 138
Cdd:PLN02860    33 RTGHEFVDGVLSLAAGLLRLGLR-NGDVVAIAALNSDLyLEWLLAVACAGGIVAPLNYRWSFEEAKSAMLLVRPVMLVTD 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  139 K------PAVITDR----GMHQEMLDWAKEQGLEGFRAIIVEDLL-----SAEADTDWhqsSPEDLALLLLTSGSTGTPK 203
Cdd:PLN02860   112 EtcsswyEELQNDRlpslMWQVFLESPSSSVFIFLNSFLTTEMLKqralgTTELDYAW---APDDAVLICFTSGTTGRPK 188
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  204 AVMLNHRN--IMSMVKgiIQMQGFTREDITFNWMPFDHVGGI----GML------------HLRDVYLGCQEINVSSETI 265
Cdd:PLN02860   189 GVTISHSAliVQSLAK--IAIVGYGEDDVYLHTAPLCHIGGLssalAMLmvgachvllpkfDAKAALQAIKQHNVTSMIT 266
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  266 LmePLKWLDWIDHYRASVTWAPNfafglvtdfaeeikdrkwdlSSMRYMLNGGEAMVAKVGRRILELLephglPADAIRP 345
Cdd:PLN02860   267 V--PAMMADLISLTRKSMTWKVF--------------------PSVRKILNGGGSLSSRLLPDAKKLF-----PNAKLFS 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  346 AWGMSETSSGVIFS--HEFTRA---------GTSDDDHF-----VEIGSPIPGFSMRIVNDhnelvEEGEIGRFQVSGLS 409
Cdd:PLN02860   320 AYGMTEACSSLTFMtlHDPTLEspkqtlqtvNQTKSSSVhqpqgVCVGKPAPHVELKIGLD-----ESSRVGRILTRGPH 394
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  410 VTSGYYQRPDLNESVFTEDGWFETGDLGFL-RNGRLTITGRTKDAIIINGINYYSHAIE----------SAV------EE 472
Cdd:PLN02860   395 VMLGYWGQNSETASVLSNDGWLDTGDIGWIdKAGNLWLIGRSNDRIKTGGENVYPEEVEavlsqhpgvaSVVvvgvpdSR 474
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  473 LSEIetsyTAACaVRLGQNSTdqlaifFVTSAKLNDEQMSQLLRNIQSHVSQVIGVTpEYLLP----VQKEEIPKTAIGK 548
Cdd:PLN02860   475 LTEM----VVAC-VRLRDGWI------WSDNEKENAKKNLTLSSETLRHHCREKNLS-RFKIPklfvQWRKPFPLTTTGK 542

                   ....*..
gi 1776025254  549 IQRTQLK 555
Cdd:PLN02860   543 IRRDEVR 549
LC_FACS_bac cd05932
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ...
1177-1578 2.68e-21

Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341255 [Multi-domain]  Cd Length: 508  Bit Score: 101.39  E-value: 2.68e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1177 QTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLEDSEVFITLT 1256
Cdd:cd05932      5 VEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFV 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1257 ------------TSELVNTLSWNGVTTALLDQDWDEI-AQTASDRKVLTRTvtPENLAYVIYTSGSTGKPKGVMIPHKAL 1323
Cdd:cd05932     85 gklddwkamapgVPEGLISISLPPPSAANCQYQWDDLiAQHPPLEERPTRF--PEQLATLIYTSGTTGQPKGVMLTFGSF 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1324 TNFLVSMGETPGLTAEDKMLAVTTYCFDIAALELFL-PLIKGAHCYICQTEHTKdVEKLKRDirtiKPTVMQATPATWkM 1402
Cdd:cd05932    163 AWAAQAGIEHIGTEENDRMLSYLPLAHVTERVFVEGgSLYGGVLVAFAESLDTF-VEDVQRA----RPTLFFSVPRLW-T 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1403 LFYSGWENE-----------------------------ENVKILCGGEA-LPETLKRYFLDTG---SEAWNMfgpTETTI 1449
Cdd:cd05932    237 KFQQGVQDKipqqklnlllkipvvnslvkrkvlkglglDQCRLAGCGSApVPPALLEWYRSLGlniLEAYGM---TENFA 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1450 WSAVQRINDEcSRATIGRPIANTQIYITDSqlapvpagvpGELCIAGDGVAKGYYKKEELTDSRFIDNPFepgsklYRTG 1529
Cdd:cd05932    314 YSHLNYPGRD-KIGTVGNAGPGVEVRISED----------GEILVRSPALMMGYYKDPEATAEAFTADGF------LRTG 376
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1530 DMARWLPGGRIEYIGRIDNQVKI-RGFRIELGDIESRLSEHPGILECVVV 1578
Cdd:cd05932    377 DKGELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKLAEHDRVEMVCVI 426
A_NRPS_ApnA-like cd17644
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ...
186-554 2.88e-21

similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341299 [Multi-domain]  Cd Length: 465  Bit Score: 100.97  E-value: 2.88e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  186 PEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTRED--ITFNWMPFDhvggigmlhlrdvylgcqeinVSSE 263
Cdd:cd17644    105 PENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGITSSDrvLQFASIAFD---------------------VAAE 163
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  264 TILMEPLKwldwidhyRASVTWAPNFAFGLVTDFAEEIKDRK---WDL--------------------SSMRYMLNGGEA 320
Cdd:cd17644    164 EIYVTLLS--------GATLVLRPEEMRSSLEDFVQYIQQWQltvLSLppaywhllvlelllstidlpSSLRLVIVGGEA 235
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  321 -------MVAKVGRRILELLEphglpadairpAWGMSETSSGVIFSHefTRAGTSDDDHFVEIGSPIPGFSMRIVNDHNE 393
Cdd:cd17644    236 vqpelvrQWQKNVGNFIQLIN-----------VYGPTEATIAATVCR--LTQLTERNITSVPIGRPIANTQVYILDENLQ 302
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  394 LVEEGEIGRFQVSGLSVTSGYYQRPDLNESVFTEDGW--------FETGDLG-FLRNGRLTITGRTKDAIIINGINYYSH 464
Cdd:cd17644    303 PVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFnsseserlYKTGDLArYLPDGNIEYLGRIDNQVKIRGFRIELG 382
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  465 AIESAVEELSEIEtsyTAACAVRLGQNSTDQLAIFFVtsAKLNDEQMSQLLRniqSHVSQVIgvtPEYLLP---VQKEEI 541
Cdd:cd17644    383 EIEAVLSQHNDVK---TAVVIVREDQPGNKRLVAYIV--PHYEESPSTVELR---QFLKAKL---PDYMIPsafVVLEEL 451
                          410
                   ....*....|...
gi 1776025254  542 PKTAIGKIQRTQL 554
Cdd:cd17644    452 PLTPNGKIDRRAL 464
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
2852-3016 3.16e-21

classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212491 [Multi-domain]  Cd Length: 234  Bit Score: 95.81  E-value: 3.16e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2852 LITGGAGSLGLLFAKEIANRtGrSTIVLTGRSvlsEDKENELEALRSIGAEVVYREADVSDQHAVHHLFEEIKERYGTLN 2931
Cdd:cd05233      2 LVTGASSGIGRAIARRLARE-G-AKVVLADRN---EEALAELAAIEALGGNAVAVQADVSDEEDVEALVEEALEEFGRLD 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2932 GIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSGLLHV-DECSKDFPLDFF---IFFSSVSGCLGNAGQADYAAANSFMDAF 3007
Cdd:cd05233     77 ILVNNAGIARPGPLEELTDEDWDRVLDVNLTGVFLLtRAALPHMKKQGGgriVNISSVAGLRPLPGQAAYAASKAALEGL 156

                   ....*....
gi 1776025254 3008 AeyrRSLAA 3016
Cdd:cd05233    157 T---RSLAL 162
PRK06710 PRK06710
long-chain-fatty-acid--CoA ligase; Validated
186-554 3.68e-21

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 180666 [Multi-domain]  Cd Length: 563  Bit Score: 101.65  E-value: 3.68e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  186 PE-DLALLLLTSGSTGTPKAVMLNHRNIMS-MVKGIIQMQGFTR-EDITFNWMPFDHVGGIGMLHLRDVYLGCQEINVSS 262
Cdd:PRK06710   204 PEnDLALLQYTGGTTGFPKGVMLTHKNLVSnTLMGVQWLYNCKEgEEVVLGVLPFFHVYGMTAVMNLSIMQGYKMVLIPK 283
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  263 ETILM--EPLKwldwiDHYRASVTWAPNFAFGLVTdfAEEIKDrkWDLSSMRYMLNGGEAMVAKVGRRIlellepHGLPA 340
Cdd:PRK06710   284 FDMKMvfEAIK-----KHKVTLFPGAPTIYIALLN--SPLLKE--YDISSIRACISGSAPLPVEVQEKF------ETVTG 348
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  341 DAIRPAWGMSETS--SGVIFSHEFTRAGTsdddhfveIGSPIPGFSMRIVN-DHNELVEEGEIGRFQVSGLSVTSGYYQR 417
Cdd:PRK06710   349 GKLVEGYGLTESSpvTHSNFLWEKRVPGS--------IGVPWPDTEAMIMSlETGEALPPGEIGEIVVKGPQIMKGYWNK 420
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  418 PDLNESVFtEDGWFETGDLGFL-RNGRLTITGRTKDAIIINGINYYSHAIESAVEELSEIETsytaacAVRLG-----QN 491
Cdd:PRK06710   421 PEETAAVL-QDGWLHTGDVGYMdEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQE------VVTIGvpdpyRG 493
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1776025254  492 STDQLAIFFVTSAKLNDEQMSQLLRNIQShvsqvigvtpEYLLPVQKE---EIPKTAIGKIQRTQL 554
Cdd:PRK06710   494 ETVKAFVVLKEGTECSEEELNQFARKYLA----------AYKVPKVYEfrdELPKTTVGKILRRVL 549
PRK09116 PRK09116
beta-ketoacyl-ACP synthase;
3436-3700 4.08e-21

beta-ketoacyl-ACP synthase;


Pssm-ID: 181657 [Multi-domain]  Cd Length: 405  Bit Score: 99.68  E-value: 4.08e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3436 KALEDAG-CPPQSLSGTGTGIFIG--TGNTGYKDLFhrANLPIEGHA----ATGH--MIPSVGPNRMSYFLNIHGPSEPV 3506
Cdd:PRK09116    83 LALEDAGlLGDPILTDGRMGIAYGssTGSTDPIGAF--GTMLLEGSMsgitATTYvrMMPHTTAVNVGLFFGLKGRVIPT 160
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3507 ETACSSSLVAIHRAVTAMQNGDCEMAIAGGVNTILTEEAHISYSKAGMLSKDGRCKT----FSADANGYVRGEGVGMVML 3582
Cdd:PRK09116   161 SSACTSGSQGIGYAYEAIKYGYQTVMLAGGAEELCPTEAAVFDTLFATSTRNDAPELtprpFDANRDGLVIGEGAGTLVL 240
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3583 KKLEDAERDGNHIYGVIRGTAENHGGRAntLTSPNPKAQADLLVRAYRQAGIDPSTVTYIEAHGTGTELGDPIEINGLKA 3662
Cdd:PRK09116   241 EELEHAKARGATIYAEIVGFGTNSDGAH--VTQPQAETMQIAMELALKDAGLAPEDIGYVNAHGTATDRGDIAESQATAA 318
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1776025254 3663 AFkelsnmrGESQPdvpdhrcgIGSVKSNIGHLELAAG 3700
Cdd:PRK09116   319 VF-------GARMP--------ISSLKSYFGHTLGACG 341
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
2850-3016 6.32e-21

NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and metabolism]; NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440651 [Multi-domain]  Cd Length: 249  Bit Score: 95.62  E-value: 6.32e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGLLFAKEIANRtGrSTIVLTGRSvlsEDKENEL-EALRSIGAEVVYREADVSDQHAVHHLFEEIKERYG 2928
Cdd:COG1028      8 VALVTGGSSGIGRAIARALAAE-G-ARVVITDRD---AEALEAAaAELRAAGGRALAVAADVTDEAAVEALVAAAVAAFG 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2929 TLNGIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSGLLHvdeCSKDFpLDFF--------IFFSSVSGCLGNAGQADYAAA 3000
Cdd:COG1028     83 RLDILVNNAGITPPGPLEELTEEDWDRVLDVNLKGPFL---LTRAA-LPHMrergggriVNISSIAGLRGSPGQAAYAAS 158
                          170
                   ....*....|....*.
gi 1776025254 3001 NSFMDAFAeyrRSLAA 3016
Cdd:COG1028    159 KAAVVGLT---RSLAL 171
PRK07967 PRK07967
beta-ketoacyl-ACP synthase I;
1776-2187 6.69e-21

beta-ketoacyl-ACP synthase I;


Pssm-ID: 181184 [Multi-domain]  Cd Length: 406  Bit Score: 98.97  E-value: 6.69e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1776 NHDEFWENLRDGKESIAFfnkeelqrfgiSKEIAENAdyvpAKASIEGKDRFDPsffqispkdAEFMDPQLRMLLTH--S 1853
Cdd:PRK07967    18 NQQEVLASLREGRSGITF-----------SPEFAEMG----MRSQVWGNVKLDP---------TGLIDRKVMRFMGDasA 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1854 W------KAIEDAGYAAGQI--PQTSVFMSASNNSYRALL-PSDTTESLETPDGYVSWVL--AQSGTIPTMISHKLGLRG 1922
Cdd:PRK07967    74 YaylameQAIADAGLSEEQVsnPRTGLIAGSGGGSTRNQVeAADAMRGPRGPKRVGPYAVtkAMASTVSACLATPFKIKG 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1923 PSYFVHANCSSSLIGLHSAYKSLLSAESDYALVGGA-----TLHTESNIGYVHQPGLNFSSDGHIKAFDASADGMIGGEG 1997
Cdd:PRK07967   154 VNYSISSACATSAHCIGNAVEQIQLGKQDIVFAGGGeeldwEMSCLFDAMGALSTKYNDTPEKASRAYDANRDGFVIAGG 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1998 VAVVLLKKAADAVKDGDHIYALLRGIGVNNDGADKVgfyAPSVKGQADVVQQVMNQTKihpESICYVEAHGTGTKLGDPI 2077
Cdd:PRK07967   234 GGVVVVEELEHALARGAKIYAEIVGYGATSDGYDMV---APSGEGAVRCMQMALATVD---TPIDYINTHGTSTPVGDVK 307
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2078 ELAALTNVyrqYTNKTQFcgIGSVKTNIGHLDTAAGLAGCIKVVMSLYHQELAPSINYKEPNPntDLASSPfyvVDQKKT 2157
Cdd:PRK07967   308 ELGAIREV---FGDKSPA--ISATKSLTGHSLGAAGVQEAIYSLLMMEHGFIAPSANIEELDP--QAAGMP---IVTETT 377
                          410       420       430
                   ....*....|....*....|....*....|.
gi 1776025254 2158 LSREIQThraALS-SFGLGGTNTHAIFEQFK 2187
Cdd:PRK07967   378 DNAELTT---VMSnSFGFGGTNATLVFRRYK 405
PRK12492 PRK12492
long-chain-fatty-acid--CoA ligase; Provisional
182-555 7.44e-21

long-chain-fatty-acid--CoA ligase; Provisional


Pssm-ID: 171539 [Multi-domain]  Cd Length: 562  Bit Score: 100.67  E-value: 7.44e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  182 HQSSPEDLALLLLTSGSTGTPKAVMLNHRNI---MSMVKGIIQMQG-----FTRE--DITFNWMPFDHVggigmlHLRDV 251
Cdd:PRK12492   202 VPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLvanMLQVRACLSQLGpdgqpLMKEgqEVMIAPLPLYHI------YAFTA 275
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  252 YLGCQEINVSSETILMEPLKWLDWIDHYRasvTWAPNFAFGLVTDFAEEIKD---RKWDLSSMRYMLNGGEAMVAKVGRR 328
Cdd:PRK12492   276 NCMCMMVSGNHNVLITNPRDIPGFIKELG---KWRFSALLGLNTLFVALMDHpgfKDLDFSALKLTNSGGTALVKATAER 352
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  329 IlellepHGLPADAIRPAWGMSETSSgVIFSH---EFTRAGTsdddhfveIGSPIPGFSMRIVNDHNELVEEGEIGRFQV 405
Cdd:PRK12492   353 W------EQLTGCTIVEGYGLTETSP-VASTNpygELARLGT--------VGIPVPGTALKVIDDDGNELPLGERGELCI 417
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  406 SGLSVTSGYYQRPDLNESVFTEDGWFETGDLGFL-RNGRLTITGRTKDAIIINGINYYSHAIESAVEELSEIetsytAAC 484
Cdd:PRK12492   418 KGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIdPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKV-----ANC 492
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1776025254  485 AVrLG---QNSTDQLAIFFVTS-AKLNDEQMSQLLR-NIQShvsqvigvtpeYLLP---VQKEEIPKTAIGKIQRTQLK 555
Cdd:PRK12492   493 AA-IGvpdERSGEAVKLFVVARdPGLSVEELKAYCKeNFTG-----------YKVPkhiVLRDSLPMTPVGKILRRELR 559
LC_FACS_bac1 cd17641
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ...
185-452 1.08e-20

bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341296 [Multi-domain]  Cd Length: 569  Bit Score: 100.19  E-value: 1.08e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  185 SPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDHVGGiGMLHLRDVYLGCQEIN-VSSE 263
Cdd:cd17641    156 KGEDVAVLCTTSGTTGKPKLAMLSHGNFLGHCAAYLAADPLGPGDEYVSVLPLPWIGE-QMYSVGQALVCGFIVNfPEEP 234
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  264 TILMEPLK-------------WLDWIDHYRASVTWAPNF---------------------------AFGLVTDFAEEI-- 301
Cdd:cd17641    235 ETMMEDLReigptfvllpprvWEGIAADVRARMMDATPFkrfmfelgmklglraldrgkrgrpvslWLRLASWLADALlf 314
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  302 ---KDRkWDLSSMRYMLNGGEAMvakvGRRILELLEPHGLPadaIRPAWGMSETSsGVIFSHeftRAGTSDDDhfvEIGS 378
Cdd:cd17641    315 rplRDR-LGFSRLRSAATGGAAL----GPDTFRFFHAIGVP---LKQLYGQTELA-GAYTVH---RDGDVDPD---TVGV 379
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1776025254  379 PIPGFSMRIVNdhnelveEGEIgrfQVSGLSVTSGYYQRPDLNESVFTEDGWFETGDLGFLR-NGRLTITGRTKD 452
Cdd:cd17641    380 PFPGTEVRIDE-------VGEI---LVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKeNGHLVVIDRAKD 444
PRK09116 PRK09116
beta-ketoacyl-ACP synthase;
4722-4988 1.93e-20

beta-ketoacyl-ACP synthase;


Pssm-ID: 181657 [Multi-domain]  Cd Length: 405  Bit Score: 97.37  E-value: 1.93e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4722 AANLSQFFDVRGPSVVVDTACSSALVGMNMAIQALRGGDIQSAIVGGVSLLSSDASHrLFDRRGILSK-----HSSFHVF 4796
Cdd:PRK09116   144 AVNVGLFFGLKGRVIPTSSACTSGSQGIGYAYEAIKYGYQTVMLAGGAEELCPTEAA-VFDTLFATSTrndapELTPRPF 222
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4797 DERADGVVLGEGVGMVMLKTVKQALEDGDTIYAVVKAASVNNDGrtAGPATPNLEAQKEVMKDALFKSGKKPEDISYLEA 4876
Cdd:PRK09116   223 DANRDGLVIGEGAGTLVLEELEHAKARGATIYAEIVGFGTNSDG--AHVTQPQAETMQIAMELALKDAGLAPEDIGYVNA 300
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4877 NGSGSIVTDLLELKAIQSVYrsGHSSPLSlgSIKPNIGHPLCAEGIASFIKVVLMLKERRFVPFLSgekeMAHFDQQKAN 4956
Cdd:PRK09116   301 HGTATDRGDIAESQATAAVF--GARMPIS--SLKSYFGHTLGACGALEAWMSIEMMNEGWFAPTLN----LTQVDPACGA 372
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1776025254 4957 ITFSRALEKWTDSQPTAAiNCFADGGTNVHVI 4988
Cdd:PRK09116   373 LDYIMGEAREIDTEYVMS-NNFAFGGINTSLI 403
entE PRK10946
(2,3-dihydroxybenzoyl)adenylate synthase;
1167-1639 2.48e-20

(2,3-dihydroxybenzoyl)adenylate synthase;


Pssm-ID: 236803 [Multi-domain]  Cd Length: 536  Bit Score: 98.52  E-value: 2.48e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1167 PDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGgaYVPLDPSYPAERLE--- 1243
Cdd:PRK10946    37 SDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLG--VAPVNALFSHQRSElna 114
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1244 YMLE----------DSEVFitlTTSELVNTL--SWNGVTTALLDQDWDE------IAQTASDrkvLTRTVTP-ENLAYVI 1304
Cdd:PRK10946   115 YASQiepalliadrQHALF---SDDDFLNTLvaEHSSLRVVLLLNDDGEhslddaINHPAED---FTATPSPaDEVAFFQ 188
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1305 YTSGSTGKPKgvMIP--HK----------------ALTNFLVS-------MGETPG----LTAEDKMLAVT----TYCFd 1351
Cdd:PRK10946   189 LSGGSTGTPK--LIPrtHNdyyysvrrsveicgftPQTRYLCAlpaahnyPMSSPGalgvFLAGGTVVLAPdpsaTLCF- 265
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1352 iaalelflPLIKgahcyicqtEHTKDVEKLkrdirtIKPTV---MQATPAtwkmlfySGWENE-ENVKIL-CGGEALPET 1426
Cdd:PRK10946   266 --------PLIE---------KHQVNVTAL------VPPAVslwLQAIAE-------GGSRAQlASLKLLqVGGARLSET 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1427 LKRYFLDT-GSEAWNMFGPTETTIwsAVQRINDECSR--ATIGRPIA-NTQIYITDSQLAPVPAGVPGELCIAGDGVAKG 1502
Cdd:PRK10946   316 LARRIPAElGCQLQQVFGMAEGLV--NYTRLDDSDERifTTQGRPMSpDDEVWVADADGNPLPQGEVGRLMTRGPYTFRG 393
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1503 YYKKEELTDSRFIDNPFepgsklYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMD 1582
Cdd:PRK10946   394 YYKSPQHNASAFDANGF------YCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMED 467
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1776025254 1583 NL-----AAYYTAKHAnasLTARELRHFVKNALPA-YMVPSYFIQLDHMPLTPNGKIDRNSLK 1639
Cdd:PRK10946   468 ELmgeksCAFLVVKEP---LKAVQLRRFLREQGIAeFKLPDRVECVDSLPLTAVGKVDKKQLR 527
A_NRPS_CmdD_like cd17652
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ...
184-554 2.82e-20

similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).


Pssm-ID: 341307 [Multi-domain]  Cd Length: 436  Bit Score: 97.32  E-value: 2.82e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  184 SSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTRED--ITFNWMPFDhvGGI----------GMLHLRDv 251
Cdd:cd17652     90 TTPDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAAFDVGPGSrvLQFASPSFD--ASVwellmallagATLVLAP- 166
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  252 ylgcqeinvSSETILMEPLkwLDWIDHYRASVTWAPNFAFGLVTDFaeeikdrkwDLSSMRYMLNGGEA----MVAK--V 325
Cdd:cd17652    167 ---------AEELLPGEPL--ADLLREHRITHVTLPPAALAALPPD---------DLPDLRTLVVAGEAcpaeLVDRwaP 226
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  326 GRRILEllephglpadairpAWGMSETSSGVifshefTRAGTSDDDHFVEIGSPIPGFSMRIVNDHNELVEEGEIGRFQV 405
Cdd:cd17652    227 GRRMIN--------------AYGPTETTVCA------TMAGPLPGGGVPPIGRPVPGTRVYVLDARLRPVPPGVPGELYI 286
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  406 SGLSVTSGYYQRPDLNESVFTEDGW-------FETGDLGFLRN-GRLTITGRTKDAIIINGinyysHAIesaveELSEIE 477
Cdd:cd17652    287 AGAGLARGYLNRPGLTAERFVADPFgapgsrmYRTGDLARWRAdGQLEFLGRADDQVKIRG-----FRI-----ELGEVE 356
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  478 TSYT-------AACAVRLGQNSTDQLAIFFVTSAKLNDEQmSQLLRNIQSHVsqvigvtPEYLLP---VQKEEIPKTAIG 547
Cdd:cd17652    357 AALTehpgvaeAVVVVRDDRPGDKRLVAYVVPAPGAAPTA-AELRAHLAERL-------PGYMVPaafVVLDALPLTPNG 428

                   ....*..
gi 1776025254  548 KIQRTQL 554
Cdd:cd17652    429 KLDRRAL 435
PRK05850 PRK05850
acyl-CoA synthetase; Validated
1158-1568 4.04e-20

acyl-CoA synthetase; Validated


Pssm-ID: 235624 [Multi-domain]  Cd Length: 578  Bit Score: 98.48  E-value: 4.04e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1158 LFEQQAKKTPDRAA---VSYEG------QTLTYRELDERSTQLAIYLQAHGVGPDRlAGIYVDRSLDMLVGLLAILKAGG 1228
Cdd:PRK05850     6 LLRERASLQPDDAAftfIDYEQdpagvaETLTWSQLYRRTLNVAEELRRHGSTGDR-AVILAPQGLEYIVAFLGALQAGL 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1229 AYVPLDPSYPA---ERLEYMLEDSEVFITLTTSELVN------TLSWNGVTTA-----LLDQDwdeiaqtaSDRKVLTRT 1294
Cdd:PRK05850    85 IAVPLSVPQGGahdERVSAVLRDTSPSVVLTTSAVVDdvteyvAPQPGQSAPPvievdLLDLD--------SPRGSDARP 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1295 VTPENLAYVIYTSGSTGKPKGVMIPHKALT-NFLVSM----GETPGLTAEDKMLaVTTYCF--DIA-ALELFLPLIKGah 1366
Cdd:PRK05850   157 RDLPSTAYLQYTSGSTRTPAGVMVSHRNVIaNFEQLMsdyfGDTGGVPPPDTTV-VSWLPFyhDMGlVLGVCAPILGG-- 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1367 cyiCQTEHTKDVEKLKRDIRTIK-----PTVMQATP------ATWK-----MlfySGWENEENVKILCGGEAL-PETLKR 1429
Cdd:PRK05850   234 ---CPAVLTSPVAFLQRPARWMQllasnPHAFSAAPnfafelAVRKtsdddM---AGLDLGGVLGIISGSERVhPATLKR 307
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1430 yFLDTGSeAWNM--------FGPTETTIWSA----------------------VQRINDECSRATIGRPIANTQIY-ITD 1478
Cdd:PRK05850   308 -FADRFA-PFNLretairpsYGLAEATVYVAtrepgqppesvrfdyeklsaghAKRCETGGGTPLVSYGSPRSPTVrIVD 385
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1479 SQ-LAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRF---IDNPFE--PGSKLYRTGDMArWLPGGRIEYIGRIDNQVKI 1552
Cdd:PRK05850   386 PDtCIECPAGTVGEIWVHGDNVAAGYWQKPEETERTFgatLVDPSPgtPEGPWLRTGDLG-FISEGELFIVGRIKDLLIV 464
                          490
                   ....*....|....*.
gi 1776025254 1553 RGFRIELGDIESRLSE 1568
Cdd:PRK05850   465 DGRNHYPDDIEATIQE 480
PRK07787 PRK07787
acyl-CoA synthetase; Validated
100-556 7.73e-20

acyl-CoA synthetase; Validated


Pssm-ID: 236096 [Multi-domain]  Cd Length: 471  Bit Score: 96.60  E-value: 7.73e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  100 AFWGCVLTGV--VPaplaVPPtyaesSSGTQKLKDawtlldkpaVITDRGMhQEMLDWAKEqGLEGFRAIIVEdlLSAEA 177
Cdd:PRK07787    61 AVVGALIAGVpvVP----VPP-----DSGVAERRH---------ILADSGA-QAWLGPAPD-DPAGLPHVPVR--LHARS 118
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  178 DTDWHQSSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDHVGGI--GML-HLRdvyLG 254
Cdd:PRK07787   119 WHRYPEPDPDAPALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAWQWTADDVLVHGLPLFHVHGLvlGVLgPLR---IG 195
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  255 CQEINVSSETilmePlkwldwiDHYRASVTWAPNFAFGLVTDFAEEIKDRKWD--LSSMRYMLNGGEAMVAKVGRRILEL 332
Cdd:PRK07787   196 NRFVHTGRPT----P-------EAYAQALSEGGTLYFGVPTVWSRIAADPEAAraLRGARLLVSGSAALPVPVFDRLAAL 264
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  333 LephGLpadaiRPA--WGMSET--SSGVIFSHEfTRAGTsdddhfveIGSPIPGFSMRIVNDH-NELVEEGE-IGRFQVS 406
Cdd:PRK07787   265 T---GH-----RPVerYGMTETliTLSTRADGE-RRPGW--------VGLPLAGVETRLVDEDgGPVPHDGEtVGELQVR 327
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  407 GLSVTSGYYQRPDLNESVFTEDGWFETGDL------GFLRngrltITGRTKDAIIINGiNYYSHAiesaveelSEIETSY 480
Cdd:PRK07787   328 GPTLFDGYLNRPDATAAAFTADGWFRTGDVavvdpdGMHR-----IVGRESTDLIKSG-GYRIGA--------GEIETAL 393
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  481 TAACAVR-----------LGQnstdQLAIFFVTSAKLNDEQMSQllrniqsHVSQvigvtpeyLLPVQK--------EEI 541
Cdd:PRK07787   394 LGHPGVReaavvgvpdddLGQ----RIVAYVVGADDVAADELID-------FVAQ--------QLSVHKrprevrfvDAL 454
                          490
                   ....*....|....*
gi 1776025254  542 PKTAIGKIQRTQLKT 556
Cdd:PRK07787   455 PRNAMGKVLKKQLLS 469
A_NRPS_ProA cd17656
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ...
61-554 9.37e-20

gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341311 [Multi-domain]  Cd Length: 479  Bit Score: 96.39  E-value: 9.37e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254   61 SYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNSQLLPAFWGCVLTGvvPAPLAVPPTYAESssgtqklKDAWTLLDKP 140
Cdd:cd17656     15 TYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAG--GAFVPIDPEYPEE-------RRIYIMLDSG 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  141 A-VITDRGMHQEMLDWAKEQGLegfraiIVEDLLSAEADTDWHQS-SPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKG 218
Cdd:cd17656     86 VrVVLTQRHLKSKLSFNKSTIL------LEDPSISQEDTSNIDYInNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLLHF 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  219 IIQMQGFTRED--ITFNWMPFDhvggIGMLHLRDVYLGCQEINVSSETILMEPLKWLDWIDHYRASVTWAPNfAF----- 291
Cdd:cd17656    160 EREKTNINFSDkvLQFATCSFD----VCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNIEVVFLPV-AFlkfif 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  292 ---GLVTDFAEEIKdrkwdlssmrYMLNGGEAMVakVGRRILELLEPHGLpadAIRPAWGMSETssgvifsHEFTRAGTS 368
Cdd:cd17656    235 serEFINRFPTCVK----------HIITAGEQLV--ITNEFKEMLHEHNV---HLHNHYGPSET-------HVVTTYTIN 292
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  369 DDDHFVE---IGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGYYQRPDLNESVFTEDGW------FETGDLG-F 438
Cdd:cd17656    293 PEAEIPElppIGKPISNTWIYILDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFdpnermYRTGDLArY 372
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  439 LRNGRLTITGRTKDAIIINGINYYSHAIESAveeLSEIETSYTAACAVRLGQNSTDQLAIFFVTSAKLNDEQMSQLLRni 518
Cdd:cd17656    373 LPDGNIEFLGRADHQVKIRGYRIELGEIEAQ---LLNHPGVSEAVVLDKADDKGEKYLCAYFVMEQELNISQLREYLA-- 447
                          490       500       510
                   ....*....|....*....|....*....|....*....
gi 1776025254  519 qshvSQVigvtPEYLLP---VQKEEIPKTAIGKIQRTQL 554
Cdd:cd17656    448 ----KQL----PEYMIPsffVPLDQLPLTPNGKVDRKAL 478
PTZ00050 PTZ00050
3-oxoacyl-acyl carrier protein synthase; Provisional
4604-4939 9.58e-20

3-oxoacyl-acyl carrier protein synthase; Provisional


Pssm-ID: 240245 [Multi-domain]  Cd Length: 421  Bit Score: 95.53  E-value: 9.58e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4604 TLESYWSLLSEGRSSIGPI---PAERWGCKTPYY-------------AGVIDGVSYFDPDFFLLHEED------VRAMDp 4661
Cdd:PTZ00050     8 GAESTWEALIAGKSGIRKLtefPKFLPDCIPEQKalenlvaampcqiAAEVDQSEFDPSDFAPTKRESrathfaMAAAR- 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4662 QALlvleECLKLLYHAGYTPEEIkGKPVGVYIGGRSQHKpDEDSLDHAKNP-------IVTVGQNYLAANLSQFFDVRGP 4734
Cdd:PTZ00050    87 EAL----ADAKLDILSEKDQERI-GVNIGSGIGSLADLT-DEMKTLYEKGHsrvspyfIPKILGNMAAGLVAIKHKLKGP 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4735 SVVVDTACSSALVGMNMAIQALRGGDIQSAIVGG----VSLLSSDASHRLfdrRGILSKH-----SSFHVFDERADGVVL 4805
Cdd:PTZ00050   161 SGSAVTACATGAHCIGEAFRWIKYGEADIMICGGteasITPVSFAGFSRM---RALCTKYnddpqRASRPFDKDRAGFVM 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4806 GEGVGMVMLKTVKQALEDGDTIYAVVKAASVNNDGRTAGPATPNLEAQKEVMKDALFKSGKKP-EDISYLEANGSGSIVT 4884
Cdd:PTZ00050   238 GEGAGILVLEELEHALRRGAKIYAEIRGYGSSSDAHHITAPHPDGRGARRCMENALKDGANINiNDVDYVNAHATSTPIG 317
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1776025254 4885 DLLELKAIQSVYRSGHSSPLSLGSIKPNIGHPLCAEGIASFIKVVLMLKERRFVP 4939
Cdd:PTZ00050   318 DKIELKAIKKVFGDSGAPKLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPP 372
PLN02836 PLN02836
3-oxoacyl-[acyl-carrier-protein] synthase
4719-4984 1.07e-19

3-oxoacyl-[acyl-carrier-protein] synthase


Pssm-ID: 215449 [Multi-domain]  Cd Length: 437  Bit Score: 95.63  E-value: 1.07e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4719 NYLAANLSQFFDVRGPSVVVDTACSSALVGMNMAIQALRGGDIQSAIVGGvSLLSSDA-SHRLFDR-RGILSKHSSFHV- 4795
Cdd:PLN02836   161 NMAAGHVSIRYGFQGPNHAAVTACATGAHSIGDAFRMIQFGDADVMVAGG-TESSIDAlSIAGFSRsRALSTKFNSCPTe 239
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4796 ----FDERADGVVLGEGVGMVMLKTVKQALEDGDTIYAVVKAASVNNDGRTAGPATPNLEAQKEVMKDALFKSGKKPEDI 4871
Cdd:PLN02836   240 asrpFDCDRDGFVIGEGAGVLVLEELEHAKRRGAKIYAEVRGYGMSGDAHHITQPHEDGRGAVLAMTRALQQSGLHPNQV 319
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4872 SYLEANGSGSIVTDLLELKAIQSVYRS-GHSSPLSLGSIKPNIGHPLCAEGIASFIKVVLMLKERRFVPFLSGEKEMAHF 4950
Cdd:PLN02836   320 DYVNAHATSTPLGDAVEARAIKTVFSEhATSGGLAFSSTKGATGHLLGAAGAVEAIFSVLAIHHGIAPPTLNLERPDPIF 399
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1776025254 4951 DQQKANITFSRAlekwtDSQPTAAINCFADGGTN 4984
Cdd:PLN02836   400 DDGFVPLTASKA-----MLIRAALSNSFGFGGTN 428
PRK09274 PRK09274
peptide synthase; Provisional
1161-1572 1.11e-19

peptide synthase; Provisional


Pssm-ID: 236443 [Multi-domain]  Cd Length: 552  Bit Score: 96.89  E-value: 1.11e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1161 QQAKKTPDRAAV----------SYEGQTLTYRELDERSTQLAIYLQAHGVGP-DRLAgIYVDRSLDMLVGLLAILKAGGA 1229
Cdd:PRK09274    14 RAAQERPDQLAVavpggrgadgKLAYDELSFAELDARSDAIAHGLNAAGIGRgMRAV-LMVTPSLEFFALTFALFKAGAV 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1230 YVPLDPSYPAERLEYMLEDS--EVFITLTTSELV------------------NTLSWNGVTTALLDQDWD----EIAQTA 1285
Cdd:PRK09274    93 PVLVDPGMGIKNLKQCLAEAqpDAFIGIPKAHLArrlfgwgkpsvrrlvtvgGRLLWGGTTLATLLRDGAaapfPMADLA 172
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1286 SDrkvltrtvtpeNLAYVIYTSGSTGKPKGVMIPHKALTNFLVSMGETPGLTAEDKMLAvttyCFDIAAleLFLPLIkGA 1365
Cdd:PRK09274   173 PD-----------DMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDLP----TFPLFA--LFGPAL-GM 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1366 HCYICQTEHTK----DVEKLKRDIRTIKPTVMQATPATWKMLFYSGWENE---ENVK-ILCGGE-ALPETLKRY--FLDT 1434
Cdd:PRK09274   235 TSVIPDMDPTRpatvDPAKLFAAIERYGVTNLFGSPALLERLGRYGEANGiklPSLRrVISAGApVPIAVIERFraMLPP 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1435 GSEAWNMFGPTE----TTIWSavQRINDECSRAT-------IGRPIANTQ---IYITD------SQLAPVPAGVPGELCI 1494
Cdd:PRK09274   315 DAEILTPYGATEalpiSSIES--REILFATRAATdngagicVGRPVDGVEvriIAISDapipewDDALRLATGEIGEIVV 392
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1776025254 1495 AGDGVAKGYYKKEELTDSRFIDNPfePGSKLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGI 1572
Cdd:PRK09274   393 AGPMVTRSYYNRPEATRLAKIPDG--QGDVWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGV 468
A_NRPS_Sfm_like cd12115
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ...
166-554 2.45e-19

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.


Pssm-ID: 341280 [Multi-domain]  Cd Length: 447  Bit Score: 94.69  E-value: 2.45e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  166 AIIVEDLLSAEADTDwhqssPEDLALLLLTSGSTGTPKAVMLNHRNIMSMvkgiIQ--MQGFTRED---------ITFNW 234
Cdd:cd12115     89 RFILEDAQARLVLTD-----PDDLAYVIYTSGSTGRPKGVAIEHRNAAAF----LQwaAAAFSAEElagvlastsICFDL 159
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  235 MPFDHVGgigmlhlrdvylgcqEINVSSETILMEPLkwLDWIDHYRASVTWAPNfafgLVTDFAEEIKDRKWDLSSMRyM 314
Cdd:cd12115    160 SVFELFG---------------PLATGGKVVLADNV--LALPDLPAAAEVTLIN----TVPSAAAELLRHDALPASVR-V 217
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  315 LN-GGEAMVAKVGRRILELLephglPADAIRPAWGMSETSSgviFS--HEFTRAGTSDddhfVEIGSPIPGFSMRIVNDH 391
Cdd:cd12115    218 VNlAGEPLPRDLVQRLYARL-----QVERVVNLYGPSEDTT---YStvAPVPPGASGE----VSIGRPLANTQAYVLDRA 285
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  392 NELVEEGEIGRFQVSGLSVTSGYYQRPDLNESVFTEDGW------FETGDLGFLR-NGRLTITGRTKDAIIINGINYYSH 464
Cdd:cd12115    286 LQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFgpgarlYRTGDLVRWRpDGLLEFLGRADNQVKVRGFRIELG 365
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  465 AIESAVEELSEIEtsytAACAVRLGQNSTD-QLAIFFVTSAKLndeqmSQLLRNIQSHVSQVIgvtPEYLLP---VQKEE 540
Cdd:cd12115    366 EIEAALRSIPGVR----EAVVVAIGDAAGErRLVAYIVAEPGA-----AGLVEDLRRHLGTRL---PAYMVPsrfVRLDA 433
                          410
                   ....*....|....
gi 1776025254  541 IPKTAIGKIQRTQL 554
Cdd:cd12115    434 LPLTPNGKIDRSAL 447
PLN02574 PLN02574
4-coumarate--CoA ligase-like
1218-1641 2.56e-19

4-coumarate--CoA ligase-like


Pssm-ID: 215312 [Multi-domain]  Cd Length: 560  Bit Score: 95.68  E-value: 2.56e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1218 VGLLAILKAGGAYVPLDPSYPAERLEYMLEDSEVFITLTTSELVNTLSWNGVTTALLDQ--DWDEIAQT--------ASD 1287
Cdd:PLN02574   107 VIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFTSPENVEKLSPLGVPVIGVPEnyDFDSKRIEfpkfyeliKED 186
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1288 RKVLTR-TVTPENLAYVIYTSGSTGKPKGVMIPHKAL-------TNFLVSMGETPGltAEDKMLAVTTYcFDIAALELFL 1359
Cdd:PLN02574   187 FDFVPKpVIKQDDVAAIMYSSGTTGASKGVVLTHRNLiamvelfVRFEASQYEYPG--SDNVYLAALPM-FHIYGLSLFV 263
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1360 P--LIKGAHCYICQ----TEHTKDVEKLKRDIRTIKPTVMQATPATWKMLfySGWENEENVKILCGGEALPETLKRYFLD 1433
Cdd:PLN02574   264 VglLSLGSTIVVMRrfdaSDMVKVIDRFKVTHFPVVPPILMALTKKAKGV--CGEVLKSLKQVSCGAAPLSGKFIQDFVQ 341
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1434 TGSEA--WNMFGPTETTiwsAV--QRINDECSR--ATIGRPIANTQIYITD-SQLAPVPAGVPGELCIAGDGVAKGYYKK 1506
Cdd:PLN02574   342 TLPHVdfIQGYGMTEST---AVgtRGFNTEKLSkySSVGLLAPNMQAKVVDwSTGCLLPPGNCGELWIQGPGVMKGYLNN 418
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1507 EELTDSRFIDNPFepgsklYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMDNLAA 1586
Cdd:PLN02574   419 PKATQSTIDKDGW------LRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECG 492
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1776025254 1587 ----YYTAKHANASLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLKNI 1641
Cdd:PLN02574   493 eipvAFVVRRQGSTLSQEAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELKRS 551
PRK14691 PRK14691
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
3475-3780 2.96e-19

3-oxoacyl-(acyl carrier protein) synthase II; Provisional


Pssm-ID: 173154 [Multi-domain]  Cd Length: 342  Bit Score: 92.87  E-value: 2.96e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3475 IEGHAATGHMI---PSVGPNRMSYFL-----------------NIHGPSEPVETACSSSLVAIHRAVTAMQNGDCEMAIA 3534
Cdd:PRK14691    36 IGGFPAIAHAVrtsDSRGPKRLSPFTvpsflvnlaaghvsikhHFKGPIGAPVTACAAGVQAIGDAVRMIRNNEADVALC 115
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3535 GGVNTILTEEAHISYSKAGMLSK------DGRCKTFSADANGYVRGEGVGMVMLKKLEDAERDGNHIYGVIRGTAENHGG 3608
Cdd:PRK14691   116 GGAEAVIDTVSLAGFAAARALSThfnstpEKASRPFDTARDGFVMGEGAGLLIIEELEHALARGAKPLAEIVGYGTSADA 195
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3609 RANTLTSPNPKAQADLLVRAYRQAGIDPSTVTYIEAHGTGTELGDPIEINGLKAAFkelsnmrGESQPdvpdhrCGIGSV 3688
Cdd:PRK14691   196 YHMTSGAEDGDGAYRAMKIALRQAGITPEQVQHLNAHATSTPVGDLGEINAIKHLF-------GESNA------LAITST 262
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3689 KSNIGHLELAAGISGLIKVLLQMKHKTLVKSLHCETLNPYLqltdspfyivqekqewKSVTDCDGNELPRR---AGISSF 3765
Cdd:PRK14691   263 KSATGHLLGAAGGLETIFTVLALRDQIVPATLNLENPDPAA----------------KGLNIIAGNAQPHDmtyALSNGF 326
                          330
                   ....*....|....*
gi 1776025254 3766 GIGGVNAHIVIEEYM 3780
Cdd:PRK14691   327 GFAGVNASILLKRWV 341
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
4169-4351 3.51e-19

NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and metabolism]; NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440651 [Multi-domain]  Cd Length: 249  Bit Score: 90.23  E-value: 3.51e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4169 KDHVLLITGGTRGIGLLCARHFAECyGVKkLVLTGReqlppREEWARfktsntslaekiQAVRELEAKGVQVEMLSLTLS 4248
Cdd:COG1028      5 KGKVALVTGGSSGIGRAIARALAAE-GAR-VVITDR-----DAEALE------------AAAAELRAAGGRALAVAADVT 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4249 DDAQVEQTLQHIKRTLGPIGGVIHCAGLTDMDTLAfiRKTSDDIQRVMEPKVSGLTTLYRHVcnepLQFF--------VL 4320
Cdd:COG1028     66 DEAAVEALVAAAVAAFGRLDILVNNAGITPPGPLE--ELTEEDWDRVLDVNLKGPFLLTRAA----LPHMrergggriVN 139
                          170       180       190
                   ....*....|....*....|....*....|.
gi 1776025254 4321 FSSVSAIIPelSAGQADYAMANSYMDYFAEA 4351
Cdd:COG1028    140 ISSIAGLRG--SPGQAAYAASKAAVVGLTRS 168
LC_FACS_bac cd05932
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ...
186-452 3.71e-19

Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341255 [Multi-domain]  Cd Length: 508  Bit Score: 94.84  E-value: 3.71e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  186 PEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDHVGGIGMLHLRDVYLGCQEINVSSETI 265
Cdd:cd05932    136 PEQLATLIYTSGTTGQPKGVMLTFGSFAWAAQAGIEHIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAESLDT 215
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  266 LMEPLKwldwidhyRASvtwaPNFAFG---LVTDFAEEIKDR----KWD---------------------LSSMRYMLNG 317
Cdd:cd05932    216 FVEDVQ--------RAR----PTLFFSvprLWTKFQQGVQDKipqqKLNlllkipvvnslvkrkvlkglgLDQCRLAGCG 283
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  318 GeamvAKVGRRILELLEPHGLPadaIRPAWGMSETSSGVIFSHEF-TRAGTsdddhfveIGSPIPGFSMRIVndhnelvE 396
Cdd:cd05932    284 S----APVPPALLEWYRSLGLN---ILEAYGMTENFAYSHLNYPGrDKIGT--------VGNAGPGVEVRIS-------E 341
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1776025254  397 EGEIgrfQVSGLSVTSGYYQRPDLNESVFTEDGWFETGDLGFL-RNGRLTITGRTKD 452
Cdd:cd05932    342 DGEI---LVRSPALMMGYYKDPEATAEAFTADGFLRTGDKGELdADGNLTITGRVKD 395
PRK05952 PRK05952
beta-ketoacyl-ACP synthase;
1985-2179 4.17e-19

beta-ketoacyl-ACP synthase;


Pssm-ID: 235653 [Multi-domain]  Cd Length: 381  Bit Score: 93.19  E-value: 4.17e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1985 FDASADGMIGGEGVAVVLLKKAADAVKDGDHIYALLRGIGVNNDgADKVGFYAPSVKGQADVVQQVMNQTKIHPESICYV 2064
Cdd:PRK05952   199 FDRQREGLVLGEGGAILVLESAELAQKRGAKIYGQILGFGLTCD-AYHMSAPEPDGKSAIAAIQQCLARSGLTPEDIDYI 277
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2065 EAHGTGTKLGDPIELAALTNVYRQYTnktqfcGIGSVKTNIGHLDTAAGLAGCIKVVMSLYHQELAPSINYKEPNPNTDL 2144
Cdd:PRK05952   278 HAHGTATRLNDQREANLIQALFPHRV------AVSSTKGATGHTLGASGALGVAFSLLALRHQQLPPCVGLQEPEFDLNF 351
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1776025254 2145 ASSPfyvvdqkktlsREIQTHRAALSSFGLGGTNT 2179
Cdd:PRK05952   352 VRQA-----------QQSPLQNVLCLSFGFGGQNA 375
entE PRK10946
(2,3-dihydroxybenzoyl)adenylate synthase;
27-555 6.14e-19

(2,3-dihydroxybenzoyl)adenylate synthase;


Pssm-ID: 236803 [Multi-domain]  Cd Length: 536  Bit Score: 94.29  E-value: 6.14e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254   27 QPATipEVLYRTAAelGDTKGIIylqpDGTEVYqSYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNSQLLPAFWGCVL 106
Cdd:PRK10946    25 LPLT--DILTRHAA--SDAIAVI----CGERQF-SYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLK 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  107 TGVVPaplaVPPTYAEsssgtQKLK-DAWTLLDKPA-VITDRGmHQEMLDwakEQGLEGFRAII---------------- 168
Cdd:PRK10946    96 LGVAP----VNALFSH-----QRSElNAYASQIEPAlLIADRQ-HALFSD---DDFLNTLVAEHsslrvvlllnddgehs 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  169 VEDLLSAEADTDWHQSSPED-LALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDH------VG 241
Cdd:PRK10946   163 LDDAINHPAEDFTATPSPADeVAFFQLSGGSTGTPKLIPRTHNDYYYSVRRSVEICGFTPQTRYLCALPAAHnypmssPG 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  242 GIGMLHLRdvylGCQEINVSSETILMEPLkwldwIDHYRASVTWAPNFAFGLVTDFAEEIKDRKwDLSSMRYMLNGGEAM 321
Cdd:PRK10946   243 ALGVFLAG----GTVVLAPDPSATLCFPL-----IEKHQVNVTALVPPAVSLWLQAIAEGGSRA-QLASLKLLQVGGARL 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  322 VAKVGRRILELLephglpADAIRPAWGMSEtssGVIfshEFTRAGTSDDDHFVEIGSPI-PGFSMRIVNDHNELVEEGEI 400
Cdd:PRK10946   313 SETLARRIPAEL------GCQLQQVFGMAE---GLV---NYTRLDDSDERIFTTQGRPMsPDDEVWVADADGNPLPQGEV 380
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  401 GRFQVSGLSVTSGYYQRPDLNESVFTEDGWFETGDLGFLR-NGRLTITGRTKDAIIINGINYYSHAIESAVeeLSEIETS 479
Cdd:PRK10946   381 GRLMTRGPYTFRGYYKSPQHNASAFDANGFYCSGDLVSIDpDGYITVVGREKDQINRGGEKIAAEEIENLL--LRHPAVI 458
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  480 YTAACAV---RLGQNStdqlAIFFVTSAKLNDEQMSQLLRNiqshvsqvIGVTpEYLLPVQKEEI---PKTAIGKIQRTQ 553
Cdd:PRK10946   459 HAALVSMedeLMGEKS----CAFLVVKEPLKAVQLRRFLRE--------QGIA-EFKLPDRVECVdslPLTAVGKVDKKQ 525

                   ..
gi 1776025254  554 LK 555
Cdd:PRK10946   526 LR 527
PRK07470 PRK07470
acyl-CoA synthetase; Validated
162-564 6.64e-19

acyl-CoA synthetase; Validated


Pssm-ID: 180988 [Multi-domain]  Cd Length: 528  Bit Score: 93.95  E-value: 6.64e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  162 EGFRAIIVEDLLSAEADTDWHQSSPedlALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQ--MQGFTREDITFNWMPFDH 239
Cdd:PRK07470   141 LDYEALVARHLGARVANAAVDHDDP---CWFFFTSGTTGRPKAAVLTHGQMAFVITNHLAdlMPGTTEQDASLVVAPLSH 217
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  240 vgGIGMLHLRDVYLGCQEINVSSETilMEPLKWLDWIDHYRASVTWA-PNFAFGLVTDFAEEikdrKWDLSSMRYMLNGG 318
Cdd:PRK07470   218 --GAGIHQLCQVARGAATVLLPSER--FDPAEVWALVERHRVTNLFTvPTILKMLVEHPAVD----RYDHSSLRYVIYAG 289
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  319 EAMVAKVGRRILELLEPhglpadAIRPAWGMSETSSGVIF----SHEftragtSDDDHFVEIGS---PIPGFSMRIVNDH 391
Cdd:PRK07470   290 APMYRADQKRALAKLGK------VLVQYFGLGEVTGNITVlppaLHD------AEDGPDARIGTcgfERTGMEVQIQDDE 357
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  392 NELVEEGEIGRFQVSGLSVTSGYYQRPDLNESVFtEDGWFETGDLGFL-RNGRLTITGRTKDAIIINGINYYSHAIES-- 468
Cdd:PRK07470   358 GRELPPGETGEICVIGPAVFAGYYNNPEANAKAF-RDGWFRTGDLGHLdARGFLYITGRASDMYISGGSNVYPREIEEkl 436
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  469 ----AVEELS----------EIEtsyTAACAVRLGqnstdqlaiffvtsAKLNDEQMSQLLRniqshvsqviGVTPEYLL 534
Cdd:PRK07470   437 lthpAVSEVAvlgvpdpvwgEVG---VAVCVARDG--------------APVDEAELLAWLD----------GKVARYKL 489
                          410       420       430
                   ....*....|....*....|....*....|....
gi 1776025254  535 P---VQKEEIPKTAIGKIQRTQLKTSFEN-GEFD 564
Cdd:PRK07470   490 PkrfFFWDALPKSGYGKITKKMVREELEErGLLD 523
PaaK COG1541
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ...
195-552 7.43e-19

Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];


Pssm-ID: 441150 [Multi-domain]  Cd Length: 423  Bit Score: 92.90  E-value: 7.43e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  195 TSGSTGTPKAVMLNHR---NIMSMVKGIIQMQGFTREDITFNWMPFD-HVGGIGMlhlrdvYLGCQEINVSseTILMEPL 270
Cdd:COG1541     91 SSGTTGKPTVVGYTRKdldRWAELFARSLRAAGVRPGDRVQNAFGYGlFTGGLGL------HYGAERLGAT--VIPAGGG 162
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  271 ---KWLDWIDHYRASVTWA-PNFAFGLvtdfAEEIKDRKWDL--SSMRYMLNGGEAMVAKVGRRILELLephGLPA-DAi 343
Cdd:COG1541    163 nteRQLRLMQDFGPTVLVGtPSYLLYL----AEVAEEEGIDPrdLSLKKGIFGGEPWSEEMRKEIEERW---GIKAyDI- 234
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  344 rpaWGMSETSSGVIFSHEfTRAGTS-DDDHF-VEIGSPIPGfsmrivndhnELVEEGEIGRfqvsgLSVTSgyyqrpdln 421
Cdd:COG1541    235 ---YGLTEVGPGVAYECE-AQDGLHiWEDHFlVEIIDPETG----------EPVPEGEEGE-----LVVTT--------- 286
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  422 esvFTEDGW----FETGDLGFLRNG---------RLT-ITGRTKDAIIINGINYYSHAIESAVEELSEIETSYTaacAVR 487
Cdd:COG1541    287 ---LTKEAMplirYRTGDLTRLLPEpcpcgrthpRIGrILGRADDMLIIRGVNVFPSQIEEVLLRIPEVGPEYQ---IVV 360
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1776025254  488 LGQNSTDQLAIFFVTSAKLNDEqmsQLLRNIQSHVSQVIGVTPEYLLpVQKEEIPKTAiGKIQRT 552
Cdd:COG1541    361 DREGGLDELTVRVELAPGASLE---ALAEAIAAALKAVLGLRAEVEL-VEPGSLPRSE-GKAKRV 420
PRK09185 PRK09185
beta-ketoacyl-ACP synthase;
1908-2183 8.17e-19

beta-ketoacyl-ACP synthase;


Pssm-ID: 236398 [Multi-domain]  Cd Length: 392  Bit Score: 92.21  E-value: 8.17e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1908 GTIPTMISHKLGLRGPSYFVHANCSSSLIGLHSAyKSLLSAE-SDYALVGGA------TLHtesniGYvhqPGLNFSSDG 1980
Cdd:PRK09185   137 GSLADFLRAYLGLSGPAYTISTACSSSAKVFASA-RRLLEAGlCDAAIVGGVdslcrlTLN-----GF---NSLESLSPQ 207
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1981 HIKAFDASADGMIGGEGVAVVLLKKAADAVkdgdhiyALLRGIGVNNDgadkvgfyA-------PSVKGQADVVQQVMNQ 2053
Cdd:PRK09185   208 PCRPFSANRDGINIGEAAAFFLLEREDDAA-------VALLGVGESSD--------AhhmsaphPEGLGAILAMQQALAD 272
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2054 TKIHPESICYVEAHGTGTKLGDPIELAALTNVYRQYTNktqfCgiGSVKTNIGHldtAAGLAGCIKVV---MSLYHQELA 2130
Cdd:PRK09185   273 AGLAPADIGYINLHGTATPLNDAMESRAVAAVFGDGVP----C--SSTKGLTGH---TLGAAGAVEAAicwLALRHGLPP 343
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1776025254 2131 PSINYKEPNPntDLAssPFYVVDQKKTLSReiqthRAALS-SFGLGGTNTHAIF 2183
Cdd:PRK09185   344 HGWNTGQPDP--ALP--PLYLVENAQALAI-----RYVLSnSFAFGGNNCSLIF 388
PRK12467 PRK12467
peptide synthase; Provisional
186-663 1.45e-18

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 94.84  E-value: 1.45e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  186 PEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDHVGGI----------GMLHLRDvylgc 255
Cdd:PRK12467  3236 GENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSFSFDGAQerflwtlicgGCLVVRD----- 3310
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  256 qeinvsseTILMEPLKWLDWIDHYRASVTwapNFAFGLVTDFAEEIKDRkwDLSSMRYMLNGGEAMVAKVGRRILELLEP 335
Cdd:PRK12467  3311 --------NDLWDPEELWQAIHAHRISIA---CFPPAYLQQFAEDAGGA--DCASLDIYVFGGEAVPPAAFEQVKRKLKP 3377
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  336 HGLpadaiRPAWGMSETSSGVIfsHEFTRAGTSDDDHFVEIGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGYY 415
Cdd:PRK12467  3378 RGL-----TNGYGPTEAVVTVT--LWKCGGDAVCEAPYAPIGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGVGLARGYH 3450
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  416 QRPDLNESVFTEDGW-------FETGDLGFLR-NGRLTITGRTKDAIIINGINYyshaiesaveELSEIETSYTAACAVR 487
Cdd:PRK12467  3451 QRPSLTAERFVADPFsgsggrlYRTGDLARYRaDGVIEYLGRIDHQVKIRGFRI----------ELGEIEARLLQHPSVR 3520
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  488 ----LGQNSTD--QLAIFFVtSAKLNDEQMSQLLRNIQSHVsqvigvtPEYLLPVQ---KEEIPKTAIGKIQRtqlktsf 558
Cdd:PRK12467  3521 eavvLARDGAGgkQLVAYVV-PADPQGDWRETLRDHLAASL-------PDYMVPAQllvLAAMPLGPNGKVDR------- 3585
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  559 engefdhllhkpnrmnDAVQDEEMQQADHVKRVREEIQEHLLTCLTEELHVSRdwVEPNANIQSLGVNSIKMMKLIRSIE 638
Cdd:PRK12467  3586 ----------------KALPDPDAKGSREYVAPRSEVEQQLAAIWADVLGVEQ--VGVTDNFFELGGDSLLALQVLSRIR 3647
                          490       500
                   ....*....|....*....|....*
gi 1776025254  639 KNYHIKLTAREIHQYPTIERLASYL 663
Cdd:PRK12467  3648 QSLGLKLSLRDLMSAPTIAELAGYS 3672
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
2852-3015 1.61e-18

short chain dehydrogenase; This family contains a wide variety of dehydrogenases.


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 86.90  E-value: 1.61e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2852 LITGGAGSLGLLFAKEIAnRTGrSTIVLTGRSVlsEDKENELEALRSIGAEVVYREADVSDQHAVHHLFEEIKERYGTLN 2931
Cdd:pfam00106    4 LVTGASSGIGRAIAKRLA-KEG-AKVVLVDRSE--EKLEAVAKELGALGGKALFIQGDVTDRAQVKALVEQAVERLGRLD 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2932 GIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSGLLHvdeCSKDFpLDFF--------IFFSSVSGCLGNAGQADYAAANSF 3003
Cdd:pfam00106   80 ILVNNAGITGLGPFSELSDEDWERVIDVNLTGVFN---LTRAV-LPAMikgsggriVNISSVAGLVPYPGGSAYSASKAA 155
                          170
                   ....*....|..
gi 1776025254 3004 MDAFAeyrRSLA 3015
Cdd:pfam00106  156 VIGFT---RSLA 164
PRK08276 PRK08276
long-chain-fatty-acid--CoA ligase; Validated
1170-1633 1.85e-18

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236215 [Multi-domain]  Cd Length: 502  Bit Score: 92.66  E-value: 1.85e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1170 AAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLEDS 1249
Cdd:PRK08276     3 VIMAPSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDS 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1250 E--VFITL-----TTSELVNTLSwNGVTTALLD-------QDWDEIAQTASDRKVLTRTVTpenlAYVIYTSGSTGKPKG 1315
Cdd:PRK08276    83 GakVLIVSaaladTAAELAAELP-AGVPLLLVVagpvpgfRSYEEALAAQPDTPIADETAG----ADMLYSSGTTGRPKG 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1316 VMI------PHKALTNFLVSMGETPGLTAEDKML--------AVTTYCFDIAAL------------ELFLPLI---KGAH 1366
Cdd:PRK08276   158 IKRplpgldPDEAPGMMLALLGFGMYGGPDSVYLspaplyhtAPLRFGMSALALggtvvvmekfdaEEALALIeryRVTH 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1367 CYICQT---------EHTK---DVEKLKRDIRTIKPTvmqATPATWKMLFYsgWeneenvkilcgGEALPETlkrYfldT 1434
Cdd:PRK08276   238 SQLVPTmfvrmlklpEEVRaryDVSSLRVAIHAAAPC---PVEVKRAMIDW--W-----------GPIIHEY---Y---A 295
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1435 GSEAwNMFgptetTIWSAVQRINdecSRATIGRPIAnTQIYITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSrf 1514
Cdd:PRK08276   296 SSEG-GGV-----TVITSEDWLA---HPGSVGKAVL-GEVRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAA-- 363
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1515 IDNPfepgSKLYRTGDMArWLPGGRIEYI-GRIDNQVKIRGFRIELGDIESRLSEHPGILECVVV----ADMDN--LAAY 1587
Cdd:PRK08276   364 ARNP----HGWVTVGDVG-YLDEDGYLYLtDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFgvpdEEMGErvKAVV 438
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*..
gi 1776025254 1588 YTAKHANAS-LTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKI 1633
Cdd:PRK08276   439 QPADGADAGdALAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKL 485
PLN02387 PLN02387
long-chain-fatty-acid-CoA ligase family protein
1154-1580 1.88e-18

long-chain-fatty-acid-CoA ligase family protein


Pssm-ID: 215217 [Multi-domain]  Cd Length: 696  Bit Score: 93.64  E-value: 1.88e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1154 TFHELFEQQAKKTPD------RAAVSYEGQT-----------------LTYRELDERSTQLAIYLQAHGVGPDRLAGIYV 1210
Cdd:PLN02387    59 TLAALFEQSCKKYSDkrllgtRKLISREFETssdgrkfeklhlgeyewITYGQVFERVCNFASGLVALGHNKEERVAIFA 138
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1211 DRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLEDSEVFI----------------TLTTSELVNTLSWNGVTTALL 1274
Cdd:PLN02387   139 DTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTvicdskqlkklidissQLETVKRVIYMDDEGVDSDSS 218
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1275 DQD---W-----DEIAQTASDRKVLTRTVTPENLAYVIYTSGSTGKPKGVMIPHKALTNFLVS-MGETPGLTAEDKMLAV 1345
Cdd:PLN02387   219 LSGssnWtvssfSEVEKLGKENPVDPDLPSPNDIAVIMYTSGSTGLPKGVMMTHGNIVATVAGvMTVVPKLGKNDVYLAY 298
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1346 --TTYCFDIAAlELFLPLIKGAHCYICQTEHTKDVEKLKR----DIRTIKPTVMQATPATW------------------K 1401
Cdd:PLN02387   299 lpLAHILELAA-ESVMAAVGAAIGYGSPLTLTDTSNKIKKgtkgDASALKPTLMTAVPAILdrvrdgvrkkvdakgglaK 377
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1402 MLF---------------YSGWENE---------ENVK---------ILCGGEALPETLKRyFLDT--GSEAWNMFGPTE 1446
Cdd:PLN02387   378 KLFdiaykrrlaaiegswFGAWGLEkllwdalvfKKIRavlggrirfMLSGGAPLSGDTQR-FINIclGAPIGQGYGLTE 456
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1447 TTIWSAVQRINDEcSRATIGRPIANTQI---------Y-ITDSqlaPVPAgvpGELCIAGDGVAKGYYKKEELTDSRFID 1516
Cdd:PLN02387   457 TCAGATFSEWDDT-SVGRVGPPLPCCYVklvsweeggYlISDK---PMPR---GEIVIGGPSVTLGYFKNQEKTDEVYKV 529
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1776025254 1517 NpfEPGSKLYRTGDMARWLPGGRIEYIGRIDNQVKIR-GFRIELGDIESRLSEHPGILECVVVAD 1580
Cdd:PLN02387   530 D--ERGMRWFYTGDIGQFHPDGCLEIIDRKKDIVKLQhGEYVSLGKVEAALSVSPYVDNIMVHAD 592
PRK07867 PRK07867
acyl-CoA synthetase; Validated
1168-1639 2.56e-18

acyl-CoA synthetase; Validated


Pssm-ID: 236120 [Multi-domain]  Cd Length: 529  Bit Score: 92.44  E-value: 2.56e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1168 DRAAVSYEGQTLTYRELDERSTQLAIYLQAHgVGPDRLA--GIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYM 1245
Cdd:PRK07867    18 DDRGLYFEDSFTSWREHIRGSAARAAALRAR-LDPTRPPhvGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARD 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1246 LEDSEVFITLTTSELVNTLSWNGVTTALLDQD---WDEIAQTASDRKVLTRTVTPENLAYVIYTSGSTGKPKGVMIPHKA 1322
Cdd:PRK07867    97 IAHADCQLVLTESAHAELLDGLDPGVRVINVDspaWADELAAHRDAEPPFRVADPDDLFMLIFTSGTSGDPKAVRCTHRK 176
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1323 LTNFLVSMGETPGLTAEDkmlavTTYC----FDIAA-LELFLP-LIKGAHCYICQtehtkdveklKRDIRTIKPTVMQ-- 1394
Cdd:PRK07867   177 VASAGVMLAQRFGLGPDD-----VCYVsmplFHSNAvMAGWAVaLAAGASIALRR----------KFSASGFLPDVRRyg 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1395 ATPATW--KMLFY------SGWENEENVKILCGGEALPETLKRYFLDTGSEAWNMFGPTETTIwsAVQRINDECSRAtIG 1466
Cdd:PRK07867   242 ATYANYvgKPLSYvlatpeRPDDADNPLRIVYGNEGAPGDIARFARRFGCVVVDGFGSTEGGV--AITRTPDTPPGA-LG 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1467 RPIANTQIYITDSqLAPVPAGVP------------GELC-IAGDGVAKGYYKKEELTDSRFIDNpfepgskLYRTGDMAR 1533
Cdd:PRK07867   319 PLPPGVAIVDPDT-GTECPPAEDadgrllnadeaiGELVnTAGPGGFEGYYNDPEADAERMRGG-------VYWSGDLAY 390
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1534 WLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMDNLaayyTAKHANASLTARELRHFVKNALPAY 1613
Cdd:PRK07867   391 RDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPV----VGDQVMAALVLAPGAKFDPDAFAEF 466
                          490       500       510
                   ....*....|....*....|....*....|....*.
gi 1776025254 1614 ----------MVPSYFIQLDHMPLTPNGKIDRNSLK 1639
Cdd:PRK07867   467 laaqpdlgpkQWPSYVRVCAELPRTATFKVLKRQLS 502
PRK09116 PRK09116
beta-ketoacyl-ACP synthase;
1985-2183 2.76e-18

beta-ketoacyl-ACP synthase;


Pssm-ID: 181657 [Multi-domain]  Cd Length: 405  Bit Score: 90.82  E-value: 2.76e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1985 FDASADGMIGGEGVAVVLLKKAADAVKDGDHIYALLRGIGVNNDGADkvgFYAPSVKGQADVVQQVMNQTKIHPESICYV 2064
Cdd:PRK09116   222 FDANRDGLVIGEGAGTLVLEELEHAKARGATIYAEIVGFGTNSDGAH---VTQPQAETMQIAMELALKDAGLAPEDIGYV 298
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2065 EAHGTGTKLGDPIELAALTNVYRQYTNktqfcgIGSVKTNIGHldtAAGLAGCIKVVMSLYHQE---LAPSINYKEPNPN 2141
Cdd:PRK09116   299 NAHGTATDRGDIAESQATAAVFGARMP------ISSLKSYFGH---TLGACGALEAWMSIEMMNegwFAPTLNLTQVDPA 369
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1776025254 2142 T-DLAsspfYVVDQkktlSREIQTHRAALSSFGLGGTNTHAIF 2183
Cdd:PRK09116   370 CgALD----YIMGE----AREIDTEYVMSNNFAFGGINTSLIF 404
PRK05852 PRK05852
fatty acid--CoA ligase family protein;
61-454 3.10e-18

fatty acid--CoA ligase family protein;


Pssm-ID: 235625 [Multi-domain]  Cd Length: 534  Bit Score: 92.26  E-value: 3.10e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254   61 SYR---RLWDDglrIVKGLRQSGLKAKQSVILQLGDNSQLLPAFWGCVLTGVVPAPLAVPPTYAESSSGTQKLKDAWTLL 137
Cdd:PRK05852    45 SYRdlaRLVDD---LAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLI 121
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  138 DKPAVI-TDRGMHQEMLDWAKEQGLEGFRAIIVEDLLSAEADTDWHQSSPEDL----ALLLLTSGSTGTPKAVMLNHRNI 212
Cdd:PRK05852   122 DADGPHdRAEPTTRWWPLTVNVGGDSGPSGGTLSVHLDAATEPTPATSTPEGLrpddAMIMFTGGTTGLPKMVPWTHANI 201
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  213 MSMVKGIIQMQGFTREDITFNWMPFDH-------------VGGIGMLHLRDVYlgcqeinvSSETIlmeplkwldWIDHY 279
Cdd:PRK05852   202 ASSVRAIITGYRLSPRDATVAVMPLYHghgliaallatlaSGGAVLLPARGRF--------SAHTF---------WDDIK 264
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  280 RASVTW---APNFAFGLVTDFAEEIKDRKwdLSSMRYMLNGGEAMVAKVGrriLELLEPHGLPadaIRPAWGMSETSSGV 356
Cdd:PRK05852   265 AVGATWytaVPTIHQILLERAATEPSGRK--PAALRFIRSCSAPLTAETA---QALQTEFAAP---VVCAFGMTEATHQV 336
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  357 ifshEFTRAGTSDDDHFVEIGSPIPGFS----MRIVNDHNELVEEGEIGRFQVSGLSVTSGYYQRPDLNESVFTeDGWFE 432
Cdd:PRK05852   337 ----TTTQIEGIGQTENPVVSTGLVGRStgaqIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANFT-DGWLR 411
                          410       420
                   ....*....|....*....|...
gi 1776025254  433 TGDLGFLR-NGRLTITGRTKDAI 454
Cdd:PRK05852   412 TGDLGSLSaAGDLSIRGRIKELI 434
MACS_like_4 cd05969
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ...
61-555 3.15e-18

Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.


Pssm-ID: 341273 [Multi-domain]  Cd Length: 442  Bit Score: 91.02  E-value: 3.15e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254   61 SYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNSQLLPAFWGCVLTGVVPAPLAvpptyaeSSSGTQKLKDAWTLLDKP 140
Cdd:cd05969      2 TFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLF-------SAFGPEAIRDRLENSEAK 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  141 AVITdrgmHQEMLDwakeqglegfraiivedllsaeadtdwhQSSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGII 220
Cdd:cd05969     75 VLIT----TEELYE----------------------------RTDPEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGK 122
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  221 QMQGFTREDITF-----NWMPFDHVGGIG-MLHlrdvylGCQEINVSSEtilMEPLKWLDWIDHYRASVTWAPNFAFGLV 294
Cdd:cd05969    123 YVLDLHPDDIYWctadpGWVTGTVYGIWApWLN------GVTNVVYEGR---FDAESWYGIIERVKVTVWYTAPTAIRML 193
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  295 TDFAEEIKdRKWDLSSMRYMLNGGEAMVAKVGRRILELLephGLPadaIRPAWGMSETSSGVIFSH--EFTRAGTsdddh 372
Cdd:cd05969    194 MKEGDELA-RKYDLSSLRFIHSVGEPLNPEAIRWGMEVF---GVP---IHDTWWQTETGSIMIANYpcMPIKPGS----- 261
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  373 fveIGSPIPGFSMRIVNDHNELVEEGEIGRFQV-SGL-SVTSGYYQRPDLNESVFTeDGWFETGDLGFL-RNGRLTITGR 449
Cdd:cd05969    262 ---MGKPLPGVKAAVVDENGNELPPGTKGILALkPGWpSMFRGIWNDEERYKNSFI-DGWYLTGDLAYRdEDGYFWFVGR 337
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  450 TKDAIIINGINYYSHAIESAVeelseIETSYTAACAVrLGQnsTDQLAIFFVT---SAKLNDEQMSQLLRNIQSHVSQVI 526
Cdd:cd05969    338 ADDIIKTSGHRVGPFEVESAL-----MEHPAVAEAGV-IGK--PDPLRGEIIKafiSLKEGFEPSDELKEEIINFVRQKL 409
                          490       500       510
                   ....*....|....*....|....*....|..
gi 1776025254  527 GVTpeyLLPVQ---KEEIPKTAIGKIQRTQLK 555
Cdd:cd05969    410 GAH---VAPREiefVDNLPKTRSGKIMRRVLK 438
PRK07910 PRK07910
beta-ketoacyl-ACP synthase;
3338-3779 3.16e-18

beta-ketoacyl-ACP synthase;


Pssm-ID: 236129 [Multi-domain]  Cd Length: 418  Bit Score: 90.94  E-value: 3.16e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3338 FEPVAIVGISGRFPGAMDIDEFWKNLEEGKDSITEVPKDrwdWREHYGNPdtdvnktdIKWGGFIdgVAEFDPLFFGISP 3417
Cdd:PRK07910    11 FPNVVVTGIAMTTALATDAETTWKLLLDGQSGIRTLDDP---FVEEFDLP--------VRIGGHL--LEEFDHQLTRVEL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3418 READYVDPQQRLLMTYVWkalEDAGCP---PQSLsgtgtGIFIGTGNTGYKDL-FHRANLPIEGHAATGHM-IPSVGPNR 3492
Cdd:PRK07910    78 RRMSYLQRMSTVLGRRVW---ENAGSPevdTNRL-----MVSIGTGLGSAEELvFAYDDMRARGLRAVSPLaVQMYMPNG 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3493 MSYF--LNIH---GPSEPVeTACSSSLVAIHRAVTAMQNGDCEMAIAGGVNTILTEEAHISYSKAGM-LSKD-----GRC 3561
Cdd:PRK07910   150 PAAAvgLERHakaGVITPV-SACASGSEAIAQAWRQIVLGEADIAICGGVETRIEAVPIAGFAQMRIvMSTNnddpaGAC 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3562 KTFSADANGYVRGEGVGMVMLKKLEDAERDGNHIYGVIRGTAENHGGRANTLTSPNPKAQADLLVRAYRQAGIDPSTVTY 3641
Cdd:PRK07910   229 RPFDKDRDGFVFGEGGALMVIETEEHAKARGANILARIMGASITSDGFHMVAPDPNGERAGHAMTRAIELAGLTPGDIDH 308
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3642 IEAHGTGTELGDPIEINGLKAAfkelsnmrgesqpdVPDHRCGIGSVKSNIGHLELAAGISGLIKVLLQMKHKTLVKSLH 3721
Cdd:PRK07910   309 VNAHATGTSVGDVAEGKAINNA--------------LGGHRPAVYAPKSALGHSVGAVGAVESILTVLALRDGVIPPTLN 374
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1776025254 3722 CETLNPYLQLTdspfyIVQEKqewksvtdcdgnelPRRAGI-----SSFGIGGVNAHIVIEEY 3779
Cdd:PRK07910   375 LENLDPEIDLD-----VVAGE--------------PRPGNYryainNSFGFGGHNVALAFGRY 418
Ac_CoA_lig_AcsA TIGR02188
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ...
1160-1641 3.31e-18

acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called acetyl-CoA synthetase and acetyl-activating enzyme. It catalyzes the reaction ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA and belongs to the family of AMP-binding enzymes described by pfam00501.


Pssm-ID: 274022 [Multi-domain]  Cd Length: 626  Bit Score: 92.31  E-value: 3.31e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1160 EQQAKKTPDRAAVSYEG------QTLTYRELDERSTQLAIYLQAHGVGP-DRLAgIYVDRSLDMLVGLLAILKAGGAYVP 1232
Cdd:TIGR02188   64 DRHLEARPDKVAIIWEGdepgevRKITYRELHREVCRFANVLKSLGVKKgDRVA-IYMPMIPEAAIAMLACARIGAIHSV 142
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1233 LDPSYPAERLEYMLEDSEVFITLTTSElvntlSWNG---------VTTALL--------------------------DQD 1277
Cdd:TIGR02188  143 VFGGFSAEALADRINDAGAKLVITADE-----GLRGgkviplkaiVDEALEkcpvsvehvlvvrrtgnpvvpwvegrDVW 217
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1278 WDEIAQTASDrKVLTRTVTPENLAYVIYTSGSTGKPKGVMipHKaltnflvsmgetpglTAEDKMLAVTT--YCFDIAAL 1355
Cdd:TIGR02188  218 WHDLMAKASA-YCEPEPMDSEDPLFILYTSGSTGKPKGVL--HT---------------TGGYLLYAAMTmkYVFDIKDG 279
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1356 ELFL-----------------PLIKGAHCYIcqTEHTKD----------VEKLKRDIRTIKPTVMqatpatwKMLFYSGw 1408
Cdd:TIGR02188  280 DIFWctadvgwitghsyivygPLANGATTVM--FEGVPTypdpgrfweiIEKHKVTIFYTAPTAI-------RALMRLG- 349
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1409 enEENVKI-------LCG--GEAL-PETLKRYFLDTGSEA-------W------NMFGP----TETTIWSAvqrindecs 1461
Cdd:TIGR02188  350 --DEWVKKhdlsslrLLGsvGEPInPEAWMWYYKVVGKERcpivdtwWqtetggIMITPlpgaTPTKPGSA--------- 418
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1462 ratiGRPIANTQIYITDSQLAPVP-AGVPGELCIAGD--GVAKGYYKKEEltdsRFIDNPFEPGSKLYRTGDMARWLPGG 1538
Cdd:TIGR02188  419 ----TLPFFGIEPAVVDEEGNPVEgPGEGGYLVIKQPwpGMLRTIYGDHE----RFVDTYFSPFPGYYFTGDGARRDKDG 490
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1539 RIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMDNL-----AAYYTAKHANA--SLTARELRHFVKNALP 1611
Cdd:TIGR02188  491 YIWITGRVDDVINVSGHRLGTAEIESALVSHPAVAEAAVVGIPDDIkgqaiYAFVTLKDGYEpdDELRKELRKHVRKEIG 570
                          570       580       590
                   ....*....|....*....|....*....|
gi 1776025254 1612 AYMVPSYFIQLDHMPLTPNGKIDRNSLKNI 1641
Cdd:TIGR02188  571 PIAKPDKIRFVPGLPKTRSGKIMRRLLRKI 600
PLN02614 PLN02614
long-chain acyl-CoA synthetase
1180-1568 3.66e-18

long-chain acyl-CoA synthetase


Pssm-ID: 166255 [Multi-domain]  Cd Length: 666  Bit Score: 92.39  E-value: 3.66e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1180 TYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLEDSEVFITLT--- 1256
Cdd:PLN02614    81 TYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVeek 160
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1257 -TSELVNT-----------LSWNGV---------TTALLDQDWDEIAQTASDRKVLTRTVTPENLAYVIYTSGSTGKPKG 1315
Cdd:PLN02614   161 kISELFKTcpnsteymktvVSFGGVsreqkeeaeTFGLVIYAWDEFLKLGEGKQYDLPIKKKSDICTIMYTSGTTGDPKG 240
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1316 VMIPHKALT-------NFLVSMGETpgLTAEDKMLAV--TTYCFDIAALELFLPLikGAHCYICQtehtKDVEKLKRDIR 1386
Cdd:PLN02614   241 VMISNESIVtliagviRLLKSANAA--LTVKDVYLSYlpLAHIFDRVIEECFIQH--GAAIGFWR----GDVKLLIEDLG 312
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1387 TIKPTVMQATPATWKMLfYSGWENE-------------------------------------------------ENVKIL 1417
Cdd:PLN02614   313 ELKPTIFCAVPRVLDRV-YSGLQKKlsdggflkkfvfdsafsykfgnmkkgqshveasplcdklvfnkvkqglgGNVRII 391
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1418 CGGEALPETLKRYFLDTGS--EAWNMFGPTETTIWSAVQRINDECSRATIGRPIANTQIyitdsQLAPVP-------AGV 1488
Cdd:PLN02614   392 LSGAAPLASHVESFLRVVAccHVLQGYGLTESCAGTFVSLPDELDMLGTVGPPVPNVDI-----RLESVPemeydalAST 466
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1489 P-GELCIAGDGVAKGYYKKEELTDSRFIDNpfepgskLYRTGDMARWLPGGRIEYIGRIDNQVKI-RGFRIELGDIESRL 1566
Cdd:PLN02614   467 PrGEICIRGKTLFSGYYKREDLTKEVLIDG-------WLHTGDVGEWQPNGSMKIIDRKKNIFKLsQGEYVAVENIENIY 539

                   ..
gi 1776025254 1567 SE 1568
Cdd:PLN02614   540 GE 541
PRK06814 PRK06814
acyl-[ACP]--phospholipid O-acyltransferase;
185-549 4.74e-18

acyl-[ACP]--phospholipid O-acyltransferase;


Pssm-ID: 235865 [Multi-domain]  Cd Length: 1140  Bit Score: 92.72  E-value: 4.74e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  185 SPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDH----VGG--IGMLHLRDVYLgcqei 258
Cdd:PRK06814   791 DPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPEDKVFNALPVFHsfglTGGlvLPLLSGVKVFL----- 865
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  259 nvssetiLMEPLkwldwidHYRA--SVTWAPN--FAFGlvTDF--------AEeikdrKWDLSSMRYMLNGGEAMVA--- 323
Cdd:PRK06814   866 -------YPSPL-------HYRIipELIYDTNatILFG--TDTflngyaryAH-----PYDFRSLRYVFAGAEKVKEetr 924
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  324 -----KVGRRILELlephglpadairpaWGMSETSSGVIFSHE-FTRAGTsdddhfveIGSPIPGFSMRIvnDHNELVEE 397
Cdd:PRK06814   925 qtwmeKFGIRILEG--------------YGVTETAPVIALNTPmHNKAGT--------VGRLLPGIEYRL--EPVPGIDE 980
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  398 GeiGRFQVSGLSVTSGYYqRPDlNESVF--TEDGWFETGDL------GFlrngrLTITGRTKDAIIINGinyyshaiE-- 467
Cdd:PRK06814   981 G--GRLFVRGPNVMLGYL-RAE-NPGVLepPADGWYDTGDIvtideeGF-----ITIKGRAKRFAKIAG--------Emi 1043
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  468 --SAVEEL-SEIETSYTAACAVRLGQNSTDQLaIFFVTSAKLNDEqmsqllrNIQSHVSQvIGVtPEYLLP---VQKEEI 541
Cdd:PRK06814  1044 slAAVEELaAELWPDALHAAVSIPDARKGERI-ILLTTASDATRA-------AFLAHAKA-AGA-SELMVPaeiITIDEI 1113

                   ....*...
gi 1776025254  542 PKTAIGKI 549
Cdd:PRK06814  1114 PLLGTGKI 1121
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
172-671 4.80e-18

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 92.80  E-value: 4.80e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  172 LLSAEADTDWHQSSPEDLALLLLTSGSTGTPKAVMLNHRNImsmVKGIIQMQ---GFTREDI-------TFN------WM 235
Cdd:PRK10252   583 PLAPQGAAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAI---VNRLLWMQnhyPLTADDVvlqktpcSFDvsvwefFW 659
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  236 PFdhvggigmlhlrdvylgcqeinVSSETILM-------EPLKWLDWIDHYRASVT-WAPNFAFGLVTDFAEEIKDRKwd 307
Cdd:PRK10252   660 PF----------------------IAGAKLVMaepeahrDPLAMQQFFAEYGVTTThFVPSMLAAFVASLTPEGARQS-- 715
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  308 LSSMRYMLNGGEAMVAKVGRRILELL--EPHGL--PADAI-----RPAWGmsetssgvifshEFTRAGTSDDdhfVEIGS 378
Cdd:PRK10252   716 CASLRQVFCSGEALPADLCREWQQLTgaPLHNLygPTEAAvdvswYPAFG------------EELAAVRGSS---VPIGY 780
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  379 PIPGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGYYQRPDLNESVFTEDGW------FETGDLG-FLRNGRLTITGRTK 451
Cdd:PRK10252   781 PVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFapgermYRTGDVArWLDDGAVEYLGRSD 860
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  452 DAIIINGINYYSHAIESAVEELSEIETSYTAACAVRLGQNSTD---QLaIFFVTSAKLNDEQMSQLlrniQSHVSQVIgv 528
Cdd:PRK10252   861 DQLKIRGQRIELGEIDRAMQALPDVEQAVTHACVINQAAATGGdarQL-VGYLVSQSGLPLDTSAL----QAQLRERL-- 933
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  529 tPEYLLP---VQKEEIPKTAIGKIQRTQLKtsfengefdhllhKPNrmndavqdeemQQADHVKRVREEIQEHLLTCLTE 605
Cdd:PRK10252   934 -PPHMVPvvlLQLDQLPLSANGKLDRKALP-------------LPE-----------LKAQVPGRAPKTGTETIIAAAFS 988
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1776025254  606 ELhVSRDWVEPNANIQSLGVNSIKMMKLIRSIEKNYHIKLTAREIHQYPTIERLASYLSEHEDLSS 671
Cdd:PRK10252   989 SL-LGCDVVDADADFFALGGHSLLAMKLAAQLSRQFARQVTPGQVMVASTVAKLATLLDAEEDESR 1053
PRK06060 PRK06060
p-hydroxybenzoic acid--AMP ligase FadD22;
34-608 5.28e-18

p-hydroxybenzoic acid--AMP ligase FadD22;


Pssm-ID: 180374 [Multi-domain]  Cd Length: 705  Bit Score: 92.02  E-value: 5.28e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254   34 VLYRTAAELGDTKGIIYLQPDGTevyqSYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNSQLLPAFWGCVLTGVVpAP 113
Cdd:PRK06060     9 LLAEQASEAGWYDRPAFYAADVV----THGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVM-AF 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  114 LAVPPTYAESSSgTQKLKDAWTLLDKPAVITDRGMHQEMLDWAkeqglegfraiiveDLLSAEA---DTDWHQSSPEDLA 190
Cdd:PRK06060    84 LANPELHRDDHA-LAARNTEPALVVTSDALRDRFQPSRVAEAA--------------ELMSEAArvaPGGYEPMGGDALA 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  191 LLLLTSGSTGTPKAVMLNHRNIMSMVKGII-QMQGFTREDITFN--------------WMPFdHVGGIGMLHlrdvylgc 255
Cdd:PRK06060   149 YATYTSGTTGPPKAAIHRHADPLTFVDAMCrKALRLTPEDTGLCsarmyfayglgnsvWFPL-ATGGSAVIN-------- 219
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  256 qEINVSSETILMeplkwldwidhyrASVTWAPNFAFGLVTDFAEEIKDRKWD-LSSMRYMLNGGEAMVAKVGRRILELLe 334
Cdd:PRK06060   220 -SAPVTPEAAAI-------------LSARFGPSVLYGVPNFFARVIDSCSPDsFRSLRCVVSAGEALELGLAERLMEFF- 284
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  335 pHGLPadaIRPAWGMSETSSGVIfsheftrAGTSDDDHFVEIGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGY 414
Cdd:PRK06060   285 -GGIP---ILDGIGSTEVGQTFV-------SNRVDEWRLGTLGRVLPPYEIRVVAPDGTTAGPGVEGDLWVRGPAIAKGY 353
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  415 YQRPDlneSVFTEDGWFETGD-LGFLRNGRLTITGRTKDAIIINGINYYSHAIESAVEElsEIETSYTAACAVRLGQNST 493
Cdd:PRK06060   354 WNRPD---SPVANEGWLDTRDrVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIE--DEAVAEAAVVAVRESTGAS 428
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  494 DQLAIFFVTSAKLNDEQ-MSQLLRNIQSHVSQVigVTPEYLLPVqkEEIPKTAIGKIQRTQL------KTSFENGEFDHL 566
Cdd:PRK06060   429 TLQAFLVATSGATIDGSvMRDLHRGLLNRLSAF--KVPHRFAVV--DRLPRTPNGKLVRGALrkqsptKPIWELSLTEPG 504
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|..
gi 1776025254  567 LHKPNRMNDAVQDEEMQQADHvkrVREEIQEHLLTCLTEELH 608
Cdd:PRK06060   505 SGVRAQRDDLSASNMTIAGGN---DGGATLRERLVALRQERQ 543
FadD3 cd17638
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ...
1299-1633 7.16e-18

acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.


Pssm-ID: 341293 [Multi-domain]  Cd Length: 330  Bit Score: 88.33  E-value: 7.16e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1299 NLAYVIYTSGSTGKPKGVMIPHKALTNFLVSMGETPGLTAEDKMLAVTTY--CFDIAAlELFLPLIKGAHCYicqTEHTK 1376
Cdd:cd17638      1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFfhTFGYKA-GIVACLLTGATVV---PVAVF 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1377 DVEKLKRDIRTIKPTVMQATPATWKMLFYSGWENEENVKIL----CGGEALPETL-KRYFLDTGSEA-WNMFGPTETTIW 1450
Cdd:cd17638     77 DVDAILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLraavTGAATVPVELvRRMRSELGFETvLTAYGLTEAGVA 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1451 SAVQRINDECSRA-TIGRPIANTQIYITDsqlapvpagvPGELCIAGDGVAKGYYKKEELTdSRFIDnpfepGSKLYRTG 1529
Cdd:cd17638    157 TMCRPGDDAETVAtTCGRACPGFEVRIAD----------DGEVLVRGYNVMQGYLDDPEAT-AEAID-----ADGWLHTG 220
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1530 DMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVV--VAD--MDNLAAYYTAKHANASLTARELRHF 1605
Cdd:cd17638    221 DVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVigVPDerMGEVGKAFVVARPGVTLTEEDVIAW 300
                          330       340
                   ....*....|....*....|....*...
gi 1776025254 1606 VKNALPAYMVPSYFIQLDHMPLTPNGKI 1633
Cdd:cd17638    301 CRERLANYKVPRFVRFLDELPRNASGKV 328
PRK13388 PRK13388
acyl-CoA synthetase; Provisional
1154-1638 8.82e-18

acyl-CoA synthetase; Provisional


Pssm-ID: 237374 [Multi-domain]  Cd Length: 540  Bit Score: 90.86  E-value: 8.82e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1154 TFHELFEQQAkkTPDRAAVSYEGQTLTYRE-LDERSTQ--LAIYLQAHGvGPDRLaGIYVDRSLDMLVGLLAILKAGGAY 1230
Cdd:PRK13388     4 TIAQLLRDRA--GDDTIAVRYGDRTWTWREvLAEAAARaaALIALADPD-RPLHV-GVLLGNTPEMLFWLAAAALGGYVL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1231 VPLDPSYPAERLEYMLEDSEVFITLTTSE---LVNTLSWNGVTtaLLDQDWDEIAQTASDRKVLT--RTVTPENLAYVIY 1305
Cdd:PRK13388    80 VGLNTTRRGAALAADIRRADCQLLVTDAEhrpLLDGLDLPGVR--VLDVDTPAYAELVAAAGALTphREVDAMDPFMLIF 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1306 TSGSTGKPKGVMIPHKALTNFLVSMGETPGLTAEDkmlavTTYCfdiaALELF----------LPLIKGAHcyICQTEHT 1375
Cdd:PRK13388   158 TSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDD-----VCYV----SMPLFhsnavmagwaPAVASGAA--VALPAKF 226
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1376 KDVEKLKrDIRTIKPTVMQ----------ATPATwkmlfysgWENEEN-VKILCGGEALPETLKRYFLDTGSEAWNMFGP 1444
Cdd:PRK13388   227 SASGFLD-DVRRYGATYFNyvgkplayilATPER--------PDDADNpLRVAFGNEASPRDIAEFSRRFGCQVEDGYGS 297
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1445 TETTIwsAVQRiNDECSRATIGRPIANTQIYITDS-QLAPV-----------PAGVPGELC-IAGDGVAKGYYKKEELTD 1511
Cdd:PRK13388   298 SEGAV--IVVR-EPGTPPGSIGRGAPGVAIYNPETlTECAVarfdahgallnADEAIGELVnTAGAGFFEGYYNNPEATA 374
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1512 SRFIDNpfepgskLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMDNlaayYTAK 1591
Cdd:PRK13388   375 ERMRHG-------MYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDE----RVGD 443
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1776025254 1592 HANASLTARELRHFVKNALPAYMV----------PSYFIQLDHMPLTPNGKIDRNSL 1638
Cdd:PRK13388   444 QVMAALVLRDGATFDPDAFAAFLAaqpdlgtkawPRYVRIAADLPSTATNKVLKREL 500
MACS_like_1 cd05974
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
1179-1639 1.50e-17

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341278 [Multi-domain]  Cd Length: 432  Bit Score: 89.16  E-value: 1.50e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1179 LTYRELDERSTQLAIYLQAHGVGPDrlagiyvDRSLDML-------VGLLAILKAGGAYVPldpsypAERLeymledsev 1251
Cdd:cd05974      1 VSFAEMSARSSRVANFLRSIGVGRG-------DRILLMLgnvvelwEAMLAAMKLGAVVIP------ATTL--------- 58
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1252 fitLTTSELVNTLSWNGVTTALLDQDwdeiaqTASDRKVLtrtvtpenlayVIYTSGSTGKPKGVMIPHKALTNFLVSMG 1331
Cdd:cd05974     59 ---LTPDDLRDRVDRGGAVYAAVDEN------THADDPML-----------LYFTSGTTSKPKLVEHTHRSYPVGHLSTM 118
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1332 ETPGLTAEDKMLAVTTYCFDIAALE-LFLPLIKGAhCYICQTEHTKDVEKLKRDIRTIKPTVMQATPATWKMLFYsgwEN 1410
Cdd:cd05974    119 YWIGLKPGDVHWNISSPGWAKHAWScFFAPWNAGA-TVFLFNYARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQ---QD 194
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1411 EENVKI----LCG-GEAL-PETLKRYfldtgSEAWNM-----FGPTETTIW---SAVQRIndecSRATIGRPIANTQIYI 1476
Cdd:cd05974    195 LASFDVklreVVGaGEPLnPEVIEQV-----RRAWGLtirdgYGQTETTALvgnSPGQPV----KAGSMGRPLPGYRVAL 265
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1477 TDSQLAPVPAGvpgELCIA-GD----GVAKGYYKKEELTDSRFidnpfepGSKLYRTGDMARWLPGGRIEYIGRIDNQVK 1551
Cdd:cd05974    266 LDPDGAPATEG---EVALDlGDtrpvGLMKGYAGDPDKTAHAM-------RGGYYRTGDIAMRDEDGYLTYVGRADDVFK 335
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1552 IRGFRIELGDIESRLSEHPGILECVVVADMDNL-----AAY--YTAKHANASLTARELRHFVKNALPAYMVPSYfIQLDH 1624
Cdd:cd05974    336 SSDYRISPFELESVLIEHPAVAEAAVVPSPDPVrlsvpKAFivLRAGYEPSPETALEIFRFSRERLAPYKRIRR-LEFAE 414
                          490
                   ....*....|....*
gi 1776025254 1625 MPLTPNGKIDRNSLK 1639
Cdd:cd05974    415 LPKTISGKIRRVELR 429
FATP_chFAT1_like cd05937
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ...
1174-1639 2.19e-17

Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.


Pssm-ID: 341260 [Multi-domain]  Cd Length: 468  Bit Score: 89.03  E-value: 2.19e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1174 YEGQTLTYRELDERSTQLAIYLQ-AHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAyvpldpsyPAerleymledsevf 1252
Cdd:cd05937      1 FEGKTWTYSETYDLVLRYAHWLHdDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAA--------PA------------- 59
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1253 itlttseLVNtlsWNGVTTALLdqdwdEIAQTASDRKVLtrtVTPENLAYVIYTSGSTGKPKGVMIPHKALTNFLVSMGE 1332
Cdd:cd05937     60 -------FIN---YNLSGDPLI-----HCLKLSGSRFVI---VDPDDPAILIYTSGTTGLPKAAAISWRRTLVTSNLLSH 121
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1333 TPGLTAEDKMLavttYCfdiaalelfLPLIKGAHCYICQTE-----------HTKDVEKLKRDIRTIKPTVMQ------- 1394
Cdd:cd05937    122 DLNLKNGDRTY----TC---------MPLYHGTAAFLGACNclmsggtlalsRKFSASQFWKDVRDSGATIIQyvgelcr 188
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1395 ---ATPAtwkmlfySGWENEENVKILCGGEALPETLKRYFLDTG-SEAWNMFGPTE-----TTIWSAVQRINDECSRATI 1465
Cdd:cd05937    189 yllSTPP-------SPYDRDHKVRVAWGNGLRPDIWERFRERFNvPEIGEFYAATEgvfalTNHNVGDFGAGAIGHHGLI 261
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1466 GRPIANTQIYI------TDSQL--------APVPAGVPGELCIA----GDGVAKGYYKKEELTDSRFIDNPFEPGSKLYR 1527
Cdd:cd05937    262 RRWKFENQVVLvkmdpeTDDPIrdpktgfcVRAPVGEPGEMLGRvpfkNREAFQGYLHNEDATESKLVRDVFRKGDIYFR 341
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1528 TGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVV----VADMDNLAAYYTAKHANASL-----T 1598
Cdd:cd05937    342 TGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVygvkVPGHDGRAGCAAITLEESSAvptefT 421
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|.
gi 1776025254 1599 ARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLK 1639
Cdd:cd05937    422 KSLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLR 462
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
2850-3015 2.26e-17

3-ketoacyl-(acyl-carrier-protein) reductase; Validated


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 84.86  E-value: 2.26e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGLLFAKEIAnRTGrSTIVLTGRSvlSEDKENEL-EALRSIGAEVVYREADVSDQHAVHHLFEEIKERYG 2928
Cdd:PRK05557     7 VALVTGASRGIGRAIAERLA-AQG-ANVVINYAS--SEAGAEALvAEIGALGGKALAVQGDVSDAESVERAVDEAKAEFG 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2929 TLNGIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSGLLHvdeCSKDFPLDF-------FIFFSSVSGCLGNAGQADYAAAN 3001
Cdd:PRK05557    83 GVDILVNNAGITRDNLLMRMKEEDWDRVIDTNLTGVFN---LTKAVARPMmkqrsgrIINISSVVGLMGNPGQANYAASK 159
                          170
                   ....*....|....
gi 1776025254 3002 SFMDAFAeyrRSLA 3015
Cdd:PRK05557   160 AGVIGFT---KSLA 170
PLN02736 PLN02736
long-chain acyl-CoA synthetase
186-452 3.49e-17

long-chain acyl-CoA synthetase


Pssm-ID: 178337 [Multi-domain]  Cd Length: 651  Bit Score: 89.39  E-value: 3.49e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  186 PEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDH----VGGIGMLHLrDVYLGCQEINVs 261
Cdd:PLN02736   220 PEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKFYPSDVHISYLPLAHiyerVNQIVMLHY-GVAVGFYQGDN- 297
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  262 setilmepLKWLDWIDHYR----ASVTWAPNFAFGLVTDFAEE---IKDR---------------------KWDL----- 308
Cdd:PLN02736   298 --------LKLMDDLAALRptifCSVPRLYNRIYDGITNAVKEsggLKERlfnaaynakkqalengknpspMWDRlvfnk 369
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  309 ------SSMRYMLNGGEAMVAKV--------GRRILEllephglpadairpAWGMSETSSgVIfsheftrAGTSDDDHFV 374
Cdd:PLN02736   370 ikaklgGRVRFMSSGASPLSPDVmeflricfGGRVLE--------------GYGMTETSC-VI-------SGMDEGDNLS 427
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  375 -EIGSPIPGFSMRIVN--DHNELVEE-----GEIGrfqVSGLSVTSGYYQRPDLNESVFTEDGWFETGDLG-FLRNGRLT 445
Cdd:PLN02736   428 gHVGSPNPACEVKLVDvpEMNYTSEDqpyprGEIC---VRGPIIFKGYYKDEVQTREVIDEDGWLHTGDIGlWLPGGRLK 504

                   ....*..
gi 1776025254  446 ITGRTKD 452
Cdd:PLN02736   505 IIDRKKN 511
C_NRPS-like cd19537
Condensation family domain with an atypical active site motif; Condensation (C) domains of ...
695-1106 3.51e-17

Condensation family domain with an atypical active site motif; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily typically have a non-canonical conserved SHXXXDX(14)Y motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380460 [Multi-domain]  Cd Length: 395  Bit Score: 87.24  E-value: 3.51e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  695 PLSEVQKGLWTLQKMSPEKSAYHVPLCFKFSSGLHLETLQQAFGLVLNQHPILKHVIQEKDGVP--ILKNEPALSIEIKT 772
Cdd:cd19537      3 ALSPIEREWWHKYQLSTGTSSFNVSFACRLSGDVDRDRLASAWNTVLARHRILRSRYVPRDGGLrrSYSSSPPRVQRVDT 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  773 ENISsmKESDIPAFLrkkvkepyvkENSPLVRVMSfSRSEqehfLLVVIHHLIFDGVSSVTFIHSLFDTYQ-LLLKGQQP 851
Cdd:cd19537     83 LDVW--KEINRPFDL----------EREDPIRVFI-SPDT----LLVVMSHIICDLTTLQLLLREVSAAYNgKLLPPVRR 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  852 EiavspaiYHDFAAWEKNMLAGkdgvkHRTYWQKQLSGtLPNLQLPKVSA-------SSVSEFREDTYTRrlssgfMNQv 924
Cdd:cd19537    146 E-------YLDSTAWSRPASPE-----DLDFWSEYLSG-LPLLNLPRRTSsksyrgtSRVFQLPGSLYRS------LLQ- 205
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  925 rmFAKEHSVN-----VTTVFLScymmlLGRYTGQKEQIVGMPAMVRPEERFDDAIGHFLNMLPIR--SELNPADTFSSFI 997
Cdd:cd19537    206 --FSTSSGITlhqlaLAAVALA-----LQDLSDRTDIVLGAPYLNRTSEEDMETVGLFLEPLPIRirFPSSSDASAADFL 278
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  998 SKLQLTILDGLDHAAyPFPKMVRDLNIPRSQAGSPVFQ---TafFYQNFLQSGSyqsllsryadfFSVDYVE--YIHQEG 1072
Cdd:cd19537    279 RAVRRSSQAALAHAI-PWHQLLEHLGLPPDSPNHPLFDvmvT--FHDDRGVSLA-----------LPIPGVEplYTWAEG 344
                          410       420       430
                   ....*....|....*....|....*....|....*.
gi 1776025254 1073 -EYELVFELWET-EEKMELNIKYNTGLFDAASISAM 1106
Cdd:cd19537    345 aKFPLMFEFTALsDDSLLLRLEYDTDCFSEEEIDRI 380
PRK06501 PRK06501
beta-ketoacyl-ACP synthase;
1904-2183 4.30e-17

beta-ketoacyl-ACP synthase;


Pssm-ID: 235817 [Multi-domain]  Cd Length: 425  Bit Score: 87.38  E-value: 4.30e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1904 LAQSGTIPTMISHKLGLRGPSYFVHANCSSSLIGLHSAYKSLLSAESDYALVGGA--TLHTESNIGYVHQPGLNFSSDGH 1981
Cdd:PRK06501   148 RFQFGSIADRLADRFGTRGLPISLSTACASGATAIQLGVEAIRRGETDRALCIATdgSVSAEALIRFSLLSALSTQNDPP 227
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1982 IKA---FDASADGMIGGEGVAVVLLKKAADAVKDGDHIYALLRGIGvnnDGADkvGFY----APSVKGQADVVQQVMNQT 2054
Cdd:PRK06501   228 EKAskpFSKDRDGFVMAEGAGALVLESLESAVARGAKILGIVAGCG---EKAD--SFHrtrsSPDGSPAIGAIRAALADA 302
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2055 KIHPESICYVEAHGTGTKLGDPIELAALTNVYRQYTNKTQfcgIGSVKTNIGHLDTAAGlagCIKVVMSLY---HQELAP 2131
Cdd:PRK06501   303 GLTPEQIDYINAHGTSTPENDKMEYLGLSAVFGERLASIP---VSSNKSMIGHTLTAAG---AVEAVFSLLtiqTGRLPP 376
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1776025254 2132 SINYKEPNPntdlaSSPFYVVDQKKtlsREIQThRAALS-SFGLGGTNTHAIF 2183
Cdd:PRK06501   377 TINYDNPDP-----AIPLDVVPNVA---RDARV-TAVLSnSFGFGGQNASLVL 420
PRK13382 PRK13382
bile acid CoA ligase;
153-555 4.36e-17

bile acid CoA ligase;


Pssm-ID: 172019 [Multi-domain]  Cd Length: 537  Bit Score: 88.28  E-value: 4.36e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  153 LDWAKEQGlegfrAIIVEDLLSAEADtDWHQSSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITF 232
Cdd:PRK13382   168 VAWTDEDH-----DLTVEVLIAAHAG-QRPEPTGRKGRVILLTSGTTGTPKGARRSGPGGIGTLKAILDRTPWRAEEPTV 241
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  233 NWMPFDHVGGIGMLHLRdVYLGCqeinvsseTILM----EPLKWLDWIDHYRASVTWAPNFAFGLVTDFAEEIKDRkWDL 308
Cdd:PRK13382   242 IVAPMFHAWGFSQLVLA-ASLAC--------TIVTrrrfDPEATLDLIDRHRATGLAVVPVMFDRIMDLPAEVRNR-YSG 311
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  309 SSMRYMLNGGEAMVAKVgrrILELLEPHGlpaDAIRPAWGMSETSSGVIFSHEFTRAgtsdddHFVEIGSPIPGFSMRIV 388
Cdd:PRK13382   312 RSLRFAAASGSRMRPDV---VIAFMDQFG---DVIYNNYNATEAGMIATATPADLRA------APDTAGRPAEGTEIRIL 379
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  389 N-DHNELvEEGEIGRFQVSGLSVTSGYYQRPDLNesvfTEDGWFETGDLGFL-RNGRLTITGRTKDAIIINGINYYSHAI 466
Cdd:PRK13382   380 DqDFREV-PTGEVGTIFVRNDTQFDGYTSGSTKD----FHDGFMASGDVGYLdENGRLFVVGRDDEMIVSGGENVYPIEV 454
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  467 ESAVEELSEIetsytAACAVR------LGQnstdQLAIFFVTSAKLndeqmSQLLRNIQSHVSQVIGvtpEYLLP---VQ 537
Cdd:PRK13382   455 EKTLATHPDV-----AEAAVIgvddeqYGQ----RLAAFVVLKPGA-----SATPETLKQHVRDNLA---NYKVPrdiVV 517
                          410
                   ....*....|....*...
gi 1776025254  538 KEEIPKTAIGKIQRTQLK 555
Cdd:PRK13382   518 LDELPRGATGKILRRELQ 535
PRK06018 PRK06018
putative acyl-CoA synthetase; Provisional
166-560 4.68e-17

putative acyl-CoA synthetase; Provisional


Pssm-ID: 235673 [Multi-domain]  Cd Length: 542  Bit Score: 88.27  E-value: 4.68e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  166 AIIVEDLLS-AEADTDWHQSSPEDLALLLLTSGSTGTPKAVMLNHR-NIM-SMVKGIIQMQGFTREDITFNWMPFDHVG- 241
Cdd:PRK06018   155 AVAYEEWIAeADGDFAWKTFDENTAAGMCYTSGTTGDPKGVLYSHRsNVLhALMANNGDALGTSAADTMLPVVPLFHANs 234
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  242 -GIGM----LHLRDVYLGCQ-------EInVSSETILME---PLKWLDWIDHYRASvtwapnfafglvtdfaeeikdrKW 306
Cdd:PRK06018   235 wGIAFsapsMGTKLVMPGAKldgasvyEL-LDTEKVTFTagvPTVWLMLLQYMEKE----------------------GL 291
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  307 DLSSMRYMLNGGEAMvakvGRRILELLEPHGLpadAIRPAWGMSETSS-GVIFSHEFTRAGTSDD---DHFVEIGSPIPG 382
Cdd:PRK06018   292 KLPHLKMVVCGGSAM----PRSMIKAFEDMGV---EVRHAWGMTEMSPlGTLAALKPPFSKLPGDarlDVLQKQGYPPFG 364
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  383 FSMRIVNDH-NELVEEGE-IGRFQVSGLSVTSGYYQrpdLNESVFTEDGWFETGDLGFL-RNGRLTITGRTKDaiiingi 459
Cdd:PRK06018   365 VEMKITDDAgKELPWDGKtFGRLKVRGPAVAAAYYR---VDGEILDDDGFFDTGDVATIdAYGYMRITDRSKD------- 434
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  460 nyyshAIESAVEELSEIETSYTA--------ACAVRLGQNSTDQLAIFFVTSAKLNDEQMSQLLRNIQSHVSQviGVTPE 531
Cdd:PRK06018   435 -----VIKSGGEWISSIDLENLAvghpkvaeAAVIGVYHPKWDERPLLIVQLKPGETATREEILKYMDGKIAK--WWMPD 507
                          410       420
                   ....*....|....*....|....*....
gi 1776025254  532 YLLPVqkEEIPKTAIGKIQRTQLKTSFEN 560
Cdd:PRK06018   508 DVAFV--DAIPHTATGKILKTALREQFKD 534
PRK08276 PRK08276
long-chain-fatty-acid--CoA ligase; Validated
51-469 6.72e-17

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236215 [Multi-domain]  Cd Length: 502  Bit Score: 87.65  E-value: 6.72e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254   51 LQPDGTEVyqSYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNSQLLPAFWGCVLTGVVPAPLAVPPTYAESssgtqkl 130
Cdd:PRK08276     5 MAPSGEVV--TYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEI------- 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  131 kdAWTLLDKPA--VITDRGMHQEMLDWAKE------------QGLEGFRAIivEDLLSAEADTDwhqssPEDL---ALLL 193
Cdd:PRK08276    76 --AYIVDDSGAkvLIVSAALADTAAELAAElpagvplllvvaGPVPGFRSY--EEALAAQPDTP-----IADEtagADML 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  194 LTSGSTGTPKAVM--LNHRNI-----MSMVKGIIQMQGFTrEDITFNWMPFDH--VGGIGMLHLRdvyLGcqeinvsSET 264
Cdd:PRK08276   147 YSSGTTGRPKGIKrpLPGLDPdeapgMMLALLGFGMYGGP-DSVYLSPAPLYHtaPLRFGMSALA---LG-------GTV 215
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  265 ILME---PLKWLDWIDHYRASVT-WAPnfafglvTDF------AEEIKDRkWDLSSMRYMLNGGEAMVAKVGRRILELle 334
Cdd:PRK08276   216 VVMEkfdAEEALALIERYRVTHSqLVP-------TMFvrmlklPEEVRAR-YDVSSLRVAIHAAAPCPVEVKRAMIDW-- 285
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  335 phglpadairpaWG--MSETSSG-------VIFSHEF-TRAGTsdddhfveIGSPIPGfSMRIVNDHNELVEEGEIGR-- 402
Cdd:PRK08276   286 ------------WGpiIHEYYASsegggvtVITSEDWlAHPGS--------VGKAVLG-EVRILDEDGNELPPGEIGTvy 344
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1776025254  403 FQVSGLSVTsgYYQRPDLNESVFTEDGWFETGDLGFL-RNGRLTITGRTKDAIIINGINYYSHAIESA 469
Cdd:PRK08276   345 FEMDGYPFE--YHNDPEKTAAARNPHGWVTVGDVGYLdEDGYLYLTDRKSDMIISGGVNIYPQEIENL 410
ACLS-CaiC cd17637
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ...
188-477 7.42e-17

acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341292 [Multi-domain]  Cd Length: 333  Bit Score: 85.40  E-value: 7.42e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  188 DLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDHVGGIGMLhlrdvyLGCQEinVSSETILM 267
Cdd:cd17637      1 DPFVIIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAGLNLA------LATFH--AGGANVVM 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  268 E---PLKWLDWIDHYRASV--TWAPnfafgLVTDFAEEIKDRKWDLSSMRYMLnggeamvakvgrrilellephGLPA-D 341
Cdd:cd17637     73 EkfdPAEALELIEEEKVTLmgSFPP-----ILSNLLDAAEKSGVDLSSLRHVL---------------------GLDApE 126
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  342 AIRP-----------AWGMSETSSGVIFSHEFTRAGTSdddhfveiGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSV 410
Cdd:cd17637    127 TIQRfeettgatfwsLYGQTETSGLVTLSPYRERPGSA--------GRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLV 198
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  411 TSGYYQRPDLNESVFtEDGWFETGDLG-FLRNGRLTITGRT--KDAIIINGINYYSHAIESAVEELSEIE 477
Cdd:cd17637    199 FQGYWNLPELTAYTF-RNGWHHTGDLGrFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIA 267
PRK06164 PRK06164
acyl-CoA synthetase; Validated
183-473 8.44e-17

acyl-CoA synthetase; Validated


Pssm-ID: 235722 [Multi-domain]  Cd Length: 540  Bit Score: 87.49  E-value: 8.44e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  183 QSSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDHVGGIGMLhlrdvyLGCQEINVss 262
Cdd:PRK06164   177 AADPDAGALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGFSTL------LGALAGGA-- 248
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  263 eTILMEPL----KWLDWIDHYRASVTWAPNFAFGLVTDFAeeikDRKWDLSSMRYMlngGEAMVAKVGRRILELLEPHGL 338
Cdd:PRK06164   249 -PLVCEPVfdaaRTARALRRHRVTHTFGNDEMLRRILDTA----GERADFPSARLF---GFASFAPALGELAALARARGV 320
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  339 PadaIRPAWGMSETSSgvIFSheftrAGTSDDDHFVEI---GSPI-PGFSMRIVN-DHNELVEEGEIGRFQVSGLSVTSG 413
Cdd:PRK06164   321 P---LTGLYGSSEVQA--LVA-----LQPATDPVSVRIeggGRPAsPEARVRARDpQDGALLPDGESGEIEIRAPSLMRG 390
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1776025254  414 YYQRPDLNESVFTEDGWFETGDLGFLR-NGRLTITGRTKDAIIINGINYYSHAIESAVEEL 473
Cdd:PRK06164   391 YLDNPDATARALTDDGYFRTGDLGYTRgDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEAL 451
PRK12582 PRK12582
acyl-CoA synthetase; Provisional
1157-1546 9.51e-17

acyl-CoA synthetase; Provisional


Pssm-ID: 237144 [Multi-domain]  Cd Length: 624  Bit Score: 87.79  E-value: 9.51e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1157 ELFEQQAKKTPDRAAVSYEGQT------LTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAY 1230
Cdd:PRK12582    53 HLLAKWAAEAPDRPWLAQREPGhgqwrkVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPA 132
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1231 VPLDPSYPA-----ERLEY----------MLEDSEVFitlttSELVNTLSWNGVTTALLDQDWDEIAQTASDRKVLT--- 1292
Cdd:PRK12582   133 APVSPAYSLmshdhAKLKHlfdlvkprvvFAQSGAPF-----ARALAALDLLDVTVVHVTGPGEGIASIAFADLAATppt 207
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1293 -------RTVTPENLAYVIYTSGSTGKPKGVMIPHKALTNFLVsMGEtpGLTAEDKMLAVTTYcfdiaaLElFLP----- 1360
Cdd:PRK12582   208 aavaaaiAAITPDTVAKYLFTSGSTGMPKAVINTQRMMCANIA-MQE--QLRPREPDPPPPVS------LD-WMPwnhtm 277
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1361 ---------LIKGAHCYIcqtEHTKDV----EKLKRDIRTIKPTVMQATPATWKMLFysgwENEENVKILC--------- 1418
Cdd:PRK12582   278 ggnanfnglLWGGGTLYI---DDGKPLpgmfEETIRNLREISPTVYGNVPAGYAMLA----EAMEKDDALRrsffknlrl 350
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1419 ---GGEALPETL--KRYFL---DTGSEA--WNMFGPTET------TIWsAVQRIndecsrATIGRPIANTQIyitdsQLA 1482
Cdd:PRK12582   351 mayGGATLSDDLyeRMQALavrTTGHRIpfYTGYGATETaptttgTHW-DTERV------GLIGLPLPGVEL-----KLA 418
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1776025254 1483 PVpaGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPFepgsklYRTGDMARWL----PGGRIEYIGRI 1546
Cdd:PRK12582   419 PV--GDKYEVRVKGPNVTPGYHKDPELTAAAFDEEGF------YRLGDAARFVdpddPEKGLIFDGRV 478
PRK08315 PRK08315
AMP-binding domain protein; Validated
195-467 1.02e-16

AMP-binding domain protein; Validated


Pssm-ID: 236236 [Multi-domain]  Cd Length: 559  Bit Score: 87.56  E-value: 1.02e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  195 TSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTRED---ITfnwMPFDHVGGIGMLHLrdvylGCqeINVSSETILM---- 267
Cdd:PRK08315   207 TSGTTGFPKGATLTHRNILNNGYFIGEAMKLTEEDrlcIP---VPLYHCFGMVLGNL-----AC--VTHGATMVYPgegf 276
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  268 EPLKWLDWIDHYRASVtwapnfAFGLVTDFAEEIKDR---KWDLSSMRYMLNGG-----EAMvakvgRRILELLephGLP 339
Cdd:PRK08315   277 DPLATLAAVEEERCTA------LYGVPTMFIAELDHPdfaRFDLSSLRTGIMAGspcpiEVM-----KRVIDKM---HMS 342
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  340 ADAIrpAWGMSETSSGvifsheFTRAGTSDD-DHFVE-IGSPIPGFSMRIVN-DHNELVEEGEIGRFQVSGLSVTSGYYQ 416
Cdd:PRK08315   343 EVTI--AYGMTETSPV------STQTRTDDPlEKRVTtVGRALPHLEVKIVDpETGETVPRGEQGELCTRGYSVMKGYWN 414
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1776025254  417 RPDLNESVFTEDGWFETGDLGFLR-NGRLTITGRTKDAIIINGINYYSHAIE 467
Cdd:PRK08315   415 DPEKTAEAIDADGWMHTGDLAVMDeEGYVNIVGRIKDMIIRGGENIYPREIE 466
FACL_like_5 cd05924
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
1296-1634 1.06e-16

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341248 [Multi-domain]  Cd Length: 364  Bit Score: 85.51  E-value: 1.06e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1296 TPENLaYVIYTSGSTGKPKGVMIPHKALtnFLVSMGETPGLTAEDKMLAVTTYCFDIAALELFL---PLIKGAHCY---- 1368
Cdd:cd05924      2 SADDL-YILYTGGTTGMPKGVMWRQEDI--FRMLMGGADFGTGEFTPSEDAHKAAAAAAGTVMFpapPLMHGTGSWtafg 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1369 -------ICQTEHTKDVEKLKRDIRTIKPTVMQ------ATPATWKMLFYSGWENEENVKILCGGEALPETLKRYFLDTG 1435
Cdd:cd05924     79 gllggqtVVLPDDRFDPEEVWRTIEKHKVTSMTivgdamARPLIDALRDAGPYDLSSLFAISSGGALLSPEVKQGLLELV 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1436 SEA--WNMFGPTETTIWSAVqrINDECSRATIGRPIANTQIYITDSQLAPVPAGVPGELCIAGDG-VAKGYYKKEELTDS 1512
Cdd:cd05924    159 PNItlVDAFGSSETGFTGSG--HSAGSGPETGPFTRANPDTVVLDDDGRVVPPGSGGVGWIARRGhIPLGYYGDEAKTAE 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1513 RF--IDnpfepGSKLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMD-----NLA 1585
Cdd:cd05924    237 TFpeVD-----GVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDerwgqEVV 311
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 1776025254 1586 AYYTAKhANASLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKID 1634
Cdd:cd05924    312 AVVQLR-EGAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGKAD 359
PRK13390 PRK13390
acyl-CoA synthetase; Provisional
1162-1639 1.18e-16

acyl-CoA synthetase; Provisional


Pssm-ID: 139538 [Multi-domain]  Cd Length: 501  Bit Score: 86.99  E-value: 1.18e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1162 QAKKTPDRAAV--SYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPA 1239
Cdd:PRK13390     6 HAQIAPDRPAVivAETGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTA 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1240 ERLEYMLEDSEVFITLTTSELVNTLSWNGVTTALLDQDWDEIAQTASDRKVLTRTVTPENL----AYVIYTSGSTGKPKG 1315
Cdd:PRK13390    86 PEADYIVGDSGARVLVASAALDGLAAKVGADLPLRLSFGGEIDGFGSFEAALAGAGPRLTEqpcgAVMLYSSGTTGFPKG 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1316 VM--IPHKALtnflvsmgETPGltaeDKMLAVTTYCFDIAALELFL---PLIKGAHCYICQTEHTK----------DVEK 1380
Cdd:PRK13390   166 IQpdLPGRDV--------DAPG----DPIVAIARAFYDISESDIYYssaPIYHAAPLRWCSMVHALggtvvlakrfDAQA 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1381 LKRDIRTIKPTVMQATPATW-KML-----FYSGWENEENVKILCGGEALPETLKRYFLD-TGSEAWNMFGPTETTIWSAV 1453
Cdd:PRK13390   234 TLGHVERYRITVTQMVPTMFvRLLkldadVRTRYDVSSLRAVIHAAAPCPVDVKHAMIDwLGPIVYEYYSSTEAHGMTFI 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1454 QRINDECSRATIGRPIANTqIYITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSrfIDNPFEPgskLYRT-GDMA 1532
Cdd:PRK13390   314 DSPDWLAHPGSVGRSVLGD-LHICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAA--AQHPAHP---FWTTvGDLG 387
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1533 RWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMD-------NLAAYYTAKHANASLTARELRHF 1605
Cdd:PRK13390   388 SVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDpemgeqvKAVIQLVEGIRGSDELARELIDY 467
                          490       500       510
                   ....*....|....*....|....*....|....
gi 1776025254 1606 VKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLK 1639
Cdd:PRK13390   468 TRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
PrpE cd05967
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ...
1166-1660 1.42e-16

Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.


Pssm-ID: 341271 [Multi-domain]  Cd Length: 617  Bit Score: 87.37  E-value: 1.42e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1166 TPDRAAVSYEG------QTLTYRELDERSTQLAIYLQAHGVGP-DRLAgIYVDRSLDMLVGLLAILKAG-------GAYV 1231
Cdd:cd05967     64 RGDQIALIYDSpvtgteRTYTYAELLDEVSRLAGVLRKLGVVKgDRVI-IYMPMIPEAAIAMLACARIGaihsvvfGGFA 142
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1232 P---------------LDPSY---PAERLEY--MLEDSevfITLTTSELVNTLSWN------GVTTALLDQDWDEIAQTA 1285
Cdd:cd05967    143 AkelasriddakpkliVTASCgiePGKVVPYkpLLDKA---LELSGHKPHHVLVLNrpqvpaDLTKPGRDLDWSELLAKA 219
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1286 SDRKVLTrtVTPENLAYVIYTSGSTGKPKGVMIP---HKALTNFlvSMGETPGLTAEDKMLAVTtycfDIA-----ALEL 1357
Cdd:cd05967    220 EPVDCVP--VAATDPLYILYTSGTTGKPKGVVRDnggHAVALNW--SMRNIYGIKPGDVWWAAS----DVGwvvghSYIV 291
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1358 FLPLIKGAHC--YICQTEHTKD-------VEKLK--------RDIRTIKptvmQATPATWKMLFY--SGWENeenvkILC 1418
Cdd:cd05967    292 YGPLLHGATTvlYEGKPVGTPDpgafwrvIEKYQvnalftapTAIRAIR----KEDPDGKYIKKYdlSSLRT-----LFL 362
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1419 GGEAL-PET-------LKRYFLDtgsEAWNmfgpTET--TIWSAVQRINDECSRA-TIGRPIANTQIYITDSQLAPVPAG 1487
Cdd:cd05967    363 AGERLdPPTlewaentLGVPVID---HWWQ----TETgwPITANPVGLEPLPIKAgSPGKPVPGYQVQVLDEDGEPVGPN 435
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1488 VPGELCIAGD---GVAKGYYKKEEltdsRFIDNPFEPGSKLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIES 1564
Cdd:cd05967    436 ELGNIVIKLPlppGCLLTLWKNDE----RFKKLYLSKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEE 511
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1565 RLSEHPGILECVVVADMDNLA-----AYYTAKhANASLTA----RELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDR 1635
Cdd:cd05967    512 SVLSHPAVAECAVVGVRDELKgqvplGLVVLK-EGVKITAeeleKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILR 590
                          570       580
                   ....*....|....*....|....*
gi 1776025254 1636 NSLKNIdLSGEQLkqrqTSPKNIQD 1660
Cdd:cd05967    591 RTLRKI-ADGEDY----TIPSTIED 610
PLN02861 PLN02861
long-chain-fatty-acid-CoA ligase
1179-1572 2.08e-16

long-chain-fatty-acid-CoA ligase


Pssm-ID: 178452 [Multi-domain]  Cd Length: 660  Bit Score: 86.82  E-value: 2.08e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1179 LTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLEDSEVFITLT-- 1256
Cdd:PLN02861    78 LTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSIAFVqe 157
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1257 -------------TSELVNTLSWNGVTTALLDQ---------DWDEIAQTASDRKVLTRTvTPENLAYVIYTSGSTGKPK 1314
Cdd:PLN02861   158 skissilsclpkcSSNLKTIVSFGDVSSEQKEEaeelgvscfSWEEFSLMGSLDCELPPK-QKTDICTIMYTSGTTGEPK 236
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1315 GVMIPHKALtnflvsmgeTPGLTAEDKMLAVTtycfDIAALE-----LFLPLikgAHCY------ICQTEHTK------D 1377
Cdd:PLN02861   237 GVILTNRAI---------IAEVLSTDHLLKVT----DRVATEedsyfSYLPL---AHVYdqvietYCISKGASigfwqgD 300
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1378 VEKLKRDIRTIKPTVMQATPATW------------------KMLF---YS--------GWENEE---------------- 1412
Cdd:PLN02861   301 IRYLMEDVQALKPTIFCGVPRVYdriytgimqkissggmlrKKLFdfaYNyklgnlrkGLKQEEasprldrlvfdkikeg 380
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1413 ---NVKILCGGEA-LPETLKRYFLDTG-SEAWNMFGPTETTIWSAVQRINDECSRATIGRPIANTQiyitdSQLAPVP-- 1485
Cdd:PLN02861   381 lggRVRLLLSGAApLPRHVEEFLRVTScSVLSQGYGLTESCGGCFTSIANVFSMVGTVGVPMTTIE-----ARLESVPem 455
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1486 -----AGVP-GELCIAGDGVAKGYYKKEELTDSRFIDNPFEpgsklyrTGDMARWLPGGRIEYIGRIDNQVKI-RGFRIE 1558
Cdd:PLN02861   456 gydalSDVPrGEICLRGNTLFSGYHKRQDLTEEVLIDGWFH-------TGDIGEWQPNGAMKIIDRKKNIFKLsQGEYVA 528
                          490
                   ....*....|....
gi 1776025254 1559 LGDIESRLSEHPGI 1572
Cdd:PLN02861   529 VENLENTYSRCPLI 542
PRK09185 PRK09185
beta-ketoacyl-ACP synthase;
3497-3776 2.23e-16

beta-ketoacyl-ACP synthase;


Pssm-ID: 236398 [Multi-domain]  Cd Length: 392  Bit Score: 84.89  E-value: 2.23e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3497 LNIHGPSEPVETACSSSLVAIHRAVTAMQNGDCEMAIAGGVNTI--LTE------EAhisyskagmLSkDGRCKTFSADA 3568
Cdd:PRK09185   147 LGLSGPAYTISTACSSSAKVFASARRLLEAGLCDAAIVGGVDSLcrLTLngfnslES---------LS-PQPCRPFSANR 216
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3569 NGYVRGEGVGMVMLKKLEDAE---------RDGNHIygvirgtaenhggrantlTSPNPK----AQAdlLVRAYRQAGID 3635
Cdd:PRK09185   217 DGINIGEAAAFFLLEREDDAAvallgvgesSDAHHM------------------SAPHPEglgaILA--MQQALADAGLA 276
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3636 PSTVTYIEAHGTGTELGDPIEINGLKAAFkelsnmrGESQPdvpdhrCgiGSVKSNIGHLELAAGISGLIKVLLQMKHKT 3715
Cdd:PRK09185   277 PADIGYINLHGTATPLNDAMESRAVAAVF-------GDGVP------C--SSTKGLTGHTLGAAGAVEAAICWLALRHGL 341
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1776025254 3716 LVKSLHCETLNPylqlTDSPFYIVQEKQewksvtdcdgnELPRRAGIS-SFGIGGVNAHIVI 3776
Cdd:PRK09185   342 PPHGWNTGQPDP----ALPPLYLVENAQ-----------ALAIRYVLSnSFAFGGNNCSLIF 388
PRK07910 PRK07910
beta-ketoacyl-ACP synthase;
1931-2183 2.37e-16

beta-ketoacyl-ACP synthase;


Pssm-ID: 236129 [Multi-domain]  Cd Length: 418  Bit Score: 85.17  E-value: 2.37e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1931 CSSSLIGLHSAYKSLLSAESDYALVGGATLHTES-NIGYVHQPGLNFSSD-----GHIKAFDASADGMIGGEGVAVVLLK 2004
Cdd:PRK07910   171 CASGSEAIAQAWRQIVLGEADIAICGGVETRIEAvPIAGFAQMRIVMSTNnddpaGACRPFDKDRDGFVFGEGGALMVIE 250
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2005 KAADAVKDGDHIYALLRGIGVNNDGADKVgfyAPSVKGQ--ADVVQQVMNQTKIHPESICYVEAHGTGTKLGDPIELAAL 2082
Cdd:PRK07910   251 TEEHAKARGANILARIMGASITSDGFHMV---APDPNGEraGHAMTRAIELAGLTPGDIDHVNAHATGTSVGDVAEGKAI 327
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2083 TNVYrqytnKTQFCGIGSVKTNIGHLDTAAGLAGCIKVVMSLYHQELAPSINYKEPNPNTDL---ASSPFYvvdqkktls 2159
Cdd:PRK07910   328 NNAL-----GGHRPAVYAPKSALGHSVGAVGAVESILTVLALRDGVIPPTLNLENLDPEIDLdvvAGEPRP--------- 393
                          250       260
                   ....*....|....*....|....*
gi 1776025254 2160 reiQTHRAALS-SFGLGGTNTHAIF 2183
Cdd:PRK07910   394 ---GNYRYAINnSFGFGGHNVALAF 415
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
2850-3015 2.63e-16

beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; This subgroup includes the Escherichai coli K12 BKR, FabG. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet) NAD(P)(H) binding region and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H) binding pattern: TGxxxGxG in classical SDRs. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P) binding motif and an altered active site motif (YXXXN). Fungal type type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P) binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr-151 and Lys-155, and well as Asn-111 (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187594 [Multi-domain]  Cd Length: 240  Bit Score: 81.83  E-value: 2.63e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGllfaKEIANRTGR--STIVLTGRSvlSEDKENELEALRSIGAEVVYREADVSDQHAVHHLFEEIKERY 2927
Cdd:cd05333      2 VALVTGASRGIG----RAIALRLAAegAKVAVTDRS--EEAAAETVEEIKALGGNAAALEADVSDREAVEALVEKVEAEF 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2928 GTLNGIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSGLLHvdeCSKDFPLDF-------FIFFSSVSGCLGNAGQADYAAA 3000
Cdd:cd05333     76 GPVDILVNNAGITRDNLLMRMSEEDWDAVINVNLTGVFN---VTQAVIRAMikrrsgrIINISSVVGLIGNPGQANYAAS 152
                          170
                   ....*....|....*
gi 1776025254 3001 NSFMDAFAeyrRSLA 3015
Cdd:cd05333    153 KAGVIGFT---KSLA 164
PLN02330 PLN02330
4-coumarate--CoA ligase-like 1
29-555 3.34e-16

4-coumarate--CoA ligase-like 1


Pssm-ID: 215189 [Multi-domain]  Cd Length: 546  Bit Score: 85.80  E-value: 3.34e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254   29 ATIPEVLYRTAAELGDTKGIIYLQPDGTEVYQSYRRlwdDGLRIVKGLRQSGLKAKQSVILQLGDNSQllpafWGCVLTG 108
Cdd:PLN02330    28 LTLPDFVLQDAELYADKVAFVEAVTGKAVTYGEVVR---DTRRFAKALRSLGLRKGQVVVVVLPNVAE-----YGIVALG 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  109 VVPAP---LAVPPTYAESssgtqKLKDAWTLLDKPAVITDRgmhqemLDWAKEQGLeGFRAIIV-----------EDLLS 174
Cdd:PLN02330   100 IMAAGgvfSGANPTALES-----EIKKQAEAAGAKLIVTND------TNYGKVKGL-GLPVIVLgeekiegavnwKELLE 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  175 AE---ADTDWHQSSPE-DLALLLLTSGSTGTPKAVMLNHRNIMSMVKGII-----QMQGftrEDITFNWMPFDHVGGIgm 245
Cdd:PLN02330   168 AAdraGDTSDNEEILQtDLCALPFSSGTTGISKGVMLTHRNLVANLCSSLfsvgpEMIG---QVVTLGLIPFFHIYGI-- 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  246 lhlrdVYLGCQEINVSSETILMEPLKWLDWIDHYRA-SVTWAPNFAFGLVTDFAEEIKDrKWDLSSMRymLNGGEAMVAK 324
Cdd:PLN02330   243 -----TGICCATLRNKGKVVVMSRFELRTFLNALITqEVSFAPIVPPIILNLVKNPIVE-EFDLSKLK--LQAIMTAAAP 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  325 VGRRILELLEPHgLPADAIRPAWGMSETSSgVIFSHeftraGTSDDDHFV----EIGSPIPGFSMRIVN-DHNELVEEGE 399
Cdd:PLN02330   315 LAPELLTAFEAK-FPGVQVQEAYGLTEHSC-ITLTH-----GDPEKGHGIakknSVGFILPNLEVKFIDpDTGRSLPKNT 387
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  400 IGRFQVSGLSVTSGYYQRPDLNESVFTEDGWFETGDLGFLRN-GRLTITGRTKDAIIINGINYYSHAIESAVEELSEIET 478
Cdd:PLN02330   388 PGELCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIGYIDDdGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVED 467
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1776025254  479 sytaACAVRLGQNSTDQLAIFFVTSAKLNDEQMSQLLRNIQSHVSQVIGVTPEYLLpvqkEEIPKTAIGKIQRTQLK 555
Cdd:PLN02330   468 ----AAVVPLPDEEAGEIPAACVVINPKAKESEEDILNFVAANVAHYKKVRVVQFV----DSIPKSLSGKIMRRLLK 536
PRK09029 PRK09029
O-succinylbenzoic acid--CoA ligase; Provisional
1163-1578 3.84e-16

O-succinylbenzoic acid--CoA ligase; Provisional


Pssm-ID: 236363 [Multi-domain]  Cd Length: 458  Bit Score: 84.92  E-value: 3.84e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1163 AKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDrlAGI-YVDR-SLDMLVGLLAILKAGGAYVPLDPSYPAE 1240
Cdd:PRK09029    13 AQVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEG--SGVaLRGKnSPETLLAYLALLQCGARVLPLNPQLPQP 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1241 RLEYMLEDSEVFITLTTSELVNtlsWNGVTTALLDQDWDEIAQTASdrkvltrtvtPENLAYVIYTSGSTGKPKGVMIPH 1320
Cdd:PRK09029    91 LLEELLPSLTLDFALVLEGENT---FSALTSLHLQLVEGAHAVAWQ----------PQRLATMTLTSGSTGLPKAAVHTA 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1321 KA----------LTNFlvsmgetpglTAEDKMLavttycfdiaaleLFLP-------------LIKGAhcyicqTEHTKD 1377
Cdd:PRK09029   158 QAhlasaegvlsLMPF----------TAQDSWL-------------LSLPlfhvsgqgivwrwLYAGA------TLVVRD 208
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1378 VEKLKRDIRtikptvmQATPAT------WKMLFYsgWENEENVK-ILCGGEALPETLKRYFLDTGSEAWNMFGPTE--TT 1448
Cdd:PRK09029   209 KQPLEQALA-------GCTHASlvptqlWRLLDN--RSEPLSLKaVLLGGAAIPVELTEQAEQQGIRCWCGYGLTEmaST 279
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1449 IwSAVQriNDecSRATIGRPIANTQIYITDsqlapvpagvpGELCIAGDGVAKGYYKKEELTdsrfidnPFEPGSKLYRT 1528
Cdd:PRK09029   280 V-CAKR--AD--GLAGVGSPLPGREVKLVD-----------GEIWLRGASLALGYWRQGQLV-------PLVNDEGWFAT 336
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1529 GDMARWLpGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVV 1578
Cdd:PRK09029   337 RDRGEWQ-NGELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVV 385
A_NRPS_LgrA-like cd17645
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ...
184-554 3.89e-16

adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.


Pssm-ID: 341300 [Multi-domain]  Cd Length: 440  Bit Score: 84.53  E-value: 3.89e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  184 SSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDHVGGIgmLHLRDVYLGCQEINVSSE 263
Cdd:cd17645    101 TNPDDLAYVIYTSGSTGLPKGVMIEHHNLVNLCEWHRPYFGVTPADKSLVYASFSFDASA--WEIFPHLTAGAALHVVPS 178
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  264 TILMEPLKWLDWIDHYRASVTWAPnfafglvTDFAEEIKdrKWDLSSMRYMLNGGEAMvAKVGRRILELLEPHGLPADAI 343
Cdd:cd17645    179 ERRLDLDALNDYFNQEGITISFLP-------TGAAEQFM--QLDNQSLRVLLTGGDKL-KKIERKGYKLVNNYGPTENTV 248
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  344 rpawgmsetssgVIFSHEFTRAGTSdddhfVEIGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGYYQRPDLNES 423
Cdd:cd17645    249 ------------VATSFEIDKPYAN-----IPIGKPIDNTRVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAE 311
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  424 VFTEDGW------FETGDLG-FLRNGRLTITGRTKDAIIINGINYYSHAIESAVEELSEIETsyTAACAVRLGQNSTdQL 496
Cdd:cd17645    312 KFIVHPFvpgermYRTGDLAkFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIEL--AAVLAKEDADGRK-YL 388
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1776025254  497 AIFFVTSAKLNDEQMSQLLRNiqshvsqvigVTPEYLLP---VQKEEIPKTAIGKIQRTQL 554
Cdd:cd17645    389 VAYVTAPEEIPHEELREWLKN----------DLPDYMIPtyfVHLKALPLTANGKVDRKAL 439
PRK05691 PRK05691
peptide synthase; Validated
184-680 4.31e-16

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 86.76  E-value: 4.31e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  184 SSPEDLALLLLTSGSTGTPKAVMLNHRnimsmvkGIIQMQgftreditFNWMPFdhvggigmLHL--RDVY--LGCQEIN 259
Cdd:PRK05691  3866 SGPDNLAYVIYTSGSTGLPKGVMVEQR-------GMLNNQ--------LSKVPY--------LALseADVIaqTASQSFD 3922
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  260 VSSETILMEPLkwldwidhYRASVTWAPN-FAF---GLVTDFAEE---------------IKDRKWDLSSMRYMLNGGEA 320
Cdd:PRK05691  3923 ISVWQFLAAPL--------FGARVEIVPNaIAHdpqGLLAHVQAQgitvlesvpsliqgmLAEDRQALDGLRWMLPTGEA 3994
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  321 MVAKVGRRILELLephglPADAIRPAWGMSETSSGVIF---SHEFTRAGtsdddhFVEIGSPIPGFSMRIVNDHNELVEE 397
Cdd:PRK05691  3995 MPPELARQWLQRY-----PQIGLVNAYGPAECSDDVAFfrvDLASTRGS------YLPIGSPTDNNRLYLLDEALELVPL 4063
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  398 GEIGRFQVSGLSVTSGYYQRPDLNESVFTEDGW-------FETGDLGFLR-NGRLTITGRTKDAIIINGINYYSHAIESA 469
Cdd:PRK05691  4064 GAVGELCVAGTGVGRGYVGDPLRTALAFVPHPFgapgerlYRTGDLARRRsDGVLEYVGRIDHQVKIRGYRIELGEIEAR 4143
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  470 VEELSEIEtsyTAACAVRLGQNSTDQLAIFFVTSAKLNDeqmSQLLRNIQSHVSQVIgvtPEYLLPVQ---KEEIPKTAI 546
Cdd:PRK05691  4144 LHEQAEVR---EAAVAVQEGVNGKHLVGYLVPHQTVLAQ---GALLERIKQRLRAEL---PDYMVPLHwlwLDRLPLNAN 4214
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  547 GKIQRTQLKtsfengefdhllhkpnrmndAVQDEEMQQADHVKRvREEIQEHLLTCLTEELHVSRdwVEPNANIQSLGVN 626
Cdd:PRK05691  4215 GKLDRKALP--------------------ALDIGQLQSQAYLAP-RNELEQTLATIWADVLKVER--VGVHDNFFELGGH 4271
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1776025254  627 SIKMMKLIRSIEKNYHIKLTAREIHQYPTIERLASYLsehEDLSSSSADKKGTD 680
Cdd:PRK05691  4272 SLLATQIASRVQKALQRNVPLRAMFECSTVEELAEYI---EGLAGSAIDEQKVD 4322
PRK08180 PRK08180
feruloyl-CoA synthase; Reviewed
1157-1534 4.53e-16

feruloyl-CoA synthase; Reviewed


Pssm-ID: 236175 [Multi-domain]  Cd Length: 614  Bit Score: 85.70  E-value: 4.53e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1157 ELFEQQAKKTPDRAAVSYEG-----QTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYV 1231
Cdd:PRK08180    43 DRLVHWAQEAPDRVFLAERGadggwRRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMYAGVPYA 122
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1232 PLDPSYPA-----ERLEYMLE----------DSEVF---ITLTTSELVNTLSWNGVTTALLDQDWDEIAQTASDRKV--L 1291
Cdd:PRK08180   123 PVSPAYSLvsqdfGKLRHVLElltpglvfadDGAAFaraLAAVVPADVEVVAVRGAVPGRAATPFAALLATPPTAAVdaA 202
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1292 TRTVTPENLAYVIYTSGSTGKPKGVMIPHKaltnflvsMgetpgLTAEDKMLAVTTYCFDIAALEL--FLP--------- 1360
Cdd:PRK08180   203 HAAVGPDTIAKFLFTSGSTGLPKAVINTHR--------M-----LCANQQMLAQTFPFLAEEPPVLvdWLPwnhtfggnh 269
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1361 -----LIKGAHCYICQTEHT-KDVEKLKRDIRTIKPTVMQATPATWKML-------------FYSgweneeNVKILC-GG 1420
Cdd:PRK08180   270 nlgivLYNGGTLYIDDGKPTpGGFDETLRNLREISPTVYFNVPKGWEMLvpalerdaalrrrFFS------RLKLLFyAG 343
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1421 EALPETL-------------KRYFLDTGseaWNMfgpTET------TIWSAvqrindecSRA-TIGRPIANTQIYItdsq 1480
Cdd:PRK08180   344 AALSQDVwdrldrvaeatcgERIRMMTG---LGM---TETapsatfTTGPL--------SRAgNIGLPAPGCEVKL---- 405
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1776025254 1481 lapVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPFepgsklYRTGDMARW 1534
Cdd:PRK08180   406 ---VPVGGKLEVRVKGPNVTPGYWRAPELTAEAFDEEGY------YRSGDAVRF 450
KR_1_FAS_SDR_x cd08954
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 1, complex (x) SDRs; ...
4173-4408 4.89e-16

beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 1, complex (x) SDRs; NADP-dependent KR domain of the multidomain type I FAS, a complex SDR family. This subfamily also includes proteins identified as polyketide synthase (PKS), a protein with related modular protein architecture and similar function. It includes the KR domains of mammalian and chicken FAS, and Dictyostelium discoideum putative polyketide synthases (PKSs). These KR domains contain two subdomains, each of which is related to SDR Rossmann fold domains. However, while the C-terminal subdomain has an active site similar to the other SDRs and a NADP-binding capability, the N-terminal SDR-like subdomain is truncated and lacks these functions, serving a supportive structural role. In some instances, such as porcine FAS, an enoyl reductase (a Rossman fold NAD-binding domain of the medium-chain dehydrogenase/reductase, MDR family) module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consists of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthesis uses a dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-ketoacyl reductase (KR), forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-enoyl reductase (ER); this KR and ER are members of the SDR family. This KR subfamily has an active site tetrad with a similar 3D orientation compared to archetypical SDRs, but the active site Lys and Asn residue positions are swapped. The characteristic NADP-binding is typical of the multidomain complex SDRs, with a GGXGXXG NADP binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187657 [Multi-domain]  Cd Length: 452  Bit Score: 84.42  E-value: 4.89e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4173 LLITGGTRGIGLLCARHFAECYGVKKLVLTGREqlPPREEWARfktsntslaekiqAVRELEAKGVQVEMLSLTLSDDAQ 4252
Cdd:cd08954    221 YLITGGSGGLGLEILKWLVKRGAVENIIILSRS--GMKWELEL-------------LIREWKSQNIKFHFVSVDVSDVSS 285
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4253 VEQTLQHI--KRTLGPIGGVIHcagltdmdtLAFIRKT--------SDDIQrVMEPKVSGLTTLYRHV--CNEPLQFFVL 4320
Cdd:cd08954    286 LEKAINLIlnAPKIGPIGGIFH---------LAFVLIDkvleidteSLFIS-VNKAKVMGAINLHNQSikRCWKLDYFVL 355
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4321 FSSVSAIIPelSAGQADYAMANSYMDYFAEaHQKHV--PIISVQWPNWKETGM---GEVTNQAYRESGLFSITNSEGLRF 4395
Cdd:cd08954    356 FSSVSSIRG--SAGQCNYVCANSVLDSLSR-YRKSIglPSIAINWGAIGDVGFvsrNESVDTLLGGQGLLPQSINSCLGT 432
                          250
                   ....*....|....
gi 1776025254 4396 LD-QIVSKMFGPVV 4408
Cdd:cd08954    433 LDlFLQNPSPNLVL 446
MACS_like_3 cd05971
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
186-555 5.11e-16

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341275 [Multi-domain]  Cd Length: 439  Bit Score: 84.41  E-value: 5.11e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  186 PEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFD--HVGGIGMLHLRDVYLGCQEINVSSE 263
Cdd:cd05971     87 SDDPALIIYTSGTTGPPKGALHAHRVLLGHLPGVQFPFNLFPRDGDLYWTPADwaWIGGLLDVLLPSLYFGVPVLAHRMT 166
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  264 TilMEPLKWLDWIDHYRASVTWAPNFAFGLVTDFAEEIKDrkWDLsSMRYMLNGGEAMVAKV---GRRILellephglpA 340
Cdd:cd05971    167 K--FDPKAALDLMSRYGVTTAFLPPTALKMMRQQGEQLKH--AQV-KLRAIATGGESLGEELlgwAREQF---------G 232
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  341 DAIRPAWGMSE-----TSSGVIFShefTRAGTsdddhfveIGSPIPGFSMRIVNDHNELVEEGEIGRFQVS-GLSVTS-G 413
Cdd:cd05971    233 VEVNEFYGQTEcnlviGNCSALFP---IKPGS--------MGKPIPGHRVAIVDDNGTPLPPGEVGEIAVElPDPVAFlG 301
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  414 YYQRPDLNESVFTEDgWFETGDLGFL-RNGRLTITGRTKDAIIINGINYYSHAIESAVEELSEIetsYTAACAVRLGQNS 492
Cdd:cd05971    302 YWNNPSATEKKMAGD-WLLTGDLGRKdSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAV---LMAAVVGIPDPIR 377
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1776025254  493 TDQLAIFFVTSAKLNDEQmsQLLRNIQSHVSQVIGvtpEYLLPVQKE---EIPKTAIGKIQRTQLK 555
Cdd:cd05971    378 GEIVKAFVVLNPGETPSD--ALAREIQELVKTRLA---AHEYPREIEfvnELPRTATGKIRRRELR 438
PRK14691 PRK14691
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
4719-4935 5.29e-16

3-oxoacyl-(acyl carrier protein) synthase II; Provisional


Pssm-ID: 173154 [Multi-domain]  Cd Length: 342  Bit Score: 82.85  E-value: 5.29e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4719 NYLAANLSQFFDVRGPSVVVDTACSSALVGMNMAIQALRGGDIQSAIVGGVSLLSSDASHRLFDRRGILSKH------SS 4792
Cdd:PRK14691    68 NLAAGHVSIKHHFKGPIGAPVTACAAGVQAIGDAVRMIRNNEADVALCGGAEAVIDTVSLAGFAAARALSTHfnstpeKA 147
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4793 FHVFDERADGVVLGEGVGMVMLKTVKQALEDGDTIYAVVKAASVNNDGRTAGPATPNLEAQKEVMKDALFKSGKKPEDIS 4872
Cdd:PRK14691   148 SRPFDTARDGFVMGEGAGLLIIEELEHALARGAKPLAEIVGYGTSADAYHMTSGAEDGDGAYRAMKIALRQAGITPEQVQ 227
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1776025254 4873 YLEANGSGSIVTDLLELKAIQSVYrsGHSSPLSLGSIKPNIGHPLCAEGIASFIKVVLMLKER 4935
Cdd:PRK14691   228 HLNAHATSTPVGDLGEINAIKHLF--GESNALAITSTKSATGHLLGAAGGLETIFTVLALRDQ 288
FUM14_C_NRPS-like cd19545
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ...
695-1121 5.30e-16

Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond forming Fusarium verticillioides FUM14 protein; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) typically catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. However, some C-domains have ester-bond forming activity. This subfamily includes Fusarium verticillioides FUM14 (also known as NRPS8), a bi-domain protein with an ester-bond forming NRPS C-domain, which catalyzes linkages between an aminoacyl/peptidyl-PCP donor and a hydroxyl-containing acceptor. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. FUM14 has an altered active site motif DHTHCD instead of the typical HHxxxD motif seen in other subfamily members. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380467 [Multi-domain]  Cd Length: 395  Bit Score: 83.89  E-value: 5.30e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  695 PLSEVQKGLWTLQKMSPEksAYHVPLCFKFSSGLHLETLQQAFGLVLNQHPILKHVIQEKDGVPilknepALSIEIKTEN 774
Cdd:cd19545      3 PCTPLQEGLMALTARQPG--AYVGQRVFELPPDIDLARLQAAWEQVVQANPILRTRIVQSDSGG------LLQVVVKESP 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  775 ISSMKESDIPAFLRKKVKEPyVKENSPLVRVMSFSRSEQEHFLLVVIHHLIFDGvSSVTFIhslFDTYQLLLKGQQPEIA 854
Cdd:cd19545     75 ISWTESTSLDEYLEEDRAAP-MGLGGPLVRLALVEDPDTERYFVWTIHHALYDG-WSLPLI---LRQVLAAYQGEPVPQP 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  855 VSPAiyhDFaaweKNMLAGKDGVKHRTYWQKQLSGTLPNL--QLPKVSASSVSEfREDTYTRRLSSGFmnqvrmfakEHS 932
Cdd:cd19545    150 PPFS---RF----VKYLRQLDDEAAAEFWRSYLAGLDPAVfpPLPSSRYQPRPD-ATLEHSISLPSSA---------SSG 212
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  933 VNVTTVFLSCYMMLLGRYTGQKEqiVGMPAMV--R--PEERFDDAIGHFLNMLPIRSELNPADTFSSFISKLQLTILDGL 1008
Cdd:cd19545    213 VTLATVLRAAWALVLSRYTGSDD--VVFGVTLsgRnaPVPGIEQIVGPTIATVPLRVRIDPEQSVEDFLQTVQKDLLDMI 290
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1009 DHAAYPFPKMvRDLNIPRSQAGSpvFQTAFFYQ-NFLQSGS------YQSLLSRYADFFSvdyveyihqegeYELVFELW 1081
Cdd:cd19545    291 PFEHTGLQNI-RRLGPDARAACN--FQTLLVVQpALPSSTSeslelgIEEESEDLEDFSS------------YGLTLECQ 355
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|
gi 1776025254 1082 ETEEKMELNIKYNTGLFDAASISAMFDHFVYVTEQAMLNP 1121
Cdd:cd19545    356 LSGSGLRVRARYDSSVISEEQVERLLDQFEHVLQQLASAP 395
CBAL cd05923
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ...
30-554 5.48e-16

4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.


Pssm-ID: 341247 [Multi-domain]  Cd Length: 493  Bit Score: 84.87  E-value: 5.48e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254   30 TIPEVLYRTAAELGDTKGIiyLQPD-GTEVyqSYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNSQLLPAFWGCVLTG 108
Cdd:cd05923      2 TVFEMLRRAASRAPDACAI--ADPArGLRL--TYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLG 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  109 VVPAPLAvpptyaesssgtqklkdaWTLldKPAVITDRGMHQEMLDWAKEQGLEGFRAIIV-----------EDLLSAEA 177
Cdd:cd05923     78 AVPALIN------------------PRL--KAAELAELIERGEMTAAVIAVDAQVMDAIFQsgvrvlalsdlVGLGEPES 137
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  178 DTD---WHQSSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQG--FTREDITFNWMPFDHVGGIGMLHLRDVY 252
Cdd:cd05923    138 AGPlieDPPREPEQPAFVFYTSGTTGLPKGAVIPQRAAESRVLFMSTQAGlrHGRHNVVLGLMPLYHVIGFFAVLVAALA 217
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  253 LGCQEINVSSetilMEPLKWLDWIDHYRASVTWA-PNFAFGLVTdfAEEIKDRKwdLSSMRYMLNGGEAMVAKVgrriLE 331
Cdd:cd05923    218 LDGTYVVVEE----FDPADALKLIEQERVTSLFAtPTHLDALAA--AAEFAGLK--LSSLRHVTFAGATMPDAV----LE 285
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  332 LLEPHgLPADAIRpAWGMSETSSGVIFSHEFT----RAGTSDDDHFVEIGspipGFSMRIVNDhnelVEEGEIgRFQVSG 407
Cdd:cd05923    286 RVNQH-LPGEKVN-IYGTTEAMNSLYMRDARTgtemRPGFFSEVRIVRIG----GSPDEALAN----GEEGEL-IVAAAA 354
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  408 LSVTSGYYQRPDLNESVFtEDGWFETGDLGFLR-NGRLTITGRTKDAIIINGINYYSHAIES------AVEELSEIETSY 480
Cdd:cd05923    355 DAAFTGYLNQPEATAKKL-QDGWYRTGDVGYVDpSGDVRILGRVDDMIISGGENIHPSEIERvlsrhpGVTEVVVIGVAD 433
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  481 T------AACAVR-LGQNSTDQLAIFFVTSAklndeqmsqlLRNIQSHVSQVIgvtpeyllpvqKEEIPKTAIGKIQRTQ 553
Cdd:cd05923    434 ErwgqsvTACVVPrEGTLSADELDQFCRASE----------LADFKRPRRYFF-----------LDELPKNAMNKVLRRQ 492

                   .
gi 1776025254  554 L 554
Cdd:cd05923    493 L 493
PLN02430 PLN02430
long-chain-fatty-acid-CoA ligase
1180-1552 5.96e-16

long-chain-fatty-acid-CoA ligase


Pssm-ID: 178049 [Multi-domain]  Cd Length: 660  Bit Score: 85.25  E-value: 5.96e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1180 TYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLEDSE---VFITLT 1256
Cdd:PLN02430    78 TYKEVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVAMEACAAHSLICVPLYDTLGPGAVDYIVDHAEidfVFVQDK 157
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1257 -TSELVN-----------TLSWNGVTTALLDQ---------DWDEIAQTASDRKVLTRTVTPENLAYVIYTSGSTGKPKG 1315
Cdd:PLN02430   158 kIKELLEpdcksakrlkaIVSFTSVTEEESDKasqigvktySWIDFLHMGKENPSETNPPKPLDICTIMYTSGTSGDPKG 237
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1316 VMIPHKALTNFLVSMgETPGLTAEDKMLAVTTYCFdiaalelFLPLikgAHCYICQTE------------HTKDVEKLKR 1383
Cdd:PLN02430   238 VVLTHEAVATFVRGV-DLFMEQFEDKMTHDDVYLS-------FLPL---AHILDRMIEeyffrkgasvgyYHGDLNALRD 306
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1384 DIRTIKPTVMQATPATW------------------KMLFYS------GWENE----------------ENVK-------- 1415
Cdd:PLN02430   307 DLMELKPTLLAGVPRVFerihegiqkalqelnprrRLIFNAlykyklAWMNRgyshkkaspmadflafRKVKaklggrlr 386
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1416 -ILCGGEALPETLKRyFLDTGSEAWNM--FGPTETTIWSAVQRINDECSRATIGRPIANTQIYITD-SQLAPVPAGVP-- 1489
Cdd:PLN02430   387 lLISGGAPLSTEIEE-FLRVTSCAFVVqgYGLTETLGPTTLGFPDEMCMLGTVGAPAVYNELRLEEvPEMGYDPLGEPpr 465
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1776025254 1490 GELCIAGDGVAKGYYKKEELTDSRFIDNPFEpgsklyrTGDMARWLPGGRIEYIGRIDNQVKI 1552
Cdd:PLN02430   466 GEICVRGKCLFSGYYKNPELTEEVMKDGWFH-------TGDIGEILPNGVLKIIDRKKNLIKL 521
beta-lac_NRPS cd19547
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ...
801-1121 9.44e-16

Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis NocB which exhibits an unusual cyclization to form beta-lactam rings in pro-nocardicin G synthesis; Nocardia uniformis NRPS NocB acts centrally in the biosynthesis of the nocardicin monocyclic beta-lactam antibiotics. Along with another NRPS NocA, it mediates an unusual cyclization to form beta-lactam rings in the synthesis of the beta-lactam-containing pentapeptide pro-nocardicin G. This small subfamily is related to DCL-type Condensation (C) domains, which catalyze condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; domains belonging to this subfamily have an HHHxxxD motif at the active site.


Pssm-ID: 380469 [Multi-domain]  Cd Length: 422  Bit Score: 83.51  E-value: 9.44e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  801 PLVRVMSFSRSEQEHFLLVVIHHLIFDGVSSVTFIHSLFDTYQLLLKGQQPEIA-VSPaiYHDFAAWEKNMLAGKDgvKH 879
Cdd:cd19547    114 PLYRLTLVRLGGGRHYLLWSHHHILLDGWCLSLIWGDVFRVYEELAHGREPQLSpCRP--YRDYVRWIRARTAQSE--ES 189
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  880 RTYWQKQLSGTLPNlqlPKVSASSVSEFREDTYTRRLSSGFMNQVRMFAKEHSVNVTTVFLSCYMMLLGRYTGQKEQIVG 959
Cdd:cd19547    190 ERFWREYLRDLTPS---PFSTAPADREGEFDTVVHEFPEQLTRLVNEAARGYGVTTNAISQAAWSMLLALQTGARDVVHG 266
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  960 MPAMVRPEER--FDDAIGHFLNMLPIRSELNPADTFSSFISKLQLTILDGLDHAAYPFPKmVRDLNIPRSQAGSPVFQTA 1037
Cdd:cd19547    267 LTIAGRPPELegSEHMVGIFINTIPLRIRLDPDQTVTGLLETIHRDLATTAAHGHVPLAQ-IKSWASGERLSGGRVFDNL 345
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1038 FFYQNFLQSgsyqsllSRYADFFSVDYVEYIHQEG-EYE---LVFELweteEKMELNIKYNTGLFDAASISAMFDHFVYV 1113
Cdd:cd19547    346 VAFENYPED-------NLPGDDLSIQIIDLHAQEKtEYPiglIVLPL----QKLAFHFNYDTTHFTRAQVDRFIEVFRLL 414

                   ....*...
gi 1776025254 1114 TEQAMLNP 1121
Cdd:cd19547    415 TEQLCRRP 422
PRK07824 PRK07824
o-succinylbenzoate--CoA ligase;
1298-1638 1.52e-15

o-succinylbenzoate--CoA ligase;


Pssm-ID: 236108 [Multi-domain]  Cd Length: 358  Bit Score: 82.02  E-value: 1.52e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1298 ENLAYVIYTSGSTGKPKGVMIPHKALtnflVSMGET-------PGltaeDKMLAVTTYcfDIAALELFL-PLIKGAHCYI 1369
Cdd:PRK07824    35 DDVALVVATSGTTGTPKGAMLTAAAL----TASADAthdrlggPG----QWLLALPAH--HIAGLQVLVrSVIAGSEPVE 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1370 CQTEHTKDVEKLKRDIRTIKP-------TVMQ-----ATPATWKMLfysgwenEENVKILCGGEALPETLKRYFLDTGSE 1437
Cdd:PRK07824   105 LDVSAGFDPTALPRAVAELGGgrrytslVPMQlakalDDPAATAAL-------AELDAVLVGGGPAPAPVLDAAAAAGIN 177
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1438 AWNMFGPTETtiwsAVQRINDecsratiGRPIANTQIYITDSQLApvpagvpgelcIAGDGVAKGYYKKEEltdsrfiDN 1517
Cdd:PRK07824   178 VVRTYGMSET----SGGCVYD-------GVPLDGVRVRVEDGRIA-----------LGGPTLAKGYRNPVD-------PD 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1518 PF-EPGskLYRTGDMARwLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMDN------LAAYYTA 1590
Cdd:PRK07824   229 PFaEPG--WFRTDDLGA-LDDGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDrlgqrvVAAVVGD 305
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*...
gi 1776025254 1591 KHAnaSLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSL 1638
Cdd:PRK07824   306 GGP--APTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRAL 351
PRK05620 PRK05620
long-chain fatty-acid--CoA ligase;
1295-1640 2.76e-15

long-chain fatty-acid--CoA ligase;


Pssm-ID: 180167 [Multi-domain]  Cd Length: 576  Bit Score: 82.91  E-value: 2.76e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1295 VTPENLAYVI-YTSGSTGKPKGVMIPHKALtnFLVSMGetpgLTAEDKmLAVT---------------TYCFDIAALELF 1358
Cdd:PRK05620   177 ELDETTAAAIcYSTGTTGAPKGVVYSHRSL--YLQSLS----LRTTDS-LAVThgesflccvpiyhvlSWGVPLAAFMSG 249
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1359 LPLIkgahcyicQTEHTKDVEKLKRDIRTIKPTVMQATPATWKMLFYSGWENEEN----VKILCGGEALPETL-----KR 1429
Cdd:PRK05620   250 TPLV--------FPGPDLSAPTLAKIIATAMPRVAHGVPTLWIQLMVHYLKNPPErmslQEIYVGGSAVPPILikaweER 321
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1430 YFLDTgSEAWNMfgpTETTIWSAVQRINDECS-------RATIGR-PIANTQIYITDSQLAPVPAGVPGELCIAGDGVAK 1501
Cdd:PRK05620   322 YGVDV-VHVWGM---TETSPVGTVARPPSGVSgearwayRVSQGRfPASLEYRIVNDGQVMESTDRNEGEIQVRGNWVTA 397
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1502 GYYK----KEELTDSRFIDNPFEPGSKLY------RTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPG 1571
Cdd:PRK05620   398 SYYHspteEGGGAASTFRGEDVEDANDRFtadgwlRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPE 477
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1572 ILECVVVADMDN-----------LAAYYTAKHAnaslTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLKN 1640
Cdd:PRK05620   478 VVECAVIGYPDDkwgerplavtvLAPGIEPTRE----TAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLRQ 553
AcpA COG3433
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ...
1468-1732 2.82e-15

Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442659 [Multi-domain]  Cd Length: 295  Bit Score: 80.18  E-value: 2.82e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1468 PIANTQIYITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPFEPGSKLYRTGDMARWLPGGRIEYIGRID 1547
Cdd:COG3433     21 PPAIVQARALLLIVDLQGYFGGFGGEGGLLGAGLLLRIRLLAAAARAPFIPVPYPAQPGRQADDLRLLLRRGLGPGGGLE 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1548 NQVKIRGFRIELGDIESRLSEHPGILECVVVADM------DNLAAYYTAKHANASLTARELRHFVKNALPAYMVPSYFIQ 1621
Cdd:COG3433    101 RLVQQVVIRAERGEEEELLLVLRAAAVVRVAVLAalrgagVGLLLIVGAVAALDGLAAAAALAALDKVPPDVVAASAVVA 180
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1622 LDHMPLTPNGKIDRNSLKnidLSGEQLKQRQTSPKNIQDTVFT------IWQEVLKTS--DIEWDDGFFDVGGDSLLAVT 1693
Cdd:COG3433    181 LDALLLLALKVVARAAPA---LAAAEALLAAASPAPALETALTeeelraDVAELLGVDpeEIDPDDNLFDLGLDSIRLMQ 257
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1776025254 1694 VADRIKhELSCEFSVTDLFEYSTIKNISQYITEQRMGNA 1732
Cdd:COG3433    258 LVERWR-KAGLDVSFADLAEHPTLAAWWALLAAAQAAAA 295
PLN02246 PLN02246
4-coumarate--CoA ligase
1176-1640 2.92e-15

4-coumarate--CoA ligase


Pssm-ID: 215137 [Multi-domain]  Cd Length: 537  Bit Score: 82.72  E-value: 2.92e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1176 GQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLEDSEVFITL 1255
Cdd:PLN02246    48 GRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLII 127
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1256 TTSELVNTLS----WNGVTTALLDQDWD------EIAQtASDRKVLTRTVTPENLAYVIYTSGSTGKPKGVMIPHKALTN 1325
Cdd:PLN02246   128 TQSCYVDKLKglaeDDGVTVVTIDDPPEgclhfsELTQ-ADENELPEVEISPDDVVALPYSSGTTGLPKGVMLTHKGLVT 206
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1326 FLVSM--GETPGL--TAEDKMLAVTTYcFDIAALE--LFLPLIKGAHCYICQT-EHTKDVEKLKRDIRTIKPTV------ 1392
Cdd:PLN02246   207 SVAQQvdGENPNLyfHSDDVILCVLPM-FHIYSLNsvLLCGLRVGAAILIMPKfEIGALLELIQRHKVTIAPFVppivla 285
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1393 MQATPATWKMLFYSgweneenVKILCGGEA-----LPETLKRYF----LDTG---SEA---WNM---FGPTETTIWSAvq 1454
Cdd:PLN02246   286 IAKSPVVEKYDLSS-------IRMVLSGAAplgkeLEDAFRAKLpnavLGQGygmTEAgpvLAMclaFAKEPFPVKSG-- 356
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1455 rindecSRATIGRpiaNTQIYITDSQL-APVPAGVPGELCIAGDGVAKGYYKKEELTDsrfidnpfepgsklyRTGDMAR 1533
Cdd:PLN02246   357 ------SCGTVVR---NAELKIVDPETgASLPRNQPGEICIRGPQIMKGYLNDPEATA---------------NTIDKDG 412
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1534 WLPGGRIEYI---------GRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMDNLA----AYYTAKHANASLTAR 1600
Cdd:PLN02246   413 WLHTGDIGYIddddelfivDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAgevpVAFVVRSNGSEITED 492
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....
gi 1776025254 1601 ELRHFVKNALPAY----MVpsYFIqlDHMPLTPNGKIDRNSLKN 1640
Cdd:PLN02246   493 EIKQFVAKQVVFYkrihKV--FFV--DSIPKAPSGKILRKDLRA 532
LC_FACS_bac1 cd17641
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ...
1177-1600 3.14e-15

bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341296 [Multi-domain]  Cd Length: 569  Bit Score: 82.86  E-value: 3.14e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1177 QTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLEDSE-VFITL 1255
Cdd:cd17641     10 QEFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGaRVVIA 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1256 TTSELVNTLSWNGVTTALLDQ--DWDE---------------------IAQTASDRKVLTRTVT---PENLAYVIYTSGS 1309
Cdd:cd17641     90 EDEEQVDKLLEIADRIPSVRYviYCDPrgmrkyddprlisfedvvalgRALDRRDPGLYEREVAagkGEDVAVLCTTSGT 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1310 TGKPKGVMIPHKALTNFLVSMGETPGLTAEDKMLAVttycfdiaaleLFLPLI--------KGAHCYICqTEHTKDVEKL 1381
Cdd:cd17641    170 TGKPKLAMLSHGNFLGHCAAYLAADPLGPGDEYVSV-----------LPLPWIgeqmysvgQALVCGFI-VNFPEEPETM 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1382 KRDIRTIKPTVMQATPATW-----------------KMLFY--------------------SGWENEE------------ 1412
Cdd:cd17641    238 MEDLREIGPTFVLLPPRVWegiaadvrarmmdatpfKRFMFelgmklglraldrgkrgrpvSLWLRLAswladallfrpl 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1413 -------NVKI-LCGGEAL-PETLkRYFLDTGSEAWNMFGPTETTIWSAVQRINDECSRaTIGRPIANTQIYITDSqlap 1483
Cdd:cd17641    318 rdrlgfsRLRSaATGGAALgPDTF-RFFHAIGVPLKQLYGQTELAGAYTVHRDGDVDPD-TVGVPFPGTEVRIDEV---- 391
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1484 vpagvpGELCIAGDGVAKGYYKKEELTDSRFIDNPFepgsklYRTGDMARWLPGGRIEYIGRI-DNQVKIRGFRIELGDI 1562
Cdd:cd17641    392 ------GEILVRSPGVFVGYYKNPEATAEDFDEDGW------LHTGDAGYFKENGHLVVIDRAkDVGTTSDGTRFSPQFI 459
                          490       500       510
                   ....*....|....*....|....*....|....*....
gi 1776025254 1563 ESRLSEHPGILECVVV-ADMDNLAAYYTAKHANASLTAR 1600
Cdd:cd17641    460 ENKLKFSPYIAEAVVLgAGRPYLTAFICIDYAIVGKWAE 498
A_NRPS_ACVS-like cd17648
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ...
184-549 3.73e-15

N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.


Pssm-ID: 341303 [Multi-domain]  Cd Length: 453  Bit Score: 81.68  E-value: 3.73e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  184 SSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTRED----ITFNWMPFDHvggigmlHLR---DVYLGCQ 256
Cdd:cd17648     91 TNSTDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSLSERYFGRDNGdeavLFFSNYVFDF-------FVEqmtLALLNGQ 163
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  257 EINVSSETILMEPLKWLDWIDHYRASVTWAPNFAFGLVtDFAEeikdrkwdLSSMRYMLNGGEAMVAKVGRRILELLeph 336
Cdd:cd17648    164 KLVVPPDEMRFDPDRFYAYINREKVTYLSGTPSVLQQY-DLAR--------LPHLKRVDAAGEEFTAPVFEKLRSRF--- 231
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  337 glpADAIRPAWGMSETSsgvIFSHEFTRAGTSDDDHfvEIGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGYYQ 416
Cdd:cd17648    232 ---AGLIINAYGPTETT---VTNHKRFFPGDQRFDK--SLGRPVRNTKCYVLNDAMKRVPVGAVGELYLGGDGVARGYLN 303
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  417 RPDLNESVFTEDGW--------------FETGDLG-FLRNGRLTITGRTKDAIIINGINYyshaiesaveELSEIE---T 478
Cdd:cd17648    304 RPELTAERFLPNPFqteqerargrnarlYKTGDLVrWLPSGELEYLGRNDFQVKIRGQRI----------EPGEVEaalA 373
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  479 SYTA--ACAV-------RLGQNSTDQLAIFFVTSAKLNDEQmsQLLRNIQSHVsqvigvtPEYLLP---VQKEEIPKTAI 546
Cdd:cd17648    374 SYPGvrECAVvakedasQAQSRIQKYLVGYYLPEPGHVPES--DLLSFLRAKL-------PRYMVParlVRLEGIPVTIN 444

                   ...
gi 1776025254  547 GKI 549
Cdd:cd17648    445 GKL 447
PRK05620 PRK05620
long-chain fatty-acid--CoA ligase;
347-564 4.00e-15

long-chain fatty-acid--CoA ligase;


Pssm-ID: 180167 [Multi-domain]  Cd Length: 576  Bit Score: 82.52  E-value: 4.00e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  347 WGMSETS---------SGVifsheftrAGTSDDDHFVEIGSPIPGFSMRIVNDHNELV----EEGEIgrfQVSGLSVTSG 413
Cdd:PRK05620   330 WGMTETSpvgtvarppSGV--------SGEARWAYRVSQGRFPASLEYRIVNDGQVMEstdrNEGEI---QVRGNWVTAS 398
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  414 YYQRP----------------DLNESVFTEDGWFETGDLGFL-RNGRLTITGRTKDAIIINGINYYSHAIESAVeelseI 476
Cdd:PRK05620   399 YYHSPteegggaastfrgedvEDANDRFTADGWLRTGDVGSVtRDGFLTIHDRARDVIRSGGEWIYSAQLENYI-----M 473
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  477 ETSYTAACAV------RLGQNStdqLAIFFVTSAKLNDEQMSQLLRNiqshvsQVIGVTPEYLLP---VQKEEIPKTAIG 547
Cdd:PRK05620   474 AAPEVVECAVigypddKWGERP---LAVTVLAPGIEPTRETAERLRD------QLRDRLPNWMLPeywTFVDEIDKTSVG 544
                          250
                   ....*....|....*..
gi 1776025254  548 KIQRTQLKTSFENGEFD 564
Cdd:PRK05620   545 KFDKKDLRQHLADGDFE 561
FACL_like_1 cd05910
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
187-469 4.15e-15

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341236 [Multi-domain]  Cd Length: 457  Bit Score: 81.74  E-value: 4.15e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  187 EDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPfdhvggigMLHLRDVYLGCQ----EINvSS 262
Cdd:cd05910     85 DEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEVDLATFP--------LFALFGPALGLTsvipDMD-PT 155
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  263 ETILMEPLKWLDWIDHYRASVTWAPNFAFGLVTDFAEEIkDRKwdLSSMRYMLNGGEAMVAKVGRRILELLEPHglpADA 342
Cdd:cd05910    156 RPARADPQKLVGAIRQYGVSIVFGSPALLERVARYCAQH-GIT--LPSLRRVLSAGAPVPIALAARLRKMLSDE---AEI 229
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  343 IRPaWGMSET-SSGVIFSHEF--TRAGTSDDDHFVEIGSPIPGFSMRIVN---------DHNELVEEGEIGRFQVSGLSV 410
Cdd:cd05910    230 LTP-YGATEAlPVSSIGSRELlaTTTAATSGGAGTCVGRPIPGVRVRIIEiddepiaewDDTLELPRGEIGEITVTGPTV 308
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1776025254  411 TSGYYQRPDLNESVFTEDG----WFETGDLGFLRN-GRLTITGRTKDAIIINGINYYSHAIESA 469
Cdd:cd05910    309 TPTYVNRPVATALAKIDDNsegfWHRMGDLGYLDDeGRLWFCGRKAHRVITTGGTLYTEPVERV 372
FATP_FACS cd05940
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ...
1176-1640 4.77e-15

Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341263 [Multi-domain]  Cd Length: 449  Bit Score: 81.25  E-value: 4.77e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1176 GQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGayvpldpsyPAERLEYmledsevfiTL 1255
Cdd:cd05940      1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGA---------VAALINY---------NL 62
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1256 TTSELVNTLswngvttalldqdwdeiaQTASDRKVLTrtvtpeNLAYVIYTSGSTGKPKGVMIPHKALTNFLVSMGETPG 1335
Cdd:cd05940     63 RGESLAHCL------------------NVSSAKHLVV------DAALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGG 118
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1336 LTAEDKmLAVTTYCFDIAALELFLP--LIKGAHCYICQTEHTKDvekLKRDIRTIKPTVMQATPATWKMLFYSGWENEE- 1412
Cdd:cd05940    119 ALPSDV-LYTCLPLYHSTALIVGWSacLASGATLVIRKKFSASN---FWDDIRKYQATIFQYIGELCRYLLNQPPKPTEr 194
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1413 --NVKILCG----GEALPETLKRYFLDTGSEawnMFGPTETTIWSavqrINDECSRATIGR---------PIANTQiYIT 1477
Cdd:cd05940    195 khKVRMIFGnglrPDIWEEFKERFGVPRIAE---FYAATEGNSGF----INFFGKPGAIGRnpsllrkvaPLALVK-YDL 266
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1478 DSQ---------LAPVPAGVPGELC--IAGDGVAKGYYKKEElTDSRFIDNPFEPGSKLYRTGDMARWLPGGRIEYIGRI 1546
Cdd:cd05940    267 ESGepirdaegrCIKVPRGEPGLLIsrINPLEPFDGYTDPAA-TEKKILRDVFKKGDAWFNTGDLMRLDGEGFWYFVDRL 345
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1547 DNQVKIRGFRIELGDIESRLSEHPGILECVV----VADMD---NLAAYYTAKHANASLTAreLRHFVKNALPAYMVPsYF 1619
Cdd:cd05940    346 GDTFRWKGENVSTTEVAAVLGAFPGVEEANVygvqVPGTDgraGMAAIVLQPNEEFDLSA--LAAHLEKNLPGYARP-LF 422
                          490       500
                   ....*....|....*....|..
gi 1776025254 1620 IQL-DHMPLTPNGKIDRNSLKN 1640
Cdd:cd05940    423 LRLqPEMEITGTFKQQKVDLRN 444
PRK07786 PRK07786
long-chain-fatty-acid--CoA ligase; Validated
170-476 5.62e-15

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 169098 [Multi-domain]  Cd Length: 542  Bit Score: 81.75  E-value: 5.62e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  170 EDLLSAEADTDWHQSSPEDL-ALLLLTSGSTGTPKAVMLNHRNIMSM-VKGIIQMQGFTREDITFNWMPFDHVGGIGMLh 247
Cdd:PRK07786   156 EDLLAEAGPAHAPVDIPNDSpALIMYTSGTTGRPKGAVLTHANLTGQaMTCLRTNGADINSDVGFVGVPLFHIAGIGSM- 234
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  248 LRDVYLGcqeinvssETILMEPLK------WLDWIDHYRAS------VTWAPNFAfglvtdfaeEIKDRKWDLSsMRYML 315
Cdd:PRK07786   235 LPGLLLG--------APTVIYPLGafdpgqLLDVLEAEKVTgiflvpAQWQAVCA---------EQQARPRDLA-LRVLS 296
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  316 NGGEAMVAKVGRRILELLephglPADAIRPAWGMSETS--SGVIFSHEFTRAGTSdddhfveIGSPIPGFSMRIVNDHNE 393
Cdd:PRK07786   297 WGAAPASDTLLRQMAATF-----PEAQILAAFGQTEMSpvTCMLLGEDAIRKLGS-------VGKVIPTVAARVVDENMN 364
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  394 LVEEGEIGRFQVSGLSVTSGYYQRPDLNESVFtEDGWFETGDLgfLR---NGRLTITGRTKDAIIINGINYYSHAIESAV 470
Cdd:PRK07786   365 DVPVGEVGEIVYRAPTLMSGYWNNPEATAEAF-AGGWFHSGDL--VRqdeEGYVWVVDRKKDMIISGGENIYCAEVENVL 441

                   ....*.
gi 1776025254  471 EELSEI 476
Cdd:PRK07786   442 ASHPDI 447
PRK04813 PRK04813
D-alanine--poly(phosphoribitol) ligase subunit DltA;
52-554 5.66e-15

D-alanine--poly(phosphoribitol) ligase subunit DltA;


Pssm-ID: 235313 [Multi-domain]  Cd Length: 503  Bit Score: 81.48  E-value: 5.66e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254   52 QPDgTEVYQ------SYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNSQLLPAFWGCVLTG--VVPAPLAVPptyAES 123
Cdd:PRK04813    15 QPD-FPAYDylgeklTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGhaYIPVDVSSP---AER 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  124 ssgTQKLKDAwtlLDKPAVITDRGMHQEMLDwakeqgLEGFRAIIVEDLLSAEADTDW-HQSSPEDLALLLLTSGSTGTP 202
Cdd:PRK04813    91 ---IEMIIEV---AKPSLIIATEELPLEILG------IPVITLDELKDIFATGNPYDFdHAVKGDDNYYIIFTSGTTGKP 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  203 KAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMP--FDhvggigmLHLRDVY----LGCQEINVSSETI-----LMEPLK 271
Cdd:PRK04813   159 KGVQISHDNLVSFTNWMLEDFALPEGPQFLNQAPysFD-------LSVMDLYptlaSGGTLVALPKDMTanfkqLFETLP 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  272 WLDwIDhyrasvTW--APNFA---FgLVTDFAEEikdrkwDLSSMRYMLNGGEAMVAKVGRRILEllephGLPADAIRPA 346
Cdd:PRK04813   232 QLP-IN------VWvsTPSFAdmcL-LDPSFNEE------HLPNLTHFLFCGEELPHKTAKKLLE-----RFPSATIYNT 292
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  347 WGMSETS---SGVIFSHEFTRAGTSdddhfVEIGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGYYQRPDLNES 423
Cdd:PRK04813   293 YGPTEATvavTSIEITDEMLDQYKR-----LPIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAE 367
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  424 VF-TEDGW--FETGDLGFLRNGRLTITGRTKDAIIING--InyyshaiesaveELSEIET-----SYT-AACAVRLGQNS 492
Cdd:PRK04813   368 AFfTFDGQpaYHTGDAGYLEDGLLFYQGRIDFQIKLNGyrI------------ELEEIEQnlrqsSYVeSAVVVPYNKDH 435
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1776025254  493 TDQLAIFFVTSAKLNDEQMSQLLRNIQSHVSQVIgvtPEYLLP---VQKEEIPKTAIGKIQRTQL 554
Cdd:PRK04813   436 KVQYLIAYVVPKEEDFEREFELTKAIKKELKERL---MEYMIPrkfIYRDSLPLTPNGKIDRKAL 497
PRK07788 PRK07788
acyl-CoA synthetase; Validated
191-557 9.82e-15

acyl-CoA synthetase; Validated


Pssm-ID: 236097 [Multi-domain]  Cd Length: 549  Bit Score: 81.13  E-value: 9.82e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  191 LLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDHVGGIGMLHLrDVYLGCQeinvsseTILME-- 268
Cdd:PRK07788   211 IVILTSGTTGTPKGAPRPEPSPLAPLAGLLSRVPFRAGETTLLPAPMFHATGWAHLTL-AMALGST-------VVLRRrf 282
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  269 -PLKWLDWIDHYRASvtwapnfafGLVT---------DFAEEIkDRKWDLSSMRYMLNGGEAMVAKVGRRILELLEP--H 336
Cdd:PRK07788   283 dPEATLEDIAKHKAT---------ALVVvpvmlsrilDLGPEV-LAKYDTSSLKIIFVSGSALSPELATRALEAFGPvlY 352
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  337 GLpadairpaWGMSETSSGVIFS-HEFTRA-GTsdddhfveIGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGY 414
Cdd:PRK07788   353 NL--------YGSTEVAFATIATpEDLAEApGT--------VGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGY 416
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  415 YQRPDLNesvfTEDGWFETGDLGFL-RNGRLTITGRTKDAIIINGINYYSHAIESAVEELSEIETSytAACAVR---LGQ 490
Cdd:PRK07788   417 TDGRDKQ----IIDGLLSSGDVGYFdEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEA--AVIGVDdeeFGQ 490
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1776025254  491 nstdQLAIFFVTS--AKLNDEQMSQLLRNiqsHVSqvigvtpEYLLP---VQKEEIPKTAIGKIQRTQLKTS 557
Cdd:PRK07788   491 ----RLRAFVVKApgAALDEDAIKDYVRD---NLA-------RYKVPrdvVFLDELPRNPTGKVLKRELREM 548
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
2852-3015 9.82e-15

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 77.22  E-value: 9.82e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2852 LITGGAGSLGllfaKEIANRTGRS--TIVLTGRSvlSEDKENEL-EALRSIGAEVVYREADVSDQHAVHHLFEEIKERYG 2928
Cdd:PRK12825    10 LVTGAARGLG----RAIALRLARAgaDVVVHYRS--DEEAAEELvEAVEALGRRAQAVQADVTDKAALEAAVAAAVERFG 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2929 TLNGIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSGLLHVDE------CSKDFplDFFIFFSSVSGCLGNAGQADYAAANS 3002
Cdd:PRK12825    84 RIDILVNNAGIFEDKPLADMSDDEWDEVIDVNLSGVFHLLRavvppmRKQRG--GRIVNISSVAGLPGWPGRSNYAAAKA 161
                          170
                   ....*....|...
gi 1776025254 3003 FMDAFAeyrRSLA 3015
Cdd:PRK12825   162 GLVGLT---KALA 171
PRK09029 PRK09029
O-succinylbenzoic acid--CoA ligase; Provisional
71-449 9.91e-15

O-succinylbenzoic acid--CoA ligase; Provisional


Pssm-ID: 236363 [Multi-domain]  Cd Length: 458  Bit Score: 80.30  E-value: 9.91e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254   71 RIVKGLRQSGLKAKQSVILqLGDNS-QLLPAFWGCVLTGVVPAPLAVPPTYAEsssgTQKLKDAWTLldkpavitdrgmh 149
Cdd:PRK09029    40 QLAAGFAQQGVVEGSGVAL-RGKNSpETLLAYLALLQCGARVLPLNPQLPQPL----LEELLPSLTL------------- 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  150 QEMLDwakeqgLEGFRAIIVEDLLS--AEADTDWHQSSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTR 227
Cdd:PRK09029   102 DFALV------LEGENTFSALTSLHlqLVEGAHAVAWQPQRLATMTLTSGSTGLPKAAVHTAQAHLASAEGVLSLMPFTA 175
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  228 EDitfNWM---PFDHVGGIG----------MLHLRDvylgcqeinvssetilMEPLkwldwiDHYRASVTWA---PNFAF 291
Cdd:PRK09029   176 QD---SWLlslPLFHVSGQGivwrwlyagaTLVVRD----------------KQPL------EQALAGCTHAslvPTQLW 230
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  292 GLVTDFAEEIkdrkwdlsSMRYMLNGGeAMVAkvgrriLEL---LEPHGlpadaIRpAW---GMSETSSGVifshefT-- 363
Cdd:PRK09029   231 RLLDNRSEPL--------SLKAVLLGG-AAIP------VELteqAEQQG-----IR-CWcgyGLTEMASTV------Cak 283
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  364 RAGTSDDdhfveIGSPIPGFSMRIVNDhnelveegEIgrfQVSGLSVTSGYYQ----RPDLNEsvfteDGWFETGDLGFL 439
Cdd:PRK09029   284 RADGLAG-----VGSPLPGREVKLVDG--------EI---WLRGASLALGYWRqgqlVPLVND-----EGWFATRDRGEW 342
                          410
                   ....*....|
gi 1776025254  440 RNGRLTITGR 449
Cdd:PRK09029   343 QNGELTILGR 352
PRK05857 PRK05857
fatty acid--CoA ligase;
178-562 1.23e-14

fatty acid--CoA ligase;


Pssm-ID: 180293 [Multi-domain]  Cd Length: 540  Bit Score: 80.82  E-value: 1.23e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  178 DTDWHQSSP----EDLALLLLTSGSTGTPKAVMLNHRNIMSmVKGIIQMQGFTRED-----ITFNWMPFDHVGGI----- 243
Cdd:PRK05857   156 DAASLAGNAdqgsEDPLAMIFTSGTTGEPKAVLLANRTFFA-VPDILQKEGLNWVTwvvgeTTYSPLPATHIGGLwwilt 234
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  244 GMLHLRDVYLGCQeiNVSSetiLMEPLkwldwIDHYRASVTWAPNfafgLVTDFAEEIKDRKWDLSSMRYMLNGGEAMVA 323
Cdd:PRK05857   235 CLMHGGLCVTGGE--NTTS---LLEIL-----TTNAVATTCLVPT----LLSKLVSELKSANATVPSLRLVGYGGSRAIA 300
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  324 KVGRRIlellephglPADAIRPA--WGMSETSSGVIfsheftrAGTSDDDHFVEI-----GSPIPGFSMRIVNDHN---- 392
Cdd:PRK05857   301 ADVRFI---------EATGVRTAqvYGLSETGCTAL-------CLPTDDGSIVKIeagavGRPYPGVDVYLAATDGigpt 364
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  393 --ELVEEGEIGRFQVSGLSVTSGYYQRPDLNESVFTeDGWFETGDLGFLR-NGRLTITGRTKDAIIINGINYYSHAIESA 469
Cdd:PRK05857   365 apGAGPSASFGTLWIKSPANMLGYWNNPERTAEVLI-DGWVNTGDLLERReDGFFYIKGRSSEMIICGGVNIAPDEVDRI 443
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  470 VEELSEIEtsyTAACAVRLGQNSTDQLAIFFVTSAKLNDEQMSQLLRNIQSHV---SQVIGvTPEYLLPVqkEEIPKTAI 546
Cdd:PRK05857   444 AEGVSGVR---EAACYEIPDEEFGALVGLAVVASAELDESAARALKHTIAARFrreSEPMA-RPSTIVIV--TDIPRTQS 517
                          410
                   ....*....|....*.
gi 1776025254  547 GKIQRTQLKTSFeNGE 562
Cdd:PRK05857   518 GKVMRASLAAAA-TAD 532
PtmA cd17636
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ...
191-486 1.31e-14

long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341291 [Multi-domain]  Cd Length: 331  Bit Score: 78.50  E-value: 1.31e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  191 LLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDHVG----GIGMLHL--RDVYLGCqeinVSSET 264
Cdd:cd17636      4 LAIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLNSGPLFHIGtlmfTLATFHAggTNVFVRR----VDAEE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  265 ILmeplkwlDWIDHYRasVTWApnFAFGLVTD-FAEEIKDRKWDLSSMRymlnggeAMVAKVGRRILellephgLPADAi 343
Cdd:cd17636     80 VL-------ELIEAER--CTHA--FLLPPTIDqIVELNADGLYDLSSLR-------SSPAAPEWNDM-------ATVDT- 133
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  344 rPAW-------GMSETSSGVIFSHeftRAGTSDDDHfveiGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGYYQ 416
Cdd:cd17636    134 -SPWgrkpggyGQTEVMGLATFAA---LGGGAIGGA----GRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWN 205
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1776025254  417 RPDLNeSVFTEDGWFETGDLGfLRN--GRLTITGrTKDAIIINGI-NYYSHAIESAVEELSEIetsytAACAV 486
Cdd:cd17636    206 RPEVN-ARRTRGGWHHTNDLG-RREpdGSLSFVG-PKTRMIKSGAeNIYPAEVERCLRQHPAV-----ADAAV 270
PRK06155 PRK06155
crotonobetaine/carnitine-CoA ligase; Provisional
19-555 1.59e-14

crotonobetaine/carnitine-CoA ligase; Provisional


Pssm-ID: 235719 [Multi-domain]  Cd Length: 542  Bit Score: 80.19  E-value: 1.59e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254   19 EPLHISEKqpaTIPEVLYRTAAELGDTkgiIYLQPDGTevyqsyRRLWDDGLRIVKG----LRQSGLKAKQSVILQLGDN 94
Cdd:PRK06155    14 DPLPPSER---TLPAMLARQAERYPDR---PLLVFGGT------RWTYAEAARAAAAaahaLAAAGVKRGDRVALMCGNR 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254   95 SQLLPAFWGCVLTGVVPAP---------------------LAVPPTYAES----SSGTQKLKDAWTLLDKPAVITDRGmh 149
Cdd:PRK06155    82 IEFLDVFLGCAWLGAIAVPintalrgpqlehilrnsgarlLVVEAALLAAleaaDPGDLPLPAVWLLDAPASVSVPAG-- 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  150 qemldWAkeqglegfraiiVEDLLSAEADTDWHQSSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTRED 229
Cdd:PRK06155   160 -----WS------------TAPLPPLDAPAPAAAVQPGDTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADD 222
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  230 ITFNWMPFDHVGGIGMLHlrdvylgcqEINVSSETILMEPlkwldwidHYRASVTWAPNFAFGLVTDFAeeikdrkwdLS 309
Cdd:PRK06155   223 VLYTTLPLFHTNALNAFF---------QALLAGATYVLEP--------RFSASGFWPAVRRHGATVTYL---------LG 276
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  310 SMRYMLNGGEAMVAKVGRRILELLEPhGLPADAIRP-----------AWGMSETSSGVIFSHEFTRAGTsdddhfveIGS 378
Cdd:PRK06155   277 AMVSILLSQPARESDRAHRVRVALGP-GVPAALHAAfrerfgvdlldGYGSTETNFVIAVTHGSQRPGS--------MGR 347
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  379 PIPGFSMRIVNDHNELVEEGEIGRFQVSG---LSVTSGYYQRPdlNESVFT-EDGWFETGDLGFLR-NGRLTITGRTKDA 453
Cdd:PRK06155   348 LAPGFEARVVDEHDQELPDGEPGELLLRAdepFAFATGYFGMP--EKTVEAwRNLWFHTGDRVVRDaDGWFRFVDRIKDA 425
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  454 IIINGINYYSHAIESAVEELSEIetsytAACAVrlgqnstdqlaiFFVTSAKLNDEQMS-------------QLLRNIQS 520
Cdd:PRK06155   426 IRRRGENISSFEVEQVLLSHPAV-----AAAAV------------FPVPSELGEDEVMAavvlrdgtalepvALVRHCEP 488
                          570       580       590
                   ....*....|....*....|....*....|....*
gi 1776025254  521 HVSQVigVTPEYLLPVQkeEIPKTAIGKIQRTQLK 555
Cdd:PRK06155   489 RLAYF--AVPRYVEFVA--ALPKTENGKVQKFVLR 519
A_NRPS_acs4 cd17654
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ...
184-554 1.60e-14

acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341309 [Multi-domain]  Cd Length: 449  Bit Score: 79.82  E-value: 1.60e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  184 SSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITF--NWMPFDH--VGGIGMLHLrdvylGCQEIN 259
Cdd:cd17654    115 RTDECLAYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFNITSEDILFltSPLTFDPsvVEIFLSLSS-----GATLLI 189
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  260 VSSETILMePLKWLDWID-HYRASVTWAPN---FAFGlvtdfAEEIKDRKWD-LSSMRYMLNGGEAMVAKVgrrILELLE 334
Cdd:cd17654    190 VPTSVKVL-PSKLADILFkRHRITVLQATPtlfRRFG-----SQSIKSTVLSaTSSLRVLALGGEPFPSLV---ILSSWR 260
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  335 PHGLPADAIRpAWGMSETSSGVIFSHeftragTSDDDHFVEIGSPIPGFSMRIVnDHNELVEEGEIGRFQVSGLSVTSGY 414
Cdd:cd17654    261 GKGNRTRIFN-IYGITEVSCWALAYK------VPEEDSPVQLGSPLLGTVIEVR-DQNGSEGTGQVFLGGLNRVCILDDE 332
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  415 YQRPdlnesvftEDGWFETGDLGFLRNGRLTITGRTKDAIIINGINYYSHAIESAVEELSEIEtsytaACAVRLGQNstD 494
Cdd:cd17654    333 VTVP--------KGTMRATGDFVTVKDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVE-----SCAVTLSDQ--Q 397
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  495 QLAIFFVTSAKLNDEQMSQLLRNIQSHvsqvigVTPEYLlpVQKEEIPKTAIGKIQRTQL 554
Cdd:cd17654    398 RLIAFIVGESSSSRIHKELQLTLLSSH------AIPDTF--VQIDKLPLTSHGKVDKSEL 449
PRK14691 PRK14691
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
1914-2140 1.63e-14

3-oxoacyl-(acyl carrier protein) synthase II; Provisional


Pssm-ID: 173154 [Multi-domain]  Cd Length: 342  Bit Score: 78.62  E-value: 1.63e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1914 ISHKLGLRGPSYFVHANCSSSLIGLHSAYKSLLSAESDYALVGGA--TLHTESNIGYVHQPGL----NFSSDGHIKAFDA 1987
Cdd:PRK14691    74 VSIKHHFKGPIGAPVTACAAGVQAIGDAVRMIRNNEADVALCGGAeaVIDTVSLAGFAAARALsthfNSTPEKASRPFDT 153
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1988 SADGMIGGEGVAVVLLKKAADAVKDGDHIYALLRGIGVNNDgADKVGFYAPSVKGQADVVQQVMNQTKIHPESICYVEAH 2067
Cdd:PRK14691   154 ARDGFVMGEGAGLLIIEELEHALARGAKPLAEIVGYGTSAD-AYHMTSGAEDGDGAYRAMKIALRQAGITPEQVQHLNAH 232
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1776025254 2068 GTGTKLGDPIELAALTNVYrqytNKTQFCGIGSVKTNIGHLDTAAGLAGCIKVVMSLYHQELAPSINYKEPNP 2140
Cdd:PRK14691   233 ATSTPVGDLGEINAIKHLF----GESNALAITSTKSATGHLLGAAGGLETIFTVLALRDQIVPATLNLENPDP 301
PRK07008 PRK07008
long-chain-fatty-acid--CoA ligase; Validated
1180-1649 1.77e-14

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235908 [Multi-domain]  Cd Length: 539  Bit Score: 80.14  E-value: 1.77e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1180 TYRELDERSTQLAIYLQAHGVGP-DRLAGI----YvdRSLDMLVGLlailkAGGAYV--PLDPSYPAERLEYML---EDS 1249
Cdd:PRK07008    41 TYRDCERRAKQLAQALAALGVEPgDRVGTLawngY--RHLEAYYGV-----SGSGAVchTINPRLFPEQIAYIVnhaEDR 113
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1250 EVFITLTTSELVNTLS--------WNGVTTA----------LLDQDWDEIAQTASDRKVLTrtvtpENLA-YVIYTSGST 1310
Cdd:PRK07008   114 YVLFDLTFLPLVDALApqcpnvkgWVAMTDAahlpagstplLCYETLVGAQDGDYDWPRFD-----ENQAsSLCYTSGTT 188
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1311 GKPKGVMIPHKA--LTNFLVSMGETPGLTAEDKMLAVT----------TYCFDIAALELFLPlikGAHCyicqtehtkDV 1378
Cdd:PRK07008   189 GNPKGALYSHRStvLHAYGAALPDAMGLSARDAVLPVVpmfhvnawglPYSAPLTGAKLVLP---GPDL---------DG 256
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1379 EKLKRDIRTIKPTVMQATPATWKMLFysGWENEENVKI------LCGGEALPETLKRYFLDT-GSE---AWNM-----FG 1443
Cdd:PRK07008   257 KSLYELIEAERVTFSAGVPTVWLGLL--NHMREAGLRFstlrrtVIGGSACPPAMIRTFEDEyGVEvihAWGMtemspLG 334
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1444 PTETTIWSAVQRINDE--CSRATIGRPIANTQIYITDSQLAPVP-AGVP-GELCIAGDGVAKGYYKKEeltDSRFIDNPF 1519
Cdd:PRK07008   335 TLCKLKWKHSQLPLDEqrKLLEKQGRVIYGVDMKIVGDDGRELPwDGKAfGDLQVRGPWVIDRYFRGD---ASPLVDGWF 411
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1520 EpgsklyrTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILE--CVVVA--DMDNLAAYYTAKHANA 1595
Cdd:PRK07008   412 P-------TGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEaaCIACAhpKWDERPLLVVVKRPGA 484
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1776025254 1596 SLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLKnidlsgEQLK 1649
Cdd:PRK07008   485 EVTREELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLR------EQFR 532
A_NRPS_MycA_like cd05908
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ...
1180-1579 1.81e-14

The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341234 [Multi-domain]  Cd Length: 499  Bit Score: 79.84  E-value: 1.81e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1180 TYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGgaYVPLdPSYPAERLEYMLEDSEVFITLTTSE 1259
Cdd:cd05908     17 SYRHLREEALGYLGALQELGIKPGQEVVFQITHNNKFLYLFWACLLGG--MIAV-PVSIGSNEEHKLKLNKVWNTLKNPY 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1260 LVNTlswngvttallDQDWDEIaqtasdrkvltrtvtPENLAYVIYTSGSTGKPKGVMIPHKALTNFLVSMGETPGLTAE 1339
Cdd:cd05908     94 LITE-----------EEVLCEL---------------ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTK 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1340 DKMLAVTTYCFDIAALELFL-PLIKGAHCYICQTEH--------TKDVEKLKRDI------------RTIKPTVMqatpa 1398
Cdd:cd05908    148 DRILSWMPLTHDMGLIAFHLaPLIAGMNQYLMPTRLfirrpilwLKKASEHKATIvsspnfgykyflKTLKPEKA----- 222
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1399 twkmlfySGWENEENVKILCGGEALPETLKRYFLDTGSE-------AWNMFGPTETTIWS-------------------- 1451
Cdd:cd05908    223 -------NDWDLSSIRMILNGAEPIDYELCHEFLDHMSKyglkrnaILPVYGLAEASVGAslpkaqspfktitlgrrhvt 295
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1452 ------AVQRINDECSR-ATIGRPIANTQIYITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPFepgsk 1524
Cdd:cd05908    296 hgepepEVDKKDSECLTfVEVGKPIDETDIRICDEDNKILPDGYIGHIQIRGKNVTPGYYNNPEATAKVFTDDGW----- 370
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1776025254 1525 lYRTGDMArWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVA 1579
Cdd:cd05908    371 -LKTGDLG-FIRNGRLVITGREKDIIFVNGQNVYPHDIERIAEELEGVELGRVVA 423
PRK07638 PRK07638
acyl-CoA synthetase; Validated
51-562 2.51e-14

acyl-CoA synthetase; Validated


Pssm-ID: 236071 [Multi-domain]  Cd Length: 487  Bit Score: 79.44  E-value: 2.51e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254   51 LQPDGTEVYQSYRRL----WDDGLRIV-KGLRQSGLKAKQSVILqLGDNSQLLPAFWGCVLTGVVPAPLAVPPTYAEsss 125
Cdd:PRK07638    13 LQPNKIAIKENDRVLtykdWFESVCKVaNWLNEKESKNKTIAIL-LENRIEFLQLFAGAAMAGWTCVPLDIKWKQDE--- 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  126 gtqkLKDAWTLLDKPAVITDRGMHQEMLDwakEQGlegfrAIIVED----LLSAEADTDWHQSSPEDLALLL-LTSGSTG 200
Cdd:PRK07638    89 ----LKERLAISNADMIVTERYKLNDLPD---EEG-----RVIEIDewkrMIEKYLPTYAPIENVQNAPFYMgFTSGSTG 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  201 TPKAVMLNHRNimsmvkgiiQMQGFTREDITFNWMPFDHVGGIGML-HLRDVYLGCQEINVSSETILME---PLKWLDWI 276
Cdd:PRK07638   157 KPKAFLRAQQS---------WLHSFDCNVHDFHMKREDSVLIAGTLvHSLFLYGAISTLYVGQTVHLMRkfiPNQVLDKL 227
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  277 DHYRASVTWA-PNFAFGLVTdfAEEIKDrkwdlSSMRYMLNGGEAMVAKVGRriLELLEPHGLPADAirpaWGMSETSSg 355
Cdd:PRK07638   228 ETENISVMYTvPTMLESLYK--ENRVIE-----NKMKIISSGAKWEAEAKEK--IKNIFPYAKLYEF----YGASELSF- 293
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  356 VIFSH--EFTRAGTSdddhfveIGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGYyqrpdLNESVF----TEDG 429
Cdd:PRK07638   294 VTALVdeESERRPNS-------VGRPFHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGY-----IIGGVLarelNADG 361
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  430 WFETGDLGFL-RNGRLTITGRTKDAIIINGINYYSHAIESAVEELSEIET--------SY--TAACAVRLGQNSTDQLAi 498
Cdd:PRK07638   362 WMTVRDVGYEdEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEivvigvpdSYwgEKPVAIIKGSATKQQLK- 440
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1776025254  499 ffvtsaklndeqmSQLLRNIQShvsqvIGVTPEYLLpvqKEEIPKTAIGKIQRTQLKTSFENGE 562
Cdd:PRK07638   441 -------------SFCLQRLSS-----FKIPKEWHF---VDEIPYTNSGKIARMEAKSWIENQE 483
PLN02736 PLN02736
long-chain acyl-CoA synthetase
1297-1587 5.33e-14

long-chain acyl-CoA synthetase


Pssm-ID: 178337 [Multi-domain]  Cd Length: 651  Bit Score: 78.99  E-value: 5.33e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1297 PENLAYVIYTSGSTGKPKGVMIPHKaltNFLVSmgetpgltAEDKMLAVTTYCFDIAALelFLPLikgAHCY----ICQT 1372
Cdd:PLN02736   220 PEDVATICYTSGTTGTPKGVVLTHG---NLIAN--------VAGSSLSTKFYPSDVHIS--YLPL---AHIYervnQIVM 283
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1373 EH--------TKDVEKLKRDIRTIKPTVMQATPATW------------------KMLFYSGW-------ENEEN------ 1413
Cdd:PLN02736   284 LHygvavgfyQGDNLKLMDDLAALRPTIFCSVPRLYnriydgitnavkesgglkERLFNAAYnakkqalENGKNpspmwd 363
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1414 ------VKILCGGE-------ALP------ETLKRYFLDTGSEAWNMfgpTETTIWSAVQRINDECSrATIGRPIANTQI 1474
Cdd:PLN02736   364 rlvfnkIKAKLGGRvrfmssgASPlspdvmEFLRICFGGRVLEGYGM---TETSCVISGMDEGDNLS-GHVGSPNPACEV 439
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1475 YITD-------SQLAPVPAGvpgELCIAGDGVAKGYYKKEELTDSrFIDnpfEPGskLYRTGDMARWLPGGRIEYIGRID 1547
Cdd:PLN02736   440 KLVDvpemnytSEDQPYPRG---EICVRGPIIFKGYYKDEVQTRE-VID---EDG--WLHTGDIGLWLPGGRLKIIDRKK 510
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1776025254 1548 NQVKI-RGFRIELGDIESRLSEHPGILEC-------------VVVADMDNLAAY 1587
Cdd:PLN02736   511 NIFKLaQGEYIAPEKIENVYAKCKFVAQCfvygdslnsslvaVVVVDPEVLKAW 564
PRK08162 PRK08162
acyl-CoA synthetase; Validated
1167-1643 9.21e-14

acyl-CoA synthetase; Validated


Pssm-ID: 236169 [Multi-domain]  Cd Length: 545  Bit Score: 77.68  E-value: 9.21e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1167 PDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGP-DRLAGIYVDRSlDMLVGLLAILKAGGAYVPLDPSYPAERLEYM 1245
Cdd:PRK08162    32 PDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRgDTVAVLLPNIP-AMVEAHFGVPMAGAVLNTLNTRLDAASIAFM 110
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1246 LEDSEVFITLTTSELVNT----LSWNGVTTALL---------------DQDWDEIAQTASDRKVLTRtvtPENLAYVI-- 1304
Cdd:PRK08162   111 LRHGEAKVLIVDTEFAEVareaLALLPGPKPLVidvddpeypggrfigALDYEAFLASGDPDFAWTL---PADEWDAIal 187
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1305 -YTSGSTGKPKGVMIPHK-----ALTNFLV-SMGETPGLTAEDKMLAVTTYCF--DIAALelflpliKGAHcyICQteHT 1375
Cdd:PRK08162   188 nYTSGTTGNPKGVVYHHRgaylnALSNILAwGMPKHPVYLWTLPMFHCNGWCFpwTVAAR-------AGTN--VCL--RK 256
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1376 KDVEKLKRDIRTIK-------PTVMQA---TPATWKMLFysgwenEENVKILCGGEALPETLKRYFLDTGSEAWNMFGPT 1445
Cdd:PRK08162   257 VDPKLIFDLIREHGvthycgaPIVLSAlinAPAEWRAGI------DHPVHAMVAGAAPPAAVIAKMEEIGFDLTHVYGLT 330
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1446 ETTIWSAVQRINDECS------RATIG-----RPIANTQIYITDSQ-LAPVPAG--VPGELCIAGDGVAKGYYKKEELTD 1511
Cdd:PRK08162   331 ETYGPATVCAWQPEWDalpldeRAQLKarqgvRYPLQEGVTVLDPDtMQPVPADgeTIGEIMFRGNIVMKGYLKNPKATE 410
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1512 SRFIDNPFEpgsklyrTGDMARWLPGGrieYIgridnQVKIR--------GFRIELGDIESRLSEHPGILECVVVADMDN 1583
Cdd:PRK08162   411 EAFAGGWFH-------TGDLAVLHPDG---YI-----KIKDRskdiiisgGENISSIEVEDVLYRHPAVLVAAVVAKPDP 475
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1776025254 1584 L-----AAYYTAKhANASLTARELRHFVKNALPAYMVPSYFIqLDHMPLTPNGKIDR-------NSLKNIDL 1643
Cdd:PRK08162   476 KwgevpCAFVELK-DGASATEEEIIAHCREHLAGFKVPKAVV-FGELPKTSTGKIQKfvlreqaKSLKAIDL 545
PRK07769 PRK07769
long-chain-fatty-acid--CoA ligase; Validated
1159-1554 9.51e-14

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 181109 [Multi-domain]  Cd Length: 631  Bit Score: 78.23  E-value: 9.51e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1159 FEQQAKKTPDRAAVSY---------EGQTLTYRELDERSTQLAIYLQAHGVGPDRLAgIYVDRSLDMLVGLLAILKAGGA 1229
Cdd:PRK07769    27 VERWAKVRGDKLAYRFldfsterdgVARDLTWSQFGARNRAVGARLQQVTKPGDRVA-ILAPQNLDYLIAFFGALYAGRI 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1230 YVPL-DPSYP--AERLEYMLEDSEVFITLTTSElvntlSWNGVTTALLDQDWDE----IAQTASDRKVLTRTVTPE---- 1298
Cdd:PRK07769   106 AVPLfDPAEPghVGRLHAVLDDCTPSAILTTTD-----SAEGVRKFFRARPAKErprvIAVDAVPDEVGATWVPPEaned 180
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1299 NLAYVIYTSGSTGKPKGVMIPHKALTNFLVSMGETPGLTAEDKMLAVTTYCFDIAALELFLPLIKGAHCYIcqtehTKDV 1378
Cdd:PRK07769   181 TIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEGQEGDRGVSWLPFFHDMGLITVLLPALLGHYITF-----MSPA 255
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1379 EKLKRDIRTIK---------PTVMQATP------ATWKMLFYSGwENE---ENVK-ILCGGEAL-PETLKRYFldtgsEA 1438
Cdd:PRK07769   256 AFVRRPGRWIRelarkpggtGGTFSAAPnfafehAAARGLPKDG-EPPldlSNVKgLLNGSEPVsPASMRKFN-----EA 329
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1439 WNMFG--PT---------ETTIWSAVQRINDECSRATIGR---------------PIANTQI---YITDSQLA------- 1482
Cdd:PRK07769   330 FAPYGlpPTaikpsygmaEATLFVSTTPMDEEPTVIYVDRdelnagrfvevpadaPNAVAQVsagKVGVSEWAvivdpet 409
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1483 --PVPAGVPGELCIAGDGVAKGYYKKEELTDSRF---IDNPF--------EPGSKLYRTGDMARWLPGGRieYI-GRIDN 1548
Cdd:PRK07769   410 asELPDGQIGEIWLHGNNIGTGYWGKPEETAATFqniLKSRLseshaegaPDDALWVRTGDYGVYFDGEL--YItGRVKD 487

                   ....*.
gi 1776025254 1549 QVKIRG 1554
Cdd:PRK07769   488 LVIIDG 493
AFD_CAR-like cd17632
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ...
145-436 1.05e-13

adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.


Pssm-ID: 341287 [Multi-domain]  Cd Length: 588  Bit Score: 77.88  E-value: 1.05e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  145 DRGMHQEMLDWAKEQGLEGFRAIIVEDLLSAE------ADTDWHQSSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKG 218
Cdd:cd17632    175 EVDAHRAALESARERLAAVGIPVTTLTLIAVRgrdlppAPLFRPEPDDDPLALLIYTSGSTGTPKGAMYTERLVATFWLK 254
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  219 IIQMQGFT-REDITFNWMPFDHVGGIGMLH--------------------LRDVYLgcqeinVSSETILMEPLKWLDWID 277
Cdd:cd17632    255 VSSIQDIRpPASITLNFMPMSHIAGRISLYgtlarggtayfaaasdmstlFDDLAL------VRPTELFLVPRVCDMLFQ 328
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  278 HYRASVTWAPNFAFGLVTDfAEEIKdrkwdlSSMRYMLNGGEAMVAKVGRRIL---------ELLEPHglpadaIRPAWG 348
Cdd:cd17632    329 RYQAELDRRSVAGADAETL-AERVK------AELRERVLGGRLLAAVCGSAPLsaemkafmeSLLDLD------LHDGYG 395
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  349 MSETsSGVIFSHEFTRagtsdddhfveigSPipgfsmriVNDHnELVEEGEIGRFQ-----------VSGLSVTSGYYQR 417
Cdd:cd17632    396 STEA-GAVILDGVIVR-------------PP--------VLDY-KLVDVPELGYFRtdrphprgellVKTDTLFPGYYKR 452
                          330
                   ....*....|....*....
gi 1776025254  418 PDLNESVFTEDGWFETGDL 436
Cdd:cd17632    453 PEVTAEVFDEDGFYRTGDV 471
PRK05952 PRK05952
beta-ketoacyl-ACP synthase;
4741-4939 1.23e-13

beta-ketoacyl-ACP synthase;


Pssm-ID: 235653 [Multi-domain]  Cd Length: 381  Bit Score: 76.24  E-value: 1.23e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4741 ACSSALVGMNMAIQALRGGDIQSAIVGGVSLLSSDASHRLFDRRGILSKHSSFHvFDERADGVVLGEGVGMVMLKTVKQA 4820
Cdd:PRK05952   145 ACATGLWAIAQGVELIQTGQCQRVIAGAVEAPITPLTLAGFQQMGALAKTGAYP-FDRQREGLVLGEGGAILVLESAELA 223
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4821 LEDGDTIYAVVKAASVNNDG-RTAGPATPNLEAQKEVmKDALFKSGKKPEDISYLEANGSGSIVTDLLELKAIQSVYrsG 4899
Cdd:PRK05952   224 QKRGAKIYGQILGFGLTCDAyHMSAPEPDGKSAIAAI-QQCLARSGLTPEDIDYIHAHGTATRLNDQREANLIQALF--P 300
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1776025254 4900 HSSPLSlgSIKPNIGHPLCAEGIASFIKVVLMLKERRFVP 4939
Cdd:PRK05952   301 HRVAVS--STKGATGHTLGASGALGVAFSLLALRHQQLPP 338
CLF cd00832
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ...
3340-3664 1.37e-13

Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic antibiotic-producing polyketide synthases (PKSs) of filamentous bacteria. CLFs have been shown to have decarboxylase activity towards malonyl-acyl carrier protein (ACP). CLFs are similar to other elongation ketosynthase domains, but their active site cysteine is replaced by a conserved glutamine.


Pssm-ID: 238428 [Multi-domain]  Cd Length: 399  Bit Score: 76.25  E-value: 1.37e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3340 PVAIVGISGRFPGAMDIDEFWKNLEEGKDSITEVpkDRWDwREHYGNPdtdvnktdikWGGFIDGvaeFDPLFfGISPRE 3419
Cdd:cd00832      2 RAVVTGIGVVAPNGLGVEEYWKAVLDGRSGLGPI--TRFD-PSGYPAR----------LAGEVPD---FDAAE-HLPGRL 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3420 ADYVDPQQRLLMTYVWKALEDAGCPPQSLSGTGTGIFIGTGNTGYkDLFHRanlpiEGHAATGHmipsvGPNRMSYFLNI 3499
Cdd:cd00832     65 LPQTDRMTRLALAAADWALADAGVDPAALPPYDMGVVTASAAGGF-EFGQR-----ELQKLWSK-----GPRHVSAYQSF 133
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3500 -----------------HGPSEPVETACSSSLVAIHRAVTAMQNGDCEMaIAGGVNTILTEEAHISYSKAGMLSKDGRCK 3562
Cdd:cd00832    134 awfyavntgqisirhgmRGPSGVVVAEQAGGLDALAQARRLVRRGTPLV-VSGGVDSALCPWGWVAQLSSGRLSTSDDPA 212
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3563 T----FSADANGYVRGEGVGMVMLKKLEDAERDGNHIYGVIrgtaenhGGRANTLTSPNPKAQADLLVRAYR----QAGI 3634
Cdd:cd00832    213 RaylpFDAAAAGYVPGEGGAILVLEDAAAARERGARVYGEI-------AGYAATFDPPPGSGRPPGLARAIRlalaDAGL 285
                          330       340       350
                   ....*....|....*....|....*....|
gi 1776025254 3635 DPSTVTYIEAHGTGTELGDPIEINGLKAAF 3664
Cdd:cd00832    286 TPEDVDVVFADAAGVPELDRAEAAALAAVF 315
AFD_CAR-like cd17632
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ...
1178-1631 1.47e-13

adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.


Pssm-ID: 341287 [Multi-domain]  Cd Length: 588  Bit Score: 77.50  E-value: 1.47e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1178 TLTYRELDERSTQLAIYLQA-HGVGP-DRLAGIYVDrSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLEDSE----- 1250
Cdd:cd17632     67 TITYAELWERVGAVAAAHDPeQPVRPgDFVAVLGFT-SPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEprlla 145
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1251 -----------------------VF-----ITLTTSELVNT---LSWNGVTTALLDQDWDeIAQTASDRKVLTRTVTPEN 1299
Cdd:cd17632    146 vsaehldlaveavleggtpprlvVFdhrpeVDAHRAALESArerLAAVGIPVTTLTLIAV-RGRDLPPAPLFRPEPDDDP 224
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1300 LAYVIYTSGSTGKPKGVMIPHKALTNF--LVSMGEtpgltaEDKMLAVTTYCF----DIAA-LELFLPLIKGAHCYICQT 1372
Cdd:cd17632    225 LALLIYTSGSTGTPKGAMYTERLVATFwlKVSSIQ------DIRPPASITLNFmpmsHIAGrISLYGTLARGGTAYFAAA 298
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1373 EhtkDVEKLKRDIRTIKPTVMQATPATWKMLF--YSGWEN------------EENVKI--------------LCGGEALP 1424
Cdd:cd17632    299 S---DMSTLFDDLALVRPTELFLVPRVCDMLFqrYQAELDrrsvagadaetlAERVKAelrervlggrllaaVCGSAPLS 375
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1425 ETLKRyFLDT--GSEAWNMFGPTETtiwSAVQRINdecsraTIGRPiantqiYITDSQLAPVP------AGVP---GELC 1493
Cdd:cd17632    376 AEMKA-FMESllDLDLHDGYGSTEA---GAVILDG------VIVRP------PVLDYKLVDVPelgyfrTDRPhprGELL 439
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1494 IAGDGVAKGYYKKEELTDSRFIDNPFepgsklYRTGD-MARWLPgGRIEYIGRIDNQVKI-RGFRIELGDIESRLSEHPG 1571
Cdd:cd17632    440 VKTDTLFPGYYKRPEVTAEVFDEDGF------YRTGDvMAELGP-DRLVYVDRRNNVLKLsQGEFVTVARLEAVFAASPL 512
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1776025254 1572 I-------------LECVVVADMDNLAAYYTAK-----HANASLTARElrhfvkNALPAYMVPSYFIqLDHMPLTP-NG 1631
Cdd:cd17632    513 VrqifvygnserayLLAVVVPTQDALAGEDTARlraalAESLQRIARE------AGLQSYEIPRDFL-IETEPFTIaNG 584
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
4174-4341 1.49e-13

classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212491 [Multi-domain]  Cd Length: 234  Bit Score: 73.47  E-value: 1.49e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4174 LITGGTRGIGLLCARHFAEcYGVkKLVLTGREqlppreewarfktsntslAEKIQAVRELEAKGVQVEMLSLTLSDDAQV 4253
Cdd:cd05233      2 LVTGASSGIGRAIARRLAR-EGA-KVVLADRN------------------EEALAELAAIEALGGNAVAVQADVSDEEDV 61
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4254 EQTLQHIKRTLGPIGGVIHCAGLTDMDTLAFIrkTSDDIQRVMEPKVSGLTtlyrHVCNEPLQFF--------VLFSSVS 4325
Cdd:cd05233     62 EALVEEALEEFGRLDILVNNAGIARPGPLEEL--TDEDWDRVLDVNLTGVF----LLTRAALPHMkkqgggriVNISSVA 135
                          170
                   ....*....|....*.
gi 1776025254 4326 AIIPelSAGQADYAMA 4341
Cdd:cd05233    136 GLRP--LPGQAAYAAS 149
FACL_like_4 cd05944
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
1297-1639 1.61e-13

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341266 [Multi-domain]  Cd Length: 359  Bit Score: 75.59  E-value: 1.61e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1297 PENLAYVIYTSGSTGKPKgvMIPHKALTnfLVSMGETPGLTA---EDKMLAVTTYCFDIAAL--ELFLPLIKGAHCYICQ 1371
Cdd:cd05944      1 SDDVAAYFHTGGTTGTPK--LAQHTHSN--EVYNAWMLALNSlfdPDDVLLCGLPLFHVNGSvvTLLTPLASGAHVVLAG 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1372 TEHTKD---VEKLKRDIRTIKPTVMQATPATWKMLFysgwENEENVKI------LCGGEALPETLKRYFLD-TGSEAWNM 1441
Cdd:cd05944     77 PAGYRNpglFDNFWKLVERYRITSLSTVPTVYAALL----QVPVNADIsslrfaMSGAAPLPVELRARFEDaTGLPVVEG 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1442 FGPTETTIWSAVQRINDECSRATIGRPIANTQIYItdSQLAPV-----PAGVP--GELCIAGDGVAKGYYKKEELTDSrF 1514
Cdd:cd05944    153 YGLTEATCLVAVNPPDGPKRPGSVGLRLPYARVRI--KVLDGVgrllrDCAPDevGEICVAGPGVFGGYLYTEGNKNA-F 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1515 IDNPFepgsklYRTGDMARWLPGGRIEYIGRIDNQVkIRG-FRIELGDIESRLSEHPGILECVVVADMDNLA-----AYY 1588
Cdd:cd05944    230 VADGW------LNTGDLGRLDADGYLFITGRAKDLI-IRGgHNIDPALIEEALLRHPAVAFAGAVGQPDAHAgelpvAYV 302
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1776025254 1589 TAKhANASLTARELRHFVKNALPAYM-VPSYFIQLDHMPLTPNGKIDRNSLK 1639
Cdd:cd05944    303 QLK-PGAVVEEEELLAWARDHVPERAaVPKHIEVLEELPVTAVGKVFKPALR 353
caiC PRK08008
putative crotonobetaine/carnitine-CoA ligase; Validated
185-438 1.63e-13

putative crotonobetaine/carnitine-CoA ligase; Validated


Pssm-ID: 181195 [Multi-domain]  Cd Length: 517  Bit Score: 77.03  E-value: 1.63e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  185 SPEDLALLLLTSGSTGTPKAVMLNHRNIM-SMVKGIIQMQgFTREDITFNWMPFDHVGgigmlhlrdvylgCQ------E 257
Cdd:PRK08008   171 STDDTAEILFTSGTTSRPKGVVITHYNLRfAGYYSAWQCA-LRDDDVYLTVMPAFHID-------------CQctaamaA 236
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  258 INVSSETILMEPL---KWLDWIDHYRASVTWA-PNFAFGLVTDFAEEiKDRKWDLSSMRYMLN----GGEAMVAKVGRRI 329
Cdd:PRK08008   237 FSAGATFVLLEKYsarAFWGQVCKYRATITECiPMMIRTLMVQPPSA-NDRQHCLREVMFYLNlsdqEKDAFEERFGVRL 315
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  330 LEllephglpadairpAWGMSETSSGVIFSheftRAGtsDDDHFVEIGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGL- 408
Cdd:PRK08008   316 LT--------------SYGMTETIVGIIGD----RPG--DKRRWPSIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKGVp 375
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1776025254  409 --SVTSGYYQRPDLNESVFTEDGWFETGDLGF 438
Cdd:PRK08008   376 gkTIFKEYYLDPKATAKVLEADGWLHTGDTGY 407
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
3111-3185 2.32e-13

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 68.43  E-value: 2.32e-13
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1776025254  3111 QTRKLEAALIQMVGAILKVNTDD-IDVNTELSEYGFDSVTFTVFTNKINEKFQLELTPTIFFEYGSVQSLAEYVVA 3185
Cdd:smart00823    9 RRRLLLDLVREQVAAVLGHAAAEaIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHLAA 84
ACS-like cd17634
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ...
33-549 2.51e-13

acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341289 [Multi-domain]  Cd Length: 587  Bit Score: 76.46  E-value: 2.51e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254   33 EVLYRTAAELGDTKGIIYLQPDGTEVYQ-SYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNSQLLPAFWGCVLTGVVP 111
Cdd:cd17634     57 NALDRHLRENGDRTAIIYEGDDTSQSRTiSYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVH 136
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  112 APLAVPPTYAESSSgtqKLKDAWTLLdkpaVITDRGMHQ--------EMLDWAKEQGLEGFRAIIVEDLLSAE------A 177
Cdd:cd17634    137 SVIFGGFAPEAVAG---RIIDSSSRL----LITADGGVRagrsvplkKNVDDALNPNVTSVEHVIVLKRTGSDidwqegR 209
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  178 DTDWHQS-------------SPEDLALLLLTSGSTGTPKAVMlnHRNIMSMVKGIIQMQ---GFTREDItfnWMPFDHVG 241
Cdd:cd17634    210 DLWWRDLiakaspehqpeamNAEDPLFILYTSGTTGKPKGVL--HTTGGYLVYAATTMKyvfDYGPGDI---YWCTADVG 284
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  242 GIgMLHLRDVYLGcqeINVSSETILME-------PLKWLDWIDHYRASVTW-APNFAFGLVTDFAEEIKdrKWDLSSMRY 313
Cdd:cd17634    285 WV-TGHSYLLYGP---LACGATTLLYEgvpnwptPARMWQVVDKHGVNILYtAPTAIRALMAAGDDAIE--GTDRSSLRI 358
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  314 MLNGGEAMVAKVGRRILELLEPHGLPadaIRPAWGMSETSSGVIFS---HEFTRAGTSDddhfveigSPIPGFSMRIVND 390
Cdd:cd17634    359 LGSVGEPINPEAYEWYWKKIGKEKCP---VVDTWWQTETGGFMITPlpgAIELKAGSAT--------RPVFGVQPAVVDN 427
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  391 HNELVEEGEIGRFqVSGLS---VTSGYYQRPDLNESVF--TEDGWFETGDLGFL-RNGRLTITGRTKDAIIINGINYYSH 464
Cdd:cd17634    428 EGHPQPGGTEGNL-VITDPwpgQTRTLFGDHERFEQTYfsTFKGMYFSGDGARRdEDGYYWITGRSDDVINVAGHRLGTA 506
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  465 AIESAVEELSEIetsytAACAVRLGQNSTDQLAIFFVTSAKLNDEQMSQLLRNIQSHVSQVIG--VTPEYLLPVQkeEIP 542
Cdd:cd17634    507 EIESVLVAHPKV-----AEAAVVGIPHAIKGQAPYAYVVLNHGVEPSPELYAELRNWVRKEIGplATPDVVHWVD--SLP 579

                   ....*..
gi 1776025254  543 KTAIGKI 549
Cdd:cd17634    580 KTRSGKI 586
PrpE cd05967
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ...
43-562 2.54e-13

Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.


Pssm-ID: 341271 [Multi-domain]  Cd Length: 617  Bit Score: 76.59  E-value: 2.54e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254   43 GDTKGIIYLQP-DGTEVYQSYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNSQLLPAFWGCVLTG----VVPAPLAVP 117
Cdd:cd05967     65 GDQIALIYDSPvTGTERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGaihsVVFGGFAAK 144
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  118 ptyaESSSgtqKLKDAwtlldKPAVI--TDRGM-------HQEMLDWAKEQGLEGFRAIIVEDLLSAEADT-------DW 181
Cdd:cd05967    145 ----ELAS---RIDDA-----KPKLIvtASCGIepgkvvpYKPLLDKALELSGHKPHHVLVLNRPQVPADLtkpgrdlDW 212
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  182 H----QSSPEDLALL--------LLTSGSTGTPK---------AVMLNH--RNIMSMVKGIIQmqgFTREDItfNWMpfd 238
Cdd:cd05967    213 SellaKAEPVDCVPVaatdplyiLYTSGTTGKPKgvvrdngghAVALNWsmRNIYGIKPGDVW---WAASDV--GWV--- 284
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  239 hVGgigmlHLRDVY----LGCQeinvsseTILME--PLKWLD----W--IDHYR-ASVTWAPNfAFGLVTDFAEEIKD-R 304
Cdd:cd05967    285 -VG-----HSYIVYgpllHGAT-------TVLYEgkPVGTPDpgafWrvIEKYQvNALFTAPT-AIRAIRKEDPDGKYiK 350
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  305 KWDLSSMRYMLNGGEamvaKVGRRILELLEPH-GLPadaIRPAWGMSETSSGVI-----FSHEFTRAGTSdddhfveiGS 378
Cdd:cd05967    351 KYDLSSLRTLFLAGE----RLDPPTLEWAENTlGVP---VIDHWWQTETGWPITanpvgLEPLPIKAGSP--------GK 415
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  379 PIPGFSMRIVNDHNELVEEGEIGRFQVSGL---SVTSGYYQRPDL-NESVFTED-GWFETGDLGFL-RNGRLTITGRTKD 452
Cdd:cd05967    416 PVPGYQVQVLDEDGEPVGPNELGNIVIKLPlppGCLLTLWKNDERfKKLYLSKFpGYYDTGDAGYKdEDGYLFIMGRTDD 495
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  453 AIIINGINYYSHAIESAVEELSEIetsytAACAVRLGQNSTD-QLAIFFV---TSAKLNDEQmsqLLRNIQSHVSQVIG- 527
Cdd:cd05967    496 VINVAGHRLSTGEMEESVLSHPAV-----AECAVVGVRDELKgQVPLGLVvlkEGVKITAEE---LEKELVALVREQIGp 567
                          570       580       590
                   ....*....|....*....|....*....|....*.
gi 1776025254  528 -VTPEYLLPVQKeeIPKTAIGKIQRTQLKtSFENGE 562
Cdd:cd05967    568 vAAFRLVIFVKR--LPKTRSGKILRRTLR-KIADGE 600
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
1660-1719 2.65e-13

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.


Pssm-ID: 425746 [Multi-domain]  Cd Length: 62  Bit Score: 67.59  E-value: 2.65e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1776025254 1660 DTVFTIWQEVLK--TSDIEWDDGFFDVGGDSLLAVTVADRIKHELSCEFSVTDLFEYSTIKN 1719
Cdd:pfam00550    1 ERLRELLAEVLGvpAEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLAE 62
PRK06334 PRK06334
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
186-548 2.66e-13

long chain fatty acid--[acyl-carrier-protein] ligase; Validated


Pssm-ID: 180533 [Multi-domain]  Cd Length: 539  Bit Score: 76.39  E-value: 2.66e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  186 PEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDHVGGIGMLHLRDVYLGcqeINVSSETI 265
Cdd:PRK06334   182 PEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLPPFHAYGFNSCTLFPLLSG---VPVVFAYN 258
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  266 LMEPLKWLDWIDHYRASVTWAPNFAFGLVTDFAeeiKDRKWDLSSMRYMLNGGEAMVAKVGRRILELlephgLPADAIRP 345
Cdd:PRK06334   259 PLYPKKIVEMIDEAKVTFLGSTPVFFDYILKTA---KKQESCLPSLRFVVIGGDAFKDSLYQEALKT-----FPHIQLRQ 330
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  346 AWGMSETSSGVIFSHEftragtSDDDHFVEIGSPIPGFSMRIVNDHNEL-VEEGEIGRFQVSGLSVTSGYYQRpDLNESV 424
Cdd:PRK06334   331 GYGTTECSPVITINTV------NSPKHESCVGMPIRGMDVLIVSEETKVpVSSGETGLVLTRGTSLFSGYLGE-DFGQGF 403
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  425 FTEDG--WFETGDLGFL-RNGRLTITGRTKDAIIINGINYYSHAIESA-VEELSEIETSYTAACAVRLGQNSTDQLAIFF 500
Cdd:PRK06334   404 VELGGetWYVTGDLGYVdRHGELFLKGRLSRFVKIGAEMVSLEALESIlMEGFGQNAADHAGPLVVCGLPGEKVRLCLFT 483
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*...
gi 1776025254  501 VTSAKLNdeQMSQLLRNIQShvSQVIGVTPEYllpvQKEEIPKTAIGK 548
Cdd:PRK06334   484 TFPTSIS--EVNDILKNSKT--SSILKISYHH----QVESIPMLGTGK 523
PRK12476 PRK12476
putative fatty-acid--CoA ligase; Provisional
1151-1330 3.02e-13

putative fatty-acid--CoA ligase; Provisional


Pssm-ID: 171527 [Multi-domain]  Cd Length: 612  Bit Score: 76.32  E-value: 3.02e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1151 PYITFHELFEQQAKKTPDRAAVSY-------EGQT--LTYRELDERSTQLAIYLQAHGVGPDRLAgIYVDRSLDMLVGLL 1221
Cdd:PRK12476    32 PGTTLISLIERNIANVGDTVAYRYldhshsaAGCAveLTWTQLGVRLRAVGARLQQVAGPGDRVA-ILAPQGIDYVAGFF 110
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1222 AILKAGGAYVPL-DPSYP--AERLEYMLEDSEVFITLTTS-------ELVNTLSWNGVTTALLdqdWDEIAQTASDRKVL 1291
Cdd:PRK12476   111 AAIKAGTIAVPLfAPELPghAERLDTALRDAEPTVVLTTTaaaeaveGFLRNLPRLRRPRVIA---IDAIPDSAGESFVP 187
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1776025254 1292 TRTVTpENLAYVIYTSGSTGKPKGVMIPHKALTNFLVSM 1330
Cdd:PRK12476   188 VELDT-DDVSHLQYTSGSTRPPVGVEITHRAVGTNLVQM 225
PLN02479 PLN02479
acetate-CoA ligase
1305-1639 3.11e-13

acetate-CoA ligase


Pssm-ID: 178097 [Multi-domain]  Cd Length: 567  Bit Score: 76.42  E-value: 3.11e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1305 YTSGSTGKPKGVMIPHK-----ALTNFLV-SMGETPGLTAEDKMLAVTTYCFDIAAlelflplikGAHC--YICQTEHTk 1376
Cdd:PLN02479   202 YTSGTTASPKGVVLHHRgaylmALSNALIwGMNEGAVYLWTLPMFHCNGWCFTWTL---------AALCgtNICLRQVT- 271
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1377 dVEKLKRDIRTIKPTVMQATPATWKMLFYSGWENE-----ENVKILCGGEALPETLKRYFLDTGSEAWNMFGPTET---- 1447
Cdd:PLN02479   272 -AKAIYSAIANYGVTHFCAAPVVLNTIVNAPKSETilplpRVVHVMTAGAAPPPSVLFAMSEKGFRVTHTYGLSETygps 350
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1448 TI------WSAVQRINDECSRATIG-RPIANTQIYITDSQ-LAPVPA--GVPGELCIAGDGVAKGYYKKEELTDSRFidn 1517
Cdd:PLN02479   351 TVcawkpeWDSLPPEEQARLNARQGvRYIGLEGLDVVDTKtMKPVPAdgKTMGEIVMRGNMVMKGYLKNPKANEEAF--- 427
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1518 pfepGSKLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMDNL-----AAYYTAK- 1591
Cdd:PLN02479   428 ----ANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERwgespCAFVTLKp 503
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1776025254 1592 ---HANASLTARELRHFVKNALPAYMVPSYFIqLDHMPLTPNGKIDRNSLK 1639
Cdd:PLN02479   504 gvdKSDEAALAEDIMKFCRERLPAYWVPKSVV-FGPLPKTATGKIQKHVLR 553
PtmA cd17636
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ...
1303-1634 3.12e-13

long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341291 [Multi-domain]  Cd Length: 331  Bit Score: 74.26  E-value: 3.12e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1303 VIYTSGSTGKPKGVMIPHKALTNFLVSMGETPGLTAEDKMLAVTTYcFDIAALELFLP--LIKGAHCYICQTehtkDVEK 1380
Cdd:cd17636      5 AIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLNSGPL-FHIGTLMFTLAtfHAGGTNVFVRRV----DAEE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1381 LKRDIrtikptvmQATPATWKMLFYSGWEneenvKILCGGEALPETLKRYFLDTGSEAWNMFGPTETTIWS--------- 1451
Cdd:cd17636     80 VLELI--------EAERCTHAFLLPPTID-----QIVELNADGLYDLSSLRSSPAAPEWNDMATVDTSPWGrkpggygqt 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1452 -----AVQRINDECSRATIGRPIANTQIYITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNpfepgskLY 1526
Cdd:cd17636    147 evmglATFAALGGGAIGGAGRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTRGG-------WH 219
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1527 RTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVV--VAD---MDNLAAYYTAKhANASLTARE 1601
Cdd:cd17636    220 HTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVigVPDprwAQSVKAIVVLK-PGASVTEAE 298
                          330       340       350
                   ....*....|....*....|....*....|...
gi 1776025254 1602 LRHFVKNALPAYMVPSYFIQLDHMPLTPNGKID 1634
Cdd:cd17636    299 LIEHCRARIASYKKPKSVEFADALPRTAGGADD 331
AMP-binding_C pfam13193
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ...
1561-1632 3.17e-13

AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.


Pssm-ID: 463804 [Multi-domain]  Cd Length: 76  Bit Score: 67.57  E-value: 3.17e-13
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1776025254 1561 DIESRLSEHPGILECVVVADMDN-----LAAYYTAKhANASLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGK 1632
Cdd:pfam13193    1 EVESALVSHPAVAEAAVVGVPDElkgeaPVAFVVLK-PGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
3117-3178 3.22e-13

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.


Pssm-ID: 425746 [Multi-domain]  Cd Length: 62  Bit Score: 67.20  E-value: 3.22e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1776025254 3117 AALIQMVGAILKVNTDDIDVNTELSEYGFDSVTFTVFTNKINEKFQLELTPTIFFEYGSVQS 3178
Cdd:pfam00550    1 ERLRELLAEVLGVPAEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLAE 62
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
4172-4297 3.60e-13

short chain dehydrogenase; This family contains a wide variety of dehydrogenases.


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 71.49  E-value: 3.60e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4172 VLLITGGTRGIGLLCARHFAEcYGvKKLVLTGReqlppreewarfktsntSLAEKIQAVRELEAKGVQVEMLSLTLSDDA 4251
Cdd:pfam00106    2 VALVTGASSGIGRAIAKRLAK-EG-AKVVLVDR-----------------SEEKLEAVAKELGALGGKALFIQGDVTDRA 62
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1776025254 4252 QVEQTLQHIKRTLGPIGGVIHCAGLTDMDTLAFIrkTSDDIQRVME 4297
Cdd:pfam00106   63 QVKALVEQAVERLGRLDILVNNAGITGLGPFSEL--SDEDWERVID 106
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
4172-4341 4.87e-13

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 72.11  E-value: 4.87e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4172 VLLITGGTRGIGLLCARHFAEcYGVKkLVLTGReqlppreewarfktsNTSLAEKIQAvrELEAKGVQVEMLSLTLSDDA 4251
Cdd:PRK05653     7 TALVTGASRGIGRAIALRLAA-DGAK-VVIYDS---------------NEEAAEALAA--ELRAAGGEARVLVFDVSDEA 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4252 QVEQTLQHIKRTLGPIGGVIHCAGLTDMDtlAFIRKTSDDIQRVMEpkVSgLTTLYrHVCNEPLQFF--------VLFSS 4323
Cdd:PRK05653    68 AVRALIEAAVEAFGALDILVNNAGITRDA--LLPRMSEEDWDRVID--VN-LTGTF-NVVRAALPPMikarygriVNISS 141
                          170
                   ....*....|....*...
gi 1776025254 4324 VSAIIPelSAGQADYAMA 4341
Cdd:PRK05653   142 VSGVTG--NPGQTNYSAA 157
PaaK cd05913
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ...
195-551 5.71e-13

Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic degradation pathway, by converting phenylacetic acid (PA) into phenylacetyl-CoA (PA-CoA). Phenylacetate-CoA ligase has been found in proteobacteria as well as gram positive prokaryotes. The enzyme is specifically induced after aerobic growth in a chemically defined medium containing PA or phenylalanine (Phe) as the sole carbon source. PaaKs are members of the adenylate-forming enzyme (AFE) family. However, sequence comparison reveals divergent features of PaaK with respect to the superfamily, including a novel N-terminal sequence.


Pssm-ID: 341239 [Multi-domain]  Cd Length: 425  Bit Score: 74.58  E-value: 5.71e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  195 TSGSTGTPKAVMLNHRNIMS---MVKGIIQMQGFTREDI---TFNWMPFdhVGGIGmLHLRDVYLGCQEINVS---SEti 265
Cdd:cd05913     86 SSGTTGKPTVVGYTKNDLDVwaeLVARCLDAAGVTPGDRvqnAYGYGLF--TGGLG-FHYGAERLGALVIPAGggnTE-- 160
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  266 lmeplKWLDWIDHYRASVTWA-PNFAFGLvtdfAEEIKDRKWDL--SSMRYMLNGGEAMVAKVGRRILELL-----EPHG 337
Cdd:cd05913    161 -----RQLQLIKDFGPTVLCCtPSYALYL----AEEAEEEGIDPreLSLKVGIFGAEPWTEEMRKRIERRLgikayDIYG 231
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  338 LPADaIRPAWGMSETSSGVIFSHEftragtsddDHFVEIgspipgfsmrIVNDH-NELVEEGEIGRFQVSGLSVTSGYYQ 416
Cdd:cd05913    232 LTEI-IGPGVAFECEEKDGLHIWE---------DHFIPE----------IIDPEtGEPVPPGEVGELVFTTLTKEAMPLI 291
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  417 RpdlnesvftedgwFETGDLGFL-----RNGRLT-----ITGRTKDAIIINGINYYSHAIESAVEELSEIETSYtaacav 486
Cdd:cd05913    292 R-------------YRTRDITRLlpgpcPCGRTHrridrITGRSDDMLIIRGVNVFPSQIEDVLLKIPGLGPHY------ 352
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1776025254  487 RL---GQNSTDQLAIFF-VTSAKLNDEQMSQLLRNIQSHVSQVIGVTPEYLLpVQKEEIPKTaIGKIQR 551
Cdd:cd05913    353 QLiltRQEHLDELTIKVeVRPEADDDEKLEALKQRLERHIKSVLGVTVEVEL-VEPGSLPRS-EGKAKR 419
PRK13383 PRK13383
acyl-CoA synthetase; Provisional
191-554 6.17e-13

acyl-CoA synthetase; Provisional


Pssm-ID: 139531 [Multi-domain]  Cd Length: 516  Bit Score: 75.03  E-value: 6.17e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  191 LLLLTSGSTGTPKAVMLNHRnIMSMVKGIIQMQGFTR----EDITFNwMPFDHVGGIGMLHLrDVYLGCQEI---NVSSE 263
Cdd:PRK13383   178 IVLLTSGTTGKPKGVPRAPQ-LRSAVGVWVTILDRTRlrtgSRISVA-MPMFHGLGLGMLML-TIALGGTVLthrHFDAE 254
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  264 TILMEPlkwldwiDHYRASVTWAPNFAFGLVTDFAEEIKDRKwDLSSMRYMLNGGEAMVAKVGRRILELLephglpADAI 343
Cdd:PRK13383   255 AALAQA-------SLHRADAFTAVPVVLARILELPPRVRARN-PLPQLRVVMSSGDRLDPTLGQRFMDTY------GDIL 320
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  344 RPAWGMSETSSGVIFSHEFTRagtsddDHFVEIGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGYYQRPdlNES 423
Cdd:PRK13383   321 YNGYGSTEVGIGALATPADLR------DAPETVGKPVAGCPVRILDRNNRPVGPRVTGRIFVGGELAGTRYTDGG--GKA 392
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  424 VFteDGWFETGDLGFLRN-GRLTITGRTKDAIIINGINYYSHAIESAVEELSEI-ETSYTAACAVRLGQnstdQLAIFFV 501
Cdd:PRK13383   393 VV--DGMTSTGDMGYLDNaGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVaDNAVIGVPDERFGH----RLAAFVV 466
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1776025254  502 T--SAKLNDEQMSQLLRNIQSHVSQvigvtPEYLLPVQkeEIPKTAIGKIQRTQL 554
Cdd:PRK13383   467 LhpGSGVDAAQLRDYLKDRVSRFEQ-----PRDINIVS--SIPRNPTGKVLRKEL 514
PLN02787 PLN02787
3-oxoacyl-[acyl-carrier-protein] synthase II
4504-4929 8.10e-13

3-oxoacyl-[acyl-carrier-protein] synthase II


Pssm-ID: 215421 [Multi-domain]  Cd Length: 540  Bit Score: 75.02  E-value: 8.10e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4504 RINRKLEAALDPSILYEYPTIQRFTDWLIGSYSERLSALFGGRISDASAPLENKIEVEAPVPAKDRALTPQIQAPAILSP 4583
Cdd:PLN02787    45 KRRKCSSASGSASILVTSCLAFGPCTHYNSSGGNALSSLFGSNSVSLNRNQRRRNRAARSGKAMAVAVQPEKEVETKKKP 124
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4584 DSHAEGIAVVGLSCRFPGAETLESYWSLLSEGRSSIGPIpaERWGCKT--PYYAGVIDGVS---YFDPDFfllheedVRA 4658
Cdd:PLN02787   125 LTKQRRVVVTGMGVVSPLGHDPDVFYNNLLEGVSGISEI--ERFDCSQfpTRIAGEIKSFStdgWVAPKL-------SKR 195
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4659 MDPQALLVLEECLKLLYHAGYTPE---EIKGKPVGVYIG-GRSQHKPDEDSLDHAK------NPI------VTVGQNYLA 4722
Cdd:PLN02787   196 MDKFMLYLLTAGKKALADGGITEDvmkELDKTKCGVLIGsAMGGMKVFNDAIEALRisyrkmNPFcvpfatTNMGSAMLA 275
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4723 ANLSQFfdvrGPSVVVDTAC-SSALVGMNMAIQALRG-------GDIQSAIVGgVSLLSSDASHRLFDRRGILSKHSsfH 4794
Cdd:PLN02787   276 MDLGWM----GPNYSISTACaTSNFCILNAANHIIRGeadvmlcGGSDAAIIP-IGLGGFVACRALSQRNDDPTKAS--R 348
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4795 VFDERADGVVLGEGVGMVMLKTVKQALEDGDTIYAVVKAASVNNDGRTAGPATPNLEAQKEVMKDALFKSGKKPEDISYL 4874
Cdd:PLN02787   349 PWDMNRDGFVMGEGAGVLLLEELEHAKKRGANIYAEFLGGSFTCDAYHMTEPHPEGAGVILCIEKALAQSGVSKEDVNYI 428
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1776025254 4875 EANGSGSIVTDLLELKAIQSVYrsGHSSPLSLGSIKPNIGHPLCAEGIASFIKVV 4929
Cdd:PLN02787   429 NAHATSTKAGDLKEYQALMRCF--GQNPELRVNSTKSMIGHLLGAAGAVEAIATV 481
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
4172-4341 1.14e-12

3-ketoacyl-(acyl-carrier-protein) reductase; Validated


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 71.38  E-value: 1.14e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4172 VLLITGGTRGIGLLCARHFAECyGVKkLVLTGReqlppreewarfktSNTSLAEKIqaVRELEAKGVQVEMLSLTLSDDA 4251
Cdd:PRK05557     7 VALVTGASRGIGRAIAERLAAQ-GAN-VVINYA--------------SSEAGAEAL--VAEIGALGGKALAVQGDVSDAE 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4252 QVEQTLQHIKRTLGPIGGVIHCAGLTDmDTLaFIRKTSDDIQRVMEPKVSGLTTLYRHVC------------Neplqffv 4319
Cdd:PRK05557    69 SVERAVDEAKAEFGGVDILVNNAGITR-DNL-LMRMKEEDWDRVIDTNLTGVFNLTKAVArpmmkqrsgriiN------- 139
                          170       180
                   ....*....|....*....|..
gi 1776025254 4320 lFSSVSAIIPelSAGQADYAMA 4341
Cdd:PRK05557   140 -ISSVVGLMG--NPGQANYAAS 158
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
2852-3028 1.16e-12

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 70.96  E-value: 1.16e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2852 LITGGAGSLGLLFAKEIAnRTGrSTIVLTGRSVlsEDKENELEALRSIGAEVVYREADVSDQHAVHHLFEEIKERYGTLN 2931
Cdd:PRK05653     9 LVTGASRGIGRAIALRLA-ADG-AKVVIYDSNE--EAAEALAAELRAAGGEARVLVFDVSDEAAVRALIEAAVEAFGALD 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2932 GIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSGllhvdecskdfpldFF------------------IFFSSVSGCLGNAG 2993
Cdd:PRK05653    85 ILVNNAGITRDALLPRMSEEDWDRVIDVNLTG--------------TFnvvraalppmikarygriVNISSVSGVTGNPG 150
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1776025254 2994 QADYAAANSFMDAFAeyrRSLAASKKRFGstISFN 3028
Cdd:PRK05653   151 QTNYSAAKAGVIGFT---KALALELASRG--ITVN 180
PRK13391 PRK13391
acyl-CoA synthetase; Provisional
1160-1633 1.18e-12

acyl-CoA synthetase; Provisional


Pssm-ID: 184022 [Multi-domain]  Cd Length: 511  Bit Score: 74.34  E-value: 1.18e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1160 EQQAKKTPDRAAV--SYEGQTLTYRELDERSTQLAIYLQAHGVGP-DRLAgIYVDRSLDMLVGLLAILKAGGAYVPLDPS 1236
Cdd:PRK13391     4 GIHAQTTPDKPAVimASTGEVVTYRELDERSNRLAHLFRSLGLKRgDHVA-IFMENNLRYLEVCWAAERSGLYYTCVNSH 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1237 YPAERLEYMLEDSEVFItlttseLVNTLSWNGVTTALLDQ------DWDEIAQTASDRKVLTRTVTPENLAYVI------ 1304
Cdd:PRK13391    83 LTPAEAAYIVDDSGARA------LITSAAKLDVARALLKQcpgvrhRLVLDGDGELEGFVGYAEAVAGLPATPIadeslg 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1305 ----YTSGSTGKPKGVM--IPHKALtnflvsmGETPGLTAEDKMLavttycFDIAALELFL---PLIKGAHCYICQT--- 1372
Cdd:PRK13391   157 tdmlYSSGTTGRPKGIKrpLPEQPP-------DTPLPLTAFLQRL------WGFRSDMVYLspaPLYHSAPQRAVMLvir 223
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1373 --------EHTkDVEKLKRDIRTIKPTVMQATPATW-KMLfysgweneenvkilcggeALP-ETLKRYFLDT-------- 1434
Cdd:PRK13391   224 lggtvivmEHF-DAEQYLALIEEYGVTHTQLVPTMFsRML------------------KLPeEVRDKYDLSSlevaihaa 284
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1435 ---------------GSEAWNMFGPTETTIWSAVQRINDECSRATIGRPIANTqIYITDSQLAPVPAGVPGELCIAGdGV 1499
Cdd:PRK13391   285 apcppqvkeqmidwwGPIIHEYYAATEGLGFTACDSEEWLAHPGTVGRAMFGD-LHILDDDGAELPPGEPGTIWFEG-GR 362
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1500 AKGYYKKEELT-DSRfidnpfEPGSKLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGIL----- 1573
Cdd:PRK13391   363 PFEYLNDPAKTaEAR------HPDGTWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVAdaavf 436
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1574 --------ECV--VVADMDNLAayytakhANASLtARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKI 1633
Cdd:PRK13391   437 gvpnedlgEEVkaVVQPVDGVD-------PGPAL-AAELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKL 498
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
2850-3000 1.27e-12

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 71.14  E-value: 1.27e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGLLFAKEIANRTGRSTIVltgrSVLSEDKENELEALRSIGAEVVYREADVSDQHAVHHLFEEIKERYGT 2929
Cdd:PRK08217     7 VIVITGGAQGLGRAMAEYLAQKGAKLALI----DLNQEKLEEAVAECGALGTEVRGYAANVTDEEDVEATFAQIAEDFGQ 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2930 LNGIIHGAG--------SIKDHFIIHKTN-EEFQEVLQPKVSGL--------LHVDECSKDfplDFFIFFSSVSGClGNA 2992
Cdd:PRK08217    83 LNGLINNAGilrdgllvKAKDGKVTSKMSlEQFQSVIDVNLTGVflcgreaaAKMIESGSK---GVIINISSIARA-GNM 158

                   ....*...
gi 1776025254 2993 GQADYAAA 3000
Cdd:PRK08217   159 GQTNYSAS 166
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
3221-3281 1.28e-12

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 66.50  E-value: 1.28e-12
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1776025254  3221 VSAILKVNSED-IDVNTELSEYGFDSVTFTVFTNKINEEFQLELTPTIFFEYGSIHSLAEYL 3281
Cdd:smart00823   21 VAAVLGHAAAEaIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHL 82
FCS cd05921
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ...
1160-1533 1.65e-12

Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.


Pssm-ID: 341245 [Multi-domain]  Cd Length: 561  Bit Score: 74.01  E-value: 1.65e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1160 EQQAKKTPDRAAVSYEG-----QTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLD 1234
Cdd:cd05921      2 AHWARQAPDRTWLAEREgnggwRRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVS 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1235 PSYPA-----ERLEYMLE----------DSEVF-------ITLTTSELVNTLSWNGVTTALLDQDWDEIAQTASDRkvLT 1292
Cdd:cd05921     82 PAYSLmsqdlAKLKHLFEllkpglvfaqDAAPFaralaaiFPLGTPLVVSRNAVAGRGAISFAELAATPPTAAVDA--AF 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1293 RTVTPENLAYVIYTSGSTGKPKGVMIPHKALTNFLVSMGETPGLTAED--KMLAVTTYCFDIAALELF-LPLIKGAHCYI 1369
Cdd:cd05921    160 AAVGPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEppVLVDWLPWNHTFGGNHNFnLVLYNGGTLYI 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1370 CQTEHT-KDVEKLKRDIRTIKPTVMQATPATWKMLFySGWENEE--------NVKILC-GGEALP----ETLKRYFLDTG 1435
Cdd:cd05921    240 DDGKPMpGGFEETLRNLREISPTVYFNVPAGWEMLV-AALEKDEalrrrffkRLKLMFyAGAGLSqdvwDRLQALAVATV 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1436 SEAWNM---FGPTET------TIWSAvqrindecSRA-TIGRPIANTQIYItdsqlapVPAGVPGELCIAGDGVAKGYYK 1505
Cdd:cd05921    319 GERIPMmagLGATETaptatfTHWPT--------ERSgLIGLPAPGTELKL-------VPSGGKYEVRVKGPNVTPGYWR 383
                          410       420
                   ....*....|....*....|....*...
gi 1776025254 1506 KEELTDSRFIDNPFepgsklYRTGDMAR 1533
Cdd:cd05921    384 QPELTAQAFDEEGF------YCLGDAAK 405
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
1654-1728 1.98e-12

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 65.65  E-value: 1.98e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1776025254 1654 SPKNIQDTVFTIWQEVLK--TSDIEWDDGFF-DVGGDSLLAVTVADRIKHELSCEFSVTDLFEYSTIKNISQYITEQR 1728
Cdd:COG0236      2 PREELEERLAEIIAEVLGvdPEEITPDDSFFeDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEEKL 79
PRK06060 PRK06060
p-hydroxybenzoic acid--AMP ligase FadD22;
1174-1740 2.33e-12

p-hydroxybenzoic acid--AMP ligase FadD22;


Pssm-ID: 180374 [Multi-domain]  Cd Length: 705  Bit Score: 73.91  E-value: 2.33e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1174 YEGQTLTYRELDERSTQLAIYLQAHGVGP-DRLAGIYVDrSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLEDSEVF 1252
Cdd:PRK06060    26 YAADVVTHGQIHDGAARLGEVLRNRGLSSgDRVLLCLPD-SPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPA 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1253 ITLTTSELVNTLSWNGVTTALldqdwDEIAQTASDRKVLTRTVTPENLAYVIYTSGSTGKPKGVMIPHKALTNFLVSM-G 1331
Cdd:PRK06060   105 LVVTSDALRDRFQPSRVAEAA-----ELMSEAARVAPGGYEPMGGDALAYATYTSGTTGPPKAAIHRHADPLTFVDAMcR 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1332 ETPGLTAEDKMLAVTTYCFDIA-ALELFLPLIKGAHCYICQTEHTKDVEKLKRdiRTIKPTVMQATPATW-KMLFYSGWE 1409
Cdd:PRK06060   180 KALRLTPEDTGLCSARMYFAYGlGNSVWFPLATGGSAVINSAPVTPEAAAILS--ARFGPSVLYGVPNFFaRVIDSCSPD 257
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1410 NEENVK-ILCGGEAL----PETLKRYFldTGSEAWNMFGPTETTiWSAVQRINDECSRATIGRPIANTQIYITDSQLAPV 1484
Cdd:PRK06060   258 SFRSLRcVVSAGEALelglAERLMEFF--GGIPILDGIGSTEVG-QTFVSNRVDEWRLGTLGRVLPPYEIRVVAPDGTTA 334
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1485 PAGVPGELCIAGDGVAKGYYKKEE--LTDSRFIDnpfepgsklyrTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDI 1562
Cdd:PRK06060   335 GPGVEGDLWVRGPAIAKGYWNRPDspVANEGWLD-----------TRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREV 403
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1563 ESRLSEHPGILECVVVA-----DMDNLAAYYTAKHAnASLTARELRHFVK---NALPAYMVPSYFIQLDHMPLTPNGKID 1634
Cdd:PRK06060   404 ERLIIEDEAVAEAAVVAvrestGASTLQAFLVATSG-ATIDGSVMRDLHRgllNRLSAFKVPHRFAVVDRLPRTPNGKLV 482
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1635 RNSLK----------------------NID-------------LSGEQLKQR-----QTSPKNIQDTVFTIWQEVLKTSD 1674
Cdd:PRK06060   483 RGALRkqsptkpiwelsltepgsgvraQRDdlsasnmtiaggnDGGATLRERlvalrQERQRLVVDAVCAEAAKMLGEPD 562
                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1776025254 1675 ---IEWDDGFFDVGGDSLLAVTVADRIKHELSCEFSVTDLFEYSTIKNISQYITEQRMGnaSDHMPTDP 1740
Cdd:PRK06060   563 pwsVDQDLAFSELGFDSQMTVTLCKRLAAVTGLRLPETVGWDYGSISGLAQYLEAELAG--GHGRLKSA 629
PRK08439 PRK08439
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
4638-4931 2.62e-12

3-oxoacyl-(acyl carrier protein) synthase II; Reviewed


Pssm-ID: 236265 [Multi-domain]  Cd Length: 406  Bit Score: 72.46  E-value: 2.62e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4638 IDGVSYFDPDFF---------------LLHEEDVRAMDPQALLVLEECLKLLYHAGYTPEEIKGKPVGVY----IGGRSQ 4698
Cdd:PRK08439    33 IKKITLFDASDFpvqiageitdfdpteVMDPKEVKKADRFIQLGLKAAREAMKDAGFLPEELDAERFGVSsasgIGGLPN 112
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4699 HKpdedsldhaKNPIV--TVGQ-------------NYLAANLSQFFDVRGPSVVVDTACSSALVGMNMAIQ--ALRGGD- 4760
Cdd:PRK08439   113 IE---------KNSIIcfEKGPrkispffipsalvNMLGGFISIEHGLKGPNLSSVTACAAGTHAIIEAVKtiMLGGADk 183
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4761 -----IQSAI----VGGVsllssdASHRLFDRRGILSKHSSfHVFDERADGVVLGEGVGMVMLKTVKQALEDGDTIYAVV 4831
Cdd:PRK08439   184 mlvvgAESAIcpvgIGGF------AAMKALSTRNDDPKKAS-RPFDKDRDGFVMGEGAGALVLEEYESAKKRGAKIYAEI 256
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4832 kaASVNNDGRTAGPATPNLEAQKEVMKDALfKSGKKPEdISYLEANGSGSIVTDLLELKAIQSVYRSGHSSPLsLGSIKP 4911
Cdd:PRK08439   257 --IGFGESGDANHITSPAPEGPLRAMKAAL-EMAGNPK-IDYINAHGTSTPYNDKNETAALKELFGSKEKVPP-VSSTKG 331
                          330       340
                   ....*....|....*....|.
gi 1776025254 4912 NIGHPLCAEG-IASFIKVVLM 4931
Cdd:PRK08439   332 QIGHCLGAAGaIEAVISIMAM 352
PLN02330 PLN02330
4-coumarate--CoA ligase-like 1
1153-1640 2.89e-12

4-coumarate--CoA ligase-like 1


Pssm-ID: 215189 [Multi-domain]  Cd Length: 546  Bit Score: 73.09  E-value: 2.89e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1153 ITFHELFEQQAKKTPDRAAV--SYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAY 1230
Cdd:PLN02330    28 LTLPDFVLQDAELYADKVAFveAVTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVF 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1231 VPLDPSYPAERLEYMLEDSEVFITLTTSELVNTLSWNGVTTALLDQ-------DWDEIAQtASDR---KVLTRTVTPENL 1300
Cdd:PLN02330   108 SGANPTALESEIKKQAEAAGAKLIVTNDTNYGKVKGLGLPVIVLGEekiegavNWKELLE-AADRagdTSDNEEILQTDL 186
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1301 AYVIYTSGSTGKPKGVMIPHKALTNFLVS---------MGE--TPGLTAEDKMLAVTTYCFD----------IAALEL-- 1357
Cdd:PLN02330   187 CALPFSSGTTGISKGVMLTHRNLVANLCSslfsvgpemIGQvvTLGLIPFFHIYGITGICCAtlrnkgkvvvMSRFELrt 266
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1358 -----------FLPLIKGAHCYICQTEHTK--DVEKLKrdirtIKPTVMQATPATWKMLfySGWENEenvkilcggeaLP 1424
Cdd:PLN02330   267 flnalitqevsFAPIVPPIILNLVKNPIVEefDLSKLK-----LQAIMTAAAPLAPELL--TAFEAK-----------FP 328
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1425 etlkryfldtGSEAWNMFGPTETTIWSAVQRINDE----CSRATIGRPIANTQIYITDSQLA-PVPAGVPGELCIAGDGV 1499
Cdd:PLN02330   329 ----------GVQVQEAYGLTEHSCITLTHGDPEKghgiAKKNSVGFILPNLEVKFIDPDTGrSLPKNTPGELCVRSQCV 398
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1500 AKGYYKKEELTDsrfidnpfepgsklyRTGDMARWLPGGRIEYIG---------RIDNQVKIRGFRIELGDIESRLSEHP 1570
Cdd:PLN02330   399 MQGYYNNKEETD---------------RTIDEDGWLHTGDIGYIDddgdifivdRIKELIKYKGFQVAPAELEAILLTHP 463
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1776025254 1571 GILECVVVADMDNLAAYYTAKHANASLTARE----LRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLKN 1640
Cdd:PLN02330   464 SVEDAAVVPLPDEEAGEIPAACVVINPKAKEseedILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKE 537
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
3219-3274 4.50e-12

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.


Pssm-ID: 425746 [Multi-domain]  Cd Length: 62  Bit Score: 63.74  E-value: 4.50e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1776025254 3219 NMVSAILKVNSEDIDVNTELSEYGFDSVTFTVFTNKINEEFQLELTPTIFFEYGSI 3274
Cdd:pfam00550    5 ELLAEVLGVPAEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTL 60
MACS_AAE_MA_like cd05970
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ...
159-555 5.00e-12

Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.


Pssm-ID: 341274 [Multi-domain]  Cd Length: 537  Bit Score: 72.14  E-value: 5.00e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  159 QGLEGFRAIIVEDLLSAEADTDWHQSSPEDLALLLLTSGSTGTPKavMLNHRNIMSMvkGIIQMQGFtreditfnWMPFD 238
Cdd:cd05970    157 EGWIDFRKLIKNASPDFERPTANSYPCGEDILLVYFSSGTTGMPK--MVEHDFTYPL--GHIVTAKY--------WQNVR 224
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  239 HVGgigmLHLR------------DVY----LGCQEINVSSEtiLMEPLKWLDWIDHYRASVTWAPN--FAFGLVTDFAee 300
Cdd:cd05970    225 EGG----LHLTvadtgwgkavwgKIYgqwiAGAAVFVYDYD--KFDPKALLEKLSKYGVTTFCAPPtiYRFLIREDLS-- 296
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  301 ikdrKWDLSSMRYMLNGGEAMVAKVGRRILELLephGLpadAIRPAWGMSETSSGV-IFSHEFTRAGTsdddhfveIGSP 379
Cdd:cd05970    297 ----RYDLSSLRYCTTAGEALNPEVFNTFKEKT---GI---KLMEGFGQTETTLTIaTFPWMEPKPGS--------MGKP 358
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  380 IPGFSMRIVnDHN----ELVEEGEIGRFQVSGLSVT--SGYYQRPDLNESVFtEDGWFETGDLGFL-RNGRLTITGRTKD 452
Cdd:cd05970    359 APGYEIDLI-DREgrscEAGEEGEIVIRTSKGKPVGlfGGYYKDAEKTAEVW-HDGYYHTGDAAWMdEDGYLWFVGRTDD 436
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  453 AIIINGINYYSHAIESA-VEELSEIETSYTAACAVRLGQnstdQLAIFFVTSAklnDEQMSQLLRN-IQSHVSQvigVTP 530
Cdd:cd05970    437 LIKSSGYRIGPFEVESAlIQHPAVLECAVTGVPDPIRGQ----VVKATIVLAK---GYEPSEELKKeLQDHVKK---VTA 506
                          410       420
                   ....*....|....*....|....*...
gi 1776025254  531 EYLLPVQKE---EIPKTAIGKIQRTQLK 555
Cdd:cd05970    507 PYKYPRIVEfvdELPKTISGKIRRVEIR 534
PLN02654 PLN02654
acetate-CoA ligase
1168-1641 5.03e-12

acetate-CoA ligase


Pssm-ID: 215353 [Multi-domain]  Cd Length: 666  Bit Score: 72.62  E-value: 5.03e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1168 DRAAVSYEGQ------TLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAER 1241
Cdd:PLN02654   104 DKIAIYWEGNepgfdaSLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAES 183
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1242 LEYMLEDSEVFITLTTSEL---VNTLSWNGVTTALLDQDWDE-----IAQTASDRKVLTRTVTP---------------- 1297
Cdd:PLN02654   184 LAQRIVDCKPKVVITCNAVkrgPKTINLKDIVDAALDESAKNgvsvgICLTYENQLAMKREDTKwqegrdvwwqdvvpny 263
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1298 -----------ENLAYVIYTSGSTGKPKGVMipHK-------ALTNFLVSMGETPG----LTAEDKMLAVTTYCfdiaal 1355
Cdd:PLN02654   264 ptkcevewvdaEDPLFLLYTSGSTGKPKGVL--HTtggymvyTATTFKYAFDYKPTdvywCTADCGWITGHSYV------ 335
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1356 eLFLPLIKGAHCYICQ-TEHTKDVEKLKRDIRTIKPTVMQATPATWKMLFYSGWE-----NEENVKILCG-GEALPETLK 1428
Cdd:PLN02654   336 -TYGPMLNGATVLVFEgAPNYPDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDEyvtrhSRKSLRVLGSvGEPINPSAW 414
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1429 RYFLDTG-------SEAWnmfGPTET---TIWSAVQRINDECSRATIgrPIANTQIYITDSQLAPVPAGVPGELCIAGD- 1497
Cdd:PLN02654   415 RWFFNVVgdsrcpiSDTW---WQTETggfMITPLPGAWPQKPGSATF--PFFGVQPVIVDEKGKEIEGECSGYLCVKKSw 489
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1498 -GVAKGYYKKEEltdsRFIDNPFEPGSKLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECV 1576
Cdd:PLN02654   490 pGAFRTLYGDHE----RYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAA 565
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1776025254 1577 VVA---DMDNLAAYYTAKHANASLTARELRH----FVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLKNI 1641
Cdd:PLN02654   566 VVGiehEVKGQGIYAFVTLVEGVPYSEELRKslilTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKI 637
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
592-666 5.73e-12

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 64.10  E-value: 5.73e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1776025254  592 REEIQEHLLTCLTEELHVSRDWVEPNAN-IQSLGVNSIKMMKLIRSIEKNYHIKLTAREIHQYPTIERLASYLSEH 666
Cdd:COG0236      3 REELEERLAEIIAEVLGVDPEEITPDDSfFEDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEEK 78
PRK08043 PRK08043
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
49-516 5.73e-12

bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;


Pssm-ID: 181207 [Multi-domain]  Cd Length: 718  Bit Score: 72.44  E-value: 5.73e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254   49 IYLQPDgtevyqSYRRLWDDGL---RIVKGLRQSGlkakQSVILQLGDNSQLLPAFWGCVLTGVVPAPLavppTYaesSS 125
Cdd:PRK08043   227 VNFTPD------SYRKLLKKTLfvgRILEKYSVEG----ERIGLMLPNATISAAVIFGASLRRRIPAMM----NY---TA 289
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  126 GTQKLKDAWTLLDKPAVITDRGMHQEMLDWAKEQGLEGFRAIIVEDLLSAEADTD-----WH---------QSSPEDLAL 191
Cdd:PRK08043   290 GVKGLTSAITAAEIKTIFTSRQFLDKGKLWHLPEQLTQVRWVYLEDLKDDVTTADklwifAHllmprlaqvKQQPEDAAL 369
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  192 LLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDHVGGIGMLHLRDVYLGcqeinvsSETILM-EPL 270
Cdd:PRK08043   370 ILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRFMSALPLFHSFGLTVGLFTPLLTG-------AEVFLYpSPL 442
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  271 kwldwidHYR----------ASVTWAPNFAFGLVTDFAEeikdrKWDLSSMRYMLNGGEAMVA--------KVGRRILEl 332
Cdd:PRK08043   443 -------HYRivpelvydrnCTVLFGTSTFLGNYARFAN-----PYDFARLRYVVAGAEKLQEstkqlwqdKFGLRILE- 509
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  333 lephglpadairpAWGMSETSSGV-IFSHEFTRAGTsdddhfveIGSPIPGFSMRIVNDHNelVEEGeiGRFQVSGLSVT 411
Cdd:PRK08043   510 -------------GYGVTECAPVVsINVPMAAKPGT--------VGRILPGMDARLLSVPG--IEQG--GRLQLKGPNIM 564
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  412 SGYY--QRPDL-------NESVFTEDGWFETGDLGFL-RNGRLTITGRTKDAIIINGINYyshAIESaVEELS-EIETSY 480
Cdd:PRK08043   565 NGYLrvEKPGVlevptaeNARGEMERGWYDTGDIVRFdEQGFVQIQGRAKRFAKIAGEMV---SLEM-VEQLAlGVSPDK 640
                          490       500       510
                   ....*....|....*....|....*....|....*.
gi 1776025254  481 TAACAVRLGQNSTDQLaIFFVTSAKLNDEQMSQLLR 516
Cdd:PRK08043   641 QHATAIKSDASKGEAL-VLFTTDSELTREKLQQYAR 675
PLN02387 PLN02387
long-chain-fatty-acid-CoA ligase family protein
173-452 6.26e-12

long-chain-fatty-acid-CoA ligase family protein


Pssm-ID: 215217 [Multi-domain]  Cd Length: 696  Bit Score: 72.46  E-value: 6.26e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  173 LSAEADTDWHQSSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQ-MQGFTREDITFNWMPFDHV----------- 240
Cdd:PLN02387   236 LGKENPVDPDLPSPNDIAVIMYTSGSTGLPKGVMMTHGNIVATVAGVMTvVPKLGKNDVYLAYLPLAHIlelaaesvmaa 315
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  241 --GGIGM---LHLRD----VYLGCQ-EINVSSETILMEPLKWLDWI-DHYRASVTWAPNFAFGLVtDFAeeIKDR----- 304
Cdd:PLN02387   316 vgAAIGYgspLTLTDtsnkIKKGTKgDASALKPTLMTAVPAILDRVrDGVRKKVDAKGGLAKKLF-DIA--YKRRlaaie 392
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  305 -----KWDLSSM------------------RYMLNGGEAMVAKVGRRILELLephGLPadaIRPAWGMSETSSGVIFShE 361
Cdd:PLN02387   393 gswfgAWGLEKLlwdalvfkkiravlggriRFMLSGGAPLSGDTQRFINICL---GAP---IGQGYGLTETCAGATFS-E 465
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  362 FtragtsDDDHFVEIGSPIPGFSMRIVN--DHNELVEE-----GEIgrfQVSGLSVTSGYYQRPDLNESVFTEDG----W 430
Cdd:PLN02387   466 W------DDTSVGRVGPPLPCCYVKLVSweEGGYLISDkpmprGEI---VIGGPSVTLGYFKNQEKTDEVYKVDErgmrW 536
                          330       340
                   ....*....|....*....|...
gi 1776025254  431 FETGDLG-FLRNGRLTITGRTKD 452
Cdd:PLN02387   537 FYTGDIGqFHPDGCLEIIDRKKD 559
ttLC_FACS_AEE21_like cd12118
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ...
170-556 7.74e-12

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.


Pssm-ID: 341283 [Multi-domain]  Cd Length: 486  Bit Score: 71.56  E-value: 7.74e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  170 EDLL-SAEADTDWHQSSPEDLALLL-LTSGSTGTPKAVMLNHRNIMSMVKGII---QMQG----------FTREDITFNW 234
Cdd:cd12118    114 EDLLaEGDPDFEWIPPADEWDPIALnYTSGTTGRPKGVVYHHRGAYLNALANIlewEMKQhpvylwtlpmFHCNGWCFPW 193
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  235 MpfdhVGGIGMLH--LRdvylgcqeiNVSSETILmeplkwlDWIDHYRasVTW---APNfAFGLVTDFAEEIKDRkwdLS 309
Cdd:cd12118    194 T----VAAVGGTNvcLR---------KVDAKAIY-------DLIEKHK--VTHfcgAPT-VLNMLANAPPSDARP---LP 247
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  310 SMRYMLNGGEAMVAKVgrriLELLEPHGLpadAIRPAWGMSETSsGVIFSHEFTRA--GTSDDDHFVEI---GSPIPGFS 384
Cdd:cd12118    248 HRVHVMTAGAPPPAAV----LAKMEELGF---DVTHVYGLTETY-GPATVCAWKPEwdELPTEERARLKarqGVRYVGLE 319
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  385 MRIVNDHNELVE---EGE-IGRFQVSGLSVTSGYYQRPDLNESVFtEDGWFETGDLGFLR-NGRLTITGRTKDAIIINGI 459
Cdd:cd12118    320 EVDVLDPETMKPvprDGKtIGEIVFRGNIVMKGYLKNPEATAEAF-RGGWFHSGDLAVIHpDGYIEIKDRSKDIIISGGE 398
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  460 NYYSHAIESAVEELSEI-ETSYTAACAVRLGQNSTDqlaifFVT---SAKLNDEQMSQLLRNIQSHvsqvigvtpeYLLP 535
Cdd:cd12118    399 NISSVEVEGVLYKHPAVlEAAVVARPDEKWGEVPCA-----FVElkeGAKVTEEEIIAFCREHLAG----------FMVP 463
                          410       420
                   ....*....|....*....|...
gi 1776025254  536 --VQKEEIPKTAIGKIQRTQLKT 556
Cdd:cd12118    464 ktVVFGELPKTSTGKIQKFVLRD 486
PRK07008 PRK07008
long-chain-fatty-acid--CoA ligase; Validated
170-567 1.20e-11

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235908 [Multi-domain]  Cd Length: 539  Bit Score: 70.89  E-value: 1.20e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  170 EDLLSAE-ADTDWHQSSPEDLALLLLTSGSTGTPKAVMLNHRNIM--SMVKGIIQMQGFTREDITFNWMPFDHVGGIGML 246
Cdd:PRK07008   158 ETLVGAQdGDYDWPRFDENQASSLCYTSGTTGNPKGALYSHRSTVlhAYGAALPDAMGLSARDAVLPVVPMFHVNAWGLP 237
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  247 HlrDVYL-GCQeinvssetiLMEPLKWLDWIDHYR----ASVTWA---PNFAFGLVTdfaeEIKDRKWDLSSMRYMLNGG 318
Cdd:PRK07008   238 Y--SAPLtGAK---------LVLPGPDLDGKSLYElieaERVTFSagvPTVWLGLLN----HMREAGLRFSTLRRTVIGG 302
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  319 ----EAMVakvgrRILEllEPHGLpadAIRPAWGMSETSS-GVIFSHEFTRAGTSDDD--HFVEI-GSPIPGFSMRIVN- 389
Cdd:PRK07008   303 sacpPAMI-----RTFE--DEYGV---EVIHAWGMTEMSPlGTLCKLKWKHSQLPLDEqrKLLEKqGRVIYGVDMKIVGd 372
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  390 DHNELVEEGE-IGRFQVSGLSVTSGYYQrpdlNESVFTEDGWFETGDLGFL-RNGRLTITGRTKDaiiinginyyshAIE 467
Cdd:PRK07008   373 DGRELPWDGKaFGDLQVRGPWVIDRYFR----GDASPLVDGWFPTGDVATIdADGFMQITDRSKD------------VIK 436
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  468 SAVEELSEIETS---------YTAACaVRLGQNSTDQLAIFFVT---SAKLNDEQMSQLLRniqshvsqviGVTPEYLLP 535
Cdd:PRK07008   437 SGGEWISSIDIEnvavahpavAEAAC-IACAHPKWDERPLLVVVkrpGAEVTREELLAFYE----------GKVAKWWIP 505
                          410       420       430
                   ....*....|....*....|....*....|....*
gi 1776025254  536 ---VQKEEIPKTAIGKIQRTQLKTSFEngefDHLL 567
Cdd:PRK07008   506 ddvVFVDAIPHTATGKLQKLKLREQFR----DYVL 536
PRK06501 PRK06501
beta-ketoacyl-ACP synthase;
4722-4921 1.27e-11

beta-ketoacyl-ACP synthase;


Pssm-ID: 235817 [Multi-domain]  Cd Length: 425  Bit Score: 70.43  E-value: 1.27e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4722 AANLSQFFDVRGPSVVVDTACSSALVGMNMAIQALRGGDIQSAIV----GGV--------SLLSSDASHRlfDRRGILSK 4789
Cdd:PRK06501   155 ADRLADRFGTRGLPISLSTACASGATAIQLGVEAIRRGETDRALCiatdGSVsaealirfSLLSALSTQN--DPPEKASK 232
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4790 HssfhvFDERADGVVLGEGVGMVMLKTVKQALEDGDTIYAVVKAASVNNDG--RT-----AGPATpnleaqkEVMKDALF 4862
Cdd:PRK06501   233 P-----FSKDRDGFVMAEGAGALVLESLESAVARGAKILGIVAGCGEKADSfhRTrsspdGSPAI-------GAIRAALA 300
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1776025254 4863 KSGKKPEDISYLEANGSGSIVTDLLELKAIQSVY--RSGHsSPLSlgSIKPNIGHPLCAEG 4921
Cdd:PRK06501   301 DAGLTPEQIDYINAHGTSTPENDKMEYLGLSAVFgeRLAS-IPVS--SNKSMIGHTLTAAG 358
PRK09185 PRK09185
beta-ketoacyl-ACP synthase;
4721-4988 1.61e-11

beta-ketoacyl-ACP synthase;


Pssm-ID: 236398 [Multi-domain]  Cd Length: 392  Bit Score: 69.87  E-value: 1.61e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4721 LAANLSQFFDVRGPSVVVDTAC-SSALVGMNmAIQALRGGDIQSAIVGGVSLLSsdashRL----FDRRGILSKHssfHV 4795
Cdd:PRK09185   139 LADFLRAYLGLSGPAYTISTACsSSAKVFAS-ARRLLEAGLCDAAIVGGVDSLC-----RLtlngFNSLESLSPQ---PC 209
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4796 --FDERADGVVLGEGVG-MVMLKTVKQAL------EDGDtiyavvkA---ASVNNDGRTAgpatpnleaqKEVMKDALFK 4863
Cdd:PRK09185   210 rpFSANRDGINIGEAAAfFLLEREDDAAVallgvgESSD-------AhhmSAPHPEGLGA----------ILAMQQALAD 272
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4864 SGKKPEDISYLEANGSGSIVTDLLELKAIQSVYrsGHSSPLSlgSIKPNIGHPLCAEGI--ASFIKVVLmlkERRFVPfl 4941
Cdd:PRK09185   273 AGLAPADIGYINLHGTATPLNDAMESRAVAAVF--GDGVPCS--STKGLTGHTLGAAGAveAAICWLAL---RHGLPP-- 343
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1776025254 4942 sgekemAHFDQQKANITFsrALEKWTDSQPTAAI-----NCFADGGTNVHVI 4988
Cdd:PRK09185   344 ------HGWNTGQPDPAL--PPLYLVENAQALAIryvlsNSFAFGGNNCSLI 387
MACS_like_2 cd05973
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
187-555 1.69e-11

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341277 [Multi-domain]  Cd Length: 437  Bit Score: 70.24  E-value: 1.69e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  187 EDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITfnWMPFDHVGGIGMLhlrdvYLGCQEINVSSETIL 266
Cdd:cd05973     88 SDPFVMMFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPEDSF--WNAADPGWAYGLY-----YAITGPLALGHPTIL 160
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  267 ME-----PLKWLDWIDHYRASVTWAPNFAFGLVTDFAEEIKDRKwdlSSMRYMLNGGEAMVAKVGRRILELLephGLPad 341
Cdd:cd05973    161 LEggfsvESTWRVIERLGVTNLAGSPTAYRLLMAAGAEVPARPK---GRLRRVSSAGEPLTPEVIRWFDAAL---GVP-- 232
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  342 aIRPAWGMSETSSGVIFSHEftragtsdDDHFVEIGS---PIPGFSMRIVNDHNELVEEGEIGRFQV----SGLSVTSGY 414
Cdd:cd05973    233 -IHDHYGQTELGMVLANHHA--------LEHPVHAGSagrAMPGWRVAVLDDDGDELGPGEPGRLAIdianSPLMWFRGY 303
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  415 YQRPDLNESvfteDGWFETGDLG-FLRNGRLTITGRTKDAIIINGINYYSHAIESAVeelseIETSYTAACAV--RLGQN 491
Cdd:cd05973    304 QLPDTPAID----GGYYLTGDTVeFDPDGSFSFIGRADDVITMSGYRIGPFDVESAL-----IEHPAVAEAAVigVPDPE 374
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1776025254  492 STDQLAIFFVTSAklNDEQMSQLLRNIQSHVSQVIGV-----TPEYLlpvqkEEIPKTAIGKIQRTQLK 555
Cdd:cd05973    375 RTEVVKAFVVLRG--GHEGTPALADELQLHVKKRLSAhayprTIHFV-----DELPKTPSGKIQRFLLR 436
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
4465-4525 2.21e-11

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.


Pssm-ID: 425746 [Multi-domain]  Cd Length: 62  Bit Score: 61.81  E-value: 2.21e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1776025254 4465 SWLIDLFTEELRIDREDFEIDGLFQDYGVDSIILAQVLQRINRKLEAALDPSILYEYPTIQ 4525
Cdd:pfam00550    1 ERLRELLAEVLGVPAEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLA 61
PLN02246 PLN02246
4-coumarate--CoA ligase
71-561 2.27e-11

4-coumarate--CoA ligase


Pssm-ID: 215137 [Multi-domain]  Cd Length: 537  Bit Score: 70.01  E-value: 2.27e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254   71 RIVKGLRQSGLKaKQSVILQLGDNS-QLLPAFWGCVLTGVVPA---PLAVPPTYAE--SSSG-----TQ-----KLKDAW 134
Cdd:PLN02246    62 RVAAGLHKLGIR-QGDVVMLLLPNCpEFVLAFLGASRRGAVTTtanPFYTPAEIAKqaKASGakliiTQscyvdKLKGLA 140
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  135 TLLDKPAVITDRGmhqemldwakEQGLEGFRaiivEDLLSAEADTDWHQSSPEDLALLLLTSGSTGTPKAVMLNHRNIMS 214
Cdd:PLN02246   141 EDDGVTVVTIDDP----------PEGCLHFS----ELTQADENELPEVEISPDDVVALPYSSGTTGLPKGVMLTHKGLVT 206
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  215 MVKGiiQMQG------FTREDITFNWMPFDHV---GGIGMLHLRdvylgcqeinVSSETILM---EPLKWLDWIDHYRas 282
Cdd:PLN02246   207 SVAQ--QVDGenpnlyFHSDDVILCVLPMFHIyslNSVLLCGLR----------VGAAILIMpkfEIGALLELIQRHK-- 272
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  283 VTWAPnFAFGLVTDFAEEIKDRKWDLSSMRYMLNGGeamvAKVGRRILELLEPHgLPADAIRPAWGMSETSSGVIFSHEF 362
Cdd:PLN02246   273 VTIAP-FVPPIVLAIAKSPVVEKYDLSSIRMVLSGA----APLGKELEDAFRAK-LPNAVLGQGYGMTEAGPVLAMCLAF 346
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  363 TR---------AGTSDDDHFVEIGSPIPGFSMRivndHNelvEEGEIGrfqVSGLSVTSGYYQRPDLNESVFTEDGWFET 433
Cdd:PLN02246   347 AKepfpvksgsCGTVVRNAELKIVDPETGASLP----RN---QPGEIC---IRGPQIMKGYLNDPEATANTIDKDGWLHT 416
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  434 GDLGFL-RNGRLTITGRTKDAIIINGinyyshaIESAVEELSEIETSYTA---ACAVRLGQNSTDQLAIFFVtsAKLNDE 509
Cdd:PLN02246   417 GDIGYIdDDDELFIVDRLKELIKYKG-------FQVAPAELEALLISHPSiadAAVVPMKDEVAGEVPVAFV--VRSNGS 487
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1776025254  510 QMSQllRNIQSHVS-QVIgvtpeYLLPVQK----EEIPKTAIGKIQRTQLKTSFENG 561
Cdd:PLN02246   488 EITE--DEIKQFVAkQVV-----FYKRIHKvffvDSIPKAPSGKILRKDLRAKLAAG 537
PRK06814 PRK06814
acyl-[ACP]--phospholipid O-acyltransferase;
1297-1634 2.71e-11

acyl-[ACP]--phospholipid O-acyltransferase;


Pssm-ID: 235865 [Multi-domain]  Cd Length: 1140  Bit Score: 70.76  E-value: 2.71e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1297 PENLAYVIYTSGSTGKPKGVMIPHKA-LTNFLVSMGETPgLTAEDKMLAVTT--YCFDIAAlELFLPLIKGAHCYICQTE 1373
Cdd:PRK06814   792 PDDPAVILFTSGSEGTPKGVVLSHRNlLANRAQVAARID-FSPEDKVFNALPvfHSFGLTG-GLVLPLLSGVKVFLYPSP 869
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1374 -HTKDVEKLkrdIRTIKPTVMQATPAtwkmlFYSGWENEENV-------KILCGGEALPETLKRYFLDT-GSEAWNMFGP 1444
Cdd:PRK06814   870 lHYRIIPEL---IYDTNATILFGTDT-----FLNGYARYAHPydfrslrYVFAGAEKVKEETRQTWMEKfGIRILEGYGV 941
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1445 TETtiwSAVQRINDEC-SRA-TIGRPIANTqiyitDSQLAPVPaGVP--GELCIAGDGVAKGYYKKEeltdsrfidNPF- 1519
Cdd:PRK06814   942 TET---APVIALNTPMhNKAgTVGRLLPGI-----EYRLEPVP-GIDegGRLFVRGPNVMLGYLRAE---------NPGv 1003
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1520 --EPGSKLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSE-HPGILECVV-VADM---DNLAAYYTAKH 1592
Cdd:PRK06814  1004 lePPADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAElWPDALHAAVsIPDArkgERIILLTTASD 1083
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|..
gi 1776025254 1593 ANAsltARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKID 1634
Cdd:PRK06814  1084 ATR---AAFLAHAKAAGASELMVPAEIITIDEIPLLGTGKID 1122
PLN02614 PLN02614
long-chain acyl-CoA synthetase
186-498 2.74e-11

long-chain acyl-CoA synthetase


Pssm-ID: 166255 [Multi-domain]  Cd Length: 666  Bit Score: 70.05  E-value: 2.74e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  186 PEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQG-----FTREDITFNWMPFDHV-------------GGIGMLH 247
Cdd:PLN02614   222 KSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLKsanaaLTVKDVYLSYLPLAHIfdrvieecfiqhgAAIGFWR 301
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  248 lRDVYLGCQEINVSSETILMEPLKWLDWI-----------DHYRASV-TWAPNFAFGLV---------TDFAEEI---KD 303
Cdd:PLN02614   302 -GDVKLLIEDLGELKPTIFCAVPRVLDRVysglqkklsdgGFLKKFVfDSAFSYKFGNMkkgqshveaSPLCDKLvfnKV 380
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  304 RKWDLSSMRYMLNGGEAMVAKVGRRILELLEPHGLPAdairpaWGMSETSSG--VIFSHEFTRAGTsdddhfveIGSPIP 381
Cdd:PLN02614   381 KQGLGGNVRIILSGAAPLASHVESFLRVVACCHVLQG------YGLTESCAGtfVSLPDELDMLGT--------VGPPVP 446
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  382 GFSMRIvndhnELVEEGEI--------GRFQVSGLSVTSGYYQRPDLNESVFTeDGWFETGDLG-FLRNGRLTITGRTKD 452
Cdd:PLN02614   447 NVDIRL-----ESVPEMEYdalastprGEICIRGKTLFSGYYKREDLTKEVLI-DGWLHTGDVGeWQPNGSMKIIDRKKN 520
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 1776025254  453 AIIINGINYYshaiesAVEELSEIETSYTAACAVRLGQNSTDQLAI 498
Cdd:PLN02614   521 IFKLSQGEYV------AVENIENIYGEVQAVDSVWVYGNSFESFLV 560
PLN02861 PLN02861
long-chain-fatty-acid-CoA ligase
188-452 3.08e-11

long-chain-fatty-acid-CoA ligase


Pssm-ID: 178452 [Multi-domain]  Cd Length: 660  Bit Score: 69.87  E-value: 3.08e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  188 DLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQM-----QGFTREDITFNWMPFDHV-------------GGIGMLH-- 247
Cdd:PLN02861   221 DICTIMYTSGTTGEPKGVILTNRAIIAEVLSTDHLlkvtdRVATEEDSYFSYLPLAHVydqvietyciskgASIGFWQgd 300
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  248 ----LRDV------------------YLGCQEiNVSSETILMEPLkwLDWIDHYRASvtwapNFAFGLVTDFAEEIKDR- 304
Cdd:PLN02861   301 irylMEDVqalkptifcgvprvydriYTGIMQ-KISSGGMLRKKL--FDFAYNYKLG-----NLRKGLKQEEASPRLDRl 372
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  305 -----KWDLSS-MRYMLNGGeamvAKVGRRILELLEPhgLPADAIRPAWGMSETSSGVIFS--HEFTRAGTsdddhfveI 376
Cdd:PLN02861   373 vfdkiKEGLGGrVRLLLSGA----APLPRHVEEFLRV--TSCSVLSQGYGLTESCGGCFTSiaNVFSMVGT--------V 438
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  377 GSPIPGFSMRIVN------DHNELVEEGEIGrfqVSGLSVTSGYYQRPDLNESVFTeDGWFETGDLGFLR-NGRLTITGR 449
Cdd:PLN02861   439 GVPMTTIEARLESvpemgyDALSDVPRGEIC---LRGNTLFSGYHKRQDLTEEVLI-DGWFHTGDIGEWQpNGAMKIIDR 514

                   ...
gi 1776025254  450 TKD 452
Cdd:PLN02861   515 KKN 517
ACSBG_like cd05933
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ...
185-472 3.23e-11

Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341256 [Multi-domain]  Cd Length: 596  Bit Score: 69.69  E-value: 3.23e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  185 SPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFT----REDITFNWMPFDHVGgIGMLhlrDVYLGcqeINV 260
Cdd:cd05933    148 KPNQCCTLIYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLRpatvGQESVVSYLPLSHIA-AQIL---DIWLP---IKV 220
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  261 SSETILMEP--LKW--------------------------------LDWIDHYRASVTWAPNFafGLVTDFAEEIKDRKw 306
Cdd:cd05933    221 GGQVYFAQPdaLKGtlvktlrevrptafmgvprvwekiqekmkavgAKSGTLKRKIASWAKGV--GLETNLKLMGGESP- 297
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  307 dlSSMRYMLngGEAMVAKVGRRILELLEPH-------GLPAD----------AIRPAWGMSETSSgvifSHEFTRagtSD 369
Cdd:cd05933    298 --SPLFYRL--AKKLVFKKVRKALGLDRCQkfftgaaPISREtlefflslniPIMELYGMSETSG----PHTISN---PQ 366
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  370 DDHFVEIGSPIPGFSMRIVNDHNElveegEIGRFQVSGLSVTSGYYQRPDLNESVFTEDGWFETGDLGFL-RNGRLTITG 448
Cdd:cd05933    367 AYRLLSCGKALPGCKTKIHNPDAD-----GIGEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLdEDGFLYITG 441
                          330       340
                   ....*....|....*....|....*
gi 1776025254  449 RTKDAIII-NGINYYSHAIESAVEE 472
Cdd:cd05933    442 RIKELIITaGGENVPPVPIEDAVKK 466
PLN02860 PLN02860
o-succinylbenzoate-CoA ligase
1251-1658 3.37e-11

o-succinylbenzoate-CoA ligase


Pssm-ID: 215464 [Multi-domain]  Cd Length: 563  Bit Score: 69.83  E-value: 3.37e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1251 VFITLTTSELVNTLSwNGVTTalldqdwDEIAQTASDRKVLTRTVTPENLAYVIYTSGSTGKPKGVMIPHKALTNFLVSM 1330
Cdd:PLN02860   133 VFLESPSSSVFIFLN-SFLTT-------EMLKQRALGTTELDYAWAPDDAVLICFTSGTTGRPKGVTISHSALIVQSLAK 204
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1331 GETPGLTAEDKMLAVTTYCfDIAALE--LFLPLIKGAHCYICQTEHTKDVEKLKRDIRT---IKPTVMQ------ATPAT 1399
Cdd:PLN02860   205 IAIVGYGEDDVYLHTAPLC-HIGGLSsaLAMLMVGACHVLLPKFDAKAALQAIKQHNVTsmiTVPAMMAdlisltRKSMT 283
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1400 WKmlfysgwENEENVKILCGGEALPETL----KRYFldTGSEAWNMFGPTETTIWSAVQRINDecsrATIGRPIANTQIY 1475
Cdd:PLN02860   284 WK-------VFPSVRKILNGGGSLSSRLlpdaKKLF--PNAKLFSAYGMTEACSSLTFMTLHD----PTLESPKQTLQTV 350
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1476 I-TDSQLAPVPAGV----PG---ELCIAGDG-------VAKGYYkkeelTDSRFIDNPFEPGSKLYR-----TGDMARWL 1535
Cdd:PLN02860   351 NqTKSSSVHQPQGVcvgkPAphvELKIGLDEssrvgriLTRGPH-----VMLGYWGQNSETASVLSNdgwldTGDIGWID 425
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1536 PGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMD-------------------NLAAYYTAKHaNAS 1596
Cdd:PLN02860   426 KAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDsrltemvvacvrlrdgwiwSDNEKENAKK-NLT 504
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1776025254 1597 LTARELRHFV-KNALPAYMVPSYFIQL-DHMPLTPNGKIDRNSLKnidlsGEQLKQRQTSPKNI 1658
Cdd:PLN02860   505 LSSETLRHHCrEKNLSRFKIPKLFVQWrKPFPLTTTGKIRRDEVR-----REVLSHLQSLPSNL 563
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
2852-3020 3.39e-11

human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid dehydrogenases (17betaHSD) are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. 17betaHSD type XI, a classical SDR, preferentially converts 3alpha-Adiol to androsterone but not numerous other tested steroids. This subgroup of classical SDRs also includes members identified as retinol dehydrogenases, which convert retinol to retinal, a property that overlaps with 17betaHSD activity. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187598 [Multi-domain]  Cd Length: 243  Bit Score: 66.88  E-value: 3.39e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2852 LITGGAGSLGLLFAKEIANRtgRSTIVLTGRSVLSEDKENELeaLRSIGAEVVYREADVSDQHAVHHLFEEIKERYGTLN 2931
Cdd:cd05339      3 LITGGGSGIGRLLALEFAKR--GAKVVILDINEKGAEETANN--VRKAGGKVHYYKCDVSKREEVYEAAKKIKKEVGDVT 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2932 GIIHGAGSIKDHFIIHKTNEEFQEVLqpKVSGLLHVDECSKDFPL------DFFIFFSSVSGCLGNAGQADYAAANSFMD 3005
Cdd:cd05339     79 ILINNAGVVSGKKLLELPDEEIEKTF--EVNTLAHFWTTKAFLPDmlernhGHIVTIASVAGLISPAGLADYCASKAAAV 156
                          170
                   ....*....|....*.
gi 1776025254 3006 AFAE-YRRSLAASKKR 3020
Cdd:cd05339    157 GFHEsLRLELKAYGKP 172
PRK07967 PRK07967
beta-ketoacyl-ACP synthase I;
4722-4994 4.66e-11

beta-ketoacyl-ACP synthase I;


Pssm-ID: 181184 [Multi-domain]  Cd Length: 406  Bit Score: 68.54  E-value: 4.66e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4722 AANLSQFFDVRGPSVVVDTACSSALVGMNMAIQALRGG--DIQSAivGGVSLLSSDASHrLFDRRGILSK------HSSF 4793
Cdd:PRK07967   142 SACLATPFKIKGVNYSISSACATSAHCIGNAVEQIQLGkqDIVFA--GGGEELDWEMSC-LFDAMGALSTkyndtpEKAS 218
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4794 HVFDERADGVVLGEGVGMVMLKTVKQALEDGDTIYAVVKAASVNNDGrtAGPATPNLEAQKEVMKDALfkSGKKpEDISY 4873
Cdd:PRK07967   219 RAYDANRDGFVIAGGGGVVVVEELEHALARGAKIYAEIVGYGATSDG--YDMVAPSGEGAVRCMQMAL--ATVD-TPIDY 293
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4874 LEANGSGSIVTDLLELKAIQSVYrsGHSSPlSLGSIKPNIGHPLCAEGIASFIKVVLMLKERrfvpFLSGEKEMAHFDQQ 4953
Cdd:PRK07967   294 INTHGTSTPVGDVKELGAIREVF--GDKSP-AISATKSLTGHSLGAAGVQEAIYSLLMMEHG----FIAPSANIEELDPQ 366
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1776025254 4954 KANITFSRaleKWTDSQP--TAAINCFADGGTNVHVIVEAWEK 4994
Cdd:PRK07967   367 AAGMPIVT---ETTDNAEltTVMSNSFGFGGTNATLVFRRYKG 406
PRK07910 PRK07910
beta-ketoacyl-ACP synthase;
4740-4934 4.89e-11

beta-ketoacyl-ACP synthase;


Pssm-ID: 236129 [Multi-domain]  Cd Length: 418  Bit Score: 68.60  E-value: 4.89e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4740 TACSSALVGMNMAIQALRGGDIQSAIVGGVSLLSSDASHRLFDR-RGILSKHS-----SFHVFDERADGVVLGEGVGMVM 4813
Cdd:PRK07910   169 SACASGSEAIAQAWRQIVLGEADIAICGGVETRIEAVPIAGFAQmRIVMSTNNddpagACRPFDKDRDGFVFGEGGALMV 248
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4814 LKTVKQALEDGDTIYAVVKAASVNNDGRTAGPATPNLEAQKEVMKDALFKSGKKPEDISYLEANGSGSIVTDLLELKAIQ 4893
Cdd:PRK07910   249 IETEEHAKARGANILARIMGASITSDGFHMVAPDPNGERAGHAMTRAIELAGLTPGDIDHVNAHATGTSVGDVAEGKAIN 328
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1776025254 4894 SVYRSGHSsplSLGSIKPNIGHPLCAEGIASFIKVVLMLKE 4934
Cdd:PRK07910   329 NALGGHRP---AVYAPKSALGHSVGAVGAVESILTVLALRD 366
PRK12827 PRK12827
short chain dehydrogenase; Provisional
2850-3056 6.06e-11

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 66.28  E-value: 6.06e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGLLFAKEIANRtGRSTIVLTGRSVLSEDKENELEAL-RSIGAEVVYREADVSDQHAVHHLFEEIKERYG 2928
Cdd:PRK12827     8 RVLITGGSGGLGRAIAVRLAAD-GADVIVLDIHPMRGRAEADAVAAGiEAAGGKALGLAFDVRDFAATRAALDAGVEEFG 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2929 TLNGIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSGLLHVDECSKdFPL------DFFIFFSSVSGCLGNAGQADYAAANS 3002
Cdd:PRK12827    87 RLDILVNNAGIATDAAFAELSIEEWDDVIDVNLDGFFNVTQAAL-PPMirarrgGRIVNIASVAGVRGNRGQVNYAASKA 165
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1776025254 3003 fmdAFAEYRRSLAASKKRFGSTISFNWPLWEEGGMQVGAEDEKRMLKTtgmVPM 3056
Cdd:PRK12827   166 ---GLIGLTKTLANELAPRGITVNAVAPGAINTPMADNAAPTEHLLNP---VPV 213
PRK12406 PRK12406
long-chain-fatty-acid--CoA ligase; Provisional
168-486 7.57e-11

long-chain-fatty-acid--CoA ligase; Provisional


Pssm-ID: 183506 [Multi-domain]  Cd Length: 509  Bit Score: 68.19  E-value: 7.57e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  168 IVEDLLSAEA-DTDWH----QSSPEDL------ALLLLTSGSTGTPKAVmlnHRN------IMSMVKGIIQMQGFTREDI 230
Cdd:PRK12406   122 ISPALLTPPAgAIDWEgwlaQQEPYDGppvpqpQSMIYTSGTTGHPKGV---RRAaptpeqAAAAEQMRALIYGLKPGIR 198
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  231 TFNWMPfdhvggigMLHLRDVYLGCQEINVSSETILM---EPLKWLDWIDHYRASVTWAPNFAFGLVTDFAEEIKdRKWD 307
Cdd:PRK12406   199 ALLTGP--------LYHSAPNAYGLRAGRLGGVLVLQprfDPEELLQLIERHRITHMHMVPTMFIRLLKLPEEVR-AKYD 269
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  308 LSSMRYMLNGGEAMVAKVGRRILELLEPhglpadAIRPAWGMSETSSgVIFSheftragTSDD--DHFVEIGSPIPGFSM 385
Cdd:PRK12406   270 VSSLRHVIHAAAPCPADVKRAMIEWWGP------VIYEYYGSTESGA-VTFA-------TSEDalSHPGTVGKAAPGAEL 335
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  386 RIVNDHNELVEEGEIGRFQVSGLSVTS-GYYQRPDLNESVfTEDGWFETGDLGFL-RNGRLTITGRTKDAIIINGINYYS 463
Cdd:PRK12406   336 RFVDEDGRPLPQGEIGEIYSRIAGNPDfTYHNKPEKRAEI-DRGGFITSGDVGYLdADGYLFLCDRKRDMVISGGVNIYP 414
                          330       340
                   ....*....|....*....|...
gi 1776025254  464 HAIESAVEELSEIetsytAACAV 486
Cdd:PRK12406   415 AEIEAVLHAVPGV-----HDCAV 432
CLF cd00832
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ...
1761-2144 1.24e-10

Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic antibiotic-producing polyketide synthases (PKSs) of filamentous bacteria. CLFs have been shown to have decarboxylase activity towards malonyl-acyl carrier protein (ACP). CLFs are similar to other elongation ketosynthase domains, but their active site cysteine is replaced by a conserved glutamine.


Pssm-ID: 238428 [Multi-domain]  Cd Length: 399  Bit Score: 67.00  E-value: 1.24e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1761 SVAIIGISCEFPGAKNHDEFWENLRDGKESIAffnkeELQRFGISKEIAENADYVP---AKASIEGkdRFDPSffqispk 1837
Cdd:cd00832      2 RAVVTGIGVVAPNGLGVEEYWKAVLDGRSGLG-----PITRFDPSGYPARLAGEVPdfdAAEHLPG--RLLPQ------- 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1838 daefMDPQLRMLLTHSWKAIEDAGYAAGQIPQTSV-FMSASNN-----SYRAL--LPSDTTESLETPDGYVSWVLAQSGT 1909
Cdd:cd00832     68 ----TDRMTRLALAAADWALADAGVDPAALPPYDMgVVTASAAggfefGQRELqkLWSKGPRHVSAYQSFAWFYAVNTGQ 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1910 IPtmISHklGLRGPSYFVHANCSSSLIGLHSAyKSLLSAESDYALVGG--ATLHTESNIGYVHQPGLNFSSDGHI--KAF 1985
Cdd:cd00832    144 IS--IRH--GMRGPSGVVVAEQAGGLDALAQA-RRLVRRGTPLVVSGGvdSALCPWGWVAQLSSGRLSTSDDPARayLPF 218
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1986 DASADGMIGGEGVAVVLLKKAADAVKDGDHIYALLRGIGVNNDGADKvgfyAPSVKGQADVVQQVMNQTKIHPESICYVE 2065
Cdd:cd00832    219 DAAAAGYVPGEGGAILVLEDAAAARERGARVYGEIAGYAATFDPPPG----SGRPPGLARAIRLALADAGLTPEDVDVVF 294
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2066 AHGTGTKLGDPIELAALTNVYrqytnktqfcGIGSV-----KTNIGHLDTAAGLAGCIKVVMSLYHQELAPSINYKEPNP 2140
Cdd:cd00832    295 ADAAGVPELDRAEAAALAAVF----------GPRGVpvtapKTMTGRLYAGGAPLDVATALLALRDGVIPPTVNVTDVPP 364

                   ....
gi 1776025254 2141 NTDL 2144
Cdd:cd00832    365 AYGL 368
PRK06334 PRK06334
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
1297-1644 1.44e-10

long chain fatty acid--[acyl-carrier-protein] ligase; Validated


Pssm-ID: 180533 [Multi-domain]  Cd Length: 539  Bit Score: 67.53  E-value: 1.44e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1297 PENLAYVIYTSGSTGKPKGVMIPHKALTNFLVSMGETPGLTAEDKMLAVT----TYCFDIAALelfLPLIKGAHcyICQT 1372
Cdd:PRK06334   182 PEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLppfhAYGFNSCTL---FPLLSGVP--VVFA 256
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1373 EHTKDVEKLKRDIRTIKPTVMQATPATWKMLFYSGWENEENVKIL----CGGEALPETL----KRYF----LDTGseawn 1440
Cdd:PRK06334   257 YNPLYPKKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQESCLPSLrfvvIGGDAFKDSLyqeaLKTFphiqLRQG----- 331
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1441 mFGPTETtiwSAVQRINDECS---RATIGRPIANTQIYITDSQL-APVPAGVPGELCIAGDGVAKGYYKKEEltDSRFID 1516
Cdd:PRK06334   332 -YGTTEC---SPVITINTVNSpkhESCVGMPIRGMDVLIVSEETkVPVSSGETGLVLTRGTSLFSGYLGEDF--GQGFVE 405
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1517 npfEPGSKLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILE---------CVVVADMDNLAAY 1587
Cdd:PRK06334   406 ---LGGETWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEGFGQNAadhagplvvCGLPGEKVRLCLF 482
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1776025254 1588 YTakhanASLTARELRHFVKNALPAYMVP-SYFIQLDHMPLTPNGKIDRNSLKNIDLS 1644
Cdd:PRK06334   483 TT-----FPTSISEVNDILKNSKTSSILKiSYHHQVESIPMLGTGKPDYCSLNALAKS 535
PRK09274 PRK09274
peptide synthase; Provisional
182-463 1.93e-10

peptide synthase; Provisional


Pssm-ID: 236443 [Multi-domain]  Cd Length: 552  Bit Score: 67.23  E-value: 1.93e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  182 HQSSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIiqmqgftREDitFNWMPfdhvGGIGM-----LHLRDVYLGCQ 256
Cdd:PRK09274   169 ADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEAL-------RED--YGIEP----GEIDLptfplFALFGPALGMT 235
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  257 ----EINvSSETILMEPLKWLDWIDHYRasVTwapNFaFG------LVTDFAEEikdRKWDLSSMRYMLNGGEAMVAKVG 326
Cdd:PRK09274   236 svipDMD-PTRPATVDPAKLFAAIERYG--VT---NL-FGspalleRLGRYGEA---NGIKLPSLRRVISAGAPVPIAVI 305
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  327 RRILELLePHGLPadaIRPAWGMSE-------TSSGVIFShefTRAGTsdDDHF-VEIGSPIPGFSMRIVN--------- 389
Cdd:PRK09274   306 ERFRAML-PPDAE---ILTPYGATEalpissiESREILFA---TRAAT--DNGAgICVGRPVDGVEVRIIAisdapipew 376
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1776025254  390 DHNELVEEGEIGRFQVSGLSVTSGYYQRPDLNESVFTEDG----WFETGDLGFLRN-GRLTITGRTKDAIIINGINYYS 463
Cdd:PRK09274   377 DDALRLATGEIGEIVVAGPMVTRSYYNRPEATRLAKIPDGqgdvWHRMGDLGYLDAqGRLWFCGRKAHRVETAGGTLYT 455
PLN02574 PLN02574
4-coumarate--CoA ligase-like
187-566 1.99e-10

4-coumarate--CoA ligase-like


Pssm-ID: 215312 [Multi-domain]  Cd Length: 560  Bit Score: 67.17  E-value: 1.99e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  187 EDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGII-----QMQGFTREDITFNWMPFDHVGGIGMLHLRDVYLGcqeinvs 261
Cdd:PLN02574   198 DDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVrfeasQYEYPGSDNVYLAALPMFHIYGLSLFVVGLLSLG------- 270
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  262 SETILMEPLKWLDW---IDHYRasVTWAPNFAFGLVTDFAEEIKDRKWDLSSMRYMLNGGEAMVAKVGRRILELLePHgl 338
Cdd:PLN02574   271 STIVVMRRFDASDMvkvIDRFK--VTHFPVVPPILMALTKKAKGVCGEVLKSLKQVSCGAAPLSGKFIQDFVQTL-PH-- 345
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  339 pADAIRpAWGMSE-TSSGvifshefTRA-GTSDDDHFVEIGSPIPGFSMRIVN-DHNELVEEGEIGRFQVSGLSVTSGYY 415
Cdd:PLN02574   346 -VDFIQ-GYGMTEsTAVG-------TRGfNTEKLSKYSSVGLLAPNMQAKVVDwSTGCLLPPGNCGELWIQGPGVMKGYL 416
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  416 QRPDLNESVFTEDGWFETGDLG-FLRNGRLTITGRTKDAIIINGINYYSHAIESAVEELSEIetsyTAACAVRLGQNSTD 494
Cdd:PLN02574   417 NNPKATQSTIDKDGWLRTGDIAyFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEI----IDAAVTAVPDKECG 492
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1776025254  495 QLAIFFVTsaKLNDEQMSQllrniqshvSQVIGVTPEYLLPVQK-------EEIPKTAIGKIQRTQLKTSFENGEFDHL 566
Cdd:PLN02574   493 EIPVAFVV--RRQGSTLSQ---------EAVINYVAKQVAPYKKvrkvvfvQSIPKSPAGKILRRELKRSLTNSVSSRL 560
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
3115-3186 2.04e-10

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 59.87  E-value: 2.04e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1776025254 3115 LEAALIQMVGAILKVNTDDIDVNTEL-SEYGFDSVTFTVFTNKINEKFQLELTPTIFFEYGSVQSLAEYVVAA 3186
Cdd:COG0236      6 LEERLAEIIAEVLGVDPEEITPDDSFfEDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEEK 78
Cyc_NRPS cd19535
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
727-1033 2.06e-10

Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Cyc (heterocyclization) domains catalyze two separate reactions in the creation of heterocyclized peptide products in nonribosomal peptide synthesis: amide bond formation followed by intramolecular cyclodehydration between a Cys, Ser, or Thr side chain and a carbonyl carbon on the peptide backbone to form a thiazoline, oxazoline, or methyloxazoline ring. Cyc-domains are homologous to standard NRPS Condensation (C) domains. C-domains typically have a conserved HHxxxD motif at the active site; Cyc-domains have an alternative, conserved DxxxxD active site motif, mutation of the aspartate residues in this motif can abolish or diminish condensation activity. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and Cyc-domains. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380458 [Multi-domain]  Cd Length: 423  Bit Score: 66.74  E-value: 2.06e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  727 GLHLETLQQAFGLVLNQHPILKHVIQEkDGVPILKNEPAlSIEIKTENISSMKESDIPAFLRK----------KVkepyv 796
Cdd:cd19535     36 DLDPDRLERAWNKLIARHPMLRAVFLD-DGTQQILPEVP-WYGITVHDLRGLSEEEAEAALEElrerlshrvlDV----- 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  797 kENSPLVRVMSFSRSEQEHFLLVVIHHLIFDGVSSVTFIHSLFDTYQlllkgqQPEIAVSPAIYH--DFAAWEKNMLAG- 873
Cdd:cd19535    109 -ERGPLFDIRLSLLPEGRTRLHLSIDLLVADALSLQILLRELAALYE------DPGEPLPPLELSfrDYLLAEQALRETa 181
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  874 --KDgvkhRTYWQKQLSgTLPN-LQLP-KVSASSVSEFREDTYTRRLSSGFMNQVRMFAKEHSVNVTTVFLSCYMMLLGR 949
Cdd:cd19535    182 yeRA----RAYWQERLP-TLPPaPQLPlAKDPEEIKEPRFTRREHRLSAEQWQRLKERARQHGVTPSMVLLTAYAEVLAR 256
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  950 YTGQKEQIVGMPAMVRPE--ERFDDAIGHFLNMLPIRSELNPADTFSSFISKLQLTILDGLDHAAYPFPKMVRDLN--IP 1025
Cdd:cd19535    257 WSGQPRFLLNLTLFNRLPlhPDVNDVVGDFTSLLLLEVDGSEGQSFLERARRLQQQLWEDLDHSSYSGVVVVRRLLrrRG 336

                   ....*...
gi 1776025254 1026 RSQAGSPV 1033
Cdd:cd19535    337 GQPVLAPV 344
PTZ00237 PTZ00237
acetyl-CoA synthetase; Provisional
1302-1661 2.78e-10

acetyl-CoA synthetase; Provisional


Pssm-ID: 240325 [Multi-domain]  Cd Length: 647  Bit Score: 67.07  E-value: 2.78e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1302 YVIYTSGSTGKPKGV-------MIPHKALTNFLVSMGETPGLTAEDKMLAVTTYCFDIAALEL--FLPLIKGAhcyICQT 1372
Cdd:PTZ00237   258 YILYTSGTTGNSKAVvrsngphLVGLKYYWRSIIEKDIPTVVFSHSSIGWVSFHGFLYGSLSLgnTFVMFEGG---IIKN 334
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1373 EHTKD-----VEKLKRDIRTIKPTVM----QATPATWKMlfYSGWENEENVKILCGGEALPETLKRYFLDT-GSEAWNMF 1442
Cdd:PTZ00237   335 KHIEDdlwntIEKHKVTHTLTLPKTIryliKTDPEATII--RSKYDLSNLKEIWCGGEVIEESIPEYIENKlKIKSSRGY 412
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1443 GPTETTIWSAVQRINDECSRATIGRPiantQIYITDSQLAP----VPAGVPGELCIA---GDGVAKGYYKKEELTDSRFi 1515
Cdd:PTZ00237   413 GQTEIGITYLYCYGHINIPYNATGVP----SIFIKPSILSEdgkeLNVNEIGEVAFKlpmPPSFATTFYKNDEKFKQLF- 487
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1516 dNPFePGskLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVA----DMDN-----LAA 1586
Cdd:PTZ00237   488 -SKF-PG--YYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGiydpDCYNvpiglLVL 563
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1776025254 1587 YYTAKHANASLT--ARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLKN-IDLSGEQLkqrqtsPKNIQDT 1661
Cdd:PTZ00237   564 KQDQSNQSIDLNklKNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPRQIISKfLNDSNYQL------PDNVNDS 635
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
2852-3030 2.81e-10

3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These proteins include members identified as KDSR, ribitol type dehydrogenase, and others. The group shows strong conservation of the active site tetrad and glycine rich NAD-binding motif of the classical SDRs. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187643 [Multi-domain]  Cd Length: 239  Bit Score: 63.81  E-value: 2.81e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2852 LITGGAGSLGLLFAKEIANRtGRStIVLTGRSV--LSEDKEN-ELEALRSiGAEVVYREADVSDQHAVHHLFEEIKERYG 2928
Cdd:cd08939      5 LITGGSSGIGKALAKELVKE-GAN-VIIVARSEskLEEAVEEiEAEANAS-GQKVSYISADLSDYEEVEQAFAQAVEKGG 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2929 TLNGIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSGLLHVdeCSKDFPL------DFFIFFSSVSGCLGNAGQADYAAANS 3002
Cdd:cd08939     82 PPDLVVNCAGISIPGLFEDLTAEEFERGMDVNYFGSLNV--AHAVLPLmkeqrpGHIVFVSSQAALVGIYGYSAYCPSKF 159
                          170       180
                   ....*....|....*....|....*...
gi 1776025254 3003 FMDAFAEyrrSLAASKKRFGSTISFNWP 3030
Cdd:cd08939    160 ALRGLAE---SLRQELKPYNIRVSVVYP 184
PRK07445 PRK07445
O-succinylbenzoic acid--CoA ligase; Reviewed
331-560 2.93e-10

O-succinylbenzoic acid--CoA ligase; Reviewed


Pssm-ID: 236019 [Multi-domain]  Cd Length: 452  Bit Score: 66.17  E-value: 2.93e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  331 ELLEP---HGLPadaIRPAWGMSETSSGV--IFSHEFTRAGTSdddhfveIGSPIPGFSMRIVNdhnelveeGEIGRFQV 405
Cdd:PRK07445   245 SLLEQarqLQLR---LAPTYGMTETASQIatLKPDDFLAGNNS-------SGQVLPHAQITIPA--------NQTGNITI 306
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  406 SGLSVTSGYYqrPDLNESvfteDGWFETGDLGFL-RNGRLTITGRTKDAIIINGINYYSHAIESAVEELSEIETsytaAC 484
Cdd:PRK07445   307 QAQSLALGYY--PQILDS----QGIFETDDLGYLdAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQD----VC 376
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  485 AVRL-----GQnstdQLAIFFVtsakLNDEQMSqlLRNIQSHVSQVIGV--TPEYLLPVQkeEIPKTAIGKIQRTQLKTS 557
Cdd:PRK07445   377 VLGLpdphwGE----VVTAIYV----PKDPSIS--LEELKTAIKDQLSPfkQPKHWIPVP--QLPRNPQGKINRQQLQQI 444

                   ...
gi 1776025254  558 FEN 560
Cdd:PRK07445   445 AVQ 447
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
4169-4341 3.10e-10

NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; NADP-dependent 3-hydroxy acid dehydrogenase YdfG is part of the Pathway/BioSystem: Pyrimidine degradation


Pssm-ID: 443365 [Multi-domain]  Cd Length: 240  Bit Score: 63.66  E-value: 3.10e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4169 KDHVLLITGGTRGIGLLCARHFAEcYGVkKLVLTGReqlppREEwarfktsntslaekiqAVRELEAK-GVQVEMLSLTL 4247
Cdd:COG4221      4 KGKVALITGASSGIGAATARALAA-AGA-RVVLAAR-----RAE----------------RLEALAAElGGRALAVPLDV 60
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4248 SDDAQVEQTLQHIKRTLGPIGGVIHCAGLTDMDTLAFIrkTSDDIQRVMEPKVSGLTTLYRHVcnepLQ--------FFV 4319
Cdd:COG4221     61 TDEAAVEAAVAAAVAEFGRLDVLVNNAGVALLGPLEEL--DPEDWDRMIDVNVKGVLYVTRAA----LPamrargsgHIV 134
                          170       180
                   ....*....|....*....|..
gi 1776025254 4320 LFSSVSAIIPelSAGQADYAMA 4341
Cdd:COG4221    135 NISSIAGLRP--YPGGAVYAAT 154
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
2850-3015 3.16e-10

glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR family, it catalyzes the NAD(P)-dependent oxidation of beta-D-glucose to D-glucono-delta-lactone. GlcDH has a typical NAD-binding site glycine-rich pattern as well as the canonical active site tetrad (YXXXK motif plus upstream Ser and Asn). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187616 [Multi-domain]  Cd Length: 253  Bit Score: 63.94  E-value: 3.16e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGLLFAKEIAnRTGrSTIVLTGRSvlSEDKENEL-EALRSIGAEVVYREADVSDQHAVHHLFEEIKERYG 2928
Cdd:cd05358      5 VALVTGASSGIGKAIAIRLA-TAG-ANVVVNYRS--KEDAAEEVvEEIKAVGGKAIAVQADVSKEEDVVALFQSAIKEFG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2929 TLNGIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSG-LLHVDECSKDF----PLDFFIFFSSVSGCLGNAGQADYAAANSF 3003
Cdd:cd05358     81 TLDILVNNAGLQGDASSHEMTLEDWNKVIDVNLTGqFLCAREAIKRFrkskIKGKIINMSSVHEKIPWPGHVNYAASKGG 160
                          170
                   ....*....|..
gi 1776025254 3004 MDAFAEyrrSLA 3015
Cdd:cd05358    161 VKMMTK---TLA 169
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
2852-3025 3.43e-10

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 63.63  E-value: 3.43e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2852 LITGGAGSLGLLFAKEIANRtGRsTIVLTGRS--VLSEDKENELEALRsigAEVVYREADVSDQHAVHHLFEEIKERYGT 2929
Cdd:PRK12824     6 LVTGAKRGIGSAIARELLND-GY-RVIATYFSgnDCAKDWFEEYGFTE---DQVRLKELDVTDTEECAEALAEIEEEEGP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2930 LNGIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSGLLHVDE------CSKDFPLdfFIFFSSVSGCLGNAGQADYAAANSF 3003
Cdd:PRK12824    81 VDILVNNAGITRDSVFKRMSHQEWNDVINTNLNSVFNVTQplfaamCEQGYGR--IINISSVNGLKGQFGQTNYSAAKAG 158
                          170       180
                   ....*....|....*....|..
gi 1776025254 3004 MDAFAeyrRSLAASKKRFGSTI 3025
Cdd:PRK12824   159 MIGFT---KALASEGARYGITV 177
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
4461-4531 3.63e-10

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 59.10  E-value: 3.63e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1776025254 4461 SETQSWLIDLFTEELRIDREDFEID-GLFQDYGVDSIILAQVLQRINRKLEAALDPSILYEYPTIQRFTDWL 4531
Cdd:COG0236      4 EELEERLAEIIAEVLGVDPEEITPDdSFFEDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYL 75
PLN02430 PLN02430
long-chain-fatty-acid-CoA ligase
55-454 4.43e-10

long-chain-fatty-acid-CoA ligase


Pssm-ID: 178049 [Multi-domain]  Cd Length: 660  Bit Score: 66.38  E-value: 4.43e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254   55 GTEVYQSYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNSQLLPAFWGCVLTGVVPAPL-------AVP--PTYAESSS 125
Cdd:PLN02430    72 GPYMWKTYKEVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVAMEACAAHSLICVPLydtlgpgAVDyiVDHAEIDF 151
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  126 GTQKLKDAWTLLDK--------PAVITDRGMHQEMLDWAKEQGLEGFRAiivEDLL--SAEADTDWHQSSPEDLALLLLT 195
Cdd:PLN02430   152 VFVQDKKIKELLEPdcksakrlKAIVSFTSVTEEESDKASQIGVKTYSW---IDFLhmGKENPSETNPPKPLDICTIMYT 228
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  196 SGSTGTPKAVMLNHRNIMSMVKGI-IQMQGF----TREDITFNWMPFDHV-------------GGIGMLH-----LRD-- 250
Cdd:PLN02430   229 SGTSGDPKGVVLTHEAVATFVRGVdLFMEQFedkmTHDDVYLSFLPLAHIldrmieeyffrkgASVGYYHgdlnaLRDdl 308
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  251 -----------------VYLG----CQEINVSSETILMEPLKW-LDWID----HYRASvTWAPNFAFglvtdfaEEIKDR 304
Cdd:PLN02430   309 melkptllagvprvferIHEGiqkaLQELNPRRRLIFNALYKYkLAWMNrgysHKKAS-PMADFLAF-------RKVKAK 380
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  305 KWdlSSMRYMLNGGeamvAKVGRRILELLEPHGLpADAIRpAWGMSETSSGVI--FSHEFTRAGTsdddhfveIGSPIPG 382
Cdd:PLN02430   381 LG--GRLRLLISGG----APLSTEIEEFLRVTSC-AFVVQ-GYGLTETLGPTTlgFPDEMCMLGT--------VGAPAVY 444
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  383 FSMRIvndhNELVEEG-------EIGRFQVSGLSVTSGYYQRPDLNESVFtEDGWFETGDLG-FLRNGRLTITGRTKDAI 454
Cdd:PLN02430   445 NELRL----EEVPEMGydplgepPRGEICVRGKCLFSGYYKNPELTEEVM-KDGWFHTGDIGeILPNGVLKIIDRKKNLI 519
PTZ00216 PTZ00216
acyl-CoA synthetase; Provisional
1131-1578 5.17e-10

acyl-CoA synthetase; Provisional


Pssm-ID: 240316 [Multi-domain]  Cd Length: 700  Bit Score: 66.15  E-value: 5.17e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1131 LPEAEKQMILKTWnatgktYPYITFHELFEQQAKKTPDRAAVSY---------------------------EGQTLTYRE 1183
Cdd:PTZ00216    53 VTDEEHERLRNEW------YYGPNFLQRLERICKERGDRRALAYrpvervekevvkdadgkertmevthfnETRYITYAE 126
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1184 LDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAI----LKAGGAYVPLDpsypAERLEYMLEDSE--------- 1250
Cdd:PTZ00216   127 LWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIwsqsMVAATVYANLG----EDALAYALRETEckaivcngk 202
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1251 ---VFITLTTS-ELVNT-LSWNGVTTALLDQD------WDEIAQTASDRKVLTRTVTPEN---LAYVIYTSGSTGKPKGV 1316
Cdd:PTZ00216   203 nvpNLLRLMKSgGMPNTtIIYLDSLPASVDTEgcrlvaWTDVVAKGHSAGSHHPLNIPENnddLALIMYTSGTTGDPKGV 282
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1317 MIPHKALTNFLVSMG----ETPGLTAEDKmlavtTYC--------FDIAALELFLplIKGAH-CYICQTEHTKDVEKLKR 1383
Cdd:PTZ00216   283 MHTHGSLTAGILALEdrlnDLIGPPEEDE-----TYCsylplahiMEFGVTNIFL--ARGALiGFGSPRTLTDTFARPHG 355
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1384 DIRTIKPTVMQATPATWKMLfysgwenEENVkilcggEA-LPE--TLKRYFLDTGSEA-------------WN------- 1440
Cdd:PTZ00216   356 DLTEFRPVFLIGVPRIFDTI-------KKAV------EAkLPPvgSLKRRVFDHAYQSrlralkegkdtpyWNekvfsap 422
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1441 ----------------------------MFGP-------TETTIWSAVQRIND-ECSraTIGRPIANTQIYITDSQL--- 1481
Cdd:PTZ00216   423 ravlggrvramlsgggplsaatqefvnvVFGMviqgwglTETVCCGGIQRTGDlEPN--AVGQLLKGVEMKLLDTEEykh 500
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1482 --APVPAGvpgELCIAGDGVAKGYYKKEELTDSRFIDNPFepgsklYRTGDMARWLPGGRIEYIGRIDNQVK-IRGFRIE 1558
Cdd:PTZ00216   501 tdTPEPRG---EILLRGPFLFKGYYKQEELTREVLDEDGW------FHTGDVGSIAANGTLRIIGRVKALAKnCLGEYIA 571
                          570       580
                   ....*....|....*....|....*
gi 1776025254 1559 LGDIESRLSEHP-----GIleCVVV 1578
Cdd:PTZ00216   572 LEALEALYGQNElvvpnGV--CVLV 594
PTZ00342 PTZ00342
acyl-CoA synthetase; Provisional
186-451 6.19e-10

acyl-CoA synthetase; Provisional


Pssm-ID: 240370 [Multi-domain]  Cd Length: 746  Bit Score: 65.90  E-value: 6.19e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  186 PEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDIT--FNWMPFDHVGGIGMLHLrDVYLGCQeINVSSE 263
Cdd:PTZ00342   303 PDFITSIVYTSGTSGKPKGVMLSNKNLYNTVVPLCKHSIFKKYNPKthLSYLPISHIYERVIAYL-SFMLGGT-INIWSK 380
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  264 -----------------------------TILME-----PLK-WL-DWIDHYRASVT--WAPNFAFGLvTDFAEEIKDRK 305
Cdd:PTZ00342   381 dinyfskdiynskgnilagvpkvfnriytNIMTEinnlpPLKrFLvKKILSLRKSNNngGFSKFLEGI-THISSKIKDKV 459
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  306 wdLSSMRYMLNGGEAMVAKVGRRILELLEPHglpadaIRPAWGMSETSSGVIFSHEftragtsDDDHFVEIGSPI-PGFS 384
Cdd:PTZ00342   460 --NPNLEVILNGGGKLSPKIAEELSVLLNVN------YYQGYGLTETTGPIFVQHA-------DDNNTESIGGPIsPNTK 524
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1776025254  385 MRIVN----DHNELVEEGEIgrfQVSGLSVTSGYYQRPDLNESVFTEDGWFETGDLGFL-RNGRLTITGRTK 451
Cdd:PTZ00342   525 YKVRTwetyKATDTLPKGEL---LIKSDSIFSGYFLEKEQTKNAFTEDGYFKTGDIVQInKNGSLTFLDRSK 593
PRK13390 PRK13390
acyl-CoA synthetase; Provisional
38-555 6.46e-10

acyl-CoA synthetase; Provisional


Pssm-ID: 139538 [Multi-domain]  Cd Length: 501  Bit Score: 65.42  E-value: 6.46e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254   38 TAAELGDTKGIIYLQPDGTEVyqSYRRLWDDGLRIVKGLRQSGLKAKQSVILqLGDNS-QLLPAFWGCVLTGVVPAPLAV 116
Cdd:PRK13390     5 THAQIAPDRPAVIVAETGEQV--SYRQLDDDSAALARVLYDAGLRTGDVVAL-LSDNSpEALVVLWAALRSGLYITAINH 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  117 PPTYAES-----SSGTQKLKdAWTLLDkpAVITDRGMHQEM-LDWAKEqgLEGFRAIivEDLLSAEADTDWHQSSPedlA 190
Cdd:PRK13390    82 HLTAPEAdyivgDSGARVLV-ASAALD--GLAAKVGADLPLrLSFGGE--IDGFGSF--EAALAGAGPRLTEQPCG---A 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  191 LLLLTSGSTGTPKAVM--LNHRNIMSMVKGIIQMQ----GFTREDITFNWMPFDHVGGI---GMLHLrdvyLGCQEINVS 261
Cdd:PRK13390   152 VMLYSSGTTGFPKGIQpdLPGRDVDAPGDPIVAIArafyDISESDIYYSSAPIYHAAPLrwcSMVHA----LGGTVVLAK 227
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  262 SetilMEPLKWLDWIDHYRASVTWAPNFAFGLVTDFAEEIKDRkWDLSSMRYMLNGGEAMVAKVGRRILELLEPHGLPAD 341
Cdd:PRK13390   228 R----FDAQATLGHVERYRITVTQMVPTMFVRLLKLDADVRTR-YDVSSLRAVIHAAAPCPVDVKHAMIDWLGPIVYEYY 302
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  342 AIRPAWGMSETSSGVIFSHEFTragtsdddhfveIGSPIPGfSMRIVNDHNELVEEGEIGRFQVSGLSVTSGYYQRPDLN 421
Cdd:PRK13390   303 SSTEAHGMTFIDSPDWLAHPGS------------VGRSVLG-DLHICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKT 369
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  422 ESVF--TEDGWFETGDLGFL-RNGRLTITGRTKDAIIINGINYYSHAIESAVEELSEI-ETSYTAACAVRLGQNStdQLA 497
Cdd:PRK13390   370 AAAQhpAHPFWTTVGDLGSVdEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVhDVAVIGVPDPEMGEQV--KAV 447
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1776025254  498 IFFVTSAKLNDEQMSQLLRNIQSHVSQvigvtpeYLLPVQKE---EIPKTAIGKIQRTQLK 555
Cdd:PRK13390   448 IQLVEGIRGSDELARELIDYTRSRIAH-------YKAPRSVEfvdELPRTPTGKLVKGLLR 501
CLF cd00832
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ...
4591-4896 7.93e-10

Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic antibiotic-producing polyketide synthases (PKSs) of filamentous bacteria. CLFs have been shown to have decarboxylase activity towards malonyl-acyl carrier protein (ACP). CLFs are similar to other elongation ketosynthase domains, but their active site cysteine is replaced by a conserved glutamine.


Pssm-ID: 238428 [Multi-domain]  Cd Length: 399  Bit Score: 64.69  E-value: 7.93e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4591 AVVGLSCRFPGAETLESYWSLLSEGRSSIGPIpaERWGCkTPYYAGVIDGVSYFDPDFF----LLHEEDVraMDPQALLV 4666
Cdd:cd00832      4 VVTGIGVVAPNGLGVEEYWKAVLDGRSGLGPI--TRFDP-SGYPARLAGEVPDFDAAEHlpgrLLPQTDR--MTRLALAA 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4667 LEECLKllyHAGYTPEEIKGKPVGVY---------IGGRSQHKPDEDSLDHaknpiVTVGQNY---LAANLSQF---FDV 4731
Cdd:cd00832     79 ADWALA---DAGVDPAALPPYDMGVVtasaaggfeFGQRELQKLWSKGPRH-----VSAYQSFawfYAVNTGQIsirHGM 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4732 RGPSVVVDTACSSALVGMNMAIQALRGGDiQSAIVGGV-------SLLSSDASHRLFD----RRGILSkhssfhvFDERA 4800
Cdd:cd00832    151 RGPSGVVVAEQAGGLDALAQARRLVRRGT-PLVVSGGVdsalcpwGWVAQLSSGRLSTsddpARAYLP-------FDAAA 222
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4801 DGVVLGEGVGMVMLKTVKQALEDGDTIYAVVKAASVNNDGRTAGPATPNLEAqkeVMKDALFKSGKKPEDISYLEANGSG 4880
Cdd:cd00832    223 AGYVPGEGGAILVLEDAAAARERGARVYGEIAGYAATFDPPPGSGRPPGLAR---AIRLALADAGLTPEDVDVVFADAAG 299
                          330
                   ....*....|....*.
gi 1776025254 4881 SIVTDLLELKAIQSVY 4896
Cdd:cd00832    300 VPELDRAEAAALAAVF 315
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
2850-3000 9.83e-10

mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes the conversion of fructose to mannitol, an acyclic 6-carbon sugar. MDH is a tetrameric member of the SDR family. This subgroup also includes various other tetrameric SDRs, including Pichia stipitis D-arabinitol dehydrogenase (aka polyol dehydrogenase), Candida albicans Sou1p, a sorbose reductase, and Candida parapsilosis (S)-specific carbonyl reductase (SCR, aka S-specific alcohol dehydrogenase) which catalyzes the enantioselective reduction of 2-hydroxyacetophenone into (S)-1-phenyl-1,2-ethanediol. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser).


Pssm-ID: 187610 [Multi-domain]  Cd Length: 252  Bit Score: 62.73  E-value: 9.83e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGLLFAKEIAnRTGRSTIVLTGRSVLSEDKENELEalRSIGAEVVYREADVSDQHAVHHLFEEIKERYGT 2929
Cdd:cd05352     10 VAIVTGGSRGIGLAIARALA-EAGADVAIIYNSAPRAEEKAEELA--KKYGVKTKAYKCDVSSQESVEKTFKQIQKDFGK 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2930 LNGIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSGLLHvdeCSKDFPLDF-------FIFFSSVSGCLGNAGQ--ADYAAA 3000
Cdd:cd05352     87 IDILIANAGITVHKPALDYTYEQWNKVIDVNLNGVFN---CAQAAAKIFkkqgkgsLIITASMSGTIVNRPQpqAAYNAS 163
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
2850-3009 1.35e-09

sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, catalyzes the NADP-dependent reduction of sepiaptern to 7,8-dihydrobiopterin (BH2). In addition to SPRs, this subgroup also contains Bacillus cereus yueD, a benzil reductase, which catalyzes the stereospecific reduction of benzil to (S)-benzoin. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187625 [Multi-domain]  Cd Length: 241  Bit Score: 61.92  E-value: 1.35e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGLLFAKEIANRTGRSTIVLTGRSvlsEDKENELEALRSIGAEVVYREADVSDQHAVHHLFEEIKERYGT 2929
Cdd:cd05367      1 VIILTGASRGIGRALAEELLKRGSPSVVVLLARS---EEPLQELKEELRPGLRVTTVKADLSDAAGVEQLLEAIRKLDGE 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2930 LNGIIHGAGSIKDHFIIHKTN-EEFQEVLQPKV-SGLLHVDECSKDFPLDFF----IFFSSVSGCLGNAGQADY----AA 2999
Cdd:cd05367     78 RDLLINNAGSLGPVSKIEFIDlDELQKYFDLNLtSPVCLTSTLLRAFKKRGLkktvVNVSSGAAVNPFKGWGLYcsskAA 157
                          170
                   ....*....|
gi 1776025254 3000 ANSFMDAFAE 3009
Cdd:cd05367    158 RDMFFRVLAA 167
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
4172-4341 1.37e-09

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 62.19  E-value: 1.37e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4172 VLLITGGTRGIGLLCARHFAecygvkklvltgreqlppREEWARFKTSNTSLAEKIQAVRELEAKGVQVEMLSLTLSDDA 4251
Cdd:PRK12825     8 VALVTGAARGLGRAIALRLA------------------RAGADVVVHYRSDEEAAEELVEAVEALGRRAQAVQADVTDKA 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4252 QVEQTLQHIKRTLGPIGGVIHCAGLTDMDTLAfiRKTSDDIQRVMEPKVSGLTTLYRHVCneP----LQF--FVLFSSVS 4325
Cdd:PRK12825    70 ALEAAVAAAVERFGRIDILVNNAGIFEDKPLA--DMSDDEWDEVIDVNLSGVFHLLRAVV--PpmrkQRGgrIVNISSVA 145
                          170
                   ....*....|....*.
gi 1776025254 4326 AIIpeLSAGQADYAMA 4341
Cdd:PRK12825   146 GLP--GWPGRSNYAAA 159
PRK08308 PRK08308
acyl-CoA synthetase; Validated
1522-1639 1.91e-09

acyl-CoA synthetase; Validated


Pssm-ID: 236231 [Multi-domain]  Cd Length: 414  Bit Score: 63.52  E-value: 1.91e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1522 GSKLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMDNLA-----AYYTAKHanaS 1596
Cdd:PRK08308   289 GDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAgervkAKVISHE---E 365
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1776025254 1597 LTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLK 1639
Cdd:PRK08308   366 IDPVQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLLE 408
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
599-657 3.02e-09

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.


Pssm-ID: 425746 [Multi-domain]  Cd Length: 62  Bit Score: 56.03  E-value: 3.02e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1776025254  599 LLTCLTEELHVSRDWVEPNANIQSLGVNSIKMMKLIRSIEKNYHIKLTAREIHQYPTIE 657
Cdd:pfam00550    3 LRELLAEVLGVPAEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLA 61
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
2850-3022 3.65e-09

17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187632 [Multi-domain]  Cd Length: 248  Bit Score: 60.71  E-value: 3.65e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGLLFAKEIANR------TGRSTIVLtgrsvlsedkeNELEALRSIGAEVVyrEADVSDQHAVHHLFEEI 2923
Cdd:cd05374      2 VVLITGCSSGIGLALALALAAQgyrviaTARNPDKL-----------ESLGELLNDNLEVL--ELDVTDEESIKAAVKEV 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2924 KERYGTLNGIIHGAGsikdhfIIHK------TNEEFQEVLQPKVSGLLHVdecSKDFpLDFF--------IFFSSVSGCL 2989
Cdd:cd05374     69 IERFGRIDVLVNNAG------YGLFgpleetSIEEVRELFEVNVFGPLRV---TRAF-LPLMrkqgsgriVNVSSVAGLV 138
                          170       180       190
                   ....*....|....*....|....*....|...
gi 1776025254 2990 GNAGQADYAAANSFMDAFAEyrrSLAASKKRFG 3022
Cdd:cd05374    139 PTPFLGPYCASKAALEALSE---SLRLELAPFG 168
MACS_euk cd05928
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ...
268-555 4.00e-09

Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.


Pssm-ID: 341251 [Multi-domain]  Cd Length: 530  Bit Score: 62.87  E-value: 4.00e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  268 EPLKWLDWIDHYRASVTWAPNFAFGLVT--DFAeeikdrKWDLSSMRYMLNGGEAMVAKVgrrILELLEPHGLpadAIRP 345
Cdd:cd05928    254 DPLVILKTLSSYPITTFCGAPTVYRMLVqqDLS------SYKFPSLQHCVTGGEPLNPEV---LEKWKAQTGL---DIYE 321
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  346 AWGMSETssGVI---FSHEFTRAGTsdddhfveIGSPIPGFSMRIVNDHNELV---EEGEIG-RFQ-VSGLSVTSGYYQR 417
Cdd:cd05928    322 GYGQTET--GLIcanFKGMKIKPGS--------MGKASPPYDVQIIDDNGNVLppgTEGDIGiRVKpIRPFGLFSGYVDN 391
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  418 PDLNESVFTEDGWFeTGDLGFL-RNGRLTITGRTKDAIIINGINYYSHAIESAVeelseIETSYTAACAVrlgQNSTDQL 496
Cdd:cd05928    392 PEKTAATIRGDFYL-TGDRGIMdEDGYFWFMGRADDVINSSGYRIGPFEVESAL-----IEHPAVVESAV---VSSPDPI 462
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1776025254  497 -----AIFFVTSAKLNDEQMSQLLRNIQSHVSQVigvTPEYLLPVQKE---EIPKTAIGKIQRTQLK 555
Cdd:cd05928    463 rgevvKAFVVLAPQFLSHDPEQLTKELQQHVKSV---TAPYKYPRKVEfvqELPKTVTGKIQRNELR 526
PRK12406 PRK12406
long-chain-fatty-acid--CoA ligase; Provisional
1179-1639 4.15e-09

long-chain-fatty-acid--CoA ligase; Provisional


Pssm-ID: 183506 [Multi-domain]  Cd Length: 509  Bit Score: 62.79  E-value: 4.15e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1179 LTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLEDS--------- 1249
Cdd:PRK12406    12 RSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSgarvliaha 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1250 --------------EVFITLTTSELvntLSWNGVTTALL-----DQDWDE--IAQTASDRkvlTRTVTPENLayvIYTSG 1308
Cdd:PRK12406    92 dllhglasalpagvTVLSVPTPPEI---AAAYRISPALLtppagAIDWEGwlAQQEPYDG---PPVPQPQSM---IYTSG 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1309 STGKPKGVM----IPHKALTNFLV---SMGETPGLTA--EDKMLAVTTYCFDIAALELflplikgAHCYICQTEHtkDVE 1379
Cdd:PRK12406   163 TTGHPKGVRraapTPEQAAAAEQMralIYGLKPGIRAllTGPLYHSAPNAYGLRAGRL-------GGVLVLQPRF--DPE 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1380 KLKRDIRTIKPTVMQATPAtwkmLFYSGWENEENVK----------ILCGGEALPETLKRYFLDT-GSEAWNMFGPTETt 1448
Cdd:PRK12406   234 ELLQLIERHRITHMHMVPT----MFIRLLKLPEEVRakydvsslrhVIHAAAPCPADVKRAMIEWwGPVIYEYYGSTES- 308
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1449 iwSAVQRINDECSRA---TIGRPIANTQIYITDSQLAPVPAGVPGELCIAGDGVAKGYY-----KKEELTDSRFIDnpfe 1520
Cdd:PRK12406   309 --GAVTFATSEDALShpgTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDFTYhnkpeKRAEIDRGGFIT---- 382
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1521 pgsklyrTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVV--VADMD---NLAAyYTAKHANA 1595
Cdd:PRK12406   383 -------SGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVfgIPDAEfgeALMA-VVEPQPGA 454
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....
gi 1776025254 1596 SLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLK 1639
Cdd:PRK12406   455 TLDEADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLR 498
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
2850-3046 4.71e-09

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 60.40  E-value: 4.71e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGLLFAKEIANRTGRstiVLTGRSVLSEDKENELEALRSIGAEVVYREADVSDQHAVHHLFEEIKERYGT 2929
Cdd:PRK12935     8 VAIVTGGAKGIGKAITVALAQEGAK---VVINYNSSKEAAENLVNELGKEGHDVYAVQADVSKVEDANRLVEEAVNHFGK 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2930 LNGIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSGLLHVDECSKDFPLDF----FIFFSSVSGCLGNAGQADYAAANSFMD 3005
Cdd:PRK12935    85 VDILVNNAGITRDRTFKKLNREDWERVIDVNLSSVFNTTSAVLPYITEAeegrIISISSIIGQAGGFGQTNYSAAKAGML 164
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1776025254 3006 AFAeyrRSLAASKKRFGSTISFNWPLWEEGGMQVGAEDEKR 3046
Cdd:PRK12935   165 GFT---KSLALELAKTNVTVNAICPGFIDTEMVAEVPEEVR 202
E-C_NRPS cd19544
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ...
801-988 6.98e-09

Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); Dual function Epimerization/Condensation (E/C) domains have both an epimerization and a DCL condensation activity. Dual E/C domains first epimerize the substrate amino acid to produce a D-configuration, then catalyze the condensation between the D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. They are D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. These Dual E/C domains contain an extended His-motif (HHx(N)GD) near the N-terminus of the domain in addition to the standard Condensation (C) domain active site motif (HHxxxD). C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains, these include the DCL-type, LCL-type, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C domains, and the X-domain.


Pssm-ID: 380466 [Multi-domain]  Cd Length: 413  Bit Score: 61.68  E-value: 6.98e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  801 PLVRV-MSFSRSEQEHFLLVVIHHLIFDGVSsvtfIHSLFDTYQLLLKGQQPEIAVsPAIYHDFAAwekNMLAGKDGVKH 879
Cdd:cd19544    111 PLLRAhVAEDPANGRWLLLLLFHHLISDHTS----LELLLEEIQAILAGRAAALPP-PVPYRNFVA---QARLGASQAEH 182
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  880 RTYWQKQLSG----TLP-NLQLPKVSASSVSEFRedtytRRLSSGFMNQVRMFAKEHSVNVTTVFLSCYMMLLGRYTGQK 954
Cdd:cd19544    183 EAFFREMLGDvdepTAPfGLLDVQGDGSDITEAR-----LALDAELAQRLRAQARRLGVSPASLFHLAWALVLARCSGRD 257
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1776025254  955 EQIVG------MPAMvrpeERFDDAIGHFLNMLPIRSELN 988
Cdd:cd19544    258 DVVFGtvlsgrMQGG----AGADRALGMFINTLPLRVRLG 293
PRK06198 PRK06198
short chain dehydrogenase; Provisional
4170-4282 7.90e-09

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 60.02  E-value: 7.90e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4170 DHVLLITGGTRGIGLLCARHFAEcYGVKKLVLTGREQLPPReewarfktsntslaekiQAVRELEAKGVQVEMLSLTLSD 4249
Cdd:PRK06198     6 GKVALVTGGTQGLGAAIARAFAE-RGAAGLVICGRNAEKGE-----------------AQAAELEALGAKAVFVQADLSD 67
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1776025254 4250 DAQVEQTLQHIKRTLGPIGGVIHCAGLTDMDTL 4282
Cdd:PRK06198    68 VEDCRRVVAAADEAFGRLDALVNAAGLTDRGTI 100
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
3219-3281 8.26e-09

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 55.24  E-value: 8.26e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1776025254 3219 NMVSAILKVNSEDIDVNTEL-SEYGFDSVTFTVFTNKINEEFQLELTPTIFFEYGSIHSLAEYL 3281
Cdd:COG0236     12 EIIAEVLGVDPEEITPDDSFfEDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYL 75
FACL_like_5 cd05924
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
185-470 8.91e-09

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341248 [Multi-domain]  Cd Length: 364  Bit Score: 60.86  E-value: 8.91e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  185 SPEDLaLLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQgfTREDITFNWM----------------PFDHvgGIGMLHL 248
Cdd:cd05924      2 SADDL-YILYTGGTTGMPKGVMWRQEDIFRMLMGGADFG--TGEFTPSEDAhkaaaaaagtvmfpapPLMH--GTGSWTA 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  249 RDVYLGCQEINVSSETILMEPLkwldWIDHYRASVTWAPnfafgLVTD-FA----EEIKDRK-WDLSSMRYMLNGGEAMV 322
Cdd:cd05924     77 FGGLLGGQTVVLPDDRFDPEEV----WRTIEKHKVTSMT-----IVGDaMArpliDALRDAGpYDLSSLFAISSGGALLS 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  323 AKVGRRILELLePHGLPADAIrpawGMSETSSGVIFS-----HE---FTRAG-----TSDDDHFVEIGSPIPGFsmrivn 389
Cdd:cd05924    148 PEVKQGLLELV-PNITLVDAF----GSSETGFTGSGHsagsgPEtgpFTRANpdtvvLDDDGRVVPPGSGGVGW------ 216
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  390 dhnelveegeIGRfqvSGLsVTSGYYQRPDLNESVFTE-DG--WFETGDLG-FLRNGRLTITGRtkDAIIIN--GINYYS 463
Cdd:cd05924    217 ----------IAR---RGH-IPLGYYGDEAKTAETFPEvDGvrYAVPGDRAtVEADGTVTLLGR--GSVCINtgGEKVFP 280

                   ....*..
gi 1776025254  464 HAIESAV 470
Cdd:cd05924    281 EEVEEAL 287
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
2850-2999 9.94e-09

17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as amyloid-peptide-binding alcohol dehydrogenase (ABAD), was previously identified as a L-3-hydroxyacyl-CoA dehydrogenase, HADH2. In fatty acid metabolism, HADH2 catalyzes the third step of beta-oxidation, the conversion of a hydroxyl to a keto group in the NAD-dependent oxidation of L-3-hydroxyacyl CoA. In addition to alcohol dehydrogenase and HADH2 activites, HSD10 has steroid dehydrogenase activity. Although the mechanism is unclear, HSD10 is implicated in the formation of amyloid beta-petide in the brain (which is linked to the development of Alzheimer's disease). Although HSD10 is normally concentrated in the mitochondria, in the presence of amyloid beta-peptide it translocates into the plasma membrane, where it's action may generate cytotoxic aldehydes and may lower estrogen levels through its use of 17-beta-estradiol as a substrate. HSD10 is a member of the SRD family, but differs from other SDRs by the presence of two insertions of unknown function. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187629 [Multi-domain]  Cd Length: 252  Bit Score: 59.61  E-value: 9.94e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGLLFAKEIANRtGRSTIVLTgrsvLSEDKENELEALrsiGAEVVYREADVSDQHAVHHLFEEIKERYGT 2929
Cdd:cd05371      4 VAVVTGGASGLGLATVERLLAQ-GAKVVILD----LPNSPGETVAKL---GDNCRFVPVDVTSEKDVKAALALAKAKFGR 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2930 LNGIIHGAGSIKDHFIIHKTN------EEFQEVLQPKVSGLLHVDECSKDF-----PLDF-----FIFFSSVSGCLGNAG 2993
Cdd:cd05371     76 LDIVVNCAGIAVAAKTYNKKGqqphslELFQRVINVNLIGTFNVIRLAAGAmgknePDQGgergvIINTASVAAFEGQIG 155

                   ....*.
gi 1776025254 2994 QADYAA 2999
Cdd:cd05371    156 QAAYSA 161
KAsynt_C_assoc pfam16197
Ketoacyl-synthetase C-terminal extension; KAsynt_C_assoc represents the very C-terminus of a ...
2138-2249 1.20e-08

Ketoacyl-synthetase C-terminal extension; KAsynt_C_assoc represents the very C-terminus of a subset of proteins from the keto-acyl-synthetase 2 family. It is found in proteins ranging from bacteria to human.


Pssm-ID: 465059 [Multi-domain]  Cd Length: 111  Bit Score: 56.01  E-value: 1.20e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2138 PNPNTD-LASSPFYVVDQKKTLSREIqthrAALSSFGLGGTNTHAIFEQFKR--DSDKGKIDGTCIVPISAKNKERLQEY 2214
Cdd:pfam16197    1 PNPDIPaLLDGRLKVVTEPTPWPGGI----VGVNSFGFGGANAHVILKSNPKpkIPPESPDNLPRLVLLSGRTEEAVKAL 76
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1776025254 2215 AEDILAYLerrgLENSQLPDFAYTLQVGREAMEHR 2249
Cdd:pfam16197   77 LEKLENHL----DDAEFLSLLNDIHSLPISGHPYR 107
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
2850-2957 1.55e-08

gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent conversion of carbon source D-gluconate and 5-keto-D-gluconate. This SDR subgroup has a classical Gly-rich NAD(P)-binding motif and a conserved active site tetrad pattern. However, it has been proposed that Arg104 (Streptococcus suis Ga5DH numbering), as well as an active site Ca2+, play a critical role in catalysis. In addition to Ga5DHs this subgroup contains Erwinia chrysanthemi KduD which is involved in pectin degradation, and is a putative 2,5-diketo-3-deoxygluconate dehydrogenase. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107,15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187605 [Multi-domain]  Cd Length: 248  Bit Score: 58.91  E-value: 1.55e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGLLFAKEIANRTgrSTIVLTGRSvlSEDKENELEALRSIGAEVVYREADVSDQHAVHHLFEEIKERYGT 2929
Cdd:cd05347      7 VALVTGASRGIGFGIASGLAEAG--ANIVINSRN--EEKAEEAQQLIEKEGVEATAFTCDVSDEEAIKAAVEAIEEDFGK 82
                           90       100
                   ....*....|....*....|....*...
gi 1776025254 2930 LNGIIHGAGSIKDHFIIHKTNEEFQEVL 2957
Cdd:cd05347     83 IDILVNNAGIIRRHPAEEFPEAEWRDVI 110
PRK12829 PRK12829
short chain dehydrogenase; Provisional
2852-3056 1.56e-08

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 59.30  E-value: 1.56e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2852 LITGGAGSLGLLFAKEIANRTGRstIVLTGRSvlsedkENELEALRSI--GAEVVYREADVSDQHAVHHLFEEIKERYGT 2929
Cdd:PRK12829    15 LVTGGASGIGRAIAEAFAEAGAR--VHVCDVS------EAALAATAARlpGAKVTATVADVADPAQVERVFDTAVERFGG 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2930 LNGIIHGAGSIKDHFIIHK-TNEEFQEVLQPKVSGLLHVdeCSKDFPL-------DFFIFFSSVSGCLGNAGQADYAAAN 3001
Cdd:PRK12829    87 LDVLVNNAGIAGPTGGIDEiTPEQWEQTLAVNLNGQFYF--ARAAVPLlkasghgGVIIALSSVAGRLGYPGRTPYAASK 164
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1776025254 3002 SfmdAFAEYRRSLAASKKRFGSTISFNWPLWEEGGMQVGAEDEKRMLKTTGMVPM 3056
Cdd:PRK12829   165 W---AVVGLVKSLAIELGPLGIRVNAILPGIVRGPRMRRVIEARAQQLGIGLDEM 216
PaaK COG1541
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ...
1294-1584 1.90e-08

Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];


Pssm-ID: 441150 [Multi-domain]  Cd Length: 423  Bit Score: 60.16  E-value: 1.90e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1294 TVTPENLAYVIYTSGSTGKPKGVmiphkaltnflvsmgetpGLTAEDkmLAVTTYCF------------DIA----ALEL 1357
Cdd:COG1541     79 AVPLEEIVRIHASSGTTGKPTVV------------------GYTRKD--LDRWAELFarslraagvrpgDRVqnafGYGL 138
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1358 F---LPLIKGAH---CYIC-----QTEHTKDVeklkrdIRTIKPTVMQATPatWKMLFYSGWENEENV--------KILC 1418
Cdd:COG1541    139 FtggLGLHYGAErlgATVIpagggNTERQLRL------MQDFGPTVLVGTP--SYLLYLAEVAEEEGIdprdlslkKGIF 210
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1419 GGEALPETLKRYFLDT-GSEAWNMFGPTETTIWSAVQ-------RINDECSRATIGRPiaNTqiyitdsqLAPVPAGVPG 1490
Cdd:COG1541    211 GGEPWSEEMRKEIEERwGIKAYDIYGLTEVGPGVAYEceaqdglHIWEDHFLVEIIDP--ET--------GEPVPEGEEG 280
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1491 ELCIAGdgvakgyykkeeLTDSrfidnpfepGSKL--YRTGDMARWLPG----G----RIEYI-GRIDNQVKIRGFRIEL 1559
Cdd:COG1541    281 ELVVTT------------LTKE---------AMPLirYRTGDLTRLLPEpcpcGrthpRIGRIlGRADDMLIIRGVNVFP 339
                          330       340       350
                   ....*....|....*....|....*....|
gi 1776025254 1560 GDIESRLSEHPGIL-ECVVVAD----MDNL 1584
Cdd:COG1541    340 SQIEEVLLRIPEVGpEYQIVVDreggLDEL 369
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
1658-1727 1.90e-08

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 54.56  E-value: 1.90e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1776025254  1658 IQDTVFTIWQEVLKTSD---IEWDDGFFDVGGDSLLAVTVADRIKHELSCEFSVTDLFEYSTIKNISQYITEQ 1727
Cdd:smart00823   13 LLDLVREQVAAVLGHAAaeaIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHLAAE 85
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
2850-3000 1.91e-08

3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes members identified as 3beta17beta hydroxysteroid dehydrogenase, 20beta hydroxysteroid dehydrogenase, and R-alcohol dehydrogenase. These proteins exhibit the canonical active site tetrad and glycine rich NAD(P)-binding motif of the classical SDRs. 17beta-dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens, and include members of the SDR family. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187600 [Multi-domain]  Cd Length: 247  Bit Score: 58.55  E-value: 1.91e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGLLFAKEIAnRTGrSTIVLTgrSVLSEDKEnelEALRSIGAEVVYREADVSDQHAVHHLFEEIKERYGT 2929
Cdd:cd05341      7 VAIVTGGARGLGLAHARLLV-AEG-AKVVLS--DILDEEGQ---AAAAELGDAARFFHLDVTDEDGWTAVVDTAREAFGR 79
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1776025254 2930 LNGIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSGLL----HVDECSKDFPLDFFIFFSSVSGCLGNAGQADYAAA 3000
Cdd:cd05341     80 LDVLVNNAGILTGGTVETTTLEEWRRLLDINLTGVFlgtrAVIPPMKEAGGGSIINMSSIEGLVGDPALAAYNAS 154
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
4172-4341 2.01e-08

beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; This subgroup includes the Escherichai coli K12 BKR, FabG. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet) NAD(P)(H) binding region and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H) binding pattern: TGxxxGxG in classical SDRs. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P) binding motif and an altered active site motif (YXXXN). Fungal type type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P) binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr-151 and Lys-155, and well as Asn-111 (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187594 [Multi-domain]  Cd Length: 240  Bit Score: 58.33  E-value: 2.01e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4172 VLLITGGTRGIGLLCARHFAEcYGVKkLVLTGReqlppreewarfktSNTSLAEKIQAVRELeakGVQVEMLSLTLSDDA 4251
Cdd:cd05333      2 VALVTGASRGIGRAIALRLAA-EGAK-VAVTDR--------------SEEAAAETVEEIKAL---GGNAAALEADVSDRE 62
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4252 QVEQTLQHIKRTLGPIGGVIHCAGLTdMDTLaFIRKTSDDIQRVMEpkvSGLTTLYRhvCNEPL------QFF---VLFS 4322
Cdd:cd05333     63 AVEALVEKVEAEFGPVDILVNNAGIT-RDNL-LMRMSEEDWDAVIN---VNLTGVFN--VTQAViramikRRSgriINIS 135
                          170
                   ....*....|....*....
gi 1776025254 4323 SVSAIIPelSAGQADYAMA 4341
Cdd:cd05333    136 SVVGLIG--NPGQANYAAS 152
BACL_like cd05929
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ...
186-470 2.03e-08

Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.


Pssm-ID: 341252 [Multi-domain]  Cd Length: 473  Bit Score: 60.47  E-value: 2.03e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  186 PEDLA---LLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQ---MQGFTREDITFNWMPFDHVGGIG--MLHLRdvyLGCQe 257
Cdd:cd05929    121 IEDEAagwKMLYSGGTTGRPKGIKRGLPGGPPDNDTLMAaalGFGPGADSVYLSPAPLYHAAPFRwsMTALF---MGGT- 196
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  258 invsseTILME---PLKWLDWIDHYRasVTWApNFA---FGLVTDFAEEIKDrKWDLSSMRYMLNGGEAMVAKVGRRILE 331
Cdd:cd05929    197 ------LVLMEkfdPEEFLRLIERYR--VTFA-QFVptmFVRLLKLPEAVRN-AYDLSSLKRVIHAAAPCPPWVKEQWID 266
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  332 LLEPhglpadAIRPAWGMSETS-SGVIFSHEF-TRAGTsdddhfveIGSPIPGfSMRIVNDHNELVEEGEIGRFQVSGlS 409
Cdd:cd05929    267 WGGP------IIWEYYGGTEGQgLTIINGEEWlTHPGS--------VGRAVLG-KVHILDEDGNEVPPGEIGEVYFAN-G 330
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1776025254  410 VTSGYYQRPDLNESVFTEDGWFETGDLGFL-RNGRLTITGRTKDAIIINGINYYSHAIESAV 470
Cdd:cd05929    331 PGFEYTNDPEKTAAARNEGGWSTLGDVGYLdEDGYLYLTDRRSDMIISGGVNIYPQEIENAL 392
KAsynt_C_assoc pfam16197
Ketoacyl-synthetase C-terminal extension; KAsynt_C_assoc represents the very C-terminus of a ...
3726-3844 2.04e-08

Ketoacyl-synthetase C-terminal extension; KAsynt_C_assoc represents the very C-terminus of a subset of proteins from the keto-acyl-synthetase 2 family. It is found in proteins ranging from bacteria to human.


Pssm-ID: 465059 [Multi-domain]  Cd Length: 111  Bit Score: 55.24  E-value: 2.04e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3726 NPYLQ-LTDSPFYIVQEKQEWKsvtdcdgnelPRRAGISSFGIGGVNAHIVIEEYMPKANSEHTATEQPNVIVLSAKNKS 3804
Cdd:pfam16197    2 NPDIPaLLDGRLKVVTEPTPWP----------GGIVGVNSFGFGGANAHVILKSNPKPKIPPESPDNLPRLVLLSGRTEE 71
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1776025254 3805 RLidraSQLLEAIRNKKYTDQGLHRIAYTLQVGREEMDER 3844
Cdd:pfam16197   72 AV----KALLEKLENHLDDAEFLSLLNDIHSLPISGHPYR 107
PRK12826 PRK12826
SDR family oxidoreductase;
2850-3008 2.36e-08

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 58.39  E-value: 2.36e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGLLFAKEIAnRTGrSTIVLTGRSvlSEDKENELEALRSIGAEVVYREADVSDQHAVHHLFEEIKERYGT 2929
Cdd:PRK12826     8 VALVTGAARGIGRAIAVRLA-ADG-AEVIVVDIC--GDDAAATAELVEAAGGKARARQVDVRDRAALKAAVAAGVEDFGR 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2930 LNGIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSGLLHVDECS----KDFPLDFFIFFSSVSG-CLGNAGQADYAAA---- 3000
Cdd:PRK12826    84 LDILVANAGIFPLTPFAEMDDEQWERVIDVNLTGTFLLTQAAlpalIRAGGGRIVLTSSVAGpRVGYPGLAHYAASkagl 163

                   ....*...
gi 1776025254 3001 NSFMDAFA 3008
Cdd:PRK12826   164 VGFTRALA 171
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
4173-4310 2.58e-08

classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187604 [Multi-domain]  Cd Length: 249  Bit Score: 58.45  E-value: 2.58e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4173 LLITGGTRGIGLLCARHFAEcyGVKKLVLTGREqlppreewarfktsntslAEKIQAVR-ELEAK-GVQVEMLSLTLSDD 4250
Cdd:cd05346      3 VLITGASSGIGEATARRFAK--AGAKLILTGRR------------------AERLQELAdELGAKfPVKVLPLQLDVSDR 62
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1776025254 4251 AQVEQTLQHIKRTLGPIGGVIHCAGLT-DMDTLAFIRKtsDDIQRVMEPKVSGLTTLYRHV 4310
Cdd:cd05346     63 ESIEAALENLPEEFRDIDILVNNAGLAlGLDPAQEADL--EDWETMIDTNVKGLLNVTRLI 121
ACSBG_like cd05933
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ...
1177-1403 3.70e-08

Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341256 [Multi-domain]  Cd Length: 596  Bit Score: 60.06  E-value: 3.70e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1177 QTLTYRELDERSTQLAIYL------QAHGVGpdrlagIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLEDSE 1250
Cdd:cd05933      7 HTLTYKEYYEACRQAAKAFlklgleRFHGVG------ILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1251 VFITLTTSE---------------LVNTLSWNGVTTALLDQ--DWDEIAQTA---SDRKVLTR--TVTPENLAYVIYTSG 1308
Cdd:cd05933     81 ANILVVENQkqlqkilqiqdklphLKAIIQYKEPLKEKEPNlySWDEFMELGrsiPDEQLDAIisSQKPNQCCTLIYTSG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1309 STGKPKGVMIPHKALTNFLVSMGETPGL-TAEDKMLAVTTY---CFdIAA--LELFLPLIKGAHCYICQtehtKDVEK-- 1380
Cdd:cd05933    161 TTGMPKGVMLSHDNITWTAKAASQHMDLrPATVGQESVVSYlplSH-IAAqiLDIWLPIKVGGQVYFAQ----PDALKgt 235
                          250       260
                   ....*....|....*....|....
gi 1776025254 1381 LKRDIRTIKPTVMQATPATW-KML 1403
Cdd:cd05933    236 LVKTLREVRPTAFMGVPRVWeKIQ 259
PLN02479 PLN02479
acetate-CoA ligase
400-556 3.87e-08

acetate-CoA ligase


Pssm-ID: 178097 [Multi-domain]  Cd Length: 567  Bit Score: 59.86  E-value: 3.87e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  400 IGRFQVSGLSVTSGYYQRPDLNESVFtEDGWFETGDLGFLR-NGRLTITGRTKDAIIINGINYYSHAIESAVEELSEI-E 477
Cdd:PLN02479   402 MGEIVMRGNMVMKGYLKNPKANEEAF-ANGWFHSGDLGVKHpDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVlE 480
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  478 TSYTAACAVRLGQNSTDqlaifFVT---SAKLNDEQmsQLLRNIQSHVSQVIgvtPEYLLP--VQKEEIPKTAIGKIQRT 552
Cdd:PLN02479   481 ASVVARPDERWGESPCA-----FVTlkpGVDKSDEA--ALAEDIMKFCRERL---PAYWVPksVVFGPLPKTATGKIQKH 550

                   ....
gi 1776025254  553 QLKT 556
Cdd:PLN02479   551 VLRA 554
PRK09192 PRK09192
fatty acyl-AMP ligase;
1179-1323 4.25e-08

fatty acyl-AMP ligase;


Pssm-ID: 236403 [Multi-domain]  Cd Length: 579  Bit Score: 59.63  E-value: 4.25e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1179 LTYRELDERSTQLAIYLQAHGVGP-DRLAGIyVDRSLDMLVGLLAILKAGGAYVPLdP---------SYpAERLEYMLED 1248
Cdd:PRK09192    50 LPYQTLRARAEAGARRLLALGLKPgDRVALI-AETDGDFVEAFFACQYAGLVPVPL-PlpmgfggreSY-IAQLRGMLAS 126
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1776025254 1249 SEVFITLTTSELVNTLswNGVTTAL---LDQDWDEIAQTASDRKVLTRtVTPENLAYVIYTSGSTGKPKGVMIPHKAL 1323
Cdd:PRK09192   127 AQPAAIITPDELLPWV--NEATHGNpllHVLSHAWFKALPEADVALPR-PTPDDIAYLQYSSGSTRFPRGVIITHRAL 201
PTZ00216 PTZ00216
acyl-CoA synthetase; Provisional
347-451 4.46e-08

acyl-CoA synthetase; Provisional


Pssm-ID: 240316 [Multi-domain]  Cd Length: 700  Bit Score: 59.60  E-value: 4.46e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  347 WGMSET-SSGVIfshefTRAGtsdDDHFVEIGSPIPGFSMRIVNdhnelVEE----------GEI---GRFqvsglsVTS 412
Cdd:PTZ00216   459 WGLTETvCCGGI-----QRTG---DLEPNAVGQLLKGVEMKLLD-----TEEykhtdtpeprGEIllrGPF------LFK 519
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1776025254  413 GYYQRPDLNESVFTEDGWFETGDLG-FLRNGRLTITGRTK 451
Cdd:PTZ00216   520 GYYKQEELTREVLDEDGWFHTGDVGsIAANGTLRIIGRVK 559
PTZ00342 PTZ00342
acyl-CoA synthetase; Provisional
1297-1582 5.31e-08

acyl-CoA synthetase; Provisional


Pssm-ID: 240370 [Multi-domain]  Cd Length: 746  Bit Score: 59.73  E-value: 5.31e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1297 PENLAYVIYTSGSTGKPKGVMIPHKALTNFLV-----SMGETPGLTAEDKMLAVT-TYCFDIAalelFLPLIKGAHCYIC 1370
Cdd:PTZ00342   303 PDFITSIVYTSGTSGKPKGVMLSNKNLYNTVVplckhSIFKKYNPKTHLSYLPIShIYERVIA----YLSFMLGGTINIW 378
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1371 qtehTKDVEKLKRDIRTIKPTVMQATPATWKMLF----------------------------YSGW-----ENEENVK-- 1415
Cdd:PTZ00342   379 ----SKDINYFSKDIYNSKGNILAGVPKVFNRIYtnimteinnlpplkrflvkkilslrksnNNGGfskflEGITHISsk 454
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1416 -----------ILCGGEAL-PETLKRYFLDTGSEAWNMFGPTETTIWSAVQRINDeCSRATIGRPIA-NTQIYITDSQLA 1482
Cdd:PTZ00342   455 ikdkvnpnlevILNGGGKLsPKIAEELSVLLNVNYYQGYGLTETTGPIFVQHADD-NNTESIGGPISpNTKYKVRTWETY 533
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1483 PVPAGVP-GELCIAGDGVAKGYYKKEELTDSRFIDNPFepgsklYRTGDMARWLPGGRIEYIGRIDNQVKI-RGFRIELG 1560
Cdd:PTZ00342   534 KATDTLPkGELLIKSDSIFSGYFLEKEQTKNAFTEDGY------FKTGDIVQINKNGSLTFLDRSKGLVKLsQGEYIETD 607
                          330       340
                   ....*....|....*....|....
gi 1776025254 1561 DIESRLSEHPGILECVVVAD--MD 1582
Cdd:PTZ00342   608 MLNNLYSQISFINFCVVYGDdsMD 631
PRK07798 PRK07798
acyl-CoA synthetase; Validated
170-457 5.68e-08

acyl-CoA synthetase; Validated


Pssm-ID: 236100 [Multi-domain]  Cd Length: 533  Bit Score: 59.13  E-value: 5.68e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  170 EDLLSA-EADTDWHQSSPEDLaLLLLTSGSTGTPKAVMLNHRNI-MSMVKGIIQMQGFTRED--------------ITFN 233
Cdd:PRK07798   146 EDALAAgSPERDFGERSPDDL-YLLYTGGTTGMPKGVMWRQEDIfRVLLGGRDFATGEPIEDeeelakraaagpgmRRFP 224
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  234 WMPFDHVGG-----IGMLhlrdvylgcqeinvSSETILMEPLKWLD----W--IDHYRASVtwapnfaFGLVTD-FA--- 298
Cdd:PRK07798   225 APPLMHGAGqwaafAALF--------------SGQTVVLLPDVRFDadevWrtIEREKVNV-------ITIVGDaMArpl 283
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  299 -EEIKDRK-WDLSSMRYMLNGGEAMVAKVGRRILELLePHGLPADAIrpawGMSETssGVIFSHEFTRAGTSDDDHFVEI 376
Cdd:PRK07798   284 lDALEARGpYDLSSLFAIASGGALFSPSVKEALLELL-PNVVLTDSI----GSSET--GFGGSGTVAKGAVHTGGPRFTI 356
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  377 GSpipgfSMRIVNDHNELVE--EGEIGRFQVSGlSVTSGYYQRPDLNESVFTE-DG--WFETGDLGFLRN-GRLTITGRt 450
Cdd:PRK07798   357 GP-----RTVVLDEDGNPVEpgSGEIGWIARRG-HIPLGYYKDPEKTAETFPTiDGvrYAIPGDRARVEAdGTITLLGR- 429

                   ....*..
gi 1776025254  451 kDAIIIN 457
Cdd:PRK07798   430 -GSVCIN 435
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
4172-4349 5.74e-08

sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, catalyzes the NADP-dependent reduction of sepiaptern to 7,8-dihydrobiopterin (BH2). In addition to SPRs, this subgroup also contains Bacillus cereus yueD, a benzil reductase, which catalyzes the stereospecific reduction of benzil to (S)-benzoin. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187625 [Multi-domain]  Cd Length: 241  Bit Score: 56.91  E-value: 5.74e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4172 VLLITGGTRGIGLLCARHFAECYGVKKLVLTGREQLPPREewarfktsntsLAEKIQAvreleakGVQVEMLSLTLSDDA 4251
Cdd:cd05367      1 VIILTGASRGIGRALAEELLKRGSPSVVVLLARSEEPLQE-----------LKEELRP-------GLRVTTVKADLSDAA 62
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4252 QVEQTLQHIKRTLGPIGGVIHCAG-LTDMDTLAFIrkTSDDIQRVMEPKVSG---LT-TLYRHVCNEPLQFFVLF-SSVS 4325
Cdd:cd05367     63 GVEQLLEAIRKLDGERDLLINNAGsLGPVSKIEFI--DLDELQKYFDLNLTSpvcLTsTLLRAFKKRGLKKTVVNvSSGA 140
                          170       180
                   ....*....|....*....|....
gi 1776025254 4326 AIIPELSAGQadYAMANSYMDYFA 4349
Cdd:cd05367    141 AVNPFKGWGL--YCSSKAARDMFF 162
PRK04319 PRK04319
acetyl-CoA synthetase; Provisional
174-436 6.49e-08

acetyl-CoA synthetase; Provisional


Pssm-ID: 235279 [Multi-domain]  Cd Length: 570  Bit Score: 59.14  E-value: 6.49e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  174 SAEADTDWhqSSPEDLALLLLTSGSTGTPKAVMLNHrNIMsmvkgIIQMQ-GFTREDitfnwmpfdhvggigmLHLRDVY 252
Cdd:PRK04319   194 SDEFDIEW--TDREDGAILHYTSGSTGKPKGVLHVH-NAM-----LQHYQtGKYVLD----------------LHEDDVY 249
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  253 ---------------------LGCQEINVSSEtilMEPLKWLDWIDHYRASVtW--APNfAFGLVTDFAEEIKdRKWDLS 309
Cdd:PRK04319   250 wctadpgwvtgtsygifapwlNGATNVIDGGR---FSPERWYRILEDYKVTV-WytAPT-AIRMLMGAGDDLV-KKYDLS 323
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  310 SMRYMLNGGEAM---VAKVGRRILellephGLPadaIRPAWGMSETSSGVIfsheftrAGTSDDDhfVEIGS---PIPGF 383
Cdd:PRK04319   324 SLRHILSVGEPLnpeVVRWGMKVF------GLP---IHDNWWMTETGGIMI-------ANYPAMD--IKPGSmgkPLPGI 385
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1776025254  384 SMRIVNDHNELVEEGEIGRFQV-SGL-SVTSGYYQRPDLNESVFtEDGWFETGDL 436
Cdd:PRK04319   386 EAAIVDDQGNELPPNRMGNLAIkKGWpSMMRGIWNNPEKYESYF-AGDWYVSGDS 439
PTZ00237 PTZ00237
acetyl-CoA synthetase; Provisional
192-551 8.25e-08

acetyl-CoA synthetase; Provisional


Pssm-ID: 240325 [Multi-domain]  Cd Length: 647  Bit Score: 58.98  E-value: 8.25e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  192 LLLTSGSTGTPKAVM---------LNHRNIMSMVKGIIQMQgFTREDItfNWMPFdHVGGIGMLHLRDVYlgcqeinVSS 262
Cdd:PTZ00237   259 ILYTSGTTGNSKAVVrsngphlvgLKYYWRSIIEKDIPTVV-FSHSSI--GWVSF-HGFLYGSLSLGNTF-------VMF 327
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  263 ETILMEPLKWLD--W--IDHYRASV--TWAPNFAFGLVTDFAEEIKDRKWDLSSMRYMLNGGEAMVAKVGRRILELLEph 336
Cdd:PTZ00237   328 EGGIIKNKHIEDdlWntIEKHKVTHtlTLPKTIRYLIKTDPEATIIRSKYDLSNLKEIWCGGEVIEESIPEYIENKLK-- 405
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  337 glpadaIRPAWGMSETSSGVIFSHEFTragtSDDDHFVEIGSPIPGFSMRIVNDHNELVEEGEIGRFQVS---GLSVTSG 413
Cdd:PTZ00237   406 ------IKSSRGYGQTEIGITYLYCYG----HINIPYNATGVPSIFIKPSILSEDGKELNVNEIGEVAFKlpmPPSFATT 475
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  414 YYQRPDLNESVFTE-DGWFETGDLGFL-RNGRLTITGRTKDAIIINGINYyshaiesaveELSEIETSYTAACAV----R 487
Cdd:PTZ00237   476 FYKNDEKFKQLFSKfPGYYNSGDLGFKdENGYYTIVSRSDDQIKISGNKV----------QLNTIETSILKHPLVleccS 545
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1776025254  488 LGQNSTDQLAIFFVTSAKLNDEQMSQL-LRNIQSHVSQVIGVTPEYLLPVQK----EEIPKTAIGKIQR 551
Cdd:PTZ00237   546 IGIYDPDCYNVPIGLLVLKQDQSNQSIdLNKLKNEINNIITQDIESLAVLRKiiivNQLPKTKTGKIPR 614
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
2853-3026 8.41e-08

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 56.56  E-value: 8.41e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2853 ITGGAGSLGLLFAKEIANRTGRstiVLTGRSVLSEDKENELEALRSIGAEVVYREADVSDQHAVHHLFEEIKERYGTLNG 2932
Cdd:PRK12938     8 VTGGMGGIGTSICQRLHKDGFK---VVAGCGPNSPRRVKWLEDQKALGFDFIASEGNVGDWDSTKAAFDKVKAEVGEIDV 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2933 IIHGAGSIKDHFIIHKTNEEFQEVLQPKVSGLLHVDECSKDFPLDF----FIFFSSVSGCLGNAGQADYAAANSFMDAFA 3008
Cdd:PRK12938    85 LVNNAGITRDVVFRKMTREDWTAVIDTNLTSLFNVTKQVIDGMVERgwgrIINISSVNGQKGQFGQTNYSTAKAGIHGFT 164
                          170
                   ....*....|....*...
gi 1776025254 3009 EYRRSLAASKKRFGSTIS 3026
Cdd:PRK12938   165 MSLAQEVATKGVTVNTVS 182
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
2852-2943 9.80e-08

classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka Tyrosine-dependent oxidoreductases) are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187628 [Multi-domain]  Cd Length: 228  Bit Score: 56.16  E-value: 9.80e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2852 LITGGAGSLGLLFAKEIANRTgrSTIVLTGRSvlsedkENELEALRSIGAEVVYREADVSDQHAVHHLFEEIKERYGTLN 2931
Cdd:cd05370      9 LITGGTSGIGLALARKFLEAG--NTVIITGRR------EERLAEAKKELPNIHTIVLDVGDAESVEALAEALLSEYPNLD 80
                           90
                   ....*....|..
gi 1776025254 2932 GIIHGAGSIKDH 2943
Cdd:cd05370     81 ILINNAGIQRPI 92
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
4169-4277 1.01e-07

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 56.51  E-value: 1.01e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4169 KDHVLLITGGTRGIGLLCARHFAECyGVKkLVLTGREQlppreewarfktsntslaEKIQ-AVRELEAKGVQVEMLSLTL 4247
Cdd:PRK08217     4 KDKVIVITGGAQGLGRAMAEYLAQK-GAK-LALIDLNQ------------------EKLEeAVAECGALGTEVRGYAANV 63
                           90       100       110
                   ....*....|....*....|....*....|
gi 1776025254 4248 SDDAQVEQTLQHIKRTLGPIGGVIHCAGLT 4277
Cdd:PRK08217    64 TDEEDVEATFAQIAEDFGQLNGLINNAGIL 93
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
592-665 1.02e-07

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 52.25  E-value: 1.02e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1776025254   592 REEIQEHLLTCLTEEL-HVSRDWVEPNANIQSLGVNSIKMMKLIRSIEKNYHIKLTAREIHQYPTIERLASYLSE 665
Cdd:smart00823   10 RRLLLDLVREQVAAVLgHAAAEAIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHLAA 84
PRK07867 PRK07867
acyl-CoA synthetase; Validated
138-239 1.18e-07

acyl-CoA synthetase; Validated


Pssm-ID: 236120 [Multi-domain]  Cd Length: 529  Bit Score: 58.15  E-value: 1.18e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  138 DKPAVITDRGmHQEMLDwakeqGLE-GFRAIIVE-----DLLSAEADTDWHQS--SPEDLALLLLTSGSTGTPKAVMLNH 209
Cdd:PRK07867   101 DCQLVLTESA-HAELLD-----GLDpGVRVINVDspawaDELAAHRDAEPPFRvaDPDDLFMLIFTSGTSGDPKAVRCTH 174
                           90       100       110
                   ....*....|....*....|....*....|
gi 1776025254  210 RNIMSMVKGIIQMQGFTREDITFNWMPFDH 239
Cdd:PRK07867   175 RKVASAGVMLAQRFGLGPDDVCYVSMPLFH 204
PRK12939 PRK12939
short chain dehydrogenase; Provisional
2850-2963 1.34e-07

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 56.13  E-value: 1.34e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGLLFAKEIAnRTGrSTIVLTgrSVLSEDKENELEALRSIGAEVVYREADVSDQHAVHHLFEEIKERYGT 2929
Cdd:PRK12939     9 RALVTGAARGLGAAFAEALA-EAG-ATVAFN--DGLAAEARELAAALEAAGGRAHAIAADLADPASVQRFFDAAAAALGG 84
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1776025254 2930 LNGIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSG 2963
Cdd:PRK12939    85 LDGLVNNAGITNSKSATELDIDTWDAVMNVNVRG 118
PRK06484 PRK06484
short chain dehydrogenase; Validated
2842-3016 1.75e-07

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 57.55  E-value: 1.75e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2842 HMPWRDEGVYLITGGAGSLGLLFAKEIANrtgrstivLTGRSVLSEDKENELEALRSI-GAEVVYREADVSDQHAVHHLF 2920
Cdd:PRK06484   263 SPLAESPRVVAITGGARGIGRAVADRFAA--------AGDRLLIIDRDAEGAKKLAEAlGDEHLSVQADITDEAAVESAF 334
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2921 EEIKERYGTLNGIIHGAGsIKDHFI--IHKTNEEFQEVLQPKVSGLLH-VDECSKDFPLDFFIF-FSSVSGCLGNAGQAD 2996
Cdd:PRK06484   335 AQIQARWGRLDVLVNNAG-IAEVFKpsLEQSAEDFTRVYDVNLSGAFAcARAAARLMSQGGVIVnLGSIASLLALPPRNA 413
                          170       180
                   ....*....|....*....|
gi 1776025254 2997 YAAANSFMDAFAeyrRSLAA 3016
Cdd:PRK06484   414 YCASKAAVTMLS---RSLAC 430
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
2850-2963 1.79e-07

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 55.62  E-value: 1.79e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLG----LLFAKEianrtGRSTIVLTGRSvlsEDKENELEA-LRSIGAEVVYREADVSDQHAVHHLFEEIK 2924
Cdd:PRK05565     7 VAIVTGASGGIGraiaELLAKE-----GAKVVIAYDIN---EEAAQELLEeIKEEGGDAIAVKADVSSEEDVENLVEQIV 78
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1776025254 2925 ERYGTLNGIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSG 2963
Cdd:PRK05565    79 EKFGKIDILVNNAGISNFGLVTDMTDEEWDRVIDVNLTG 117
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
4461-4533 1.96e-07

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 51.48  E-value: 1.96e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1776025254  4461 SETQSWLIDLFTEEL-----RIDREDFEIDGLFQDYGVDSIILAQVLQRINRKLEAALDPSILYEYPTIQRFTDWLIG 4533
Cdd:smart00823    7 AERRRLLLDLVREQVaavlgHAAAEAIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHLAA 84
E_NRPS cd19534
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
695-894 2.46e-07

Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Epimerization (E) domains of nonribosomal peptide synthetases (NRPS) flip the chirality of the end amino acid of a peptide being manufactured by the NRPS. E-domains are homologous to the Condensation (C) domains. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Specialized tailoring NRPS domains such as E-domains greatly increase the range of possible peptide products created by the NRPS machinery. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the E-domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380457 [Multi-domain]  Cd Length: 428  Bit Score: 56.88  E-value: 2.46e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  695 PLSEVQKglWTLQKMSPEKSAYHVPLCFKFSSGLHLETLQQAFGLVLNQHPILKHVIQEKDGVPILKNEPALSIEIKTEn 774
Cdd:cd19534      3 PLTPIQR--WFFEQNLAGRHHFNQSVLLRVPQGLDPDALRQALRALVEHHDALRMRFRREDGGWQQRIRGDVEELFRLE- 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  775 ISSMKESDIPAFLRKKVkEPYVK----ENSPLVRVMSFSRSEQEHFLLVVIHHLIFDGVSSVTFIHSLFDTYQLLLKGQQ 850
Cdd:cd19534     80 VVDLSSLAQAAAIEALA-AEAQSsldlEEGPLLAAALFDGTDGGDRLLLVIHHLVVDGVSWRILLEDLEAAYEQALAGEP 158
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1776025254  851 PEIAVSPAiYHDFAAWEKNMLAGKDGVKHRTYWQKQLSGTLPNL 894
Cdd:cd19534    159 IPLPSKTS-FQTWAELLAEYAQSPALLEELAYWRELPAADYWGL 201
PRK06147 PRK06147
3-oxoacyl-(acyl carrier protein) synthase; Validated
3500-3706 2.59e-07

3-oxoacyl-(acyl carrier protein) synthase; Validated


Pssm-ID: 235715 [Multi-domain]  Cd Length: 348  Bit Score: 56.18  E-value: 2.59e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3500 HGPSEPVETACSSSLVAIHRAVTAMQNGDCEMAIAGGVNTILTEEAHISYskagmlSKDGRCKTfSADANGYVRGEGVGM 3579
Cdd:PRK06147   123 EPGSAVIARGRVSGAVALAQARRLIAAGGCPRVLVAGVDSLLTGPTLAHY------EARDRLLT-SQNSNGFIPGEAAAA 195
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3580 VMLKKLEDAERDGNHIYGVIRGTAENHGGRANTLTSpnpkaQADLLVRAYRQAgIDPSTVTYieaHGTGTELGDpieING 3659
Cdd:PRK06147   196 VLLGRPAGGEAPGLPLLGLGLGREPAPVGESEDLPL-----RGDGLTQAIRAA-LAEAGCGL---EDMDYRIAD---LNG 263
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1776025254 3660 LKAAFKE--LSNMRGESQPD-VPDHRC---GIGSVKSNIGHLELAAGISGLIK 3706
Cdd:PRK06147   264 EQYRFKEaaLAEMRLFRVRKeFFDLWHpaeCIGEIGAAIGPALLGVALAASRK 316
PRK13388 PRK13388
acyl-CoA synthetase; Provisional
142-467 2.69e-07

acyl-CoA synthetase; Provisional


Pssm-ID: 237374 [Multi-domain]  Cd Length: 540  Bit Score: 56.96  E-value: 2.69e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  142 VITDRGmHQEMLDwakEQGLEGFRAIIVED-----LLSAEADTDWHQS-SPEDLALLLLTSGSTGTPKAVMLNHRNIMSM 215
Cdd:PRK13388   103 LVTDAE-HRPLLD---GLDLPGVRVLDVDTpayaeLVAAAGALTPHREvDAMDPFMLIFTSGTTGAPKAVRCSHGRLAFA 178
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  216 VKGIIQMQGFTREDITFNWMPfdhvggigMLHLRDVYLGCQEINVSSETILMEPlkwldwidHYRASvtwapnfafGLVT 295
Cdd:PRK13388   179 GRALTERFGLTRDDVCYVSMP--------LFHSNAVMAGWAPAVASGAAVALPA--------KFSAS---------GFLD 233
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  296 DFaeeikdRKWDLSSMRYmlnggeamvakVGRRILELLEPHGLPADA---IRPAWGmSETSSGVIfsHEFTRA------- 365
Cdd:PRK13388   234 DV------RRYGATYFNY-----------VGKPLAYILATPERPDDAdnpLRVAFG-NEASPRDI--AEFSRRfgcqved 293
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  366 --GTSD-------DDHFVE--IGSPIPGfsMRIVNDhnELVEEGEIGRFQVSG-----------LSVT------SGYYQR 417
Cdd:PRK13388   294 gyGSSEgavivvrEPGTPPgsIGRGAPG--VAIYNP--ETLTECAVARFDAHGallnadeaigeLVNTagagffEGYYNN 369
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1776025254  418 PDLNESVFtEDGWFETGDLGFL-RNGRLTITGRTKDAIIINGINYYSHAIE 467
Cdd:PRK13388   370 PEATAERM-RHGMYWSGDLAYRdADGWIYFAGRTADWMRVDGENLSAAPIE 419
PRK06198 PRK06198
short chain dehydrogenase; Provisional
2847-2938 3.01e-07

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 55.40  E-value: 3.01e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2847 DEGVYLITGGAGSLGLLFAKEIANRtGRSTIVLTGRS-VLSEDKENELEALrsiGAEVVYREADVSDQHAVHHLFEEIKE 2925
Cdd:PRK06198     5 DGKVALVTGGTQGLGAAIARAFAER-GAAGLVICGRNaEKGEAQAAELEAL---GAKAVFVQADLSDVEDCRRVVAAADE 80
                           90
                   ....*....|...
gi 1776025254 2926 RYGTLNGIIHGAG 2938
Cdd:PRK06198    81 AFGRLDALVNAAG 93
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
4169-4341 3.33e-07

mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes the conversion of fructose to mannitol, an acyclic 6-carbon sugar. MDH is a tetrameric member of the SDR family. This subgroup also includes various other tetrameric SDRs, including Pichia stipitis D-arabinitol dehydrogenase (aka polyol dehydrogenase), Candida albicans Sou1p, a sorbose reductase, and Candida parapsilosis (S)-specific carbonyl reductase (SCR, aka S-specific alcohol dehydrogenase) which catalyzes the enantioselective reduction of 2-hydroxyacetophenone into (S)-1-phenyl-1,2-ethanediol. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser).


Pssm-ID: 187610 [Multi-domain]  Cd Length: 252  Bit Score: 55.03  E-value: 3.33e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4169 KDHVLLITGGTRGIGLLCARHFAEcYGVKKLVLTGREqlpPREEWArfktsntslAEKIQavrelEAKGVQVEMLSLTLS 4248
Cdd:cd05352      7 KGKVAIVTGGSRGIGLAIARALAE-AGADVAIIYNSA---PRAEEK---------AEELA-----KKYGVKTKAYKCDVS 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4249 DDAQVEQTLQHIKRTLGPIGGVIHCAGLTdmDTLAFIRKTSDDIQRVMEPKVSGLTtlyrHVCNEPLQFF--------VL 4320
Cdd:cd05352     69 SQESVEKTFKQIQKDFGKIDILIANAGIT--VHKPALDYTYEQWNKVIDVNLNGVF----NCAQAAAKIFkkqgkgslII 142
                          170       180
                   ....*....|....*....|.
gi 1776025254 4321 FSSVSAIIPELSAGQADYAMA 4341
Cdd:cd05352    143 TASMSGTIVNRPQPQAAYNAS 163
PT_fungal_PKS TIGR04532
iterative type I PKS product template domain; Sequences found by this model are the so-called ...
2381-2580 3.99e-07

iterative type I PKS product template domain; Sequences found by this model are the so-called product template (PT) domain of various fungal iterative type I polyketide synthases. This domain resembles pfam14765, designated polyketide synthase dehydratase by Pfam, but members of that family are primarily bacterial, where type I PKS are predominantly modular, not iterative. The dehydratase active site residues well-conserved in pfam14765 (His in the first hot dog domain, Asp in the second hot dog domain) seem well conserved in this family also.


Pssm-ID: 275325  Cd Length: 324  Bit Score: 55.71  E-value: 3.99e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2381 SDFSEQKFSSVFTGdefflrdHVVRGKPVLPGVAYLEMAYAAIN----QAAGSEIGQDVRIRLNHTVWVQPVVVD----- 2451
Cdd:TIGR04532   23 SDLSDPDLLAAIQG-------HRVNGVPLCPSSVYADMALTAAKyllkRLRGSKDAADVGLDVRDMEVDKPLVADpsdsd 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2452 ----RHSAQVDISLfpeeDGKITFDIYSTQEDGDDPVIHSQGSAELASAAETPVAD----LTEISRRC---------GKG 2514
Cdd:TIGR04532   96 pqllRVTATADAST----SSRVSISFSSSSSSGKKTEEHATCTVRFGDPAAAWLAEwsrtAYLVKSRIdalrqsakeGSA 171
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1776025254 2515 -KMSPDQFYEegrsrgMF-----HGPAFQGIKNVNI--GNREVLAQLQLPEIVSGTNeqFVLHPSIMDSALQTA 2580
Cdd:TIGR04532  172 hRLSRRMAYK------LFsslvdYSPKYRGMQEVVLdsDGLEATATVKLPTDPPDGG--FTVSPYWIDSLLHLA 237
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
2863-3017 4.08e-07

Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) reductases.


Pssm-ID: 433310 [Multi-domain]  Cd Length: 236  Bit Score: 54.36  E-value: 4.08e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2863 LFAKEIANrtgrstIVLTGRSvlsEDKENELEAL-RSIGAEVVyrEADVSDQHAVHHLFEEIKERYGTLNGIIHGAG-SI 2940
Cdd:pfam13561   15 ALAEEGAE------VVLTDLN---EALAKRVEELaEELGAAVL--PCDVTDEEQVEALVAAAVEKFGRLDILVNNAGfAP 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2941 KDHFIIHKTN-EEFQEVLQPKVSGLLHvdeCSKDFpLDFF------IFFSSVSGCLGNAGQADYAAANSFMDAFAeyrRS 3013
Cdd:pfam13561   84 KLKGPFLDTSrEDFDRALDVNLYSLFL---LAKAA-LPLMkeggsiVNLSSIGAERVVPNYNAYGAAKAALEALT---RY 156

                   ....
gi 1776025254 3014 LAAS 3017
Cdd:pfam13561  157 LAVE 160
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
2850-2938 5.45e-07

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 54.52  E-value: 5.45e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGLLFAKEIAnRTGRSTIVLtGRSVlsEDKENELEALRSIGAEVVYREADVSDQHAVHHLFEEIKERYGT 2929
Cdd:PRK08277    12 VAVITGGGGVLGGAMAKELA-RAGAKVAIL-DRNQ--EKAEAVVAEIKAAGGEALAVKADVLDKESLEQARQQILEDFGP 87

                   ....*....
gi 1776025254 2930 LNGIIHGAG 2938
Cdd:PRK08277    88 CDILINGAG 96
hsFATP2a_ACSVL_like cd05938
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ...
1174-1340 5.76e-07

Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341261 [Multi-domain]  Cd Length: 537  Bit Score: 55.76  E-value: 5.76e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1174 YEGQTLTYRELDERSTQLAIYLQAH-GVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLEDSEVF 1252
Cdd:cd05938      1 FEGETYTYRDVDRRSNQAARALLAHaGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1253 ITLTTSELVNT-------LSWNGV-------------TTALLDQdwdeiAQTASDRKV---LTRTVTPENLAYVIYTSGS 1309
Cdd:cd05938     81 VLVVAPELQEAveevlpaLRADGVsvwylshtsntegVISLLDK-----VDAASDEPVpasLRAHVTIKSPALYIYTSGT 155
                          170       180       190
                   ....*....|....*....|....*....|....
gi 1776025254 1310 TGKPKGVMIPHK---ALTNFLvsmgETPGLTAED 1340
Cdd:cd05938    156 TGLPKAARISHLrvlQCSGFL----SLCGVTADD 185
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
4174-4310 6.99e-07

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 54.18  E-value: 6.99e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4174 LITGGTRGIGLLCARHFAEcYGVkKLVLTGREQlppreewarfktsntslAEKIQAVRELEAKGVQVEMLSLTLSDDAQV 4253
Cdd:PRK08213    16 LVTGGSRGLGLQIAEALGE-AGA-RVVLSARKA-----------------EELEEAAAHLEALGIDALWIAADVADEADI 76
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1776025254 4254 EQTLQHIKRTLGPIGGVIHCAGLT------DMDTLAFirktsddiQRVMEPKVSGLTTLYRHV 4310
Cdd:PRK08213    77 ERLAEETLERFGHVDILVNNAGATwgapaeDHPVEAW--------DKVMNLNVRGLFLLSQAV 131
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
3909-4006 7.68e-07

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 56.03  E-value: 7.68e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3909 LADLWVKGVSIQWNTLYGETKPRLISLPSYPFAKDHYWVPAKEHSERDKKELVNAIEDRAACFLTKQWSLSPIGSAVPGT 3988
Cdd:COG3321    837 LAQLWVAGVPVDWSALYPGRGRRRVPLPTYPFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAA 916
                           90
                   ....*....|....*...
gi 1776025254 3989 RTVAILCCQETADLAAEV 4006
Cdd:COG3321    917 AALALAAAALAALLALVA 934
PRK07768 PRK07768
long-chain-fatty-acid--CoA ligase; Validated
1175-1563 8.41e-07

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236091 [Multi-domain]  Cd Length: 545  Bit Score: 55.39  E-value: 8.41e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1175 EGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYP----------AERLEY 1244
Cdd:PRK07768    26 APVRHTWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTMLHQPTPrtdlavwaedTLRVIG 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1245 MLEDSEVFITLTTSELVNTLSWNGVTTALLDQDWDEiaqtASDRKVLTrtvTPENLAYVIYTSGSTGKPKGVMIPHKALT 1324
Cdd:PRK07768   106 MIGAKAVVVGEPFLAAAPVLEEKGIRVLTVADLLAA----DPIDPVET---GEDDLALMQLTSGSTGSPKAVQITHGNLY 178
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1325 NFLVSMGETPGLTAE-DKMLAVTTYCFDIAALE-LFLPLIKGAhcyicqtehtkdveklkrDIRTIKPTVMQATPATWKM 1402
Cdd:PRK07768   179 ANAEAMFVAAEFDVEtDVMVSWLPLFHDMGMVGfLTVPMYFGA------------------ELVKVTPMDFLRDPLLWAE 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1403 LF--------------YS------------GWENEENVKI-LCGGEAL-PETLKRyFLDTG------SEAW-NMFGPTET 1447
Cdd:PRK07768   241 LIskyrgtmtaapnfaYAllarrlrrqakpGAFDLSSLRFaLNGAEPIdPADVED-LLDAGarfglrPEAIlPAYGMAEA 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1448 TI------WSAVQRINDEC-------------------SRATIGRPIANTQIYITDSQLAPVPAGVPGELCIAGDGVAKG 1502
Cdd:PRK07768   320 TLavsfspCGAGLVVDEVDadllaalrravpatkgntrRLATLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRGESVTPG 399
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1776025254 1503 YykkeeLTDSRFIdnPFEPGSKLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIE 1563
Cdd:PRK07768   400 Y-----LTMDGFI--PAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIE 453
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
2313-2347 1.02e-06

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 55.65  E-value: 1.02e-06
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1776025254 2313 LAEMWSKGAHIDWMQLYKGERPNRMSLPTYPFAKE 2347
Cdd:COG3321    837 LAQLWVAGVPVDWSALYPGRGRRRVPLPTYPFQRE 871
PRK07791 PRK07791
short chain dehydrogenase; Provisional
2850-3000 1.18e-06

short chain dehydrogenase; Provisional


Pssm-ID: 236099 [Multi-domain]  Cd Length: 286  Bit Score: 53.91  E-value: 1.18e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLG----LLFAKEIA----NRTGRStivLTGRSVLSEDKENELEALRSIGAEVVYREADVSDQHAVHHLFE 2921
Cdd:PRK07791     8 VVIVTGAGGGIGrahaLAFAAEGArvvvNDIGVG---LDGSASGGSAAQAVVDEIVAAGGEAVANGDDIADWDGAANLVD 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2922 EIKERYGTLNGIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSG---LLHV------DECSKDFPLDFFIF-FSSVSGCLGN 2991
Cdd:PRK07791    85 AAVETFGGLDVLVNNAGILRDRMIANMSEEEWDAVIAVHLKGhfaTLRHaaaywrAESKAGRAVDARIInTSSGAGLQGS 164

                   ....*....
gi 1776025254 2992 AGQADYAAA 3000
Cdd:PRK07791   165 VGQGNYSAA 173
PRK12826 PRK12826
SDR family oxidoreductase;
4172-4303 1.52e-06

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 53.00  E-value: 1.52e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4172 VLLITGGTRGIGLLCARHFAEcYGVKKLVLTgreqlppreewarfkTSNTSLAEkiqAVRELEAKGVQVEMLSLTLSDDA 4251
Cdd:PRK12826     8 VALVTGAARGIGRAIAVRLAA-DGAEVIVVD---------------ICGDDAAA---TAELVEAAGGKARARQVDVRDRA 68
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1776025254 4252 QVEQTLQHIKRTLGPIGGVIHCAGLTDMDTLAFIrkTSDDIQRVMEPKVSGL 4303
Cdd:PRK12826    69 ALKAAVAAGVEDFGRLDILVANAGIFPLTPFAEM--DDEQWERVIDVNLTGT 118
PRK07109 PRK07109
short chain dehydrogenase; Provisional
4172-4297 2.09e-06

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 53.39  E-value: 2.09e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4172 VLLITGGTRGIGLLCARHFAEcYGVKKLVLtgreqlppreewARfktSNTSLAEkiqAVRELEAKGVQVEMLSLTLSDDA 4251
Cdd:PRK07109    10 VVVITGASAGVGRATARAFAR-RGAKVVLL------------AR---GEEGLEA---LAAEIRAAGGEALAVVADVADAE 70
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1776025254 4252 QVEQTLQHIKRTLGPIGGVIHCAGLTDMDTlaFIRKTSDDIQRVME 4297
Cdd:PRK07109    71 AVQAAADRAEEELGPIDTWVNNAMVTVFGP--FEDVTPEEFRRVTE 114
ttLC_FACS_like cd05915
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
1168-1639 2.13e-06

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.


Pssm-ID: 213283 [Multi-domain]  Cd Length: 509  Bit Score: 53.97  E-value: 2.13e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1168 DRAAVSYEGQTL-----TYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERL 1242
Cdd:cd05915      9 GRKEVVSRLHTGevhrtTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEI 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1243 EYMLEDSEVFITLTTSE----------LVNTLSWNGVTTALLDQdWDEIAQTASDRKVLTRTVTPENLAYVIYTSGSTGK 1312
Cdd:cd05915     89 AYILNHAEDKVLLFDPNllplveairgELKTVQHFVVMDEKAPE-GYLAYEEALGEEADPVRVPERAACGMAYTTGTTGL 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1313 PKGVMIPHKALTNFLVSMG--------ETPGLTAEDKMLAVTTYCFdIAALELFLPLIkgahcyICQTEHTKDvEKLKRD 1384
Cdd:cd05915    168 PKGVVYSHRALVLHSLAASlvdgtalsEKDVVLPVVPMFHVNAWCL-PYAATLVGAKQ------VLPGPRLDP-ASLVEL 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1385 IRTIKPTVMQATPATWKMLFYSGWENEEN----VKILCGGEALPET------LKRYFLDTGSEAWNMFGPTETTIW-SAV 1453
Cdd:cd05915    240 FDGEGVTFTAGVPTVWLALADYLESTGHRlktlRRLVVGGSAAPRSliarfeRMGVEVRQGYGLTETSPVVVQNFVkSHL 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1454 QRINDECSRATIGRPIANTQIYITDSqLAPVPAGVPGE------LCIAGDGVAKGYYKKEELTDSrfidNPFEPGskLYR 1527
Cdd:cd05915    320 ESLSEEEKLTLKAKTGLPIPLVRLRV-ADEEGRPVPKDgkalgeVQLKGPWITGGYYGNEEATRS----ALTPDG--FFR 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1528 TGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMD-----NLAAYYTAKHANASltAREL 1602
Cdd:cd05915    393 TGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHpkwqeRPLAVVVPRGEKPT--PEEL 470
                          490       500       510
                   ....*....|....*....|....*....|....*...
gi 1776025254 1603 RHFVKNALPAY-MVPSYFIQLDHMPLTPNGKIDRNSLK 1639
Cdd:cd05915    471 NEHLLKAGFAKwQLPDAYVFAEEIPRTSAGKFLKRALR 508
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
2850-3008 2.15e-06

Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR which catalyzes the NADPH-dependent reduction of ketones on steroids and prostaglandins. Unlike most SDRs, PTCR functions as a monomer. This subgroup also includes human carbonyl reductase 1 (CBR1) and CBR3. CBR1 is an NADPH-dependent SDR with broad substrate specificity and may be responsible for the in vivo reduction of quinones, prostaglandins, and other carbonyl-containing compounds. In addition it includes poppy NADPH-dependent salutaridine reductase which catalyzes the stereospecific reduction of salutaridine to 7(S)-salutaridinol in the biosynthesis of morphine, and Arabidopsis SDR1,a menthone reductase, which catalyzes the reduction of menthone to neomenthol, a compound with antimicrobial activity; SDR1 can also carry out neomenthol oxidation. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187585 [Multi-domain]  Cd Length: 225  Bit Score: 52.24  E-value: 2.15e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGLLFAKEIANRtGRSTIVLTGRSVlsEDKENELEALRSIGAEVVYREADVSDQHAVHHLFEEIKERYGT 2929
Cdd:cd05324      2 VALVTGANRGIGFEIVRQLAKS-GPGTVILTARDV--ERGQAAVEKLRAEGLSVRFHQLDVTDDASIEAAADFVEEKYGG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2930 LNGIIHGAGSIKDHFIIHKTN-EEFQEVLQPKVSGLLHVDECS----KDFPLDFFIFFSSVSGCLGNAGQADYAAANSFM 3004
Cdd:cd05324     79 LDILVNNAGIAFKGFDDSTPTrEQARETMKTNFFGTVDVTQALlpllKKSPAGRIVNVSSGLGSLTSAYGVSKAALNALT 158

                   ....
gi 1776025254 3005 DAFA 3008
Cdd:cd05324    159 RILA 162
omega_3_PfaA TIGR02813
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ...
2398-2647 2.27e-06

polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this alignment are involved in omega-3 polyunsaturated fatty acid biosynthesis, such as the protein PfaA from the eicosapentaenoic acid biosynthesis operon in Photobacterium profundum strain SS9. PfaA is encoded together with PfaB, PfaC, and PfaD, and the functions of the individual polypeptides have not yet been described. More distant homologs of PfaA, also included with the reach of this model, appear to be involved in polyketide-like biosynthetic mechanisms of polyunsaturated fatty acid biosynthesis, an alternative to the more familiar iterated mechanism of chain extension and desaturation, and in most cases are encoded near genes for homologs of PfaB, PfaC, and/or PfaD.


Pssm-ID: 274311 [Multi-domain]  Cd Length: 2582  Bit Score: 54.63  E-value: 2.27e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2398 FLRDHVVRGKPVLPGVAylemAYAAINQAAGSEIGQDVRIRlNHTVwVQPVVVDRHSAQVDISLFPEEDGKITFD---IY 2474
Cdd:TIGR02813 2310 FIADHCIGGDKVLPTVC----AIAWMREAAMVALGAFVGVA-DYKL-LKGVIFDGSEATEYIDMILQLELTPLVVdtkIS 2383
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2475 STQEDGDdPVIHSQGSAELASAAET---PVADL---TEISRRCGKGKMSPDQFYEEGRSRG-MFHGPAFQGIKNVNIGNR 2547
Cdd:TIGR02813 2384 TTNEQAL-ISFHYRPQYTAVLVAERkeaPTAELflpEALPELLPETVLSSIEEAGALYSNGtLFHGPRLQGIKAVLAFDD 2462
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2548 E-VLAQLQLPEIVSGTNEQFVlhPSIMDSALQT-------ATICIMQELTDQKLILPFALEELEVIKGCSSSMWAYARLS 2619
Cdd:TIGR02813 2463 QgLLAKCQLPAVASLDCGEFP--PSPLNSGSQPfaedillQAMLVWARLKYGAASLPSSIGEFVSYRPVSLGEKFYLKLD 2540
                          250       260
                   ....*....|....*....|....*...
gi 1776025254 2620 DSDHSGGVVQkADIDVIDESGSVCVRIK 2647
Cdd:TIGR02813 2541 VVKSSGRSLV-ANIELYHQDGRLSSEMK 2567
PRK13391 PRK13391
acyl-CoA synthetase; Provisional
51-467 2.98e-06

acyl-CoA synthetase; Provisional


Pssm-ID: 184022 [Multi-domain]  Cd Length: 511  Bit Score: 53.54  E-value: 2.98e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254   51 LQPDGTEVyqSYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNSQLLPAFWG---------CVLTGVVPAPLAvpptYA 121
Cdd:PRK13391    18 MASTGEVV--TYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAaersglyytCVNSHLTPAEAA----YI 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  122 ESSSGTQKLKDAWTLLDKPAVITD---RGMHQEMLDWAKEqgLEGFRAiiVEDLLSAEADTDWHQSSPEDLalLLLTSGS 198
Cdd:PRK13391    92 VDDSGARALITSAAKLDVARALLKqcpGVRHRLVLDGDGE--LEGFVG--YAEAVAGLPATPIADESLGTD--MLYSSGT 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  199 TGTPKAVM--LNHRNI---MSMVKGIIQMQGFTREDITFNWMPFDHVGGigmlhLRDVYLGcqeINVSSETILME---PL 270
Cdd:PRK13391   166 TGRPKGIKrpLPEQPPdtpLPLTAFLQRLWGFRSDMVYLSPAPLYHSAP-----QRAVMLV---IRLGGTVIVMEhfdAE 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  271 KWLDWIDHYRASVT-WAPNFaFGLVTDFAEEIKDRkWDLSSMRYMLNGGEAMVAKVGRRILELLEPhglpadAIRPAWGM 349
Cdd:PRK13391   238 QYLALIEEYGVTHTqLVPTM-FSRMLKLPEEVRDK-YDLSSLEVAIHAAAPCPPQVKEQMIDWWGP------IIHEYYAA 309
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  350 SEtSSGVIF--SHEF-TRAGTsdddhfveIGSPIPGfSMRIVNDHNELVEEGEIGRFQVSGLSVTSgYYQRPD-LNESVF 425
Cdd:PRK13391   310 TE-GLGFTAcdSEEWlAHPGT--------VGRAMFG-DLHILDDDGAELPPGEPGTIWFEGGRPFE-YLNDPAkTAEARH 378
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|...
gi 1776025254  426 TEDGWFETGDLGFL-RNGRLTITGRTKDAIIINGINYYSHAIE 467
Cdd:PRK13391   379 PDGTWSTVGDIGYVdEDGYLYLTDRAAFMIISGGVNIYPQEAE 421
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
2850-3015 3.13e-06

tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6,8-tetrahydroxynaphthalene reductase (4HNR) of Magnaporthe grisea and the related 1,3,8-trihydroxynaphthalene reductase (3HNR) are typical members of the SDR family containing the canonical glycine rich NAD(P)-binding site and active site tetrad, and function in fungal melanin biosynthesis. This subgroup also includes an SDR from Norway spruce that may function to protect against both biotic and abitoic stress. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187620 [Multi-domain]  Cd Length: 243  Bit Score: 51.89  E-value: 3.13e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGLLFAKEIANRtGRSTIVLTGRSvlSEDKENELEALRSIGAEVVYREADVSDQHAVHHLFEEIKERYGT 2929
Cdd:cd05362      5 VALVTGASRGIGRAIAKRLARD-GASVVVNYASS--KAAAEEVVAEIEAAGGKAIAVQADVSDPSQVARLFDAAEKAFGG 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2930 LNGIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSGLLHV-DECSKDF-PLDFFIFFSSVSGCLGNAGQADYAAANSFMDAF 3007
Cdd:cd05362     82 VDILVNNAGVMLKKPIAETSEEEFDRMFTVNTKGAFFVlQEAAKRLrDGGRIINISSSLTAAYTPNYGAYAGSKAAVEAF 161

                   ....*...
gi 1776025254 3008 AeyrRSLA 3015
Cdd:cd05362    162 T---RVLA 166
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
4172-4340 3.60e-06

HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC 7120 HetN, a putative oxidoreductase involved in heterocyst differentiation, and related proteins. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212493 [Multi-domain]  Cd Length: 223  Bit Score: 51.59  E-value: 3.60e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4172 VLLITGGTRGIGLLCARHFAECYgvKKLVLTGREQlppreewarfktsntslaekiQAVRELEAKGVQVEMLSLTLSDDA 4251
Cdd:cd08932      2 VALVTGASRGIGIEIARALARDG--YRVSLGLRNP---------------------EDLAALSASGGDVEAVPYDARDPE 58
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4252 QVEQTLQHIKRTLGPIGGVIHCAGLTDMDTLAFIrkTSDDIQRVMEPKVSGLTTLYR----HVCNEPLQFFVLFSSVSAI 4327
Cdd:cd08932     59 DARALVDALRDRFGRIDVLVHNAGIGRPTTLREG--SDAELEAHFSINVIAPAELTRallpALREAGSGRVVFLNSLSGK 136
                          170
                   ....*....|...
gi 1776025254 4328 IPElsAGQADYAM 4340
Cdd:cd08932    137 RVL--AGNAGYSA 147
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
4169-4339 4.24e-06

17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as amyloid-peptide-binding alcohol dehydrogenase (ABAD), was previously identified as a L-3-hydroxyacyl-CoA dehydrogenase, HADH2. In fatty acid metabolism, HADH2 catalyzes the third step of beta-oxidation, the conversion of a hydroxyl to a keto group in the NAD-dependent oxidation of L-3-hydroxyacyl CoA. In addition to alcohol dehydrogenase and HADH2 activites, HSD10 has steroid dehydrogenase activity. Although the mechanism is unclear, HSD10 is implicated in the formation of amyloid beta-petide in the brain (which is linked to the development of Alzheimer's disease). Although HSD10 is normally concentrated in the mitochondria, in the presence of amyloid beta-peptide it translocates into the plasma membrane, where it's action may generate cytotoxic aldehydes and may lower estrogen levels through its use of 17-beta-estradiol as a substrate. HSD10 is a member of the SRD family, but differs from other SDRs by the presence of two insertions of unknown function. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187629 [Multi-domain]  Cd Length: 252  Bit Score: 51.52  E-value: 4.24e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4169 KDHVLLITGGTRGIGLLCARHFAEcYGVKKLVLtgreQLPPreewarfktsntslaEKIQAVRELEAKGVQVEmlsLTLS 4248
Cdd:cd05371      1 KGLVAVVTGGASGLGLATVERLLA-QGAKVVIL----DLPN---------------SPGETVAKLGDNCRFVP---VDVT 57
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4249 DDAQVEQTLQHIKRTLGPIGGVIHCAGLtdmdTLAFirKT----------SDDIQRVMEPKVSGLTTLYRHVC-----NE 4313
Cdd:cd05371     58 SEKDVKAALALAKAKFGRLDIVVNCAGI----AVAA--KTynkkgqqphsLELFQRVINVNLIGTFNVIRLAAgamgkNE 131
                          170       180       190
                   ....*....|....*....|....*....|.
gi 1776025254 4314 PLQF-----FVLFSSVSAIipELSAGQADYA 4339
Cdd:cd05371    132 PDQGgergvIINTASVAAF--EGQIGQAAYS 160
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
4171-4339 5.04e-06

3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These proteins include members identified as KDSR, ribitol type dehydrogenase, and others. The group shows strong conservation of the active site tetrad and glycine rich NAD-binding motif of the classical SDRs. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187643 [Multi-domain]  Cd Length: 239  Bit Score: 51.10  E-value: 5.04e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4171 HVLlITGGTRGIGLLCARHFAEcYGvKKLVLTGReqlppreewarfktSNTSLAEKIQAVR-ELEAKGVQVEMLSLTLSD 4249
Cdd:cd08939      3 HVL-ITGGSSGIGKALAKELVK-EG-ANVIIVAR--------------SESKLEEAVEEIEaEANASGQKVSYISADLSD 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4250 DAQVEQTLQHIKRTLGPIGGVIHCAG------LTDMdtlafirkTSDDIQRVMEpkVSGLTTLY------RHVCNEPLQF 4317
Cdd:cd08939     66 YEEVEQAFAQAVEKGGPPDLVVNCAGisipglFEDL--------TAEEFERGMD--VNYFGSLNvahavlPLMKEQRPGH 135
                          170       180
                   ....*....|....*....|..
gi 1776025254 4318 FVLFSSVSAIIPelSAGQADYA 4339
Cdd:cd08939    136 IVFVSSQAALVG--IYGYSAYC 155
PRK00174 PRK00174
acetyl-CoA synthetase; Provisional
1168-1641 5.10e-06

acetyl-CoA synthetase; Provisional


Pssm-ID: 234677 [Multi-domain]  Cd Length: 637  Bit Score: 52.84  E-value: 5.10e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1168 DRAAVSYEG------QTLTYRELDERSTQLAIYLQAHGVGP-DRLAgIYvdrsLDMLV-GLLAILKA-----------GG 1228
Cdd:PRK00174    82 DKVAIIWEGddpgdsRKITYRELHREVCRFANALKSLGVKKgDRVA-IY----MPMIPeAAVAMLACarigavhsvvfGG 156
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1229 ayvpldpsYPAERLEYMLEDSE--VFIT--------------------LTTSELVNT---LSWNGVTTALL---DQDWDE 1280
Cdd:PRK00174   157 --------FSAEALADRIIDAGakLVITadegvrggkpiplkanvdeaLANCPSVEKvivVRRTGGDVDWVegrDLWWHE 228
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1281 IAQTASDrkvltrTVTPENLA-----YVIYTSGSTGKPKGVMipHkaltnflvsmgeTPG--LTaedkmLAVTT--YCFD 1351
Cdd:PRK00174   229 LVAGASD------ECEPEPMDaedplFILYTSGSTGKPKGVL--H------------TTGgyLV-----YAAMTmkYVFD 283
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1352 IAALELF-----LPLIKGaHCYIcqtehtkdveklkrdirTIKPTVMQATpatwkMLFYSG----------WE--NEENV 1414
Cdd:PRK00174   284 YKDGDVYwctadVGWVTG-HSYI-----------------VYGPLANGAT-----TLMFEGvpnypdpgrfWEviDKHKV 340
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1415 KILC-----------GGEALPetlKRYFLDT----GS-------EAWNMFgptettiwsavqrindecsRATIGR---PI 1469
Cdd:PRK00174   341 TIFYtaptairalmkEGDEHP---KKYDLSSlrllGSvgepinpEAWEWY-------------------YKVVGGercPI 398
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1470 ANT-------QIYIT-------------------------DSQLAPVPAGVPGELCIAGD--GVAKGYYKKEEltdsRFI 1515
Cdd:PRK00174   399 VDTwwqtetgGIMITplpgatplkpgsatrplpgiqpavvDEEGNPLEGGEGGNLVIKDPwpGMMRTIYGDHE----RFV 474
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1516 DNPFEPGSKLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMDNLA-----AYYTA 1590
Cdd:PRK00174   475 KTYFSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKgqgiyAFVTL 554
                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1776025254 1591 KH---ANASLtARELRHFVKNALPAYMVPSyFIQL-DHMPLTPNGKIDRNSLKNI 1641
Cdd:PRK00174   555 KGgeePSDEL-RKELRNWVRKEIGPIAKPD-VIQFaPGLPKTRSGKIMRRILRKI 607
PRK06484 PRK06484
short chain dehydrogenase; Validated
2850-3015 5.64e-06

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 52.54  E-value: 5.64e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGLLFAKEIANrtgrstivlTGRSVLSEDKENE--LEALRSIGAEVVYREADVSDQHAVHHLFEEIKERY 2927
Cdd:PRK06484     7 VVLVTGAAGGIGRAACQRFAR---------AGDQVVVADRNVEraRERADSLGPDHHALAMDVSDEAQIREGFEQLHREF 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2928 GTLNGIIHGAGsIKDHF---IIHKTNEEFQEVLQPKVSG-LLHVDECSK----DFPLDFFIFFSSVSGCLGNAGQADYAA 2999
Cdd:PRK06484    78 GRIDVLVNNAG-VTDPTmtaTLDTTLEEFARLQAINLTGaYLVAREALRlmieQGHGAAIVNVASGAGLVALPKRTAYSA 156
                          170
                   ....*....|....*.
gi 1776025254 3000 ANSFMDAFAeyrRSLA 3015
Cdd:PRK06484   157 SKAAVISLT---RSLA 169
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
2847-3025 7.15e-06

(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids in eukaryotes occurs by a four-reaction cycle, that may take place in mitochondria or in peroxisomes. (3R)-hydroxyacyl-CoA dehydrogenase is part of rat peroxisomal multifunctional MFE-2, it is a member of the NAD-dependent SDRs, but contains an additional small C-terminal domain that completes the active site pocket and participates in dimerization. The atypical, additional C-terminal extension allows for more extensive dimerization contact than other SDRs. MFE-2 catalyzes the second and third reactions of the peroxisomal beta oxidation cycle. Proteins in this subgroup have a typical catalytic triad, but have a His in place of the usual upstream Asn. This subgroup also contains members identified as 17-beta-hydroxysteroid dehydrogenases, including human peroxisomal 17-beta-hydroxysteroid dehydrogenase type 4 (17beta-HSD type 4, aka MFE-2, encoded by HSD17B4 gene) which is involved in fatty acid beta-oxidation and steroid metabolism. This subgroup also includes two SDR domains of the Neurospora crassa and Saccharomyces cerevisiae multifunctional beta-oxidation protein (MFP, aka Fox2). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187611 [Multi-domain]  Cd Length: 250  Bit Score: 50.78  E-value: 7.15e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2847 DEGVYLITGGAGSLGLLFAKEIANRtGRSTIV------LTGRSVLSEDKENELEALRSIGAEVVYREADVSDQHAvhhLF 2920
Cdd:cd05353      4 DGRVVLVTGAGGGLGRAYALAFAER-GAKVVVndlggdRKGSGKSSSAADKVVDEIKAAGGKAVANYDSVEDGEK---IV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2921 EEIKERYGTLNGIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSGLLHVDECS----KDFPLDFFIFFSSVSGCLGNAGQAD 2996
Cdd:cd05353     80 KTAIDAFGRVDILVNNAGILRDRSFAKMSEEDWDLVMRVHLKGSFKVTRAAwpymRKQKFGRIINTSSAAGLYGNFGQAN 159
                          170       180
                   ....*....|....*....|....*....
gi 1776025254 2997 YAAANSFMDAFAEyrrSLAASKKRFGSTI 3025
Cdd:cd05353    160 YSAAKLGLLGLSN---TLAIEGAKYNITC 185
PRK12744 PRK12744
SDR family oxidoreductase;
2850-2955 7.27e-06

SDR family oxidoreductase;


Pssm-ID: 183716 [Multi-domain]  Cd Length: 257  Bit Score: 50.89  E-value: 7.27e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGLLFAKEIANRtGRSTIVLTGRSVLSE-DKENELEALRSIGAEVVYREADVSDQHAVHHLFEEIKERYG 2928
Cdd:PRK12744    10 VVLIAGGAKNLGGLIARDLAAQ-GAKAVAIHYNSAASKaDAEETVAAVKAAGAKAVAFQADLTTAAAVEKLFDDAKAAFG 88
                           90       100
                   ....*....|....*....|....*..
gi 1776025254 2929 TLNGIIHGAGSIKDHFIIHKTNEEFQE 2955
Cdd:PRK12744    89 RPDIAINTVGKVLKKPIVEISEAEYDE 115
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
2852-3056 7.40e-06

3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 50.68  E-value: 7.40e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2852 LITGGAGSLGLLFAKeIANRTGrSTIVLTGRSVlsedkeNELEALRS-IGAEVVYREADVSDQHAVHHLFEEIKERYGTL 2930
Cdd:PRK12936    10 LVTGASGGIGEEIAR-LLHAQG-AIVGLHGTRV------EKLEALAAeLGERVKIFPANLSDRDEVKALGQKAEADLEGV 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2931 NGIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSGLLHVD-ECSKDFPLDFF---IFFSSVSGCLGNAGQADYAAANSFMDA 3006
Cdd:PRK12936    82 DILVNNAGITKDGLFVRMSDEDWDSVLEVNLTATFRLTrELTHPMMRRRYgriINITSVVGVTGNPGQANYCASKAGMIG 161
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3007 FAeyrRSLAASKKRFGSTISFNWPLWEEGGMqVGAEDEKRMLKTTGMVPM 3056
Cdd:PRK12936   162 FS---KSLAQEIATRNVTVNCVAPGFIESAM-TGKLNDKQKEAIMGAIPM 207
BACL_like cd05929
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ...
1302-1639 7.42e-06

Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.


Pssm-ID: 341252 [Multi-domain]  Cd Length: 473  Bit Score: 51.99  E-value: 7.42e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1302 YVIYTSGSTGKPKGVM--IPHKALTNFLVSMGETP-GLTAEDKMLAVT----TYCFDIAALELFLplikGAHCYI----C 1370
Cdd:cd05929    129 KMLYSGGTTGRPKGIKrgLPGGPPDNDTLMAAALGfGPGADSVYLSPAplyhAAPFRWSMTALFM----GGTLVLmekfD 204
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1371 QTEHTKDVEKLKRDIRTIKPTVMQatpatwKML-FYSGWENEENV---KILCGGEA-LPETLKRYFLDTGSEA-WNMFGP 1444
Cdd:cd05929    205 PEEFLRLIERYRVTFAQFVPTMFV------RLLkLPEAVRNAYDLsslKRVIHAAApCPPWVKEQWIDWGGPIiWEYYGG 278
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1445 TETtiwSAVQRINDE---CSRATIGRPIANtQIYITDSQLAPVPAGVPGELCIAGdGVAKGYYKKEELTDSRFIDNPFEP 1521
Cdd:cd05929    279 TEG---QGLTIINGEewlTHPGSVGRAVLG-KVHILDEDGNEVPPGEIGEVYFAN-GPGFEYTNDPEKTAAARNEGGWST 353
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1522 gsklyrTGDMArWLPGGRIEYIG-RIDNQVKIRGFRIELGDIESRLSEHPGILECVVV----ADMDN--LAAYYTAKHAN 1594
Cdd:cd05929    354 ------LGDVG-YLDEDGYLYLTdRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVgvpdEELGQrvHAVVQPAPGAD 426
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 1776025254 1595 AS-LTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLK 1639
Cdd:cd05929    427 AGtALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLR 472
PRK08279 PRK08279
long-chain-acyl-CoA synthetase; Validated
23-243 7.45e-06

long-chain-acyl-CoA synthetase; Validated


Pssm-ID: 236217 [Multi-domain]  Cd Length: 600  Bit Score: 52.57  E-value: 7.45e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254   23 ISEKQPATIPEVLYRTAAELGDTKGIIYlqpDGTEVyqSYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNSQLLPAFW 102
Cdd:PRK08279    31 ITPDSKRSLGDVFEEAAARHPDRPALLF---EDQSI--SYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWL 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  103 GCVLTGVVPAPLavpptyaeSSSGTQK-LKDAWTLLDKPAVITDR-----------GMHQEMLDWAkEQGLEGFRAIIVE 170
Cdd:PRK08279   106 GLAKLGAVVALL--------NTQQRGAvLAHSLNLVDAKHLIVGEelveafeearaDLARPPRLWV-AGGDTLDDPEGYE 176
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  171 DL--LSAEADTDWHQSSP----EDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDH-VGGI 243
Cdd:PRK08279   177 DLaaAAAGAPTTNPASRSgvtaKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDVLYCCLPLYHnTGGT 256
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
4171-4372 9.76e-06

Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR which catalyzes the NADPH-dependent reduction of ketones on steroids and prostaglandins. Unlike most SDRs, PTCR functions as a monomer. This subgroup also includes human carbonyl reductase 1 (CBR1) and CBR3. CBR1 is an NADPH-dependent SDR with broad substrate specificity and may be responsible for the in vivo reduction of quinones, prostaglandins, and other carbonyl-containing compounds. In addition it includes poppy NADPH-dependent salutaridine reductase which catalyzes the stereospecific reduction of salutaridine to 7(S)-salutaridinol in the biosynthesis of morphine, and Arabidopsis SDR1,a menthone reductase, which catalyzes the reduction of menthone to neomenthol, a compound with antimicrobial activity; SDR1 can also carry out neomenthol oxidation. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187585 [Multi-domain]  Cd Length: 225  Bit Score: 50.31  E-value: 9.76e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4171 HVLLITGGTRGIGLLCARHFAECYGVKkLVLTGReqlppreewarfktsNTSLAEkiQAVRELEAKGVQVEMLSLTLSDD 4250
Cdd:cd05324      1 KVALVTGANRGIGFEIVRQLAKSGPGT-VILTAR---------------DVERGQ--AAVEKLRAEGLSVRFHQLDVTDD 62
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4251 AQVEQTLQHIKRTLGPIGGVIHCAGLTdMDTLAFIRKTSDDIQRVMEPKVSGLttlyRHVCNE--PLqffvLFSSVSAII 4328
Cdd:cd05324     63 ASIEAAADFVEEKYGGLDILVNNAGIA-FKGFDDSTPTREQARETMKTNFFGT----VDVTQAllPL----LKKSPAGRI 133
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1776025254 4329 PELSAG----QADYAMA----NSYMDYFAEAHQK---HVPIISvqwPNWKETGMG 4372
Cdd:cd05324    134 VNVSSGlgslTSAYGVSkaalNALTRILAKELKEtgiKVNACC---PGWVKTDMG 185
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
2852-3000 1.01e-05

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 50.46  E-value: 1.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2852 LITGGAGSLG----LLFAKEIANrtgrstIVLTGRSvlSEDKENELEALRSIGAEVVYREADVSDQHAVHHLFEEIKERY 2927
Cdd:PRK07666    11 LITGAGRGIGravaIALAKEGVN------VGLLART--EENLKAVAEEVEAYGVKVVIATADVSDYEEVTAAIEQLKNEL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2928 GTLNGIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSGLLHV---------DECSKDfpldfFIFFSSVSGCLGNAGQADYA 2998
Cdd:PRK07666    83 GSIDILINNAGISKFGKFLELDPAEWEKIIQVNLMGVYYAtravlpsmiERQSGD-----IINISSTAGQKGAAVTSAYS 157

                   ..
gi 1776025254 2999 AA 3000
Cdd:PRK07666   158 AS 159
PRK12939 PRK12939
short chain dehydrogenase; Provisional
4172-4302 1.36e-05

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 49.97  E-value: 1.36e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4172 VLLITGGTRGIGllcaRHFAEcygvkKLVLTGreqlppreewARFKTSNTSLAEKIQAVRELEAKGVQVEMLSLTLSDDA 4251
Cdd:PRK12939     9 RALVTGAARGLG----AAFAE-----ALAEAG----------ATVAFNDGLAAEARELAAALEAAGGRAHAIAADLADPA 69
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1776025254 4252 QVEQTLQHIKRTLGPIGGVIHCAGLTDMDTLAFIrkTSDDIQRVMEPKVSG 4302
Cdd:PRK12939    70 SVQRFFDAAAAALGGLDGLVNNAGITNSKSATEL--DIDTWDAVMNVNVRG 118
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
4180-4310 1.44e-05

Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) reductases.


Pssm-ID: 433310 [Multi-domain]  Cd Length: 236  Bit Score: 49.74  E-value: 1.44e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4180 RGIGLLCARHFAECyGVKkLVLTGReqlppreewarfktsNTSLAEKIQAVreleAKGVQVEMLSLTLSDDAQVEQTLQH 4259
Cdd:pfam13561    6 SGIGWAIARALAEE-GAE-VVLTDL---------------NEALAKRVEEL----AEELGAAVLPCDVTDEEQVEALVAA 64
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1776025254 4260 IKRTLGPIGGVIHCAGLTDMDTLAFIRKTSDDIQRVMEPKVSGLTTLYRHV 4310
Cdd:pfam13561   65 AVEKFGRLDILVNNAGFAPKLKGPFLDTSREDFDRALDVNLYSLFLLAKAA 115
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
2850-2938 1.45e-05

putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes the NAD-dependent interconversion of D-mannonate and D-fructuronate. This subgroup includes Bacillus subtitils UxuB/YjmF, a putative D-mannonate oxidoreductase; the B. subtilis UxuB gene is part of a putative ten-gene operon (the Yjm operon) involved in hexuronate catabolism. Escherichia coli UxuB does not belong to this subgroup. This subgroup has a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187640 [Multi-domain]  Cd Length: 271  Bit Score: 50.15  E-value: 1.45e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGLLFAKEIAnRTGRSTIVLTGRSVLSEDKENELEALrsiGAEVVYREADVSDQHAVHHLFEEIKERYGT 2929
Cdd:cd08935      7 VAVITGGTGVLGGAMARALA-QAGAKVAALGRNQEKGDKVAKEITAL---GGRAIALAADVLDRASLERAREEIVAQFGT 82

                   ....*....
gi 1776025254 2930 LNGIIHGAG 2938
Cdd:cd08935     83 VDILINGAG 91
PLN03102 PLN03102
acyl-activating enzyme; Provisional
400-555 1.64e-05

acyl-activating enzyme; Provisional


Pssm-ID: 215576 [Multi-domain]  Cd Length: 579  Bit Score: 51.17  E-value: 1.64e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  400 IGRFQVSGLSVTSGYYQRPDLNESVFtEDGWFETGDLGFLR-NGRLTITGRTKDAIIINGINYYSHAIESAVEELSEI-E 477
Cdd:PLN03102   392 MGEIVIKGSSIMKGYLKNPKATSEAF-KHGWLNTGDVGVIHpDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVlE 470
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  478 TSYTAACAVRLGQnsTDQLAIFFVTSAKLNDEQMSQLLRNIQSHVSQVIGVTPEYLLP---VQKEEIPKTAIGKIQRTQL 554
Cdd:PLN03102   471 TAVVAMPHPTWGE--TPCAFVVLEKGETTKEDRVDKLVTRERDLIEYCRENLPHFMCPrkvVFLQELPKNGNGKILKPKL 548

                   .
gi 1776025254  555 K 555
Cdd:PLN03102   549 R 549
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
2851-2967 1.78e-05

carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl reductase of the classical SDR family. Studies in Drosophila melanogaster implicate Sniffer in the prevention of neurodegeneration due to aging and oxidative-stress. This subgroup also includes Rhodococcus sp. AD45 IsoH, which is an NAD-dependent 1-hydroxy-2-glutathionyl-2-methyl-3-butene dehydrogenase involved in isoprene metabolism, Aspergillus nidulans StcE encoded by a gene which is part of a proposed sterigmatocystin biosynthesis gene cluster, Bacillus circulans SANK 72073 BtrF encoded by a gene found in the butirosin biosynthesis gene cluster, and Aspergillus parasiticus nor-1 involved in the biosynthesis of aflatoxins. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187586 [Multi-domain]  Cd Length: 233  Bit Score: 49.60  E-value: 1.78e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2851 YLITGGAGSLGLLFAKEIANRtGRSTIVLTGRSVlseDKENELEALRSIGAEVVYREADVSD--QHAVhhlfEEIKERYG 2928
Cdd:cd05325      1 VLITGASRGIGLELVRQLLAR-GNNTVIATCRDP---SAATELAALGASHSRLHILELDVTDeiAESA----EAVAERLG 72
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1776025254 2929 T--LNGIIHGAGsikdhfIIHKTN-------EEFQEVLQPKVSGLLHV 2967
Cdd:cd05325     73 DagLDVLINNAG------ILHSYGpasevdsEDLLEVFQVNVLGPLLL 114
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
2850-2939 2.00e-05

enoyl-[acyl-carrier-protein] reductase FabL;


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 49.72  E-value: 2.00e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGLLFAKEIANRTGRSTIVLTGRSVLSEDKENELEALrsiGAEVVYREADVSDQHAVHHLFEEIKERYGT 2929
Cdd:PRK08063     6 VALVTGSSRGIGKAIALRLAEEGYDIAVNYARSRKAAEETAEEIEAL---GRKALAVKANVGDVEKIKEMFAQIDEEFGR 82
                           90
                   ....*....|
gi 1776025254 2930 LNGIIHGAGS 2939
Cdd:PRK08063    83 LDVFVNNAAS 92
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
4174-4312 2.05e-05

2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 dihydrozybenzoate dehydrogenase shares the characteristics of the classical SDRs. This subgroup includes Escherichai coli EntA which catalyzes the NAD+-dependent oxidation of 2,3-dihydro-2,3-dihydroxybenzoate to 2,3-dihydroxybenzoate during biosynthesis of the siderophore Enterobactin. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187592 [Multi-domain]  Cd Length: 244  Bit Score: 49.39  E-value: 2.05e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4174 LITGGTRGIGLLCARHFAECyGVKKLVLTGREQlppreewarfktsntslaekiqavrELEAKGVQVEMLSLTLSDDAQV 4253
Cdd:cd05331      2 IVTGAAQGIGRAVARHLLQA-GATVIALDLPFV-------------------------LLLEYGDPLRLTPLDVADAAAV 55
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1776025254 4254 EQTLQHIKRTLGPIGGVIHCAGLTDMDtlAFIRKTSDDIQRVMEPKVSGLTTLYRHVCN 4312
Cdd:cd05331     56 REVCSRLLAEHGPIDALVNCAGVLRPG--ATDPLSTEDWEQTFAVNVTGVFNLLQAVAP 112
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
2850-3045 2.16e-05

cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol reductases,including (6R)-2,2,6-trimethyl-1,4-cyclohexanedione (levodione) reductase of Corynebacterium aquaticum, catalyze the reversible oxidoreduction of hydroxycyclohexanone derivatives. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187591 [Multi-domain]  Cd Length: 257  Bit Score: 49.44  E-value: 2.16e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGLLFAKEIANRTGRSTIVLTGRSVLSEDKENELEALRSigAEVVYREADVSDQHAVHHLFEEIKERYGT 2929
Cdd:cd05330      5 VVLITGGGSGLGLATAVRLAKEGAKLSLVDLNEEGLEAAKAALLEIAPD--AEVLLIKADVSDEAQVEAYVDATVEQFGR 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2930 LNGIIHGAG-SIKDHFIIHKTNEEFQEVLQPKVS----GLLHVDECSKDFPLDFFIFFSSVSGCLGNAGQADYAAANSfm 3004
Cdd:cd05330     83 IDGFFNNAGiEGKQNLTEDFGADEFDKVVSINLRgvfyGLEKVLKVMREQGSGMIVNTASVGGIRGVGNQSGYAAAKH-- 160
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1776025254 3005 dAFAEYRRSLAASKKRFGSTI------SFNWPLWEEGGMQVGAEDEK 3045
Cdd:cd05330    161 -GVVGLTRNSAVEYGQYGIRInaiapgAILTPMVEGSLKQLGPENPE 206
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
2852-3069 2.31e-05

classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a canonical active site tetrad and a fairly well conserved typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187608 [Multi-domain]  Cd Length: 239  Bit Score: 49.25  E-value: 2.31e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2852 LITGGAGSLGLLFAKEIANRtGRStIVLTGRsvlsedKENELEALRS------IGAEVVyrEADVSDQHAVHHLFEEIKE 2925
Cdd:cd05350      2 LITGASSGIGRALAREFAKA-GYN-VALAAR------RTDRLDELKAellnpnPSVEVE--ILDVTDEERNQLVIAELEA 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2926 RYGTLNGIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSGLLHVDECSkdfpLDFF--------IFFSSVSGCLGNAGQADY 2997
Cdd:cd05350     72 ELGGLDLVIINAGVGKGTSLGDLSFKAFRETIDTNLLGAAAILEAA----LPQFrakgrghlVLISSVAALRGLPGAAAY 147
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1776025254 2998 AAANSFMDAFAEyrrSLAASKKRFGSTISFNWPlweegGMqVGAEDEKRMLKTTGMvpMPTDSGLKAFYQGI 3069
Cdd:cd05350    148 SASKAALSSLAE---SLRYDVKKRGIRVTVINP-----GF-IDTPLTANMFTMPFL--MSVEQAAKRIYKAI 208
PRK09072 PRK09072
SDR family oxidoreductase;
4169-4297 2.70e-05

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 49.17  E-value: 2.70e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4169 KDHVLLITGGTRGIGLLCARHFAECyGVkKLVLTGREqlppreewarfktsntslAEKIQAVRELEAKGVQVEMLSLTLS 4248
Cdd:PRK09072     4 KDKRVLLTGASGGIGQALAEALAAA-GA-RLLLVGRN------------------AEKLEALAARLPYPGRHRWVVADLT 63
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1776025254 4249 DDAQVEQTLQHIKRtLGPIGGVIHCAGLTDMDTLAfiRKTSDDIQRVME 4297
Cdd:PRK09072    64 SEAGREAVLARARE-MGGINVLINNAGVNHFALLE--DQDPEAIERLLA 109
Dip2 cd05905
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ...
1175-1345 2.77e-05

Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.


Pssm-ID: 341231 [Multi-domain]  Cd Length: 571  Bit Score: 50.42  E-value: 2.77e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1175 EGQTLTYRELDERSTQLAIYLQAH-GVGP-DRLAGIYVDrSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLEDSEVF 1252
Cdd:cd05905     11 EATTLTWGKLLSRAEKIAAVLQKKvGLKPgDRVALMYPD-PLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLLGTCKVR 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1253 ITLTTsELVNT----LSWNGVTTALLDQD--WDEIAQTASDRKVLTRTVTP---------ENLAYVIYTSGSTGKPKGVM 1317
Cdd:cd05905     90 VALTV-EACLKglpkKLLKSKTAAEIAKKkgWPKILDFVKIPKSKRSKLKKwgphpptrdGDTAYIEYSFSSDGSLSGVA 168
                          170       180
                   ....*....|....*....|....*...
gi 1776025254 1318 IPHKALTNFLVSMGETPGLTAEDKMLAV 1345
Cdd:cd05905    169 VSHSSLLAHCRALKEACELYESRPLVTV 196
AACS cd05943
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ...
1512-1651 2.99e-05

Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.


Pssm-ID: 341265 [Multi-domain]  Cd Length: 629  Bit Score: 50.35  E-value: 2.99e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1512 SRFIDNPFE--PGskLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVA----DMDNLA 1585
Cdd:cd05943    472 SRYRAAYFAkyPG--VWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGqewkDGDERV 549
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1776025254 1586 AYYTAKHANASLT---ARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLKNIdLSGEQLKQR 1651
Cdd:cd05943    550 ILFVKLREGVELDdelRKRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGKKVEVAVKKI-IAGRPVKNA 617
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
4173-4276 3.22e-05

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 48.98  E-value: 3.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4173 LLITGGTRGIGLLCARHFAEcYGVKKLVltgreqlppreewarfktsNTSLAEKIQ-AVRELEAKGVQVEMLSLTLSDDA 4251
Cdd:PRK08085    12 ILITGSAQGIGFLLATGLAE-YGAEIII-------------------NDITAERAElAVAKLRQEGIKAHAAPFNVTHKQ 71
                           90       100
                   ....*....|....*....|....*
gi 1776025254 4252 QVEQTLQHIKRTLGPIGGVIHCAGL 4276
Cdd:PRK08085    72 EVEAAIEHIEKDIGPIDVLINNAGI 96
PRK08162 PRK08162
acyl-CoA synthetase; Validated
398-555 3.24e-05

acyl-CoA synthetase; Validated


Pssm-ID: 236169 [Multi-domain]  Cd Length: 545  Bit Score: 50.33  E-value: 3.24e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  398 GE-IGRFQVSGLSVTSGYYQRPDLNESVFtEDGWFETGDLGFLR-NGRLTITGRTKDAIIINGINYYSHAIESAVEELSE 475
Cdd:PRK08162   385 GEtIGEIMFRGNIVMKGYLKNPKATEEAF-AGGWFHTGDLAVLHpDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPA 463
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  476 IETSYTAA----------CA-VRLGQNSTdqlaiffVTSAKlndeqmsqllrnIQSHVSQVIgvtPEYLLP--VQKEEIP 542
Cdd:PRK08162   464 VLVAAVVAkpdpkwgevpCAfVELKDGAS-------ATEEE------------IIAHCREHL---AGFKVPkaVVFGELP 521
                          170
                   ....*....|...
gi 1776025254  543 KTAIGKIQRTQLK 555
Cdd:PRK08162   522 KTSTGKIQKFVLR 534
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
4172-4275 3.87e-05

retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) OxidoReductase (LPOR) and related proteins, classical (c) SDRs; Classical SDR subgroup containing retinol-DHs, LPORs, and related proteins. Retinol is processed by a medium chain alcohol dehydrogenase followed by retinol-DHs. Pchlide reductases act in chlorophyll biosynthesis. There are distinct enzymes that catalyze Pchlide reduction in light or dark conditions. Light-dependent reduction is via an NADP-dependent SDR, LPOR. Proteins in this subfamily share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. This subgroup includes the human proteins: retinol dehydrogenase -12, -13 ,and -14, dehydrogenase/reductase SDR family member (DHRS)-12 , -13 and -X (a DHRS on chromosome X), and WWOX (WW domain-containing oxidoreductase), as well as a Neurospora crassa SDR encoded by the blue light inducible bli-4 gene. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212492 [Multi-domain]  Cd Length: 269  Bit Score: 48.76  E-value: 3.87e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4172 VLLITGGTRGIGLLCARHFAEcYGVkKLVLTGREQlppreewarfktsntslaEKIQAVRE---LEAKGVQVEMLSLTLS 4248
Cdd:cd05327      3 VVVITGANSGIGKETARELAK-RGA-HVIIACRNE------------------EKGEEAAAeikKETGNAKVEVIQLDLS 62
                           90       100
                   ....*....|....*....|....*..
gi 1776025254 4249 DDAQVEQTLQHIKRTLGPIGGVIHCAG 4275
Cdd:cd05327     63 SLASVRQFAEEFLARFPRLDILINNAG 89
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
2850-2966 4.08e-05

putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup resembles the SDR family, but does not have a perfect match to the NAD-binding motif or the catalytic tetrad characteristic of the SDRs. It includes the SDRs, Q9HYA2 from Pseudomonas aeruginosa PAO1 and APE0912 from Aeropyrum pernix K1. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187602 [Multi-domain]  Cd Length: 253  Bit Score: 48.81  E-value: 4.08e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGLLFAKEIAnRTGrSTIVLTGRSVlsEDKENELEALRSIGAEVVYREADVSDQHAVHHLFEEIKERYGT 2929
Cdd:cd05344      3 VALVTAASSGIGLAIARALA-REG-ARVAICARNR--ENLERAASELRAGGAGVLAVVADLTDPEDIDRLVEKAGDAFGR 78
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1776025254 2930 LNGIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSGLLH 2966
Cdd:cd05344     79 VDILVNNAGGPPPGPFAELTDEDWLEAFDLKLLSVIR 115
PRK05875 PRK05875
short chain dehydrogenase; Provisional
2847-2938 4.26e-05

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 48.65  E-value: 4.26e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2847 DEGVYLITGGAGSLGLLFAKEIANRTGRSTIVltGRSvlsEDK----ENELEALRSIGAeVVYREADVSDQHAVHHLFEE 2922
Cdd:PRK05875     6 QDRTYLVTGGGSGIGKGVAAGLVAAGAAVMIV--GRN---PDKlaaaAEEIEALKGAGA-VRYEPADVTDEDQVARAVDA 79
                           90
                   ....*....|....*.
gi 1776025254 2923 IKERYGTLNGIIHGAG 2938
Cdd:PRK05875    80 ATAWHGRLHGVVHCAG 95
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
2850-3025 4.81e-05

putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) SDR; This subgroup includes Rhizobium sp. NGR234 FabG1. The Escherichai coli K12 BKR, FabG, belongs to a different subgroup. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187607 [Multi-domain]  Cd Length: 246  Bit Score: 48.22  E-value: 4.81e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGLLFAKEIAnRTGRSTIVLTGRSVLSEDKeneleALRSIGAEVVYREADVSDQHAVHHLFEEIKERYGT 2929
Cdd:cd05349      2 VVLVTGASRGLGAAIARSFA-REGARVVVNYYRSTESAEA-----VAAEAGERAIAIQADVRDRDQVQAMIEEAKNHFGP 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2930 LNGIIHGA-GSIKDHFIIHKTNEE-----FQEVLQPKVSGLLHV-DECSKDFPldffiffSSVSGCLGNAGQ-------- 2994
Cdd:cd05349     76 VDTIVNNAlIDFPFDPDQRKTFDTidwedYQQQLEGAVKGALNLlQAVLPDFK-------ERGSGRVINIGTnlfqnpvv 148
                          170       180       190
                   ....*....|....*....|....*....|...
gi 1776025254 2995 --ADYAAANSFMDAFAeyrRSLAASKKRFGSTI 3025
Cdd:cd05349    149 pyHDYTTAKAALLGFT---RNMAKELGPYGITV 178
Thiolase_N pfam00108
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
3413-3537 6.20e-05

Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl synthase (pfam00109), and also chalcone synthase.


Pssm-ID: 459676 [Multi-domain]  Cd Length: 260  Bit Score: 48.07  E-value: 6.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3413 FGISPREADYVDpqqrLLMTYVWKALEDAGCPPQSLSGtgtgIFIGTGNTGYKD------LFHRANLPieghaatgHMIP 3486
Cdd:pfam00108   14 FGGSLKDVSAVE----LGAEAIKAALERAGVDPEDVDE----VIVGNVLQAGEGqnparqAALKAGIP--------DSAP 77
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1776025254 3487 SVGPNRMsyflnihgpsepvetaCSSSLVAIHRAVTAMQNGDCEMAIAGGV 3537
Cdd:pfam00108   78 AVTINKV----------------CGSGLKAVYLAAQSIASGDADVVLAGGV 112
PRK08628 PRK08628
SDR family oxidoreductase;
4169-4278 7.29e-05

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 48.03  E-value: 7.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4169 KDHVLLITGGTRGIGLLCARHFAECYGVKklVLTGREqlppreewarfktsntslAEKIQAVRELEAKGVQVEMLSLTLS 4248
Cdd:PRK08628     6 KDKVVIVTGGASGIGAAISLRLAEEGAIP--VIFGRS------------------APDDEFAEELRALQPRAEFVQVDLT 65
                           90       100       110
                   ....*....|....*....|....*....|
gi 1776025254 4249 DDAQVEQTLQHIKRTLGPIGGVIHCAGLTD 4278
Cdd:PRK08628    66 DDAQCRDAVEQTVAKFGRIDGLVNNAGVND 95
PRK06483 PRK06483
dihydromonapterin reductase; Provisional
2852-2937 7.81e-05

dihydromonapterin reductase; Provisional


Pssm-ID: 180586 [Multi-domain]  Cd Length: 236  Bit Score: 47.62  E-value: 7.81e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2852 LITGGAGSLGLLFAKEIANRtgRSTIVLTGRSvlsedKENELEALRSIGAEVVYreADVSDQHAVHHLFEEIKERYGTLN 2931
Cdd:PRK06483     6 LITGAGQRIGLALAWHLLAQ--GQPVIVSYRT-----HYPAIDGLRQAGAQCIQ--ADFSTNAGIMAFIDELKQHTDGLR 76

                   ....*.
gi 1776025254 2932 GIIHGA 2937
Cdd:PRK06483    77 AIIHNA 82
AcpA COG3433
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ...
4393-4531 8.49e-05

Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442659 [Multi-domain]  Cd Length: 295  Bit Score: 48.21  E-value: 8.49e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4393 LRFLDQIVSKMFGPVVLPAManqtnwEPELLMKRRKPHEGGLQEAALQSPPARDIEEADevskcdGLLSETQSWLIDLFT 4472
Cdd:COG3433    162 LAALDKVPPDVVAASAVVAL------DALLLLALKVVARAAPALAAAEALLAAASPAPA------LETALTEEELRADVA 229
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1776025254 4473 EELRIDREDFEIDGLFQDYGVDSIILAQVLQRInRKLEAALDPSILYEYPTIQRFTDWL 4531
Cdd:COG3433    230 ELLGVDPEEIDPDDNLFDLGLDSIRLMQLVERW-RKAGLDVSFADLAEHPTLAAWWALL 287
PRK06181 PRK06181
SDR family oxidoreductase;
2850-2961 8.64e-05

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 47.67  E-value: 8.64e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGLLFAKEIAnRTGRStIVLTGRSvlsEDKENEL-EALRSIGAEVVYREADVSDQHAVHHLFEEIKERYG 2928
Cdd:PRK06181     3 VVIITGASEGIGRALAVRLA-RAGAQ-LVLAARN---ETRLASLaQELADHGGEALVVPTDVSDAEACERLIEAAVARFG 77
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1776025254 2929 TLNGIIHGAGsikdhfIIHKTNeeFQEVLQPKV 2961
Cdd:PRK06181    78 GIDILVNNAG------ITMWSR--FDELTDLSV 102
PRK07445 PRK07445
O-succinylbenzoic acid--CoA ligase; Reviewed
1466-1641 1.06e-04

O-succinylbenzoic acid--CoA ligase; Reviewed


Pssm-ID: 236019 [Multi-domain]  Cd Length: 452  Bit Score: 48.45  E-value: 1.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1466 GRPIANTQIYITDSQLapvpagvpGELCIAGDGVAKGYYKKeeltdsrFIDNPfepgsKLYRTGDMARWLPGGRIEYIGR 1545
Cdd:PRK07445   286 GQVLPHAQITIPANQT--------GNITIQAQSLALGYYPQ-------ILDSQ-----GIFETDDLGYLDAQGYLHILGR 345
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1546 IDNQVKIRGFRIELGDIESRLSEhPGILE--CVV-VADMD---NLAAYYTAKHANASLtaRELRHFVKNALPAYMVPSYF 1619
Cdd:PRK07445   346 NSQKIITGGENVYPAEVEAAILA-TGLVQdvCVLgLPDPHwgeVVTAIYVPKDPSISL--EELKTAIKDQLSPFKQPKHW 422
                          170       180
                   ....*....|....*....|..
gi 1776025254 1620 IQLDHMPLTPNGKIDRNSLKNI 1641
Cdd:PRK07445   423 IPVPQLPRNPQGKINRQQLQQI 444
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
2852-2964 1.25e-04

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 47.25  E-value: 1.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2852 LITGGAGSLGLlfakEIANRTGR--STIVLTGRsvlsedKENELEA----LRSIGAEVVYREADVSDQHAVHHLFEEIKE 2925
Cdd:PRK08213    16 LVTGGSRGLGL----QIAEALGEagARVVLSAR------KAEELEEaaahLEALGIDALWIAADVADEADIERLAEETLE 85
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1776025254 2926 RYGTLNGIIHGAGS-----IKDHFIihktnEEFQEVLQPKVSGL 2964
Cdd:PRK08213    86 RFGHVDILVNNAGAtwgapAEDHPV-----EAWDKVMNLNVRGL 124
PRK07454 PRK07454
SDR family oxidoreductase;
4174-4296 1.27e-04

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 46.88  E-value: 1.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4174 LITGGTRGIGLLCARHFAECyGVKkLVLTGREQlppreewarfktsntslaEKIQAVR-ELEAKGVQVEMLSLTLSDDAQ 4252
Cdd:PRK07454    10 LITGASSGIGKATALAFAKA-GWD-LALVARSQ------------------DALEALAaELRSTGVKAAAYSIDLSNPEA 69
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1776025254 4253 VEQTLQHIKRTLGPIGGVIHCAGLTDMDTLAfirKTS-DDIQRVM 4296
Cdd:PRK07454    70 IAPGIAELLEQFGCPDVLINNAGMAYTGPLL---EMPlSDWQWVI 111
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
2850-2965 1.63e-04

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 46.94  E-value: 1.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGLLFAKEIANRTGRSTIVltgrsvlSEDKENELEALRSIGAEVVYREADVSDQHAVHHLFEEIKERYGT 2929
Cdd:PRK07067     8 VALLTGAASGIGEAVAERYLAEGARVVIA-------DIKPARARLAALEIGPAAIAVSLDVTRQDSIDRIVAAAVERFGG 80
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1776025254 2930 LNGIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSGLL 2965
Cdd:PRK07067    81 IDILFNNAALFDMAPILDISRDSYDRLFAVNVKGLF 116
PRK07677 PRK07677
short chain dehydrogenase; Provisional
4172-4274 1.67e-04

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 46.60  E-value: 1.67e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4172 VLLITGGTRGIGLLCARHFAEcYGVKkLVLTGREQlppreewarfktsntslaEKI-QAVRELEAKGVQVEMLSLTLSDD 4250
Cdd:PRK07677     3 VVIITGGSSGMGKAMAKRFAE-EGAN-VVITGRTK------------------EKLeEAKLEIEQFPGQVLTVQMDVRNP 62
                           90       100
                   ....*....|....*....|....
gi 1776025254 4251 AQVEQTLQHIKRTLGPIGGVIHCA 4274
Cdd:PRK07677    63 EDVQKMVEQIDEKFGRIDALINNA 86
PRK08251 PRK08251
SDR family oxidoreductase;
2852-2938 1.73e-04

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 46.47  E-value: 1.73e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2852 LITGGAGSLGLLFAKEIANRtGRStIVLTGRSV--LSEDKEnELEAlRSIGAEVVYREADVSDQHAVHHLFEEIKERYGT 2929
Cdd:PRK08251     6 LITGASSGLGAGMAREFAAK-GRD-LALCARRTdrLEELKA-ELLA-RYPGIKVAVAALDVNDHDQVFEVFAEFRDELGG 81

                   ....*....
gi 1776025254 2930 LNGIIHGAG 2938
Cdd:PRK08251    82 LDRVIVNAG 90
PRK06484 PRK06484
short chain dehydrogenase; Validated
4172-4302 1.81e-04

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 47.92  E-value: 1.81e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4172 VLLITGGTRGIGLLCARHFAECYGVkkLVLTGREQLPPREEWARFKTSNTSLAekiqavreleakgvqvemlsLTLSDDA 4251
Cdd:PRK06484     7 VVLVTGAAGGIGRAACQRFARAGDQ--VVVADRNVERARERADSLGPDHHALA--------------------MDVSDEA 64
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1776025254 4252 QVEQTLQHIKRTLGPIGGVIHCAGLTDMDTLAFIRKTSDDIQRVMEPKVSG 4302
Cdd:PRK06484    65 QIREGFEQLHREFGRIDVLVNNAGVTDPTMTATLDTTLEEFARLQAINLTG 115
hsFATP2a_ACSVL_like cd05938
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ...
61-258 1.83e-04

Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341261 [Multi-domain]  Cd Length: 537  Bit Score: 47.67  E-value: 1.83e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254   61 SYRRLWDDGLRIVKGL-RQSGLKAKQSVILQLGdNSQLLPAFW------GCVLTGVVPAPLAVPPTYAESSSGTQKLKDA 133
Cdd:cd05938      7 TYRDVDRRSNQAARALlAHAGLRPGDTVALLLG-NEPAFLWIWlglaklGCPVAFLNTNIRSKSLLHCFRCCGAKVLVVA 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  134 WTLLDkpAVitdrgmhQEMLDWAKEQGL-----------EGFRAIIveDLLSAEADT----DWH-QSSPEDLALLLLTSG 197
Cdd:cd05938     86 PELQE--AV-------EEVLPALRADGVsvwylshtsntEGVISLL--DKVDAASDEpvpaSLRaHVTIKSPALYIYTSG 154
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1776025254  198 STGTPKAVMLNHRNIMsMVKGIIQMQGFTREDITFNWMPFDHVGG--IGMlhlrdvyLGCQEI 258
Cdd:cd05938    155 TTGLPKAARISHLRVL-QCSGFLSLCGVTADDVIYITLPLYHSSGflLGI-------GGCIEL 209
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
2850-2957 1.91e-04

classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad and domain size of the classical SDRs, but has an atypical NAD-binding motif ([ST]G[GA]XGXXG). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187635 [Multi-domain]  Cd Length: 250  Bit Score: 46.56  E-value: 1.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGLLFAKEIANRTGRstIVLTGRSVLS-EDKENELEALRsiGAEVVYREADVSDQHAVHHLFEEIKERYG 2928
Cdd:cd08930      4 IILITGAAGLIGKAFCKALLSAGAR--LILADINAPAlEQLKEELTNLY--KNRVIALELDITSKESIKELIESYLEKFG 79
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1776025254 2929 TLNGIIHGAG-SIKDHFI--IHKTNEEFQEVL 2957
Cdd:cd08930     80 RIDILINNAYpSPKVWGSrfEEFPYEQWNEVL 111
PRK06125 PRK06125
short chain dehydrogenase; Provisional
4174-4308 2.10e-04

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 46.58  E-value: 2.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4174 LITGGTRGIGLLCARHFAE--CYgvkkLVLTGREqlppreewarfktsntslAEKI-QAVRELEAK-GVQVEMLSLTLSD 4249
Cdd:PRK06125    11 LITGASKGIGAAAAEAFAAegCH----LHLVARD------------------ADALeALAADLRAAhGVDVAVHALDLSS 68
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1776025254 4250 DAQVEQtlqhIKRTLGPI------GGVIHCAGLTDMDTLAFirktsddiQRVMEPKVSGLTTLYR 4308
Cdd:PRK06125    69 PEAREQ----LAAEAGDIdilvnnAGAIPGGGLDDVDDAAW--------RAGWELKVFGYIDLTR 121
PRK05872 PRK05872
short chain dehydrogenase; Provisional
2850-2938 2.15e-04

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 46.89  E-value: 2.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGLLFAKEIANRTGRstIVLTGrsvLSEDKENELEALRSIGAEVVYREADVSDQHAVHHLFEEIKERYGT 2929
Cdd:PRK05872    11 VVVVTGAARGIGAELARRLHARGAK--LALVD---LEEAELAALAAELGGDDRVLTVVADVTDLAAMQAAAEEAVERFGG 85

                   ....*....
gi 1776025254 2930 LNGIIHGAG 2938
Cdd:PRK05872    86 IDVVVANAG 94
FATP_FACS cd05940
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ...
188-243 2.15e-04

Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341263 [Multi-domain]  Cd Length: 449  Bit Score: 47.35  E-value: 2.15e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1776025254  188 DLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDH-VGGI 243
Cdd:cd05940     82 DAALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGALPSDVLYTCLPLYHsTALI 138
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
4169-4302 2.25e-04

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 46.22  E-value: 2.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4169 KDHVLLITGGTRGIGLLCARHFAEcYGVKkLVLTGREqlppreewarfktsntslAEKIQAV-RELEAKGVQVEMLSLTL 4247
Cdd:PRK07666     6 QGKNALITGAGRGIGRAVAIALAK-EGVN-VGLLART------------------EENLKAVaEEVEAYGVKVVIATADV 65
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1776025254 4248 SDDAQVEQTLQHIKRTLGPIGGVIHCAGLTDMDTlaFIRKTSDDIQRVMEPKVSG 4302
Cdd:PRK07666    66 SDYEEVTAAIEQLKNELGSIDILINNAGISKFGK--FLELDPAEWEKIIQVNLMG 118
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
4172-4340 2.28e-04

human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid dehydrogenases (17betaHSD) are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. 17betaHSD type XI, a classical SDR, preferentially converts 3alpha-Adiol to androsterone but not numerous other tested steroids. This subgroup of classical SDRs also includes members identified as retinol dehydrogenases, which convert retinol to retinal, a property that overlaps with 17betaHSD activity. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187598 [Multi-domain]  Cd Length: 243  Bit Score: 46.08  E-value: 2.28e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4172 VLLITGGTRGIGLLCARHFAECYGvkKLVLtgreqlppreeWARFKTSNTSLAEKIqavrelEAKGVQVEMLSLTLSDDA 4251
Cdd:cd05339      1 IVLITGGGSGIGRLLALEFAKRGA--KVVI-----------LDINEKGAEETANNV------RKAGGKVHYYKCDVSKRE 61
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4252 QVEQTLQHIKRTLGPIGGVIHCAGLtdMDTLAFIRKTSDDIQRVMEPKVSGLTTLYRHVCNEPLQ----FFVLFSSVSAI 4327
Cdd:cd05339     62 EVYEAAKKIKKEVGDVTILINNAGV--VSGKKLLELPDEEIEKTFEVNTLAHFWTTKAFLPDMLErnhgHIVTIASVAGL 139
                          170
                   ....*....|...
gi 1776025254 4328 IPelSAGQADYAM 4340
Cdd:cd05339    140 IS--PAGLADYCA 150
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
2850-3000 2.38e-04

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 46.43  E-value: 2.38e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGLLFAKEIAnRTGrSTIVLTGrsvLSEDKENE-LEALRSIGAEVVYREADVSDQHAVHHLFEEIKERYG 2928
Cdd:PRK13394     9 TAVVTGAASGIGKEIALELA-RAG-AAVAIAD---LNQDGANAvADEINKAGGKAIGVAMDVTNEDAVNAGIDKVAERFG 83
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1776025254 2929 TLNGIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSGLLHVDECS-----KDFPLDFFIFFSSVSGCLGNAGQADYAAA 3000
Cdd:PRK13394    84 SVDILVSNAGIQIVNPIENYSFADWKKMQAIHVDGAFLTTKAAlkhmyKDDRGGVVIYMGSVHSHEASPLKSAYVTA 160
KAsynt_C_assoc pfam16197
Ketoacyl-synthetase C-terminal extension; KAsynt_C_assoc represents the very C-terminus of a ...
4973-5010 2.77e-04

Ketoacyl-synthetase C-terminal extension; KAsynt_C_assoc represents the very C-terminus of a subset of proteins from the keto-acyl-synthetase 2 family. It is found in proteins ranging from bacteria to human.


Pssm-ID: 465059 [Multi-domain]  Cd Length: 111  Bit Score: 43.30  E-value: 2.77e-04
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1776025254 4973 AAINCFADGGTNVHVIVEAWEKdeKHAIKRSPKSPPQL 5010
Cdd:pfam16197   27 VGVNSFGFGGANAHVILKSNPK--PKIPPESPDNLPRL 62
AcpA COG3433
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ...
576-666 3.32e-04

Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442659 [Multi-domain]  Cd Length: 295  Bit Score: 46.28  E-value: 3.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  576 AVQDEEMQQADHVKRV---REEIQEHLLTCLTEELHVSRDWVEPNANIQSLGVNSIKMMKLIRSIEKNyHIKLTAREIHQ 652
Cdd:COG3433    198 ALAAAEALLAAASPAPaleTALTEEELRADVAELLGVDPEEIDPDDNLFDLGLDSIRLMQLVERWRKA-GLDVSFADLAE 276
                           90
                   ....*....|....
gi 1776025254  653 YPTIERLASYLSEH 666
Cdd:COG3433    277 HPTLAAWWALLAAA 290
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
2852-3077 3.46e-04

Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase (KR) domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187535 [Multi-domain]  Cd Length: 186  Bit Score: 44.81  E-value: 3.46e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2852 LITGGAGSLGLLFAKEIANRTGRSTIVLTGRSVLsedkenelealrsigaevvyreadvsdqhavhhlfeeikerygtln 2931
Cdd:cd02266      2 LVTGGSGGIGGAIARWLASRGSPKVLVVSRRDVV---------------------------------------------- 35
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2932 giIHGAGSIKDHFIIHKTNEEFQEVLQPKVSGLLHVDECSKdfPLDF------FIFFSSVSGCLGNAGQADYAAANSFMD 3005
Cdd:cd02266     36 --VHNAAILDDGRLIDLTGSRIERAIRANVVGTRRLLEAAR--ELMKakrlgrFILISSVAGLFGAPGLGGYAASKAALD 111
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1776025254 3006 AFAEYRRSLAASkkrFGSTISF-NWPLWEEGGM-QVGAEDEKRMLKTT-GMVPMPTDSGLKAFYQGIASDKPQVF 3077
Cdd:cd02266    112 GLAQQWASEGWG---NGLPATAvACGTWAGSGMaKGPVAPEEILGNRRhGVRTMPPEEVARALLNALDRPKAGVC 183
PRK06194 PRK06194
hypothetical protein; Provisional
2849-2938 3.56e-04

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 46.16  E-value: 3.56e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2849 GVYLITGGAGSLGLLFAKeIANRTGRStIVLTgrSVLSEDKENELEALRSIGAEVVYREADVSDQHAVHHLFEEIKERYG 2928
Cdd:PRK06194     7 KVAVITGAASGFGLAFAR-IGAALGMK-LVLA--DVQQDALDRAVAELRAQGAEVLGVRTDVSDAAQVEALADAALERFG 82
                           90
                   ....*....|
gi 1776025254 2929 TLNGIIHGAG 2938
Cdd:PRK06194    83 AVHLLFNNAG 92
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
2850-3012 3.67e-04

clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent reduction of clavulanate-9-aldehyde to clavulanic acid, a beta-lactamase inhibitor. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187639 [Multi-domain]  Cd Length: 243  Bit Score: 45.61  E-value: 3.67e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGLLFAKEIANRtGRSTIVLTGRSVLSEDKENELEALrsiGAEVVYREADVSDQHAVHHLFEEIKERYGT 2929
Cdd:cd08934      5 VALVTGASSGIGEATARALAAE-GAAVAIAARRVDRLEALADELEAE---GGKALVLELDVTDEQQVDAAVERTVEALGR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2930 LNGIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSGLLHVDECSkdFPLDF------FIFFSSVSGCLGNAGQADYAAANSF 3003
Cdd:cd08934     81 LDILVNNAGIMLLGPVEDADTTDWTRMIDTNLLGLMYTTHAA--LPHHLlrnkgtIVNISSVAGRVAVRNSAVYNATKFG 158

                   ....*....
gi 1776025254 3004 MDAFAEYRR 3012
Cdd:cd08934    159 VNAFSEGLR 167
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
4169-4275 3.67e-04

Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER is a peroxisomal protein with a proposed role in fatty acid elongation. Fatty acid synthesis is known to occur in the both endoplasmic reticulum and mitochondria; peroxisomal TER has been proposed as an additional fatty acid elongation system, it reduces the double bond at C-2 as the last step of elongation. This system resembles the mitochondrial system in that acetyl-CoA is used as a carbon donor. TER may also function in phytol metabolism, reducting phytenoyl-CoA to phytanoyl-CoA in peroxisomes. DECR processes double bonds in fatty acids to increase their utility in fatty acid metabolism; it reduces 2,4-dienoyl-CoA to an enoyl-CoA. DECR is active in mitochondria and peroxisomes. This subgroup has the Gly-rich NAD-binding motif of the classical SDR family, but does not display strong identity to the canonical active site tetrad, and lacks the characteristic Tyr at the usual position. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187627 [Multi-domain]  Cd Length: 249  Bit Score: 45.66  E-value: 3.67e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4169 KDHVLLITGGTRGIGLLCARHFAECyGVkKLVLTGReqlppREEwarfKTSNTslAEKIQAVRELEAKGVQVEmlsltLS 4248
Cdd:cd05369      2 KGKVAFITGGGTGIGKAIAKAFAEL-GA-SVAIAGR-----KPE----VLEAA--AEEISSATGGRAHPIQCD-----VR 63
                           90       100
                   ....*....|....*....|....*..
gi 1776025254 4249 DDAQVEQTLQHIKRTLGPIGGVIHCAG 4275
Cdd:cd05369     64 DPEAVEAAVDETLKEFGKIDILINNAA 90
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
4172-4312 3.68e-04

2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 45.65  E-value: 3.68e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4172 VLLITGGTRGIGLLCARHFAECyGVKklvLTGREQlppreewarfktsntslaekiqavRELEAKGVQVEMLSLTLSDDA 4251
Cdd:PRK08220    10 TVWVTGAAQGIGYAVALAFVEA-GAK---VIGFDQ------------------------AFLTQEDYPFATFVLDVSDAA 61
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1776025254 4252 QVEQTLQHIKRTLGPIGGVIHCAGLTDM---DTLafirkTSDDIQRVMEPKVSGLTTLYRHVCN 4312
Cdd:PRK08220    62 AVAQVCQRLLAETGPLDVLVNAAGILRMgatDSL-----SDEDWQQTFAVNAGGAFNLFRAVMP 120
PRK07201 PRK07201
SDR family oxidoreductase;
4172-4297 3.99e-04

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 46.87  E-value: 3.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4172 VLLITGGTRGIGLLCARHFAECYGvkKLVLTGREqlppreewarfktsntslAEKIQAVR-ELEAKGVQVEMLSLTLSDD 4250
Cdd:PRK07201   373 VVLITGASSGIGRATAIKVAEAGA--TVFLVARN------------------GEALDELVaEIRAKGGTAHAYTCDLTDS 432
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1776025254 4251 AQVEQTLQHIKRTLGPIGGVIHCAGLTdmdtlafIRKTSD-------DIQRVME 4297
Cdd:PRK07201   433 AAVDHTVKDILAEHGHVDYLVNNAGRS-------IRRSVEnstdrfhDYERTMA 479
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
2850-2938 4.40e-04

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 45.65  E-value: 4.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGLLFAKEIAnRTGrSTIVLTGrsVLSEDKENELEALRSIGAEVVYREADVSDQHAVHHLFEEIKERYGT 2929
Cdd:PRK12429     6 VALVTGAASGIGLEIALALA-KEG-AKVVIAD--LNDEAAAAAAEALQKAGGKAIGVAMDVTDEEAINAGIDYAVETFGG 81

                   ....*....
gi 1776025254 2930 LNGIIHGAG 2938
Cdd:PRK12429    82 VDILVNNAG 90
PRK06483 PRK06483
dihydromonapterin reductase; Provisional
4173-4296 4.96e-04

dihydromonapterin reductase; Provisional


Pssm-ID: 180586 [Multi-domain]  Cd Length: 236  Bit Score: 44.92  E-value: 4.96e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4173 LLITGGTRGIGLLCARHFAEcYGvKKLVLTGREQLPpreewarfktsntslaeKIQAVRELEAKGVQVEmlsltLSDDAQ 4252
Cdd:PRK06483     5 ILITGAGQRIGLALAWHLLA-QG-QPVIVSYRTHYP-----------------AIDGLRQAGAQCIQAD-----FSTNAG 60
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1776025254 4253 VEQTLQHIKRTLGPIGGVIHCAGLTDMDTLAFirKTSDDIQRVM 4296
Cdd:PRK06483    61 IMAFIDELKQHTDGLRAIIHNASDWLAEKPGA--PLADVLARMM 102
PRK09186 PRK09186
flagellin modification protein A; Provisional
2847-2937 5.10e-04

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 45.37  E-value: 5.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2847 DEGVYLITGGAGSLGLLFAKEIANRTGRSTIVLTGRSVLSEDKENELEALRSIGAEVVyrEADVSDQHAVHHLFEEIKER 2926
Cdd:PRK09186     3 KGKTILITGAGGLIGSALVKAILEAGGIVIAADIDKEALNELLESLGKEFKSKKLSLV--ELDITDQESLEEFLSKSAEK 80
                           90
                   ....*....|.
gi 1776025254 2927 YGTLNGIIHGA 2937
Cdd:PRK09186    81 YGKIDGAVNCA 91
ACS cd05966
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ...
376-555 5.65e-04

Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.


Pssm-ID: 341270 [Multi-domain]  Cd Length: 608  Bit Score: 46.40  E-value: 5.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  376 IGSPIPGFSMRIVNDHnelveegeiGRFQVSGLSVTSGYYqrpdlnesvFTEDGWFETGDlgflrnGRLTITGRTKDAII 455
Cdd:cd05966    441 IKRPWPGMARTIYGDH---------ERYEDTYFSKFPGYY---------FTGDGARRDED------GYYWITGRVDDVIN 496
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  456 INGINYYSHAIESAVEELSEIetsytAACAVrLGQNstDQL---AIF-FVTsakLND-EQMSQLLRN-IQSHVSQVIG-- 527
Cdd:cd05966    497 VSGHRLGTAEVESALVAHPAV-----AEAAV-VGRP--HDIkgeAIYaFVT---LKDgEEPSDELRKeLRKHVRKEIGpi 565
                          170       180
                   ....*....|....*....|....*...
gi 1776025254  528 VTPEYLLPVqkEEIPKTAIGKIQRTQLK 555
Cdd:cd05966    566 ATPDKIQFV--PGLPKTRSGKIMRRILR 591
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
4172-4329 5.95e-04

11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human 11beta_HSD1 catalyzes the NADP(H)-dependent interconversion of cortisone and cortisol. This subgroup also includes human dehydrogenase/reductase SDR family member 7C (DHRS7C) and DHRS7B. These proteins have the GxxxGxG nucleotide binding motif and S-Y-K catalytic triad characteristic of the SDRs, but have an atypical C-terminal domain that contributes to homodimerization contacts. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187593 [Multi-domain]  Cd Length: 257  Bit Score: 45.27  E-value: 5.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4172 VLLITGGTRGIGLLCARHFAE--CygvkKLVLTGReqlppREEwarfktsntSLAEKIQAVRELEAKgvQVEMLSLTLSD 4249
Cdd:cd05332      5 VVIITGASSGIGEELAYHLARlgA----RLVLSAR-----REE---------RLEEVKSECLELGAP--SPHVVPLDMSD 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4250 DAQVEQTLQHIKRTLGPIGGVIHCAGltdMDTLAFIRKTSDDIQR-VMEPKVSGLTTLYRHVcnEP-LQF-----FVLFS 4322
Cdd:cd05332     65 LEDAEQVVEEALKLFGGLDILINNAG---ISMRSLFHDTSIDVDRkIMEVNYFGPVALTKAA--LPhLIErsqgsIVVVS 139

                   ....*..
gi 1776025254 4323 SVSAIIP 4329
Cdd:cd05332    140 SIAGKIG 146
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
4172-4310 6.04e-04

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 44.83  E-value: 6.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4172 VLLITGGTRGIGLLCARHFAECyGVKKLVLTGReqlppREEWARfktsntslaekiQAVRELEAKGVQVEMLSLTLSDDA 4251
Cdd:PRK05565     7 VAIVTGASGGIGRAIAELLAKE-GAKVVIAYDI-----NEEAAQ------------ELLEEIKEEGGDAIAVKADVSSEE 68
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1776025254 4252 QVEQTLQHIKRTLGPIGGVIHCAGLtdMDTLAFIRKTSDDIQRVMEPKVSGLTTLYRHV 4310
Cdd:PRK05565    69 DVENLVEQIVEKFGKIDILVNNAGI--SNFGLVTDMTDEEWDRVIDVNLTGVMLLTRYA 125
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
4169-4276 6.30e-04

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 44.88  E-value: 6.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4169 KDHVLLITGGTRGIGLLCARHFAEcYGvKKLVLTGREQlppreewarfktsntslAEKIQAVRELEAKGVQVEMLSLTLS 4248
Cdd:PRK12429     3 KGKVALVTGAASGIGLEIALALAK-EG-AKVVIADLND-----------------EAAAAAAEALQKAGGKAIGVAMDVT 63
                           90       100
                   ....*....|....*....|....*...
gi 1776025254 4249 DDAQVEQTLQHIKRTLGPIGGVIHCAGL 4276
Cdd:PRK12429    64 DEEAINAGIDYAVETFGGVDILVNNAGI 91
PRK05872 PRK05872
short chain dehydrogenase; Provisional
4172-4302 6.66e-04

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 45.35  E-value: 6.66e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4172 VLLITGGTRGIGLLCARHFAECyGVkKLVLTGREQLPPREEWARFKTSNTSLaEKIQAVRELEAkgvqvemlsltlsdda 4251
Cdd:PRK05872    11 VVVVTGAARGIGAELARRLHAR-GA-KLALVDLEEAELAALAAELGGDDRVL-TVVADVTDLAA---------------- 71
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1776025254 4252 qVEQTLQHIKRTLGPIGGVIHCAGLT------DMDTLAFirktsddiQRVMEPKVSG 4302
Cdd:PRK05872    72 -MQAAAEEAVERFGGIDVVVANAGIAsggsvaQVDPDAF--------RRVIDVNLLG 119
ENR_SDR cd05372
Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ...
2851-2935 7.63e-04

Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ENRs includes Escherichia coli ENR. ENR catalyzes the NAD(P)H-dependent reduction of enoyl-ACP in the last step of fatty acid biosynthesis. De novo fatty acid biosynthesis is catalyzed by the fatty acid synthetase complex, through the serial addition of 2-carbon subunits. In bacteria and plants,ENR catalyzes one of six synthetic steps in this process. Oilseed rape ENR, and also apparently the NADH-specific form of Escherichia coli ENR, is tetrameric. Although similar to the classical SDRs, this group does not have the canonical catalytic tetrad, nor does it have the typical Gly-rich NAD-binding pattern. Such so-called divergent SDRs have a GXXXXXSXA NAD-binding motif and a YXXMXXXK (or YXXXMXXXK) active site motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187630 [Multi-domain]  Cd Length: 250  Bit Score: 44.49  E-value: 7.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2851 YLITGGAGSLGLLF--AKEIANRTGrsTIVLTGRSVLSEDKENELEALRSIGAEVVyrEADVSDQHAVHHLFEEIKERYG 2928
Cdd:cd05372      4 ILITGIANDRSIAWgiAKALHEAGA--ELAFTYQPEALRKRVEKLAERLGESALVL--PCDVSNDEEIKELFAEVKKDWG 79

                   ....*..
gi 1776025254 2929 TLNGIIH 2935
Cdd:cd05372     80 KLDGLVH 86
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
4169-4329 8.46e-04

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 44.89  E-value: 8.46e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4169 KDHVLLITGGTrgiGLLC---ARHFAECyGVKKLVLtGREQlppreewarfktsntslaEKIQA-VRELEAKGVQVEMLS 4244
Cdd:PRK08277     9 KGKVAVITGGG---GVLGgamAKELARA-GAKVAIL-DRNQ------------------EKAEAvVAEIKAAGGEALAVK 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4245 LTLSDDAQVEQTLQHIKRTLGPIGGVIHCAG------LTDMDTLAFIRKT-------SDDIQRVMEPKVSGltTLYrhvc 4311
Cdd:PRK08277    66 ADVLDKESLEQARQQILEDFGPCDILINGAGgnhpkaTTDNEFHELIEPTktffdldEEGFEFVFDLNLLG--TLL---- 139
                          170       180       190
                   ....*....|....*....|....*....|
gi 1776025254 4312 nePLQFF------------VLFSSVSAIIP 4329
Cdd:PRK08277   140 --PTQVFakdmvgrkggniINISSMNAFTP 167
PRK08219 PRK08219
SDR family oxidoreductase;
4174-4310 8.56e-04

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 44.15  E-value: 8.56e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4174 LITGGTRGIGLLCARHFAECYgvkKLVLTGREQlppreewarfktsntslaekiQAVRELEAKGVQVEMLSLTLSDDAQV 4253
Cdd:PRK08219     7 LITGASRGIGAAIARELAPTH---TLLLGGRPA---------------------ERLDELAAELPGATPFPVDLTDPEAI 62
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1776025254 4254 EQTLQHIKRtlgpIGGVIHCAGLTDMDTLAfiRKTSDDIQRVMEPKVSGLTTLYRHV 4310
Cdd:PRK08219    63 AAAVEQLGR----LDVLVHNAGVADLGPVA--ESTVDEWRATLEVNVVAPAELTRLL 113
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
4169-4277 8.72e-04

Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related proteins have a canonical classical SDR nucleotide-binding motif and active site tetrad. They are predicted oxoacyl-(acyl carrier protein/ACP) reductases. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187599 [Multi-domain]  Cd Length: 236  Bit Score: 44.49  E-value: 8.72e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4169 KDHVLLITGGTRGIGLLCARHFAEcYGVkKLVLTGReqlppREEwarfktsntSLAEKIQAVRELEAKGVQVEMLSLTLS 4248
Cdd:cd05340      3 NDRIILVTGASDGIGREAALTYAR-YGA-TVILLGR-----NEE---------KLRQVADHINEEGGRQPQWFILDLLTC 66
                           90       100
                   ....*....|....*....|....*....
gi 1776025254 4249 DDAQVEQTLQHIKRTLGPIGGVIHCAGLT 4277
Cdd:cd05340     67 TSENCQQLAQRIAVNYPRLDGVLHNAGLL 95
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
4172-4364 8.78e-04

human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup includes human DHRS1 and human HSDL2 and related proteins. These are members of the classical SDR family, with a canonical Gly-rich NAD-binding motif and the typical YXXXK active site motif. However, the rest of the catalytic tetrad is not strongly conserved. DHRS1 mRNA has been detected in many tissues, liver, heart, skeletal muscle, kidney and pancreas; a longer transcript is predominantly expressed in the liver , a shorter one in the heart. HSDL2 may play a part in fatty acid metabolism, as it is found in peroxisomes. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187597 [Multi-domain]  Cd Length: 246  Bit Score: 44.31  E-value: 8.78e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4172 VLLITGGTRGIGLLCARHFAEC-YGVkklVLTGREQLPPReewarfKTSNTSLAEKIQ-AVRELEAKGVQVEMLSLTLSD 4249
Cdd:cd05338      5 VAFVTGASRGIGRAIALRLAKAgATV---VVAAKTASEGD------NGSAKSLPGTIEeTAEEIEAAGGQALPIVVDVRD 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4250 DAQVEQTLQHIKRTLGPIGGVIHCAGLTDMD-TLAFIRKTSDDIQRVMePKVSGLTTLY--RHVCNEPLQFFVLFSSVSA 4326
Cdd:cd05338     76 EDQVRALVEATVDQFGRLDILVNNAGAIWLSlVEDTPAKRFDLMQRVN-LRGTYLLSQAalPHMVKAGQGHILNISPPLS 154
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1776025254 4327 IIPelSAGQADYAMANSYMDYF----AEAHQKHVPIISVQWP 4364
Cdd:cd05338    155 LRP--ARGDVAYAAGKAGMSRLtlglAAELRRHGIAVNSLWP 194
PRK06914 PRK06914
SDR family oxidoreductase;
2850-3069 8.89e-04

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 44.63  E-value: 8.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGLLFAKEIANRTGRstIVLTGRSVLSEDKENELEALRSIGAEVVYREADVSDQHAVHHlFEEIKERYGT 2929
Cdd:PRK06914     5 IAIVTGASSGFGLLTTLELAKKGYL--VIATMRNPEKQENLLSQATQLNLQQNIKVQQLDVTDQNSIHN-FQLVLKEIGR 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2930 LNGIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSGLLHVDEC----------SKdfpldfFIFFSSVSGCLGNAGQADYAA 2999
Cdd:PRK06914    82 IDLLVNNAGYANGGFVEEIPVEEYRKQFETNVFGAISVTQAvlpymrkqksGK------IINISSISGRVGFPGLSPYVS 155
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1776025254 3000 ANSFMDAFAEyrrSLAASKKRFGSTI------SFNWPLWEEGgmqvgaedekrmlKTTGMVPMPTDSGLKAFYQGI 3069
Cdd:PRK06914   156 SKYALEGFSE---SLRLELKPFGIDValiepgSYNTNIWEVG-------------KQLAENQSETTSPYKEYMKKI 215
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
4174-4293 9.50e-04

1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup contains classical SDR proteins, including members identified as 1-cyclohexenylcarbonyl coenzyme A reductase. ChcA of Streptomyces collinus is implicated in the final reduction step of shikimic acid to ansatrienin. ChcA shows sequence similarity to the SDR family of NAD-binding proteins, but it lacks the conserved Tyr of the characteristic catalytic site. This subgroup also contains the NADH-dependent enoyl-[acyl-carrier-protein(ACP)] reductase FabL from Bacillus subtilis. This enzyme participates in bacterial fatty acid synthesis, in type II fatty-acid synthases and catalyzes the last step in each elongation cycle. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187617 [Multi-domain]  Cd Length: 242  Bit Score: 44.27  E-value: 9.50e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4174 LITGGTRGIGLLCARHFAEcYGVkKLVLTGREqlppreewarfktsntSLAEKIQAVRELEAKGVQVEMLSLTLSDDAQV 4253
Cdd:cd05359      2 LVTGGSRGIGKAIALRLAE-RGA-DVVINYRK----------------SKDAAAEVAAEIEELGGKAVVVRADVSQPQDV 63
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1776025254 4254 EQTLQHIKRTLGPIGGVIHCAG------LTDMDTLAFIRKTSDDIQ 4293
Cdd:cd05359     64 EEMFAAVKERFGRLDVLVSNAAagafrpLSELTPAHWDAKMNTNLK 109
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
4169-4281 9.73e-04

d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, catalyzes the interconversion of D-3-hydroxybutyrate and acetoacetate. It is a classical SDR, with the canonical NAD-binding motif and active site tetrad. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187644 [Multi-domain]  Cd Length: 258  Bit Score: 44.36  E-value: 9.73e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4169 KDHVLLITGGTRGIGLLCARHFAECYGvkKLVLTGREQlppreewarfktsntslAEKIQAVRE--LEAKGVQVEMLSLT 4246
Cdd:cd08940      1 KGKVALVTGSTSGIGLGIARALAAAGA--NIVLNGFGD-----------------AAEIEAVRAglAAKHGVKVLYHGAD 61
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1776025254 4247 LSDDAQVEQTLQHIKRTLGPI------GGVIHCAGLTDMDT 4281
Cdd:cd08940     62 LSKPAAIEDMVAYAQRQFGGVdilvnnAGIQHVAPIEDFPT 102
AcpA COG3433
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ...
3115-3190 1.00e-03

Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442659 [Multi-domain]  Cd Length: 295  Bit Score: 44.74  E-value: 1.00e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1776025254 3115 LEAALIQMVGAILKVNTDDIDVNTELSEYGFDSVTFTVFTNKInEKFQLELTPTIFFEYGSVQSLAEYVVAAYQGE 3190
Cdd:COG3433    220 TEEELRADVAELLGVDPEEIDPDDNLFDLGLDSIRLMQLVERW-RKAGLDVSFADLAEHPTLAAWWALLAAAQAAA 294
PRK12449 PRK12449
acyl carrier protein; Provisional
592-666 1.02e-03

acyl carrier protein; Provisional


Pssm-ID: 183533 [Multi-domain]  Cd Length: 80  Bit Score: 40.84  E-value: 1.02e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1776025254  592 REEIQEHLLTCLTEELHVSRDWVEPNANIQS-LGVNSIKMMKLIRSIEKNYHIKLTAREIHQYPTIERLASYLSEH 666
Cdd:PRK12449     3 REEIFERLINLIQKQRSYLSLAITEQTHLKDdLAVDSIELVEFIINVEDEFHIAIPDEDVEDMVSMGDLLDYLVQR 78
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
2849-3012 1.04e-03

classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a canonical active site triad (and also active site Asn) and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187618 [Multi-domain]  Cd Length: 233  Bit Score: 44.30  E-value: 1.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2849 GVYLITGGAGSLGLLFAKEIANRtgRSTIVLTGRSvlSEDKENELEALRSIGAEVVYREADVSDQHAVHHLFEEIKERYG 2928
Cdd:cd05360      1 QVVVITGASSGIGRATALAFAER--GAKVVLAARS--AEALHELAREVRELGGEAIAVVADVADAAQVERAADTAVERFG 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2929 TLNGIIHGAG-SIKDHFiIHKTNEEFQEVLqpKVSGLLHVDECSKDFPL------DFFIFFSSVSGCLGNAGQADYAAAN 3001
Cdd:cd05360     77 RIDTWVNNAGvAVFGRF-EDVTPEEFRRVF--DVNYLGHVYGTLAALPHlrrrggGALINVGSLLGYRSAPLQAAYSASK 153
                          170
                   ....*....|.
gi 1776025254 3002 SFMDAFAEYRR 3012
Cdd:cd05360    154 HAVRGFTESLR 164
PRK08628 PRK08628
SDR family oxidoreductase;
2850-2958 1.04e-03

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 44.18  E-value: 1.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLG----LLFAKEIAnrtgrsTIVLTGRSvlseDKENE-LEALRSIGAEVVYREADVSDQHAVHHLFEEIK 2924
Cdd:PRK08628     9 VVIVTGGASGIGaaisLRLAEEGA------IPVIFGRS----APDDEfAEELRALQPRAEFVQVDLTDDAQCRDAVEQTV 78
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1776025254 2925 ERYGTLNGIIHGAGsIKDHFIIHKTNEEFQEVLQ 2958
Cdd:PRK08628    79 AKFGRIDGLVNNAG-VNDGVGLEAGREAFVASLE 111
prpE PRK10524
propionyl-CoA synthetase; Provisional
1275-1641 1.05e-03

propionyl-CoA synthetase; Provisional


Pssm-ID: 182517 [Multi-domain]  Cd Length: 629  Bit Score: 45.32  E-value: 1.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1275 DQDWDEIAQTASDRKVLTRTVTPENLAYVIYTSGSTGKPKGVMiphkaltnflvsmGETPGLTaedkmLAVTT---YCFD 1351
Cdd:PRK10524   210 DVDYATLRAQHLGARVPVEWLESNEPSYILYTSGTTGKPKGVQ-------------RDTGGYA-----VALATsmdTIFG 271
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1352 IAALELFL-----------------PLIKGAHCYICQ-TEHTKD-------VEKLKRDIRTIKPT---VMQATPATW--- 1400
Cdd:PRK10524   272 GKAGETFFcasdigwvvghsyivyaPLLAGMATIMYEgLPTRPDagiwwriVEKYKVNRMFSAPTairVLKKQDPALlrk 351
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1401 ------KMLFYSGweneenvkilcggEALPETLKRYFldtgSEAWNM-----FGPTET--TIWSAVQRINDECSR-ATIG 1466
Cdd:PRK10524   352 hdlsslRALFLAG-------------EPLDEPTASWI----SEALGVpvidnYWQTETgwPILAIARGVEDRPTRlGSPG 414
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1467 RPIA--NTQIyITDSQLAPVPAGVPGELCIAGD---GVAKGYYKKeeltDSRFIDNPFEP-GSKLYRTGDMARWLPGGRI 1540
Cdd:PRK10524   415 VPMYgyNVKL-LNEVTGEPCGPNEKGVLVIEGPlppGCMQTVWGD----DDRFVKTYWSLfGRQVYSTFDWGIRDADGYY 489
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1541 EYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMDNL-----AAYYTAKHANASLTA-------RELRHFVKN 1608
Cdd:PRK10524   490 FILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALkgqvaVAFVVPKDSDSLADRearlaleKEIMALVDS 569
                          410       420       430
                   ....*....|....*....|....*....|....*
gi 1776025254 1609 ALPAYMVPS--YFIQLdhMPLTPNGKIDRNSLKNI 1641
Cdd:PRK10524   570 QLGAVARPArvWFVSA--LPKTRSGKLLRRAIQAI 602
PRK07677 PRK07677
short chain dehydrogenase; Provisional
2850-2937 1.06e-03

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 44.28  E-value: 1.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGLLFAKEIANRTGRstIVLTGRS--VLSEDKeNELEAlrsIGAEVVYREADVSDQHAVHHLFEEIKERY 2927
Cdd:PRK07677     3 VVIITGGSSGMGKAMAKRFAEEGAN--VVITGRTkeKLEEAK-LEIEQ---FPGQVLTVQMDVRNPEDVQKMVEQIDEKF 76
                           90
                   ....*....|
gi 1776025254 2928 GTLNGIIHGA 2937
Cdd:PRK07677    77 GRIDALINNA 86
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
4171-4356 1.13e-03

clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent reduction of clavulanate-9-aldehyde to clavulanic acid, a beta-lactamase inhibitor. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187639 [Multi-domain]  Cd Length: 243  Bit Score: 44.07  E-value: 1.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4171 HVLLITGGTRGIGLLCARHFAEcYGVKkLVLTGREqlppreewarfktsntslAEKIQAV-RELEAKGVQVEMLSLTLSD 4249
Cdd:cd08934      4 KVALVTGASSGIGEATARALAA-EGAA-VAIAARR------------------VDRLEALaDELEAEGGKALVLELDVTD 63
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4250 DAQVEQTLQHIKRTLGPIGGVIHCAGL------TDMDTLafirktsdDIQRVMEPKVSGLttLYRHVCNEPLQF------ 4317
Cdd:cd08934     64 EQQVDAAVERTVEALGRLDILVNNAGImllgpvEDADTT--------DWTRMIDTNLLGL--MYTTHAALPHHLlrnkgt 133
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1776025254 4318 FVLFSSVSAIIpeLSAGQADYAMANSYMDYFAEAHQKHV 4356
Cdd:cd08934    134 IVNISSVAGRV--AVRNSAVYNATKFGVNAFSEGLRQEV 170
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
2850-3013 1.29e-03

classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site tetrad and glycine-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187648 [Multi-domain]  Cd Length: 246  Bit Score: 44.02  E-value: 1.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGLLFAKEIANRTGRstIVLTGRsvlseDKENELEALRSIGAEVVYREADVSDQHAVHHLFEEIKERYGT 2929
Cdd:cd08944      5 VAIVTGAGAGIGAACAARLAREGAR--VVVADI-----DGGAAQAVVAQIAGGALALRVDVTDEQQVAALFERAVEEFGG 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2930 LNGIIHGAGSIK-DHFIIHKTNEEFQEVLQPKVSGLLHVdeCSKDFPL------DFFIFFSSVSGCLGNAGQADYAAANS 3002
Cdd:cd08944     78 LDLLVNNAGAMHlTPAIIDTDLAVWDQTMAINLRGTFLC--CRHAAPRmiarggGSIVNLSSIAGQSGDPGYGAYGASKA 155
                          170
                   ....*....|....*.
gi 1776025254 3003 FMD-----AFAEYRRS 3013
Cdd:cd08944    156 AIRnltrtLAAELRHA 171
FabI COG0623
Enoyl-[acyl-carrier-protein] reductase FabI [Lipid transport and metabolism]; Enoyl- ...
2876-2940 1.39e-03

Enoyl-[acyl-carrier-protein] reductase FabI [Lipid transport and metabolism]; Enoyl-[acyl-carrier-protein] reductase FabI is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440388 [Multi-domain]  Cd Length: 254  Bit Score: 43.86  E-value: 1.39e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1776025254 2876 TIVLTGRSVLSEDKENELeaLRSIGAEVVYrEADVSDQHAVHHLFEEIKERYGTLNGIIHgagSI 2940
Cdd:COG0623     33 ELAFTYQGEALKKRVEPL--AEELGSALVL-PCDVTDDEQIDALFDEIKEKWGKLDFLVH---SI 91
PRK05876 PRK05876
short chain dehydrogenase; Provisional
2852-3058 1.46e-03

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 44.18  E-value: 1.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2852 LITGGAGSLGLLFAKEIANRTGRSTIVLTGRSVLsedkENELEALRSIGAEVVYREADVSDQHAVHHLFEEIKERYGTLN 2931
Cdd:PRK05876    10 VITGGASGIGLATGTEFARRGARVVLGDVDKPGL----RQAVNHLRAEGFDVHGVMCDVRHREEVTHLADEAFRLLGHVD 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2932 GIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSGLLHVDECSKDFPLD-----FFIFFSSVSGCLGNAGQADYAAANSFMDA 3006
Cdd:PRK05876    86 VVFSNAGIVVGGPIVEMTHDDWRWVIDVDLWGSIHTVEAFLPRLLEqgtggHVVFTASFAGLVPNAGLGAYGVAKYGVVG 165
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1776025254 3007 FAEyrrSLAASKKRFGSTISFNWPLWEEGGMQVGAEDEK----RMLKTTG-MVPMPT 3058
Cdd:PRK05876   166 LAE---TLAREVTADGIGVSVLCPMVVETNLVANSERIRgaacAQSSTTGsPGPLPL 219
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
2852-2986 1.47e-03

Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 44.20  E-value: 1.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2852 LITGGAGSLGLLFAKEIANRtGRSTIVLtgrsVLSEDKENELEALRsiGAEVVyrEADVSDQHAVHHLFEEIkerygtlN 2931
Cdd:COG0451      3 LVTGGAGFIGSHLARRLLAR-GHEVVGL----DRSPPGAANLAALP--GVEFV--RGDLRDPEALAAALAGV-------D 66
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1776025254 2932 GIIHGAGsikdhfIIHKTNEEFQEVLQPKVSGLLHVDECSKDFPLDFFIFFSSVS 2986
Cdd:COG0451     67 AVVHLAA------PAGVGEEDPDETLEVNVEGTLNLLEAARAAGVKRFVYASSSS 115
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
2850-2999 1.59e-03

meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases (BDHs) catalyze the NAD+ dependent conversion of 2,3-butanediol to acetonin; BDHs are classified into types according to their stereospecificity as to substrates and products. Included in this subgroup are Klebsiella pneumonia meso-BDH which catalyzes meso-2,3-butanediol to D(-)-acetonin, and Corynebacterium glutamicum L-BDH which catalyzes lX+)-2,3-butanediol to L(+)-acetonin. This subgroup is comprised of classical SDRs with the characteristic catalytic triad and NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187624 [Multi-domain]  Cd Length: 257  Bit Score: 43.90  E-value: 1.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGLLFAKEIANRTGRSTIVLTGRSVLSEDKENELEALrsiGAEVVYREADVSDQHAVHHLFEEIKERYGT 2929
Cdd:cd05366      4 VAIITGAAQGIGRAIAERLAADGFNIVLADLNLEEAAKSTIQEISEA---GYNAVAVGADVTDKDDVEALIDQAVEKFGS 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1776025254 2930 LNGIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSG-LLHVDECSKDFpLDF-----FIFFSSVSGCLGNAGQADYAA 2999
Cdd:cd05366     81 FDVMVNNAGIAPITPLLTITEEDLKKVYAVNVFGvLFGIQAAARQF-KKLghggkIINASSIAGVQGFPNLGAYSA 155
PRK07109 PRK07109
short chain dehydrogenase; Provisional
2841-2938 1.97e-03

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 44.14  E-value: 1.97e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2841 LHMPWRDEGVYLITGGAGSLGLLFAKEIANRTGRstIVLTGRSvlsEDKENELEA-LRSIGAEVVYREADVSDQHAVHHL 2919
Cdd:PRK07109     1 MMLKPIGRQVVVITGASAGVGRATARAFARRGAK--VVLLARG---EEGLEALAAeIRAAGGEALAVVADVADAEAVQAA 75
                           90
                   ....*....|....*....
gi 1776025254 2920 FEEIKERYGTLNGIIHGAG 2938
Cdd:PRK07109    76 ADRAEEELGPIDTWVNNAM 94
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
2847-2967 2.03e-03

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 43.54  E-value: 2.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2847 DEGVYLITGGAGSLGLLFAKEIAnRTGRSTIVLTGRSvlsEDKENELeaLRSIGAEVVYREADVSDQHAVHHLFEEIKER 2926
Cdd:PRK08642     4 SEQTVLVTGGSRGLGAAIARAFA-REGARVVVNYHQS---EDAAEAL--ADELGDRAIALQADVTDREQVQAMFATATEH 77
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1776025254 2927 YG-TLNGIIHGA-------GSIKDHFiIHKTNEEFQEVLQPKVSGLLHV 2967
Cdd:PRK08642    78 FGkPITTVVNNAladfsfdGDARKKA-DDITWEDFQQQLEGSVKGALNT 125
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
2852-2939 2.06e-03

1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup contains classical SDR proteins, including members identified as 1-cyclohexenylcarbonyl coenzyme A reductase. ChcA of Streptomyces collinus is implicated in the final reduction step of shikimic acid to ansatrienin. ChcA shows sequence similarity to the SDR family of NAD-binding proteins, but it lacks the conserved Tyr of the characteristic catalytic site. This subgroup also contains the NADH-dependent enoyl-[acyl-carrier-protein(ACP)] reductase FabL from Bacillus subtilis. This enzyme participates in bacterial fatty acid synthesis, in type II fatty-acid synthases and catalyzes the last step in each elongation cycle. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187617 [Multi-domain]  Cd Length: 242  Bit Score: 43.11  E-value: 2.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2852 LITGGAGSLGLLFAKEIANRTgrSTIVLTGRSvlSEDKENELEA-LRSIGAEVVYREADVSDQHAVHHLFEEIKERYGTL 2930
Cdd:cd05359      2 LVTGGSRGIGKAIALRLAERG--ADVVINYRK--SKDAAAEVAAeIEELGGKAVVVRADVSQPQDVEEMFAAVKERFGRL 77

                   ....*....
gi 1776025254 2931 NGIIHGAGS 2939
Cdd:cd05359     78 DVLVSNAAA 86
SCP-x_thiolase cd00829
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ...
1898-1963 2.28e-03

Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; SCP-2 has multiple roles in intracellular lipid circulation and metabolism. The N-terminal presequence in the SCP-x isoform represents a peroxisomal 3-ketacyl-Coa thiolase specific for branched-chain acyl CoAs, which is proteolytically cleaved from the sterol carrier protein.


Pssm-ID: 238425 [Multi-domain]  Cd Length: 375  Bit Score: 43.79  E-value: 2.28e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1776025254 1898 GYVSWVLAQSgTIPTMISHKLGLRG-PSYFVHANCSSSLIGLHSAYKSLLSAESDYALVGGATLHTE 1963
Cdd:cd00829     44 GNAAGGRFQS-FPGALIAEYLGLLGkPATRVEAAGASGSAAVRAAAAAIASGLADVVLVVGAEKMSD 109
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
4172-4276 2.31e-03

gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent conversion of carbon source D-gluconate and 5-keto-D-gluconate. This SDR subgroup has a classical Gly-rich NAD(P)-binding motif and a conserved active site tetrad pattern. However, it has been proposed that Arg104 (Streptococcus suis Ga5DH numbering), as well as an active site Ca2+, play a critical role in catalysis. In addition to Ga5DHs this subgroup contains Erwinia chrysanthemi KduD which is involved in pectin degradation, and is a putative 2,5-diketo-3-deoxygluconate dehydrogenase. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107,15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187605 [Multi-domain]  Cd Length: 248  Bit Score: 43.12  E-value: 2.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4172 VLLITGGTRGIGLLCARHFAEcYGVKkLVLTGReqlppreewarfktsNTSLAEKIQAvrELEAKGVQVEMLSLTLSDDA 4251
Cdd:cd05347      7 VALVTGASRGIGFGIASGLAE-AGAN-IVINSR---------------NEEKAEEAQQ--LIEKEGVEATAFTCDVSDEE 67
                           90       100
                   ....*....|....*....|....*
gi 1776025254 4252 QVEQTLQHIKRTLGPIGGVIHCAGL 4276
Cdd:cd05347     68 AIKAAVEAIEEDFGKIDILVNNAGI 92
hsFATP4_like cd05939
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ...
165-243 2.41e-03

Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341262 [Multi-domain]  Cd Length: 474  Bit Score: 43.95  E-value: 2.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254  165 RAIIVEDLLSAEADTDWHQSSPEDLA-----LLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDH 239
Cdd:cd05939     77 KALIFNLLDPLLTQSSTEPPSQDDVNfrdklFYIYTSGTTGLPKAAVIVHSRYYRIAAGAYYAFGMRPEDVVYDCLPLYH 156

                   ....*
gi 1776025254  240 -VGGI 243
Cdd:cd05939    157 sAGGI 161
PRK06123 PRK06123
SDR family oxidoreductase;
2850-3005 2.46e-03

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 43.23  E-value: 2.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGLLFAKeIANRTGRSTIVLTGRSvlSEDKENELEALRSIGAEVVYREADVSDQHAVHHLFEEIKERYGT 2929
Cdd:PRK06123     4 VMIITGASRGIGAATAL-LAAERGYAVCLNYLRN--RDAAEAVVQAIRRQGGEALAVAADVADEADVLRLFEAVDRELGR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2930 LNGIIHGAGSIKDHFII-HKTNEEFQEVLQPKVSG-LLHVDECSKDFPLDF------FIFFSSVSGCLGNAGQ-ADYAAA 3000
Cdd:PRK06123    81 LDALVNNAGILEAQMRLeQMDAARLTRIFATNVVGsFLCAREAVKRMSTRHggrggaIVNVSSMAARLGSPGEyIDYAAS 160

                   ....*
gi 1776025254 3001 NSFMD 3005
Cdd:PRK06123   161 KGAID 165
PRK08340 PRK08340
SDR family oxidoreductase;
2852-2941 2.62e-03

SDR family oxidoreductase;


Pssm-ID: 169390 [Multi-domain]  Cd Length: 259  Bit Score: 43.25  E-value: 2.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2852 LITGGAGSLGLLFAKEIANRTGRstIVLTGRSvlSEDKENELEALRSIGaEVVYREADVSDQHAVHHLFEEIKERYGTLN 2931
Cdd:PRK08340     4 LVTASSRGIGFNVARELLKKGAR--VVISSRN--EENLEKALKELKEYG-EVYAVKADLSDKDDLKNLVKEAWELLGGID 78
                           90
                   ....*....|
gi 1776025254 2932 GIIHGAGSIK 2941
Cdd:PRK08340    79 ALVWNAGNVR 88
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
2845-2964 2.63e-03

human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These proteins are members of the SDR family, with a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187601 [Multi-domain]  Cd Length: 250  Bit Score: 42.89  E-value: 2.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2845 WRDEgVYLITGGAGSLGLLFAKEIANRTGRstIVLTGRSVlseDKENELEA-LRSIG-AEVVYREADVSDQHAVHHLFEE 2922
Cdd:cd05343      4 WRGR-VALVTGASVGIGAAVARALVQHGMK--VVGCARRV---DKIEALAAeCQSAGyPTLFPYQCDLSNEEQILSMFSA 77
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1776025254 2923 IKERYGTLNGIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSGL 2964
Cdd:cd05343     78 IRTQHQGVDVCINNAGLARPEPLLSGKTEGWKEMFDVNVLAL 119
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
2850-2938 2.71e-03

Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER is a peroxisomal protein with a proposed role in fatty acid elongation. Fatty acid synthesis is known to occur in the both endoplasmic reticulum and mitochondria; peroxisomal TER has been proposed as an additional fatty acid elongation system, it reduces the double bond at C-2 as the last step of elongation. This system resembles the mitochondrial system in that acetyl-CoA is used as a carbon donor. TER may also function in phytol metabolism, reducting phytenoyl-CoA to phytanoyl-CoA in peroxisomes. DECR processes double bonds in fatty acids to increase their utility in fatty acid metabolism; it reduces 2,4-dienoyl-CoA to an enoyl-CoA. DECR is active in mitochondria and peroxisomes. This subgroup has the Gly-rich NAD-binding motif of the classical SDR family, but does not display strong identity to the canonical active site tetrad, and lacks the characteristic Tyr at the usual position. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187627 [Multi-domain]  Cd Length: 249  Bit Score: 42.96  E-value: 2.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGllfaKEIANRTGR--STIVLTGRS--VLSEDKEnELEALRsiGAEVVYREADVSDQHAVHHLFEEIKE 2925
Cdd:cd05369      5 VAFITGGGTGIG----KAIAKAFAElgASVAIAGRKpeVLEAAAE-EISSAT--GGRAHPIQCDVRDPEAVEAAVDETLK 77
                           90
                   ....*....|...
gi 1776025254 2926 RYGTLNGIIHGAG 2938
Cdd:cd05369     78 EFGKIDILINNAA 90
UDP_invert_4-6DH_SDR_e cd05237
UDP-Glcnac (UDP-linked N-acetylglucosamine) inverting 4,6-dehydratase, extended (e) SDRs; ...
2852-2984 2.80e-03

UDP-Glcnac (UDP-linked N-acetylglucosamine) inverting 4,6-dehydratase, extended (e) SDRs; UDP-Glcnac inverting 4,6-dehydratase was identified in Helicobacter pylori as the hexameric flaA1 gene product (FlaA1). FlaA1 is hexameric, possesses UDP-GlcNAc-inverting 4,6-dehydratase activity, and catalyzes the first step in the creation of a pseudaminic acid derivative in protein glycosylation. Although this subgroup has the NADP-binding motif characteristic of extended SDRs, its members tend to have a Met substituted for the active site Tyr found in most SDR families. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187548 [Multi-domain]  Cd Length: 287  Bit Score: 43.38  E-value: 2.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2852 LITGGAGSLGLLFAKEIAnRTGRSTIVLTGRsvlSEDKENELE---ALRSIGAEVVYREADVSDQHAVHHLFEEIKERYg 2928
Cdd:cd05237      6 LVTGGAGSIGSELVRQIL-KFGPKKLIVFDR---DENKLHELVrelRSRFPHDKLRFIIGDVRDKERLRRAFKERGPDI- 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1776025254 2929 tlngIIHgAGSIKdhfiiHKTNEE--FQEVLQPKVSGLLHVDECSKDFPLDFFIFFSS 2984
Cdd:cd05237     81 ----VFH-AAALK-----HVPSMEdnPEEAIKTNVLGTKNVIDAAIENGVEKFVCIST 128
Qor COG0604
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ...
2852-2913 3.00e-03

NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and conversion, General function prediction only];


Pssm-ID: 440369 [Multi-domain]  Cd Length: 322  Bit Score: 43.21  E-value: 3.00e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1776025254 2852 LITGGAGSLGlLFAKEIANRTGRSTIVLTGrsvlSEDKeneLEALRSIGAEVV--YREADVSDQ 2913
Cdd:COG0604    144 LVHGAAGGVG-SAAVQLAKALGARVIATAS----SPEK---AELLRALGADHVidYREEDFAER 199
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
2850-2938 3.22e-03

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 42.85  E-value: 3.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGLLFAKEIAnRTGRSTIVLTGRSvlsedkENELEALRSIGAEVVyrEADVSDQHAVHHLFEEIKERYGT 2929
Cdd:PRK06463     9 VALITGGTRGIGRAIAEAFL-REGAKVAVLYNSA------ENEAKELREKGVFTI--KCDVGNRDQVKKSKEVVEKEFGR 79

                   ....*....
gi 1776025254 2930 LNGIIHGAG 2938
Cdd:PRK06463    80 VDVLVNNAG 88
PRK06124 PRK06124
SDR family oxidoreductase;
4172-4310 3.55e-03

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 42.78  E-value: 3.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4172 VLLITGGTRGIGLLCARHFAECyGVKKLVlTGREqlppreewarfktsntslAEKIQ-AVRELEAKGVQVEMLSLTLSDD 4250
Cdd:PRK06124    13 VALVTGSARGLGFEIARALAGA-GAHVLV-NGRN------------------AATLEaAVAALRAAGGAAEALAFDIADE 72
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4251 AQVEQTLQHIKRTLGPIGGVIHCAGLTDMDTLAFIrkTSDDIQRVMEPKVSGLTTLYRHV 4310
Cdd:PRK06124    73 EAVAAAFARIDAEHGRLDILVNNVGARDRRPLAEL--DDAAIRALLETDLVAPILLSRLA 130
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
4172-4290 3.63e-03

tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6,8-tetrahydroxynaphthalene reductase (4HNR) of Magnaporthe grisea and the related 1,3,8-trihydroxynaphthalene reductase (3HNR) are typical members of the SDR family containing the canonical glycine rich NAD(P)-binding site and active site tetrad, and function in fungal melanin biosynthesis. This subgroup also includes an SDR from Norway spruce that may function to protect against both biotic and abitoic stress. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187620 [Multi-domain]  Cd Length: 243  Bit Score: 42.65  E-value: 3.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4172 VLLITGGTRGIGLLCARHFAECyGVKKLVLTGreqlppreewarfktSNTSLAEKIqaVRELEAKGVQVEMLSLTLSDDA 4251
Cdd:cd05362      5 VALVTGASRGIGRAIAKRLARD-GASVVVNYA---------------SSKAAAEEV--VAEIEAAGGKAIAVQADVSDPS 66
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1776025254 4252 QVEQTLQHIKRTLGPIGGVIHCAGLTDMdtlAFIRKTSD 4290
Cdd:cd05362     67 QVARLFDAAEKAFGGVDILVNNAGVMLK---KPIAETSE 102
Thiolase_N pfam00108
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
4734-4780 4.67e-03

Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl synthase (pfam00109), and also chalcone synthase.


Pssm-ID: 459676 [Multi-domain]  Cd Length: 260  Bit Score: 42.29  E-value: 4.67e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1776025254 4734 PSVVVDTACSSALVGMNMAIQALRGGDIQSAIVGGVSLLsSDASHRL 4780
Cdd:pfam00108   77 PAVTINKVCGSGLKAVYLAAQSIASGDADVVLAGGVESM-SHAPYAL 122
dTDP_GD_SDR_e cd05246
dTDP-D-glucose 4,6-dehydratase, extended (e) SDRs; This subgroup contains dTDP-D-glucose 4, ...
2851-2996 4.85e-03

dTDP-D-glucose 4,6-dehydratase, extended (e) SDRs; This subgroup contains dTDP-D-glucose 4,6-dehydratase and related proteins, members of the extended-SDR family, with the characteristic Rossmann fold core region, active site tetrad and NAD(P)-binding motif. dTDP-D-glucose 4,6-dehydratase is closely related to other sugar epimerases of the SDR family. dTDP-D-dlucose 4,6,-dehydratase catalyzes the second of four steps in the dTDP-L-rhamnose pathway (the dehydration of dTDP-D-glucose to dTDP-4-keto-6-deoxy-D-glucose) in the synthesis of L-rhamnose, a cell wall component of some pathogenic bacteria. In many gram negative bacteria, L-rhamnose is an important constituent of lipopoylsaccharide O-antigen. The larger N-terminal portion of dTDP-D-Glucose 4,6-dehydratase forms a Rossmann fold NAD-binding domain, while the C-terminus binds the sugar substrate. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187557 [Multi-domain]  Cd Length: 315  Bit Score: 42.54  E-value: 4.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2851 YLITGGAGSLGLLFAKEIANRTGRSTIVltgrsVLseDKEN---ELEALRSIGAEVVYR--EADVSDQHAVHHLFEEIKe 2925
Cdd:cd05246      3 ILVTGGAGFIGSNFVRYLLNKYPDYKII-----NL--DKLTyagNLENLEDVSSSPRYRfvKGDICDAELVDRLFEEEK- 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2926 rygtLNGIIHGAG------SIKDHFIIHKTNeefqevlqpkVSG---LLhvdECSKDFPLDFFIFFSS--VSGCLGNAGQ 2994
Cdd:cd05246     75 ----IDAVIHFAAeshvdrSISDPEPFIRTN----------VLGtytLL---EAARKYGVKRFVHISTdeVYGDLLDDGE 137

                   ..
gi 1776025254 2995 AD 2996
Cdd:cd05246    138 FT 139
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
4172-4341 5.02e-03

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 42.26  E-value: 5.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4172 VLLITGGTRGIGLLCARHFAecygvkklvltgreqlppREEWARFKTSNTSLAEKIQAVRELEAKGVQVEMLSLTLSDDA 4251
Cdd:PRK12745     4 VALVTGGRRGIGLGIARALA------------------AAGFDLAINDRPDDEELAATQQELRALGVEVIFFPADVADLS 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4252 QVEQTLQHIKRTLGPIGGVIHCAGLTDMDTLAFIRKTSDDIQRVMEPKVSG---LTTLY-------RHVCNEPLQFFVLF 4321
Cdd:PRK12745    66 AHEAMLDAAQAAWGRIDCLVNNAGVGVKVRGDLLDLTPESFDRVLAINLRGpffLTQAVakrmlaqPEPEELPHRSIVFV 145
                          170       180
                   ....*....|....*....|
gi 1776025254 4322 SSVSAIIpeLSAGQADYAMA 4341
Cdd:PRK12745   146 SSVNAIM--VSPNRGEYCIS 163
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
2850-2943 5.20e-03

insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains insect type ADH, and 15-hydroxyprostaglandin dehydrogenase (15-PGDH) type I; these proteins are classical SDRs. ADH catalyzes the NAD+-dependent oxidation of alcohols to aldehydes/ketones. This subgroup is distinct from the zinc-dependent alcohol dehydrogenases of the medium chain dehydrogenase/reductase family, and evolved in fruit flies to allow the digestion of fermenting fruit. 15-PGDH catalyzes the NAD-dependent interconversion of (5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-13-enoate and (5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-13-enoate, and has a typical SDR glycine-rich NAD-binding motif, which is not fully present in ADH. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187584 [Multi-domain]  Cd Length: 244  Bit Score: 41.90  E-value: 5.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGLLFAKEIANRtgrstivltGRSVLSEDKENELEALRSIGA-----EVVYREADVSDQHAVHHLFEEIK 2924
Cdd:cd05323      2 VAIITGGASGIGLATAKLLLKK---------GAKVAILDRNENPGAAAELQAinpkvKATFVQCDVTSWEQLAAAFKKAI 72
                           90
                   ....*....|....*....
gi 1776025254 2925 ERYGTLNGIIHGAGSIKDH 2943
Cdd:cd05323     73 EKFGRVDILINNAGILDEK 91
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
4169-4303 5.87e-03

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 41.94  E-value: 5.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4169 KDHVLLITGGTRGIGllcaRHFAECYGvkklvltgreqlpprEEWARFKTSNTSLAEKIQAVRELeakGVQVEMLSLTLS 4248
Cdd:PRK07067     5 QGKVALLTGAASGIG----EAVAERYL---------------AEGARVVIADIKPARARLAALEI---GPAAIAVSLDVT 62
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1776025254 4249 DDAQVEQTLQHIKRTLGPIGGVIHCAGLTDMDTLAFIrkTSDDIQRVMEPKVSGL 4303
Cdd:PRK07067    63 RQDSIDRIVAAAVERFGGIDILFNNAALFDMAPILDI--SRDSYDRLFAVNVKGL 115
PRK07856 PRK07856
SDR family oxidoreductase;
2850-2938 7.94e-03

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 41.46  E-value: 7.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGLLFAKEIAnRTGrSTIVLTGRSVLSEDKenelealrsiGAEVVYREADVSDQHAVHHLFEEIKERYGT 2929
Cdd:PRK07856     8 VVLVTGGTRGIGAGIARAFL-AAG-ATVVVCGRRAPETVD----------GRPAEFHAADVRDPDQVAALVDAIVERHGR 75

                   ....*....
gi 1776025254 2930 LNGIIHGAG 2938
Cdd:PRK07856    76 LDVLVNNAG 84
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
2850-2963 9.30e-03

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 41.56  E-value: 9.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGLLFAKEIANRTGRSTIV-LTGRSV--LSEDKENELEALRSIGAEVvyreaDVSDQHAVHHLFEEIKER 2926
Cdd:PRK12384     4 VAVVIGGGQTLGAFLCHGLAEEGYRVAVAdINSEKAanVAQEINAEYGEGMAYGFGA-----DATSEQSVLALSRGVDEI 78
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1776025254 2927 YGTLNGIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSG 2963
Cdd:PRK12384    79 FGRVDLLVYNAGIAKAAFITDFQLGDFDRSLQVNLVG 115
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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