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Conserved domains on  [gi|53747904|emb|CAF05649|]
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TubD protein [Archangium disciforme]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
 13-1382 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: 1087.21  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   13 IALVGMAGRFPGAPDVESFWRNLVAGVESISFFSEEELRQAG--VSEQIRRRPEYVPAKGVLEDLELFDAGFFGYSPREA 90
Cdd:COG3321    6 IAIIGMACRFPGADDPEEFWRNLRAGRDAITEVPADRWDADAyyDPDPDAPGKTYVRWGGFLDDVDEFDALFFGISPREA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   91 SHLDPQQRLLLECSWEALEDAGLRPDQLPGW-VGVYVGAGDTSYrFQLLRGHGDPLSGSkdvaGFFGNYPDFLATRVAYK 169
Cdd:COG3321   86 EAMDPQQRLLLEVAWEALEDAGYDPESLAGSrTGVFVGASSNDY-ALLLLADPEAIDAY----ALTGNAKSVLAGRISYK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  170 LNLRGPALGIHTACSTSLVSINMACSALRGFECDMALAGGVSLRLPARSGYLYEEGGVASKDGHCRPFDARAtgtvtgdg 249
Cdd:COG3321  161 LDLRGPSVTVDTACSSSLVAVHLACQSLRSGECDLALAGGVNLMLTPESFILFSKGGMLSPDGRCRAFDADAdgyvrgeg 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  250 vgvvvLKRLEDALKARDPIHAVIRGWALNNDGASRaGFTAPSVEGQSEVIALAHAAAGISARDITYVEAHGTGTPLGDPI 329
Cdd:COG3321  241 vgvvvLKRLSDALRDGDRIYAVIRGSAVNQDGRSN-GLTAPNGPAQAAVIRRALADAGVDPATVDYVEAHGTGTPLGDPI 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  330 EVAALTRAFRAHTADTAFCTLGAVKSNIGHLDAAAGVAGVIKTVQALRHRLIPPTLHFERPNPALHLEQSPFFVNTQPLP 409
Cdd:COG3321  320 EAAALTAAFGQGRPADQPCAIGSVKSNIGHLEAAAGVAGLIKAVLALRHGVLPPTLHFETPNPHIDFENSPFYVNTELRP 399

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  410 WESPRGPRLAGVSSFGIGGTNAHTLFEEAPP--PPASGPTRPNQVLLLSARSTSALEHIAGRLAAHLRRHPDLELADVAF 487
Cdd:COG3321  400 WPAGGGPRRAGVSSFGFGGTNAHVVLEEAPAaaPAAAAAARPPQLLVLSAKTEEALRALAARLAAFLEAHPDLDLADVAY 479

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  488 TLQVGRARFPYRRALTCRTLAEAMER---LEAPEPRPPEPLAHEGERPPLVMLFPGQGTPLVGTARALHESEPTFRQAVE 564
Cdd:COG3321  480 TLATGRAHFEHRLAVVASSREELAAKlraLAAGEAAPGVVTGAAAAAPKVAFLFPGQGSQYVGMGRELYETEPVFRAALD 559

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  565 QCARLLRQTLGLDVREVLFPsaeqEEQARRLaAQTRVAQPALFTLEYALAQTWLGWGLQPQALAGHSLGELVAACLAGVF 644
Cdd:COG3321  560 ECDALLRPHLGWSLREVLFP----DEEESRL-DRTEVAQPALFAVEYALARLWRSWGVRPDAVIGHSVGEYAAACVAGVL 634

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  645 SLEDALQLVAARGQLMQGCPP-GAMLAVPLPEAELAALLGS--ELCIAAVNGPRACVASGPLPAVEALTAALESRGVSSR 721
Cdd:COG3321  635 SLEDALRLVAARGRLMQALPGgGAMLAVGLSEEEVEALLAGydGVSIAAVNGPRSTVVSGPAEAVEALAARLEARGIRAR 714

                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  722 RLETSHAFHSASMEACQGPLTTLLRRMRLQAPRLPCVSGLTGRWLTGEEATePTYWARQLREPVRFSEALETLWSLKEPV 801
Cdd:COG3321  715 RLPVSHAFHSPLMEPALEEFRAALAGVTPRAPRIPLISNVTGTWLTGEALD-ADYWVRHLRQPVRFADAVEALLADGVRV 793

                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  802 LLEVGPGTTLTALARRHPTRPARTQEVASLPvQPDTAVPCIEEAVGELWQAGLELDWSALHA-APRHRAHLPPYPFERQR 880
Cdd:COG3321  794 FLEVGPGPVLTGLVRQCLAAAGDAVVLPSLR-RGEDELAQLLTALAQLWVAGVPVDWSALYPgRGRRRVPLPTYPFQRED 872

                        890       900       910       920       930       940       950       960
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  881 YWIEPEAAPQPRAQQPTPASLVPPEQPSREALEDWFYVPTWEQAPATSGGGQPLAGPVLAFMDSSGLAEQVLAALWPADS 960
Cdd:COG3321  873 AAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAAAALLALAAAAAAA 952

                        970       980       990      1000      1010      1020      1030      1040
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  961 GALLTRVEPAGHyeqlsehafrlrPESEEDWDALFQALQSQGRLPRRILHAWALTAEPGPCTPDGEAVLEQGFFSLLRLA 1040
Cdd:COG3321  953 AAALAAAEAGAL------------LLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAA 1020

                       1050      1060      1070      1080      1090      1100      1110      1120
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1041 RALGRHAPERPVQLEVLSSFVHAVGPREPLEPLKATLLGACAVLPLEYPHVQCRTIDVRPGSEPREVLVRSLAAELAAPM 1120
Cdd:COG3321 1021 LLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALALA 1100

                       1130      1140      1150      1160      1170      1180      1190      1200
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1121 GESPVAWRDGQRYVRRATRQRLEASRPLRSLRERGVylvaggLGGIGLVLARALAQRARARLALLTHSPFPPREQWEQWL 1200
Cdd:COG3321 1101 ALAAALLLLALLAALALAAAAAALLALAALLAAAAA------AAALAAAAAAAAALALAAAAAALAAALAAALLAAAALL 1174

                       1210      1220      1230      1240      1250      1260      1270      1280
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1201 EEAPAHPEPAWRSEADPSERRRTQHRIRCLLELEQLGAEVQVYTADVAEEAAVRSVVEQVHARWGKIHGVLHAAATFDDG 1280
Cdd:COG3321 1175 LALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAA 1254

                       1290      1300      1310      1320      1330      1340      1350      1360
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1281 VIQLRTHEQSSRALRTKVRGSMVLHEVLASEGLDWFALCSSLASALGSFGQADYCAANAFQDAYAHHLRRQGFTGALALD 1360
Cdd:COG3321 1255 LLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAALA 1334

                       1370      1380
                 ....*....|....*....|..
gi 53747904 1361 WGTWRDTGAAMRLVARTRRGGH 1382
Cdd:COG3321 1335 AAVAAALALAAAAAAAAAAAAA 1356
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
 2172-3503 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: 731.27  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2172 PDPAARFEPFPLTDVQEAYWVGRRSAFELGGVAAHGYFEIESPGLEVERFIQCWRQLLQRHDMLRMVVLPDGRQQVLEQV 2251
Cdd:COG1020   14 AAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRPVQVIQPVVAAP 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2252 PEYTPEVVELRGLSPQEAESRRLQLRERMAHQVLRSD-RWPLFELVLCRYEGGVRIHMSMDALMLDAWSSAVLRQDFAQL 2330
Cdd:COG1020   94 LPVVVLLVDLEALAEAAAEAAAAAEALAPFDLLRGPLlRLLLLLLLLLLLLLLLALHHIISDGLSDGLLLAELLRLYLAA 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2331 YHEPGRPLEPLAITFRDYVLAERRLREGEAHERARAYWWARLDTLPPPPELPLVKEPSQLEHARFTHREARLEPHRWARL 2410
Cdd:COG1020  174 YAGAPLPLPPLPIQYADYALWQREWLQGEELARQLAYWRQQLAGLPPLLELPTDRPRPAVQSYRGARVSFRLPAELTAAL 253

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2411 QERARAHGLTPSAACMAAFAEVLARWSRHPRFTLNLTLFQRLplHPQVDELVGDFTSLVLLEVEAHAASTFAERASRLQA 2490
Cdd:COG1020  254 RALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRP--RPELEGLVGFFVNTLPLRVDLSGDPSFAELLARVRE 331

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2491 QLWRDLEHGSVSAVQLIREL--VRTGRRSPgaimpvVFTSILSLDARRGPQGSLSFFEGELVYSISQTPQVWLDHGVHEE 2568
Cdd:COG1020  332 TLLAAYAHQDLPFERLVEELqpERDLSRNP------LFQVMFVLQNAPADELELPGLTLEPLELDSGTAKFDLTLTVVET 405

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2569 EGALVLAWDSVEALFPPGMVDDMFHAYQRLLGALAEEEQAWEGELPELLPPAQRELLARYNATQAPRPSGR-LEEGFFTQ 2647
Cdd:COG1020  406 GDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQLLAEWNATAAPYPADAtLHELFEAQ 485

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2648 ARLHPELPALLAPERTLSYGELARRAQALAARLRELEVQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLDPEQPPLRL 2727
Cdd:COG1020  486 AARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERL 565

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2728 HQLLEEGPARVVLTQSSLLHTVPwPPGVQVIAVDELEPATEAPPLPPRG-TPEHLAYVIYTSGSTGKPKGVAIEHRAALN 2806
Cdd:COG1020  566 AYMLEDAGARLVLTQSALAARLP-ELGVPVLALDALALAAEPATNPPVPvTPDDLAYVIYTSGSTGRPKGVMVEHRALVN 644

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2807 TVVDLNTRFGVGPEDRVLGLSALTFDLSVYDVLGLLGAGGALVLPAAEAEKDPAHWWERLVAGRVTVWNSTPALMLLLVE 2886
Cdd:COG1020  645 LLAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLLRALLD 724

                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2887 YAEQRglklPAALRLVMLSGDWIPVALPDRIRALGRDVQVVSLGGATEASIWSIAYPIGQVAPQWKSIPYGMPLANQRFH 2966
Cdd:COG1020  725 AAPEA----LPSLRLVLVGGEALPPELVRRWRARLPGARLVNLYGPTETTVDSTYYEVTPPDADGGSVPIGRPIANTRVY 800

                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2967 VLDGRLEARPWWVPGELYIGGEGLAREYWRDEPLTATRFIRHP--RTGERLYRTGDQGRMLPEGSIEFLGREDLQVKVQG 3044
Cdd:COG1020  801 VLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPfgFPGARLYRTGDLARWLPDGNLEFLGRADDQVKIRG 880

                        890       900       910       920       930       940       950       960
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3045 FRVELGEIEAALAQHPALSASVVVARGEPRGVRRLVAYAVPRSGQTPAAGELRRYLAERLPAYMVPSAFVLLESLPRSRN 3124
Cdd:COG1020  881 FRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGN 960

                        970       980       990      1000      1010      1020      1030      1040
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3125 GKIARDQLPEPQQTQGLAAQAAAADPLVERLAALVkEALRLERVEPQDSLLDLGADSVALIRLINRLEAELQFRPRLADI 3204
Cdd:COG1020  961 GKLDRLALPAPAAAAAAAAAAPPAEEEEEEAALAL-LLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLL 1039

                       1050      1060      1070      1080      1090      1100      1110      1120
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3205 YENPTVQGLATLHQEKTKSQGEGGAPRLTAPRSTLLPAEEWGRFKANRPGLRRFPDGTPEVALPGSGLAPAPEELTALER 3284
Cdd:COG1020 1040 FLAAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLALLL 1119

                       1130      1140      1150      1160      1170      1180      1190      1200
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3285 RRSVRTYSLEPVSHEQLGRLLAPLREWEVQGSRRYLYASAGGLYPVQLYLHLKPGRARGLEPGTWYYDPSTHRLVLLSAG 3364
Cdd:COG1020 1120 ALLAALRARRAVRQEGPRLRLLVALAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLLLLLLLLL 1199

                       1210      1220      1230      1240      1250      1260      1270      1280
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3365 AGLDRRIHDPHQNQAIFDSAAFSLFLIARMGAVEPVYAEHALHFATLEAGLMTQLLDLGAAPsglglchigDLDFAQARG 3444
Cdd:COG1020 1200 LLLLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALLA---------LALALLALA 1270

                       1290      1300      1310      1320      1330
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 53747904 3445 LFHLEEEHVLLHSLVGGVLPTRGQEAASVPAEGGTEARQLAQLLQQVKTLTPEAARALL 3503
Cdd:COG1020 1271 LLLLALALLLPALARARAARTARALALLLLLALLLLLALALALLLLLLLLLALLLLALL 1329
PKS_ER smart00829
Enoylreductase; Enoylreductase in Polyketide synthases.
 1703-1988 6.80e-106

Enoylreductase; Enoylreductase in Polyketide synthases.


:

Pssm-ID: 214840 [Multi-domain]  Cd Length: 287  Bit Score: 340.90  E-value: 6.80e-106
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904    1703 IEVEAAGLNFLDVLGALGMMPaleaEESVLGRECSGRIAAVGEGVSGLRVGDEVLAVAPGCFRSYVLVDESQVVRRPASL 1782
Cdd:smart00829    1 IEVRAAGLNFRDVLIALGLYP----GEAVLGGECAGVVTRVGPGVTGLAVGDRVMGLAPGAFATRVVTDARLVVPIPDGW 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904    1783 GLAEGAAQMVPFATAYFALHTVGRLRRGERILIHAAAGGLGLAAVQLASRTGAEILATAGSEQKREYLRSLGI--AHVLD 1860
Cdd:smart00829   77 SFEEAATVPVVFLTAYYALVDLARLRPGESVLIHAAAGGVGQAAIQLARHLGAEVFATAGSPEKRDFLRALGIpdDHIFS 156

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904    1861 SRSTSFVSEVRERTGGRGVDVVLNSLAGELLLAGLSVLAPHGRFLELGKRDLYADQQVGLRTLARGQTFAAIDFGP--HH 1938
Cdd:smart00829  157 SRDLSFADEILRATGGRGVDVVLNSLSGEFLDASLRCLAPGGRFVEIGKRDIRDNSQLAMAPFRPNVSYHAVDLDAleEG 236

                           250       260       270       280       290
                    ....*....|....*....|....*....|....*....|....*....|.
gi 53747904    1939 PD-FRAVLEEVATQLTQGQLEPLPTRLFPARQVAEAFSFMARALHIGRVAV 1988
Cdd:smart00829  237 PDrIRELLAEVLELFAEGVLRPLPVTVFPISDAEDAFRYMQQGKHIGKVVL 287
hot_dog super family cl00509
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 1410-1659 2.58e-28

The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl carrier protein (ACP)-dehydratase) structure and subsequently in 4HBT (4-hydroxybenzoyl-CoA thioesterase) from Pseudomonas. A number of other seemingly unrelated proteins also share the hotdog fold. These proteins have related, but distinct, catalytic activities that include metabolic roles such as thioester hydrolysis in fatty acid metabolism, and degradation of phenylacetic acid and the environmental pollutant 4-chlorobenzoate. This superfamily also includes the PaaI-like protein FapR, a non-catalytic bacterial homolog involved in transcriptional regulation of fatty acid biosynthesis.


The actual alignment was detected with superfamily member pfam14765:

Pssm-ID: 469797  Cd Length: 296  Bit Score: 117.86  E-value: 2.58e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   1410 TLRGGEDWVVDEHRLQGVPTLPGVAYLELARAACAQALGAEAVELAELLL-LEPLTVPRGESRQVRVVLQPEGQAHALRV 1488
Cdd:pfam14765   21 RLRLADLPWLRDHRVGGTVVLPGAGYLEMALEAARQLFGGSGAVALRDVSiLKALVLPEDDPVEVQTSLTPEEDGADSWW 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   1489 E----SRSEEARGWNEHARGRVRAVPRL-AERIQPELLRAACehEQPVPGEPQEQGPVHAGARWHGL-----FQWVR--- 1555
Cdd:pfam14765  101 EfeifSRAGGGWEWTLHATGTVRLAPGEpAAPVDLESLPARC--AQPADPRSVSSAEFYERLAARGLfygpaFQGLRriw 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   1556 RGPRQALAQLALPEPFHGDLERFELHPALMDMA--------TSFAIPGGVPWLAFGYERVLIHGPLPPQ--VLSHVSLPE 1625
Cdd:pfam14765  179 RGDGEALAEARLPEAAAGGESPYLLHPALLDAAlqllgaalPAEAEHADQAYLPVGIERLRIYRSLPPGepLWVHARLER 258

                          250       260       270
                   ....*....|....*....|....*....|....
gi 53747904   1626 EsqaGAQQLRLQVRLLDLEGWERVRIDGYLLRPL 1659
Cdd:pfam14765  259 R---GGRTIVGDLTLVDEDGRVVARIEGLRLRRV 289
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
 2083-2145 1.21e-11

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: 62.95  E-value: 1.21e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 53747904 2083 PPSSLEQLIEQVWRKHLGV--ERVQPTDSFFQ-LGGDSLLGIQVAADLRRHLGVELPTATLFSHPT 2145
Cdd:COG0236    2 PREELEERLAEIIAEVLGVdpEEITPDDSFFEdLGLDSLDAVELIAALEEEFGIELPDTELFEYPT 67
 
Name Accession Description Interval E-value
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
 13-1382 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: 1087.21  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   13 IALVGMAGRFPGAPDVESFWRNLVAGVESISFFSEEELRQAG--VSEQIRRRPEYVPAKGVLEDLELFDAGFFGYSPREA 90
Cdd:COG3321    6 IAIIGMACRFPGADDPEEFWRNLRAGRDAITEVPADRWDADAyyDPDPDAPGKTYVRWGGFLDDVDEFDALFFGISPREA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   91 SHLDPQQRLLLECSWEALEDAGLRPDQLPGW-VGVYVGAGDTSYrFQLLRGHGDPLSGSkdvaGFFGNYPDFLATRVAYK 169
Cdd:COG3321   86 EAMDPQQRLLLEVAWEALEDAGYDPESLAGSrTGVFVGASSNDY-ALLLLADPEAIDAY----ALTGNAKSVLAGRISYK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  170 LNLRGPALGIHTACSTSLVSINMACSALRGFECDMALAGGVSLRLPARSGYLYEEGGVASKDGHCRPFDARAtgtvtgdg 249
Cdd:COG3321  161 LDLRGPSVTVDTACSSSLVAVHLACQSLRSGECDLALAGGVNLMLTPESFILFSKGGMLSPDGRCRAFDADAdgyvrgeg 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  250 vgvvvLKRLEDALKARDPIHAVIRGWALNNDGASRaGFTAPSVEGQSEVIALAHAAAGISARDITYVEAHGTGTPLGDPI 329
Cdd:COG3321  241 vgvvvLKRLSDALRDGDRIYAVIRGSAVNQDGRSN-GLTAPNGPAQAAVIRRALADAGVDPATVDYVEAHGTGTPLGDPI 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  330 EVAALTRAFRAHTADTAFCTLGAVKSNIGHLDAAAGVAGVIKTVQALRHRLIPPTLHFERPNPALHLEQSPFFVNTQPLP 409
Cdd:COG3321  320 EAAALTAAFGQGRPADQPCAIGSVKSNIGHLEAAAGVAGLIKAVLALRHGVLPPTLHFETPNPHIDFENSPFYVNTELRP 399

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  410 WESPRGPRLAGVSSFGIGGTNAHTLFEEAPP--PPASGPTRPNQVLLLSARSTSALEHIAGRLAAHLRRHPDLELADVAF 487
Cdd:COG3321  400 WPAGGGPRRAGVSSFGFGGTNAHVVLEEAPAaaPAAAAAARPPQLLVLSAKTEEALRALAARLAAFLEAHPDLDLADVAY 479

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  488 TLQVGRARFPYRRALTCRTLAEAMER---LEAPEPRPPEPLAHEGERPPLVMLFPGQGTPLVGTARALHESEPTFRQAVE 564
Cdd:COG3321  480 TLATGRAHFEHRLAVVASSREELAAKlraLAAGEAAPGVVTGAAAAAPKVAFLFPGQGSQYVGMGRELYETEPVFRAALD 559

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  565 QCARLLRQTLGLDVREVLFPsaeqEEQARRLaAQTRVAQPALFTLEYALAQTWLGWGLQPQALAGHSLGELVAACLAGVF 644
Cdd:COG3321  560 ECDALLRPHLGWSLREVLFP----DEEESRL-DRTEVAQPALFAVEYALARLWRSWGVRPDAVIGHSVGEYAAACVAGVL 634

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  645 SLEDALQLVAARGQLMQGCPP-GAMLAVPLPEAELAALLGS--ELCIAAVNGPRACVASGPLPAVEALTAALESRGVSSR 721
Cdd:COG3321  635 SLEDALRLVAARGRLMQALPGgGAMLAVGLSEEEVEALLAGydGVSIAAVNGPRSTVVSGPAEAVEALAARLEARGIRAR 714

                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  722 RLETSHAFHSASMEACQGPLTTLLRRMRLQAPRLPCVSGLTGRWLTGEEATePTYWARQLREPVRFSEALETLWSLKEPV 801
Cdd:COG3321  715 RLPVSHAFHSPLMEPALEEFRAALAGVTPRAPRIPLISNVTGTWLTGEALD-ADYWVRHLRQPVRFADAVEALLADGVRV 793

                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  802 LLEVGPGTTLTALARRHPTRPARTQEVASLPvQPDTAVPCIEEAVGELWQAGLELDWSALHA-APRHRAHLPPYPFERQR 880
Cdd:COG3321  794 FLEVGPGPVLTGLVRQCLAAAGDAVVLPSLR-RGEDELAQLLTALAQLWVAGVPVDWSALYPgRGRRRVPLPTYPFQRED 872

                        890       900       910       920       930       940       950       960
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  881 YWIEPEAAPQPRAQQPTPASLVPPEQPSREALEDWFYVPTWEQAPATSGGGQPLAGPVLAFMDSSGLAEQVLAALWPADS 960
Cdd:COG3321  873 AAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAAAALLALAAAAAAA 952

                        970       980       990      1000      1010      1020      1030      1040
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  961 GALLTRVEPAGHyeqlsehafrlrPESEEDWDALFQALQSQGRLPRRILHAWALTAEPGPCTPDGEAVLEQGFFSLLRLA 1040
Cdd:COG3321  953 AAALAAAEAGAL------------LLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAA 1020

                       1050      1060      1070      1080      1090      1100      1110      1120
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1041 RALGRHAPERPVQLEVLSSFVHAVGPREPLEPLKATLLGACAVLPLEYPHVQCRTIDVRPGSEPREVLVRSLAAELAAPM 1120
Cdd:COG3321 1021 LLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALALA 1100

                       1130      1140      1150      1160      1170      1180      1190      1200
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1121 GESPVAWRDGQRYVRRATRQRLEASRPLRSLRERGVylvaggLGGIGLVLARALAQRARARLALLTHSPFPPREQWEQWL 1200
Cdd:COG3321 1101 ALAAALLLLALLAALALAAAAAALLALAALLAAAAA------AAALAAAAAAAAALALAAAAAALAAALAAALLAAAALL 1174

                       1210      1220      1230      1240      1250      1260      1270      1280
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1201 EEAPAHPEPAWRSEADPSERRRTQHRIRCLLELEQLGAEVQVYTADVAEEAAVRSVVEQVHARWGKIHGVLHAAATFDDG 1280
Cdd:COG3321 1175 LALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAA 1254

                       1290      1300      1310      1320      1330      1340      1350      1360
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1281 VIQLRTHEQSSRALRTKVRGSMVLHEVLASEGLDWFALCSSLASALGSFGQADYCAANAFQDAYAHHLRRQGFTGALALD 1360
Cdd:COG3321 1255 LLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAALA 1334

                       1370      1380
                 ....*....|....*....|..
gi 53747904 1361 WGTWRDTGAAMRLVARTRRGGH 1382
Cdd:COG3321 1335 AAVAAALALAAAAAAAAAAAAA 1356
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
 2172-3503 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: 731.27  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2172 PDPAARFEPFPLTDVQEAYWVGRRSAFELGGVAAHGYFEIESPGLEVERFIQCWRQLLQRHDMLRMVVLPDGRQQVLEQV 2251
Cdd:COG1020   14 AAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRPVQVIQPVVAAP 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2252 PEYTPEVVELRGLSPQEAESRRLQLRERMAHQVLRSD-RWPLFELVLCRYEGGVRIHMSMDALMLDAWSSAVLRQDFAQL 2330
Cdd:COG1020   94 LPVVVLLVDLEALAEAAAEAAAAAEALAPFDLLRGPLlRLLLLLLLLLLLLLLLALHHIISDGLSDGLLLAELLRLYLAA 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2331 YHEPGRPLEPLAITFRDYVLAERRLREGEAHERARAYWWARLDTLPPPPELPLVKEPSQLEHARFTHREARLEPHRWARL 2410
Cdd:COG1020  174 YAGAPLPLPPLPIQYADYALWQREWLQGEELARQLAYWRQQLAGLPPLLELPTDRPRPAVQSYRGARVSFRLPAELTAAL 253

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2411 QERARAHGLTPSAACMAAFAEVLARWSRHPRFTLNLTLFQRLplHPQVDELVGDFTSLVLLEVEAHAASTFAERASRLQA 2490
Cdd:COG1020  254 RALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRP--RPELEGLVGFFVNTLPLRVDLSGDPSFAELLARVRE 331

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2491 QLWRDLEHGSVSAVQLIREL--VRTGRRSPgaimpvVFTSILSLDARRGPQGSLSFFEGELVYSISQTPQVWLDHGVHEE 2568
Cdd:COG1020  332 TLLAAYAHQDLPFERLVEELqpERDLSRNP------LFQVMFVLQNAPADELELPGLTLEPLELDSGTAKFDLTLTVVET 405

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2569 EGALVLAWDSVEALFPPGMVDDMFHAYQRLLGALAEEEQAWEGELPELLPPAQRELLARYNATQAPRPSGR-LEEGFFTQ 2647
Cdd:COG1020  406 GDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQLLAEWNATAAPYPADAtLHELFEAQ 485

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2648 ARLHPELPALLAPERTLSYGELARRAQALAARLRELEVQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLDPEQPPLRL 2727
Cdd:COG1020  486 AARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERL 565

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2728 HQLLEEGPARVVLTQSSLLHTVPwPPGVQVIAVDELEPATEAPPLPPRG-TPEHLAYVIYTSGSTGKPKGVAIEHRAALN 2806
Cdd:COG1020  566 AYMLEDAGARLVLTQSALAARLP-ELGVPVLALDALALAAEPATNPPVPvTPDDLAYVIYTSGSTGRPKGVMVEHRALVN 644

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2807 TVVDLNTRFGVGPEDRVLGLSALTFDLSVYDVLGLLGAGGALVLPAAEAEKDPAHWWERLVAGRVTVWNSTPALMLLLVE 2886
Cdd:COG1020  645 LLAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLLRALLD 724

                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2887 YAEQRglklPAALRLVMLSGDWIPVALPDRIRALGRDVQVVSLGGATEASIWSIAYPIGQVAPQWKSIPYGMPLANQRFH 2966
Cdd:COG1020  725 AAPEA----LPSLRLVLVGGEALPPELVRRWRARLPGARLVNLYGPTETTVDSTYYEVTPPDADGGSVPIGRPIANTRVY 800

                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2967 VLDGRLEARPWWVPGELYIGGEGLAREYWRDEPLTATRFIRHP--RTGERLYRTGDQGRMLPEGSIEFLGREDLQVKVQG 3044
Cdd:COG1020  801 VLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPfgFPGARLYRTGDLARWLPDGNLEFLGRADDQVKIRG 880

                        890       900       910       920       930       940       950       960
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3045 FRVELGEIEAALAQHPALSASVVVARGEPRGVRRLVAYAVPRSGQTPAAGELRRYLAERLPAYMVPSAFVLLESLPRSRN 3124
Cdd:COG1020  881 FRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGN 960

                        970       980       990      1000      1010      1020      1030      1040
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3125 GKIARDQLPEPQQTQGLAAQAAAADPLVERLAALVkEALRLERVEPQDSLLDLGADSVALIRLINRLEAELQFRPRLADI 3204
Cdd:COG1020  961 GKLDRLALPAPAAAAAAAAAAPPAEEEEEEAALAL-LLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLL 1039

                       1050      1060      1070      1080      1090      1100      1110      1120
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3205 YENPTVQGLATLHQEKTKSQGEGGAPRLTAPRSTLLPAEEWGRFKANRPGLRRFPDGTPEVALPGSGLAPAPEELTALER 3284
Cdd:COG1020 1040 FLAAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLALLL 1119

                       1130      1140      1150      1160      1170      1180      1190      1200
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3285 RRSVRTYSLEPVSHEQLGRLLAPLREWEVQGSRRYLYASAGGLYPVQLYLHLKPGRARGLEPGTWYYDPSTHRLVLLSAG 3364
Cdd:COG1020 1120 ALLAALRARRAVRQEGPRLRLLVALAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLLLLLLLLL 1199

                       1210      1220      1230      1240      1250      1260      1270      1280
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3365 AGLDRRIHDPHQNQAIFDSAAFSLFLIARMGAVEPVYAEHALHFATLEAGLMTQLLDLGAAPsglglchigDLDFAQARG 3444
Cdd:COG1020 1200 LLLLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALLA---------LALALLALA 1270

                       1290      1300      1310      1320      1330
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 53747904 3445 LFHLEEEHVLLHSLVGGVLPTRGQEAASVPAEGGTEARQLAQLLQQVKTLTPEAARALL 3503
Cdd:COG1020 1271 LLLLALALLLPALARARAARTARALALLLLLALLLLLALALALLLLLLLLLALLLLALL 1329
Cyc_NRPS cd19535
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
 2180-2606 0e+00

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: 602.56  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2180 PFPLTDVQEAYWVGRRSAFELGGVAAHGYFEIESPGLEVERFIQCWRQLLQRHDMLRMVVLPDGRQQVLEQVPEYTPEVV 2259
Cdd:cd19535    1 PFPLTDVQYAYWIGRQDDQELGGVGCHAYLEFDGEDLDPDRLERAWNKLIARHPMLRAVFLDDGTQQILPEVPWYGITVH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2260 ELRGLSPQEAESRRLQLRERMAHQVLRSDRWPLFELVLCRY-EGGVRIHMSMDALMLDAWSSAVLRQDFAQLYHEPGRPL 2338
Cdd:cd19535   81 DLRGLSEEEAEAALEELRERLSHRVLDVERGPLFDIRLSLLpEGRTRLHLSIDLLVADALSLQILLRELAALYEDPGEPL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2339 EPLAITFRDYVLAERRLREgEAHERARAYWWARLDTLPPPPELPLVKEPSQLEHARFTHREARLEPHRWARLQERARAHG 2418
Cdd:cd19535  161 PPLELSFRDYLLAEQALRE-TAYERARAYWQERLPTLPPAPQLPLAKDPEEIKEPRFTRREHRLSAEQWQRLKERARQHG 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2419 LTPSAACMAAFAEVLARWSRHPRFTLNLTLFQRLPLHPQVDELVGDFTSLVLLEVEAHAASTFAERASRLQAQLWRDLEH 2498
Cdd:cd19535  240 VTPSMVLLTAYAEVLARWSGQPRFLLNLTLFNRLPLHPDVNDVVGDFTSLLLLEVDGSEGQSFLERARRLQQQLWEDLDH 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2499 GSVSAVQLIRELVRTgRRSPGAIMPVVFTSILSLDArrGPQGSLSFFeGELVYSISQTPQVWLDHGVHEEEGALVLAWDS 2578
Cdd:cd19535  320 SSYSGVVVVRRLLRR-RGGQPVLAPVVFTSNLGLPL--LDEEVREVL-GELVYMISQTPQVWLDHQVYEEDGGLLLNWDA 395

                        410       420
                 ....*....|....*....|....*...
gi 53747904 2579 VEALFPPGMVDDMFHAYQRLLGALAEEE 2606
Cdd:cd19535  396 VDELFPEGMLDDMFDAYVRLLERLADDD 423
PKS cd00833
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ...
 13-432 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: 570.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   13 IALVGMAGRFPGAPDVESFWRNLVAGVESISFFSEEELRQAGVSEQIRRR-PEYVPAKGVLEDLELFDAGFFGYSPREAS 91
Cdd:cd00833    3 IAIVGMACRFPGAADPDEFWENLLEGRDAISEIPEDRWDADGYYPDPGKPgKTYTRRGGFLDDVDAFDAAFFGISPREAE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   92 HLDPQQRLLLECSWEALEDAGLRPDQLPGW-VGVYVGAGDTSYRFQLLRGHGDPlsgskDVAGFFGNYPDFLATRVAYKL 170
Cdd:cd00833   83 AMDPQQRLLLEVAWEALEDAGYSPESLAGSrTGVFVGASSSDYLELLARDPDEI-----DAYAATGTSRAFLANRISYFF 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  171 NLRGPALGIHTACSTSLVSINMACSALRGFECDMALAGGVSLRLPARSGYLYEEGGVASKDGHCRPFDARATGTVTGDGV 250
Cdd:cd00833  158 DLRGPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLSPDGRCRPFDADADGYVRGEGV 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  251 GVVVLKRLEDALKARDPIHAVIRGWALNNDGASRAGfTAPSVEGQSEVIALAHAAAGISARDITYVEAHGTGTPLGDPIE 330
Cdd:cd00833  238 GVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRTKGI-TAPSGEAQAALIRRAYARAGVDPSDIDYVEAHGTGTPLGDPIE 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  331 VAALTRAFRAHTADTAFCTLGAVKSNIGHLDAAAGVAGVIKTVQALRHRLIPPTLHFERPNPALHLEQSPFFVNTQPLPW 410
Cdd:cd00833  317 VEALAKVFGGSRSADQPLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKIDFEESPLRVPTEARPW 396

                        410       420
                 ....*....|....*....|..
gi 53747904  411 ESPRGPRLAGVSSFGIGGTNAH 432
Cdd:cd00833  397 PAPAGPRRAGVSSFGFGGTNAH 418
PRK12467 PRK12467
peptide synthase; Provisional
 2083-3219 1.83e-139

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 493.52  E-value: 1.83e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2083 PPSSLEQLIEQVWRKHLGVERVQPTDSFFQLGGDSLLGIQVAADLRRHLGVELPTATLFSHPTLAALAAALRARQGEAAA 2162
Cdd:PRK12467 1027 PQTELEKRLAAIWADVLKVERVGLTDNFFELGGHSLLATQVISRVRQRLGIQVPLRTLFEHQTLAGFAQAVAAQQQGAQP 1106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2163 PTApapalvpdPAARFEPFPLTDVQEAYWVGRRsaFELGGVAAHGYFEIESPG-LEVERFIQCWRQLLQRHDMLRMV-VL 2240
Cdd:PRK12467 1107 ALP--------DVDRDQPLPLSYAQERQWFLWQ--LEPGSAAYHIPQALRLKGpLDIEALERSFDALVARHESLRTTfVQ 1176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2241 PDGR-QQVLEQVPEYTPEVVELRGLSPQEAESRrlQLRERMAHQVLRSDRWPLFELVLCRY--EGGVRIhMSMDALMLDA 2317
Cdd:PRK12467 1177 EDGRtRQVIHPVGSLTLEEPLLLAADKDEAQLK--VYVEAEARQPFDLEQGPLLRVGLLRLaaDEHVLV-LTLHHIVSDG 1253

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2318 WSSAVLRQDFAQLY--HEPGRPLE--PLAITFRDYVLAERRLREGEAHERARAYWWARLDTlppppelplvkEPSQLE-- 2391
Cdd:PRK12467 1254 WSMQVLVDELVALYaaYSQGQSLQlpALPIQYADYAVWQRQWMDAGERARQLAYWKAQLGG-----------EQPVLElp 1322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2392 -----HARFTHREAR----LEPHRWARLQERARAHGLTPSAACMAAFAEVLARWSRHPRFTLNLTLFQRLPLhpQVDELV 2462
Cdd:PRK12467 1323 tdrprPAVQSHRGARlafeLPPALAEGLRALARREGVTLFMLLLASFQTLLHRYSGQDDIRVGVPIANRNRA--ETEGLI 1400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2463 GDFTSLVLLEVEAHAASTFAE-----RASRLQAQLWRDLEHGS-VSAVQLIRELvrtgrrSPGAIMPVVFtsilslDARR 2536
Cdd:PRK12467 1401 GFFVNTQVLRAEVDGQASFQQllqqvKQAALEAQAHQDLPFEQlVEALQPERSL------SHSPLFQVMF------NHQR 1468

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2537 GPQGSLSFFEGELVYSIS---QTPQVWLDHGVHEEEGALVLAWDSVEALFPPGMVDDMFHAYQRLLGALAEEEQAWEGEL 2613
Cdd:PRK12467 1469 DDHQAQAQLPGLSVESLSwesQTAQFDLTLDTYESSEGLQASLTYATDLFEASTIERLAGHWLNLLQGLVADPERRLGEL 1548

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2614 PELLPPAQRELLARYNATQAPRPSGRLEEGFFT-QARLHPELPALLAPERTLSYGELARRAQALAARLRELEVQPQELVA 2692
Cdd:PRK12467 1549 DLLDEAERRQILEGWNATHTGYPLARLVHQLIEdQAAATPEAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVG 1628

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2693 IAMHKGWEQATAVLGVLQAAAAYLPLDPEQPPLRLHQLLEEGPARVVLTQSSLLHTVPWPPGVQVIAVDELEPATEA-PP 2771
Cdd:PRK12467 1629 IAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQSHLQARLPLPDGLRSLVLDQEDDWLEGySD 1708

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2772 LPP--RGTPEHLAYVIYTSGSTGKPKGVAIEHRAALNTVVDLNTRFGVGPEDRVLGLSALTFDLSVYDVLGLLGAGGALV 2849
Cdd:PRK12467 1709 SNPavNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFAFDVSVWELFWPLINGARLV 1788

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2850 LPAAEAEKDPAHWWERLVAGRVTVWNSTPALMLLLVEYAEQRGlkLPAALRLVMLSGDWIPVALPDRIRALGRDVQVVSL 2929
Cdd:PRK12467 1789 IAPPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQMDEQVE--HPLSLRRVVCGGEALEVEALRPWLERLPDTGLFNL 1866

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2930 GGATEASIWSIAYPIGQVAPQWK-SIPYGMPLANQRFHVLDGRLEARPWWVPGELYIGGEGLAREYWRDEPLTATRFIRH 3008
Cdd:PRK12467 1867 YGPTETAVDVTHWTCRRKDLEGRdSVPIGQPIANLSTYILDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFVAD 1946

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  3009 P--RTGERLYRTGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPALSASVVVARgEPRGVRRLVAYAVPR 3086
Cdd:PRK12467 1947 PfgTVGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQ-DGANGKQLVAYVVPT 2025

                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  3087 SGQTPAA--------GELRRYLAERLPAYMVPSAFVLLESLPRSRNGKIARDQLPEPQQTQGLAAQAAAADPLVERLAAL 3158
Cdd:PRK12467 2026 DPGLVDDdeaqvalrAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKALPAPDASELQQAYVAPQSELEQRLAAI 2105

                        1130      1140      1150      1160      1170      1180
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 53747904  3159 VKEALRLERVEPQDSLLDLGADSVALIRLINRL-EAELQFRPRlaDIYENPTVQGLATLHQE 3219
Cdd:PRK12467 2106 WQDVLGLEQVGLHDNFFELGGDSIISIQVVSRArQAGIRFTPK--DLFQHQTVQSLAAVAQE 2165
PKS_KS smart00825
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ...
 13-437 2.93e-133

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: 419.81  E-value: 2.93e-133
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904      13 IALVGMAGRFPGAPDVESFWRNLVAGvesisffseeelrqagvseqirrrpeyvpakgvLEDLELFDAGFFGYSPREASH 92
Cdd:smart00825    1 IAIVGMSCRFPGADDPEEFWDLLLAG---------------------------------LDDVDLFDAAFFGISPREAEA 47

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904      93 LDPQQRLLLECSWEALEDAGLRPDQLPGW-VGVYVGAGDTSYrfqllrghgdplsgskdvagffgnypdflatrvaykln 171
Cdd:smart00825   48 MDPQQRLLLEVAWEALEDAGIDPESLRGSrTGVFVGVSSSDY-------------------------------------- 89

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904     172 lrgpALGIHTACSTSLVSINMACSALRGFECDMALAGGVSLRLPARSGYLYEEGGVASKDGHCRPFDARAtgtvtgdgvg 251
Cdd:smart00825   90 ----SVTVDTACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLSPDGRCKTFDASAdgyvrgegvg 165

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904     252 vvvLKRLEDALKARDPIHAVIRGWALNNDGASrAGFTAPSVEGQsevialahaaagisardityveahgtgtplgdpiev 331
Cdd:smart00825  166 vvvLKRLSDALRDGDPILAVIRGSAVNQDGRS-NGITAPSGPAQ------------------------------------ 208

                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904     332 aaltrafrahtadtafCTLGAVKSNIGHLDAAAGVAGVIKTVQALRHRLIPPTLHFERPNPALHLEQSPFFVNTQPLPWE 411
Cdd:smart00825  209 ----------------LLIGSVKSNIGHLEAAAGVAGLIKVVLALKHGVIPPTLHFETPNPHIDLEESPLRVPTELTPWP 272

                           410       420
                    ....*....|....*....|....*.
gi 53747904     412 SPRGPRLAGVSSFGIGGTNAHTLFEE 437
Cdd:smart00825  273 PPGRPRRAGVSSFGFGGTNAHVILEE 298
mycolic_Pks13 NF040607
polyketide synthase Pks13;
13-884 8.81e-123

polyketide synthase Pks13;


Pssm-ID: 468580 [Multi-domain]  Cd Length: 1671  Bit Score: 430.88  E-value: 8.81e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904    13 IALVGMAGRFPGA-PDVESFWRNLVAGVESISFFSEEELRQAGVSEQIRRRPEYVPAKG-VLEDLELFDAGFFGYSPREA 90
Cdd:NF040607  102 IAIVGLATRFPGAgNTPEEMWEALIEGRDGITDLPEGRWSEFAADPRIAERVAKANTRGgYLDDIKGFDAEFFALSPLEA 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904    91 SHLDPQQRLLLECSWEALEDAGLRPDQLPGW-VGVYVGAGDTSYrfQLLRGhGDPlsGSKDVAGFFGNYPDFLATRVAYK 169
Cdd:NF040607  182 ENVDPQQRLALELTWEALEHARIPASSLRGEpVGVFIGSSNNDY--QMLAV-ADP--AEAHPYALTGTSSSIIANRVSYF 256

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   170 LNLRGPALGIHTACSTSLVSINMACSALRGFECDMALAGGVSLRL-PARSGYLYEEGGVASKDGHCRPFDARATGTVTGD 248
Cdd:NF040607  257 FDFRGPSVAVDTACSSSLVAVHQAVRALRSGEADVAVAGGVNMLLtPAVTLGFDELGGVLAPDGRIKAFSSDADGMVRSE 336

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   249 GVGVVVLKRLEDALKARDPIHAVIRGWALNNDGASRaGFTAPSVEGQSEVIALAHAAAGISARDITYVEAHGTGTPLGDP 328
Cdd:NF040607  337 GGGVVVLKRLADARRDGDTILAVIAGSAVNSDGRSN-GLTAPNPDAQVDVLRRAYADAGIDPRTVDYVEAHGTGTILGDP 415

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   329 IEVAALTRAF-RAHTADTAfCTLGAVKSNIGHLDAAAGVAGVIKTVQALRHRLIPPTLHFERPNP-----ALHLEqspff 402
Cdd:NF040607  416 IEADALGRVVgRGRDADKP-ALLGSAKTNFGHLESAAGAAGLAKVVLAMQHDKLPPSLNYAGPNPyidfdAEHLK----- 489

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   403 VNTQPLPWesPR--GPRLAGVSSFGIGGTNAHTLFEEAPPPPASGPTRPNQVLLLSARSTSALEhiAGRLAAHLRRHPDL 480
Cdd:NF040607  490 VVDEPTEW--PRysGHAVAGVSGFGFGGTNAHVVVREVLPADLVEPEAQPDEDTEAELAGLTAE--AKRLLAEAELAAEF 565

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   481 ELA---DVAFTLQVGrARFPYRRALTCRTLAEAMErleapeprppeplAHEGERPPL------------------VM--- 536
Cdd:NF040607  566 APAapeGPVVPLPVS-GFLPSRRRAAAADLADWLE-------------SEEGRATPLadvaralarrnhgrsravVLaht 631

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   537 ----------LFPGQGTPLVGTA-----------------------RALHESEPTFRQAVEQCARLLRQTLGLDVREVLF 583
Cdd:NF040607  632 heeaikglraVAEGKPGPGVFSAdapaangpvwvlsgfgsqhrkmaKQLYLENPVFAARIDEVDELVQDESGYSIVELIL 711

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   584 PSAEQEEqarrlaaqTRVAQPALFTLEYALAQTWLGWGLQPQALAGHSLGELVAACLAGVFSLEDALQLVAARGQLM--- 660
Cdd:NF040607  712 DDEQTYD--------IETAQVGIFAIQIALADLLRHHGAKPAAVVGHSMGEAAAAYAAGGLSLEDAVRVICHRSRLMgeg 783

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   661 ----QGCPPGAMLAVPLPEAELAALLGS----ELCIAAvnGPRACVASGPLPAVEALTAALESRGVSSRRLETSHAFHSA 732
Cdd:NF040607  784 eamlPGDDIRLMALVEYSAEEIETVLADfpdlEVCVYA--APTHTVIGGPREQVDAIVARAEAEGKFARKLQTKGASHTS 861

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   733 SMEACQGPLTTLLRRMRLQAPRLPCVS----GLTGRwlTGEEATEPT-YWARQLREPVRFSEALETLWSLKEPVLLEVGP 807
Cdd:NF040607  862 QMDPLLGELAAELAGIEPQPLTVGLYSsvdrGTFYR--PGHEPIHDVdYWVKGLRHSVWFTQAVRKAVDAGHTTFLELAP 939

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   808 ---------GTTLTA----------LARRHPtrpartqEVASLPvqpdtavpcieEAVGELWQAGLELDWSALhAAPRHR 868
Cdd:NF040607  940 npvalmsvaATTFAAglhdaqliptLKRKED-------ESESVL-----------NALAQLYVHGHDVDLRSL-FGAGDY 1000

                         970
                  ....*....|....*.
gi 53747904   869 AHLPPYPFERQRYWIE 884
Cdd:NF040607 1001 ADIPRTRFKRKPYWLD 1016
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
 2685-3067 2.49e-122

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: 393.55  E-value: 2.49e-122
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   2685 VQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLDPEQPPLRLHQLLEEGPARVVLTQSSLLHTVPW-PPGVQVIAVDEL 2763
Cdd:TIGR01733   22 VGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDSALASRLAGlVLPVILLDPLEL 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   2764 EPATEAPPLPPRGT---PEHLAYVIYTSGSTGKPKGVAIEHRAALNTVVDLNTRFGVGPEDRVLGLSALTFDLSVYDVLG 2840
Cdd:TIGR01733  102 AALDDAPAPPPPDApsgPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDPDDRVLQFASLSFDASVEEIFG 181

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   2841 LLGAGGALVLPAAEAEKDPAHWWERLVA-GRVTVWNSTPALMLLLVEYAEQRglklPAALRLVMLSGDWIPVALPDRIRA 2919
Cdd:TIGR01733  182 ALLAGATLVVPPEDEERDDAALLAALIAeHPVTVLNLTPSLLALLAAALPPA----LASLRLVILGGEALTPALVDRWRA 257

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   2920 LGRDVQVVSLGGATEASIWSIAYPI-GQVAPQWKSIPYGMPLANQRFHVLDGRLEARPWWVPGELYIGGEGLAREYWRDE 2998
Cdd:TIGR01733  258 RGPGARLINLYGPTETTVWSTATLVdPDDAPRESPVPIGRPLANTRLYVLDDDLRPVPVGVVGELYIGGPGVARGYLNRP 337

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 53747904   2999 PLTATRFIRHP---RTGERLYRTGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPALSASVV 3067
Cdd:TIGR01733  338 ELTAERFVPDPfagGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
PKS_ER smart00829
Enoylreductase; Enoylreductase in Polyketide synthases.
 1703-1988 6.80e-106

Enoylreductase; Enoylreductase in Polyketide synthases.


Pssm-ID: 214840 [Multi-domain]  Cd Length: 287  Bit Score: 340.90  E-value: 6.80e-106
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904    1703 IEVEAAGLNFLDVLGALGMMPaleaEESVLGRECSGRIAAVGEGVSGLRVGDEVLAVAPGCFRSYVLVDESQVVRRPASL 1782
Cdd:smart00829    1 IEVRAAGLNFRDVLIALGLYP----GEAVLGGECAGVVTRVGPGVTGLAVGDRVMGLAPGAFATRVVTDARLVVPIPDGW 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904    1783 GLAEGAAQMVPFATAYFALHTVGRLRRGERILIHAAAGGLGLAAVQLASRTGAEILATAGSEQKREYLRSLGI--AHVLD 1860
Cdd:smart00829   77 SFEEAATVPVVFLTAYYALVDLARLRPGESVLIHAAAGGVGQAAIQLARHLGAEVFATAGSPEKRDFLRALGIpdDHIFS 156

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904    1861 SRSTSFVSEVRERTGGRGVDVVLNSLAGELLLAGLSVLAPHGRFLELGKRDLYADQQVGLRTLARGQTFAAIDFGP--HH 1938
Cdd:smart00829  157 SRDLSFADEILRATGGRGVDVVLNSLSGEFLDASLRCLAPGGRFVEIGKRDIRDNSQLAMAPFRPNVSYHAVDLDAleEG 236

                           250       260       270       280       290
                    ....*....|....*....|....*....|....*....|....*....|.
gi 53747904    1939 PD-FRAVLEEVATQLTQGQLEPLPTRLFPARQVAEAFSFMARALHIGRVAV 1988
Cdd:smart00829  237 PDrIRELLAEVLELFAEGVLRPLPVTVFPISDAEDAFRYMQQGKHIGKVVL 287
enoyl_red cd05195
enoyl reductase of polyketide synthase; Putative enoyl reductase of polyketide synthase. ...
 1700-1988 7.50e-100

enoyl reductase of polyketide synthase; Putative enoyl reductase of polyketide synthase. Polyketide synthases produce polyketides in step by step mechanism that is similar to fatty acid synthesis. Enoyl reductase reduces a double to single bond. Erythromycin is one example of a polyketide generated by 3 complex enzymes (megasynthases). 2-enoyl thioester reductase (ETR) catalyzes the NADPH-dependent dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains, at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding.


Pssm-ID: 176179 [Multi-domain]  Cd Length: 293  Bit Score: 324.14  E-value: 7.50e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1700 QVEIEVEAAGLNFLDVLGALGMMPAleaEESVLGRECSGRIAAVGEGVSGLRVGDEVLAVAPGCFRSYVLVDESQVVRRP 1779
Cdd:cd05195    2 EVEVEVKAAGLNFRDVLVALGLLPG---DETPLGLECSGIVTRVGSGVTGLKVGDRVMGLAPGAFATHVRVDARLVVKIP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1780 ASLGLAEGAAQMVPFATAYFALHTVGRLRRGERILIHAAAGGLGLAAVQLASRTGAEILATAGSEQKREYLRSLG--IAH 1857
Cdd:cd05195   79 DSLSFEEAATLPVAYLTAYYALVDLARLQKGESVLIHAAAGGVGQAAIQLAQHLGAEVFATVGSEEKREFLRELGgpVDH 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1858 VLDSRSTSFVSEVRERTGGRGVDVVLNSLAGELLLAGLSVLAPHGRFLELGKRDLYADQQVGLRTLARGQTFAAIDFGP- 1936
Cdd:cd05195  159 IFSSRDLSFADGILRATGGRGVDVVLNSLSGELLRASWRCLAPFGRFVEIGKRDILSNSKLGMRPFLRNVSFSSVDLDQl 238

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 53747904 1937 --HHPD-FRAVLEEVATQLTQGQLEPLPTRLFPARQVAEAFSFMARALHIGRVAV 1988
Cdd:cd05195  239 arERPElLRELLREVLELLEAGVLKPLPPTVVPSASEIDAFRLMQSGKHIGKVVL 293
omega_3_PfaA TIGR02813
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ...
 13-914 1.50e-90

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: 331.58  E-value: 1.50e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904     13 IALVGMAGRFPGAPDVESFWRNLVAGVESISFFSEEELRQAGVSEQIRRRPE--YVPAKGVLEDLElFDAGFFGYSPREA 90
Cdd:TIGR02813    9 IAIVGMASIFANSRYLNKFWDLIFEKIDAITDVPSDHWAKDDYYDSDKSEADksYCKRGGFLPEVD-FNPMEFGLPPNIL 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904     91 SHLDPQQRLLLECSWEALEDAGLRPDQLPGWVGVYVGAGDTSYRFQLL--RGHGDPL------SGSKDV----------- 151
Cdd:TIGR02813   88 ELTDISQLLSLVVAKEVLNDAGLPDGYDRDKIGITLGVGGGQKQSSSLnaRLQYPVLkkvfkaSGVEDEdsemlikkfqd 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904    152 -------AGFFGNYPDFLATRVAYKLNLRGPALGIHTACSTSLVSINMACSALRGFECDMALAGGVSLRlpaRSGYLY-- 222
Cdd:TIGR02813  168 qyihweeNSFPGSLGNVISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGGVCTD---NSPFMYms 244

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904    223 -EEGGVASKDGHCRPFDARATGTVTGDGVGVVVLKRLEDALKARDPIHAVIRGWALNNDGASRAGFtAPSVEGQSEVIAL 301
Cdd:TIGR02813  245 fSKTPAFTTNEDIQPFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGKFKSIY-APRPEGQAKALKR 323

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904    302 AHAAAGISARDITYVEAHGTGTPLGDPIEVAALTRAFRAHTADTAFCTLGAVKSNIGHLDAAAGVAGVIKTVQALRHRLI 381
Cdd:TIGR02813  324 AYDDAGFAPHTCGLIEAHGTGTAAGDVAEFGGLVSVFSQDNDQKQHIALGSVKSQIGHTKSTAGTAGMIKAVLALHHKVL 403

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904    382 PPTLHFERPNPALHLEQSPFFVNTQPLPW--ESPRGPRLAGVSSFGIGGTNAHTLFEEAPPPPASGPT-RPNQV---LLL 455
Cdd:TIGR02813  404 PPTINVDQPNPKLDIENSPFYLNTETRPWmqREDGTPRRAGISSFGFGGTNFHMVLEEYSPKHQRDDQyRQRAVaqtLLF 483

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904    456 SARSTSALehIAGRLAAHLRRHPDLELADVAF----------TLQVGRARFpyrrALTCRTLAEAMERLEAPEPRPPEPL 525
Cdd:TIGR02813  484 TAANEKAL--VSSLKDWKNKLSAKADDQPYAFnalaventlrTIAVALARL----GFVAKNADELITMLEQAITQLEAKS 557

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904    526 AHEGERPP---------------LVMLFPGQGTPLVGTARALHESEPTFRQAVEQCARLLRQTLGLDVREVLFP------ 584
Cdd:TIGR02813  558 CEEWQLPSgisyrksalvvesgkVAALFAGQGSQYLNMGRELACNFPEVRQAAADMDSVFTQAGKGALSPVLYPipvfnd 637

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904    585 -SAEQEEQARRLaaqTRVAQPALFTLEYALAQTWLGWGLQPQALAGHSLGELVAACLAGVFSLEDALQLVAARGQLMQGC 663
Cdd:TIGR02813  638 eSRKAQEEALTN---TQHAQSAIGTLSMGQYKLFTQAGFKADMTAGHSFGELSALCAAGVISDDDYMMLAFSRGQAMAAP 714

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904    664 P----PGAMLAVPLPEAELAALLGSELC------IAAVNGPRACVASGPLPAVEALTAALESRGVSSRRLETSHAFHSAS 733
Cdd:TIGR02813  715 TgeadIGFMYAVILAVVGSPTVIANCIKdfegvsIANYNSPTQLVIAGVSTQIQIAAKALKEKGFKAIPLPVSGAFHTPL 794

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904    734 MEACQGPLTTLLRRMRLQAPRLPCVSGLTGRWLTGEEATEPTYWARQLREPVRFSEALETLWSLKEPVLLEVGPGTTLTA 813
Cdd:TIGR02813  795 VAHAQKPFSAAIDKAKFNTPLVPLYSNGTGKLHSNDAAAIKKALKNHMLQSVHFSEQLEAMYAAGARVFVEFGPKNILQK 874

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904    814 LARRhpTRPARTQEVASLPVQPD---TAVPCIEEAVGELWQAGLELDwsalhaaprhraHLPPYPFErqrywIEPEAAPQ 890
Cdd:TIGR02813  875 LVEN--TLKDKENELCAISINPNpkgDSDMQLRQAAVQLAVLGLELT------------EIDPYQAE-----KRPPAATS 935

                          970       980
                   ....*....|....*....|....
gi 53747904    891 PRAQQPTPASLVPPEqpSREALED 914
Cdd:TIGR02813  936 PMNIKLNAANYISPA--TRKKMDD 957
Qor COG0604
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ...
 1675-1991 9.11e-76

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: 255.84  E-value: 9.11e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1675 VAVGTPGLLESLGLRRCTRPAPGPRQVEIEVEAAGLNFLDVLGALGMMPALEAEESVLGRECSGRIAAVGEGVSGLRVGD 1754
Cdd:COG0604    4 IVITEFGGPEVLELEEVPVPEPGPGEVLVRVKAAGVNPADLLIRRGLYPLPPGLPFIPGSDAAGVVVAVGEGVTGFKVGD 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1755 EVLA-VAPGCFRSYVLVDESQVVRRPASLGLAEGAAQMVPFATAYFALHTVGRLRRGERILIHaaagglglaaVQLASRT 1833
Cdd:COG0604   84 RVAGlGRGGGYAEYVVVPADQLVPLPDGLSFEEAAALPLAGLTAWQALFDRGRLKPGETVLVHgaaggvgsaaVQLAKAL 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1834 GAEILATAGSEQKREYLRSLGIAHVLDSRSTSFVSEVRERTGGRGVDVVLNSLAGELLLAGLSVLAPHGRFLELGKRDLY 1913
Cdd:COG0604  164 GARVIATASSPEKAELLRALGADHVIDYREEDFAERVRALTGGRGVDVVLDTVGGDTLARSLRALAPGGRLVSIGAASGA 243

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 53747904 1914 ADQQVGLRTLARGQTFAAIDFGPHHPD-FRAVLEEVATQLTQGQLEPLPTRLFPARQVAEAFSFMARALHIGRVAVSMQ 1991
Cdd:COG0604  244 PPPLDLAPLLLKGLTLTGFTLFARDPAeRRAALAELARLLAAGKLRPVIDRVFPLEEAAEAHRLLESGKHRGKVVLTVD 322
AMP-binding pfam00501
AMP-binding enzyme;
2644-3043 1.17e-74

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 256.47  E-value: 1.17e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   2644 FFTQARLHPELPALL-APERTLSYGELARRAQALAARLRELEVQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLDPEQ 2722
Cdd:pfam00501    1 LERQAARTPDKTALEvGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   2723 PPLRLHQLLEEGPARVVLTQSSLL------HTVPWPPGVQVIAVD------------ELEPATEAPPLPPRGTPEHLAYV 2784
Cdd:pfam00501   81 PAEELAYILEDSGAKVLITDDALKleelleALGKLEVVKLVLVLDrdpvlkeeplpeEAKPADVPPPPPPPPDPDDLAYI 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   2785 IYTSGSTGKPKGVAIEHRAALNTVVDL----NTRFGVGPEDRVLGLSALTFDLSV-YDVLGLLGAGGALVLPAAEAEKDP 2859
Cdd:pfam00501  161 IYTSGTTGKPKGVMLTHRNLVANVLSIkrvrPRGFGLGPDDRVLSTLPLFHDFGLsLGLLGPLLAGATVVLPPGFPALDP 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   2860 AHWWERLVAGRVTVWNSTPALMLLLVEYAEQRGLKLPaALRLVMLSGDWIPVALPDRIRALGRDvQVVSLGGATEASIWS 2939
Cdd:pfam00501  241 AALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLS-SLRLVLSGGAPLPPELARRFRELFGG-ALVNGYGLTETTGVV 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   2940 IAYPIGQvaPQWKSIP-YGMPLANQRFHVLD-GRLEARPWWVPGELYIGGEGLAREYWRDEPLTATRFIRhprtgERLYR 3017
Cdd:pfam00501  319 TTPLPLD--EDLRSLGsVGRPLPGTEVKIVDdETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDE-----DGWYR 391

                          410       420
                   ....*....|....*....|....*.
gi 53747904   3018 TGDQGRMLPEGSIEFLGREDLQVKVQ 3043
Cdd:pfam00501  392 TGDLGRRDEDGYLEIVGRKKDQIKLG 417
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
 11-241 5.70e-68

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: 230.60  E-value: 5.70e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904     11 SSIALVGMAGRFPGAPDVESFWRNLVAGVESISFFSEEELRQAGVSEQIRRRPEYVPAK-GVLEDLELFDAGFFGYSPRE 89
Cdd:pfam00109    1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIPADRWDPDKLYDPPSRIAGKIYTKwGGLDDIFDFDPLFFGISPRE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904     90 ASHLDPQQRLLLECSWEALEDAGLRPDQLPG-WVGVYVGAGDTSYR-FQLLRGHGDPLSGSkdvAGFFGNYPDFLATRVA 167
Cdd:pfam00109   81 AERMDPQQRLLLEAAWEALEDAGITPDSLDGsRTGVFIGSGIGDYAaLLLLDEDGGPRRGS---PFAVGTMPSVIAGRIS 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 53747904    168 YKLNLRGPALGIHTACSTSLVSINMACSALRGFECDMALAGGVSLRLPARSGYLYEEGGVASKDGHCRPFDARA 241
Cdd:pfam00109  158 YFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSPDGPCKAFDPFA 231
PTZ00050 PTZ00050
3-oxoacyl-acyl carrier protein synthase; Provisional
 27-435 1.21e-39

3-oxoacyl-acyl carrier protein synthase; Provisional


Pssm-ID: 240245 [Multi-domain]  Cd Length: 421  Bit Score: 154.47  E-value: 1.21e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904    27 DVESFWRNLVAGVESISFFSEEELRQAGVSEQIRRRPEYVPAK----GVLEDLELFDAGFFGYSPREashlDPQQRLLLE 102
Cdd:PTZ00050    8 GAESTWEALIAGKSGIRKLTEFPKFLPDCIPEQKALENLVAAMpcqiAAEVDQSEFDPSDFAPTKRE----SRATHFAMA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   103 CSWEALEDAGLRP--DQLPGWVGVYVGAGDTSYRFQL-------LRGHgdplsgsKDVAGFFgnYPDFLATR----VAYK 169
Cdd:PTZ00050   84 AAREALADAKLDIlsEKDQERIGVNIGSGIGSLADLTdemktlyEKGH-------SRVSPYF--IPKILGNMaaglVAIK 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   170 LNLRGPALGIHTACSTSLVSINMACSALRGFECDMALAGGV-----------SLRLPARSGYLYEEGGVASkdghcRPFD 238
Cdd:PTZ00050  155 HKLKGPSGSAVTACATGAHCIGEAFRWIKYGEADIMICGGTeasitpvsfagFSRMRALCTKYNDDPQRAS-----RPFD 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   239 ARATGTVTGDGVGVVVLKRLEDALKARDPIHAVIRGWalnndGASRAGF--TAPSVEGQSEVIALAHA---AAGISARDI 313
Cdd:PTZ00050  230 KDRAGFVMGEGAGILVLEELEHALRRGAKIYAEIRGY-----GSSSDAHhiTAPHPDGRGARRCMENAlkdGANININDV 304

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   314 TYVEAHGTGTPLGDPIEVAALTRAFRAHTADTafCTLGAVKSNIGHLDAAAGVAGVIKTVQALRHRLIPPTLHFERPNPA 393
Cdd:PTZ00050  305 DYVNAHATSTPIGDKIELKAIKKVFGDSGAPK--LYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINLENPDAE 382

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 53747904   394 LHLEQSPffvNTQPLPwesPRGPRLAGVSSFGIGGTNAHTLF 435
Cdd:PTZ00050  383 CDLNLVQ---GKTAHP---LQSIDAVLSTSFGFGGVNTALLF 418
PTZ00354 PTZ00354
alcohol dehydrogenase; Provisional
 1680-1996 6.07e-33

alcohol dehydrogenase; Provisional


Pssm-ID: 173547 [Multi-domain]  Cd Length: 334  Bit Score: 132.46  E-value: 6.07e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  1680 PGLLESLGLRRCTRPAPGPRQVEIEVEAAGLNFLDVLGALGMMPALEAEESVLGRECSGRIAAVGEGVSGLRVGDEVLAV 1759
Cdd:PTZ00354   10 FGGVDVLKIGESPKPAPKRNDVLIKVSAAGVNRADTLQRQGKYPPPPGSSEILGLEVAGYVEDVGSDVKRFKEGDRVMAL 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  1760 APG-CFRSYVLVDESQVVRRPASLGLAEGAAQMVPFATAYFALHTVGRLRRGERILIHAAAGGLGLAAVQLASRTGAEIL 1838
Cdd:PTZ00354   90 LPGgGYAEYAVAHKGHVMHIPQGYTFEEAAAIPEAFLTAWQLLKKHGDVKKGQSVLIHAGASGVGTAAAQLAEKYGAATI 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  1839 ATAGSEQKREYLRSLGIAHVLDSRS-TSFVSEVRERTGGRGVDVVLNSLAGELLLAGLSVLAPHGRFLELGKRDLYADQQ 1917
Cdd:PTZ00354  170 ITTSSEEKVDFCKKLAAIILIRYPDeEGFAPKVKKLTGEKGVNLVLDCVGGSYLSETAEVLAVDGKWIVYGFMGGAKVEK 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  1918 VGLRTLARGQtfAAIDFGPHHP---DFRAVL-----EEVATQLTQGQLEPLPTRLFPARQVAEAFSFMARALHIGRVAVS 1989
Cdd:PTZ00354  250 FNLLPLLRKR--ASIIFSTLRSrsdEYKADLvasfeREVLPYMEEGEIKPIVDRTYPLEEVAEAHTFLEQNKNIGKVVLT 327


                  ....*..
gi 53747904  1990 MQGATAL 1996
Cdd:PTZ00354  328 VNEPLSL 334
PS-DH pfam14765
Polyketide synthase dehydratase; This is the dehydratase domain of polyketide synthases. ...
 1410-1659 2.58e-28

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: 117.86  E-value: 2.58e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   1410 TLRGGEDWVVDEHRLQGVPTLPGVAYLELARAACAQALGAEAVELAELLL-LEPLTVPRGESRQVRVVLQPEGQAHALRV 1488
Cdd:pfam14765   21 RLRLADLPWLRDHRVGGTVVLPGAGYLEMALEAARQLFGGSGAVALRDVSiLKALVLPEDDPVEVQTSLTPEEDGADSWW 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   1489 E----SRSEEARGWNEHARGRVRAVPRL-AERIQPELLRAACehEQPVPGEPQEQGPVHAGARWHGL-----FQWVR--- 1555
Cdd:pfam14765  101 EfeifSRAGGGWEWTLHATGTVRLAPGEpAAPVDLESLPARC--AQPADPRSVSSAEFYERLAARGLfygpaFQGLRriw 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   1556 RGPRQALAQLALPEPFHGDLERFELHPALMDMA--------TSFAIPGGVPWLAFGYERVLIHGPLPPQ--VLSHVSLPE 1625
Cdd:pfam14765  179 RGDGEALAEARLPEAAAGGESPYLLHPALLDAAlqllgaalPAEAEHADQAYLPVGIERLRIYRSLPPGepLWVHARLER 258

                          250       260       270
                   ....*....|....*....|....*....|....
gi 53747904   1626 EsqaGAQQLRLQVRLLDLEGWERVRIDGYLLRPL 1659
Cdd:pfam14765  259 R---GGRTIVGDLTLVDEDGRVVARIEGLRLRRV 289
ADH_zinc_N pfam00107
Zinc-binding dehydrogenase;
1827-1950 2.93e-17

Zinc-binding dehydrogenase;


Pssm-ID: 395057 [Multi-domain]  Cd Length: 129  Bit Score: 80.73  E-value: 2.93e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   1827 VQLASRTGAEILATAGSEQKREYLRSLGIAHVLDSRSTSFVSEVRERTGGRGVDVVLN-SLAGELLLAGLSVLAPHGRFL 1905
Cdd:pfam00107    7 IQLAKAAGAKVIAVDGSEEKLELAKELGADHVINPKETDLVEEIKELTGGKGVDVVFDcVGSPATLEQALKLLRPGGRVV 86

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 53747904   1906 ELGKrdLYADQQVGLRTLA-RGQTFAAIDFGpHHPDFRAVLEEVAT 1950
Cdd:pfam00107   87 VVGL--PGGPLPLPLAPLLlKELTILGSFLG-SPEEFPEALDLLAS 129
PKS_DH smart00826
Dehydratase domain in polyketide synthase (PKS) enzymes;
1400-1534 7.24e-13

Dehydratase domain in polyketide synthase (PKS) enzymes;


Pssm-ID: 214837  Cd Length: 167  Bit Score: 69.18  E-value: 7.24e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904    1400 EPGGTHWLGlTLRGGEDWVVDEHRLQGVPTLPGVAYLELARAACAQALGAEAVELAELLLLEPLTVPRGESRQVRVVLQP 1479
Cdd:smart00826   12 DGGGVVLTG-RLSLRTHPWLADHRVGGTVVLPGAAYVELALAAADEVGGGAPARLEELTLEAPLVLPEDGAVRVQVVVGA 90

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 53747904    1480 EGQAH--ALRVESRSEEARGWNEHARGRVRAVPRLAERIQPELLRAACEHEQPVPGE 1534
Cdd:smart00826   91 PDEDGrrTFTVYSRPDGDGPWTRHATGTLRPAAAAPAAPAADLAAWPPAGAEPVDVD 147
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
 2083-2145 1.21e-11

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: 62.95  E-value: 1.21e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 53747904 2083 PPSSLEQLIEQVWRKHLGV--ERVQPTDSFFQ-LGGDSLLGIQVAADLRRHLGVELPTATLFSHPT 2145
Cdd:COG0236    2 PREELEERLAEIIAEVLGVdpEEITPDDSFFEdLGLDSLDAVELIAALEEEFGIELPDTELFEYPT 67
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
 2089-2145 1.30e-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: 62.20  E-value: 1.30e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 53747904   2089 QLIEQVWRKHLGV--ERVQPTDSFFQLGGDSLLGIQVAADLRRHLGVELPTATLFSHPT 2145
Cdd:pfam00550    1 ERLRELLAEVLGVpaEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPT 59
PRK12467 PRK12467
peptide synthase; Provisional
 2083-2145 8.65e-11

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 68.65  E-value: 8.65e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 53747904  2083 PPSSLEQLIEQVWRKHLGVERVQPTDSFFQLGGDSLLGIQVAADLRRHLGVELPTATLFSHPT 2145
Cdd:PRK12467 3602 PRSEVEQQLAAIWADVLGVEQVGVTDNFFELGGDSLLALQVLSRIRQSLGLKLSLRDLMSAPT 3664
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
 2079-2145 2.35e-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: 53.79  E-value: 2.35e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 53747904    2079 PQALPPSSLEQLIEQVWRKHLGV-------ERVQPTDSFFQLGGDSLLGIQVAADLRRHLGVELPTATLFSHPT 2145
Cdd:smart00823    1 LAALPPAERRRLLLDLVREQVAAvlghaaaEAIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPT 74
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
 2072-2145 1.02e-07

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: 58.54  E-value: 1.02e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 53747904   2072 GRAAAAEPQALppSSLEQLIEQVWRKHL--GVERVQPTDSFFQLGGDSLLGIQVAADLRRHLGVELPTATLFSHPT 2145
Cdd:TIGR03443  836 NRSASAADEEF--TETEREIRDLWLELLpnRPATISPDDSFFDLGGHSILATRMIFELRKKLNVELPLGLIFKSPT 909
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
 3149-3214 3.53e-06

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: 47.63  E-value: 3.53e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 53747904    3149 DPLVERLAALVKEALRL---ERVEPQDSLLDLGADSVALIRLINRLEAELQFRPRLADIYENPTVQGLA 3214
Cdd:smart00823   11 RLLLDLVREQVAAVLGHaaaEAIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALA 79
B4_12hDH TIGR02825
leukotriene B4 12-hydroxydehydrogenase/15-oxo-prostaglandin 13-reductase; Leukotriene B4 ...
 1748-1880 6.50e-05

leukotriene B4 12-hydroxydehydrogenase/15-oxo-prostaglandin 13-reductase; Leukotriene B4 12-hydroxydehydrogenase is an NADP-dependent enzyme of arachidonic acid metabolism, responsible for converting leukotriene B4 to the much less active metabolite 12-oxo-leukotriene B4. The BRENDA database lists leukotriene B4 12-hydroxydehydrogenase as one of the synonyms of 2-alkenal reductase (EC 1.3.1.74), while 1.3.1.48 is 15-oxoprostaglandin 13-reductase.


Pssm-ID: 131872 [Multi-domain]  Cd Length: 325  Bit Score: 48.07  E-value: 6.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   1748 SGLRVGDEVLAvAPGcFRSYVLVDESQVVRRPAS------LGLAEGAAQMvPFATAYFALHTVGRLRRGERILIHAAAGG 1821
Cdd:TIGR02825   74 VALPKGTIVLA-SPG-WTSHSISDGKDLEKLLTEwpdtlpLSLALGTVGM-PGLTAYFGLLEICGVKGGETVMVNAAAGA 150

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 53747904   1822 LGLAAVQLASRTGAEILATAGSEQKREYLRSLGIAHVLDSRSTSFVSEVRERTGGRGVD 1880
Cdd:TIGR02825  151 VGSVVGQIAKLKGCKVVGAAGSDEKVAYLKKLGFDVAFNYKTVKSLEETLKKASPDGYD 209
 
Name Accession Description Interval E-value
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
 13-1382 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: 1087.21  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   13 IALVGMAGRFPGAPDVESFWRNLVAGVESISFFSEEELRQAG--VSEQIRRRPEYVPAKGVLEDLELFDAGFFGYSPREA 90
Cdd:COG3321    6 IAIIGMACRFPGADDPEEFWRNLRAGRDAITEVPADRWDADAyyDPDPDAPGKTYVRWGGFLDDVDEFDALFFGISPREA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   91 SHLDPQQRLLLECSWEALEDAGLRPDQLPGW-VGVYVGAGDTSYrFQLLRGHGDPLSGSkdvaGFFGNYPDFLATRVAYK 169
Cdd:COG3321   86 EAMDPQQRLLLEVAWEALEDAGYDPESLAGSrTGVFVGASSNDY-ALLLLADPEAIDAY----ALTGNAKSVLAGRISYK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  170 LNLRGPALGIHTACSTSLVSINMACSALRGFECDMALAGGVSLRLPARSGYLYEEGGVASKDGHCRPFDARAtgtvtgdg 249
Cdd:COG3321  161 LDLRGPSVTVDTACSSSLVAVHLACQSLRSGECDLALAGGVNLMLTPESFILFSKGGMLSPDGRCRAFDADAdgyvrgeg 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  250 vgvvvLKRLEDALKARDPIHAVIRGWALNNDGASRaGFTAPSVEGQSEVIALAHAAAGISARDITYVEAHGTGTPLGDPI 329
Cdd:COG3321  241 vgvvvLKRLSDALRDGDRIYAVIRGSAVNQDGRSN-GLTAPNGPAQAAVIRRALADAGVDPATVDYVEAHGTGTPLGDPI 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  330 EVAALTRAFRAHTADTAFCTLGAVKSNIGHLDAAAGVAGVIKTVQALRHRLIPPTLHFERPNPALHLEQSPFFVNTQPLP 409
Cdd:COG3321  320 EAAALTAAFGQGRPADQPCAIGSVKSNIGHLEAAAGVAGLIKAVLALRHGVLPPTLHFETPNPHIDFENSPFYVNTELRP 399

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  410 WESPRGPRLAGVSSFGIGGTNAHTLFEEAPP--PPASGPTRPNQVLLLSARSTSALEHIAGRLAAHLRRHPDLELADVAF 487
Cdd:COG3321  400 WPAGGGPRRAGVSSFGFGGTNAHVVLEEAPAaaPAAAAAARPPQLLVLSAKTEEALRALAARLAAFLEAHPDLDLADVAY 479

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  488 TLQVGRARFPYRRALTCRTLAEAMER---LEAPEPRPPEPLAHEGERPPLVMLFPGQGTPLVGTARALHESEPTFRQAVE 564
Cdd:COG3321  480 TLATGRAHFEHRLAVVASSREELAAKlraLAAGEAAPGVVTGAAAAAPKVAFLFPGQGSQYVGMGRELYETEPVFRAALD 559

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  565 QCARLLRQTLGLDVREVLFPsaeqEEQARRLaAQTRVAQPALFTLEYALAQTWLGWGLQPQALAGHSLGELVAACLAGVF 644
Cdd:COG3321  560 ECDALLRPHLGWSLREVLFP----DEEESRL-DRTEVAQPALFAVEYALARLWRSWGVRPDAVIGHSVGEYAAACVAGVL 634

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  645 SLEDALQLVAARGQLMQGCPP-GAMLAVPLPEAELAALLGS--ELCIAAVNGPRACVASGPLPAVEALTAALESRGVSSR 721
Cdd:COG3321  635 SLEDALRLVAARGRLMQALPGgGAMLAVGLSEEEVEALLAGydGVSIAAVNGPRSTVVSGPAEAVEALAARLEARGIRAR 714

                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  722 RLETSHAFHSASMEACQGPLTTLLRRMRLQAPRLPCVSGLTGRWLTGEEATePTYWARQLREPVRFSEALETLWSLKEPV 801
Cdd:COG3321  715 RLPVSHAFHSPLMEPALEEFRAALAGVTPRAPRIPLISNVTGTWLTGEALD-ADYWVRHLRQPVRFADAVEALLADGVRV 793

                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  802 LLEVGPGTTLTALARRHPTRPARTQEVASLPvQPDTAVPCIEEAVGELWQAGLELDWSALHA-APRHRAHLPPYPFERQR 880
Cdd:COG3321  794 FLEVGPGPVLTGLVRQCLAAAGDAVVLPSLR-RGEDELAQLLTALAQLWVAGVPVDWSALYPgRGRRRVPLPTYPFQRED 872

                        890       900       910       920       930       940       950       960
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  881 YWIEPEAAPQPRAQQPTPASLVPPEQPSREALEDWFYVPTWEQAPATSGGGQPLAGPVLAFMDSSGLAEQVLAALWPADS 960
Cdd:COG3321  873 AAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAAAALLALAAAAAAA 952

                        970       980       990      1000      1010      1020      1030      1040
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  961 GALLTRVEPAGHyeqlsehafrlrPESEEDWDALFQALQSQGRLPRRILHAWALTAEPGPCTPDGEAVLEQGFFSLLRLA 1040
Cdd:COG3321  953 AAALAAAEAGAL------------LLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAA 1020

                       1050      1060      1070      1080      1090      1100      1110      1120
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1041 RALGRHAPERPVQLEVLSSFVHAVGPREPLEPLKATLLGACAVLPLEYPHVQCRTIDVRPGSEPREVLVRSLAAELAAPM 1120
Cdd:COG3321 1021 LLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALALA 1100

                       1130      1140      1150      1160      1170      1180      1190      1200
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1121 GESPVAWRDGQRYVRRATRQRLEASRPLRSLRERGVylvaggLGGIGLVLARALAQRARARLALLTHSPFPPREQWEQWL 1200
Cdd:COG3321 1101 ALAAALLLLALLAALALAAAAAALLALAALLAAAAA------AAALAAAAAAAAALALAAAAAALAAALAAALLAAAALL 1174

                       1210      1220      1230      1240      1250      1260      1270      1280
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1201 EEAPAHPEPAWRSEADPSERRRTQHRIRCLLELEQLGAEVQVYTADVAEEAAVRSVVEQVHARWGKIHGVLHAAATFDDG 1280
Cdd:COG3321 1175 LALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAA 1254

                       1290      1300      1310      1320      1330      1340      1350      1360
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1281 VIQLRTHEQSSRALRTKVRGSMVLHEVLASEGLDWFALCSSLASALGSFGQADYCAANAFQDAYAHHLRRQGFTGALALD 1360
Cdd:COG3321 1255 LLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAALA 1334

                       1370      1380
                 ....*....|....*....|..
gi 53747904 1361 WGTWRDTGAAMRLVARTRRGGH 1382
Cdd:COG3321 1335 AAVAAALALAAAAAAAAAAAAA 1356
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
 2172-3503 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: 731.27  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2172 PDPAARFEPFPLTDVQEAYWVGRRSAFELGGVAAHGYFEIESPGLEVERFIQCWRQLLQRHDMLRMVVLPDGRQQVLEQV 2251
Cdd:COG1020   14 AAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRPVQVIQPVVAAP 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2252 PEYTPEVVELRGLSPQEAESRRLQLRERMAHQVLRSD-RWPLFELVLCRYEGGVRIHMSMDALMLDAWSSAVLRQDFAQL 2330
Cdd:COG1020   94 LPVVVLLVDLEALAEAAAEAAAAAEALAPFDLLRGPLlRLLLLLLLLLLLLLLLALHHIISDGLSDGLLLAELLRLYLAA 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2331 YHEPGRPLEPLAITFRDYVLAERRLREGEAHERARAYWWARLDTLPPPPELPLVKEPSQLEHARFTHREARLEPHRWARL 2410
Cdd:COG1020  174 YAGAPLPLPPLPIQYADYALWQREWLQGEELARQLAYWRQQLAGLPPLLELPTDRPRPAVQSYRGARVSFRLPAELTAAL 253

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2411 QERARAHGLTPSAACMAAFAEVLARWSRHPRFTLNLTLFQRLplHPQVDELVGDFTSLVLLEVEAHAASTFAERASRLQA 2490
Cdd:COG1020  254 RALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRP--RPELEGLVGFFVNTLPLRVDLSGDPSFAELLARVRE 331

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2491 QLWRDLEHGSVSAVQLIREL--VRTGRRSPgaimpvVFTSILSLDARRGPQGSLSFFEGELVYSISQTPQVWLDHGVHEE 2568
Cdd:COG1020  332 TLLAAYAHQDLPFERLVEELqpERDLSRNP------LFQVMFVLQNAPADELELPGLTLEPLELDSGTAKFDLTLTVVET 405

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2569 EGALVLAWDSVEALFPPGMVDDMFHAYQRLLGALAEEEQAWEGELPELLPPAQRELLARYNATQAPRPSGR-LEEGFFTQ 2647
Cdd:COG1020  406 GDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQLLAEWNATAAPYPADAtLHELFEAQ 485

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2648 ARLHPELPALLAPERTLSYGELARRAQALAARLRELEVQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLDPEQPPLRL 2727
Cdd:COG1020  486 AARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERL 565

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2728 HQLLEEGPARVVLTQSSLLHTVPwPPGVQVIAVDELEPATEAPPLPPRG-TPEHLAYVIYTSGSTGKPKGVAIEHRAALN 2806
Cdd:COG1020  566 AYMLEDAGARLVLTQSALAARLP-ELGVPVLALDALALAAEPATNPPVPvTPDDLAYVIYTSGSTGRPKGVMVEHRALVN 644

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2807 TVVDLNTRFGVGPEDRVLGLSALTFDLSVYDVLGLLGAGGALVLPAAEAEKDPAHWWERLVAGRVTVWNSTPALMLLLVE 2886
Cdd:COG1020  645 LLAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLLRALLD 724

                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2887 YAEQRglklPAALRLVMLSGDWIPVALPDRIRALGRDVQVVSLGGATEASIWSIAYPIGQVAPQWKSIPYGMPLANQRFH 2966
Cdd:COG1020  725 AAPEA----LPSLRLVLVGGEALPPELVRRWRARLPGARLVNLYGPTETTVDSTYYEVTPPDADGGSVPIGRPIANTRVY 800

                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2967 VLDGRLEARPWWVPGELYIGGEGLAREYWRDEPLTATRFIRHP--RTGERLYRTGDQGRMLPEGSIEFLGREDLQVKVQG 3044
Cdd:COG1020  801 VLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPfgFPGARLYRTGDLARWLPDGNLEFLGRADDQVKIRG 880

                        890       900       910       920       930       940       950       960
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3045 FRVELGEIEAALAQHPALSASVVVARGEPRGVRRLVAYAVPRSGQTPAAGELRRYLAERLPAYMVPSAFVLLESLPRSRN 3124
Cdd:COG1020  881 FRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGN 960

                        970       980       990      1000      1010      1020      1030      1040
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3125 GKIARDQLPEPQQTQGLAAQAAAADPLVERLAALVkEALRLERVEPQDSLLDLGADSVALIRLINRLEAELQFRPRLADI 3204
Cdd:COG1020  961 GKLDRLALPAPAAAAAAAAAAPPAEEEEEEAALAL-LLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLL 1039

                       1050      1060      1070      1080      1090      1100      1110      1120
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3205 YENPTVQGLATLHQEKTKSQGEGGAPRLTAPRSTLLPAEEWGRFKANRPGLRRFPDGTPEVALPGSGLAPAPEELTALER 3284
Cdd:COG1020 1040 FLAAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLALLL 1119

                       1130      1140      1150      1160      1170      1180      1190      1200
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3285 RRSVRTYSLEPVSHEQLGRLLAPLREWEVQGSRRYLYASAGGLYPVQLYLHLKPGRARGLEPGTWYYDPSTHRLVLLSAG 3364
Cdd:COG1020 1120 ALLAALRARRAVRQEGPRLRLLVALAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLLLLLLLLL 1199

                       1210      1220      1230      1240      1250      1260      1270      1280
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3365 AGLDRRIHDPHQNQAIFDSAAFSLFLIARMGAVEPVYAEHALHFATLEAGLMTQLLDLGAAPsglglchigDLDFAQARG 3444
Cdd:COG1020 1200 LLLLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALLA---------LALALLALA 1270

                       1290      1300      1310      1320      1330
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 53747904 3445 LFHLEEEHVLLHSLVGGVLPTRGQEAASVPAEGGTEARQLAQLLQQVKTLTPEAARALL 3503
Cdd:COG1020 1271 LLLLALALLLPALARARAARTARALALLLLLALLLLLALALALLLLLLLLLALLLLALL 1329
Cyc_NRPS cd19535
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
 2180-2606 0e+00

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: 602.56  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2180 PFPLTDVQEAYWVGRRSAFELGGVAAHGYFEIESPGLEVERFIQCWRQLLQRHDMLRMVVLPDGRQQVLEQVPEYTPEVV 2259
Cdd:cd19535    1 PFPLTDVQYAYWIGRQDDQELGGVGCHAYLEFDGEDLDPDRLERAWNKLIARHPMLRAVFLDDGTQQILPEVPWYGITVH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2260 ELRGLSPQEAESRRLQLRERMAHQVLRSDRWPLFELVLCRY-EGGVRIHMSMDALMLDAWSSAVLRQDFAQLYHEPGRPL 2338
Cdd:cd19535   81 DLRGLSEEEAEAALEELRERLSHRVLDVERGPLFDIRLSLLpEGRTRLHLSIDLLVADALSLQILLRELAALYEDPGEPL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2339 EPLAITFRDYVLAERRLREgEAHERARAYWWARLDTLPPPPELPLVKEPSQLEHARFTHREARLEPHRWARLQERARAHG 2418
Cdd:cd19535  161 PPLELSFRDYLLAEQALRE-TAYERARAYWQERLPTLPPAPQLPLAKDPEEIKEPRFTRREHRLSAEQWQRLKERARQHG 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2419 LTPSAACMAAFAEVLARWSRHPRFTLNLTLFQRLPLHPQVDELVGDFTSLVLLEVEAHAASTFAERASRLQAQLWRDLEH 2498
Cdd:cd19535  240 VTPSMVLLTAYAEVLARWSGQPRFLLNLTLFNRLPLHPDVNDVVGDFTSLLLLEVDGSEGQSFLERARRLQQQLWEDLDH 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2499 GSVSAVQLIRELVRTgRRSPGAIMPVVFTSILSLDArrGPQGSLSFFeGELVYSISQTPQVWLDHGVHEEEGALVLAWDS 2578
Cdd:cd19535  320 SSYSGVVVVRRLLRR-RGGQPVLAPVVFTSNLGLPL--LDEEVREVL-GELVYMISQTPQVWLDHQVYEEDGGLLLNWDA 395

                        410       420
                 ....*....|....*....|....*...
gi 53747904 2579 VEALFPPGMVDDMFHAYQRLLGALAEEE 2606
Cdd:cd19535  396 VDELFPEGMLDDMFDAYVRLLERLADDD 423
A_NRPS_TlmIV_like cd12114
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ...
 2652-3132 0e+00

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: 576.14  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2652 PELPALLAPERTLSYGELARRAQALAARLRELEVQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLDPEQPPLRLHQLL 2731
Cdd:cd12114    1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2732 EEGPARVVLTQSSLLHTVPWPPGVQVIAVDELEPatEAPPLPPRGTPEHLAYVIYTSGSTGKPKGVAIEHRAALNTVVDL 2811
Cdd:cd12114   81 ADAGARLVLTDGPDAQLDVAVFDVLILDLDALAA--PAPPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTILDI 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2812 NTRFGVGPEDRVLGLSALTFDLSVYDVLGLLGAGGALVLPAAEAEKDPAHWWERLVAGRVTVWNSTPALMLLLVEYAEQR 2891
Cdd:cd12114  159 NRRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDPAHWAELIERHGVTLWNSVPALLEMLLDVLEAA 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2892 GlKLPAALRLVMLSGDWIPVALPDRIRALGRDVQVVSLGGATEASIWSIAYPIGQVAPQWKSIPYGMPLANQRFHVLDGR 2971
Cdd:cd12114  239 Q-ALLPSLRLVLLSGDWIPLDLPARLRALAPDARLISLGGATEASIWSIYHPIDEVPPDWRSIPYGRPLANQRYRVLDPR 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2972 LEARPWWVPGELYIGGEGLAREYWRDEPLTATRFIRHPrTGERLYRTGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGE 3051
Cdd:cd12114  318 GRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHP-DGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGE 396

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3052 IEAALAQHPALSASVVVARGEPrGVRRLVAYAVPRSGQTPAA-GELRRYLAERLPAYMVPSAFVLLESLPRSRNGKIARD 3130
Cdd:cd12114  397 IEAALQAHPGVARAVVVVLGDP-GGKRLAAFVVPDNDGTPIApDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRA 475


                 ..
gi 53747904 3131 QL 3132
Cdd:cd12114  476 AL 477
PKS cd00833
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ...
 13-432 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: 570.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   13 IALVGMAGRFPGAPDVESFWRNLVAGVESISFFSEEELRQAGVSEQIRRR-PEYVPAKGVLEDLELFDAGFFGYSPREAS 91
Cdd:cd00833    3 IAIVGMACRFPGAADPDEFWENLLEGRDAISEIPEDRWDADGYYPDPGKPgKTYTRRGGFLDDVDAFDAAFFGISPREAE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   92 HLDPQQRLLLECSWEALEDAGLRPDQLPGW-VGVYVGAGDTSYRFQLLRGHGDPlsgskDVAGFFGNYPDFLATRVAYKL 170
Cdd:cd00833   83 AMDPQQRLLLEVAWEALEDAGYSPESLAGSrTGVFVGASSSDYLELLARDPDEI-----DAYAATGTSRAFLANRISYFF 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  171 NLRGPALGIHTACSTSLVSINMACSALRGFECDMALAGGVSLRLPARSGYLYEEGGVASKDGHCRPFDARATGTVTGDGV 250
Cdd:cd00833  158 DLRGPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLSPDGRCRPFDADADGYVRGEGV 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  251 GVVVLKRLEDALKARDPIHAVIRGWALNNDGASRAGfTAPSVEGQSEVIALAHAAAGISARDITYVEAHGTGTPLGDPIE 330
Cdd:cd00833  238 GVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRTKGI-TAPSGEAQAALIRRAYARAGVDPSDIDYVEAHGTGTPLGDPIE 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  331 VAALTRAFRAHTADTAFCTLGAVKSNIGHLDAAAGVAGVIKTVQALRHRLIPPTLHFERPNPALHLEQSPFFVNTQPLPW 410
Cdd:cd00833  317 VEALAKVFGGSRSADQPLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKIDFEESPLRVPTEARPW 396

                        410       420
                 ....*....|....*....|..
gi 53747904  411 ESPRGPRLAGVSSFGIGGTNAH 432
Cdd:cd00833  397 PAPAGPRRAGVSSFGFGGTNAH 418
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
 2652-3132 6.77e-142

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: 451.21  E-value: 6.77e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2652 PELPALLAPERTLSYGELARRAQALAARLRELEVQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLDPEQPPLRLHQLL 2731
Cdd:cd05930    1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2732 EEGPARVVLTQssllhtvpwppgvqviavdelepateapplpprgtPEHLAYVIYTSGSTGKPKGVAIEHRAALNTVVDL 2811
Cdd:cd05930   81 EDSGAKLVLTD-----------------------------------PDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWM 125

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2812 NTRFGVGPEDRVLGLSALTFDLSVYDVLGLLGAGGALVLPAAEAEKDPAHWWERLVAGRVTVWNSTPALMLLLVEYAEqr 2891
Cdd:cd05930  126 QEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQELE-- 203

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2892 gLKLPAALRLVMLSGDWIPVALPDRIRALGRDVQVVSLGGATEASIWSIAYPIGQVAPQWKSIPYGMPLANQRFHVLDGR 2971
Cdd:cd05930  204 -LAALPSLRLVLVGGEALPPDLVRRWRELLPGARLVNLYGPTEATVDATYYRVPPDDEEDGRVPIGRPIPNTRVYVLDEN 282

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2972 LEARPWWVPGELYIGGEGLAREYWRDEPLTATRFIRHP-RTGERLYRTGDQGRMLPEGSIEFLGREDLQVKVQGFRVELG 3050
Cdd:cd05930  283 LRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPfGPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELG 362

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3051 EIEAALAQHPALSASVVVARGEPRGVRRLVAYAVPRSGQTPAAGELRRYLAERLPAYMVPSAFVLLESLPRSRNGKIARD 3130
Cdd:cd05930  363 EIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRK 442


                 ..
gi 53747904 3131 QL 3132
Cdd:cd05930  443 AL 444
PRK12467 PRK12467
peptide synthase; Provisional
 2083-3219 1.83e-139

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 493.52  E-value: 1.83e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2083 PPSSLEQLIEQVWRKHLGVERVQPTDSFFQLGGDSLLGIQVAADLRRHLGVELPTATLFSHPTLAALAAALRARQGEAAA 2162
Cdd:PRK12467 1027 PQTELEKRLAAIWADVLKVERVGLTDNFFELGGHSLLATQVISRVRQRLGIQVPLRTLFEHQTLAGFAQAVAAQQQGAQP 1106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2163 PTApapalvpdPAARFEPFPLTDVQEAYWVGRRsaFELGGVAAHGYFEIESPG-LEVERFIQCWRQLLQRHDMLRMV-VL 2240
Cdd:PRK12467 1107 ALP--------DVDRDQPLPLSYAQERQWFLWQ--LEPGSAAYHIPQALRLKGpLDIEALERSFDALVARHESLRTTfVQ 1176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2241 PDGR-QQVLEQVPEYTPEVVELRGLSPQEAESRrlQLRERMAHQVLRSDRWPLFELVLCRY--EGGVRIhMSMDALMLDA 2317
Cdd:PRK12467 1177 EDGRtRQVIHPVGSLTLEEPLLLAADKDEAQLK--VYVEAEARQPFDLEQGPLLRVGLLRLaaDEHVLV-LTLHHIVSDG 1253

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2318 WSSAVLRQDFAQLY--HEPGRPLE--PLAITFRDYVLAERRLREGEAHERARAYWWARLDTlppppelplvkEPSQLE-- 2391
Cdd:PRK12467 1254 WSMQVLVDELVALYaaYSQGQSLQlpALPIQYADYAVWQRQWMDAGERARQLAYWKAQLGG-----------EQPVLElp 1322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2392 -----HARFTHREAR----LEPHRWARLQERARAHGLTPSAACMAAFAEVLARWSRHPRFTLNLTLFQRLPLhpQVDELV 2462
Cdd:PRK12467 1323 tdrprPAVQSHRGARlafeLPPALAEGLRALARREGVTLFMLLLASFQTLLHRYSGQDDIRVGVPIANRNRA--ETEGLI 1400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2463 GDFTSLVLLEVEAHAASTFAE-----RASRLQAQLWRDLEHGS-VSAVQLIRELvrtgrrSPGAIMPVVFtsilslDARR 2536
Cdd:PRK12467 1401 GFFVNTQVLRAEVDGQASFQQllqqvKQAALEAQAHQDLPFEQlVEALQPERSL------SHSPLFQVMF------NHQR 1468

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2537 GPQGSLSFFEGELVYSIS---QTPQVWLDHGVHEEEGALVLAWDSVEALFPPGMVDDMFHAYQRLLGALAEEEQAWEGEL 2613
Cdd:PRK12467 1469 DDHQAQAQLPGLSVESLSwesQTAQFDLTLDTYESSEGLQASLTYATDLFEASTIERLAGHWLNLLQGLVADPERRLGEL 1548

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2614 PELLPPAQRELLARYNATQAPRPSGRLEEGFFT-QARLHPELPALLAPERTLSYGELARRAQALAARLRELEVQPQELVA 2692
Cdd:PRK12467 1549 DLLDEAERRQILEGWNATHTGYPLARLVHQLIEdQAAATPEAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVG 1628

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2693 IAMHKGWEQATAVLGVLQAAAAYLPLDPEQPPLRLHQLLEEGPARVVLTQSSLLHTVPWPPGVQVIAVDELEPATEA-PP 2771
Cdd:PRK12467 1629 IAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQSHLQARLPLPDGLRSLVLDQEDDWLEGySD 1708

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2772 LPP--RGTPEHLAYVIYTSGSTGKPKGVAIEHRAALNTVVDLNTRFGVGPEDRVLGLSALTFDLSVYDVLGLLGAGGALV 2849
Cdd:PRK12467 1709 SNPavNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFAFDVSVWELFWPLINGARLV 1788

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2850 LPAAEAEKDPAHWWERLVAGRVTVWNSTPALMLLLVEYAEQRGlkLPAALRLVMLSGDWIPVALPDRIRALGRDVQVVSL 2929
Cdd:PRK12467 1789 IAPPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQMDEQVE--HPLSLRRVVCGGEALEVEALRPWLERLPDTGLFNL 1866

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2930 GGATEASIWSIAYPIGQVAPQWK-SIPYGMPLANQRFHVLDGRLEARPWWVPGELYIGGEGLAREYWRDEPLTATRFIRH 3008
Cdd:PRK12467 1867 YGPTETAVDVTHWTCRRKDLEGRdSVPIGQPIANLSTYILDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFVAD 1946

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  3009 P--RTGERLYRTGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPALSASVVVARgEPRGVRRLVAYAVPR 3086
Cdd:PRK12467 1947 PfgTVGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQ-DGANGKQLVAYVVPT 2025

                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  3087 SGQTPAA--------GELRRYLAERLPAYMVPSAFVLLESLPRSRNGKIARDQLPEPQQTQGLAAQAAAADPLVERLAAL 3158
Cdd:PRK12467 2026 DPGLVDDdeaqvalrAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKALPAPDASELQQAYVAPQSELEQRLAAI 2105

                        1130      1140      1150      1160      1170      1180
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 53747904  3159 VKEALRLERVEPQDSLLDLGADSVALIRLINRL-EAELQFRPRlaDIYENPTVQGLATLHQE 3219
Cdd:PRK12467 2106 WQDVLGLEQVGLHDNFFELGGDSIISIQVVSRArQAGIRFTPK--DLFQHQTVQSLAAVAQE 2165
PKS_KS smart00825
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ...
 13-437 2.93e-133

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: 419.81  E-value: 2.93e-133
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904      13 IALVGMAGRFPGAPDVESFWRNLVAGvesisffseeelrqagvseqirrrpeyvpakgvLEDLELFDAGFFGYSPREASH 92
Cdd:smart00825    1 IAIVGMSCRFPGADDPEEFWDLLLAG---------------------------------LDDVDLFDAAFFGISPREAEA 47

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904      93 LDPQQRLLLECSWEALEDAGLRPDQLPGW-VGVYVGAGDTSYrfqllrghgdplsgskdvagffgnypdflatrvaykln 171
Cdd:smart00825   48 MDPQQRLLLEVAWEALEDAGIDPESLRGSrTGVFVGVSSSDY-------------------------------------- 89

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904     172 lrgpALGIHTACSTSLVSINMACSALRGFECDMALAGGVSLRLPARSGYLYEEGGVASKDGHCRPFDARAtgtvtgdgvg 251
Cdd:smart00825   90 ----SVTVDTACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLSPDGRCKTFDASAdgyvrgegvg 165

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904     252 vvvLKRLEDALKARDPIHAVIRGWALNNDGASrAGFTAPSVEGQsevialahaaagisardityveahgtgtplgdpiev 331
Cdd:smart00825  166 vvvLKRLSDALRDGDPILAVIRGSAVNQDGRS-NGITAPSGPAQ------------------------------------ 208

                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904     332 aaltrafrahtadtafCTLGAVKSNIGHLDAAAGVAGVIKTVQALRHRLIPPTLHFERPNPALHLEQSPFFVNTQPLPWE 411
Cdd:smart00825  209 ----------------LLIGSVKSNIGHLEAAAGVAGLIKVVLALKHGVIPPTLHFETPNPHIDLEESPLRVPTELTPWP 272

                           410       420
                    ....*....|....*....|....*.
gi 53747904     412 SPRGPRLAGVSSFGIGGTNAHTLFEE 437
Cdd:smart00825  273 PPGRPRRAGVSSFGFGGTNAHVILEE 298
PRK12467 PRK12467
peptide synthase; Provisional
 2216-3214 1.04e-132

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 471.18  E-value: 1.04e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2216 LEVERFIQCWRQLLQRHDMLRMVVLPDG---RQQVLEQVPeYTPEVVELRGLSPQEAESRRLQLRERMAHQVLRSDRWPL 2292
Cdd:PRK12467   84 LDVSALRRAFDALVARHESLRTRFVQDEegfRQVIDASLS-LTIPLDDLANEQGRARESQIEAYINEEVARPFDLANGPL 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2293 FELVLCRYEGGVRI-HMSMDALMLDAWSSAVLRQDFAQLY--HEPGR--PLEPLAITFRDYVLAERRLREGEAHERARAY 2367
Cdd:PRK12467  163 LRVRLLRLADDEHVlVVTLHHIISDGWSMRVLVEELVQLYsaYSQGRepSLPALPIQYADYAIWQRSWLEAGERERQLAY 242

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2368 WWARLDTLPPPPELPLVKEPSQLEHARFTHREARLEPHRWARLQERARAHGLTPSAACMAAFAEVLARWSRHPRFTLNLT 2447
Cdd:PRK12467  243 WQEQLGGEHTVLELPTDRPRPAVPSYRGARLRVDLPQALSAGLKALAQREGVTLFMVLLASFQTLLHRYSGQSDIRIGVP 322

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2448 LFQRLplHPQVDELVGDFTSLVLLEVEAHAASTFAE-----RASRLQAQLWRDLEHGS-VSAVQLIRELvrtgrrSPGAI 2521
Cdd:PRK12467  323 NANRN--RVETERLIGFFVNTQVLKAEVDPQASFLEllqqvKRTALGAQAHQDLPFEQlVEALQPERSL------SHSPL 394

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2522 MPVVFTSILSLDARRGPQGS-LSFFEGELVYSISQTPQVWLDHGVHEEEGALVLAWDSVEALFPPGMVDDMFHAYQRLLG 2600
Cdd:PRK12467  395 FQVMFNHQNTATGGRDREGAqLPGLTVEELSWARHTAQFDLALDTYESAQGLWAAFTYATDLFEATTIERLATHWRNLLE 474

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2601 ALAEEEQAWEGELPELLPPAQRELLARYNATQAPRPSGRLEEGFFTQARLHPELPALLAPERTLSYGELARRAQALAARL 2680
Cdd:PRK12467  475 AIVAEPRRRLGELPLLDAEERARELVRWNAPATEYAPDCVHQLIEAQARQHPERPALVFGEQVLSYAELNRQANRLAHVL 554

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2681 RELEVQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLDPEQPPLRLHQLLEEGPARVVLTQSSLLHTVPWPPGVQVIAV 2760
Cdd:PRK12467  555 IAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQSHLLAQLPVPAGLRSLCL 634

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2761 DELEPATEAPP---LPPRGTPEHLAYVIYTSGSTGKPKGVAIEHRAALNTVVDLNTRFGVGPEDRVLGLSALTFDLSVYD 2837
Cdd:PRK12467  635 DEPADLLCGYSghnPEVALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTE 714

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2838 VLGLLGAGGALVLPAAEAEKDPAHWWERLVAGRVTVWNSTPALMLLLVEYAEQrglKLPAALRLVMLSGDWIPVALPDRI 2917
Cdd:PRK12467  715 LFGALASGATLHLLPPDCARDAEAFAALMADQGVTVLKIVPSHLQALLQASRV---ALPRPQRALVCGGEALQVDLLARV 791

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2918 RALGRDVQVVSLGGATEASIWSIAYPIGQVAPQWKSIPYGMPLANQRFHVLDGRLEARPWWVPGELYIGGEGLAREYWRD 2997
Cdd:PRK12467  792 RALGPGARLINHYGPTETTVGVSTYELSDEERDFGNVPIGQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRR 871

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2998 EPLTATRFIRHP--RTGERLYRTGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPALSASVVVARGEPRG 3075
Cdd:PRK12467  872 PALTAERFVPDPfgADGGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAG 951

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  3076 vRRLVAYAVPR---SGQTPAA--GELRRYLAERLPAYMVPSAFVLLESLPRSRNGKIARDQLPEPQQTQGLAAQAAAADP 3150
Cdd:PRK12467  952 -LQLVAYLVPAavaDGAEHQAtrDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPKPDASAVQATFVAPQTE 1030

                         970       980       990      1000      1010      1020
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 53747904  3151 LVERLAALVKEALRLERVEPQDSLLDLGADSVALIRLINRLEAELQFRPRLADIYENPTVQGLA 3214
Cdd:PRK12467 1031 LEKRLAAIWADVLKVERVGLTDNFFELGGHSLLATQVISRVRQRLGIQVPLRTLFEHQTLAGFA 1094
PRK12316 PRK12316
peptide synthase; Provisional
 2211-3214 1.12e-131

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 468.28  E-value: 1.12e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2211 IESPGLEVERFIQCWRQLLQRHDMLRMVVLPDGRQ----QVLEQVPEYTPEVVELRGLSPQEAESRRLQLRERMAHQVLR 2286
Cdd:PRK12316 4131 VDVQGLDVERFRAAWQAALDRHDVLRSGFVWQGELgrplQVVHKQVSLPFAELDWRGRADLQAALDALAAAERERGFDLQ 4210

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2287 sdRWPLFELVLCRY-EGGVRIHMSMDALMLDAWSSAVLRQDFAQLYhePGRPLEPLAITFRDYVLAERRlregEAHERAR 2365
Cdd:PRK12316 4211 --RAPLLRLVLVRTaEGRHHLIYTNHHILMDGWSNSQLLGEVLERY--SGRPPAQPGGRYRDYIAWLQR----QDAAASE 4282

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2366 AYWWARL-DTLPPPPELPLVKEPSQLEHARFTHREARLEPHRWARLQERARAHGLTPSAACMAAFAEVLARWSRHPRFTL 2444
Cdd:PRK12316 4283 AFWREQLaALDEPTRLAQAIARADLRSANGYGEHVRELDATATARLREFARTQRVTLNTLVQAAWLLLLQRYTGQDTVAF 4362

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2445 NLTLFQRLPLHPQVDELVGDFTSLVLLEVEAHAASTFAERASRLQAQ--LWRDLEHGSVSAVQlirelvrtgrRSPGAIM 2522
Cdd:PRK12316 4363 GATVAGRPAELPGIEGQIGLFINTLPVIATPRAQQSVVEWLQQVQRQnlALREHEHTPLYEIQ----------RWAGQGG 4432

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2523 PVVFTSILSLDA-------RRGPQGSLSFFEgelVYSISQTP-QVWLDHGVHEeegALVLAWDSVEALFPPGMVDDMFHA 2594
Cdd:PRK12316 4433 EALFDSLLVFENypvsealQQGAPGGLRFGE---VTNHEQTNyPLTLAVGLGE---TLSLQFSYDRGHFDAATIERLARH 4506

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2595 YQRLLGALAEEEQAWEGELPELLPPAQRELLARYNATQAPRPSGR-LEEGFFTQARLHPELPALLAPERTLSYGELARRA 2673
Cdd:PRK12316 4507 LTNLLEAMAEDPQRRLGELQLLEKAEQQRIVALWNRTDAGYPATRcVHQLVAERARMTPDAVAVVFDEEKLTYAELNRRA 4586

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2674 QALAARLRELEVQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLDPEQPPLRLHQLLEEGPARVVLTQSSLLHTVPWPP 2753
Cdd:PRK12316 4587 NRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALLLTQSHLLQRLPIPD 4666

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2754 GVQVIAVDELEPATEAPPLPP--RGTPEHLAYVIYTSGSTGKPKGVAIEHRAALNTVVDLNTRFGVGPEDRVLGLSALTF 2831
Cdd:PRK12316 4667 GLASLALDRDEDWEGFPAHDPavRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSF 4746

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2832 DLSVYDVLGLLGAGGALVLPAAEAEkDPAHWWERLVAGRVTVWNSTPALMLLLVEYAEQRGlkLPAALRLVMLSGDWIPV 2911
Cdd:PRK12316 4747 DGSHEGLYHPLINGASVVIRDDSLW-DPERLYAEIHEHRVTVLVFPPVYLQQLAEHAERDG--EPPSLRVYCFGGEAVAQ 4823

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2912 ALPDRIRALGRDVQVVSLGGATEASIWSIAYPI-GQVAPQWKSIPYGMPLANQRFHVLDGRLEARPWWVPGELYIGGEGL 2990
Cdd:PRK12316 4824 ASYDLAWRALKPVYLFNGYGPTETTVTVLLWKArDGDACGAAYMPIGTPLGNRSGYVLDGQLNPLPVGVAGELYLGGEGV 4903

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2991 AREYWRDEPLTATRFIRHP--RTGERLYRTGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPALSASVVV 3068
Cdd:PRK12316 4904 ARGYLERPALTAERFVPDPfgAPGGRLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVI 4983

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  3069 ARGEPRGvRRLVAYAVPR--------SGQTPAAGELRRYLAERLPAYMVPSAFVLLESLPRSRNGKIARDQLPEPQQTQG 3140
Cdd:PRK12316 4984 AQEGAVG-KQLVGYVVPQdpaladadEAQAELRDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKALPQPDASLL 5062

                         970       980       990      1000      1010      1020      1030
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 53747904  3141 LAAQAAAADPLVERLAALVKEALRLERVEPQDSLLDLGADSVALIRLINRLEAELQFRPRLADIYENPTVQGLA 3214
Cdd:PRK12316 5063 QQAYVAPRSELEQQVAAIWAEVLQLERVGLDDNFFELGGHSLLAIQVTSRIQLELGLELPLRELFQTPTLAAFV 5136
PRK12316 PRK12316
peptide synthase; Provisional
 2017-3216 2.52e-131

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 467.13  E-value: 2.52e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2017 PRLAGGISSEEGAEAF---LRALEQGAPQLIISPQDFSSLLRGLGGSQGVREKERLVTGRAAAAEPQALPPSS-LEQLIE 2092
Cdd:PRK12316 2443 KQLVAYVVPDDAAEDLlaeLRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPKPDVSQLRQAYVAPQEgLEQRLA 2522

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2093 QVWRKHLGVERVQPTDSFFQLGGDSLLGIQVAADLRRHLGVELPTATLFSHPTLAALAAALRARQgeaaaptaPAPALVP 2172
Cdd:PRK12316 2523 AIWQAVLKVEQVGLDDHFFELGGHSLLATQVVSRVRQDLGLEVPLRILFERPTLAAFAASLESGQ--------TSRAPVL 2594

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2173 DPAARFEPFPLTDVQEAYWVGRRsaFELGGVAAHGYFEIESPG-LEVERFIQCWRQLLQRHDMLRMVVLPDGrqqvlEQV 2251
Cdd:PRK12316 2595 QKVTRVQPLPLSHAQQRQWFLWQ--LEPESAAYHLPSALHLRGvLDQAALEQAFDALVLRHETLRTRFVEVG-----EQT 2667

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2252 PEYTPEVVELRGLSPQEAESRRLQLRERMAHQVLRS---DRWPLFELVLCRYEGGV-RIHMSMDALMLDAWSSAVLRQDF 2327
Cdd:PRK12316 2668 RQVILPNMSLRIVLEDCAGVADAAIRQRVAEEIQRPfdlARGPLLRVRLLALDGQEhVLVITQHHIVSDGWSMQVMVDEL 2747

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2328 AQLYHEPGR----PLEPLAITFRDYVLAERRLREGEAHERARAYWWARLDTLPPPPELPLVKEPSQLEHARFTHREARLE 2403
Cdd:PRK12316 2748 VQAYAGARRgeqpTLPPLPLQYADYAAWQRAWMDSGEGARQLDYWRERLGGEQPVLELPLDRPRPALQSHRGARLDVALD 2827

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2404 PHRWARLQERARAHGLTPSAACMAAFAEVLARWSRHPRFTLNLTLFQRLplHPQVDELVGDFTSLVLLEVEAHAASTFAE 2483
Cdd:PRK12316 2828 VALSRELLALARREGVTLFMLLLASFQVLLHRYSGQSDIRVGVPIANRN--RAETERLIGFFVNTQVLRAQVDAQLAFRD 2905

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2484 RASRLQAQLWRDLEHGSVSAVQLIRELVRTGRRSPGAIMPVVFTSILSLDArrgpQGSLSFFEGELVYSISQTPQVWLDH 2563
Cdd:PRK12316 2906 LLGQVKEQALGAQAHQDLPFEQLVEALQPERSLSHSPLFQVMYNHQSGERA----AAQLPGLHIESFAWDGAATQFDLAL 2981

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2564 GVHEEEGALVLAWDSVEALFPPGMVDDMFHAYQRLLGALAEEEQAWEGELPELLPPAQRELLARYNATQAPRPSGR-LEE 2642
Cdd:PRK12316 2982 DTWESAEGLGASLTYATDLFDARTVERLARHWQNLLRGMVENPQRSVDELAMLDAEERGQLLEAWNATAAEYPLERgVHR 3061

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2643 GFFTQARLHPELPALLAPERTLSYGELARRAQALAARLRELEVQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLDPEQ 2722
Cdd:PRK12316 3062 LFEEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEY 3141

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2723 PPLRLHQLLEEGPARVVLTQSSLlhTVPWPPGVQVIAVDELEPATEAPPLPPRGTPEHLAYVIYTSGSTGKPKGVAIEHR 2802
Cdd:PRK12316 3142 PEERLAYMLEDSGAQLLLSQSHL--RLPLAQGVQVLDLDRGDENYAEANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHS 3219

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2803 AALNTVVDLNTRFGVGPEDRVLGLSALTFDLSVYDVLGLLGAGGALVLPAAEAEKDPAHWWERLvagRVTVWNSTPALML 2882
Cdd:PRK12316 3220 ALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDPALLVELI---NSEGVDVLHAYPS 3296

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2883 LLVEYAEQRGLKLPAALRLVMLSGDWIPVALPDRIRALGrdvQVVSLGGATEASIWSIAYPIgqVAPQWKSIPYGMPLAN 2962
Cdd:PRK12316 3297 MLQAFLEEEDAHRCTSLKRIVCGGEALPADLQQQVFAGL---PLYNLYGPTEATITVTHWQC--VEEGKDAVPIGRPIAN 3371

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2963 QRFHVLDGRLEARPWWVPGELYIGGEGLAREYWRDEPLTATRFIRHP-RTGERLYRTGDQGRMLPEGSIEFLGREDLQVK 3041
Cdd:PRK12316 3372 RACYILDGSLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPfVPGERLYRTGDLARYRADGVIEYIGRVDHQVK 3451

                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  3042 VQGFRVELGEIEAALAQHPALSASVVVARGEprgvRRLVAYAVPRSGQTPAAGELRRYLAERLPAYMVPSAFVLLESLPR 3121
Cdd:PRK12316 3452 IRGFRIELGEIEARLLEHPWVREAVVLAVDG----RQLVAYVVPEDEAGDLREALKAHLKASLPEYMVPAHLLFLERMPL 3527

                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  3122 SRNGKIARDQLPEPQQTQGLAAQAAAADPLVERLAALVKEALRLERVEPQDSLLDLGADSVALIRLINRL-EAELQFRPR 3200
Cdd:PRK12316 3528 TPNGKLDRKALPRPDAALLQQDYVAPVNELERRLAAIWADVLKLEQVGLTDNFFELGGDSIISLQVVSRArQAGIRFTPK 3607

                        1210
                  ....*....|....*.
gi 53747904  3201 laDIYENPTVQGLATL 3216
Cdd:PRK12316 3608 --DLFQHQTIQGLARV 3621
PRK12316 PRK12316
peptide synthase; Provisional
 2228-3225 7.37e-125

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 445.94  E-value: 7.37e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2228 LLQRHDMLRmVVLPDGRQQVLEQVPEYTPEVVELRGLSPQEAESRRLQLRERMAHQVLRS---DRWPLFELVLCRYEGGV 2304
Cdd:PRK12316   96 LVQRHETLR-TVFPRGADDSLAQVPLDRPLEVEFEDCSGLPEAEQEARLRDEAQRESLQPfdlCEGPLLRVRLLRLGEEE 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2305 RI-HMSMDALMLDAWSSAVLRQDFAQLY--HEPGRP--LEPLAITFRDYVLAERRLREGEAHERARAYWWARLDTLPPPP 2379
Cdd:PRK12316  175 HVlLLTLHHIVSDGWSMNVLIEEFSRFYsaYATGAEpgLPALPIQYADYALWQRSWLEAGEQERQLEYWRAQLGEEHPVL 254

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2380 ELPLVKEPSQLEHARFTHREARLEPHRWARLQERARAHGLTPSAACMAAFAEVLARWSRHPRFTLNLTLFQRLplHPQVD 2459
Cdd:PRK12316  255 ELPTDHPRPAVPSYRGSRYEFSIDPALAEALRGTARRQGLTLFMLLLGAFNVLLHRYSGQTDIRVGVPIANRN--RAEVE 332

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2460 ELVGDFTSLVLLEVEAHAASTFAE-----RASRLQAQLWRDLEHGS-VSAVQLIRELVRTgrrspgaimPV--VFTSILS 2531
Cdd:PRK12316  333 GLIGFFVNTQVLRSVFDGRTRVATllagvKDTVLGAQAHQDLPFERlVEALKVERSLSHS---------PLfqVMYNHQP 403

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2532 LDARRGPQGSLSFFEGELVYSISQTPQVWLDHGVHEEEGALVLAWDSVEALFPPGMVDDMFHAYQRLLGALAEEEQAWEG 2611
Cdd:PRK12316  404 LVADIEALDTVAGLEFGQLEWKSRTTQFDLTLDTYEKGGRLHAALTYATDLFEARTVERMARHWQNLLRGMVENPQARVD 483

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2612 ELPELLPPAQRELLARYNATQAPRPSGR-LEEGFFTQARLHPELPALLAPERTLSYGELARRAQALAARLRELEVQPQEL 2690
Cdd:PRK12316  484 ELPMLDAEERGQLVEGWNATAAEYPLQRgVHRLFEEQVERTPEAPALAFGEETLDYAELNRRANRLAHALIERGVGPDVL 563

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2691 VAIAMHKGWEQATAVLGVLQAAAAYLPLDPEQPPLRLHQLLEEGPARVVLTQSSLLHTVPWPPGVQVIAVDELEPATEAP 2770
Cdd:PRK12316  564 VGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQSHLGRKLPLAAGVQVLDLDRPAAWLEGY 643

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2771 PLPPRGT---PEHLAYVIYTSGSTGKPKGVAIEHRAALNTVVDLNTRFGVGPEDRVLGLSALTFDLSVYDVLGLLGAGGA 2847
Cdd:PRK12316  644 SEENPGTelnPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGAR 723

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2848 LVLPAAEAEKDPAHWWERLVAGRVTVWNSTPALMLLLVEYAeqrGLKLPAALRLVMLSGDWIPVALPDRIRALGRDVQVV 2927
Cdd:PRK12316  724 LVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDE---DVASCTSLRRIVCSGEALPADAQEQVFAKLPQAGLY 800

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2928 SLGGATEASI----WSIAYPIGqvapqwKSIPYGMPLANQRFHVLDGRLEARPWWVPGELYIGGEGLAREYWRDEPLTAT 3003
Cdd:PRK12316  801 NLYGPTEAAIdvthWTCVEEGG------DSVPIGRPIANLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAE 874

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  3004 RFIRHP-RTGERLYRTGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPALSASVVVARGEprgvRRLVAY 3082
Cdd:PRK12316  875 RFVPSPfVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDG----KQLVGY 950

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  3083 AVPRSGQTPAAGELRRYLAERLPAYMVPSAFVLLESLPRSRNGKIARDQLPEPQQTQGLAAQAAAADPLVERLAALVKEA 3162
Cdd:PRK12316  951 VVLESEGGDWREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKALPAPEASVAQQGYVAPRNALERTLAAIWQDV 1030

                         970       980       990      1000      1010      1020
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 53747904  3163 LRLERVEPQDSLLDLGADSVALIRLINRL-EAELQFRPRlaDIYENPTVQGL---ATLHQEKTKSQG 3225
Cdd:PRK12316 1031 LGVERVGLDDNFFELGGDSIVSIQVVSRArQAGIQLSPR--DLFQHQTIRSLalvAKAGQATAADQG 1095
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
2179-3255 1.37e-123

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 426.00  E-value: 1.37e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2179 EPFPLTDVQEAYWVGRRSAFELGGVAAHGYFEIESPgLEVERFIQCWRQLLQRHDMLRM--VVLPDGRQQVL-EQVPEYT 2255
Cdd:PRK10252    6 QHLPLVAAQPGIWMAEKLSPLPSAWSVAHYVELTGE-LDAPLLARAVVAGLAEADTLRMrfTEDNGEVWQWVdPALTFPL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2256 PEVVELRGLSPQEAESRRLQLRERMahQVLRSDRW-PLFELVLCR--------YEggvRIHMsmdaLMLDAWSSAVLRQD 2326
Cdd:PRK10252   85 PEIIDLRTQPDPHAAAQALMQADLQ--QDLRVDSGkPLVFHQLIQlgdnrwywYQ---RYHH----LLVDGFSFPAITRR 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2327 FAQLYHEPGRPLEPLAITFRDY--VLAE-RRLREGEAHERARAYWWARLdtlppppelPLVKEPSQLEHARFTHREARLE 2403
Cdd:PRK10252  156 IAAIYCAWLRGEPTPASPFTPFadVVEEyQRYRASEAWQRDAAFWAEQR---------RQLPPPASLSPAPLPGRSASAD 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2404 PHRWARL-------QERARAHGLTPSAACMAAFAEVLARWSRHPRFTLNLTLFQRLplhpqvDELVGDFTSLVL----LE 2472
Cdd:PRK10252  227 ILRLKLEftdgafrQLAAQASGVQRPDLALALVALWLGRLCGRMDYAAGFIFMRRL------GSAALTATGPVLnvlpLR 300

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2473 VEAHAASTFAERASRLQAQLWRDLEHGSVSAVQLIRELVRTG--RRSPGAIMPV-VFTSILSLDarrGPQGSLsffegel 2549
Cdd:PRK10252  301 VHIAAQETLPELATRLAAQLKKMRRHQRYDAEQIVRDSGRAAgdEPLFGPVLNIkVFDYQLDFP---GVQAQT------- 370

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2550 vYSISQTPQVWLDHGVH-EEEGALVLAWDSVEALFPPGMVDDMFHAYQRLLGALAEEEQAWEGELPeLLPPAQRELLARY 2628
Cdd:PRK10252  371 -HTLATGPVNDLELALFpDEHGGLSIEILANPQRYDEATLIAHAERLKALIAQFAADPALLCGDVD-ILLPGEYAQLAQV 448

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2629 NATQAPRPSGRLEEGFFTQARLHPELPALLAPERTLSYGELARRAQALAARLRELEVQPQELVAIAMHKGWEQATAVLGV 2708
Cdd:PRK10252  449 NATAVEIPETTLSALVAQQAAKTPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAI 528

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2709 LQAAAAYLPLDPEQPPLRLHQLLEEGPARVVLTQSSLLHTVPWPPGVQVIAVDELEPATEAPPLpPRGTPEHLAYVIYTS 2788
Cdd:PRK10252  529 VEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTADQLPRFADVPDLTSLCYNAPLAPQGAAPL-QLSQPHHTAYIIFTS 607

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2789 GSTGKPKGVAIEHRAALNTVVDLNTRFGVGPEDRVLGLSALTFDLSVYDVLGLLGAGGALVLPAAEAEKDPAhWWERLVA 2868
Cdd:PRK10252  608 GSTGRPKGVMVGQTAIVNRLLWMQNHYPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPL-AMQQFFA 686

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2869 G-RVTVWNSTPALMLLLVEYAEQRGLKLP-AALRLVMLSGDWIPVALPDRIRALgRDVQVVSLGGATEASI---WSIAYP 2943
Cdd:PRK10252  687 EyGVTTTHFVPSMLAAFVASLTPEGARQScASLRQVFCSGEALPADLCREWQQL-TGAPLHNLYGPTEAAVdvsWYPAFG 765

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2944 IGQVAPQWKSIPYGMPLANQRFHVLDGRLEARPWWVPGELYIGGEGLAREYWRDEPLTATRFIRHP-RTGERLYRTGDQG 3022
Cdd:PRK10252  766 EELAAVRGSSVPIGYPVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPfAPGERMYRTGDVA 845

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  3023 RMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPALSASVVVAR------GEPRGVRRLVAYAVPRSGQTPAAGEL 3096
Cdd:PRK10252  846 RWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVTHACvinqaaATGGDARQLVGYLVSQSGLPLDTSAL 925

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  3097 RRYLAERLPAYMVPSAFVLLESLPRSRNGKIARDQLPEPQQTQGLAAQAAAAdPLVERLAALVKEALRLERVEPQDSLLD 3176
Cdd:PRK10252  926 QAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKALPLPELKAQVPGRAPKT-GTETIIAAAFSSLLGCDVVDADADFFA 1004

                        1050      1060      1070      1080      1090      1100      1110
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 53747904  3177 LGADSVALIRLINRLEAELQFRPRLADIYENPTVQGLATLHQEKTKSQGEGGAprltaprSTLLPAEEwgrfkANRPGL 3255
Cdd:PRK10252 1005 LGGHSLLAMKLAAQLSRQFARQVTPGQVMVASTVAKLATLLDAEEDESRRLGF-------GTILPLRE-----GDGPTL 1071
mycolic_Pks13 NF040607
polyketide synthase Pks13;
13-884 8.81e-123

polyketide synthase Pks13;


Pssm-ID: 468580 [Multi-domain]  Cd Length: 1671  Bit Score: 430.88  E-value: 8.81e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904    13 IALVGMAGRFPGA-PDVESFWRNLVAGVESISFFSEEELRQAGVSEQIRRRPEYVPAKG-VLEDLELFDAGFFGYSPREA 90
Cdd:NF040607  102 IAIVGLATRFPGAgNTPEEMWEALIEGRDGITDLPEGRWSEFAADPRIAERVAKANTRGgYLDDIKGFDAEFFALSPLEA 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904    91 SHLDPQQRLLLECSWEALEDAGLRPDQLPGW-VGVYVGAGDTSYrfQLLRGhGDPlsGSKDVAGFFGNYPDFLATRVAYK 169
Cdd:NF040607  182 ENVDPQQRLALELTWEALEHARIPASSLRGEpVGVFIGSSNNDY--QMLAV-ADP--AEAHPYALTGTSSSIIANRVSYF 256

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   170 LNLRGPALGIHTACSTSLVSINMACSALRGFECDMALAGGVSLRL-PARSGYLYEEGGVASKDGHCRPFDARATGTVTGD 248
Cdd:NF040607  257 FDFRGPSVAVDTACSSSLVAVHQAVRALRSGEADVAVAGGVNMLLtPAVTLGFDELGGVLAPDGRIKAFSSDADGMVRSE 336

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   249 GVGVVVLKRLEDALKARDPIHAVIRGWALNNDGASRaGFTAPSVEGQSEVIALAHAAAGISARDITYVEAHGTGTPLGDP 328
Cdd:NF040607  337 GGGVVVLKRLADARRDGDTILAVIAGSAVNSDGRSN-GLTAPNPDAQVDVLRRAYADAGIDPRTVDYVEAHGTGTILGDP 415

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   329 IEVAALTRAF-RAHTADTAfCTLGAVKSNIGHLDAAAGVAGVIKTVQALRHRLIPPTLHFERPNP-----ALHLEqspff 402
Cdd:NF040607  416 IEADALGRVVgRGRDADKP-ALLGSAKTNFGHLESAAGAAGLAKVVLAMQHDKLPPSLNYAGPNPyidfdAEHLK----- 489

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   403 VNTQPLPWesPR--GPRLAGVSSFGIGGTNAHTLFEEAPPPPASGPTRPNQVLLLSARSTSALEhiAGRLAAHLRRHPDL 480
Cdd:NF040607  490 VVDEPTEW--PRysGHAVAGVSGFGFGGTNAHVVVREVLPADLVEPEAQPDEDTEAELAGLTAE--AKRLLAEAELAAEF 565

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   481 ELA---DVAFTLQVGrARFPYRRALTCRTLAEAMErleapeprppeplAHEGERPPL------------------VM--- 536
Cdd:NF040607  566 APAapeGPVVPLPVS-GFLPSRRRAAAADLADWLE-------------SEEGRATPLadvaralarrnhgrsravVLaht 631

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   537 ----------LFPGQGTPLVGTA-----------------------RALHESEPTFRQAVEQCARLLRQTLGLDVREVLF 583
Cdd:NF040607  632 heeaikglraVAEGKPGPGVFSAdapaangpvwvlsgfgsqhrkmaKQLYLENPVFAARIDEVDELVQDESGYSIVELIL 711

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   584 PSAEQEEqarrlaaqTRVAQPALFTLEYALAQTWLGWGLQPQALAGHSLGELVAACLAGVFSLEDALQLVAARGQLM--- 660
Cdd:NF040607  712 DDEQTYD--------IETAQVGIFAIQIALADLLRHHGAKPAAVVGHSMGEAAAAYAAGGLSLEDAVRVICHRSRLMgeg 783

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   661 ----QGCPPGAMLAVPLPEAELAALLGS----ELCIAAvnGPRACVASGPLPAVEALTAALESRGVSSRRLETSHAFHSA 732
Cdd:NF040607  784 eamlPGDDIRLMALVEYSAEEIETVLADfpdlEVCVYA--APTHTVIGGPREQVDAIVARAEAEGKFARKLQTKGASHTS 861

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   733 SMEACQGPLTTLLRRMRLQAPRLPCVS----GLTGRwlTGEEATEPT-YWARQLREPVRFSEALETLWSLKEPVLLEVGP 807
Cdd:NF040607  862 QMDPLLGELAAELAGIEPQPLTVGLYSsvdrGTFYR--PGHEPIHDVdYWVKGLRHSVWFTQAVRKAVDAGHTTFLELAP 939

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   808 ---------GTTLTA----------LARRHPtrpartqEVASLPvqpdtavpcieEAVGELWQAGLELDWSALhAAPRHR 868
Cdd:NF040607  940 npvalmsvaATTFAAglhdaqliptLKRKED-------ESESVL-----------NALAQLYVHGHDVDLRSL-FGAGDY 1000

                         970
                  ....*....|....*.
gi 53747904   869 AHLPPYPFERQRYWIE 884
Cdd:NF040607 1001 ADIPRTRFKRKPYWLD 1016
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
 2685-3067 2.49e-122

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: 393.55  E-value: 2.49e-122
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   2685 VQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLDPEQPPLRLHQLLEEGPARVVLTQSSLLHTVPW-PPGVQVIAVDEL 2763
Cdd:TIGR01733   22 VGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDSALASRLAGlVLPVILLDPLEL 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   2764 EPATEAPPLPPRGT---PEHLAYVIYTSGSTGKPKGVAIEHRAALNTVVDLNTRFGVGPEDRVLGLSALTFDLSVYDVLG 2840
Cdd:TIGR01733  102 AALDDAPAPPPPDApsgPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDPDDRVLQFASLSFDASVEEIFG 181

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   2841 LLGAGGALVLPAAEAEKDPAHWWERLVA-GRVTVWNSTPALMLLLVEYAEQRglklPAALRLVMLSGDWIPVALPDRIRA 2919
Cdd:TIGR01733  182 ALLAGATLVVPPEDEERDDAALLAALIAeHPVTVLNLTPSLLALLAAALPPA----LASLRLVILGGEALTPALVDRWRA 257

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   2920 LGRDVQVVSLGGATEASIWSIAYPI-GQVAPQWKSIPYGMPLANQRFHVLDGRLEARPWWVPGELYIGGEGLAREYWRDE 2998
Cdd:TIGR01733  258 RGPGARLINLYGPTETTVWSTATLVdPDDAPRESPVPIGRPLANTRLYVLDDDLRPVPVGVVGELYIGGPGVARGYLNRP 337

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 53747904   2999 PLTATRFIRHP---RTGERLYRTGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPALSASVV 3067
Cdd:TIGR01733  338 ELTAERFVPDPfagGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
PRK12467 PRK12467
peptide synthase; Provisional
 2215-3214 4.51e-120

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 429.58  E-value: 4.51e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2215 GLEVERFIQCWRQLLQRHDMLRMVVLPDGRQQVLEQV--PEYTPEVVEL----RGLSPQEAESrrLQLRERMAHQVLRSD 2288
Cdd:PRK12467 2679 GLDVERFRTAWQAVIDRHEILRSGFLWDGELEEPLQVvyKQARLPFSRLdwrdRADLEQALDA--LAAADRQQGFDLLSA 2756

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2289 rwPLFELVLCRYeGGVRIHM--SMDALMLDAWSSAVLRQDFAQLYHepGRPLEPLAITFRDYVLAERRlregEAHERARA 2366
Cdd:PRK12467 2757 --PLLRLTLVRT-GEDRHHLiyTNHHILMDGWSGSQLLGEVLQRYF--GQPPPAREGRYRDYIAWLQA----QDAEASEA 2827

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2367 YWWARLdtlppppelPLVKEPSQLEHArFTHREAR-----------LEPHRWARLQERARAHGLTPSAACMAAFAEVLAR 2435
Cdd:PRK12467 2828 FWKEQL---------AALEEPTRLARA-LYPAPAEavaghgahylhLDATQTRQLIEFARRHRVTLNTLVQGAWLLLLQR 2897

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2436 WSRHPRFTLNLTLFQRLPLHPQVDELVGDFTSLVLLEVEAHAASTFAERASRLQAQ--LWRDLEHGSVSAVQlirelvrt 2513
Cdd:PRK12467 2898 FTGQDTVCFGATVAGRPAQLRGAEQQLGLFINTLPVIASPRAEQTVSDWLQQVQAQnlALREFEHTPLADIQ-------- 2969

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2514 grRSPGAIMPVVFTSILSLD----ARRGPQGSLSFFEGELVYSISQTpQVWLDHGVHEEEgALVLAWDSVEALFPPGMVD 2589
Cdd:PRK12467 2970 --RWAGQGGEALFDSILVFEnypiSEALKQGAPSGLRFGAVSSREQT-NYPLTLAVGLGD-TLELEFSYDRQHFDAAAIE 3045

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2590 DMFHAYQRLLGALAEEEQAWEGELPELLPPAQRELLARYNATQAPRPSGRL-EEGFFTQARLHPELPALLAPERTLSYGE 2668
Cdd:PRK12467 3046 RLAESFDRLLQAMLNNPAARLGELPTLAAHERRQVLHAWNATAAAYPSERLvHQLIEAQVARTPEAPALVFGDQQLSYAE 3125

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2669 LARRAQALAARLRELEVQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLDPEQPPLRLHQLLEEGPARVVLTQSSLLHT 2748
Cdd:PRK12467 3126 LNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQAHLLEQ 3205

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2749 VPWPPGVQVIAVDELEPATEAPPLP-PRGTPEHLAYVIYTSGSTGKPKGVAIEHRAALNTVVDLNTRFGVGPEDRVLGLS 2827
Cdd:PRK12467 3206 LPAPAGDTALTLDRLDLNGYSENNPsTRVMGENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFM 3285

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2828 ALTFDLSVYDVLGLLGAGGALVLpAAEAEKDPAHWWERLVAGRVTVWNSTPALMLLLVEYAEQRGLklpAALRLVMLSGD 2907
Cdd:PRK12467 3286 SFSFDGAQERFLWTLICGGCLVV-RDNDLWDPEELWQAIHAHRISIACFPPAYLQQFAEDAGGADC---ASLDIYVFGGE 3361

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2908 WIPVALPDRIRALGRDVQVVSLGGATEASIWSIAYPIGQVA-PQWKSIPYGMPLANQRFHVLDGRLEARPWWVPGELYIG 2986
Cdd:PRK12467 3362 AVPPAAFEQVKRKLKPRGLTNGYGPTEAVVTVTLWKCGGDAvCEAPYAPIGRPVAGRSIYVLDGQLNPVPVGVAGELYIG 3441

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2987 GEGLAREYWRDEPLTATRFIRHP--RTGERLYRTGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPALSA 3064
Cdd:PRK12467 3442 GVGLARGYHQRPSLTAERFVADPfsGSGGRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVRE 3521

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  3065 SVVVARGEPRGvRRLVAYAVPRSGQTPAAGELRRYLAERLPAYMVPSAFVLLESLPRSRNGKIARDQLPEPQQTQGLAAQ 3144
Cdd:PRK12467 3522 AVVLARDGAGG-KQLVAYVVPADPQGDWRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDPDAKGSREYV 3600

                         970       980       990      1000      1010      1020      1030
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  3145 AAAADpLVERLAALVKEALRLERVEPQDSLLDLGADSVALIRLINRLEAELQFRPRLADIYENPTVQGLA 3214
Cdd:PRK12467 3601 APRSE-VEQQLAAIWADVLGVEQVGVTDNFFELGGDSLLALQVLSRIRQSLGLKLSLRDLMSAPTIAELA 3669
A_NRPS_AB3403-like cd17646
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ...
 2642-3132 8.37e-120

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: 389.33  E-value: 8.37e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2642 EGFFTQARLHPELPALLAPERTLSYGELARRAQALAARLRELEVQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLDPE 2721
Cdd:cd17646    2 ALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2722 QPPLRLHQLLEEGPARVVLTQSSLlhtVPWPPGVQVIAVDELEPATEAPPLPPRGT--PEHLAYVIYTSGSTGKPKGVAI 2799
Cdd:cd17646   82 YPADRLAYMLADAGPAVVLTTADL---AARLPAGGDVALLGDEALAAPPATPPLVPprPDNLAYVIYTSGSTGRPKGVMV 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2800 EHRAALNTVVDLNTRFGVGPEDRVLGLSALTFDLSVYDVLGLLGAGGALVLPAAEAEKDPAHWWERLVAGRVTVWNSTPA 2879
Cdd:cd17646  159 THAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDPAYLAALIREHGVTTCHFVPS 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2880 LMLLLVEYAEQRGLklpAALRLVMLSGDWIPVALPDRIRALGrDVQVVSLGGATEASIWSIAYPIGQVAPQwKSIPYGMP 2959
Cdd:cd17646  239 MLRVFLAEPAAGSC---ASLRRVFCSGEALPPELAARFLALP-GAELHNLYGPTEAAIDVTHWPVRGPAET-PSVPIGRP 313

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2960 LANQRFHVLDGRLEARPWWVPGELYIGGEGLAREYWRDEPLTATRFIRHP-RTGERLYRTGDQGRMLPEGSIEFLGREDL 3038
Cdd:cd17646  314 VPNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPfGPGSRMYRTGDLARWRPDGALEFLGRSDD 393

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3039 QVKVQGFRVELGEIEAALAQHPALSASVVVARGEPRGVRRLVAYAVPRSGQT-PAAGELRRYLAERLPAYMVPSAFVLLE 3117
Cdd:cd17646  394 QVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAGAAgPDTAALRAHLAERLPEYMVPAAFVVLD 473

                        490
                 ....*....|....*
gi 53747904 3118 SLPRSRNGKIARDQL 3132
Cdd:cd17646  474 ALPLTANGKLDRAAL 488
PRK12316 PRK12316
peptide synthase; Provisional
 2215-3214 1.13e-118

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 425.53  E-value: 1.13e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2215 GLEVERFIQCWRQLLQRHDMLRMVV-----LPDGRQQVLEQVpEYTPEVVELRGLSPQEAESRRLQLRERMAHQVLrsDR 2289
Cdd:PRK12316 1589 GLDPDRFRAAWQATVDRHEILRSGFlwqdgLEQPLQVIHKQV-ELPFAELDWRGREDLGQALDALAQAERQKGFDL--TR 1665

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2290 WPLFELVLCRyEGGVRIHM--SMDALMLDAWSSAVLRQDFAQLYhePGRPLEPLAITFRDYV--LAERRLREGEAherar 2365
Cdd:PRK12316 1666 APLLRLVLVR-TGEGRHHLiyTNHHILMDGWSNAQLLGEVLQRY--AGQPVAAPGGRYRDYIawLQRQDAAASEA----- 1737

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2366 aYWWARLdtlppppelPLVKEPSQLEHARFTHREAR--------LEPHRWARLQERARAHGLTPSAACMAAFAEVLARWS 2437
Cdd:PRK12316 1738 -FWKEQL---------AALEEPTRLAQAARTEDGQVgygdhqqlLDPAQTRALAEFARAQKVTLNTLVQAAWLLLLQRYT 1807

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2438 RHPRFTLNLTLFQRLPLHPQVDELVGDFTSLVLLEVEAHAASTFAERASRLQAQ--LWRDLEHGSVSAVQlirelvrtgr 2515
Cdd:PRK12316 1808 GQETVAFGATVAGRPAELPGIEQQIGLFINTLPVIAAPRPDQSVADWLQEVQALnlALREHEHTPLYDIQ---------- 1877

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2516 RSPGAIMPVVFTSILSLD-------ARRGPQGSLSFFEgelVYSISQTpQVWLDHGVHEEEgALVLAWDSVEALFPPGMV 2588
Cdd:PRK12316 1878 RWAGQGGEALFDSLLVFEnypvaeaLKQGAPAGLVFGR---VSNHEQT-NYPLTLAVTLGE-TLSLQYSYDRGHFDAAAI 1952

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2589 DDMFHAYQRLLGALAEEEQAWEGELPELLPPAQRELLARYNATQAPRPSG-RLEEGFFTQARLHPELPALLAPERTLSYG 2667
Cdd:PRK12316 1953 ERLDRHLLHLLEQMAEDAQAALGELALLDAGERQRILADWDRTPEAYPRGpGVHQRIAEQAARAPEAIAVVFGDQHLSYA 2032

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2668 ELARRAQALAARLRELEVQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLDPEQPPLRLHQLLEEGPARVVLTQSSLLH 2747
Cdd:PRK12316 2033 ELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQRHLLE 2112

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2748 TVPWPPGVQVIAVDELEPATEAPPLPP--RGTPEHLAYVIYTSGSTGKPKGVAIEHRAALNTVVDLNTRFGVGPEDRVLG 2825
Cdd:PRK12316 2113 RLPLPAGVARLPLDRDAEWADYPDTAPavQLAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCELQ 2192

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2826 LSALTFDLSVYDVLGLLGAGGALVLPAAEaEKDPAHWWERLVAGRVTVWNSTPALMLLLVEYAEQRGlkLPAALRLVMLS 2905
Cdd:PRK12316 2193 FMSFSFDGAHEQWFHPLLNGARVLIRDDE-LWDPEQLYDEMERHGVTILDFPPVYLQQLAEHAERDG--RPPAVRVYCFG 2269

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2906 GDWIPVALPDRIRALGRDVQVVSLGGATEASIWSIAYPIG-QVAPQWKSIPYGMPLANQRFHVLDGRLEARPWWVPGELY 2984
Cdd:PRK12316 2270 GEAVPAASLRLAWEALRPVYLFNGYGPTEAVVTPLLWKCRpQDPCGAAYVPIGRALGNRRAYILDADLNLLAPGMAGELY 2349

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2985 IGGEGLAREYWRDEPLTATRFIRHP--RTGERLYRTGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPAL 3062
Cdd:PRK12316 2350 LGGEGLARGYLNRPGLTAERFVPDPfsASGERLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAV 2429

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  3063 SASVVVARGEPRGvRRLVAYAVPRSGQTPAAGELRRYLAERLPAYMVPSAFVLLESLPRSRNGKIARDQLPEPQQTQGLA 3142
Cdd:PRK12316 2430 REAVVVAQDGASG-KQLVAYVVPDDAAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPKPDVSQLRQ 2508

                         970       980       990      1000      1010      1020      1030
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 53747904  3143 AQAAAADPLVERLAALVKEALRLERVEPQDSLLDLGADSVALIRLINRLEAELQFRPRLADIYENPTVQGLA 3214
Cdd:PRK12316 2509 AYVAPQEGLEQRLAAIWQAVLKVEQVGLDDHFFELGGHSLLATQVVSRVRQDLGLEVPLRILFERPTLAAFA 2580
PRK05691 PRK05691
peptide synthase; Validated
 2072-3190 2.29e-118

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 424.20  E-value: 2.29e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2072 GRAAAAEPQALPPSSLEQLIEQVWRKHLGVERVQPTDSFFQLGGDSLLGIQVAADLRRHLGVELPTATLFSHPTLAALAA 2151
Cdd:PRK05691  572 LQAVEAAQTAASGDELQARIAAIWCEQLKVEQVAADDHFFLLGGNSIAATQVVARLRDELGIDLNLRQLFEAPTLAAFSA 651

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2152 ALRARQGEAAAPTAPAPALvpdpaARFEPFPLTDVQEAYWV-----GRRSAFEL-GGVAAHGyfEIESPGLEverfiQCW 2225
Cdd:PRK05691  652 AVARQLAGGGAAQAAIARL-----PRGQALPQSLAQNRLWLlwqldPQSAAYNIpGGLHLRG--ELDEAALR-----ASF 719

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2226 RQLLQRHDMLRMVVLP-DGR--QQVLEQvPEYTPEVVELRGLSPQEAESRRLQLRERMAHQVLRSDRWPLFELVLCRY-E 2301
Cdd:PRK05691  720 QRLVERHESLRTRFYErDGValQRIDAQ-GEFALQRIDLSDLPEAEREARAAQIREEEARQPFDLEKGPLLRVTLVRLdD 798

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2302 GGVRIHMSMDALMLDAWSSAVLRQDFAQLYHEP--GRPLE--PLAITFRDYVLAERR-LREGEAhERARAYWWARL-DTL 2375
Cdd:PRK05691  799 EEHQLLVTLHHIVADGWSLNILLDEFSRLYAAAcqGQTAElaPLPLGYADYGAWQRQwLAQGEA-ARQLAYWKAQLgDEQ 877

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2376 PPPPELPLVKEPSQLEH--ARFThreARLEPHRWARLQERARAHGLTPSAACMAAFAEVLARWSRHPRFTLNLTLFQRLP 2453
Cdd:PRK05691  878 PVLELATDHPRSARQAHsaARYS---LRVDASLSEALRGLAQAHQATLFMVLLAAFQALLHRYSGQGDIRIGVPNANRPR 954

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2454 LHPQvdELVGDFTSLVLLEVEAHAASTFAE-----RASRLQAQLWRDLEHGsvsavQLIRELVRTGRRSPGAIMpvvfts 2528
Cdd:PRK05691  955 LETQ--GLVGFFINTQVLRAQLDGRLPFTAllaqvRQATLGAQAHQDLPFE-----QLVEALPQAREQGLFQVM------ 1021

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2529 ilsLDARRGPQGSLSFFEGELVYSIS-QTPQVWLDHGVHEEE---GALVLAWDSVEALFPPGMVDDMFHAYQRLLGALAE 2604
Cdd:PRK05691 1022 ---FNHQQRDLSALRRLPGLLAEELPwHSREAKFDLQLHSEEdrnGRLTLSFDYAAELFDAATIERLAEHFLALLEQVCE 1098

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2605 EEQAWEGELpELLPPAQRELLARYNATQAPRPSGRLEEGFFTQARLHPELPALLAPERTLSYGELARRAQALAARLRELE 2684
Cdd:PRK05691 1099 DPQRALGDV-QLLDAAERAQLAQWGQAPCAPAQAWLPELLNEQARQTPERIALVWDGGSLDYAELHAQANRLAHYLRDKG 1177

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2685 VQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLDPEQPPLRLHQLLEEGPARVVLTQSSLLHTVPWPPGVQVIAVDELE 2764
Cdd:PRK05691 1178 VGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQSHLLERLPQAEGVSAIALDSLH 1257

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2765 PA---TEAPPLPPRGtpEHLAYVIYTSGSTGKPKGVAIEHRAALNTVVDLNTRFGVGPEDRVLGLSALTFDLSVYDVLGL 2841
Cdd:PRK05691 1258 LDswpSQAPGLHLHG--DNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPISFDVSVWECFWP 1335

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2842 LGAGGALVLPAAEAEKDPAHWWERLVAGRVTVWNSTPALMLLLVeyaEQRGLKLPAALRLVMLSGDWIPVALPDRIRALG 2921
Cdd:PRK05691 1336 LITGCRLVLAGPGEHRDPQRIAELVQQYGVTTLHFVPPLLQLFI---DEPLAAACTSLRRLFSGGEALPAELRNRVLQRL 1412

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2922 RDVQVVSLGGATEASIwSIAYPIGQVAPQWKSiPYGMPLANQRFHVLDGRLEARPWWVPGELYIGGEGLAREYWRDEPLT 3001
Cdd:PRK05691 1413 PQVQLHNRYGPTETAI-NVTHWQCQAEDGERS-PIGRPLGNVLCRVLDAELNLLPPGVAGELCIGGAGLARGYLGRPALT 1490

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  3002 ATRFIRHP--RTGERLYRTGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPALSASVVVARGEPRGvRRL 3079
Cdd:PRK05691 1491 AERFVPDPlgEDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVREGAAG-AQL 1569

                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  3080 VAYAVPRSGQTPAAGELRRYLAERLPAYMVPSAFVLLESLPRSRNGKIARDQLPEPqqTQGLAAQAAAADPLVERLAALV 3159
Cdd:PRK05691 1570 VGYYTGEAGQEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRALPEP--VWQQREHVEPRTELQQQIAAIW 1647

                        1130      1140      1150
                  ....*....|....*....|....*....|.
gi 53747904  3160 KEALRLERVEPQDSLLDLGADSVALIRLINR 3190
Cdd:PRK05691 1648 REVLGLPRVGLRDDFFALGGHSLLATQIVSR 1678
A_NRPS_Srf_like cd12117
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...
 2647-3132 9.93e-116

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: 377.31  E-value: 9.93e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2647 QARLHPELPALLAPERTLSYGELARRAQALAARLRELEVQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLDPEQPPLR 2726
Cdd:cd12117    6 QAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAER 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2727 LHQLLEEGPARVVLTQSSLlhTVPWPPGVQVIAVDELEPATEAPPLPPRGTPEHLAYVIYTSGSTGKPKGVAIEHRAALN 2806
Cdd:cd12117   86 LAFMLADAGAKVLLTDRSL--AGRAGGLEVAVVIDEALDAGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAVTHRGVVR 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2807 TVvdLNTRFG-VGPEDRVLGLSALTFDLSVYDVLGLLGAGGALVLPAAEAEKDPAHWWERLVAGRVTVWNSTPALMLLLV 2885
Cdd:cd12117  164 LV--KNTNYVtLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPDALGALIAEEGVTVLWLTAALFNQLA 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2886 EYAEQRglklPAALRLVMLSGDWIPVALPDRIRALGRDVQVVSLGGATEASIWSIAYPIGQVAPQWKSIPYGMPLANQRF 2965
Cdd:cd12117  242 DEDPEC----FAGLRELLTGGEVVSPPHVRRVLAACPGLRLVNGYGPTENTTFTTSHVVTELDEVAGSIPIGRPIANTRV 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2966 HVLDGRLEARPWWVPGELYIGGEGLAREYWRDEPLTATRFIRHPRT-GERLYRTGDQGRMLPEGSIEFLGREDLQVKVQG 3044
Cdd:cd12117  318 YVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFGpGERLYRTGDLARWLPDGRLEFLGRIDDQVKIRG 397

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3045 FRVELGEIEAALAQHPALSASVVVARGEPRGVRRLVAYAVPRsgQTPAAGELRRYLAERLPAYMVPSAFVLLESLPRSRN 3124
Cdd:cd12117  398 FRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVAE--GALDAAELRAFLRERLPAYMVPAAFVVLDELPLTAN 475


                 ....*...
gi 53747904 3125 GKIARDQL 3132
Cdd:cd12117  476 GKVDRRAL 483
A_NRPS_Ta1_like cd12116
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ...
 2652-3132 7.21e-115

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: 374.32  E-value: 7.21e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2652 PELPALLAPERTLSYGELARRAQALAARLRELEVQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLDPEQPPLRLHQLL 2731
Cdd:cd12116    1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2732 EEGPARVVLTQSSLLHTVPWPPGVqviaVDELEPATEAPPLPPRGT--PEHLAYVIYTSGSTGKPKGVAIEHRAALNTVV 2809
Cdd:cd12116   81 EDAEPALVLTDDALPDRLPAGLPV----LLLALAAAAAAPAAPRTPvsPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLH 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2810 DLNTRFGVGPEDRVLGLSALTFDLSVYDVLGLLGAGGALVLPAAEAEKDPAHWWERLVAGRVTVWNSTPALMLLLVeYAE 2889
Cdd:cd12116  157 SMRERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSITVMQATPATWRMLL-DAG 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2890 QRGLklpAALRLVmLSGDWIPVALPDRIRALGRdvQVVSLGGATEASIWSIAypiGQVAPQWKSIPYGMPLANQRFHVLD 2969
Cdd:cd12116  236 WQGR---AGLTAL-CGGEALPPDLAARLLSRVG--SLWNLYGPTETTIWSTA---ARVTAAAGPIPIGRPLANTQVYVLD 306

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2970 GRLEARPWWVPGELYIGGEGLAREYWRDEPLTATRFIRHPRT--GERLYRTGDQGRMLPEGSIEFLGREDLQVKVQGFRV 3047
Cdd:cd12116  307 AALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAgpGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRI 386

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3048 ELGEIEAALAQHPALSASVVVARGEpRGVRRLVAYAVPRSGQTPAAGELRRYLAERLPAYMVPSAFVLLESLPRSRNGKI 3127
Cdd:cd12116  387 ELGEIEAALAAHPGVAQAAVVVRED-GGDRRLVAYVVLKAGAAPDAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKL 465


                 ....*
gi 53747904 3128 ARDQL 3132
Cdd:cd12116  466 DRKAL 470
A_NRPS_VisG_like cd17651
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ...
 2644-3133 1.64e-112

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: 368.59  E-value: 1.64e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2644 FFTQARLHPELPALLAPERTLSYGELARRAQALAARLRELEVQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLDPEQP 2723
Cdd:cd17651    1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2724 PLRLHQLLEEGPARVVLTQSSLLHTVPWPPGVQVIAVDELEPATEAPPLPPRGTPEHLAYVIYTSGSTGKPKGVAIEHRA 2803
Cdd:cd17651   81 AERLAFMLADAGPVLVLTHPALAGELAVELVAVTLLDQPGAAAGADAEPDPALDADDLAYVIYTSGSTGRPKGVVMPHRS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2804 ALNTVVDLNTRFGVGPEDRVLGLSALTFDLSVYDVLGLLGAGGALVLPAAEAEKDPAHWWERLVAGRVTVWNSTPALMLL 2883
Cdd:cd17651  161 LANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPPALAAWLDEQRISRVFLPTVALRA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2884 LVEYAeQRGLKLPAALRLVMLSGDwiPVALPDRIRALGRDV---QVVSLGGATEASIWSiAYPIGQVAPQWKSIP-YGMP 2959
Cdd:cd17651  241 LAEHG-RPLGVRLAALRYLLTGGE--QLVLTEDLREFCAGLpglRLHNHYGPTETHVVT-ALSLPGDPAAWPAPPpIGRP 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2960 LANQRFHVLDGRLEARPWWVPGELYIGGEGLAREYWRDEPLTATRFIRHP-RTGERLYRTGDQGRMLPEGSIEFLGREDL 3038
Cdd:cd17651  317 IDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPfVPGARMYRTGDLARWLPDGELEFLGRADD 396

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3039 QVKVQGFRVELGEIEAALAQHPALSASVVVARGEPRGVRRLVAYAVPRSGQTPAAGELRRYLAERLPAYMVPSAFVLLES 3118
Cdd:cd17651  397 QVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEAPVDAAELRAALATHLPEYMVPSAFVLLDA 476

                        490
                 ....*....|....*
gi 53747904 3119 LPRSRNGKIARDQLP 3133
Cdd:cd17651  477 LPLTPNGKLDRRALP 491
A_NRPS_Bac cd17655
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...
 2644-3135 1.16e-110

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: 363.19  E-value: 1.16e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2644 FFTQARLHPELPALLAPERTLSYGELARRAQALAARLRELEVQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLDPEQP 2723
Cdd:cd17655    3 FEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2724 PLRLHQLLEEGPARVVLTQSSLLHTVPWPPGVQVIAVDELEpATEAPPLPPRGTPEHLAYVIYTSGSTGKPKGVAIEHRA 2803
Cdd:cd17655   83 EERIQYILEDSGADILLTQSHLQPPIAFIGLIDLLDEDTIY-HEESENLEPVSKSDDLAYVIYTSGSTGKPKGVMIEHRG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2804 ALNTVVDLNTRFGVGPEDRVLGLSALTFDLSVYDVLGLLGAGGALVLPAAEAEKDPAHWWERLVAGRVTVWNSTPALMLL 2883
Cdd:cd17655  162 VVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQALTQYIRQNRITIIDLTPAHLKL 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2884 LVEYAEQRGLKLpaalRLVMLSGDWIPVALPDRIRALGRD-VQVVSLGGATEASIWSIAYPIGQVAPQWKSIPYGMPLAN 2962
Cdd:cd17655  242 LDAADDSEGLSL----KHLIVGGEALSTELAKKIIELFGTnPTITNAYGPTETTVDASIYQYEPETDQQVSVPIGKPLGN 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2963 QRFHVLDGRLEARPWWVPGELYIGGEGLAREYWRDEPLTATRFIRHP-RTGERLYRTGDQGRMLPEGSIEFLGREDLQVK 3041
Cdd:cd17655  318 TRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPfVPGERMYRTGDLARWLPDGNIEFLGRIDHQVK 397

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3042 VQGFRVELGEIEAALAQHPALSASVVVARGEPRGVRRLVAYAVPRSGQTPAagELRRYLAERLPAYMVPSAFVLLESLPR 3121
Cdd:cd17655  398 IRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEKELPVA--QLREFLARELPDYMIPSYFIKLDEIPL 475

                        490
                 ....*....|....
gi 53747904 3122 SRNGKIARDQLPEP 3135
Cdd:cd17655  476 TPNGKVDRKALPEP 489
A_NRPS_CmdD_like cd17652
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ...
 2652-3133 4.62e-110

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: 359.26  E-value: 4.62e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2652 PELPALLAPERTLSYGELARRAQALAARLRELEVQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLDPEQPPLRLHQLL 2731
Cdd:cd17652    1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2732 EEGPARVVLTQssllhtvpwppgvqviavdelepateapplpprgtPEHLAYVIYTSGSTGKPKGVAIEHRAALNTVVDL 2811
Cdd:cd17652   81 ADARPALLLTT-----------------------------------PDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQ 125

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2812 NTRFGVGPEDRVLGLSALTFDLSVYDVLGLLGAGGALVLPAAEAEKDPAHWWERLVAGRVTVWNSTPALMLLLVEYAeqr 2891
Cdd:cd17652  126 IAAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREHRITHVTLPPAALAALPPDD--- 202

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2892 glkLPAaLRLVMLSGDWIPVALPDRIrALGRdvQVVSLGGATEASIWSIAYpigQVAPQWKSIPYGMPLANQRFHVLDGR 2971
Cdd:cd17652  203 ---LPD-LRTLVVAGEACPAELVDRW-APGR--RMINAYGPTETTVCATMA---GPLPGGGVPPIGRPVPGTRVYVLDAR 272

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2972 LEARPWWVPGELYIGGEGLAREYWRDEPLTATRFIRHP--RTGERLYRTGDQGRMLPEGSIEFLGREDLQVKVQGFRVEL 3049
Cdd:cd17652  273 LRPVPPGVPGELYIAGAGLARGYLNRPGLTAERFVADPfgAPGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIEL 352

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3050 GEIEAALAQHPALSASVVVARGEPRGVRRLVAYAVPRSGQTPAAGELRRYLAERLPAYMVPSAFVLLESLPRSRNGKIAR 3129
Cdd:cd17652  353 GEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPGAAPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDR 432


                 ....
gi 53747904 3130 DQLP 3133
Cdd:cd17652  433 RALP 436
A_NRPS_ApnA-like cd17644
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ...
 2644-3133 1.46e-109

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: 359.06  E-value: 1.46e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2644 FFTQARLHPELPALLAPERTLSYGELARRAQALAARLRELEVQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLDPEQP 2723
Cdd:cd17644    6 FEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDPNYP 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2724 PLRLHQLLEEGPARVVLTQssllhtvpwppgvqviavdelepateapplpprgtPEHLAYVIYTSGSTGKPKGVAIEHRA 2803
Cdd:cd17644   86 QERLTYILEDAQISVLLTQ-----------------------------------PENLAYVIYTSGSTGKPKGVMIEHQS 130

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2804 ALNTVVDLNTRFGVGPEDRVLGLSALTFDLSVYDVLGLLGAGGALVLPAAEAEKDPAHWWERLVAGRVTVWNSTPALMLL 2883
Cdd:cd17644  131 LVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEDFVQYIQQWQLTVLSLPPAYWHL 210

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2884 LVEYAEQRGLKLPAALRLVMLSGDWIpvaLPDRIR----ALGRDVQVVSLGGATEASIWSIAYPIGQV-APQWKSIPYGM 2958
Cdd:cd17644  211 LVLELLLSTIDLPSSLRLVIVGGEAV---QPELVRqwqkNVGNFIQLINVYGPTEATIAATVCRLTQLtERNITSVPIGR 287

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2959 PLANQRFHVLDGRLEARPWWVPGELYIGGEGLAREYWRDEPLTATRFIRHP---RTGERLYRTGDQGRMLPEGSIEFLGR 3035
Cdd:cd17644  288 PIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPfnsSESERLYKTGDLARYLPDGNIEYLGR 367

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3036 EDLQVKVQGFRVELGEIEAALAQHPALSASVVVARGEPRGVRRLVAYAVPRSGQTPAAGELRRYLAERLPAYMVPSAFVL 3115
Cdd:cd17644  368 IDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIVPHYEESPSTVELRQFLKAKLPDYMIPSAFVV 447

                        490
                 ....*....|....*...
gi 53747904 3116 LESLPRSRNGKIARDQLP 3133
Cdd:cd17644  448 LEELPLTPNGKIDRRALP 465
PKS_ER smart00829
Enoylreductase; Enoylreductase in Polyketide synthases.
 1703-1988 6.80e-106

Enoylreductase; Enoylreductase in Polyketide synthases.


Pssm-ID: 214840 [Multi-domain]  Cd Length: 287  Bit Score: 340.90  E-value: 6.80e-106
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904    1703 IEVEAAGLNFLDVLGALGMMPaleaEESVLGRECSGRIAAVGEGVSGLRVGDEVLAVAPGCFRSYVLVDESQVVRRPASL 1782
Cdd:smart00829    1 IEVRAAGLNFRDVLIALGLYP----GEAVLGGECAGVVTRVGPGVTGLAVGDRVMGLAPGAFATRVVTDARLVVPIPDGW 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904    1783 GLAEGAAQMVPFATAYFALHTVGRLRRGERILIHAAAGGLGLAAVQLASRTGAEILATAGSEQKREYLRSLGI--AHVLD 1860
Cdd:smart00829   77 SFEEAATVPVVFLTAYYALVDLARLRPGESVLIHAAAGGVGQAAIQLARHLGAEVFATAGSPEKRDFLRALGIpdDHIFS 156

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904    1861 SRSTSFVSEVRERTGGRGVDVVLNSLAGELLLAGLSVLAPHGRFLELGKRDLYADQQVGLRTLARGQTFAAIDFGP--HH 1938
Cdd:smart00829  157 SRDLSFADEILRATGGRGVDVVLNSLSGEFLDASLRCLAPGGRFVEIGKRDIRDNSQLAMAPFRPNVSYHAVDLDAleEG 236

                           250       260       270       280       290
                    ....*....|....*....|....*....|....*....|....*....|.
gi 53747904    1939 PD-FRAVLEEVATQLTQGQLEPLPTRLFPARQVAEAFSFMARALHIGRVAV 1988
Cdd:smart00829  237 PDrIRELLAEVLELFAEGVLRPLPVTVFPISDAEDAFRYMQQGKHIGKVVL 287
PKS_AT smart00827
Acyl transferase domain in polyketide synthase (PKS) enzymes;
537-831 1.20e-104

Acyl transferase domain in polyketide synthase (PKS) enzymes;


Pssm-ID: 214838 [Multi-domain]  Cd Length: 298  Bit Score: 337.84  E-value: 1.20e-104
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904     537 LFPGQGTPLVGTARALHESEPTFRQAVEQCARLLRQTLGLDVREVLFPSAEQEEQARrlaaqTRVAQPALFTLEYALAQT 616
Cdd:smart00827    1 VFTGQGSQWAGMGRELYETEPVFREALDECDAALQPLLGWSLLDVLLGEDGAASLLD-----TEVAQPALFAVQVALARL 75

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904     617 WLGWGLQPQALAGHSLGELVAACLAGVFSLEDALQLVAARGQLMQGCPP-GAMLAVPLPEAELAALL---GSELCIAAVN 692
Cdd:smart00827   76 LRSWGVRPDAVVGHSSGEIAAAYVAGVLSLEDAARLVAARGRLMQALPGgGAMLAVGLSEEEVEPLLagvPDRVSVAAVN 155

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904     693 GPRACVASGPLPAVEALTAALESRGVSSRRLETSHAFHSASMEACQGPLTTLLRRMRLQAPRLPCVSGLTGRWLTGEEAT 772
Cdd:smart00827  156 SPSSVVLSGDEDAVDELAARLEAEGIFARRLKVDHAFHSPHMEPILDEFRAALAGLTPRPPRIPFVSTVTGTLIDGAELD 235

                           250       260       270       280       290       300
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904     773 EPTYWARQLREPVRFSEALETLWSLKEP-VLLEVGPGTTLTALARRHPTRPARTQEVASL 831
Cdd:smart00827  236 DADYWVRNLREPVRFADAVRALLAEGGVtVFLEVGPHPVLTGPIKQTLAAAGSAVVLPSL 295
A_NRPS_Sfm_like cd12115
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ...
 2640-3132 5.33e-104

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: 342.37  E-value: 5.33e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2640 LEEGFFTQARLHPELPALLAPERTLSYGELARRAQALAARLRELEVQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLD 2719
Cdd:cd12115    1 LHDLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2720 PEQPPLRLHQLLEEGPARVVLTQssllhtvpwppgvqviavdelepateapplpprgtPEHLAYVIYTSGSTGKPKGVAI 2799
Cdd:cd12115   81 PAYPPERLRFILEDAQARLVLTD-----------------------------------PDDLAYVIYTSGSTGRPKGVAI 125

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2800 EHRAALNTVVDLNTRFGVGPEDRVLGLSALTFDLSVYDV-------LGLLGAGGALVLPAAEAEKDpahwwerlvagrVT 2872
Cdd:cd12115  126 EHRNAAAFLQWAAAAFSAEELAGVLASTSICFDLSVFELfgplatgGKVVLADNVLALPDLPAAAE------------VT 193

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2873 VWNSTPALMLLLVEYAeqrglKLPAALRLVMLSGDWIPVALPDRIRALGRDVQVVSLGGATEASIWSIAYPIGQVAPQWK 2952
Cdd:cd12115  194 LINTVPSAAAELLRHD-----ALPASVRVVNLAGEPLPRDLVQRLYARLQVERVVNLYGPSEDTTYSTVAPVPPGASGEV 268

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2953 SIpyGMPLANQRFHVLDGRLEARPWWVPGELYIGGEGLAREYWRDEPLTATRFIRHPR-TGERLYRTGDQGRMLPEGSIE 3031
Cdd:cd12115  269 SI--GRPLANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFgPGARLYRTGDLVRWRPDGLLE 346

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3032 FLGREDLQVKVQGFRVELGEIEAALAQHPALSASVVVARGEPRGVRRLVAYAVPRSGQTPAAGELRRYLAERLPAYMVPS 3111
Cdd:cd12115  347 FLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPGAAGLVEDLRRHLGTRLPAYMVPS 426

                        490       500
                 ....*....|....*....|.
gi 53747904 3112 AFVLLESLPRSRNGKIARDQL 3132
Cdd:cd12115  427 RFVRLDALPLTPNGKIDRSAL 447
A_NRPS_Cytc1-like cd17643
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...
 2652-3132 9.01e-104

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: 341.60  E-value: 9.01e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2652 PELPALLAPERTLSYGELARRAQALAARLRELEVQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLDPEQPPLRLHQLL 2731
Cdd:cd17643    1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2732 EEGPARVVLTQssllhtvpwppgvqviavdelepateapplpprgtPEHLAYVIYTSGSTGKPKGVAIEHRAALNTVVDL 2811
Cdd:cd17643   81 ADSGPSLLLTD-----------------------------------PDDLAYVIYTSGSTGRPKGVVVSHANVLALFAAT 125

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2812 NTRFGVGPEDRVLGLSALTFDLSVYDVLGLLGAGGALVLPAAEAEKDPAHWWERLVAGRVTVWNSTPALMLLLVEyAEQR 2891
Cdd:cd17643  126 QRWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGVTVLNQTPSAFYQLVE-AADR 204

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2892 GLKLPAALRLVMLSGDWIPVAL--PDRIRALGRDVQVVSLGGATEASIWSIAYPI--GQVAPQWKSiPYGMPLANQRFHV 2967
Cdd:cd17643  205 DGRDPLALRYVIFGGEALEAAMlrPWAGRFGLDRPQLVNMYGITETTVHVTFRPLdaADLPAAAAS-PIGRPLPGLRVYV 283

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2968 LDGRLEARPWWVPGELYIGGEGLAREYWRDEPLTATRFIRHPRT--GERLYRTGDQGRMLPEGSIEFLGREDLQVKVQGF 3045
Cdd:cd17643  284 LDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFGgpGSRMYRTGDLARRLPDGELEYLGRADEQVKIRGF 363

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3046 RVELGEIEAALAQHPALSASVVVARGEPRGVRRLVAYAVPRSGQTPAAGELRRYLAERLPAYMVPSAFVLLESLPRSRNG 3125
Cdd:cd17643  364 RIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADDGAAADIAELRALLKELLPDYMVPARYVPLDALPLTVNG 443


                 ....*..
gi 53747904 3126 KIARDQL 3132
Cdd:cd17643  444 KLDRAAL 450
PRK05691 PRK05691
peptide synthase; Validated
 2083-3245 1.45e-101

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 368.73  E-value: 1.45e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2083 PPSSLEQLIEQVWRKHLGVERVQPTDSFFQLGGDSLLGIQVAADLRRHLGVELPTATLFSHPTLAALAAALRARQGEAAA 2162
Cdd:PRK05691 1635 PRTELQQQIAAIWREVLGLPRVGLRDDFFALGGHSLLATQIVSRTRQACDVELPLRALFEASELGAFAEQVARIQAAGER 1714

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2163 PTAPAPALVPdpaaRFEPFPLTDVQEAYWV-----GRRSAFELGGVAAHgyfeieSPGLEVERFIQCWRQLLQRHDMLRm 2237
Cdd:PRK05691 1715 NSQGAIARVD----RSQPVPLSYSQQRMWFlwqmePDSPAYNVGGMARL------SGVLDVDRFEAALQALILRHETLR- 1783

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2238 VVLPDGRQQVLEQVPEYTPEVVELRGLSPQEAESR--RLQ-LRERMAHQVLRSDRWPLfeLVLCRYEGGVRIH---MSMD 2311
Cdd:PRK05691 1784 TTFPSVDGVPVQQVAEDSGLRMDWQDFSALPADARqqRLQqLADSEAHQPFDLERGPL--LRACLVKAAEREHyfvLTLH 1861

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2312 ALMLDAWSSAVLRQDFAQLYH----EPGRPLEPLAITFRDYVLAERRLREGEAHERARAYWWARLDTLPPPPELPLVKEP 2387
Cdd:PRK05691 1862 HIVTEGWAMDIFARELGALYEafldDRESPLEPLPVQYLDYSVWQRQWLESGERQRQLDYWKAQLGNEHPLLELPADRPR 1941

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2388 SQLEHARFTHREARLEPHRWARLQERARAHGLTPSAACMAAFAEVLARWSRHPRFTLNLTLFQRLplHPQVDELVGDFTS 2467
Cdd:PRK05691 1942 PPVQSHRGELYRFDLSPELAARVRAFNAQRGLTLFMTMTATLAALLYRYSGQRDLRIGAPVANRI--RPESEGLIGAFLN 2019

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2468 LVLLEVEAHAASTFAE-----RASRLQAQLWRDL--EHgSVSAVQLIRElvrtgrrspGAIMPV--VFTSILSLDARRGP 2538
Cdd:PRK05691 2020 TQVLRCQLDGQMSVSElleqvRQTVIEGQSHQDLpfDH-LVEALQPPRS---------AAYNPLfqVMCNVQRWEFQQSR 2089

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2539 QgsLSFFEGELVYSISQTPQVWLDHGVHEEEGALVLAWDSVEALFPPGMVDDMFHAYQRLLGALAEEEQAWEGELPELLP 2618
Cdd:PRK05691 2090 Q--LAGMTVEYLVNDARATKFDLNLEVTDLDGRLGCCLTYSRDLFDEPRIARMAEHWQNLLEALLGDPQQRLAELPLLAA 2167

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2619 PAQRELLARYNATQA-PRPSGRLEEGFFTQARLHPELPALLAPERTLSYGELARRAQALAARLRELEVQPQELVAIAMHK 2697
Cdd:PRK05691 2168 AEQQQLLDSLAGEAGeARLDQTLHGLFAAQAARTPQAPALTFAGQTLSYAELDARANRLARALRERGVGPQVRVGLALER 2247

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2698 GWEQATAVLGVLQAAAAYLPLDPEQPPLRLHQLLEEGPARVVLTQSSLLHTV-PWPPGVQVIAVDELEPATEA---PPLP 2773
Cdd:PRK05691 2248 SLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGIGLLLSDRALFEALgELPAGVARWCLEDDAAALAAysdAPLP 2327

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2774 PRGTPEHLAYVIYTSGSTGKPKGVAIEHRAALNTVVDLNTRFGVGPEDRVLGLSALTFDlSVYDVLGLLGAGGALVLPAA 2853
Cdd:PRK05691 2328 FLSLPQHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDCELHFYSINFD-AASERLLVPLLCGARVVLRA 2406

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2854 EAEKDPAHWWERLVAGRVTVWNSTPALMLLLVEYAEQRGLKLPaaLRLVMLSGDWIPVALPDRIRALGRDVQVVSLGGAT 2933
Cdd:PRK05691 2407 QGQWGAEEICQLIREQQVSILGFTPSYGSQLAQWLAGQGEQLP--VRMCITGGEALTGEHLQRIRQAFAPQLFFNAYGPT 2484

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2934 EASIWSIAYPIGQVAPQ-WKSIPYGMPLANQRFHVLDGRLEARPWWVPGELYIGGEGLAREYWRDEPLTATRFIRHP--R 3010
Cdd:PRK05691 2485 ETVVMPLACLAPEQLEEgAASVPIGRVVGARVAYILDADLALVPQGATGELYVGGAGLAQGYHDRPGLTAERFVADPfaA 2564

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  3011 TGERLYRTGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPALSASVVVARGEPRGvRRLVAYAV-PRSGQ 3089
Cdd:PRK05691 2565 DGGRLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALDTPSG-KQLAGYLVsAVAGQ 2643

                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  3090 TPAA-----GELRRYLAERLPAYMVPSAFVLLESLPRSRNGKIARDQLPEPQQTQGLAAQAAAADPLVERLAALVKEALR 3164
Cdd:PRK05691 2644 DDEAqaalrEALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRALPAPDPELNRQAYQAPRSELEQQLAQIWREVLN 2723

                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  3165 LERVEPQDSLLDLGADSVALIRLINRL-EAELQFRPRlaDIYENPTVQGLATLHQEKTKSQGEGGaprLTAPRSTLLPAE 3243
Cdd:PRK05691 2724 VERVGLGDNFFELGGDSILSIQVVSRArQLGIHFSPR--DLFQHQTVQTLAAVATHSEAAQAEQG---PLQGASGLTPIQ 2798


                  ..
gi 53747904  3244 EW 3245
Cdd:PRK05691 2799 HW 2800
enoyl_red cd05195
enoyl reductase of polyketide synthase; Putative enoyl reductase of polyketide synthase. ...
 1700-1988 7.50e-100

enoyl reductase of polyketide synthase; Putative enoyl reductase of polyketide synthase. Polyketide synthases produce polyketides in step by step mechanism that is similar to fatty acid synthesis. Enoyl reductase reduces a double to single bond. Erythromycin is one example of a polyketide generated by 3 complex enzymes (megasynthases). 2-enoyl thioester reductase (ETR) catalyzes the NADPH-dependent dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains, at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding.


Pssm-ID: 176179 [Multi-domain]  Cd Length: 293  Bit Score: 324.14  E-value: 7.50e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1700 QVEIEVEAAGLNFLDVLGALGMMPAleaEESVLGRECSGRIAAVGEGVSGLRVGDEVLAVAPGCFRSYVLVDESQVVRRP 1779
Cdd:cd05195    2 EVEVEVKAAGLNFRDVLVALGLLPG---DETPLGLECSGIVTRVGSGVTGLKVGDRVMGLAPGAFATHVRVDARLVVKIP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1780 ASLGLAEGAAQMVPFATAYFALHTVGRLRRGERILIHAAAGGLGLAAVQLASRTGAEILATAGSEQKREYLRSLG--IAH 1857
Cdd:cd05195   79 DSLSFEEAATLPVAYLTAYYALVDLARLQKGESVLIHAAAGGVGQAAIQLAQHLGAEVFATVGSEEKREFLRELGgpVDH 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1858 VLDSRSTSFVSEVRERTGGRGVDVVLNSLAGELLLAGLSVLAPHGRFLELGKRDLYADQQVGLRTLARGQTFAAIDFGP- 1936
Cdd:cd05195  159 IFSSRDLSFADGILRATGGRGVDVVLNSLSGELLRASWRCLAPFGRFVEIGKRDILSNSKLGMRPFLRNVSFSSVDLDQl 238

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 53747904 1937 --HHPD-FRAVLEEVATQLTQGQLEPLPTRLFPARQVAEAFSFMARALHIGRVAV 1988
Cdd:cd05195  239 arERPElLRELLREVLELLEAGVLKPLPPTVVPSASEIDAFRLMQSGKHIGKVVL 293
A_NRPS_PpsD_like cd17650
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ...
 2652-3132 3.37e-99

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: 328.27  E-value: 3.37e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2652 PELPALLAPERTLSYGELARRAQALAARLRELEVQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLDPEQPPLRLHQLL 2731
Cdd:cd17650    1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2732 EEGPARVVLTQssllhtvpwppgvqviavdelepateapplpprgtPEHLAYVIYTSGSTGKPKGVAIEHRAALNTVVDL 2811
Cdd:cd17650   81 EDSGAKLLLTQ-----------------------------------PEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAW 125

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2812 NTRFGVGPED-RVLGLSALTFDLSVYDVLGLLGAGGALVLPAAEAEKDPAHWWERLVAGRVTVWNSTPALMLLLVEYAEQ 2890
Cdd:cd17650  126 RREYELDSFPvRLLQMASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRITLMESTPALIRPVMAYVYR 205

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2891 RGLKLPAaLRLVMLSGDWIPVALP-DRIRALGRDVQVVSLGGATEASIWSIAYPIGQV-APQWKSIPYGMPLANQRFHVL 2968
Cdd:cd17650  206 NGLDLSA-MRLLIVGSDGCKAQDFkTLAARFGQGMRIINSYGVTEATIDSTYYEEGRDpLGDSANVPIGRPLPNTAMYVL 284

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2969 DGRLEARPWWVPGELYIGGEGLAREYWRDEPLTATRFIRHP-RTGERLYRTGDQGRMLPEGSIEFLGREDLQVKVQGFRV 3047
Cdd:cd17650  285 DERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPfAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRI 364

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3048 ELGEIEAALAQHPALSASVVVARGEPRGVRRLVAYAVPRSgqTPAAGELRRYLAERLPAYMVPSAFVLLESLPRSRNGKI 3127
Cdd:cd17650  365 ELGEIESQLARHPAIDEAVVAVREDKGGEARLCAYVVAAA--TLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKV 442


                 ....*
gi 53747904 3128 ARDQL 3132
Cdd:cd17650  443 DRRAL 447
A_NRPS_PvdJ-like cd17649
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ...
 2652-3133 3.48e-98

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: 325.48  E-value: 3.48e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2652 PELPALLAPERTLSYGELARRAQALAARLRELEVQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLDPEQPPLRLHQLL 2731
Cdd:cd17649    1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2732 EEGPARVVLTQssllhtvpwppgvqviavdelepateapplpprgTPEHLAYVIYTSGSTGKPKGVAIEHRAALNTVVDL 2811
Cdd:cd17649   81 EDSGAGLLLTH----------------------------------HPRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQAT 126

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2812 NTRFGVGPEDRVLGLSALTFDLSVYDVLGLLGAGGALVLPAAEAEKDPAHWWERLVAGRVTVWNSTPALMLLLVEYAEQR 2891
Cdd:cd17649  127 AERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVTVLDLPPAYLQQLAEEADRT 206

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2892 GLKLPAALRLVMLSGDWIPvalPDRI-RALGRDVQVVSLGGATEASIWSIAYPI-GQVAPQWKSIPYGMPLANQRFHVLD 2969
Cdd:cd17649  207 GDGRPPSLRLYIFGGEALS---PELLrRWLKAPVRLFNAYGPTEATVTPLVWKCeAGAARAGASMPIGRPLGGRSAYILD 283

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2970 GRLEARPWWVPGELYIGGEGLAREYWRDEPLTATRFIRHP--RTGERLYRTGDQGRMLPEGSIEFLGREDLQVKVQGFRV 3047
Cdd:cd17649  284 ADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPfgAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRI 363

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3048 ELGEIEAALAQHPALSASVVVARGEPrGVRRLVAYAVPRSGQTPAA--GELRRYLAERLPAYMVPSAFVLLESLPRSRNG 3125
Cdd:cd17649  364 ELGEIEAALLEHPGVREAAVVALDGA-GGKQLVAYVVLRAAAAQPElrAQLRTALRASLPDYMVPAHLVFLARLPLTPNG 442


                 ....*...
gi 53747904 3126 KIARDQLP 3133
Cdd:cd17649  443 KLDRKALP 450
omega_3_PfaA TIGR02813
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ...
 13-914 1.50e-90

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: 331.58  E-value: 1.50e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904     13 IALVGMAGRFPGAPDVESFWRNLVAGVESISFFSEEELRQAGVSEQIRRRPE--YVPAKGVLEDLElFDAGFFGYSPREA 90
Cdd:TIGR02813    9 IAIVGMASIFANSRYLNKFWDLIFEKIDAITDVPSDHWAKDDYYDSDKSEADksYCKRGGFLPEVD-FNPMEFGLPPNIL 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904     91 SHLDPQQRLLLECSWEALEDAGLRPDQLPGWVGVYVGAGDTSYRFQLL--RGHGDPL------SGSKDV----------- 151
Cdd:TIGR02813   88 ELTDISQLLSLVVAKEVLNDAGLPDGYDRDKIGITLGVGGGQKQSSSLnaRLQYPVLkkvfkaSGVEDEdsemlikkfqd 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904    152 -------AGFFGNYPDFLATRVAYKLNLRGPALGIHTACSTSLVSINMACSALRGFECDMALAGGVSLRlpaRSGYLY-- 222
Cdd:TIGR02813  168 qyihweeNSFPGSLGNVISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGGVCTD---NSPFMYms 244

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904    223 -EEGGVASKDGHCRPFDARATGTVTGDGVGVVVLKRLEDALKARDPIHAVIRGWALNNDGASRAGFtAPSVEGQSEVIAL 301
Cdd:TIGR02813  245 fSKTPAFTTNEDIQPFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGKFKSIY-APRPEGQAKALKR 323

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904    302 AHAAAGISARDITYVEAHGTGTPLGDPIEVAALTRAFRAHTADTAFCTLGAVKSNIGHLDAAAGVAGVIKTVQALRHRLI 381
Cdd:TIGR02813  324 AYDDAGFAPHTCGLIEAHGTGTAAGDVAEFGGLVSVFSQDNDQKQHIALGSVKSQIGHTKSTAGTAGMIKAVLALHHKVL 403

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904    382 PPTLHFERPNPALHLEQSPFFVNTQPLPW--ESPRGPRLAGVSSFGIGGTNAHTLFEEAPPPPASGPT-RPNQV---LLL 455
Cdd:TIGR02813  404 PPTINVDQPNPKLDIENSPFYLNTETRPWmqREDGTPRRAGISSFGFGGTNFHMVLEEYSPKHQRDDQyRQRAVaqtLLF 483

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904    456 SARSTSALehIAGRLAAHLRRHPDLELADVAF----------TLQVGRARFpyrrALTCRTLAEAMERLEAPEPRPPEPL 525
Cdd:TIGR02813  484 TAANEKAL--VSSLKDWKNKLSAKADDQPYAFnalaventlrTIAVALARL----GFVAKNADELITMLEQAITQLEAKS 557

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904    526 AHEGERPP---------------LVMLFPGQGTPLVGTARALHESEPTFRQAVEQCARLLRQTLGLDVREVLFP------ 584
Cdd:TIGR02813  558 CEEWQLPSgisyrksalvvesgkVAALFAGQGSQYLNMGRELACNFPEVRQAAADMDSVFTQAGKGALSPVLYPipvfnd 637

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904    585 -SAEQEEQARRLaaqTRVAQPALFTLEYALAQTWLGWGLQPQALAGHSLGELVAACLAGVFSLEDALQLVAARGQLMQGC 663
Cdd:TIGR02813  638 eSRKAQEEALTN---TQHAQSAIGTLSMGQYKLFTQAGFKADMTAGHSFGELSALCAAGVISDDDYMMLAFSRGQAMAAP 714

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904    664 P----PGAMLAVPLPEAELAALLGSELC------IAAVNGPRACVASGPLPAVEALTAALESRGVSSRRLETSHAFHSAS 733
Cdd:TIGR02813  715 TgeadIGFMYAVILAVVGSPTVIANCIKdfegvsIANYNSPTQLVIAGVSTQIQIAAKALKEKGFKAIPLPVSGAFHTPL 794

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904    734 MEACQGPLTTLLRRMRLQAPRLPCVSGLTGRWLTGEEATEPTYWARQLREPVRFSEALETLWSLKEPVLLEVGPGTTLTA 813
Cdd:TIGR02813  795 VAHAQKPFSAAIDKAKFNTPLVPLYSNGTGKLHSNDAAAIKKALKNHMLQSVHFSEQLEAMYAAGARVFVEFGPKNILQK 874

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904    814 LARRhpTRPARTQEVASLPVQPD---TAVPCIEEAVGELWQAGLELDwsalhaaprhraHLPPYPFErqrywIEPEAAPQ 890
Cdd:TIGR02813  875 LVEN--TLKDKENELCAISINPNpkgDSDMQLRQAAVQLAVLGLELT------------EIDPYQAE-----KRPPAATS 935

                          970       980
                   ....*....|....*....|....
gi 53747904    891 PRAQQPTPASLVPPEqpSREALED 914
Cdd:TIGR02813  936 PMNIKLNAANYISPA--TRKKMDD 957
DltA cd05945
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ...
 2648-3132 2.11e-86

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: 291.46  E-value: 2.11e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2648 ARLHPELPALLAPERTLSYGELARRAQALAARLRELEVQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLDPEQPPLRL 2727
Cdd:cd05945    1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2728 HQLLEEGPARVVLTqssllhtvpwppgvqviavdelepateapplpprgTPEHLAYVIYTSGSTGKPKGVAIEHRAALNT 2807
Cdd:cd05945   81 REILDAAKPALLIA-----------------------------------DGDDNAYIIFTSGSTGRPKGVQISHDNLVSF 125

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2808 VVDLNTRFGVGPEDRVLGLSALTFDLSVYDVLGLLGAGGALVLPAAEAEKDPAHWWERLVAGRVTVWNSTPALMLLLVEY 2887
Cdd:cd05945  126 TNWMLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADPKQLFRFLAEHGITVWVSTPSFAAMCLLS 205

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2888 AEQRGLKLPaALRLVMLSGDWIPVALPDRIRALGRDVQVVSLGGATEASIWSIAYPIGQ-VAPQWKSIPYGMPLANQRFH 2966
Cdd:cd05945  206 PTFTPESLP-SLRHFLFCGEVLPHKTARALQQRFPDARIYNTYGPTEATVAVTYIEVTPeVLDGYDRLPIGYAKPGAKLV 284

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2967 VLDGRLEARPWWVPGELYIGGEGLAREYWRDEPLTATRFIRHPrtGERLYRTGDQGRMLPEGSIEFLGREDLQVKVQGFR 3046
Cdd:cd05945  285 ILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDE--GQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYR 362

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3047 VELGEIEAALAQHPALSASVVVARGEPRGVRRLVAYAVPRSGQTPAAG-ELRRYLAERLPAYMVPSAFVLLESLPRSRNG 3125
Cdd:cd05945  363 IELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPGAEAGLTkAIKAELAERLPPYMIPRRFVYLDELPLNANG 442


                 ....*..
gi 53747904 3126 KIARDQL 3132
Cdd:cd05945  443 KIDRKAL 449
A_NRPS_LgrA-like cd17645
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ...
 2644-3133 1.45e-85

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: 288.68  E-value: 1.45e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2644 FFTQARLHPELPALLAPERTLSYGELARRAQALAARLRELEVQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLDPEQP 2723
Cdd:cd17645    4 FEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYP 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2724 PLRLHQLLEEGPARVVLTQssllhtvpwppgvqviavdelepateapplpprgtPEHLAYVIYTSGSTGKPKGVAIEHRA 2803
Cdd:cd17645   84 GERIAYMLADSSAKILLTN-----------------------------------PDDLAYVIYTSGSTGLPKGVMIEHHN 128

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2804 ALNTVVDLNTRFGVGPEDRVLGLSALTFDLSVYDVLgllgaggalvlpaaeaekdpAHWwerLVAGRVTVWNSTPALMLL 2883
Cdd:cd17645  129 LVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIF--------------------PHL---TAGAALHVVPSERRLDLD 185

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2884 -LVEYAEQRGLK---LPA------------ALRLVMLSGDWIPvalpdriRALGRDVQVVSLGGATEASIWSIAYPIGqv 2947
Cdd:cd17645  186 aLNDYFNQEGITisfLPTgaaeqfmqldnqSLRVLLTGGDKLK-------KIERKGYKLVNNYGPTENTVVATSFEID-- 256

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2948 aPQWKSIPYGMPLANQRFHVLDGRLEARPWWVPGELYIGGEGLAREYWRDEPLTATRFIRHPR-TGERLYRTGDQGRMLP 3026
Cdd:cd17645  257 -KPYANIPIGKPIDNTRVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFvPGERMYRTGDLAKFLP 335

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3027 EGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPALSASVVVARGEPRGVRRLVAYAVPRSGQTPaaGELRRYLAERLPA 3106
Cdd:cd17645  336 DGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTAPEEIPH--EELREWLKNDLPD 413

                        490       500
                 ....*....|....*....|....*..
gi 53747904 3107 YMVPSAFVLLESLPRSRNGKIARDQLP 3133
Cdd:cd17645  414 YMIPTYFVHLKALPLTANGKVDRKALP 440
A_NRPS_ProA cd17656
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ...
 2652-3133 5.40e-84

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: 285.52  E-value: 5.40e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2652 PELPALLAPERTLSYGELARRAQALAARLRELEVQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLDPEQPPLRLHQLL 2731
Cdd:cd17656    2 PDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIM 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2732 EEGPARVVLTQSSllHTVPWP-PGVQVIAVDELEPATEAPPLPPRGTPEHLAYVIYTSGSTGKPKGVAIEHRAALNTVVD 2810
Cdd:cd17656   82 LDSGVRVVLTQRH--LKSKLSfNKSTILLEDPSISQEDTSNIDYINNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLLHF 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2811 LNTRFGVGPEDRVLGLSALTFDLSVYDVLGLLGAGGALVLPAAEAEKDPAHWWERLVAGRVTVWNSTPALMLLLveyAEQ 2890
Cdd:cd17656  160 EREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNIEVVFLPVAFLKFI---FSE 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2891 RGLK--LPAALRLVMLSGDWIPVALPDRIRALGRDVQVVSLGGATEASIWSiAYPIGQVAPQWKSIPYGMPLANQRFHVL 2968
Cdd:cd17656  237 REFInrFPTCVKHIITAGEQLVITNEFKEMLHEHNVHLHNHYGPSETHVVT-TYTINPEAEIPELPPIGKPISNTWIYIL 315

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2969 DGRLEARPWWVPGELYIGGEGLAREYWRDEPLTATRFIRHP-RTGERLYRTGDQGRMLPEGSIEFLGREDLQVKVQGFRV 3047
Cdd:cd17656  316 DQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPfDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRI 395

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3048 ELGEIEAALAQHPALSASVVVARGEPRGVRRLVAYAVPRsgQTPAAGELRRYLAERLPAYMVPSAFVLLESLPRSRNGKI 3127
Cdd:cd17656  396 ELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVME--QELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKV 473


                 ....*.
gi 53747904 3128 ARDQLP 3133
Cdd:cd17656  474 DRKALP 479
A_NRPS_ACVS-like cd17648
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ...
 2684-3133 9.44e-82

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: 278.13  E-value: 9.44e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2684 EVQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLDPEQPPLRLHQLLEEGPARVVLTQSSllhtvpwppgvqviavdel 2763
Cdd:cd17648   34 EIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFILEDTGARVVITNST------------------- 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2764 epateapplpprgtpeHLAYVIYTSGSTGKPKGVAIEHRAALNTVVDLNTRFGVGPED--RVLGLSALTFDLSVYDVLGL 2841
Cdd:cd17648   95 ----------------DLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSLSERYFGRDNGdeAVLFFSNYVFDFFVEQMTLA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2842 LGAGGALVLPAAEAEKDPAHWWERLVAGRVTVWNSTPALmLLLVEYAeqrglKLPAaLRLVMLSGDWIPVALPDRIRALG 2921
Cdd:cd17648  159 LLNGQKLVVPPDEMRFDPDRFYAYINREKVTYLSGTPSV-LQQYDLA-----RLPH-LKRVDAAGEEFTAPVFEKLRSRF 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2922 RDvQVVSLGGATEASIWSIAYPIGQVAPQWKSIpyGMPLANQRFHVLDGRLEARPWWVPGELYIGGEGLAREYWRDEPLT 3001
Cdd:cd17648  232 AG-LIINAYGPTETTVTNHKRFFPGDQRFDKSL--GRPVRNTKCYVLNDAMKRVPVGAVGELYLGGDGVARGYLNRPELT 308

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3002 ATRFIRHPRTGE---------RLYRTGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPALSASVVVARGE 3072
Cdd:cd17648  309 AERFLPNPFQTEqerargrnaRLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKED 388

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 53747904 3073 P-----RGVRRLVAYAVPRSGQTPAAgELRRYLAERLPAYMVPSAFVLLESLPRSRNGKIARDQLP 3133
Cdd:cd17648  389 AsqaqsRIQKYLVGYYLPEPGHVPES-DLLSFLRAKLPRYMVPARLVRLEGIPVTINGKLDVRALP 453
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
 2644-3132 1.00e-80

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: 276.35  E-value: 1.00e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2644 FFTQARLHPELPALLAPERTLSYGELARRAQALAARLRELEVQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLDPEQP 2723
Cdd:cd05918    5 IEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLDPSHP 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2724 PLRLHQLLEEGPARVVLTqssllhtvpwppgvqviavdelepateapplpprGTPEHLAYVIYTSGSTGKPKGVAIEHRA 2803
Cdd:cd05918   85 LQRLQEILQDTGAKVVLT----------------------------------SSPSDAAYVIFTSGSTGKPKGVVIEHRA 130

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2804 ALNTVVDLNTRFGVGPEDRVLGLSALTFDLSVYDVLGLLGAGGALVLPAAEAEK-DPAHWWERLvagRVTVWNSTPALML 2882
Cdd:cd05918  131 LSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLCIPSEEDRLnDLAGFINRL---RVTWAFLTPSVAR 207

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2883 LLveyaeqrGLKLPAALRLVMLSGDwiPVAlPDRIRALGRDVQVVSLGGATEASIWSIAypiGQVAPQWKSIPYGMPLAn 2962
Cdd:cd05918  208 LL-------DPEDVPSLRTLVLGGE--ALT-QSDVDTWADRVRLINAYGPAECTIAATV---SPVVPSTDPRNIGRPLG- 273

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2963 QRFHVLD----GRLeaRPWWVPGELYIGGEGLAREYWRDEPLTATRFIRHP--------RTGERLYRTGDQGRMLPEGSI 3030
Cdd:cd05918  274 ATCWVVDpdnhDRL--VPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPawlkqegsGRGRRLYRTGDLVRYNPDGSL 351

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3031 EFLGREDLQVKVQGFRVELGEIEAALAQHPALSASVVVA---RGEPRGVRRLVAYAVPRSGQT----------------- 3090
Cdd:cd05918  352 EYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKEVVVEvvkPKDGSSSPQLVAFVVLDGSSSgsgdgdslflepsdefr 431

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|..
gi 53747904 3091 PAAGELRRYLAERLPAYMVPSAFVLLESLPRSRNGKIARDQL 3132
Cdd:cd05918  432 ALVAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRAL 473
PRK05691 PRK05691
peptide synthase; Validated
 2171-3214 1.62e-77

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 289.38  E-value: 1.62e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2171 VPDPAARFEP-FPLTDVQEAYWVGRRSAFELGGVAAHGYFEIESPgLEVERFIQCWRQLLQRHDMLRMVVLPDGRQQVLE 2249
Cdd:PRK05691 3247 LPVPAAEIEDvYPLTPMQEGLLLHTLLEPGTGLYYMQDRYRINSA-LDPERFAQAWQAVVARHEALRASFSWNAGETMLQ 3325

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2250 QV--PEYTP-EVVELRGLSP--QEAESRRLQLRERMAHQVLRsdRWPLFELVLCRY-EGGVRIHMSMDALMLDAWSSAVL 2323
Cdd:PRK05691 3326 VIhkPGRTPiDYLDWRGLPEdgQEQRLQALHKQEREAGFDLL--NQPPFHLRLIRVdEARYWFMMSNHHILIDAWCRSLL 3403

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2324 RQDFAQLYHE--PGRPLE-PLAITFRDYV--LAERRLREgeaherARAYWWARLDTLPPPPELPLvKEPSQLEHARFTH- 2397
Cdd:PRK05691 3404 MNDFFEIYTAlgEGREAQlPVPPRYRDYIgwLQRQDLAQ------ARQWWQDNLRGFERPTPIPS-DRPFLREHAGDSGg 3476

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2398 -----REARLEPHRWARLQERARAHGLTPSAACMAAFAEVLARWSRHPRFTLNLTLFQRLPLHPQVDELVGDFTSLVLLE 2472
Cdd:PRK05691 3477 mvvgdCYTRLDAADGARLRELAQAHQLTVNTFAQAAWALVLRRYSGDRDVLFGVTVAGRPVSMPQMQRTVGLFINSIALR 3556

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2473 VEAHAASTFAERASRLQAQL-----WRDLEHGSVSAVQLIRELvrtgrrspgaimpvvftsilsldarrgPQGSlSFFEG 2547
Cdd:PRK05691 3557 VQLPAAGQRCSVRQWLQGLLdsnmeLREYEYLPLVAIQECSEL---------------------------PKGQ-PLFDS 3608

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2548 ELVYSISQTPQVWLDHGVH----------------------EEEGALVLAWDsvEALFPPGMVDDMFHAYQRLLGALAEE 2605
Cdd:PRK05691 3609 LFVFENAPVEVSVLDRAQSlnassdsgrthtnfpltavcypGDDLGLHLSYD--QRYFDAPTVERLLGEFKRLLLALVQG 3686

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2606 EQAWEGELPELLPPAQRELLARYNATQAPRPsgrLEEG----FFTQARLHPELPALLAPERTLSYGELARRAQALAARLR 2681
Cdd:PRK05691 3687 FHGDLSELPLLGEQERDFLLDGCNRSERDYP---LEQSyvrlFEAQVAAHPQRIAASCLDQQWSYAELNRAANRLGHALR 3763

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2682 ELEVQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLDPEQPPLRLHQLLEEGPARVVLTQSS-------LLHTVPWPPG 2754
Cdd:PRK05691 3764 AAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGLPAQRLQRIIELSRTPVLVCSAAcreqaraLLDELGCANR 3843

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2755 VQVIAVDELEPATEAPPLPPR-GTPEHLAYVIYTSGSTGKPKGVAIEHRAALNTVVDLNTRFGVGPEDRVLGLSALTFDL 2833
Cdd:PRK05691 3844 PRLLVWEEVQAGEVASHNPGIySGPDNLAYVIYTSGSTGLPKGVMVEQRGMLNNQLSKVPYLALSEADVIAQTASQSFDI 3923

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2834 SVYDVLGLLGAGGALVLPAAEAEKDPAHWWERLVAGRVTVWNSTPALMLLLVEyAEQRGLklpAALRLVMLSGDWIPVAL 2913
Cdd:PRK05691 3924 SVWQFLAAPLFGARVEIVPNAIAHDPQGLLAHVQAQGITVLESVPSLIQGMLA-EDRQAL---DGLRWMLPTGEAMPPEL 3999

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2914 PDRIRALGRDVQVVSLGGATEASIWSIAYPIGQVAPQWKSIPYGMPLANQRFHVLDGRLEARPWWVPGELYIGGEGLARE 2993
Cdd:PRK05691 4000 ARQWLQRYPQIGLVNAYGPAECSDDVAFFRVDLASTRGSYLPIGSPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRG 4079

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2994 YWRDEPLTATRFIRHP--RTGERLYRTGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPALSASVVVARG 3071
Cdd:PRK05691 4080 YVGDPLRTALAFVPHPfgAPGERLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAVQE 4159

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  3072 EPRGvRRLVAYAVPRSG-QTPAA--GELRRYLAERLPAYMVPSAFVLLESLPRSRNGKIARDQLPEPQQTQGLAAQ-AAA 3147
Cdd:PRK05691 4160 GVNG-KHLVGYLVPHQTvLAQGAllERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKALPALDIGQLQSQAyLAP 4238

                        1050      1060      1070      1080      1090      1100
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 53747904  3148 ADPLVERLAALVKEALRLERVEPQDSLLDLGADSVALIRLINRLEAELQFRPRLADIYENPTVQGLA 3214
Cdd:PRK05691 4239 RNELEQTLATIWADVLKVERVGVHDNFFELGGHSLLATQIASRVQKALQRNVPLRAMFECSTVEELA 4305
Qor COG0604
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ...
 1675-1991 9.11e-76

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: 255.84  E-value: 9.11e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1675 VAVGTPGLLESLGLRRCTRPAPGPRQVEIEVEAAGLNFLDVLGALGMMPALEAEESVLGRECSGRIAAVGEGVSGLRVGD 1754
Cdd:COG0604    4 IVITEFGGPEVLELEEVPVPEPGPGEVLVRVKAAGVNPADLLIRRGLYPLPPGLPFIPGSDAAGVVVAVGEGVTGFKVGD 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1755 EVLA-VAPGCFRSYVLVDESQVVRRPASLGLAEGAAQMVPFATAYFALHTVGRLRRGERILIHaaagglglaaVQLASRT 1833
Cdd:COG0604   84 RVAGlGRGGGYAEYVVVPADQLVPLPDGLSFEEAAALPLAGLTAWQALFDRGRLKPGETVLVHgaaggvgsaaVQLAKAL 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1834 GAEILATAGSEQKREYLRSLGIAHVLDSRSTSFVSEVRERTGGRGVDVVLNSLAGELLLAGLSVLAPHGRFLELGKRDLY 1913
Cdd:COG0604  164 GARVIATASSPEKAELLRALGADHVIDYREEDFAERVRALTGGRGVDVVLDTVGGDTLARSLRALAPGGRLVSIGAASGA 243

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 53747904 1914 ADQQVGLRTLARGQTFAAIDFGPHHPD-FRAVLEEVATQLTQGQLEPLPTRLFPARQVAEAFSFMARALHIGRVAVSMQ 1991
Cdd:COG0604  244 PPPLDLAPLLLKGLTLTGFTLFARDPAeRRAALAELARLLAAGKLRPVIDRVFPLEEAAEAHRLLESGKHRGKVVLTVD 322
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
 2644-3134 2.11e-75

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: 259.74  E-value: 2.11e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2644 FFTQARLHPELPALLAPERTLSYGELARRAQALAARLRELEVQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLDPEQP 2723
Cdd:COG0318    5 LRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLT 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2724 PLRLHQLLEEGPARVVLTqssllhtvpwppgvqviavdelepateapplpprgtpehlAYVIYTSGSTGKPKGVAIEHRA 2803
Cdd:COG0318   85 AEELAYILEDSGARALVT----------------------------------------ALILYTSGTTGRPKGVMLTHRN 124

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2804 ALNTVVDLNTRFGVGPEDRVLGLSALTFDLSVYDVLGLLGAGGALVLPAAEAekDPAHWWERLVAGRVTVWNSTPALMLL 2883
Cdd:COG0318  125 LLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPRF--DPERVLELIERERVTVLFGVPTMLAR 202

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2884 LVEYAEQRGLKLPAaLRLVMLSGDWIPVALPDRIRALGrDVQVVSLGGATEASIWSIAYPIGQVAPQWKSIpyGMPLANQ 2963
Cdd:COG0318  203 LLRHPEFARYDLSS-LRLVVSGGAPLPPELLERFEERF-GVRIVEGYGLTETSPVVTVNPEDPGERRPGSV--GRPLPGV 278

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2964 RFHVLDGRLEARPWWVPGELYIGGEGLAREYWRDEPLTATRFIrhprtgERLYRTGDQGRMLPEGSIEFLGREDLQVKVQ 3043
Cdd:COG0318  279 EVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFR------DGWLRTGDLGRLDEDGYLYIVGRKKDMIISG 352

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3044 GFRVELGEIEAALAQHPALSASVVVARGEPRGVRRLVAYAVPRSGQTPAAGELRRYLAERLPAYMVPSAFVLLESLPRSR 3123
Cdd:COG0318  353 GENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAELDAEELRAFLRERLARYKVPRRVEFVDELPRTA 432

                        490
                 ....*....|.
gi 53747904 3124 NGKIARDQLPE 3134
Cdd:COG0318  433 SGKIDRRALRE 443
A_NRPS_GliP_like cd17653
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ...
 2644-3132 3.29e-75

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: 258.39  E-value: 3.29e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2644 FFTQARLHPELPALLAPERTLSYGELARRAQALAARLRELEVQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLDPEQP 2723
Cdd:cd17653    3 FERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2724 PLRLHQLLEEGPARVVLTQSSllhtvpwppgvqviavdelepateapplpprgtPEHLAYVIYTSGSTGKPKGVAIEHRA 2803
Cdd:cd17653   83 SARIQAILRTSGATLLLTTDS---------------------------------PDDLAYIIFTSGSTGIPKGVMVPHRG 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2804 ALNTVVDLNTRFGVGPEDRVLGLSALTFDLSVYDVLGLLGAGgalvlpAAEAEKDPAHWWERlVAGRVTVWNSTPAlmlL 2883
Cdd:cd17653  130 VLNYVSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNG------GTLVLADPSDPFAH-VARTVDALMSTPS---I 199

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2884 LVEYAEQRglkLPaALRLVMLSGDWIPvalPDRIRALGRDVQVVSLGGATEASIwSIAYPigQVAPQwKSIPYGMPLANQ 2963
Cdd:cd17653  200 LSTLSPQD---FP-NLKTIFLGGEAVP---PSLLDRWSPGRRLYNAYGPTECTI-SSTMT--ELLPG-QPVTIGKPIPNS 268

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2964 RFHVLDGRLEARPWWVPGELYIGGEGLAREYWRDEPLTATRFIRHPR-TGERLYRTGDQGRMLPEGSIEFLGREDLQVKV 3042
Cdd:cd17653  269 TCYILDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFwPGSRMYRTGDYGRWTEDGGLEFLGREDNQVKV 348

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3043 QGFRVELGEIEAALAQHPAL--SASVVVARGeprgvrRLVAYAVPrsgQTPAAGELRRYLAERLPAYMVPSAFVLLESLP 3120
Cdd:cd17653  349 RGFRINLEEIEEVVLQSQPEvtQAAAIVVNG------RLVAFVTP---ETVDVDGLRSELAKHLPSYAVPDRIIALDSFP 419

                        490
                 ....*....|..
gi 53747904 3121 RSRNGKIARDQL 3132
Cdd:cd17653  420 LTANGKVDRKAL 431
AMP-binding pfam00501
AMP-binding enzyme;
2644-3043 1.17e-74

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 256.47  E-value: 1.17e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   2644 FFTQARLHPELPALL-APERTLSYGELARRAQALAARLRELEVQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLDPEQ 2722
Cdd:pfam00501    1 LERQAARTPDKTALEvGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   2723 PPLRLHQLLEEGPARVVLTQSSLL------HTVPWPPGVQVIAVD------------ELEPATEAPPLPPRGTPEHLAYV 2784
Cdd:pfam00501   81 PAEELAYILEDSGAKVLITDDALKleelleALGKLEVVKLVLVLDrdpvlkeeplpeEAKPADVPPPPPPPPDPDDLAYI 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   2785 IYTSGSTGKPKGVAIEHRAALNTVVDL----NTRFGVGPEDRVLGLSALTFDLSV-YDVLGLLGAGGALVLPAAEAEKDP 2859
Cdd:pfam00501  161 IYTSGTTGKPKGVMLTHRNLVANVLSIkrvrPRGFGLGPDDRVLSTLPLFHDFGLsLGLLGPLLAGATVVLPPGFPALDP 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   2860 AHWWERLVAGRVTVWNSTPALMLLLVEYAEQRGLKLPaALRLVMLSGDWIPVALPDRIRALGRDvQVVSLGGATEASIWS 2939
Cdd:pfam00501  241 AALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLS-SLRLVLSGGAPLPPELARRFRELFGG-ALVNGYGLTETTGVV 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   2940 IAYPIGQvaPQWKSIP-YGMPLANQRFHVLD-GRLEARPWWVPGELYIGGEGLAREYWRDEPLTATRFIRhprtgERLYR 3017
Cdd:pfam00501  319 TTPLPLD--EDLRSLGsVGRPLPGTEVKIVDdETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDE-----DGWYR 391

                          410       420
                   ....*....|....*....|....*.
gi 53747904   3018 TGDQGRMLPEGSIEFLGREDLQVKVQ 3043
Cdd:pfam00501  392 TGDLGRRDEDGYLEIVGRKKDQIKLG 417
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
 11-241 5.70e-68

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: 230.60  E-value: 5.70e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904     11 SSIALVGMAGRFPGAPDVESFWRNLVAGVESISFFSEEELRQAGVSEQIRRRPEYVPAK-GVLEDLELFDAGFFGYSPRE 89
Cdd:pfam00109    1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIPADRWDPDKLYDPPSRIAGKIYTKwGGLDDIFDFDPLFFGISPRE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904     90 ASHLDPQQRLLLECSWEALEDAGLRPDQLPG-WVGVYVGAGDTSYR-FQLLRGHGDPLSGSkdvAGFFGNYPDFLATRVA 167
Cdd:pfam00109   81 AERMDPQQRLLLEAAWEALEDAGITPDSLDGsRTGVFIGSGIGDYAaLLLLDEDGGPRRGS---PFAVGTMPSVIAGRIS 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 53747904    168 YKLNLRGPALGIHTACSTSLVSINMACSALRGFECDMALAGGVSLRLPARSGYLYEEGGVASKDGHCRPFDARA 241
Cdd:pfam00109  158 YFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSPDGPCKAFDPFA 231
polyketide_synthase cd08251
polyketide synthase; Polyketide synthases produce polyketides in step by step mechanism that ...
 1694-1988 7.81e-64

polyketide synthase; Polyketide synthases produce polyketides in step by step mechanism that is similar to fatty acid synthesis. Enoyl reductase reduces a double to single bond. Erythromycin is one example of a polyketide generated by 3 complex enzymes (megasynthases). 2-enoyl thioester reductase (ETR) catalyzes the NADPH-dependent dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding.


Pssm-ID: 176213 [Multi-domain]  Cd Length: 303  Bit Score: 220.76  E-value: 7.81e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1694 PAPGPRQVEIEVEAAGLNFLDVLGALGMMPALEAEESVLGRECSGRIAAVGEGVSGLRVGDEVLAVAP---GCFRSYVLV 1770
Cdd:cd08251    3 APPGPGEVRIQVRAFSLNFGDLLCVRGLYPTMPPYPFTPGFEASGVVRAVGPHVTRLAVGDEVIAGTGesmGGHATLVTV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1771 DESQVVRRPASLGLAEGAAQMVPFATAYFALHTvGRLRRGERILIHAAAGGLGLAAVQLASRTGAEILATAGSEQKREYL 1850
Cdd:cd08251   83 PEDQVVRKPASLSFEEACALPVVFLTVIDAFAR-AGLAKGEHILIQTATGGTGLMAVQLARLKGAEIYATASSDDKLEYL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1851 RSLGIAHVLDSRSTSFVSEVRERTGGRGVDVVLNSLAGELLLAGLSVLAPHGRFLELGKRDLYADQQVGLRTLARGQTFA 1930
Cdd:cd08251  162 KQLGVPHVINYVEEDFEEEIMRLTGGRGVDVVINTLSGEAIQKGLNCLAPGGRYVEIAMTALKSAPSVDLSVLSNNQSFH 241

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 53747904 1931 AIDF---GPHHPDFRA-VLEEVATQLTQGQLEPLPTRLFPARQVAEAFSFMARALHIGRVAV 1988
Cdd:cd08251  242 SVDLrklLLLDPEFIAdYQAEMVSLVEEGELRPTVSRIFPFDDIGEAYRYLSDRENIGKVVV 303
AFD_class_I cd04433
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ...
 2780-3127 1.93e-62

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: 217.92  E-value: 1.93e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2780 HLAYVIYTSGSTGKPKGVAIEHRAALNTVVDLNTRFGVGPEDRVLGLSALTFDLSVYDVLGLLGAGGALVLPAAEaekDP 2859
Cdd:cd04433    1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKF---DP 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2860 AHWWERLVAGRVTVWNSTPALMLLLVEYAEQRGLKLPAaLRLVMLSGDWIPVALPDRIRALgRDVQVVSLGGATEASIWS 2939
Cdd:cd04433   78 EAALELIEREKVTILLGVPTLLARLLKAPESAGYDLSS-LRALVSGGAPLPPELLERFEEA-PGIKLVNGYGLTETGGTV 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2940 IAYPIGQVAPQWKSIpyGMPLANQRFHVLDGRLEARPWWVPGELYIGGEGLAREYWRDEPLTAtrfirhPRTGERLYRTG 3019
Cdd:cd04433  156 ATGPPDDDARKPGSV--GRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATA------AVDEDGWYRTG 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3020 DQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPALSASVVVARGEPRGVRRLVAYAVPRSGQTPAAGELRRY 3099
Cdd:cd04433  228 DLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDAEELRAH 307

                        330       340
                 ....*....|....*....|....*...
gi 53747904 3100 LAERLPAYMVPSAFVLLESLPRSRNGKI 3127
Cdd:cd04433  308 VRERLAPYKVPRRVVFVDALPRTASGKI 335
FabD COG0331
Malonyl CoA-acyl carrier protein transacylase [Lipid transport and metabolism]; Malonyl ...
 534-817 1.27e-61

Malonyl CoA-acyl carrier protein transacylase [Lipid transport and metabolism]; Malonyl CoA-acyl carrier protein transacylase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440100 [Multi-domain]  Cd Length: 306  Bit Score: 214.61  E-value: 1.27e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  534 LVMLFPGQGTPLVGTARALHESEPTFRQAVEQcarlLRQTLGLDVREVLFPSAEQEeqarrlAAQTRVAQPALFTLEYAL 613
Cdd:COG0331    3 LAFLFPGQGSQYVGMGKDLYENFPVAREVFEE----ASEALGYDLSALCFEGPEEE------LNLTENTQPAILAASVAA 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  614 AQTWLGWGLQPQALAGHSLGELVAACLAGVFSLEDALQLVAARGQLMQGCPP---GAMLAV-PLPEAELAALL-----GS 684
Cdd:COG0331   73 YRALEEEGIRPDAVAGHSLGEYSALVAAGALSFEDALRLVRLRGRLMQEAVPagpGGMAAVlGLDDEEVEALCaeaaqGE 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  685 ELCIAAVNGPRACVASGPLPAVEALTAALESRGVS-SRRLETSHAFHSASMEACQGPLTTLLRRMRLQAPRLPCVSGLTG 763
Cdd:COG0331  153 VVEIANYNSPGQIVISGEKEAVEAAAELAKEAGAKrAVPLPVSGPFHTPLMAPAAEKLAEALAAVTFADPKIPVVSNVDA 232

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 53747904  764 RWLTGEEATePTYWARQLREPVRFSEALETLWSLKEPVLLEVGPGTTLTALARR 817
Cdd:COG0331  233 APVTDPEEI-RELLVRQLTSPVRWDESVEALAEAGVTTFVELGPGKVLSGLVKR 285
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
 23-431 1.46e-58

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: 209.32  E-value: 1.46e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   23 PGAPDVESFWRNLVAG---VESISFFSEEELRqagvseqiRRRPEYVPAkgvledlelFDAGFFGySPREASHLDPQQRL 99
Cdd:cd00834   13 PLGNGVEEFWEALLAGrsgIRPITRFDASGFP--------SRIAGEVPD---------FDPEDYL-DRKELRRMDRFAQF 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  100 LLECSWEALEDAGLRPDQLPGW-VGVYVG---AGDTSYRFQLLRGHGDplsGSKDVAGFFGNY--PDFLATRVAYKLNLR 173
Cdd:cd00834   75 ALAAAEEALADAGLDPEELDPErIGVVIGsgiGGLATIEEAYRALLEK---GPRRVSPFFVPMalPNMAAGQVAIRLGLR 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  174 GPALGIHTACSTSLVSINMACSALRGFECDMALAGGV-SLRLP------ARSGYLYEEGGVASKdgHCRPFDAR------ 240
Cdd:cd00834  152 GPNYTVSTACASGAHAIGDAARLIRLGRADVVIAGGAeALITPltlagfAALRALSTRNDDPEK--ASRPFDKDrdgfvl 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  241 ----ATGTvtgdgvgvvvLKRLEDALKARDPIHAVIRGWALNNDGASragFTAPSV--EGQSEVIALAHAAAGISARDIT 314
Cdd:cd00834  230 gegaGVLV----------LESLEHAKARGAKIYAEILGYGASSDAYH---ITAPDPdgEGAARAMRAALADAGLSPEDID 296

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  315 YVEAHGTGTPLGDPIEVAALTRAFRAHTADTAFCtlgAVKSNIGHLDAAAGVAGVIKTVQALRHRLIPPTLHFERPNPAL 394
Cdd:cd00834  297 YINAHGTSTPLNDAAESKAIKRVFGEHAKKVPVS---STKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPEC 373

                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 53747904  395 HLEqspfFVNTQPLPWESPrgprlAGVS-SFGIGGTNA 431
Cdd:cd00834  374 DLD----YVPNEAREAPIR-----YALSnSFGFGGHNA 402
decarbox_cond_enzymes cd00825
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ...
 96-432 6.06e-56

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: 199.40  E-value: 6.06e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   96 QQRLLLECSWEALEDAGLRPDQLPGW-VGVYVGAGDTSYRFQLLRGHGDPLSGSKDVAGFFgnYPdFLATRVAYKLNLRG 174
Cdd:cd00825   11 VSILGFEAAERAIADAGLSREYQKNPiVGVVVGTGGGSPRFQVFGADAMRAVGPYVVTKAM--FP-GASGQIATPLGIHG 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  175 PALGIHTACSTSLVSINMACSALRGFECDMALAGGVSLRLPARSGYLYEEGGVASKDGHCRPFDARATGTVTGDGVGVVV 254
Cdd:cd00825   88 PAYDVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAPMDCEFDAMGALSTPEKASRTFDAAADGFVFGDGAGALV 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  255 LKRLEDALKARDPIHAVIRGWALNNDGASRaGFTAPSVEGQSEVIALAHAAAGISARDITYVEAHGTGTPLGDPIEVAAL 334
Cdd:cd00825  168 VEELEHALARGAHIYAEIVGTAATIDGAGM-GAFAPSAEGLARAAKEALAVAGLTVWDIDYLVAHGTGTPIGDVKELKLL 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  335 TRAFRAHTAdtafcTLGAVKSNIGHLDAAAGVAGVIKTVQALRHRLIPPTLHFERPNPALHLEQSPffvntqplpwESPR 414
Cdd:cd00825  247 RSEFGDKSP-----AVSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPPSIHIEELDEAGLNIVTE----------TTPR 311

                        330
                 ....*....|....*...
gi 53747904  415 GPRLAGVSSFGIGGTNAH 432
Cdd:cd00825  312 ELRTALLNGFGLGGTNAT 329
p53_inducible_oxidoreductase cd05276
PIG3 p53-inducible quinone oxidoreductase; PIG3 p53-inducible quinone oxidoreductase, a medium ...
 1675-1986 1.24e-54

PIG3 p53-inducible quinone oxidoreductase; PIG3 p53-inducible quinone oxidoreductase, a medium chain dehydrogenase/reductase family member, acts in the apoptotic pathway. PIG3 reduces ortho-quinones, but its apoptotic activity has been attributed to oxidative stress generation, since overexpression of PIG3 accumulates reactive oxygen species. PIG3 resembles the MDR family member quinone reductases, which catalyze the reduction of quinone to hydroxyquinone. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176180 [Multi-domain]  Cd Length: 323  Bit Score: 194.97  E-value: 1.24e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1675 VAVGTPGLLESLGLRRCTRPAPGPRQVEIEVEAAGLNFLDVLGALGMMPALEAEESVLGRECSGRIAAVGEGVSGLRVGD 1754
Cdd:cd05276    4 IVIKEPGGPEVLELGEVPKPAPGPGEVLIRVAAAGVNRADLLQRQGLYPPPPGASDILGLEVAGVVVAVGPGVTGWKVGD 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1755 EVLAVAPGC-FRSYVLVDESQVVRRPASLGLAEGAAqmVP--FATAYFALHTVGRLRRGERILIHAAAGGLGLAAVQLAS 1831
Cdd:cd05276   84 RVCALLAGGgYAEYVVVPAGQLLPVPEGLSLVEAAA--LPevFFTAWQNLFQLGGLKAGETVLIHGGASGVGTAAIQLAK 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1832 RTGAEILATAGSEQKREYLRSLGIAHVLDSRSTSFVSEVRERTGGRGVDVVLNSLAGELLLAGLSVLAPHGRFLELG--- 1908
Cdd:cd05276  162 ALGARVIATAGSEEKLEACRALGADVAINYRTEDFAEEVKEATGGRGVDVILDMVGGDYLARNLRALAPDGRLVLIGllg 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1909 -------------KRdlyadqqvgLR----TLaRGQTF---AAIdfgphhpdFRAVLEEVATQLTQGQLEPLPTRLFPAR 1968
Cdd:cd05276  242 gakaeldlapllrKR---------LTltgsTL-RSRSLeekAAL--------AAAFREHVWPLFASGRIRPVIDKVFPLE 303

                        330
                 ....*....|....*...
gi 53747904 1969 QVAEAFSFMARALHIGRV 1986
Cdd:cd05276  304 EAAEAHRRMESNEHIGKI 321
FabB COG0304
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...
 23-431 5.26e-54

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: 196.08  E-value: 5.26e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   23 PGAPDVESFWRNLVAG---VESISFFSEEELRqagvseqirrrpeyVPAKGVLEDLELFDAgffgYSPREASHLDPQQRL 99
Cdd:COG0304   13 PLGNGVEEFWEALLAGrsgIRPITRFDASGLP--------------VRIAGEVKDFDPEEY----LDRKELRRMDRFTQY 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  100 LLECSWEALEDAGLRPDQLPGW-VGVYVGAG----DTSYRF-QLLRGHGDPLSGSKDVAGFFGNYPdflATRVAYKLNLR 173
Cdd:COG0304   75 ALAAAREALADAGLDLDEVDPDrTGVIIGSGigglDTLEEAyRALLEKGPRRVSPFFVPMMMPNMA---AGHVSIRFGLK 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  174 GPALGIHTACSTSLVSINMACSALRGFECDMALAGGVSLRL-PARSGYLYEEGGVASKDGH----CRPFDARAtgtvtgd 248
Cdd:COG0304  152 GPNYTVSTACASGAHAIGEAYRLIRRGRADVMIAGGAEAAItPLGLAGFDALGALSTRNDDpekaSRPFDKDRdgfvlge 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  249 gvgvvvLKRLEDAlKARD-PIHAVIRGWALNNDGASRAGfTAPSVEGQSEVIALAHAAAGISARDITYVEAHGTGTPLGD 327
Cdd:COG0304  232 gagvlvLEELEHA-KARGaKIYAEVVGYGASSDAYHITA-PAPDGEGAARAMRAALKDAGLSPEDIDYINAHGTSTPLGD 309

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  328 PIEVAALTRAFRAHTADTAfctLGAVKSNIGHLDAAAGVAGVIKTVQALRHRLIPPTLHFERPNPALHLEqspfFVNTQP 407
Cdd:COG0304  310 AAETKAIKRVFGDHAYKVP---VSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPECDLD----YVPNEA 382

                        410       420
                 ....*....|....*....|....
gi 53747904  408 LPWEsprgPRLAGVSSFGIGGTNA 431
Cdd:COG0304  383 REAK----IDYALSNSFGFGGHNA 402
C_NRPS-like cd19066
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
 2180-2605 6.83e-54

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: 196.48  E-value: 6.83e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2180 PFPLTDVQEAYWVGR-----RSAFelggvaaHGYFEIESPG-LEVERFIQCWRQLLQRHDMLRMVVL---PDGRQQVLEQ 2250
Cdd:cd19066    1 KIPLSPMQRGMWFLKklatdPSAF-------NVAIEMFLTGsLDLARLKQALDAVMERHDVLRTRFCeeaGRYEQVVLDK 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2251 VPEYTPEVVELRGLSPQEAesRRLQLRERMAHQVLRSDRWPLFELVLCRY-EGGVRIHMSMDALMLDAWSSAVLRQDFAQ 2329
Cdd:cd19066   74 TVRFRIEIIDLRNLADPEA--RLLELIDQIQQTIYDLERGPLVRVALFRLaDERDVLVVAIHHIIVDGGSFQILFEDISS 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2330 LY--HEPGRP-LEPLAITFRDYVLAERRLREGEAHERARAYWWARLDTLPPPPELPLVKEPSQLEHARFTHREARLEPHR 2406
Cdd:cd19066  152 VYdaAERQKPtLPPPVGSYADYAAWLEKQLESEAAQADLAYWTSYLHGLPPPLPLPKAKRPSQVASYEVLTLEFFLRSEE 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2407 WARLQERARAHGLTPSAACMAAFAEVLARWSRHPRFTLNLTLFQRLPlhPQVDELVGDFTSLVLLEVEAHAASTFAERAS 2486
Cdd:cd19066  232 TKRLREVARESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPD--EAVEDTIGLFLNLLPLRIDTSPDATFPELLK 309

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2487 RLQAQLWRDLEHGSVSAVQLIRELVRTGRRSPGAIMPVVFTSILsldarrGPQGSLS---FFEGELVYSISQTPQVWLDH 2563
Cdd:cd19066  310 RTKEQSREAIEHQRVPFIELVRHLGVVPEAPKHPLFEPVFTFKN------NQQQLGKtggFIFTTPVYTSSEGTVFDLDL 383

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 53747904 2564 GVHEE-EGALVLAWDSVEALFPPGMVDDMFHAYQRLLGALAEE 2605
Cdd:cd19066  384 EASEDpDGDLLLRLEYSRGVYDERTIDRFAERYMTALRQLIEN 426
McbC_SagB-like_oxidoreductase cd02142
oxidase similar to the microcin B17 processing protein McbC; This family is the oxidase domain ...
 3261-3462 1.32e-53

oxidase similar to the microcin B17 processing protein McbC; This family is the oxidase domain of NRPS (non-ribosomal peptide synthetase) and other systems that modify polypeptides by cyclizing a thioester to form a ring. These include EpoB, part of the epothilone biosynthesis pathway; TubD, part of the tubulysin biosynthesis pathway, MtsD, part of the myxothiozol biosynthesis pathway; IndC, part of the indigoidine biosynthesis pathway and TfxB, part of the trifitoxin processing pathway. All are FMN-dependent and oxidize the product of the cyclization of thioesters in short polypeptides.


Pssm-ID: 380318  Cd Length: 200  Bit Score: 187.24  E-value: 1.32e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3261 GTPEVALPGSGLAPAPEELTALERRRSVRTYSLEPVSHEQLGRLLAplREWEVQGSRRYLYASAGGLYPVQLYLHLKPGR 3340
Cdd:cd02142    3 VPLPDPNLKPALLATLDLSEALLNRRSRRTFSSEPLTLRELSRLAA--RGIPGSGYGLRPYPSAGALYPIEVYVIVKNVE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3341 arGLEPGTWYYDPSTHRLVLLSAGAGLDRRIHdPHQNQAIFDSAAFSLFLIARMGAVEPVYAEHALHFATLEAGLMTQLL 3420
Cdd:cd02142   81 --GLPAGIYHYDPKRHRLVLIREGDFRLDLAH-AAGNQAAFGSAAFSLIIVARFERIAWKYGERAYRYILLEAGHLAQNL 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 53747904 3421 DLGAAPSGLGLCHIGDLDFAQARGLFHLEE-EHVLLHSLVGGV 3462
Cdd:cd02142  158 YLAATALGLGLCAIGAFDDDALRELLGLDEvEEVVLYAFVVGG 200
QOR1 cd08241
Quinone oxidoreductase (QOR); QOR catalyzes the conversion of a quinone + NAD(P)H to a ...
 1694-1988 1.56e-53

Quinone oxidoreductase (QOR); QOR catalyzes the conversion of a quinone + NAD(P)H to a hydroquinone + NAD(P)+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR acts in the respiratory chains of bacteria and mitochondria, while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family, but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176203 [Multi-domain]  Cd Length: 323  Bit Score: 191.94  E-value: 1.56e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1694 PAPG-PRQVEIEVEAAGLNFLDVLGALG---MMPALEAeesVLGRECSGRIAAVGEGVSGLRVGDEVLAVAP-GCFRSYV 1768
Cdd:cd08241   22 PEPGaPGEVRIRVEAAGVNFPDLLMIQGkyqVKPPLPF---VPGSEVAGVVEAVGEGVTGFKVGDRVVALTGqGGFAEEV 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1769 LVDESQVVRRPASLGLAEGAAQMVPFATAYFALHTVGRLRRGERILIHAAAGGLGLAAVQLASRTGAEILATAGSEQKRE 1848
Cdd:cd08241   99 VVPAAAVFPLPDGLSFEEAAALPVTYGTAYHALVRRARLQPGETVLVLGAAGGVGLAAVQLAKALGARVIAAASSEEKLA 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1849 YLRSLGIAHVLDSRSTSFVSEVRERTGGRGVDVVLNSLAGELLLAGLSVLAPHGRFLELGkrdlYAD---QQVGL-RTLA 1924
Cdd:cd08241  179 LARALGADHVIDYRDPDLRERVKALTGGRGVDVVYDPVGGDVFEASLRSLAWGGRLLVIG----FASgeiPQIPAnLLLL 254

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 53747904 1925 RGQTFAAIDFGP---HHPD-FRAVLEEVATQLTQGQLEPLPTRLFPARQVAEAFSFMARALHIGRVAV 1988
Cdd:cd08241  255 KNISVVGVYWGAyarREPElLRANLAELFDLLAEGKIRPHVSAVFPLEQAAEALRALADRKATGKVVL 322
MDR2 cd08268
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 1694-1988 1.76e-51

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176229 [Multi-domain]  Cd Length: 328  Bit Score: 186.27  E-value: 1.76e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1694 PAPGPRQVEIEVEAAGLNFLDVL---GALGMMPALEAeesVLGRECSGRIAAVGEGVSGLRVGDEVLAVAP------GCF 1764
Cdd:cd08268   23 PAPGAGEVLIRVEAIGLNRADAMfrrGAYIEPPPLPA---RLGYEAAGVVEAVGAGVTGFAVGDRVSVIPAadlgqyGTY 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1765 RSYVLVDESQVVRRPASLGLAEGAAQMVPFATAYFALHTVGRLRRGERILIHAAAGGLGLAAVQLASRTGAEILATAGSE 1844
Cdd:cd08268  100 AEYALVPAAAVVKLPDGLSFVEAAALWMQYLTAYGALVELAGLRPGDSVLITAASSSVGLAAIQIANAAGATVIATTRTS 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1845 QKREYLRSLGIAHVLDSRSTSFVSEVRERTGGRGVDVVLNSLAGELLLAGLSVLAPHGRFLELGKRDLYADQQVGLRTLA 1924
Cdd:cd08268  180 EKRDALLALGAAHVIVTDEEDLVAEVLRITGGKGVDVVFDPVGGPQFAKLADALAPGGTLVVYGALSGEPTPFPLKAALK 259

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 53747904 1925 RGQTFAAIDFGPHHPD---FRAVLEEVATQLTQGQLEPLPTRLFPARQVAEAFSFMARALHIGRVAV 1988
Cdd:cd08268  260 KSLTFRGYSLDEITLDpeaRRRAIAFILDGLASGALKPVVDRVFPFDDIVEAHRYLESGQQIGKIVV 326
Ketoacyl-synt_C pfam02801
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ...
 269-388 5.02e-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: 5.02e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904    269 HAVIRGWALNNDGASrAGFTAPSVEGQSEVIALAHAAAGISARDITYVEAHGTGTPLGDPIEVAALTRAFRAHtADTAFC 348
Cdd:pfam02801    1 YAVIKGSAVNHDGRH-NGLTAPNGEGQARAIRRALADAGVDPEDVDYVEAHGTGTPLGDPIEAEALKRVFGSG-ARKQPL 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 53747904    349 TLGAVKSNIGHLDAAAGVAGVIKTVQALRHRLIPPTLHFE 388
Cdd:pfam02801   79 AIGSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLNLE 118
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
 967-1373 1.02e-50

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: 187.57  E-value: 1.02e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  967 VEPAGHYEQLSEHAFRLRPEseEDWDALFQALQSQGRLPRRILHAWALTAEPGPC---TPDGEAVL-------EQGFFSL 1036
Cdd:cd08953   10 VIDLAYTLQVGREAMEERRR--LEALASLQPVWAPAALASAFLALAYEAALLGLAaaeAALLDALSaldpaaaLQLLESL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1037 LRLARALGRHApeRPVQLEVLSSFVHAVG--PREPLEPLKATLLGACAVLPLEYPHVQCRTIDVRPGSEPREVLVRSLAA 1114
Cdd:cd08953   88 QRLLKAGLLAA--RASGRALLQVVTGLPGalGLDALDPAGAGLAGLLRTLAQEYPGLTCRLIDLDAGEASAEALARELAA 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1115 ELAAPMGESpVAWRDGQRYVRRATRQRLEASRPLRS-LRERGVYLVAGGLGGIGLVLARALAQRARARLALLTHSPFPPR 1193
Cdd:cd08953  166 ELAAPGAAE-VRYRDGLRYVQTLEPLPLPAGAAASApLKPGGVYLVTGGAGGIGRALARALARRYGARLVLLGRSPLPPE 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1194 EQWEQWLeeapahpepawrseadpserrrtqhrircLLELEQLGAEVQVYTADVAEEAAVRSVVEQVHARWGKIHGVLHA 1273
Cdd:cd08953  245 EEWKAQT-----------------------------LAALEALGARVLYISADVTDAAAVRRLLEKVRERYGAIDGVIHA 295

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1274 AATFDDGVIQLRTHEQSSRALRTKVRGSMVLHEVLASEGLDWFALCSSLASALGSFGQADYCAANAFQDAYAHHLRRQG- 1352
Cdd:cd08953  296 AGVLRDALLAQKTAEDFEAVLAPKVDGLLNLAQALADEPLDFFVLFSSVSAFFGGAGQADYAAANAFLDAFAAYLRQRGp 375

                        410       420
                 ....*....|....*....|.
gi 53747904 1353 FTGALALDWGTWRDTGAAMRL 1373
Cdd:cd08953  376 QGRVLSINWPAWREGGMAADL 396
PRK04813 PRK04813
D-alanine--poly(phosphoribitol) ligase subunit DltA;
2648-3132 7.28e-48

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


Pssm-ID: 235313 [Multi-domain]  Cd Length: 503  Bit Score: 180.86  E-value: 7.28e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2648 ARLHPELPALLAPERTLSYGELARRAQALAARLRELEVQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLDPEQPPLRL 2727
Cdd:PRK04813   12 AQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVDVSSPAERI 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2728 HQLLEEGPARVVLTqssllhTVPWPP---GVQVIAVDELEPATEAPPLPPrgtPEHL------AYVIYTSGSTGKPKGVA 2798
Cdd:PRK04813   92 EMIIEVAKPSLIIA------TEELPLeilGIPVITLDELKDIFATGNPYD---FDHAvkgddnYYIIFTSGTTGKPKGVQ 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2799 IEHrAALNTVVD-LNTRFGVGPEDRVLGLSALTFDLSVYDvlgllgaggalVLPA-----------AEAEKDPAHWWERL 2866
Cdd:PRK04813  163 ISH-DNLVSFTNwMLEDFALPEGPQFLNQAPYSFDLSVMD-----------LYPTlasggtlvalpKDMTANFKQLFETL 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2867 VAGRVTVWNSTPALM---LLLVEYAEQrglKLPaALRLVMLSGDWIPVALPDRIRALGRDVQVVSLGGATEASIWSIAYP 2943
Cdd:PRK04813  231 PQLPINVWVSTPSFAdmcLLDPSFNEE---HLP-NLTHFLFCGEELPHKTAKKLLERFPSATIYNTYGPTEATVAVTSIE 306

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2944 IGQ-VAPQWKSIPYGMPLANQRFHVLDGRLEARPWWVPGELYIGGEGLAREYWRDEPLTATRFIrhPRTGERLYRTGDQG 3022
Cdd:PRK04813  307 ITDeMLDQYKRLPIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFF--TFDGQPAYHTGDAG 384

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  3023 RMlPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPALSASVVVARGEPRGVRRLVAYAVPRSGQTPAAGEL----RR 3098
Cdd:PRK04813  385 YL-EDGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYNKDHKVQYLIAYVVPKEEDFEREFELtkaiKK 463

                         490       500       510
                  ....*....|....*....|....*....|....
gi 53747904  3099 YLAERLPAYMVPSAFVLLESLPRSRNGKIARDQL 3132
Cdd:PRK04813  464 ELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
elong_cond_enzymes cd00828
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ...
 24-434 7.52e-47

"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: 175.32  E-value: 7.52e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   24 GAPDVESFWRNLVAGVESISFFSEEELRQA-GVSEQIRrrpeyvpakgvledlelfDAGFFGYSPREASHLDPQQRLLLE 102
Cdd:cd00828   17 GCDEVEEFWEALREGRSGIAPVARLKSRFDrGVAGQIP------------------TGDIPGWDAKRTGIVDRTTLLALV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  103 CSWEALEDAGLRPDQL--PGWVGVYVGAGDTSYRFQLLRGHGDPLSGSKDVAGFFGNYPDFLATRVAYKLNL-RGPALGI 179
Cdd:cd00828   79 ATEEALADAGITDPYEvhPSEVGVVVGSGMGGLRFLRRGGKLDARAVNPYVSPKWMLSPNTVAGWVNILLLSsHGPIKTP 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  180 HTACSTSLVSINMACSALRGFECDMALAGGVSLRLP------ARSGYLYEEGGVASkdGHCRPFDARATGTVTGDGVGVV 253
Cdd:cd00828  159 VGACATALEALDLAVEAIRSGKADIVVVGGVEDPLEeglsgfANMGALSTAEEEPE--EMSRPFDETRDGFVEAEGAGVL 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  254 VLKRLEDALKARDPIHAVIRGWALNNDGASRAGftAPSVEGQSEVIALAHAAAGISARDITYVEAHGTGTPLGDPIEVAA 333
Cdd:cd00828  237 VLERAELALARGAPIYGRVAGTASTTDGAGRSV--PAGGKGIARAIRTALAKAGLSLDDLDVISAHGTSTPANDVAESRA 314

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  334 LTRAFRAHTADTAfctLGAVKSNIGHLDAAAGVAGVIKTVQALRHRLIPPTLHFERPNPALhleqSPFFVNTQPLPWesP 413
Cdd:cd00828  315 IAEVAGALGAPLP---VTAQKALFGHSKGAAGALQLIGALQSLEHGLIPPTANLDDVDPDV----EHLSVVGLSRDL--N 385

                        410       420
                 ....*....|....*....|.
gi 53747904  414 RGPRLAGVSSFGIGGTNAHTL 434
Cdd:cd00828  386 LKVRAALVNAFGFGGSNAALV 406
zeta_crystallin cd08253
Zeta-crystallin with NADP-dependent quinone reductase activity (QOR); Zeta-crystallin is a eye ...
 1684-1973 7.97e-47

Zeta-crystallin with NADP-dependent quinone reductase activity (QOR); Zeta-crystallin is a eye lens protein with NADP-dependent quinone reductase activity (QOR). It has been cited as a structural component in mammalian eyes, but also has homology to quinone reductases in unrelated species. QOR catalyzes the conversion of a quinone and NAD(P)H to a hydroquinone and NAD(P+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR acts in the respiratory chains of bacteria and mitochondria, while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family, but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176215 [Multi-domain]  Cd Length: 325  Bit Score: 172.38  E-value: 7.97e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1684 ESLGLRRCTRPAPGPRQVEIEVEAAGLNFLDVLGALGMMPALEAEESVLGRECSGRIAAVGEGVSGLRVGDEV------L 1757
Cdd:cd08253   13 DVLRLGDLPVPTPGPGEVLVRVHASGVNPVDTYIRAGAYPGLPPLPYVPGSDGAGVVEAVGEGVDGLKVGDRVwltnlgW 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1758 AVAPGCFRSYVLVDESQVVRRPASLGLAEGAAQMVPFATAYFALHTVGRLRRGERILIHAAAGGLGLAAVQLASRTGAEI 1837
Cdd:cd08253   93 GRRQGTAAEYVVVPADQLVPLPDGVSFEQGAALGIPALTAYRALFHRAGAKAGETVLVHGGSGAVGHAAVQLARWAGARV 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1838 LATAGSEQKREYLRSLGIAHVLDSRSTSFVSEVRERTGGRGVDVVLNSLAGELLLAGLSVLAPHGRFLELGKRDLYADqq 1917
Cdd:cd08253  173 IATASSAEGAELVRQAGADAVFNYRAEDLADRILAATAGQGVDVIIEVLANVNLAKDLDVLAPGGRIVVYGSGGLRGT-- 250

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1918 VGLRTLARGQtfAAID----FGPHHPDFRAVLEEVATQLTQGQLEPLPTRLFPARQVAEA 1973
Cdd:cd08253  251 IPINPLMAKE--ASIRgvllYTATPEERAAAAEAIAAGLADGALRPVIAREYPLEEAAAA 308
MDR_like_2 cd05289
alcohol dehydrogenase and quinone reductase-like medium chain degydrogenases/reductases; ...
 1693-1988 2.26e-46

alcohol dehydrogenase and quinone reductase-like medium chain degydrogenases/reductases; Members identified as zinc-dependent alcohol dehydrogenases and quinone oxidoreductase. QOR catalyzes the conversion of a quinone + NAD(P)H to a hydroquinone + NAD(P)+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR actin the respiratory chains of bacteria and mitochondria, while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family, but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176191 [Multi-domain]  Cd Length: 309  Bit Score: 170.82  E-value: 2.26e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1693 RPAPGPRQVEIEVEAAGLNFLDVL---GALGMMPALEaEESVLGRECSGRIAAVGEGVSGLRVGDEVLAVAP----GCFR 1765
Cdd:cd05289   22 TPEPGPGEVLVKVHAAGVNPVDLKireGLLKAAFPLT-LPLIPGHDVAGVVVAVGPGVTGFKVGDEVFGMTPftrgGAYA 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1766 SYVLVDESQVVRRPASLGLAEGAAqmVPFA--TAYFALHTVGRLRRGERILIHAAAGGLGLAAVQLASRTGAEILATAgS 1843
Cdd:cd05289  101 EYVVVPADELALKPANLSFEEAAA--LPLAglTAWQALFELGGLKAGQTVLIHGAAGGVGSFAVQLAKARGARVIATA-S 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1844 EQKREYLRSLGIAHVLDSRSTSFVsevrERTGGRGVDVVLNSLAGELLLAGLSVLAPHGRFLELgkrdlyADQQVGLRTL 1923
Cdd:cd05289  178 AANADFLRSLGADEVIDYTKGDFE----RAAAPGGVDAVLDTVGGETLARSLALVKPGGRLVSI------AGPPPAEQAA 247

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 53747904 1924 ARGQtfAAIDFGPHHPDfRAVLEEVATQLTQGQLEPLPTRLFPARQVAEAFSFMARALHIGRVAV 1988
Cdd:cd05289  248 KRRG--VRAGFVFVEPD-GEQLAELAELVEAGKLRPVVDRVFPLEDAAEAHERLESGHARGKVVL 309
MDR3 cd08275
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 1675-1990 5.70e-46

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176236 [Multi-domain]  Cd Length: 337  Bit Score: 170.46  E-value: 5.70e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1675 VAVGTPGLLESLGLRRCTRPAPGPRQVEIEVEAAGLNFLDVLGALGMMPALEAEESVLGRECSGRIAAVGEGVSGLRVGD 1754
Cdd:cd08275    3 VVLTGFGGLDKLKVEKEALPEPSSGEVRVRVEACGLNFADLMARQGLYDSAPKPPFVPGFECAGTVEAVGEGVKDFKVGD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1755 EVLAVAP-GCFRSYVLVDESQVVRRPASLGLAEGAAQMVPFATAYFALHTVGRLRRGERILIHAAAGGLGLAAVQLASR- 1832
Cdd:cd08275   83 RVMGLTRfGGYAEVVNVPADQVFPLPDGMSFEEAAAFPVNYLTAYYALFELGNLRPGQSVLVHSAAGGVGLAAGQLCKTv 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1833 TGAEILATAgSEQKREYLRSLGIAHVLDSRSTSFVSEVRERTgGRGVDVVLNSLAGELLLAGLSVLAPHGRFLELGKRDL 1912
Cdd:cd08275  163 PNVTVVGTA-SASKHEALKENGVTHVIDYRTQDYVEEVKKIS-PEGVDIVLDALGGEDTRKSYDLLKPMGRLVVYGAANL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1913 YADQQVGLRTLARG--QTF--------------AAIDFG---PHHPDFRAVLEEVATQLTQGQLEPLPTRLFPARQVAEA 1973
Cdd:cd08275  241 VTGEKRSWFKLAKKwwNRPkvdpmklisenksvLGFNLGwlfEERELLTEVMDKLLKLYEEGKIKPKIDSVFPFEEVGEA 320

                        330
                 ....*....|....*..
gi 53747904 1974 FSFMARALHIGRVAVSM 1990
Cdd:cd08275  321 MRRLQSRKNIGKVVLTP 337
KR_2_FAS_SDR_x cd08955
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 2, complex (x); ...
 1008-1378 6.40e-46

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: 171.70  E-value: 6.40e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1008 ILHAWALTAEPgpCTPDGEAVLEQGFFSLLRLARALGRHAPERPVQLEVLSSFVHAVGP-REPLEPLKATLLGACAVLPL 1086
Cdd:cd08955   11 VVHLWSLDAPR--EEPADAASQELGCASALHLVQALSKAGLRRAPRLWLVTRGAQSVLAdGEPVSPAQAPLWGLGRVIAL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1087 EYPHVQCRTIDVRPgSEPREVLVRSLAAELAAPMGESPVAWRDGQRYVRRATRQRLEASRPLRSlrergvYLVAGGLGGI 1166
Cdd:cd08955   89 EHPELRCGLVDLDP-EATAAEEAEALLAELLAADAEDQVALRGGARYVARLVRAPARPLRPDAT------YLITGGLGGL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1167 GLVLAralaqrararlallthspfppreqweQWLEEAPA-HPEPAWRSEADPSERRRtqhrircLLELEQLGAEVQVYTA 1245
Cdd:cd08955  162 GLLVA--------------------------EWLVERGArHLVLTGRRAPSAAARQA-------IAALEEAGAEVVVLAA 208

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1246 DVAEEAAVRSVVEQVHARWGKIHGVLHAAATFDDGVIQLRTHEQSSRALRTKVRGSMVLHEVLASEGLDWFALCSSLASA 1325
Cdd:cd08955  209 DVSDRDALAAALAQIRASLPPLRGVIHAAGVLDDGVLANQDWERFRKVLAPKVQGAWNLHQLTQDLPLDFFVLFSSVASL 288

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 53747904 1326 LGSFGQADYCAANAFQDAYAHHLRRQGFTgALALDWGTWRDTGAAMRLVARTR 1378
Cdd:cd08955  289 LGSPGQANYAAANAFLDALAHYRRARGLP-ALSINWGPWAEVGMAASLARQAR 340
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 1212-1366 2.81e-45

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: 162.65  E-value: 2.81e-45
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904    1212 RSEADPSERRRTqhrircLLELEQLGAEVQVYTADVAEEAAVRSVVEQVHARWGKIHGVLHAAATFDDGVIQLRTHEQSS 1291
Cdd:smart00822   33 RSGPDAPGAAAL------LAELEAAGARVTVVACDVADRDALAAVLAAIPAVEGPLTGVIHAAGVLDDGVLASLTPERFA 106

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 53747904    1292 RALRTKVRGSMVLHEVLASEGLDWFALCSSLASALGSFGQADYCAANAFQDAYAHHLRRQGfTGALALDWGTWRD 1366
Cdd:smart00822  107 AVLAPKAAGAWNLHELTADLPLDFFVLFSSIAGVLGSPGQANYAAANAFLDALAEYRRARG-LPALSIAWGAWAE 180
ligase_PEP_1 TIGR03098
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ...
 2648-3132 8.08e-43

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: 166.50  E-value: 8.08e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   2648 ARLHPELPALLAPERTLSYGELARRAQALAARLRELEVQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLDP----EQ- 2722
Cdd:TIGR03098   10 AARLPDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPllkaEQv 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   2723 --------------PPLRLhQLLEEGPA-----RVVLTQSSLLHTVPWPPGVQVIAVDELEPATEAPPlPPRGTPEHLAY 2783
Cdd:TIGR03098   90 ahiladcnvrllvtSSERL-DLLHPALPgchdlRTLIIVGDPAHASEGHPGEEPASWPKLLALGDADP-PHPVIDSDMAA 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   2784 VIYTSGSTGKPKGVAIEHRAALNTVVDLNTRFGVGPEDRVLGLSALTFDLSVYDVLGLLGAGGALVLPAAEAEKDPAhww 2863
Cdd:TIGR03098  168 ILYTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPLSFDYGFNQLTTAFYVGATVVLHDYLLPRDVL--- 244

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   2864 ERLVAGRVTVWNSTPALMLLLVEyaeqrgLKLP----AALRLVMLSGDWIPVALPDRIRALGRDVQVVSLGGATEAsIWS 2939
Cdd:TIGR03098  245 KALEKHGITGLAAVPPLWAQLAQ------LDWPesaaPSLRYLTNSGGAMPRATLSRLRSFLPNARLFLMYGLTEA-FRS 317

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   2940 IAYPIGQVAPQWKSIPYGMPlaNQRFHVL--DGRlEARPwWVPGELYIGGEGLAREYWRDEPLTATRFIRHPRTGERLYR 3017
Cdd:TIGR03098  318 TYLPPEEVDRRPDSIGKAIP--NAEVLVLreDGS-ECAP-GEEGELVHRGALVAMGYWNDPEKTAERFRPLPPFPGELHL 393

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   3018 T------GDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPALSASVVVARGEPRGVRRLVAYAVPRSGQTP 3091
Cdd:TIGR03098  394 PelavwsGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAFGVPDPTLGQAIVLVVTPPGGEEL 473

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|.
gi 53747904   3092 AAGELRRYLAERLPAYMVPSAFVLLESLPRSRNGKIARDQL 3132
Cdd:TIGR03098  474 DRAALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKAL 514
QOR2 cd05286
Quinone oxidoreductase (QOR); Quinone oxidoreductase (QOR) and 2-haloacrylate reductase. QOR ...
 1675-1973 1.11e-42

Quinone oxidoreductase (QOR); Quinone oxidoreductase (QOR) and 2-haloacrylate reductase. QOR catalyzes the conversion of a quinone + NAD(P)H to a hydroquinone + NAD(P)+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR actin the respiratory chains of bacteria and mitochondria, while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family, but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. 2-haloacrylate reductase, a member of this subgroup, catalyzes the NADPH-dependent reduction of a carbon-carbon double bond in organohalogen compounds. Although similar to QOR, Burkholderia 2-haloacrylate reductase does not act on the quinones 1,4-benzoquinone and 1,4-naphthoquinone. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176189 [Multi-domain]  Cd Length: 320  Bit Score: 160.30  E-value: 1.11e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1675 VAVGTPGLLESLGLRRCTRPAPGPRQVEIEVEAAGLNFLDVLGALGMMPAleAEESVLGRECSGRIAAVGEGVSGLRVGD 1754
Cdd:cd05286    3 VRIHKTGGPEVLEYEDVPVPEPGPGEVLVRNTAIGVNFIDTYFRSGLYPL--PLPFVLGVEGAGVVEAVGPGVTGFKVGD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1755 EVL-AVAPGCFRSYVLVDESQVVRRPASLGLAEGAAQMVPFATAYFALHTVGRLRRGERILIHAAAGGLGLAAVQLASRT 1833
Cdd:cd05286   81 RVAyAGPPGAYAEYRVVPASRLVKLPDGISDETAAALLLQGLTAHYLLRETYPVKPGDTVLVHAAAGGVGLLLTQWAKAL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1834 GAEILATAGSEQKREYLRSLGIAHVLDSRSTSFVSEVRERTGGRGVDVVLNSLAGELLLAGLSVLAPHGRF--------- 1904
Cdd:cd05286  161 GATVIGTVSSEEKAELARAAGADHVINYRDEDFVERVREITGGRGVDVVYDGVGKDTFEGSLDSLRPRGTLvsfgnasgp 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 53747904 1905 ------LELGKRDLYadqqvglrtLARGQTFaaidfgpHHPDFRAVLEEVATQL----TQGQLEPLPTRLFPARQVAEA 1973
Cdd:cd05286  241 vppfdlLRLSKGSLF---------LTRPSLF-------HYIATREELLARAAELfdavASGKLKVEIGKRYPLADAAQA 303
Acyl_transf_1 pfam00698
Acyl transferase domain;
535-817 1.37e-42

Acyl transferase domain;


Pssm-ID: 395567  Cd Length: 319  Bit Score: 159.95  E-value: 1.37e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904    535 VMLFPGQGTPLVGTARALHESEPTFRQAVEQCARLLRQTLGLDVREVLfpsAEQEEQarrLAAQTRVAQPALFTLEYALA 614
Cdd:pfam00698    1 VFVFSGQGSQWAGMGMQLLKTSPAFAAVIDRADEAFKPQYGFSVSDVL---RNNPEG---TLDGTQFVQPALFAMQIALA 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904    615 QTWLGWGLQPQALAGHSLGELVAACLAGVFSLEDALQLVAARGQLM-QGCPPGAMLAVPLPEAELAALLGSELCIAAVNG 693
Cdd:pfam00698   75 ALLQSYGVRPDAVVGHSLGEYAAAVVAGALSPEEALLAAVLRSRLMmQLAGPGGMAAVELSAEEVEQRWPDDVVGAVVNS 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904    694 PRACVASGPLPAVEALTAALESRGVSSRRLETSHAFHSASMEACQGPLTTLLRRMRLQAPRLPCVSGLTGRWLTGEEATE 773
Cdd:pfam00698  155 PRSVVISGPQEAVRELVERVSKEGVGALVENVNYAVHSPQMDAIAPALLSALADIAPRTPRVPFISSTSIDPSDQRTLSA 234

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 53747904    774 pTYWARQLREPVRFSEAletLWSLKEP---VLLEVGPGTTLTALARR 817
Cdd:pfam00698  235 -EYWVRNLRSPVRFAEA---ILSAAEPgplVFIEISPHPLLLAALID 277
MDR6 cd08272
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 1675-1990 5.16e-42

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176233 [Multi-domain]  Cd Length: 326  Bit Score: 158.49  E-value: 5.16e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1675 VAVGTPGLLESLGLRRCTRPAPGPRQVEIEVEAAGLNFLDVLGALGMMPALEAEESVLGRECSGRIAAVGEGVSGLRVGD 1754
Cdd:cd08272    4 LVLESFGGPEVFELREVPRPQPGPGQVLVRVHASGVNPLDTKIRRGGAAARPPLPAILGCDVAGVVEAVGEGVTRFRVGD 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1755 EV------LAVAPGCFRSYVLVDESQVVRRPASLGLAEGAAQMVPFATAYFALHTVGRLRRGERILIHAAAGGLGLAAVQ 1828
Cdd:cd08272   84 EVygcaggLGGLQGSLAEYAVVDARLLALKPANLSMREAAALPLVGITAWEGLVDRAAVQAGQTVLIHGGAGGVGHVAVQ 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1829 LASRTGAEILATAGSEqKREYLRSLGiAHVLDSRSTSFVSEVRERTGGRGVDVVLNSLAGELLLAGLSVLAPHGRF---L 1905
Cdd:cd08272  164 LAKAAGARVYATASSE-KAAFARSLG-ADPIIYYRETVVEYVAEHTGGRGFDVVFDTVGGETLDASFEAVALYGRVvsiL 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1906 ELGKRDLyadqqVGLRtlARGQTF------AAIDFGPHHPDFRAVLEEVATQLTQGQLEP-LPTRLFPARQVAEAFSFMA 1978
Cdd:cd08272  242 GGATHDL-----APLS--FRNATYsgvftlLPLLTGEGRAHHGEILREAARLVERGQLRPlLDPRTFPLEEAAAAHARLE 314

                        330
                 ....*....|..
gi 53747904 1979 RALHIGRVAVSM 1990
Cdd:cd08272  315 SGSARGKIVIDV 326
FACL_like_6 cd05922
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 2687-3132 5.25e-42

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: 162.61  E-value: 5.25e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2687 PQELVAIAMHKGWEQATAVLGVLQAAAA----YLPLDPEQPPLRLHQLLEEGPARVVLTQSSL------LHTVPWPPGVq 2756
Cdd:cd05922   17 RGERVVLILPNRFTYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRIVLADAGAadrlrdALPASPDPGT- 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2757 VIAVDELEPA-TEAPPLPPrgTPEHLAYVIYTSGSTGKPKGVAIEHRAALNTVVDLNTRFGVGPEDRVLGLSALTFD--L 2833
Cdd:cd05922   96 VLDADGIRAArASAPAHEV--SHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDRALTVLPLSYDygL 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2834 SVYDVLGLLGAGGALvlpaAEAEKDPAHWWERLVAGRVTVWNSTPAL--MLLLVEYAEQrglKLPaALRLVMLSGDWIPV 2911
Cdd:cd05922  174 SVLNTHLLRGATLVL----TNDGVLDDAFWEDLREHGATGLAGVPSTyaMLTRLGFDPA---KLP-SLRYLTQAGGRLPQ 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2912 ALPDRIRALGRDVQVVSLGGATEASIWSIAYPIGQVAPQWKSIpyGMPLANQRFHVL--DGRLEarPWWVPGELYIGGEG 2989
Cdd:cd05922  246 ETIARLRELLPGAQVYVMYGQTEATRRMTYLPPERILEKPGSI--GLAIPGGEFEILddDGTPT--PPGEPGEIVHRGPN 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2990 LAREYWRDEPltatrFIRHPRTGERLYRTGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPALSASVVVA 3069
Cdd:cd05922  322 VMKGYWNDPP-----YRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVG 396

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 53747904 3070 RGEPRGvRRLVAYAVPRSGQTPAAgeLRRYLAERLPAYMVPSAFVLLESLPRSRNGKIARDQL 3132
Cdd:cd05922  397 LPDPLG-EKLALFVTAPDKIDPKD--VLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAAL 456
fabD TIGR00128
malonyl CoA-acyl carrier protein transacylase; This enzyme of fatty acid biosynthesis ...
 536-817 9.72e-42

malonyl CoA-acyl carrier protein transacylase; This enzyme of fatty acid biosynthesis transfers the malonyl moeity from coenzyme A to acyl-carrier protein. The seed alignment for this family of proteins contains a single member each from a number of bacterial species but also an additional pair of closely related, uncharacterized proteins from B. subtilis, one of which has a long C-terminal extension. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 272922 [Multi-domain]  Cd Length: 290  Bit Score: 156.86  E-value: 9.72e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904    536 MLFPGQGTPLVGTARALHESEPTFRQAVEQCArllrQTLGLDVREVLFpsaEQEEQARRLAAQTrvaQPALFTLEYALAQ 615
Cdd:TIGR00128    5 YVFPGQGSQTVGMGKDLYEQYPIAKELFDQAS----EALGYDLKKLCQ---EGPAEELNKTQYT---QPALYVVSAILYL 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904    616 TWL-GWGLQPQALAGHSLGELVAACLAGVFSLEDALQLVAARGQLMQGCPP---GAMLAV-PLPEAELAALLG----SEL 686
Cdd:TIGR00128   75 KLKeQGGLKPDFAAGHSLGEYSALVAAGALDFETALKLVKKRGELMQEAVPeggGAMAAViGLDEEQLAQACEeateNDV 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904    687 CIAAVNGPRACVASGPLPAVEALTAALESRGVssRR---LETSHAFHSASMEACQGPLTTLLRRMRLQAPRLPCVSGLTG 763
Cdd:TIGR00128  155 DLANFNSPGQVVISGTKDGVEAAAALFKEMGA--KRavpLEVSGAFHSRFMKPAAEKFAETLEACQFNDPTVPVISNVDA 232

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 53747904    764 RWLTGEEATEPTYwARQLREPVRFSEALETLWSLKEPVLLEVGPGTTLTALARR 817
Cdd:TIGR00128  233 KPYTNGDRIKEKL-SEQLTSPVRWTDSVEKLMARGVTEFAEVGPGKVLTGLIKR 285
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
 2615-3214 2.22e-41

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: 169.09  E-value: 2.22e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   2615 ELLPPAQRELLarynatqaPRPS---------GRLEEGFFTQARLHP------ELPALLAPE---RTLSYGELARRAQAL 2676
Cdd:TIGR03443  212 SLITPSQKSLL--------PDPTkdldwsgfrGAIHDIFADNAEKHPdrtcvvETPSFLDPSsktRSFTYKQINEASNIL 283

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   2677 AARLRELEVQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLDPEQPPLRlhQLLEEGPAR----VVLTQSSLLHtvpwp 2752
Cdd:TIGR03443  284 AHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPAR--QTIYLSVAKpralIVIEKAGTLD----- 356

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   2753 PGVQVIAVDELEPATEAPPL------------PPRGTPEHLA-YVIY-------------------TSGSTGKPKGVAIE 2800
Cdd:TIGR03443  357 QLVRDYIDKELELRTEIPALalqddgslvggsLEGGETDVLApYQALkdtptgvvvgpdsnptlsfTSGSEGIPKGVLGR 436

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   2801 HRAALNTVVDLNTRFGVGPEDRVLGLSALTFDLSVYDVLGLLGAGGALVLPAAEAEKDPAHWWERLVAGRVTVWNSTPAL 2880
Cdd:TIGR03443  437 HFSLAYYFPWMAKRFGLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTADDIGTPGRLAEWMAKYGATVTHLTPAM 516

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   2881 MLLLVEYAEQrglKLPAaLRLVMLSGDWIPVALPDRIRALGRDVQVVSLGGATEA-------SIWSIAYPIGQVAPQWKS 2953
Cdd:TIGR03443  517 GQLLSAQATT---PIPS-LHHAFFVGDILTKRDCLRLQTLAENVCIVNMYGTTETqravsyfEIPSRSSDSTFLKNLKDV 592

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   2954 IPYGMPLANQRFHVLDGRLEARPWWVP--GELYIGGEGLAREYwRDEP-LTATRFIRH---------------------- 3008
Cdd:TIGR03443  593 MPAGKGMKNVQLLVVNRNDRTQTCGVGevGEIYVRAGGLAEGY-LGLPeLNAEKFVNNwfvdpshwidldkennkperef 671

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   3009 ---PRtgERLYRTGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPALSASVVVARGEPRGVRRLVAYAVP 3085
Cdd:TIGR03443  672 wlgPR--DRLYRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVRRDKDEEPTLVSYIVP 749

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   3086 RSGQT----------------PAAGELRRY----------LAERLPAYMVPSAFVLLESLPRSRNGKIARDQLPEPQQTQ 3139
Cdd:TIGR03443  750 QDKSDeleefksevddeessdPVVKGLIKYrklikdireyLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKPALPFPDTAQ 829

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   3140 GLAAQAAAADPLVERLAALVKEALR---LE-------RVEPQDSLLDLGADSVALIRLINRLEAELQFRPRLADIYENPT 3209
Cdd:TIGR03443  830 LAAVAKNRSASAADEEFTETEREIRdlwLEllpnrpaTISPDDSFFDLGGHSILATRMIFELRKKLNVELPLGLIFKSPT 909


                   ....*
gi 53747904   3210 VQGLA 3214
Cdd:TIGR03443  910 IKGFA 914
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
 1220-1366 1.05e-40

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: 149.63  E-value: 1.05e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   1220 RRRTQHRIRcllELEQLGAEVQVYTADVAEEAAVRSVVEQVHARWGKIHGVLHAAATFDDGVIQLRTHEQSSRALRTKVR 1299
Cdd:pfam08659   38 RPDAQALIA---ELEARGVEVVVVACDVSDPDAVAALLAEIKAEGPPIRGVIHAAGVLRDALLENMTDEDWRRVLAPKVT 114

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 53747904   1300 GSMVLHEVLASEGLDWFALCSSLASALGSFGQADYCAANAFQDAYAHHLRRQGfTGALALDWGTWRD 1366
Cdd:pfam08659  115 GTWNLHEATPDEPLDFFVLFSSIAGLLGSPGQANYAAANAFLDALAEYRRSQG-LPATSINWGPWAE 180
PTZ00050 PTZ00050
3-oxoacyl-acyl carrier protein synthase; Provisional
 27-435 1.21e-39

3-oxoacyl-acyl carrier protein synthase; Provisional


Pssm-ID: 240245 [Multi-domain]  Cd Length: 421  Bit Score: 154.47  E-value: 1.21e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904    27 DVESFWRNLVAGVESISFFSEEELRQAGVSEQIRRRPEYVPAK----GVLEDLELFDAGFFGYSPREashlDPQQRLLLE 102
Cdd:PTZ00050    8 GAESTWEALIAGKSGIRKLTEFPKFLPDCIPEQKALENLVAAMpcqiAAEVDQSEFDPSDFAPTKRE----SRATHFAMA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   103 CSWEALEDAGLRP--DQLPGWVGVYVGAGDTSYRFQL-------LRGHgdplsgsKDVAGFFgnYPDFLATR----VAYK 169
Cdd:PTZ00050   84 AAREALADAKLDIlsEKDQERIGVNIGSGIGSLADLTdemktlyEKGH-------SRVSPYF--IPKILGNMaaglVAIK 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   170 LNLRGPALGIHTACSTSLVSINMACSALRGFECDMALAGGV-----------SLRLPARSGYLYEEGGVASkdghcRPFD 238
Cdd:PTZ00050  155 HKLKGPSGSAVTACATGAHCIGEAFRWIKYGEADIMICGGTeasitpvsfagFSRMRALCTKYNDDPQRAS-----RPFD 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   239 ARATGTVTGDGVGVVVLKRLEDALKARDPIHAVIRGWalnndGASRAGF--TAPSVEGQSEVIALAHA---AAGISARDI 313
Cdd:PTZ00050  230 KDRAGFVMGEGAGILVLEELEHALRRGAKIYAEIRGY-----GSSSDAHhiTAPHPDGRGARRCMENAlkdGANININDV 304

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   314 TYVEAHGTGTPLGDPIEVAALTRAFRAHTADTafCTLGAVKSNIGHLDAAAGVAGVIKTVQALRHRLIPPTLHFERPNPA 393
Cdd:PTZ00050  305 DYVNAHATSTPIGDKIELKAIKKVFGDSGAPK--LYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINLENPDAE 382

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 53747904   394 LHLEQSPffvNTQPLPwesPRGPRLAGVSSFGIGGTNAHTLF 435
Cdd:PTZ00050  383 CDLNLVQ---GKTAHP---LQSIDAVLSTSFGFGGVNTALLF 418
BCL_4HBCL cd05959
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ...
 2644-3132 1.47e-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: 1.47e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2644 FFTQARLHPELPALLAPERTLSYGELARRAQALAARLRELEVQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLDPEQP 2723
Cdd:cd05959   10 DLNLNEGRGDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLT 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2724 PLRLHQLLEEGPARVVLTQSSLLHTV------PWPPGVQVIAVD-----------ELEPATEAPPLPPRGT-PEHLAYVI 2785
Cdd:cd05959   90 PDDYAYYLEDSRARVVVVSGELAPVLaaaltkSEHTLVVLIVSGgagpeagalllAELVAAEAEQLKPAAThADDPAFWL 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2786 YTSGSTGKPKGVAIEHrAALNTVVDLNTR--FGVGPEDRVL---------GL-SALTFDLSVydvlgLLGAGGALVLPAa 2853
Cdd:cd05959  170 YSSGSTGRPKGVVHLH-ADIYWTAELYARnvLGIREDDVCFsaaklffayGLgNSLTFPLSV-----GATTVLMPERPT- 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2854 eaekdPAHWWERLVAGRVTVWNSTPALM--LLLVEYAEQRGLKlpaALRLVMLSGDWIPVALPDRIRALgRDVQVVSLGG 2931
Cdd:cd05959  243 -----PAAVFKRIRRYRPTVFFGVPTLYaaMLAAPNLPSRDLS---SLRLCVSAGEALPAEVGERWKAR-FGLDILDGIG 313

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2932 ATEA-SIWSIAYPiGQVAPQWKSIP---YGMPLANQRFH-VLDGrlearpwwVPGELYIGGEGLAREYWRDEPLTATRFI 3006
Cdd:cd05959  314 STEMlHIFLSNRP-GRVRYGTTGKPvpgYEVELRDEDGGdVADG--------EPGELYVRGPSSATMYWNNRDKTRDTFQ 384

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3007 rhprtGErLYRTGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPALSASVVVARGEPRGVRRLVAYAVPR 3086
Cdd:cd05959  385 -----GE-WTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLR 458

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*....
gi 53747904 3087 SGQTP---AAGELRRYLAERLPAYMVPSAFVLLESLPRSRNGKIARDQL 3132
Cdd:cd05959  459 PGYEDseaLEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKL 507
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 1700-1948 1.09e-38

Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; The medium chain reductase/dehydrogenases (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH) , quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines. Other MDR members have only a catalytic zinc, and some contain no coordinated zinc.


Pssm-ID: 176178 [Multi-domain]  Cd Length: 271  Bit Score: 147.08  E-value: 1.09e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1700 QVEIEVEAAGLNFLDVLGALGMMPALEAEESVLGRECSGRIAAVGEGVSGLRVGDEVLA--------------------- 1758
Cdd:cd05188    1 EVLVRVEAAGLCGTDLHIRRGGYPPPPKLPLILGHEGAGVVVEVGPGVTGVKVGDRVVVlpnlgcgtcelcrelcpgggi 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1759 ---VAPGCFRSYVLVDESQVVRRPASLGLAEGAAQMVPFATAYFALHTVGRLRRGERILIHaaagglglaaVQLASRTGA 1835
Cdd:cd05188   81 lgeGLDGGFAEYVVVPADNLVPLPDGLSLEEAALLPEPLATAYHALRRAGVLKPGDTVLVLgaggv-gllaAQLAKAAGA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1836 EILATAGSEQKREYLRSLGIAHVLDSRSTSFVSEVRErTGGRGVDVVLNSL-AGELLLAGLSVLAPHGRFLELGKRDLYA 1914
Cdd:cd05188  160 RVIVTDRSDEKLELAKELGADHVIDYKEEDLEEELRL-TGGGGADVVIDAVgGPETLAQALRLLRPGGRIVVVGGTSGGP 238

                        250       260       270
                 ....*....|....*....|....*....|....
gi 53747904 1915 DQQVGLRTLARGQTFAAIDFGPHHpDFRAVLEEV 1948
Cdd:cd05188  239 PLDDLRRLLFKELTIIGSTGGTRE-DFEEALDLL 271
Zn_ADH_like1 cd08266
Alcohol dehydrogenases of the MDR family; This group contains proteins related to the ...
 1693-1988 3.01e-38

Alcohol dehydrogenases of the MDR family; This group contains proteins related to the zinc-dependent alcohol dehydrogenases. However, while the group has structural zinc site characteristic of these enzymes, it lacks the consensus site for a catalytic zinc. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176227 [Multi-domain]  Cd Length: 342  Bit Score: 148.17  E-value: 3.01e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1693 RPAPGPRQVEIEVEAAGLNFLDVLGALGMMPALEAEESVLGRECSGRIAAVGEGVSGLRVGDEVlAVAPG---------- 1762
Cdd:cd08266   22 EPEPGPDEVLVRVKAAALNHLDLWVRRGMPGIKLPLPHILGSDGAGVVEAVGPGVTNVKPGQRV-VIYPGiscgrceycl 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1763 ------CFRS-------------YVLVDESQVVRRPASLGLAEGAAQMVPFATAYFALHTVGRLRRGERILIHAAAGGLG 1823
Cdd:cd08266  101 agrenlCAQYgilgehvdggyaeYVAVPARNLLPIPDNLSFEEAAAAPLTFLTAWHMLVTRARLRPGETVLVHGAGSGVG 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1824 LAAVQLASRTGAEILATAGSEQKREYLRSLGIAHVLDSRSTSFVSEVRERTGGRGVDVVLNSLAGELLLAGLSVLAPHGR 1903
Cdd:cd08266  181 SAAIQIAKLFGATVIATAGSEDKLERAKELGADYVIDYRKEDFVREVRELTGKRGVDVVVEHVGAATWEKSLKSLARGGR 260

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1904 FLELGKRDLYaDQQVGLRTLARGQTFAAIDFGPHHPDFRAVLEEVAtqltQGQLEPLPTRLFPARQVAEAFSFMARALHI 1983
Cdd:cd08266  261 LVTCGATTGY-EAPIDLRHVFWRQLSILGSTMGTKAELDEALRLVF----RGKLKPVIDSVFPLEEAAEAHRRLESREQF 335


                 ....*
gi 53747904 1984 GRVAV 1988
Cdd:cd08266  336 GKIVL 340
A_NRPS_acs4 cd17654
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ...
 2689-3132 1.11e-37

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: 149.54  E-value: 1.11e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2689 ELVAIAMHKGWEQATAVLGVLQAAAAYLPLDPEQPPLR-LHQLLEEGPARVVltQSSLLHTVPwppgvqviavDELEPAT 2767
Cdd:cd17654   42 RAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRsLTVMKKCHVSYLL--QNKELDNAP----------LSFTPEH 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2768 EAPPLPprgTPEHLAYVIYTSGSTGKPKGVAIEHRAALNTVVDLNTRFGVGPEDRVLGLSALTFDLSVYDVLGLLGAGGA 2847
Cdd:cd17654  110 RHFNIR---TDECLAYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFNITSEDILFLTSPLTFDPSVVEIFLSLSSGAT 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2848 LVLPAAEAEKDPAHWWERLVAG-RVTVWNSTPALM-LLLVEYAEQRGLKLPAALRLVMLSGDWIPVALPDRIRA-LGRDV 2924
Cdd:cd17654  187 LLIVPTSVKVLPSKLADILFKRhRITVLQATPTLFrRFGSQSIKSTVLSATSSLRVLALGGEPFPSLVILSSWRgKGNRT 266

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2925 QVVSLGGATEASIWSIAYpigQVAPQWKSIPYGMPLANQRFHVLDGRLEArpwwVPGELYIGgeGLAREYWRDEPLTatr 3004
Cdd:cd17654  267 RIFNIYGITEVSCWALAY---KVPEEDSPVQLGSPLLGTVIEVRDQNGSE----GTGQVFLG--GLNRVCILDDEVT--- 334

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3005 firhpRTGERLYRTGDQGRmLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPALSASVVVARGEprgvRRLVAYAV 3084
Cdd:cd17654  335 -----VPKGTMRATGDFVT-VKDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAVTLSDQ----QRLIAFIV 404

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*...
gi 53747904 3085 PRSGQTPAAGELRRYLaerLPAYMVPSAFVLLESLPRSRNGKIARDQL 3132
Cdd:cd17654  405 GESSSSRIHKELQLTL---LSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
fabF TIGR03150
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 ...
 27-435 1.26e-37

beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 (KAS-II, FabF) is involved in the condensation step of fatty acid biosynthesis in which the malonyl donor group is decarboxylated and the resulting carbanion used to attack and extend the acyl group attached to the acyl carrier protein. Most genomes encoding fatty acid biosynthesis contain a number of condensing enzymes, often of all three types: 1, 2 and 3. Synthase 2 is mechanistically related to synthase 1 (KAS-I, FabB) containing a number of absolutely conserved catalytic residues in common. This model is based primarily on genes which are found in apparent operons with other essential genes of fatty acid biosynthesis (GenProp0681). The large gap between the trusted cutoff and the noise cutoff contains many genes which are not found adjacent to genes of the fatty acid pathway in genomes that often also contain a better hit to this model. These genes may be involved in other processes such as polyketide biosyntheses. Some genomes contain more than one above-trusted hit to this model which may result from recent paralogous expansions. Second hits to this model which are not next to other fatty acid biosynthesis genes may be involved in other processes. FabB sequences should fall well below the noise cutoff of this model. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 274452 [Multi-domain]  Cd Length: 407  Bit Score: 148.40  E-value: 1.26e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904     27 DVESFWRNLVA---GVESISFFSEEELrqagvseqirrrpeyvPAK--GVLEDlelFDAGFFgYSPREASHLDPQQRLLL 101
Cdd:TIGR03150   17 GVEEFWENLLAgksGIGPITRFDASDL----------------PVKiaGEVKD---FDPEDY-IDKKEARRMDRFIQYAL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904    102 ECSWEALEDAGLRPDQLPGW-VGVYVGAG--------DTSYRFQLlrghgdplSGSKDVAGFF--GNYPDFLATRVAYKL 170
Cdd:TIGR03150   77 AAAKEAVEDSGLDIEEEDAErVGVIIGSGiggletieEQHIVLLE--------KGPRRVSPFFipMSIINMAAGQISIRY 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904    171 NLRGPALGIHTACSTSLVSINMACSALRGFECDMALAGGV-------------SLR-LPARSgylyEEGGVASkdghcRP 236
Cdd:TIGR03150  149 GAKGPNHAVVTACATGTHAIGDAFRLIQRGDADVMIAGGAeaaitplgiagfaAMKaLSTRN----DDPEKAS-----RP 219

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904    237 FDARATGTVTGDGVGVVVLKRLEDALK--ARdpIHAVIRGWALNNDgasrAG-FTAPSVEG--QSEVIALAHAAAGISAR 311
Cdd:TIGR03150  220 FDKDRDGFVMGEGAGVLVLEELEHAKArgAK--IYAEIVGYGMSGD----AYhITAPAPEGegAARAMRAALKDAGINPE 293

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904    312 DITYVEAHGTGTPLGDPIEVAALTRAFRAHTADTAfctLGAVKSNIGHLDAAAGVAGVIKTVQALRHRLIPPTLHFERPN 391
Cdd:TIGR03150  294 DVDYINAHGTSTPLGDKAETKAIKKVFGDHAYKLA---VSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVPPTINLDNPD 370

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*
gi 53747904    392 PALHLEqspfFVntqplPWES-PRGPRLAGVSSFGIGGTNAHTLF 435
Cdd:TIGR03150  371 PECDLD----YV-----PNEArEAKIDYALSNSFGFGGTNASLVF 406
FC-FACS_FadD_like cd05936
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ...
 2647-3132 2.70e-37

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: 148.87  E-value: 2.70e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2647 QARLHPELPALLAPERTLSYGELARRAQALAARLRELEVQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLDPEQPPLR 2726
Cdd:cd05936    8 AARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPRE 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2727 LHQLLEEGPARVVLTQSSLLHtvpwppgvqVIAvdelepATEAPPLPPRGTPEHLAYVIYTSGSTGKPKGVAIEHRAALN 2806
Cdd:cd05936   88 LEHILNDSGAKALIVAVSFTD---------LLA------AGAPLGERVALTPEDVAVLQYTSGTTGVPKGAMLTHRNLVA 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2807 TVVDLNTRFGVG--PEDRVLGlsAL----TFDLSVydvlgllgagGALVLPAAEAEK------DPAHWWERLVAGRVTVW 2874
Cdd:cd05936  153 NALQIKAWLEDLleGDDVVLA--ALplfhVFGLTV----------ALLLPLALGATIvliprfRPIGVLKEIRKHRVTIF 220

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2875 NSTPALMLLLVEYAEQRGLkLPAALRLVMLSGDWIPVALPDRIRALGRdVQVVSLGGATEASiwsiayPIGQVAPQWK-- 2952
Cdd:cd05936  221 PGVPTMYIALLNAPEFKKR-DFSSLRLCISGGAPLPVEVAERFEELTG-VPIVEGYGLTETS------PVVAVNPLDGpr 292

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2953 ---SIpyGMPLANQRFHVLDGRLEARPWWVPGELYIGGEGLAREYWRDEPLTATRFirhprTGERLyRTGDQGRMLPEGS 3029
Cdd:cd05936  293 kpgSI--GIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAF-----VDGWL-RTGDIGYMDEDGY 364

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3030 IEFLGR-EDLqVKVQGFRVELGEIEAALAQHPALSASVVVarGEPRGVR--RLVAYAVPRSGQTPAAGELRRYLAERLPA 3106
Cdd:cd05936  365 FFIVDRkKDM-IIVGGFNVYPREVEEVLYEHPAVAEAAVV--GVPDPYSgeAVKAFVVLKEGASLTEEEIIAFCREQLAG 441

                        490       500
                 ....*....|....*....|....*.
gi 53747904 3107 YMVPSAFVLLESLPRSRNGKIARDQL 3132
Cdd:cd05936  442 YKVPRQVEFRDELPKSAVGKILRREL 467
cond_enzymes cd00327
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ...
 96-432 7.23e-37

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: 141.43  E-value: 7.23e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   96 QQRLLLECSWEALEDAGLRPDQLpgwVGVYVGAGDTSYRFQllrghgdplsgskdvagffgnypdFLATRVAYKLNLR-G 174
Cdd:cd00327    7 ASELGFEAAEQAIADAGLSKGPI---VGVIVGTTGGSGEFS------------------------GAAGQLAYHLGISgG 59

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  175 PALGIHTACSTSLVSINMACSALRGFECDMALAGGVSLRLPArsgylyeEGGVAskdghcrpfdaratgtvtgdgvgvVV 254
Cdd:cd00327   60 PAYSVNQACATGLTALALAVQQVQNGKADIVLAGGSEEFVFG-------DGAAA------------------------AV 108

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  255 LKRLEDALKARDPIHAVIRGWALNNDGASRAgfTAPSVEGQSEVIALAHAAAGISARDITYVEAHGTGTPLGDPIEVAAL 334
Cdd:cd00327  109 VESEEHALRRGAHPQAEIVSTAATFDGASMV--PAVSGEGLARAARKALEGAGLTPSDIDYVEAHGTGTPIGDAVELALG 186

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  335 TRAFRAHTAdtafcTLGAVKSNIGHLDAAAGVAGVIKTVQALRHRLIPPTlhferpnpalhleqspffvntqplpwesPR 414
Cdd:cd00327  187 LDPDGVRSP-----AVSATLIMTGHPLGAAGLAILDELLLMLEHEFIPPT----------------------------PR 233

                        330
                 ....*....|....*...
gi 53747904  415 GPRLAGVSSFGIGGTNAH 432
Cdd:cd00327  234 EPRTVLLLGFGLGGTNAA 251
A_NRPS_alphaAR cd17647
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ...
 2659-3135 7.96e-37

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: 148.43  E-value: 7.96e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2659 APERTLSYGELARRAQALAARLRELEVQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLDPEQPPLRlhQLLEEGPARv 2738
Cdd:cd17647   16 SKTRSFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPAR--QNIYLGVAK- 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2739 vltqssllhtvpwPPGVQVIAVDELepateapPLPPRGTPEhlayVIYTSGSTGKPKGVAIEHRAALNTVVDLNTRFGVG 2818
Cdd:cd17647   93 -------------PRGLIVIRAAGV-------VVGPDSNPT----LSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFNLS 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2819 PEDRVLGLSALTFDLSVYDVLGLLGAGGALVLPAAEAEKDPAHWWERLVAGRVTVWNSTPALMLLLVEYAEQRGLKLPAA 2898
Cdd:cd17647  149 ENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTQDDIGTPGRLAEWMAKYGATVTHLTPAMGQLLTAQATTPFPKLHHA 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2899 LrlvmLSGDWIPVALPDRIRALGRDVQVVSLGGATEASiWSIAY---PIGQVAPQW----KS-IPYGMPLANQRFHVLDG 2970
Cdd:cd17647  229 F----FVGDILTKRDCLRLQTLAENVRIVNMYGTTETQ-RAVSYfevPSRSSDPTFlknlKDvMPAGRGMLNVQLLVVNR 303

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2971 RLEARPWWVP--GELYIGGEGLAREYWRDEPLTATRFIRH-------------------------PRtgERLYRTGDQGR 3023
Cdd:cd17647  304 NDRTQICGIGevGEIYVRAGGLAEGYRGLPELNKEKFVNNwfvepdhwnyldkdnnepwrqfwlgPR--DRLYRTGDLGR 381

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3024 MLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPALSASVVVARGEPRGVRRLVAYAVPR----------------- 3086
Cdd:cd17647  382 YLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRRDKDEEPTLVSYIVPRfdkpddesfaqedvpke 461

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 53747904 3087 SGQTPAAGELRRY----------LAERLPAYMVPSAFVLLESLPRSRNGKIARDQLPEP 3135
Cdd:cd17647  462 VSTDPIVKGLIGYrklikdirefLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKLQFP 520
KR_FAS_SDR_x cd05274
ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of ...
 1021-1381 2.59e-36

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: 143.68  E-value: 2.59e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1021 CTPDGEAVLEQGFFSLLRLARALGRHAPERPVQLEVLSSFVHAVGPREPLEPLKATLLGACAVLPLEYPHVQCRTIDVRP 1100
Cdd:cd05274   18 APACGAADAVLALAALLALVAALLAAYASTGPPLWLVTRGAEAVSADDVAALAQAALWGLLRVLALEHPELWGGLVDLDA 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1101 GSEPREVlvRSLAAELAAPMGESPVAWRDGQRYVRRATRQRLEASR-PLRSLRERGVYLVAGGLGGIGLVLAralaqrar 1179
Cdd:cd05274   98 ADAADEA--AALAALLAGAPGEDELALRGGQRLVPRLVRAPAAALElAAAPGGLDGTYLITGGLGGLGLLVA-------- 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1180 arlallthspfppreqweQWLEEAPAhpepawRSEADPSERRRTQHRIRCLLELEQLGAEVQVYTADVAEEAAVRSVVEQ 1259
Cdd:cd05274  168 ------------------RWLAARGA------RHLVLLSRRGPAPRAAARAALLRAGGARVSVVRCDVTDPAALAALLAE 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1260 vHARWGKIHGVLHAAATFDDGVIQLRTHEQSSRALRTKVRGSMVLHEVLASEGLDWFALCSSLASALGSFGQADYCAANA 1339
Cdd:cd05274  224 -LAAGGPLAGVIHAAGVLRDALLAELTPAAFAAVLAAKVAGALNLHELTPDLPLDFFVLFSSVAALLGGAGQAAYAAANA 302

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 53747904 1340 FQDAYAHHLRRQGFTgALALDWGTWRDTGAAMR--LVARTRRGG 1381
Cdd:cd05274  303 FLDALAAQRRRRGLP-ATSVQWGAWAGGGMAAAaaLRARLARSG 345
MDR1 cd08267
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 1693-1974 4.06e-36

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176228 [Multi-domain]  Cd Length: 319  Bit Score: 141.20  E-value: 4.06e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1693 RPAPGPRQVEIEVEAAGLNFLDVLGALGMMPALEAEES--VLGRECSGRIAAVGEGVSGLRVGDEVLAVAP----GCFRS 1766
Cdd:cd08267   21 IPTPKPGEVLVKVHAASVNPVDWKLRRGPPKLLLGRPFppIPGMDFAGEVVAVGSGVTRFKVGDEVFGRLPpkggGALAE 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1767 YVLVDESQVVRRPASLGLAEGAAqmVPFA--TAYFALHTVGRLRRGERILI--------HAaagglglaAVQLASRTGAE 1836
Cdd:cd08267  101 YVVAPESGLAKKPEGVSFEEAAA--LPVAglTALQALRDAGKVKPGQRVLIngasggvgTF--------AVQIAKALGAH 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1837 ILATAgSEQKREYLRSLGIAHVLDSRSTSFVSevrERTGGRGVDVVLN--SLAGELLLAGLSVLAPHGRFLELG---KRD 1911
Cdd:cd08267  171 VTGVC-STRNAELVRSLGADEVIDYTTEDFVA---LTAGGEKYDVIFDavGNSPFSLYRASLALKPGGRYVSVGggpSGL 246

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 53747904 1912 LYADQQVGLRTLARGQTFAAIDFGPHHPDfravLEEVATQLTQGQLEPLPTRLFPARQVAEAF 1974
Cdd:cd08267  247 LLVLLLLPLTLGGGGRRLKFFLAKPNAED----LEQLAELVEEGKLKPVIDSVYPLEDAPEAY 305
MDR7 cd08276
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 1683-1990 4.37e-36

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176237 [Multi-domain]  Cd Length: 336  Bit Score: 141.90  E-value: 4.37e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1683 LESLGLRRCTRPAPGPRQVEIEVEAAGLNFLDVLGALGMMPALEAEESVLGRECSGRIAAVGEGVSGLRVGDEVLA---- 1758
Cdd:cd08276   12 LDNLKLVEEPVPEPGPGEVLVRVHAVSLNYRDLLILNGRYPPPVKDPLIPLSDGAGEVVAVGEGVTRFKVGDRVVPtffp 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1759 ------------------VAPGCFRSYVLVDESQVVRRPASLGLAEGAAqmVPFA--TAYFALHTVGRLRRGERILIHaa 1818
Cdd:cd08276   92 nwldgpptaedeasalggPIDGVLAEYVVLPEEGLVRAPDHLSFEEAAT--LPCAglTAWNALFGLGPLKPGDTVLVQgt 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1819 agglglaAVQLASRTGAEILATAGSEQKREYLRSLGIAHVLDSRSTS-FVSEVRERTGGRGVDVVLNSLAGELLLAGLSV 1897
Cdd:cd08276  170 gg-vslfALQFAKAAGARVIATSSSDEKLERAKALGADHVINYRTTPdWGEEVLKLTGGRGVDHVVEVGGPGTLAQSIKA 248

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1898 LAPHGR-----FLElgkrdlYADQQVGL-RTLARGQTFAAIDFGPhhpdfRAVLEEVATQLTQGQLEPLPTRLFPARQVA 1971
Cdd:cd08276  249 VAPGGVisligFLS------GFEAPVLLlPLLTKGATLRGIAVGS-----RAQFEAMNRAIEAHRIRPVIDRVFPFEEAK 317

                        330
                 ....*....|....*....
gi 53747904 1972 EAFSFMARALHIGRVAVSM 1990
Cdd:cd08276  318 EAYRYLESGSHFGKVVIRV 336
BCL_like cd05919
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ...
 2655-3132 4.77e-36

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: 144.53  E-value: 4.77e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2655 PALLAPERTLSYGELARRAQALAARLRELEVQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLDPEQPPLRLHQLLEEG 2734
Cdd:cd05919    2 TAFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDC 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2735 PARVVLTQSsllhtvpwppgvqviavdelepateapplpprgtpEHLAYVIYTSGSTGKPKGVAIEHRAALNTVVDLNTR 2814
Cdd:cd05919   82 EARLVVTSA-----------------------------------DDIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMARE 126

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2815 -FGVGPEDRVLGLSALTFDLSVYDVLGLLGAGGALVLPAAEAeKDPAHWWERLVAGRVTVWNSTPALM--LLLVEYAEQR 2891
Cdd:cd05919  127 aLGLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGASAVLNPGW-PTAERVLATLARFRPTVLYGVPTFYanLLDSCAGSPD 205

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2892 GLKlpaALRLVMLSGDWIPVALPDRIRALGrDVQVVSLGGATEASIWSIAYPIGQvapqWKSIPYGMPLANQRFHVLDGR 2971
Cdd:cd05919  206 ALR---SLRLCVSAGEALPRGLGERWMEHF-GGPILDGIGATEVGHIFLSNRPGA----WRLGSTGRPVPGYEIRLVDEE 277

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2972 LEARPWWVPGELYIGGEGLAREYWRDEPLTATRFIrhprtgERLYRTGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGE 3051
Cdd:cd05919  278 GHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFN------GGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVE 351

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3052 IEAALAQHPALSASVVVARGEPRGVRRLVAYAVPRSGQTPA---AGELRRYLAERLPAYMVPSAFVLLESLPRSRNGKIA 3128
Cdd:cd05919  352 VESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQeslARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQ 431


                 ....
gi 53747904 3129 RDQL 3132
Cdd:cd05919  432 RFKL 435
FACL_FadD13-like cd17631
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ...
 2648-3129 6.84e-36

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: 143.90  E-value: 6.84e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2648 ARLHPELPALLAPERTLSYGELARRAQALAARLRELEVQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLDPEQPPLRL 2727
Cdd:cd17631    5 ARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2728 HQLLEEGPARVVLtqssllhtvpwppgvqviavdelepateapplpprgtpEHLAYVIYTSGSTGKPKGVAIEHRAALNT 2807
Cdd:cd17631   85 AYILADSGAKVLF--------------------------------------DDLALLMYTSGTTGRPKGAMLTHRNLLWN 126

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2808 VVDLNTRFGVGPEDRVLGLSAL--TFDLSVYDVLGLLGAGGALVLPAAeaekDPAHWWERLVAGRVTVWNSTPALMLLLV 2885
Cdd:cd17631  127 AVNALAALDLGPDDVLLVVAPLfhIGGLGVFTLPTLLRGGTVVILRKF----DPETVLDLIERHRVTSFFLVPTMIQALL 202

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2886 EYAEQRGLKLPAaLRLVMLSGDWIPVALPDRIRAlgRDVQVVSLGGATEAS-IWSIAYPIGQVApqwKSIPYGMPLANQR 2964
Cdd:cd17631  203 QHPRFATTDLSS-LRAVIYGGAPMPERLLRALQA--RGVKFVQGYGMTETSpGVTFLSPEDHRR---KLGSAGRPVFFVE 276

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2965 FHVLDGRLEARPWWVPGELYIGGEGLAREYWRDEPLTATRFirhpRTGerLYRTGDQGRMLPEGSIEFLGREDLQVKVQG 3044
Cdd:cd17631  277 VRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAF----RDG--WFHTGDLGRLDEDGYLYIVDRKKDMIISGG 350

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3045 FRVELGEIEAALAQHPALSASVVVARGEPRGVRRLVAYAVPRSGQTPAAGELRRYLAERLPAYMVPSAFVLLESLPRSRN 3124
Cdd:cd17631  351 ENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGAELDEDELIAHCRERLARYKIPKSVEFVDALPRNAT 430


                 ....*
gi 53747904 3125 GKIAR 3129
Cdd:cd17631  431 GKILK 435
PRK07314 PRK07314
beta-ketoacyl-ACP synthase II;
23-435 1.07e-35

beta-ketoacyl-ACP synthase II;


Pssm-ID: 235987 [Multi-domain]  Cd Length: 411  Bit Score: 142.62  E-value: 1.07e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904    23 PGAPDVESFWRNLVAGVESISFFSEEElrqagvseqirrrPEYVPAK--GVLEDlelFDAGFFgYSPREASHLDPQQRLL 100
Cdd:PRK07314   14 PLGNDVESTWKNLLAGKSGIGPITHFD-------------TSDLAVKiaGEVKD---FNPDDY-MSRKEARRMDRFIQYG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   101 LECSWEALEDAGLRPDQL-PGWVGVYVGAG--------DTSYRfqLLRGhgdplsGSKDVAGFF--GNYPDFLATRVAYK 169
Cdd:PRK07314   77 IAAAKQAVEDAGLEITEEnADRIGVIIGSGiggletieEQHIT--LLEK------GPRRVSPFFvpMAIINMAAGHVSIR 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   170 LNLRGPALGIHTACSTSLVSINMACSALRGFECDMALAGGV-------------SLRL-------PARSgylyeeggvas 229
Cdd:PRK07314  149 YGAKGPNHSIVTACATGAHAIGDAARLIAYGDADVMVAGGAeaaitplgiagfaAARAlstrnddPERA----------- 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   230 kdghCRPFDARATGTVTGDGVGVVVLKRLEDALK--ARdpIHAVIRGWALNNDGASragFTAPSVEGQSEV--IALAHAA 305
Cdd:PRK07314  218 ----SRPFDKDRDGFVMGEGAGILVLEELEHAKArgAK--IYAEVVGYGMTGDAYH---MTAPAPDGEGAAraMKLALKD 288

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   306 AGISARDITYVEAHGTGTPLGDPIEVAALTRAFRAHTADTAfctLGAVKSNIGHLDAAAGVAGVIKTVQALRHRLIPPTL 385
Cdd:PRK07314  289 AGINPEDIDYINAHGTSTPAGDKAETQAIKRVFGEHAYKVA---VSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTI 365

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 53747904   386 HFERPNPALHLEqspfFVntqplPWES-PRGPRLAGVSSFGIGGTNAHTLF 435
Cdd:PRK07314  366 NLDNPDEECDLD----YV-----PNEArERKIDYALSNSFGFGGTNASLVF 407
PRK07656 PRK07656
long-chain-fatty-acid--CoA ligase; Validated
 2648-3134 1.04e-34

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


Pssm-ID: 236072 [Multi-domain]  Cd Length: 513  Bit Score: 141.97  E-value: 1.04e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2648 ARLHPELPALLAPERTLSYGELARRAQALAARLRELEVQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLDPEQPPLRL 2727
Cdd:PRK07656   15 ARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEA 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2728 HQLLEEGPARVVLTQSSLLHT----VPWPPGVQVIAVDELEPATEAPPL----------------PPRGTPEHLAYVIYT 2787
Cdd:PRK07656   95 AYILARGDAKALFVLGLFLGVdysaTTRLPALEHVVICETEEDDPHTEKmktftdflaagdpaerAPEVDPDDVADILFT 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2788 SGSTGKPKGVAIEHRAALNTVVDLNTRFGVGPEDRVL---------GLSA---------------LTFdlsvydvlgllg 2843
Cdd:PRK07656  175 SGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLaanpffhvfGYKAgvnaplmrgatilplPVF------------ 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2844 aggalvlpaaeaekDPAHWWERLVAGRVTVWNSTPALMLLLVEYAEQRGLKLpAALRLVMLSGDWIPVALPDRIRALgRD 2923
Cdd:PRK07656  243 --------------DPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAEDL-SSLRLAVTGAASMPVALLERFESE-LG 306

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2924 VQVVSLG-GATEASIWSIAYPIGQVApqwKSIPY--GMPLANQRFHVLDGRLEARPWWVPGELYIGGEGLAREYWRDEPL 3000
Cdd:PRK07656  307 VDIVLTGyGLSEASGVTTFNRLDDDR---KTVAGtiGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEA 383

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  3001 TAtrfirHPRTGERLYRTGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPALSASVVVARGEPRGVRRLV 3080
Cdd:PRK07656  384 TA-----AAIDADGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGK 458

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....
gi 53747904  3081 AYAVPRSGQTPAAGELRRYLAERLPAYMVPSAFVLLESLPRSRNGKIARDQLPE 3134
Cdd:PRK07656  459 AYVVLKPGAELTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRALRE 512
CBAL cd05923
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ...
 2652-3132 1.60e-34

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: 141.11  E-value: 1.60e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2652 PELPALLAPERT--LSYGELARRAQALAARLRELEVQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLDPEQPPLRLHQ 2729
Cdd:cd05923   15 PDACAIADPARGlrLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAE 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2730 LLEEGPARVVltqsslLHTVPWPP-------GVQVIAVD------ELEPATEAPPLPPRGtPEHLAYVIYTSGSTGKPKG 2796
Cdd:cd05923   95 LIERGEMTAA------VIAVDAQVmdaifqsGVRVLALSdlvglgEPESAGPLIEDPPRE-PEQPAFVFYTSGTTGLPKG 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2797 VAIEHRAALNTVVDLNTRFGV--GPEDRVLGLSALTFDLSVYDVLGLLGAGGALVLPAAEAekDPAHWWERLVAGRVTVW 2874
Cdd:cd05923  168 AVIPQRAAESRVLFMSTQAGLrhGRHNVVLGLMPLYHVIGFFAVLVAALALDGTYVVVEEF--DPADALKLIEQERVTSL 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2875 NSTPALMLLLVEYAEQRGLKLpAALRLVMLSGDWIPVALPDRIRALgRDVQVVSLGGATEASIWSIaypigqvAPQWKSI 2954
Cdd:cd05923  246 FATPTHLDALAAAAEFAGLKL-SSLRHVTFAGATMPDAVLERVNQH-LPGEKVNIYGTTEAMNSLY-------MRDARTG 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2955 PYGMPLANQRFH---VLDGRLEARPWWVPGELYIGGEGLA--REYWRDEPLTATRFIrhprtgERLYRTGDQGRMLPEGS 3029
Cdd:cd05923  317 TEMRPGFFSEVRivrIGGSPDEALANGEEGELIVAAAADAafTGYLNQPEATAKKLQ------DGWYRTGDVGYVDPSGD 390

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3030 IEFLGREDLQVKVQGFRVELGEIEAALAQHPALSASVVVARGEPRGVRRLVAYAVPRSGqTPAAGELRRY-LAERLPAYM 3108
Cdd:cd05923  391 VRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREG-TLSADELDQFcRASELADFK 469

                        490       500
                 ....*....|....*....|....
gi 53747904 3109 VPSAFVLLESLPRSRNGKIARDQL 3132
Cdd:cd05923  470 RPRRYFFLDELPKNAMNKVLRRQL 493
MDR5 cd08271
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 1679-1973 3.07e-34

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176232 [Multi-domain]  Cd Length: 325  Bit Score: 135.87  E-value: 3.07e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1679 TPGLLESLGLRRCTRPAPGPRQVEIEVEAAGLNFLDVLGALGMMPALEAEEsVLGRECSGRIAAVGEGVSGLRVGDEVLA 1758
Cdd:cd08271    8 KPGAALQLTLEEIEIPGPGAGEVLVKVHAAGLNPVDWKVIAWGPPAWSYPH-VPGVDGAGVVVAVGAKVTGWKVGDRVAY 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1759 VA----PGCFRSYVLVDESQVVRRPASLGLAEGAAQMVPFATAYFALHTVGRLRRGERILIHAAAGGLGLAAVQLASRTG 1834
Cdd:cd08271   87 HAslarGGSFAEYTVVDARAVLPLPDSLSFEEAAALPCAGLTAYQALFKKLRIEAGRTILITGGAGGVGSFAVQLAKRAG 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1835 AEILATAgSEQKREYLRSLGIAHVLDSRSTSFVSEVRERTGGRGVDVVLNSLAGELLLAGLSVLAPHGRFLELGKRDLYA 1914
Cdd:cd08271  167 LRVITTC-SKRNFEYVKSLGADHVIDYNDEDVCERIKEITGGRGVDAVLDTVGGETAAALAPTLAFNGHLVCIQGRPDAS 245

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 53747904 1915 DQQVGLRTLARGQTF--AAIDFG--PHHPDFRAVLEEVATQLTQGQLEPLPTRLFPARQVAEA 1973
Cdd:cd08271  246 PDPPFTRALSVHEVAlgAAHDHGdpAAWQDLRYAGEELLELLAAGKLEPLVIEVLPFEQLPEA 308
Acs COG0365
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
2766-3132 4.41e-34

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


Pssm-ID: 440134 [Multi-domain]  Cd Length: 565  Bit Score: 141.02  E-value: 4.41e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2766 ATEAPPLPPRGTP-EHLAYVIYTSGSTGKPKGVAIEHRA-ALNTVVDLNTRFGVGPEDRVL---------GLS-ALTFDL 2833
Cdd:COG0365  170 AAASAEFEPEPTDaDDPLFILYTSGTTGKPKGVVHTHGGyLVHAATTAKYVLDLKPGDVFWctadigwatGHSyIVYGPL 249

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2834 S------VYDVLGLLGaggalvlpaaeaekDPAHWWERLVAGRVTVWNSTP----ALMLLLVEYAEQRGLKlpaALRLVM 2903
Cdd:COG0365  250 LngatvvLYEGRPDFP--------------DPGRLWELIEKYGVTVFFTAPtairALMKAGDEPLKKYDLS---SLRLLG 312

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2904 LSGDWIPVALPDRIR-ALGrdVQVVSLGGATEA-SIWSIAYPIGQVAPqwKSIpyGMPLANQRFHVLDGRLEARPWWVPG 2981
Cdd:COG0365  313 SAGEPLNPEVWEWWYeAVG--VPIVDGWGQTETgGIFISNLPGLPVKP--GSM--GKPVPGYDVAVVDEDGNPVPPGEEG 386

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2982 ELYIGGE--GLAREYWRDEPLTATRFIRhprTGERLYRTGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQH 3059
Cdd:COG0365  387 ELVIKGPwpGMFRGYWNDPERYRETYFG---RFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSH 463

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 53747904 3060 PALSASVVVarGEP---RGVRrLVAYAVPRSGQTPA---AGELRRYLAERLPAYMVPSAFVLLESLPRSRNGKIARDQL 3132
Cdd:COG0365  464 PAVAEAAVV--GVPdeiRGQV-VKAFVVLKPGVEPSdelAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLL 539
menE TIGR01923
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ...
 2685-3132 5.95e-34

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: 137.97  E-value: 5.95e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   2685 VQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLDPEQPPLRLHQLLEEGPARVVLTQSSLLHTvpwppGVQVIAVDELE 2764
Cdd:TIGR01923   21 IRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDSLLEEK-----DFQADSLDRIE 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   2765 -PATEAPPLPPRGTPEHLAYVIYTSGSTGKPKGVAIEHRAALNTVVDLNTRFGVGPEDRVL---------GLSAL----- 2829
Cdd:TIGR01923   96 aAGRYETSLSASFNMDQIATLMFTSGTTGKPKAVPHTFRNHYASAVGSKENLGFTEDDNWLlslplyhisGLSILfrwli 175

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   2830 -TFDLSVYDVLgllgaggalvlpaaeaekdpAHWWERLVAGRVTVWNSTPALmllLVEYAEQRGLklPAALRLVMLSGDW 2908
Cdd:TIGR01923  176 eGATLRIVDKF--------------------NQLLEMIANERVTHISLVPTQ---LNRLLDEGGH--NENLRKILLGGSA 230

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   2909 IPVALPDRIRALGRDVQvvsLG-GATEASIWSIAYPIGQVAPQWKSipyGMPLANQrfhvlDGRLEARPWWVPGELYIGG 2987
Cdd:TIGR01923  231 IPAPLIEEAQQYGLPIY---LSyGMTETCSQVTTATPEMLHARPDV---GRPLAGR-----EIKIKVDNKEGHGEIMVKG 299

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   2988 EGLAREYWRDEPLTATRFirhprtGERLYRTGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPALSASVV 3067
Cdd:TIGR01923  300 ANLMKGYLYQGELTPAFE------QQGWFNTGDIGELDGEGFLYVLGRRDDLIISGGENIYPEEIETVLYQHPGIQEAVV 373

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 53747904   3068 VARGEPRGVRRLVAYAVPRSgqTPAAGELRRYLAERLPAYMVPSAFVLLESLPRSRNGKIARDQL 3132
Cdd:TIGR01923  374 VPKPDAEWGQVPVAYIVSES--DISQAKLIAYLTEKLAKYKVPIAFEKLDELPYNASGKILRNQL 436
PLN02836 PLN02836
3-oxoacyl-[acyl-carrier-protein] synthase
 28-439 1.65e-33

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


Pssm-ID: 215449 [Multi-domain]  Cd Length: 437  Bit Score: 136.85  E-value: 1.65e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904    28 VESFWRNLVAGVESISFFSEEELRQAGVSEQIRRR-------------PEYVPAKGVLEDLELFD---AGFFGYSPREAS 91
Cdd:PLN02836   23 VETTWRRLIAGECGVRALTQDDLKMKSEDEETQLYtldqlpsrvaalvPRGTGPGDFDEELWLNSrssSRFIGYALCAAD 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904    92 hldpqqrlllecswEALEDAGLRP--DQLPGWVGVYVGAG-----DTSYRFQLLRGhgdplSGSKDVAGFFgnYPDFL-- 162
Cdd:PLN02836  103 --------------EALSDARWLPseDEAKERTGVSIGGGigsitDILEAAQLICE-----KRLRRLSPFF--VPRILin 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   163 --ATRVAYKLNLRGPALGIHTACSTSLVSINMACSALRGFECDMALAGG-------VSL----RLPARSGYLYEEGGVAS 229
Cdd:PLN02836  162 maAGHVSIRYGFQGPNHAAVTACATGAHSIGDAFRMIQFGDADVMVAGGtessidaLSIagfsRSRALSTKFNSCPTEAS 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   230 kdghcRPFDARATGTVTGDGVGVVVLKRLEDALKARDPIHAVIRGWALNNDGASragFTAPSVEGQSEVIALAHA--AAG 307
Cdd:PLN02836  242 -----RPFDCDRDGFVIGEGAGVLVLEELEHAKRRGAKIYAEVRGYGMSGDAHH---ITQPHEDGRGAVLAMTRAlqQSG 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   308 ISARDITYVEAHGTGTPLGDPIEVAALTRAFRAHtADTAFCTLGAVKSNIGHLDAAAGVAGVIKTVQALRHRLIPPTLHF 387
Cdd:PLN02836  314 LHPNQVDYVNAHATSTPLGDAVEARAIKTVFSEH-ATSGGLAFSSTKGATGHLLGAAGAVEAIFSVLAIHHGIAPPTLNL 392

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 53747904   388 ERPNPALHleqsPFFVntqPLPwESPRGPRLAGVS-SFGIGGTNAHTLFEEAP 439
Cdd:PLN02836  393 ERPDPIFD----DGFV---PLT-ASKAMLIRAALSnSFGFGGTNASLLFTSPP 437
PRK06333 PRK06333
beta-ketoacyl-ACP synthase;
13-435 5.40e-33

beta-ketoacyl-ACP synthase;


Pssm-ID: 235781 [Multi-domain]  Cd Length: 424  Bit Score: 135.13  E-value: 5.40e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904    13 IALVGMAGRFPGAPDVESFWRNLVAGVESISFFSEE--ELRQAGVSEQIRRRPEYVPAKgvledlelFDAGFFgYSPREA 90
Cdd:PRK06333    6 IVVTGMGAVSPLGCGVETFWQRLLAGQSGIRTLTDFpvGDLATKIGGQVPDLAEDAEAG--------FDPDRY-LDPKDQ 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904    91 SHLDPQQRLLLECSWEALEDAGLRPDQLPGWV--GVYVGAG-------DTSYRFQLLRGHgdplsgsKDVAGFFgnYPDF 161
Cdd:PRK06333   77 RKMDRFILFAMAAAKEALAQAGWDPDTLEDRErtATIIGSGvggfpaiAEAVRTLDSRGP-------RRLSPFT--IPSF 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   162 L----ATRVAYKLNLRGPALGIHTACSTSLVSINMACSALRGFECDMALAGG-------VSLR--LPARSgylYEEGGVA 228
Cdd:PRK06333  148 LtnmaAGHVSIRYGFKGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGteaaidrVSLAgfAAARA---LSTRFND 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   229 SKDGHCRPFDARATGTVTGDGVGVVVLKRLEDALKARDPIHAVIRGWALNNDGASragFTAPSV--EGQSEVIALAHAAA 306
Cdd:PRK06333  225 APEQASRPFDRDRDGFVMGEGAGILVIETLEHALARGAPPLAELVGYGTSADAYH---MTAGPEdgEGARRAMLIALRQA 301

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   307 GISARDITYVEAHGTGTPLGDPIEVAALTRAFrAHTADTAfctLGAVKSNIGHLDAAAGVAGVIKTVQALRHRLIPPTLH 386
Cdd:PRK06333  302 GIPPEEVQHLNAHATSTPVGDLGEVAAIKKVF-GHVSGLA---VSSTKSATGHLLGAAGGVEAIFTILALRDQIAPPTLN 377

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 53747904   387 FERPNPALhleQSPFFVNTQPLPWESprgpRLAGVSSFGIGGTNAHTLF 435
Cdd:PRK06333  378 LENPDPAA---EGLDVVANKARPMDM----DYALSNGFGFGGVNASILF 419
PTZ00354 PTZ00354
alcohol dehydrogenase; Provisional
 1680-1996 6.07e-33

alcohol dehydrogenase; Provisional


Pssm-ID: 173547 [Multi-domain]  Cd Length: 334  Bit Score: 132.46  E-value: 6.07e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  1680 PGLLESLGLRRCTRPAPGPRQVEIEVEAAGLNFLDVLGALGMMPALEAEESVLGRECSGRIAAVGEGVSGLRVGDEVLAV 1759
Cdd:PTZ00354   10 FGGVDVLKIGESPKPAPKRNDVLIKVSAAGVNRADTLQRQGKYPPPPGSSEILGLEVAGYVEDVGSDVKRFKEGDRVMAL 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  1760 APG-CFRSYVLVDESQVVRRPASLGLAEGAAQMVPFATAYFALHTVGRLRRGERILIHAAAGGLGLAAVQLASRTGAEIL 1838
Cdd:PTZ00354   90 LPGgGYAEYAVAHKGHVMHIPQGYTFEEAAAIPEAFLTAWQLLKKHGDVKKGQSVLIHAGASGVGTAAAQLAEKYGAATI 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  1839 ATAGSEQKREYLRSLGIAHVLDSRS-TSFVSEVRERTGGRGVDVVLNSLAGELLLAGLSVLAPHGRFLELGKRDLYADQQ 1917
Cdd:PTZ00354  170 ITTSSEEKVDFCKKLAAIILIRYPDeEGFAPKVKKLTGEKGVNLVLDCVGGSYLSETAEVLAVDGKWIVYGFMGGAKVEK 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  1918 VGLRTLARGQtfAAIDFGPHHP---DFRAVL-----EEVATQLTQGQLEPLPTRLFPARQVAEAFSFMARALHIGRVAVS 1989
Cdd:PTZ00354  250 FNLLPLLRKR--ASIIFSTLRSrsdEYKADLvasfeREVLPYMEEGEIKPIVDRTYPLEEVAEAHTFLEQNKNIGKVVLT 327


                  ....*..
gi 53747904  1990 MQGATAL 1996
Cdd:PTZ00354  328 VNEPLSL 334
malonate_mdcH TIGR03131
malonate decarboxylase, epsilon subunit; Members of this protein family are the epsilon ...
 534-824 8.62e-33

malonate decarboxylase, epsilon subunit; Members of this protein family are the epsilon subunit of malonate decarboxylase. This subunit has malonyl-CoA/dephospho-CoA acyltransferase activity. Malonate decarboxylase may be a soluble enzyme, or linked to membrane subunits and active as a sodium pump. The epsilon subunit is closely related to the malonyl CoA-acyl carrier protein (ACP) transacylase family described by TIGR00128, but acts on an ACP subunit of malonate decarboxylase that has an unusual coenzyme A derivative as its prothetic group.


Pssm-ID: 132175  Cd Length: 295  Bit Score: 130.90  E-value: 8.62e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904    534 LVMLFPGQGTPlvgTARALHE--SEPTFRQAVEQCARLlrqtLGLDVREVlfpsaeQEEQARrlaAQTRVAQPALFTLEY 611
Cdd:TIGR03131    1 IALLFPGQGSQ---RAGMLAElpDHPAVAAVLAEASDV----LGIDPREL------DDAEAL---ASTRSAQLCILAAGV 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904    612 ALAQTWLGWGLQPQALAGHSLGELVAACLAGVFSLEDALQLVAARGQLMQGCPPG--AMLAVP-LPEAELAALL-GSELC 687
Cdd:TIGR03131   65 AAWRALLALLPRPSAVAGYSVGEYAAAVVAGVLTFDDALRLVALRAALMDQAVPGgyGMLAVLgLDLAAVEALIaKHGVY 144

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904    688 IAAVNGPRACVASGPLPAVEALTAALESRGVS-SRRLETSHAFHSASMEACQGPLTTLLRRMRLQAPRLPCVSGLTGRwL 766
Cdd:TIGR03131  145 LAIINAPDQVVIAGSRAALRAVAELARAAGASrAKRLAVRVPSHTPLLAKAAEQFAEALAEIPLAAPRLPYLSGIDAR-L 223

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 53747904    767 TGEEATEPTYWARQLREPVRFSEALETLWSLKEPVLLEVGPGTTLTALAR-RHPTRPAR 824
Cdd:TIGR03131  224 VRDAAQIRDDLARQIATPVDWHDCMQAAYERGARLVIELGPGDVLTKLANeAFPELPAR 282
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
 2182-2625 2.19e-32

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: 134.00  E-value: 2.19e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   2182 PLTDVQEAYWVgrrsaFELGGVAAHGY-----FEIEsPGLEVERFIQCWRQLLQRHDMLRMVVLPDG----RQQVLEQVP 2252
Cdd:pfam00668    6 PLSPAQKRMWF-----LEKLEPHSSAYnmpavLKLT-GELDPERLEKALQELINRHDALRTVFIRQEngepVQVILEERP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   2253 eYTPEVVELRGLSPQEAESRRLQLRERMAHQVLRSDRWPLFELVLCRY-EGGVRIHMSMDALMLDAWSSAVLRQDFAQLY 2331
Cdd:pfam00668   80 -FELEIIDISDLSESEEEEAIEAFIQRDLQSPFDLEKGPLFRAGLFRIaENRHHLLLSMHHIIVDGVSLGILLRDLADLY 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   2332 H--EPGRPLEPLAIT-FRDYVLAERRLREGEAHERARAYWWARLDTLPPPPELPLVKEPSQLEHARFTHREARLEPHRWA 2408
Cdd:pfam00668  159 QqlLKGEPLPLPPKTpYKDYAEWLQQYLQSEDYQKDAAYWLEQLEGELPVLQLPKDYARPADRSFKGDRLSFTLDEDTEE 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   2409 RLQERARAHGLTPSAACMAAFAEVLARWSRHPRFTLNLTLFQRlpLHPQVDELVGDFTSLVLLEVEAHAASTFAERASRL 2488
Cdd:pfam00668  239 LLRKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGR--PSPDIERMVGMFVNTLPLRIDPKGGKTFSELIKRV 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   2489 QAQLWRDLEHGSVSAVQLIR--ELVRTGRRSPgaimpvVFTSILSLDARRGPQGSLSFF---EGELVYSISQTPQVWLDH 2563
Cdd:pfam00668  317 QEDLLSAEPHQGYPFGDLVNdlRLPRDLSRHP------LFDPMFSFQNYLGQDSQEEEFqlsELDLSVSSVIEEEAKYDL 390

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 53747904   2564 GVH--EEEGALVLAWDSVEALFPPGMVDDMFHAYQRLLGALAEEEQAWEGELpELLPPAQRELL 2625
Cdd:pfam00668  391 SLTasERGGGLTIKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSEL-DLLSDAEKQKL 453
LC_FACS_like cd05935
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ...
 2664-3132 3.25e-32

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: 132.99  E-value: 3.25e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2664 LSYGELARRAQALAARLRELEVQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLDPEQPPLRLHQLLEEGPARVVLTQS 2743
Cdd:cd05935    2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2744 SLlhtvpwppgvqviavdelepateapplpprgtpEHLAYVIYTSGSTGKPKGVAIEHRAALNTVVDLNTRFGVGPEDRV 2823
Cdd:cd05935   82 EL---------------------------------DDLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSDVI 128

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2824 LGLSAL--------TFDLSVYDVLGLLGAGGALVLPAAEAEKDPahwwerlvagRVTVWNSTPALMLLLVEYAEQRGLKL 2895
Cdd:cd05935  129 LACLPLfhvtgfvgSLNTAVYVGGTYVLMARWDRETALELIEKY----------KVTFWTNIPTMLVDLLATPEFKTRDL 198

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2896 pAALRLVMLSGDWIPVALPDRIRALGrDVQVVSLGGATEASIWSIAYPIGQVapqwKSIPYGMPLANQRFHVLDGR-LEA 2974
Cdd:cd05935  199 -SSLKVLTGGGAPMPPAVAEKLLKLT-GLRFVEGYGLTETMSQTHTNPPLRP----KLQCLGIP*FGVDARVIDIEtGRE 272

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2975 RPWWVPGELYIGGEGLAREYWRDEPLTATRFIRhpRTGERLYRTGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEA 3054
Cdd:cd05935  273 LPPNEVGEIVVRGPQIFKGYWNRPEETEESFIE--IKGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEA 350

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3055 ALAQHPALSASVVVARGEPRGVRRLVAYAVPRSGQ--TPAAGELRRYLAERLPAYMVPSAFVLLESLPRSRNGKIARDQL 3132
Cdd:cd05935  351 KLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYrgKVTEEDIIEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
MCS cd05941
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ...
 2655-3132 2.22e-31

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: 130.49  E-value: 2.22e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2655 PALLAPERTLSYGELARRAQALAARLRELE-VQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLDPEQPPlrlHQLlee 2733
Cdd:cd05941    3 IAIVDDGDSITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPL---AEL--- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2734 gpaRVVLTQSsllhtvpwppGVQVIavdeLEPATeapplpprgtpehlayVIYTSGSTGKPKGVAIEHRAALNTVVDLNT 2813
Cdd:cd05941   77 ---EYVITDS----------EPSLV----LDPAL----------------ILYTSGTTGRPKGVVLTHANLAANVRALVD 123

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2814 RFGVGPEDRVL---------GL-SALTFDLSVydvlgllgaggalvlpAAEAEK----DPAHWWERLVAGRVTVWNSTPA 2879
Cdd:cd05941  124 AWRWTEDDVLLhvlplhhvhGLvNALLCPLFA----------------GASVEFlpkfDPKEVAISRLMPSITVFMGVPT 187

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2880 LMLLLVEYAEQRGLKL-------PAALRLvMLSGDW-IPVALPDRIRALGRDVqVVSLGGATEASIwSIAYPI-GQVAPQ 2950
Cdd:cd05941  188 IYTRLLQYYEAHFTDPqfaraaaAERLRL-MVSGSAaLPVPTLEEWEAITGHT-LLERYGMTEIGM-ALSNPLdGERRPG 264

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2951 WksipYGMPLANQRFHVLD-GRLEARPWWVPGELYIGGEGLAREYWRDEPLTATRFirhprTGERLYRTGDQGRMLPEGS 3029
Cdd:cd05941  265 T----VGMPLPGVQARIVDeETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEF-----TDDGWFKTGDLGVVDEDGY 335

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3030 IEFLGRE-DLQVKVQGFRVELGEIEAALAQHPALSASVVVARGEPRGVRRLVAYAVPRSG-QTPAAGELRRYLAERLPAY 3107
Cdd:cd05941  336 YWILGRSsVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGaAALSLEELKEWAKQRLAPY 415

                        490       500
                 ....*....|....*....|....*
gi 53747904 3108 MVPSAFVLLESLPRSRNGKIARDQL 3132
Cdd:cd05941  416 KRPRRLILVDELPRNAMGKVNKKEL 440
MDR8 cd08273
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 1672-1987 7.77e-31

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176234 [Multi-domain]  Cd Length: 331  Bit Score: 126.22  E-value: 7.77e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1672 NVEVAVGTPGLLESLGLRRCTRPAPGPRQVEIEVEAAGLNFLDVLGALGMMPALEAEESVLGRECSGRIAAVGEGVSGLR 1751
Cdd:cd08273    1 NREVVVTRRGGPEVLKVVEADLPEPAAGEVVVKVEASGVSFADVQMRRGLYPDQPPLPFTPGYDLVGRVDALGSGVTGFE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1752 VGDEVLAVAP-GCFRSYVLVDESQVVRRPASLGLAEGAAQMVPFATAYFALHTVGRLRRGERILIHAAAGGLGLAAVQLA 1830
Cdd:cd08273   81 VGDRVAALTRvGGNAEYINLDAKYLVPVPEGVDAAEAVCLVLNYVTAYQMLHRAAKVLTGQRVLIHGASGGVGQALLELA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1831 SRTGAEILATAgSEQKREYLRSLGiAHVLDsRSTSFVSEVRERTGgrGVDVVLNSLAGELLLAGLSVLAPHGRFLELGKR 1910
Cdd:cd08273  161 LLAGAEVYGTA-SERNHAALRELG-ATPID-YRTKDWLPAMLTPG--GVDVVFDGVGGESYEESYAALAPGGTLVCYGGN 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1911 DLYADQQVGLRTLA---------------RGQTFAAI--DFGPHHPDFRAVLEEVATQLTQGQLEPLPTRLFPARQVAEA 1973
Cdd:cd08273  236 SSLLQGRRSLAALGsllarlaklkllptgRRATFYYVwrDRAEDPKLFRQDLTELLDLLAKGKIRPKIAKRLPLSEVAEA 315

                        330
                 ....*....|....
gi 53747904 1974 FsfmaRALHIGRVA 1987
Cdd:cd08273  316 H----RLLESGKVV 325
FACL_fum10p_like cd05926
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ...
 2652-3129 8.31e-31

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: 129.74  E-value: 8.31e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2652 PELPALLAPERT--LSYGELARRAQALAARLRELEVQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLDPEQPPLRLHQ 2729
Cdd:cd05926    1 PDAPALVVPGSTpaLTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2730 LLEEGPARVVLTQS--------SLLHTVP------WPPGVQVIAVDE-----LEPATEAPPLPPRGTPEHLAYVIYTSGS 2790
Cdd:cd05926   81 YLADLGSKLVLTPKgelgpasrAASKLGLailelaLDVGVLIRAPSAeslsnLLADKKNAKSEGVPLPDDLALILHTSGT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2791 TGKPKGVAIEHRAALNTVVDLNTRFGVGPEDRVLG--------------LSALTFDLSVydvlgllgaggalVLPAAeae 2856
Cdd:cd05926  161 TGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLVvmplfhvhglvaslLSTLAAGGSV-------------VLPPR--- 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2857 KDPAHWWERLVAGRVTVWNSTPALMLLLVEYAEQRGLKLPAALRLVMLSGDWIPVALPDRIRALGRdVQVVSLGGATEAS 2936
Cdd:cd05926  225 FSASTFWPDVRDYNATWYTAVPTIHQILLNRPEPNPESPPPKLRFIRSCSASLPPAVLEALEATFG-APVLEAYGMTEAA 303

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2937 IWSIAYPIGQVAPQWKSipYGMPlANQRFHVLDGRLEARPWWVPGELYIGGEGLAREYWRDEPLTATRFirhprTGERLY 3016
Cdd:cd05926  304 HQMTSNPLPPGPRKPGS--VGKP-VGVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAA-----FKDGWF 375

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3017 RTGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPALSASVVVARGEPRGVRRLVAYAVPRSGQTPAAGEL 3096
Cdd:cd05926  376 RTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGASVTEEEL 455

                        490       500       510
                 ....*....|....*....|....*....|...
gi 53747904 3097 RRYLAERLPAYMVPSAFVLLESLPRSRNGKIAR 3129
Cdd:cd05926  456 RAFCRKHLAAFKVPKKVYFVDELPKTATGKIQR 488
PRK06187 PRK06187
long-chain-fatty-acid--CoA ligase; Validated
 2644-3135 8.52e-31

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


Pssm-ID: 235730 [Multi-domain]  Cd Length: 521  Bit Score: 130.31  E-value: 8.52e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2644 FFTQARLHPELPALLAPERTLSYGELARRAQALAARLRELEVQPQELVAIAMHKGWEQATAVLGVLQAAAAYLP----LD 2719
Cdd:PRK06187   12 LRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPinirLK 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2720 PEQpplrLHQLLEEGPARVVLTQSSLL-------------HTVPW-------PPGVQVIAVDELEPATEAPPLPPRGTPE 2779
Cdd:PRK06187   92 PEE----IAYILNDAEDRVVLVDSEFVpllaailpqlptvRTVIVegdgpaaPLAPEVGEYEELLAAASDTFDFPDIDEN 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2780 HLAYVIYTSGSTGKPKGVAIEHRAALNTVVDLNTRFGVGPEDRVL-----------GLSALTFDL---SVYdvlgllgag 2845
Cdd:PRK06187  168 DAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLvivpmfhvhawGLPYLALMAgakQVI--------- 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2846 galvlpaaEAEKDPAHWWERLVAGRVTVWNSTPALMLLLVEYAEQRGLKLpAALRLVMLSGDWIPVALPDRIRALGRdVQ 2925
Cdd:PRK06187  239 --------PRRFDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFVDF-SSLRLVIYGGAALPPALLREFKEKFG-ID 308

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2926 VVSLGGATEAS-IWSIAYPIGQVAPQW-KSIPYGMPLANQRFHVLDGRLEARPWWV--PGELYIGGEGLAREYWRDEPLT 3001
Cdd:PRK06187  309 LVQGYGMTETSpVVSVLPPEDQLPGQWtKRRSAGRPLPGVEARIVDDDGDELPPDGgeVGEIIVRGPWLMQGYWNRPEAT 388

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  3002 AtRFIRHprtGerLYRTGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPALSASVVVARGEPRGVRRLVA 3081
Cdd:PRK06187  389 A-ETIDG---G--WLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVA 462

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....
gi 53747904  3082 YAVPRSGQTPAAGELRRYLAERLPAYMVPSAFVLLESLPRSRNGKIARDQLPEP 3135
Cdd:PRK06187  463 VVVLKPGATLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLREQ 516
CT_NRPS-like cd19542
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ...
 2181-2605 1.25e-30

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: 127.42  E-value: 1.25e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2181 FPLTDVQEAYWvgRRSAFELGGVAAHGYFEIESPgLEVERFIQCWRQLLQRHDMLRMVVLPDGRQQVLEQV--PEYTPEV 2258
Cdd:cd19542    2 YPCTPMQEGML--LSQLRSPGLYFNHFVFDLDSS-VDVERLRNAWRQLVQRHDILRTVFVESSAEGTFLQVvlKSLDPPI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2259 VELRGLSPQEAESRR--LQLRERMAHqvlrsdrwPLFELVLCRYEGG---VRIHMSmDALMlDAWSSAVLRQDFAQLYHe 2333
Cdd:cd19542   79 EEVETDEDSLDALTRdlLDDPTLFGQ--------PPHRLTLLETSSGevyLVLRIS-HALY-DGVSLPIILRDLAAAYN- 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2334 pGRPLEPlAITFRDYVlaerRLREGEAHERARAYWWARLDTlppppeLPLVKEPSqLEHARFTHREARLEPHRWARLQER 2413
Cdd:cd19542  148 -GQLLPP-APPFSDYI----SYLQSQSQEESLQYWRKYLQG------ASPCAFPS-LSPKRPAERSLSSTRRSLAKLEAF 214

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2414 ARAHGLTPSAACMAAFAEVLARWSRHPRFTLNLTLFQRLPLHPQVDELVGDFTSLVLLEVEAHAASTFAERASRLQAQLW 2493
Cdd:cd19542  215 CASLGVTLASLFQAAWALVLARYTGSRDVVFGYVVSGRDLPVPGIDDIVGPCINTLPVRVKLDPDWTVLDLLRQLQQQYL 294

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2494 RDLEHGSVSAVQLIRELVRTGRRSPgaimpvvFTSILSLDaRRGPQGSLSFFEGELVYSISQTPQ----VWLDHGVHEEE 2569
Cdd:cd19542  295 RSLPHQHLSLREIQRALGLWPSGTL-------FNTLVSYQ-NFEASPESELSGSSVFELSAAEDPteypVAVEVEPSGDS 366

                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 53747904 2570 GALVLAWDsvEALFPPGMVDDMFHAYQRLLGALAEE 2605
Cdd:cd19542  367 LKVSLAYS--TSVLSEEQAEELLEQFDDILEALLAN 400
Firefly_Luc_like cd05911
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ...
 2682-3127 4.02e-30

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: 127.71  E-value: 4.02e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2682 ELEVQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLDPEQPPLRLHQLLEEGPARVVLTQSSLLHTV-----PWPPGVQ 2756
Cdd:cd05911   29 KLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTDPDGLEKVkeaakELGPKDK 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2757 VIAVDELEP---------------ATEAPPLPPRGTPEHLAYVIYTSGSTGKPKGVAIEHRAALNTVVDLNTRFG--VGP 2819
Cdd:cd05911  109 IIVLDDKPDgvlsiedllsptlgeEDEDLPPPLKDGKDDTAAILYSSGTTGLPKGVCLSHRNLIANLSQVQTFLYgnDGS 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2820 EDRVLGlsALTFDlSVYDVLGLLGAGGALVLPAAEAEKDPAHWWERLVAGRVTVWNSTPALMLLLVEYAEQRGLKLPAaL 2899
Cdd:cd05911  189 NDVILG--FLPLY-HIYGLFTTLASLLNGATVIIMPKFDSELFLDLIEKYKITFLYLVPPIAAALAKSPLLDKYDLSS-L 264

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2900 RLVMLSGDWIPVALPDRIRALGRDVQVVSLGGATEASIWSIAYPIGQVAPQwkSIpyGMPLANQRFHVLD--GRLEARPW 2977
Cdd:cd05911  265 RVILSGGAPLSKELQELLAKRFPNATIKQGYGMTETGGILTVNPDGDDKPG--SV--GRLLPNVEAKIVDddGKDSLGPN 340

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2978 wVPGELYIGGEGLAREYWRDEPLTATRFirhprTGERLYRTGDQGRMLPEGSIEFLGR-EDLqVKVQGFRVELGEIEAAL 3056
Cdd:cd05911  341 -EPGEICVRGPQVMKGYYNNPEATKETF-----DEDGWLHTGDIGYFDEDGYLYIVDRkKEL-IKYKGFQVAPAELEAVL 413

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 53747904 3057 AQHPALSASVVVARGEPRGVRRLVAYAVPRSGQTPAAGELRRYLAERLPAYM-----VpsafVLLESLPRSRNGKI 3127
Cdd:cd05911  414 LEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEKLTEKEVKDYVAKKVASYKqlrggV----VFVDEIPKSASGKI 485
MACS_like_4 cd05969
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ...
 2685-3132 7.44e-30

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: 126.08  E-value: 7.44e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2685 VQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLDPEQPPLRLHQLLEEGPARVVLTQSSLLHtvpwppgvqviavdele 2764
Cdd:cd05969   22 VGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTEELYE----------------- 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2765 pateapplppRGTPEHLAYVIYTSGSTGKPKGVAIEHRAALNTVVDLNTRFGVGPEDR---------VLGLSALTF---- 2831
Cdd:cd05969   85 ----------RTDPEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLHPDDIywctadpgwVTGTVYGIWapwl 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2832 -DLSVYdvlgllgaggalvlpAAEAEKDPAHWWERLVAGRVTVWNSTPA----LMLLLVEYAEQRGLklpAALRLVMLSG 2906
Cdd:cd05969  155 nGVTNV---------------VYEGRFDAESWYGIIERVKVTVWYTAPTairmLMKEGDELARKYDL---SSLRFIHSVG 216

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2907 DwiPVAlPDRIR----ALGrdVQVVSLGGATEASIWSIA-YPIGQVAPQwksiPYGMPLANQRFHVLDGRLEARPWWVPG 2981
Cdd:cd05969  217 E--PLN-PEAIRwgmeVFG--VPIHDTWWQTETGSIMIAnYPCMPIKPG----SMGKPLPGVKAAVVDENGNELPPGTKG 287

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2982 ELYI--GGEGLAREYWRDEPLTATRFIrhprTGerLYRTGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQH 3059
Cdd:cd05969  288 ILALkpGWPSMFRGIWNDEERYKNSFI----DG--WYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEH 361

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 53747904 3060 PALSASVVVARGEPRGVRRLVAYAVPRSGQTPAAG---ELRRYLAERLPAYMVPSAFVLLESLPRSRNGKIARDQL 3132
Cdd:cd05969  362 PAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSDElkeEIINFVRQKLGAHVAPREIEFVDNLPKTRSGKIMRRVL 437
ETR_like cd05282
2-enoyl thioester reductase-like; 2-enoyl thioester reductase (ETR) catalyzes the ...
 1680-1986 5.95e-29

2-enoyl thioester reductase-like; 2-enoyl thioester reductase (ETR) catalyzes the NADPH-dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. Candida tropicalis enoyl thioester reductase (Etr1p) catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis. Etr1p forms homodimers with each subunit containing a nucleotide-binding Rossmann fold domain and a catalytic domain.


Pssm-ID: 176645 [Multi-domain]  Cd Length: 323  Bit Score: 120.46  E-value: 5.95e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1680 PGLLESLGLRRCTRPAPGPRQVEIEVEAAGLNFLDVL---GALGMMPALEAeesVLGRECSGRIAAVGEGVSGLRVGDEV 1756
Cdd:cd05282    8 EPLPLVLELVSLPIPPPGPGEVLVRMLAAPINPSDLItisGAYGSRPPLPA---VPGNEGVGVVVEVGSGVSGLLVGQRV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1757 LAVAP-GCFRSYVLVDESQVVRRPASLGLAEgAAQMV--PFaTAYFALHTVGRLRRGERILIHAAAGGLGLAAVQLASRT 1833
Cdd:cd05282   85 LPLGGeGTWQEYVVAPADDLIPVPDSISDEQ-AAMLYinPL-TAWLMLTEYLKLPPGDWVIQNAANSAVGRMLIQLAKLL 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1834 GAEILATAGSEQKREYLRSLGIAHVLDSRSTSFVSEVRERTGGRGVDVVLNSLAGELLLAGLSVLAPHGRFLELG----- 1908
Cdd:cd05282  163 GFKTINVVRRDEQVEELKALGADEVIDSSPEDLAQRVKEATGGAGARLALDAVGGESATRLARSLRPGGTLVNYGllsge 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1909 ----KRDLYADQQVGLRTLARGQTFAAIdfgpHHPDFRAVLEEVATQLTQGQLEPLPTRLFPARQVAEAFSFMARALHIG 1984
Cdd:cd05282  243 pvpfPRSVFIFKDITVRGFWLRQWLHSA----TKEAKQETFAEVIKLVEAGVLTTPVGAKFPLEDFEEAVAAAEQPGRGG 318


                 ..
gi 53747904 1985 RV 1986
Cdd:cd05282  319 KV 320
FACL_DitJ_like cd05934
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 2781-3133 6.51e-29

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: 122.79  E-value: 6.51e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2781 LAYVIYTSGSTGKPKGVAIEHRAALNTVVDLNTRFGVGPEDrVLGLSALTFDL-----SVYdvlgllgAGGALVLPAAEA 2855
Cdd:cd05934   83 PASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGEDD-VYLTVLPLFHInaqavSVL-------AALSVGATLVLL 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2856 EK-DPAHWWERLVAGRVTVWNSTPALMLLLveyaeqrgLKLPAA-------LRLVMLSGdwipvALPDRIRALGR--DVQ 2925
Cdd:cd05934  155 PRfSASRFWSDVRRYGATVTNYLGAMLSYL--------LAQPPSpddrahrLRAAYGAP-----NPPELHEEFEErfGVR 221

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2926 VVSLGGATEASIWSIAyPIGQVAPqWKSIPYGMPLANQRfhVLDGRLEARPWWVPGELYIGGE---GLAREYWRDEPLTA 3002
Cdd:cd05934  222 LLEGYGMTETIVGVIG-PRDEPRR-PGSIGRPAPGYEVR--IVDDDGQELPAGEPGELVIRGLrgwGFFKGYYNMPEATA 297

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3003 TRFirhpRTGerLYRTGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPALSASVVVARGEPRGVRRLVAY 3082
Cdd:cd05934  298 EAM----RNG--WFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAV 371

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 53747904 3083 AVPRSGQTPAAGELRRYLAERLPAYMVPSAFVLLESLPRSRNGKIARDQLP 3133
Cdd:cd05934  372 VVLRPGETLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
RTN4I1 cd08248
Human Reticulon 4 Interacting Protein 1; Human Reticulon 4 Interacting Protein 1 is a member ...
 1698-1977 1.67e-28

Human Reticulon 4 Interacting Protein 1; Human Reticulon 4 Interacting Protein 1 is a member of the medium chain dehydrogenase/ reductase (MDR) family. Riticulons are endoplasmic reticulum associated proteins involved in membrane trafficking and neuroendocrine secretion. The MDR/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES.


Pssm-ID: 176210 [Multi-domain]  Cd Length: 350  Bit Score: 120.02  E-value: 1.67e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1698 PRQVEIEVEAAGLNFLDVLGALG--------MMPALEAEES------VLGRECSGRIAAVGEGVSGLRVGDEVLAVAP-- 1761
Cdd:cd08248   29 PNQVLIKVHAASVNPIDVLMRSGygrtllnkKRKPQSCKYSgiefplTLGRDCSGVVVDIGSGVKSFEIGDEVWGAVPpw 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1762 --GCFRSYVLVDESQVVRRPASLGLAEGAAqmVPFA--TAYFALHTVGRLR----RGERILIHAAAGGLGLAAVQLASRT 1833
Cdd:cd08248  109 sqGTHAEYVVVPENEVSKKPKNLSHEEAAS--LPYAglTAWSALVNVGGLNpknaAGKRVLILGGSGGVGTFAIQLLKAW 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1834 GAEILATAgSEQKREYLRSLGIAHVLDSRSTSFVSEVRERTggrGVDVVLNSLAGELLLAGLSVLAPHGRFLELGKRDLY 1913
Cdd:cd08248  187 GAHVTTTC-STDAIPLVKSLGADDVIDYNNEDFEEELTERG---KFDVILDTVGGDTEKWALKLLKKGGTYVTLVSPLLK 262

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1914 ADQQVGlrtLARGQTFAAIDFGPH----------------HPDfRAVLEEVATQLTQGQLEPLPTRLFPARQVAEAFSFM 1977
Cdd:cd08248  263 NTDKLG---LVGGMLKSAVDLLKKnvksllkgshyrwgffSPS-GSALDELAKLVEDGKIKPVIDKVFPFEEVPEAYEKV 338
PS-DH pfam14765
Polyketide synthase dehydratase; This is the dehydratase domain of polyketide synthases. ...
 1410-1659 2.58e-28

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: 117.86  E-value: 2.58e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   1410 TLRGGEDWVVDEHRLQGVPTLPGVAYLELARAACAQALGAEAVELAELLL-LEPLTVPRGESRQVRVVLQPEGQAHALRV 1488
Cdd:pfam14765   21 RLRLADLPWLRDHRVGGTVVLPGAGYLEMALEAARQLFGGSGAVALRDVSiLKALVLPEDDPVEVQTSLTPEEDGADSWW 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   1489 E----SRSEEARGWNEHARGRVRAVPRL-AERIQPELLRAACehEQPVPGEPQEQGPVHAGARWHGL-----FQWVR--- 1555
Cdd:pfam14765  101 EfeifSRAGGGWEWTLHATGTVRLAPGEpAAPVDLESLPARC--AQPADPRSVSSAEFYERLAARGLfygpaFQGLRriw 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   1556 RGPRQALAQLALPEPFHGDLERFELHPALMDMA--------TSFAIPGGVPWLAFGYERVLIHGPLPPQ--VLSHVSLPE 1625
Cdd:pfam14765  179 RGDGEALAEARLPEAAAGGESPYLLHPALLDAAlqllgaalPAEAEHADQAYLPVGIERLRIYRSLPPGepLWVHARLER 258

                          250       260       270
                   ....*....|....*....|....*....|....
gi 53747904   1626 EsqaGAQQLRLQVRLLDLEGWERVRIDGYLLRPL 1659
Cdd:pfam14765  259 R---GGRTIVGDLTLVDEDGRVVARIEGLRLRRV 289
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
 1693-1991 4.92e-28

Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and metabolism, General function prediction only]; Threonine dehydrogenase or related Zn-dependent dehydrogenase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 440683 [Multi-domain]  Cd Length: 341  Bit Score: 118.32  E-value: 4.92e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1693 RPAPGPRQVEIEVEAAGLNFLDVLGALGMMPALEAEeSVLGRECSGRIAAVGEGVSGLRVGDEVlAVAP----------- 1761
Cdd:COG1063   19 DPEPGPGEVLVRVTAVGICGSDLHIYRGGYPFVRPP-LVLGHEFVGEVVEVGEGVTGLKVGDRV-VVEPnipcgecrycr 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1762 -------------------GCFRSYVLVDESQVVRRPASLGLAEGAaqMV-PFATAYFALHtVGRLRRGERILI------ 1815
Cdd:COG1063   97 rgrynlcenlqflgiagrdGGFAEYVRVPAANLVKVPDGLSDEAAA--LVePLAVALHAVE-RAGVKPGDTVLVigagpi 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1816 ---HaaagglglaaVQLASRTGA-EILATAGSEQKREYLRSLGIAHVLDSRSTSFVSEVRERTGGRGVDVVLN-SLAGEL 1890
Cdd:COG1063  174 gllA----------ALAARLAGAaRVIVVDRNPERLELARELGADAVVNPREEDLVEAVRELTGGRGADVVIEaVGAPAA 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1891 LLAGLSVLAPHGRFLELGkrdLYADQ-QVGLRTL-ARGQTFAAIdFGPHHPDFRAVLEEVAtqltQGQL--EPLPTRLFP 1966
Cdd:COG1063  244 LEQALDLVRPGGTVVLVG---VPGGPvPIDLNALvRKELTLRGS-RNYTREDFPEALELLA----SGRIdlEPLITHRFP 315

                        330       340
                 ....*....|....*....|....*.
gi 53747904 1967 ARQVAEAF-SFMARALHIGRVAVSMQ 1991
Cdd:COG1063  316 LDDAPEAFeAAADRADGAIKVVLDPD 341
KR_1_SDR_x cd08952
ketoreductase (KR), subgroup 1, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
 903-1380 8.16e-27

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: 117.66  E-value: 8.16e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  903 PPEQPSREALEDWFYVPTWEQAPATSGGgqPLAGP---VLAFMDSSGLAEQVLAALwpADSGALLTRVEPAGHYEQLSEH 979
Cdd:cd08952    2 RRRRRERAAVDSWRYRVTWRPLPDPPAA--RLTGTwlvVVPAGADDALAAAVARAL--AAAGAEVVVLEVDAADADAAAA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  980 AFRLRPESEEDWDAlfqalqsqgrlprrILHAWALTAEPGPCTPDGEAVLEqgffSLLRLARALGRHAPERPvqLEVLSS 1059
Cdd:cd08952   78 AALAAAAAGGPVAG--------------VLSLLALDERPHPDHPAVPAGLA----ATLALVQALGDAGVDAP--LWCVTR 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1060 FVHAVGPREPL-EPLKATLLGACAVLPLEYPHVQCRTIDVRPGSEPRevLVRSLAAELAAPMGESPVAWRDGQRYVRRAT 1138
Cdd:cd08952  138 GAVAVGPDDPLpDPAQAAVWGLGRVAALEHPDRWGGLVDLPADLDAR--ALRRLAAVLAGAGGEDQVAVRASGVFARRLV 215

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1139 RQRLEASRP----------------------LRSLRERGVylvagglggiglvlaralaqrararlallthspfppreqw 1196
Cdd:cd08952  216 RAPAPAPAArpwrprgtvlvtggtgalgahvARWLARRGA---------------------------------------- 255

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1197 EQWL------EEAPAHPEPAwrseadpserrrtqhrirclLELEQLGAEVQVYTADVAEEAAVRSVVEQVHARWGkIHGV 1270
Cdd:cd08952  256 EHLVltsrrgPDAPGAAELV--------------------AELTALGARVTVAACDVADRDALAALLAALPAGHP-LTAV 314

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1271 LHAAATFDDGVIQLRTHEQSSRALRTKVRGSMVLHEVLASEGLDWFALCSSLASALGSFGQADYCAANAFQDAYAHHLRR 1350
Cdd:cd08952  315 VHAAGVLDDGPLDDLTPERLAEVLRAKVAGARHLDELTRDRDLDAFVLFSSIAGVWGSGGQGAYAAANAYLDALAERRRA 394

                        490       500       510
                 ....*....|....*....|....*....|..
gi 53747904 1351 QGFTgALALDWGTWRDTGAAMRLVAR--TRRG 1380
Cdd:cd08952  395 RGLP-ATSVAWGPWAGGGMAAGAAAErlRRRG 425
PLN02752 PLN02752
[acyl-carrier protein] S-malonyltransferase
 531-817 8.58e-27

[acyl-carrier protein] S-malonyltransferase


Pssm-ID: 215401 [Multi-domain]  Cd Length: 343  Bit Score: 114.86  E-value: 8.58e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   531 RPPLVMLFPGQGTPLVGTARALHE---SEPTFRQAveqcarllRQTLGLDVREVLFpsaeqEEQARRLAAqTRVAQPALF 607
Cdd:PLN02752   37 KPTTAFLFPGQGAQAVGMGKEAAEvpaAKALFDKA--------SEILGYDLLDVCV-----NGPKEKLDS-TVVSQPAIY 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   608 TLEYALAQTWLGWGLQPQAL------AGHSLGELVAACLAGVFSLEDALQLVAARGQLMQGC---PPGAMLAV------- 671
Cdd:PLN02752  103 VASLAAVEKLRARDGGQAVIdsvdvcAGLSLGEYTALVFAGALSFEDGLKLVKLRGEAMQAAadaGPSGMVSVigldsdk 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   672 --PLPEAELAALLGSELC-IAAVNGPRACVASGPLPAVEALTAALESRGV-SSRRLETSHAFHSASMEACQGPLTTLLRR 747
Cdd:PLN02752  183 vqELCAAANEEVGEDDVVqIANYLCPGNYAVSGGKKGIDAVEAKAKSFKArMTVRLAVAGAFHTSFMEPAVDALEAALAA 262

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   748 MRLQAPRLPCVSGLTGRwLTGEEATEPTYWARQLREPVRFSEALETLWSLKEPVLLEVGPGTTLTALARR 817
Cdd:PLN02752  263 VEIRTPRIPVISNVDAQ-PHSDPATIKKILARQVTSPVQWETTVKTLLEKGLEKSYELGPGKVIAGIVKR 331
AdhP COG1064
D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport ...
 1693-1986 1.07e-26

D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport and metabolism];


Pssm-ID: 440684 [Multi-domain]  Cd Length: 332  Bit Score: 114.05  E-value: 1.07e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1693 RPAPGPRQVEIEVEAAGLNFLDVLGALGMMPALeAEESVLGRECSGRIAAVGEGVSGLRVGDEVlAVAP--GC------- 1763
Cdd:COG1064   20 RPEPGPGEVLVKVEACGVCHSDLHVAEGEWPVP-KLPLVPGHEIVGRVVAVGPGVTGFKVGDRV-GVGWvdSCgtceycr 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1764 --------------------FRSYVLVDESQVVRRPASLGLAEGAAQMVPFATAYFALHTVGrLRRGERILI-------H 1816
Cdd:COG1064   98 sgrenlcengrftgyttdggYAEYVVVPARFLVKLPDGLDPAEAAPLLCAGITAYRALRRAG-VGPGDRVAVigagglgH 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1817 AaagglglaAVQLASRTGAEILATAGSEQKREYLRSLGIAHVLDSRSTSFVSEVRERTggrGVDVVLN-SLAGELLLAGL 1895
Cdd:COG1064  177 L--------AVQIAKALGAEVIAVDRSPEKLELARELGADHVVNSSDEDPVEAVRELT---GADVVIDtVGAPATVNAAL 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1896 SVLAPHGRFLelgkrdlyadqQVGL----------RTLARGQTFAaidfGPHH---PDFRAVLEEVAtqltQGQLEPLpT 1962
Cdd:COG1064  246 ALLRRGGRLV-----------LVGLpggpiplppfDLILKERSIR----GSLIgtrADLQEMLDLAA----EGKIKPE-V 305

                        330       340
                 ....*....|....*....|....
gi 53747904 1963 RLFPARQVAEAFSFMARALHIGRV 1986
Cdd:COG1064  306 ETIPLEEANEALERLRAGKVRGRA 329
PRK13295 PRK13295
cyclohexanecarboxylate-CoA ligase; Reviewed
 2652-3134 2.11e-26

cyclohexanecarboxylate-CoA ligase; Reviewed


Pssm-ID: 171961 [Multi-domain]  Cd Length: 547  Bit Score: 117.08  E-value: 2.11e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2652 PELPALLAPE------RTLSYGELARRAQALAARLRELEVQPQELVAIAMHKGWEQATAVLGVLQAAAAylpLDPEQPPL 2725
Cdd:PRK13295   38 PDKTAVTAVRlgtgapRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAV---LNPLMPIF 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2726 RLHQL---LEEGPARVVLTQSSL-----------LHTvPWPPGVQVIAVD----------------ELEPATEAPPLPPR 2775
Cdd:PRK13295  115 RERELsfmLKHAESKVLVVPKTFrgfdhaamarrLRP-ELPALRHVVVVGgdgadsfeallitpawEQEPDAPAILARLR 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2776 GTPEHLAYVIYTSGSTGKPKGVAIEHRAALNTVVDLNTRFGVGPEDRVLGLSALtfdlsvydvLGLLGAGGALVLPAAEA 2855
Cdd:PRK13295  194 PGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPM---------AHQTGFMYGLMMPVMLG 264

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2856 EK-------DPAHWWERLVAGRVT-VWNSTPALMlLLVEYAEQRGLKLPaALRLVMLSGDWIPVALPDRIRA-LGrdVQV 2926
Cdd:PRK13295  265 ATavlqdiwDPARAAELIRTEGVTfTMASTPFLT-DLTRAVKESGRPVS-SLRTFLCAGAPIPGALVERARAaLG--AKI 340

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2927 VSLGGATEASIWSIAYPigQVAPQWKSIPYGMPLANQRFHVLDGRLEARPWWVPGELYIGGEGLAREYWRDEPLTATRFi 3006
Cdd:PRK13295  341 VSAWGMTENGAVTLTKL--DDPDERASTTDGCPLPGVEVRVVDADGAPLPAGQIGRLQVRGCSNFGGYLKRPQLNGTDA- 417

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  3007 rhprtgERLYRTGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPALSASVVVARGEPRGVRRLVAYAVPR 3086
Cdd:PRK13295  418 ------DGWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPR 491

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*....
gi 53747904  3087 SGQTPAAGELRRYL-AERLPAYMVPSAFVLLESLPRSRNGKIARDQLPE 3134
Cdd:PRK13295  492 PGQSLDFEEMVEFLkAQKVAKQYIPERLVVRDALPRTPSGKIQKFRLRE 540
enoyl_reductase_like cd08249
enoyl_reductase_like; Member identified as possible enoyl reductase of the MDR family. 2-enoyl ...
 1694-1966 3.53e-26

enoyl_reductase_like; Member identified as possible enoyl reductase of the MDR family. 2-enoyl thioester reductase (ETR) catalyzes the NADPH-dependent dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. Candida tropicalis enoyl thioester reductase (Etr1p) catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis. Etr1p forms homodimers with each subunit containing a nucleotide-binding Rossmann fold domain and a catalytic domain.


Pssm-ID: 176211 [Multi-domain]  Cd Length: 339  Bit Score: 112.68  E-value: 3.53e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1694 PAPGPRQVEIEVEAAGLNFLDV----LGALGMMPAleaeesVLGRECSGRIAAVGEGVSGLRVGDEVLAVAPGC------ 1763
Cdd:cd08249   22 PKPGPDEVLVKVKAVALNPVDWkhqdYGFIPSYPA------ILGCDFAGTVVEVGSGVTRFKVGDRVAGFVHGGnpndpr 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1764 ---FRSYVLVDESQVVRRPASLGLAEGAAQMVPFATAYFALHTVGRLR----------RGERILIHAAAGGLGLAAVQLA 1830
Cdd:cd08249   96 ngaFQEYVVADADLTAKIPDNISFEEAATLPVGLVTAALALFQKLGLPlpppkpspasKGKPVLIWGGSSSVGTLAIQLA 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1831 SRTGAEILATAgSEQKREYLRSLGIAHVLDSRSTSFVSEVRERTGGR---GVDVVlnsLAGELLLAGLSVLAPH--GRFL 1905
Cdd:cd08249  176 KLAGYKVITTA-SPKNFDLVKSLGADAVFDYHDPDVVEDIRAATGGKlryALDCI---STPESAQLCAEALGRSggGKLV 251

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 53747904 1906 ELGKRDLYADQQVGLRTlarGQTFAAIDFG--PHHPDFRAVLEEVATQ-LTQGQLEPLPTRLFP 1966
Cdd:cd08249  252 SLLPVPEETEPRKGVKV---KFVLGYTVFGeiPEDREFGEVFWKYLPElLEEGKLKPHPVRVVE 312
KR_3_FAS_SDR_x cd08956
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 3, complex (x); ...
 1232-1381 4.72e-26

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: 114.67  E-value: 4.72e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1232 ELEQLGAEVQVYTADVAEEAAVRSVVEQVHARWGkIHGVLHAAATFDDGVIQLRTHEQSSRALRTKVRGSMVLHEVLASE 1311
Cdd:cd08956  241 ELAALGAEVTVAACDVADRAALAALLAAVPADHP-LTAVVHAAGVLDDGVLTSLTPERLDAVLRPKVDAAWHLHELTRDL 319

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 53747904 1312 GLDWFALCSSLASALGSFGQADYCAANAFQDAYAHHLRRQGFTgALALDWGTWRDTGAAMRL-----VARTRRGG 1381
Cdd:cd08956  320 DLAAFVLFSSAAGVLGSPGQANYAAANAFLDALAQHRRARGLP-ATSLAWGLWAQASGMTAHlsdadLARLARGG 393
MDR_enoyl_red cd08244
Possible enoyl reductase; Member identified as possible enoyl reductase of the MDR family. ...
 1684-1973 4.73e-26

Possible enoyl reductase; Member identified as possible enoyl reductase of the MDR family. 2-enoyl thioester reductase (ETR) catalyzes the NADPH-dependent dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. Candida tropicalis enoyl thioester reductase (Etr1p) catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis. Etr1p forms homodimers, with each subunit containing a nucleotide-binding Rossmann fold domain and a catalytic domain.


Pssm-ID: 176206 [Multi-domain]  Cd Length: 324  Bit Score: 112.08  E-value: 4.73e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1684 ESLGLRRCTRPAPGPRQVEIEVEAAGLNFLD--VLGALGMMPALEAEESVLGRECSGRIAAVGEGVSGLRVGDEV---LA 1758
Cdd:cd08244   13 EVLVPEDVPDPVPGPGQVRIAVAAAGVHFVDtqLRSGWGPGPFPPELPYVPGGEVAGVVDAVGPGVDPAWLGRRVvahTG 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1759 VAPGCFRSYVLVDESQVVRRPASLGLAEGAAQMVPFATAyFALHTVGRLRRGERILIHAAAGGLGLAAVQLASRTGAEIL 1838
Cdd:cd08244   93 RAGGGYAELAVADVDSLHPVPDGLDLEAAVAVVHDGRTA-LGLLDLATLTPGDVVLVTAAAGGLGSLLVQLAKAAGATVV 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1839 ATAGSEQKREYLRSLGIAHVLDSRSTSFVSEVRERTGGRGVDVVLNSLAGELLLAGLSVLAPHGRFLELGKRDLYADQQV 1918
Cdd:cd08244  172 GAAGGPAKTALVRALGADVAVDYTRPDWPDQVREALGGGGVTVVLDGVGGAIGRAALALLAPGGRFLTYGWASGEWTALD 251

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 53747904 1919 GLRTLARGQT-FAAIDFGPHHPDFRAVLEEVATQLTQGQLEPLPTRLFPARQVAEA 1973
Cdd:cd08244  252 EDDARRRGVTvVGLLGVQAERGGLRALEARALAEAAAGRLVPVVGQTFPLERAAEA 307
PRK08722 PRK08722
beta-ketoacyl-ACP synthase II;
13-437 4.86e-26

beta-ketoacyl-ACP synthase II;


Pssm-ID: 181539 [Multi-domain]  Cd Length: 414  Bit Score: 113.94  E-value: 4.86e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904    13 IALVGMAGRFPGAPDVESFWRNLVAGVESISffSEEELRQAGVSEQIrrrpeyvpaKGVLEDlelFDAGFFgYSPREASH 92
Cdd:PRK08722    6 VVVTGMGMLSPVGNTVESSWKALLAGQSGIV--NIEHFDTTNFSTRF---------AGLVKD---FNCEEY-MSKKDARK 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904    93 LDPQQRLLLECSWEALEDAGLR-PDQLPGWVGVYVGAGDTSYRFqLLRGHGDPLS-GSKDVAGFFgnYPDFLATRVAYKL 170
Cdd:PRK08722   71 MDLFIQYGIAAGIQALDDSGLEvTEENAHRIGVAIGSGIGGLGL-IEAGHQALVEkGPRKVSPFF--VPSTIVNMIAGNL 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   171 N----LRGPALGIHTACSTSLVSINMACSALRGFECDMALAGGVS-LRLPARSGYLYEEGGVASKDGH----CRPFDARA 241
Cdd:PRK08722  148 SimrgLRGPNIAISTACTTGLHNIGHAARMIAYGDADAMVAGGAEkASTPLGMAGFGAAKALSTRNDEpqkaSRPWDKDR 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   242 TGTVTGDGVGVVVLKRLEDAlKARDP-IHAVIRGWALNNDGASragFTAPSVEGQSEVIALAHAA--AGISARDITYVEA 318
Cdd:PRK08722  228 DGFVLGDGAGMMVLEEYEHA-KARGAkIYAELVGFGMSGDAYH---MTSPSEDGSGGALAMEAAMrdAGVTGEQIGYVNA 303

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   319 HGTGTPLGDPIEVAALTRAFRAHTADTAFCTlgAVKSNIGHLDAAAGVAGVIKTVQALRHRLIPPTLHFERPNPALHLEQ 398
Cdd:PRK08722  304 HGTSTPAGDVAEIKGIKRALGEAGSKQVLVS--STKSMTGHLLGAAGSVEAIITVMSLVDQIVPPTINLDDPEEGLDIDL 381

                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 53747904   399 SPFFVntqplpwESPRGPRLAGVSSFGIGGTNAHTLFEE 437
Cdd:PRK08722  382 VPHTA-------RKVESMEYAICNSFGFGGTNGSLIFKK 413
PRK08314 PRK08314
long-chain-fatty-acid--CoA ligase; Validated
 2648-3134 5.00e-26

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


Pssm-ID: 236235 [Multi-domain]  Cd Length: 546  Bit Score: 116.21  E-value: 5.00e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2648 ARLHPELPALLAPERTLSYGELARRAQALAA-RLRELEVQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLDPEQPPLR 2726
Cdd:PRK08314   20 ARRYPDKTAIVFYGRAISYRELLEEAERLAGyLQQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEE 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2727 LHQLLEEGPARVVLTQSSLL-------------H--------TVPWPPGVQVIAVDELEPATEA---------------- 2769
Cdd:PRK08314  100 LAHYVTDSGARVAIVGSELApkvapavgnlrlrHvivaqysdYLPAEPEIAVPAWLRAEPPLQAlapggvvawkealaag 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2770 -PPLPPRGTPEHLAYVIYTSGSTGKPKGVAIEHRAALNTVVDLNTRFGVGPEDRVLGLSALtFDL---------SVYDVL 2839
Cdd:PRK08314  180 lAPPPHTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPL-FHVtgmvhsmnaPIYAGA 258

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2840 GLLGAGGalvlpaaeaekdpahwWERLVAG------RVTVWNSTPALM--LLLVEYAEQRGLklpAALRLVMLSGDWIPV 2911
Cdd:PRK08314  259 TVVLMPR----------------WDREAAArlieryRVTHWTNIPTMVvdFLASPGLAERDL---SSLRYIGGGGAAMPE 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2912 ALPDRIRAL-GrdVQVVSLGGATEASIWSIAYPIGQVAPQWKSIPYgmplanqrFHVlDGR------LEARPWWVPGELY 2984
Cdd:PRK08314  320 AVAERLKELtG--LDYVEGYGLTETMAQTHSNPPDRPKLQCLGIPT--------FGV-DARvidpetLEELPPGEVGEIV 388

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2985 IGGEGLAREYWRDEPLTATRFIRhpRTGERLYRTGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPALSA 3064
Cdd:PRK08314  389 VHGPQVFKGYWNRPEATAEAFIE--IDGKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQE 466

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 53747904  3065 SVVVARGEPRGVRRLVAYAVPRSGQ--TPAAGELRRYLAERLPAYMVPSAFVLLESLPRSRNGKIARDQLPE 3134
Cdd:PRK08314  467 ACVIATPDPRRGETVKAVVVLRPEArgKTTEEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQLQE 538
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
 2206-2421 6.05e-26

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


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 109.36  E-value: 6.05e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2206 HGYFEIESPgLEVERFIQCWRQLLQRHDMLRMV-VLPDGR-QQVLEQVPEYTPEVVELRGLSPQEAESRRLQLRERMAHQ 2283
Cdd:COG4908   21 PAVLRLEGP-LDVEALERALRELVRRHPALRTRfVEEDGEpVQRIDPDADLPLEVVDLSALPEPEREAELEELVAEEASR 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2284 VLRSDRWPLFELVL-CRYEGGVRIHMSMDALMLDAWSSAVLRQDFAQLYHEPGR----PLEPLAITFRDYVLAERRLREG 2358
Cdd:COG4908  100 PFDLARGPLLRAALiRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALLEgeppPLPELPIQYADYAAWQRAWLQS 179

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 53747904 2359 EAHERARAYWWARLDTLPPPPELPLVKEPSQLEHARFTHREARLEPHRWARLQERARAHGLTP 2421
Cdd:COG4908  180 EALEKQLEYWRQQLAGAPPVLELPTDRPRPAVQTFRGATLSFTLPAELTEALKALAKAHGATV 242
CHC_CoA_lg cd05903
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ...
 2663-3134 7.53e-26

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: 114.01  E-value: 7.53e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2663 TLSYGELARRAQALAARLRELEVQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLdpeQPPLRLHQL---LEEGPARVV 2739
Cdd:cd05903    1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPI---LPFFREHELafiLRRAKAKVF 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2740 LTQSSLLHTVPWPpgvqviavdelepateapplpprgTPEHLAYVIYTSGSTGKPKGVAIEHRAALNTVVDLNTRFGVGP 2819
Cdd:cd05903   78 VVPERFRQFDPAA------------------------MPDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGP 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2820 EDRVLGLSALT-FDLSVYdvlgLLGAGGALVLPAAEAEK-DPAHWWERLVAGRVTVWNSTPALMLLLVEYAEQRGLKLPa 2897
Cdd:cd05903  134 GDVFLVASPMAhQTGFVY----GFTLPLLLGAPVVLQDIwDPDKALALMREHGVTFMMGATPFLTDLLNAVEEAGEPLS- 208

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2898 ALRLVMLSGDWIPVALPDRIRALGRDVqVVSLGGATEASIWSIAYPIGQVAPQWKSipYGMPLANQRFHVLDGRLEARPW 2977
Cdd:cd05903  209 RLRTFVCGGATVPRSLARRAAELLGAK-VCSAYGSTECPGAVTSITPAPEDRRLYT--DGRPLPGVEIKVVDDTGATLAP 285

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2978 WVPGELYIGGEGLAREYWRDEPLTATRFirhprtGERLYRTGDQGRMLPEGSIEFLGR-EDLQVKvQGFRVELGEIEAAL 3056
Cdd:cd05903  286 GVEGELLSRGPSVFLGYLDRPDLTADAA------PEGWFRTGDLARLDEDGYLRITGRsKDIIIR-GGENIPVLEVEDLL 358

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 53747904 3057 AQHPALSASVVVARGEPRGVRRLVAYAVPRSGQTPAAGELRRYL-AERLPAYMVPSAFVLLESLPRSRNGKIARDQLPE 3134
Cdd:cd05903  359 LGHPGVIEAAVVALPDERLGERACAVVVTKSGALLTFDELVAYLdRQGVAKQYWPERLVHVDDLPRTPSGKVQKFRLRE 437
PRK07103 PRK07103
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
 98-431 9.38e-26

polyketide beta-ketoacyl:acyl carrier protein synthase; Validated


Pssm-ID: 180839 [Multi-domain]  Cd Length: 410  Bit Score: 113.20  E-value: 9.38e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904    98 RLLLECSWEALEDAGLRPDQlPGWVGVYVGAGDTSYRFQLLrghgdplsgskdVAGFFGNYPDFLATR------------ 165
Cdd:PRK07103   82 QAALAAAREAWRDAALGPVD-PDRIGLVVGGSNLQQREQAL------------VHETYRDRPAFLRPSyglsfmdtdlvg 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   166 -VAYKLNLRGPALGIHTACSTSLVSINMACSALRGFECDMALAGGVSLRLP-------ARSGYLYEEGGVASKDGHCRPF 237
Cdd:PRK07103  149 lCSEQFGIRGEGFTVGGASASGQLAVIQAARLVQSGSVDACIAVGALMDLSywecqalRSLGAMGSDRFADEPEAACRPF 228

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   238 DARATGTVTGDGVGVVVLKRLEDALKARDPIHAVIRGWALNNDGASRagfTAPSVEGQSEVIALAHAAAGISARDITYVE 317
Cdd:PRK07103  229 DQDRDGFIYGEACGAVVLESAESARRRGARPYAKLLGWSMRLDANRG---PDPSLEGEMRVIRAALRRAGLGPEDIDYVN 305

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   318 AHGTGTPLGDPIEVAALTRAFRAHtadtafCTLGAVKSNIGHLDAAAGVAGVIKTVQALRHRLIPPTLHFERP-NPALHl 396
Cdd:PRK07103  306 PHGTGSPLGDETELAALFASGLAH------AWINATKSLTGHGLSAAGIVELIATLLQMRAGFLHPSRNLDEPiDERFR- 378

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 53747904   397 eqspfFVNTQPLPWESprgpRLAGVSSFGIGGTNA 431
Cdd:PRK07103  379 -----WVGSTAESARI----RYALSLSFGFGGINT 404
MACS_like_2 cd05973
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
 2664-3129 8.67e-25

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: 110.69  E-value: 8.67e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2664 LSYGELARRAQALAARLRELEVQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLDPEQPPLRLHQLLEEGPARVVLTQS 2743
Cdd:cd05973    1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTDA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2744 SLLHTVPWPPGVQviavdelepateapplpprgtpehlayvIYTSGSTGKPKGVAIEHRAALNTVVDLNTRFGVGPEDRV 2823
Cdd:cd05973   81 ANRHKLDSDPFVM----------------------------MFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPEDSF 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2824 LGLSALTFDLSVYdvlgllgaggalvlpaaEAEKDPahwwerLVAGRVTVWN----STPALMLLLVEYAEQRGLKLPAAL 2899
Cdd:cd05973  133 WNAADPGWAYGLY-----------------YAITGP------LALGHPTILLeggfSVESTWRVIERLGVTNLAGSPTAY 189

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2900 RLVMLSGDWIPVALPDRIRalgrdvqVVSLGG---ATEASIWSIAYPIGQVAPQWKSIPYGMPLANQ------------- 2963
Cdd:cd05973  190 RLLMAAGAEVPARPKGRLR-------RVSSAGeplTPEVIRWFDAALGVPIHDHYGQTELGMVLANHhalehpvhagsag 262

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2964 ------RFHVLDGRLEARPWWVPGELYIGGeglareywRDEPLTATRFIRHPRTGE---RLYRTGDQGRMLPEGSIEFLG 3034
Cdd:cd05973  263 rampgwRVAVLDDDGDELGPGEPGRLAIDI--------ANSPLMWFRGYQLPDTPAidgGYYLTGDTVEFDPDGSFSFIG 334

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3035 REDLQVKVQGFRVELGEIEAALAQHPALSASVVVARGEPRGVRRLVAYAVPRSGQ--TPA-AGELRRYLAERLPAYMVPS 3111
Cdd:cd05973  335 RADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHegTPAlADELQLHVKKRLSAHAYPR 414

                        490
                 ....*....|....*...
gi 53747904 3112 AFVLLESLPRSRNGKIAR 3129
Cdd:cd05973  415 TIHFVDELPKTPSGKIQR 432
ArgR-Cyc_NRPS-like cd20480
Cyc (heterocyclization)-like domain of Vibrio anguillarum AngR and similar proteins; belongs ...
 2208-2606 9.44e-25

Cyc (heterocyclization)-like domain of Vibrio anguillarum AngR and similar proteins; belongs to the Condensation-domain family; Vibrio anguillarum AngR plays a role in regulating the expression of iron transport genes as well as in the production of the siderophore anguibactin. Cyc-domains are a type of Condensation (C) domain. Cyc-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. C-domains typically have a conserved HHxxxD motif at the active site; Cyc-domains have a alternative, conserved DxxxxD active site motif, mutation of the aspartate residues in this motif can abolish or diminish condensation activity. Members of this subfamily have an SxxxD motif at the active site. 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). In addition to Cyc-domains there are various other 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. 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: 380470 [Multi-domain]  Cd Length: 406  Bit Score: 109.90  E-value: 9.44e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2208 YFEIESPGLEVERFIQCWRQLLQRHDMLRMVVLPDGRQQVLEQVPEYTPEVVELRGLSPQEAEsrrlqlrERMAH---QV 2284
Cdd:cd20480   29 YQEFDYENISVDTLERCLTVLINHHPMLHALLSDDFYLHINSKNQIDAFAVNDLSSASEQEAA-------EQLARtraTL 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2285 LRSDRWPLFELVLCRYEGG-VRIHMSMDALMLDAWSSAVLRQDFAQLYHepGRPLEPLAITfrDYVLAERRLREGEAHE- 2362
Cdd:cd20480  102 TKSRSKATISVVLSLLPANkIRLHVRFNSVVVDHPSVNLFFEQLCQLLR--GSLLSFLAQE--QVILAHNQLVISELQSt 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2363 -RARAYWWARLDTLPPPPELPLVKEPSQLEHARFTHREARLEPHRWARLQERARAHGLTPSAACMAAFAEVLARWSRHPR 2441
Cdd:cd20480  178 gLSSAFWNEQILQLPSSANLPTVCEPEKLRETGITRRTLTLSSDKWQQLVTISKQHNVTPELTLASIFSAVLSLWGNQKD 257

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2442 FTLnltlfqRLPLHPQVD--ELVGDFTSLVLLEVEAHAAStFAERASRLQAQLWRDLEHGSVSAVQLIRELVRT--GRRS 2517
Cdd:cd20480  258 MML------RFDLNKKNDvaGVIGQFTQPLLVGLSGFGQS-FLSLVKENQKHFEQAYPFRQIPIFDLVRQLAKLseSHRY 330

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2518 PGAImpvVFTSILSldarrGPQGSlsffeGELVYSISQTPQVWLD-HGVHEEEGaLVLAWDSVEALFPPGMVDDMFHAYQ 2596
Cdd:cd20480  331 PANI---AFSSQLS-----GNNTL-----GRSGWGCRQSANTWLSlHAFISQGG-LILQWDSQDALFPKDMIQDMLTSYS 396

                        410
                 ....*....|
gi 53747904 2597 RLLGALAEEE 2606
Cdd:cd20480  397 KLLESLSQSD 406
ACS-like cd17634
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ...
 2662-3127 1.63e-24

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: 111.90  E-value: 1.63e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2662 RTLSYGELARRAQALAARLRELEVQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLDPEQPPLRLHQLLEEGPARVVLT 2741
Cdd:cd17634   83 RTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLIT 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2742 QSSLLH---TVPWPPGV------------QVIAVDELEPATEAPP------------LPPRGTPEHLA-----YVIYTSG 2789
Cdd:cd17634  163 ADGGVRagrSVPLKKNVddalnpnvtsveHVIVLKRTGSDIDWQEgrdlwwrdliakASPEHQPEAMNaedplFILYTSG 242

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2790 STGKPKGVAIEHRA-ALNTVVDLNTRFGVGPEDRVLGLSALTFDLS----VYDVLGLLGAGGALVlpAAEAEKDPAHWWE 2864
Cdd:cd17634  243 TTGKPKGVLHTTGGyLVYAATTMKYVFDYGPGDIYWCTADVGWVTGhsylLYGPLACGATTLLYE--GVPNWPTPARMWQ 320

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2865 RLVAGRVTVWNSTP----ALMLLLVEYAEQRGLklpAALRLVMLSGD-WIPVALPDRIRALGRD-VQVVSLGGATEASiW 2938
Cdd:cd17634  321 VVDKHGVNILYTAPtairALMAAGDDAIEGTDR---SSLRILGSVGEpINPEAYEWYWKKIGKEkCPVVDTWWQTETG-G 396

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2939 SIAYPIGQVAPQWKSIPYgMPLANQRFHVLDGRLEARPWWVPGELYIGGE--GLAREYWRDEPltaTRFIRHPRTGERLY 3016
Cdd:cd17634  397 FMITPLPGAIELKAGSAT-RPVFGVQPAVVDNEGHPQPGGTEGNLVITDPwpGQTRTLFGDHE---RFEQTYFSTFKGMY 472

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3017 RTGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPALSASVVVARGEPRGVRRLVAYAVPRSGQTPAAG-- 3094
Cdd:cd17634  473 FSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNHGVEPSPEly 552

                        490       500       510
                 ....*....|....*....|....*....|....
gi 53747904 3095 -ELRRYLAERLPAYMVPSAFVLLESLPRSRNGKI 3127
Cdd:cd17634  553 aELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
PRK12316 PRK12316
peptide synthase; Provisional
 2083-2642 2.45e-24

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 113.51  E-value: 2.45e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2083 PPSSLEQLIEQVWRKHLGVERVQPTDSFFQLGGDSLLGIQVAADLRRhLGVELPTATLFSHPTLAALAAALRARQGEAAA 2162
Cdd:PRK12316 3553 PVNELERRLAAIWADVLKLEQVGLTDNFFELGGDSIISLQVVSRARQ-AGIRFTPKDLFQHQTIQGLARVARVGGGVAVD 3631

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2163 PTAPAPALVPDPAARfEPFPLtDVQEAYWVGRRSAFELGGVaahgyfeiespgLEVERFIQCWRQLLQRHDMLRMVVLPD 2242
Cdd:PRK12316 3632 QGPVSGETLLLPIQQ-QFFEE-PVPERHHWNQSLLLKPREA------------LDAAALEAALQALVEHHDALRLRFVED 3697

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2243 GRQQVLEQVPeytpevVELRGLSPQEAESRRLQLRERMAHQVLRS---DRWPLFELVLCRY-EGGVRIHMSMDALMLDAW 2318
Cdd:PRK12316 3698 AGGWTAEHLP------VELGGALLWRAELDDAEELERLGEEAQRSldlADGPLLRALLATLaDGSQRLLLVIHHLVVDGV 3771

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2319 SSAVLRQDFAQLYH--EPGRP--LEPLAITFRDYVLAERRLREGEAHERARAYWWARLDTLPPPPELPLVKEPSQLEHAR 2394
Cdd:PRK12316 3772 SWRILLEDLQQAYQqlLQGEAprLPAKTSSFKAWAERLQEHARGEALKAELAYWQEQLQGVSSELPCDHPQGALQNRHAA 3851

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2395 ftHREARLEpHRWAR--LQERARAHGLTPSAACMAAFAEVLARWSRHPRFTLNLTLFQRLPLHPQVD--ELVGDFTSLVL 2470
Cdd:PRK12316 3852 --SVQTRLD-RELTRrlLQQAPAAYRTQVNDLLLTALARVVCRWTGEASALVQLEGHGREDLFADIDlsRTVGWFTSLFP 3928

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2471 LEVEAHAASTFAERASRLQAQLWRDLEHGsvsaVQLIRELVRTGRRSPGAIMPV---VFTSILSLDARRGPQGSLSFFEG 2547
Cdd:PRK12316 3929 VRLSPVEDLGASIKAIKEQLRAIPNKGIG----FGLLRYLGDEESRRTLAGLPVpriTFNYLGQFDGSFDEEMALFVPAG 4004

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2548 ELVYSiSQTPQV----WLDHGVHEEEGALVLAWDSVEALFPPGMVDDMFHAYQRLLGALAEE--EQAWEGELPELLPPAQ 2621
Cdd:PRK12316 4005 ESAGA-EQSPDApldnWLSLNGRVYGGELSLDWTFSREMFEEATIQRLADDYAAELTALVEHccDAERHGVTPSDFPLAG 4083

                         570       580
                  ....*....|....*....|.
gi 53747904  2622 relLARYNATQAPRPSGRLEE 2642
Cdd:PRK12316 4084 ---LDQARLDALPLPLGEIED 4101
PRK05952 PRK05952
beta-ketoacyl-ACP synthase;
106-431 3.13e-24

beta-ketoacyl-ACP synthase;


Pssm-ID: 235653 [Multi-domain]  Cd Length: 381  Bit Score: 107.83  E-value: 3.13e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   106 EALEDAGLRPdQLPGWvGVYVGAgDTSYRFQLLRGHGDPLSG--SKDVAGFFGN----YPDFLATRVAYKLNLRGPALGI 179
Cdd:PRK05952   66 AALKDAGLTP-PLTDC-GVVIGS-SRGCQGQWEKLARQMYQGddSPDEELDLENwldtLPHQAAIAAARQIGTQGPVLAP 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   180 HTACSTSLVSINMACSALRGFECDMALAGGVSLRLPARSGYLYEEGGVASKDGhCRPFDARATGTVTGDGVGVVVLKRLE 259
Cdd:PRK05952  143 MAACATGLWAIAQGVELIQTGQCQRVIAGAVEAPITPLTLAGFQQMGALAKTG-AYPFDRQREGLVLGEGGAILVLESAE 221

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   260 DALKARDPIHAVIRGWALNNDGASRagfTAPSVEGQSEVIALAH--AAAGISARDITYVEAHGTGTPLGDPIEVAALTRA 337
Cdd:PRK05952  222 LAQKRGAKIYGQILGFGLTCDAYHM---SAPEPDGKSAIAAIQQclARSGLTPEDIDYIHAHGTATRLNDQREANLIQAL 298

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   338 FRAHTADTAfcTLGAVksniGHLDAAAGVAGVIKTVQALRHRLIPPTLHFERPNPALHLEQSPffvNTQPLpwesprgpR 417
Cdd:PRK05952  299 FPHRVAVSS--TKGAT----GHTLGASGALGVAFSLLALRHQQLPPCVGLQEPEFDLNFVRQA---QQSPL--------Q 361

                         330
                  ....*....|....
gi 53747904   418 LAGVSSFGIGGTNA 431
Cdd:PRK05952  362 NVLCLSFGFGGQNA 375
SgcC5_NRPS-like cd19539
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ...
 2182-2604 1.34e-23

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: 107.08  E-value: 1.34e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2182 PLTDVQEAYWVGRrsAFELGGVAAH--GYFEIEsPGLEVERFIQCWRQLLQRHDMLRMVVLPDG----RQQVLEQVPEYT 2255
Cdd:cd19539    3 PLSFAQERLWFID--QGEDGGPAYNipGAWRLT-GPLDVEALREALRDVVARHEALRTLLVRDDggvpRQEILPPGPAPL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2256 PEVVELRGLSPQEAESRRLqLRERmAHQVLRSDRWPLFELVLCRYEGGvRIHMSMDA--LMLDAWSSAVLRQDFAQLY-- 2331
Cdd:cd19539   80 EVRDLSDPDSDRERRLEEL-LRER-ESRGFDLDEEPPIRAVLGRFDPD-DHVLVLVAhhTAFDAWSLDVFARDLAALYaa 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2332 --HEPGRPLEPLAITFRDYVLAERRLREGEAHERARAYWWARLDTLPPPPELPLVKEPSQLEhARFTHREARLEPHRWAR 2409
Cdd:cd19539  157 rrKGPAAPLPELRQQYKEYAAWQREALAAPRAAELLDFWRRRLRGAEPTALPTDRPRPAGFP-YPGADLRFELDAELVAA 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2410 LQERARAHGLTPSAACMAAFAEVLARWSRHPRFTLNLTLFQRlpLHPQVDELVGDFTSLVLLEVEAHAASTFAERASRLQ 2489
Cdd:cd19539  236 LRELAKRARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGR--NHPRFESTVGFFVNLLPLRVDVSDCATFRDLIARVR 313

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2490 AQLWRDLEHGSVSAVQLIREL--VRTGRRSPGAIMPVVFTSilSLDARRGPQGSLSFFEGELvysISQTPQVWLDHGVHE 2567
Cdd:cd19539  314 KALVDAQRHQELPFQQLVAELpvDRDAGRHPLVQIVFQVTN--APAGELELAGGLSYTEGSD---IPDGAKFDLNLTVTE 388

                        410       420       430
                 ....*....|....*....|....*....|....*..
gi 53747904 2568 EEGALVLAWDSVEALFPPGMVDDMFHAYQRLLGALAE 2604
Cdd:cd19539  389 EGTGLRGSLGYATSLFDEETIQGFLADYLQVLRQLLA 425
PRK09088 PRK09088
acyl-CoA synthetase; Validated
 2647-3134 1.44e-23

acyl-CoA synthetase; Validated


Pssm-ID: 181644 [Multi-domain]  Cd Length: 488  Bit Score: 107.59  E-value: 1.44e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2647 QARLHPELPAL--LAPERTLSYGELARRAQALAARLRELEVQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLDPEQPP 2724
Cdd:PRK09088    4 HARLQPQRLAAvdLALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2725 LRLHQLLEEGPARVVLTQSSLLHTVPWPPGVQVI--AVDELEPAtEAPPLPPrgtpEHLAYVIYTSGSTGKPKGVAIEHR 2802
Cdd:PRK09088   84 SELDALLQDAEPRLLLGDDAVAAGRTDVEDLAAFiaSADALEPA-DTPSIPP----ERVSLILFTSGTSGQPKGVMLSER 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2803 AALNTVVDLNTRFGVGPEDRVLGLSAL--TFDLSVYDVLGLLGAGGALVLPAAEAEKDPAhWWERLVAGrVTVWNSTPAL 2880
Cdd:PRK09088  159 NLQQTAHNFGVLGRVDAHSSFLCDAPMfhIIGLITSVRPVLAVGGSILVSNGFEPKRTLG-RLGDPALG-ITHYFCVPQM 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2881 MLLLveyAEQRGLKlPAALR-LVMLSGDWIPVALPDRIRALGRDVQVVSLGGATEA-SIWSIAYPIGQVAPQWKSIPYGM 2958
Cdd:PRK09088  237 AQAF---RAQPGFD-AAALRhLTALFTGGAPHAAEDILGWLDDGIPMVDGFGMSEAgTVFGMSVDCDVIRAKAGAAGIPT 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2959 PLANQRfhVLDGRLEARPWWVPGELYIGGEGLAREYWRDEPLTATRFirhprTGERLYRTGDQGRMLPEGSIEFLGREDL 3038
Cdd:PRK09088  313 PTVQTR--VVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAF-----TGDGWFRTGDIARRDADGFFWVVDRKKD 385

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  3039 QVKVQGFRVELGEIEAALAQHPALSASVVVARGEPRGVRRLVAYAVPRSGQTPAAGELRRYLAERLPAYMVPSAFVLLES 3118
Cdd:PRK09088  386 MFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAPLDLERIRSHLSTRLAKYKVPKHLRLVDA 465

                         490
                  ....*....|....*.
gi 53747904  3119 LPRSRNGKIARDQLPE 3134
Cdd:PRK09088  466 LPRTASGKLQKARLRD 481
OSB_MenE-like cd17630
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ...
 2781-3132 1.58e-23

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: 104.72  E-value: 1.58e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2781 LAYVIYTSGSTGKPKGVAIEHRAALNTVVDLNTRFGVGPEDRVLglsaLTFDLSVYDVLGLLGAGGALVLPAAEAEKDPA 2860
Cdd:cd17630    2 LATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWL----LSLPLYHVGGLAILVRSLLAGAELVLLERNQA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2861 HWwERLVAGRVTVWNSTPA-LMLLLVEYAEQRGLKlpaALRLVMLSGDWIPVALpdRIRALGRDVQVVSLGGATEASiws 2939
Cdd:cd17630   78 LA-EDLAPPGVTHVSLVPTqLQRLLDSGQGPAALK---SLRAVLLGGAPIPPEL--LERAADRGIPLYTTYGMTETA--- 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2940 iaypiGQVAPQwksiPYGMPLANQRFHVLDGRLEARPwwVPGELYIGGEGLAREYWRDEpltatrfIRHPRTGERLYRTG 3019
Cdd:cd17630  149 -----SQVATK----RPDGFGRGGVGVLLPGRELRIV--EDGEIWVGGASLAMGYLRGQ-------LVPEFNEDGWFTTK 210

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3020 DQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPALSASVVVARGEPRGVRRLVAYAVPRSGQTPAagELRRY 3099
Cdd:cd17630  211 DLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGPADPA--ELRAW 288

                        330       340       350
                 ....*....|....*....|....*....|...
gi 53747904 3100 LAERLPAYMVPSAFVLLESLPRSRNGKIARDQL 3132
Cdd:cd17630  289 LKDKLARFKLPKRIYPVPELPRTGGGKVDRRAL 321
PRK07910 PRK07910
beta-ketoacyl-ACP synthase;
12-435 2.54e-23

beta-ketoacyl-ACP synthase;


Pssm-ID: 236129 [Multi-domain]  Cd Length: 418  Bit Score: 105.97  E-value: 2.54e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904    12 SIALVGMAGRFPGAPDVESFWRNLVAGVESI-----SFFSEEELrqagvseqirrrPeyVPAKGVLedLELFDAGFFGYS 86
Cdd:PRK07910   13 NVVVTGIAMTTALATDAETTWKLLLDGQSGIrtlddPFVEEFDL------------P--VRIGGHL--LEEFDHQLTRVE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904    87 PREASHLdpqQRLLLECSWEALEDAG---LRPDQLPGWVGVYVGAGDT-SYRFQLLRGHG----DPLSgskdVAGFFGNY 158
Cdd:PRK07910   77 LRRMSYL---QRMSTVLGRRVWENAGspeVDTNRLMVSIGTGLGSAEElVFAYDDMRARGlravSPLA----VQMYMPNG 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   159 PdflATRVAYKLNLRGPALGIHTACSTSLVSINMACSALRGFECDMALAGGVSLRLPARS-GYLYEEGGVASKD-----G 232
Cdd:PRK07910  150 P---AAAVGLERHAKAGVITPVSACASGSEAIAQAWRQIVLGEADIAICGGVETRIEAVPiAGFAQMRIVMSTNnddpaG 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   233 HCRPFDaRATGTVTGDGVGVVVLKRLEDALKARD-PIHAVIRGWALNNDGASragFTAPSVEGQSEVIALAHAA--AGIS 309
Cdd:PRK07910  227 ACRPFD-KDRDGFVFGEGGALMVIETEEHAKARGaNILARIMGASITSDGFH---MVAPDPNGERAGHAMTRAIelAGLT 302

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   310 ARDITYVEAHGTGTPLGDPIEVAALTRAFRAHTAdtafcTLGAVKSNIGHLDAAAGVAGVIKTVQALRHRLIPPTLHFER 389
Cdd:PRK07910  303 PGDIDHVNAHATGTSVGDVAEGKAINNALGGHRP-----AVYAPKSALGHSVGAVGAVESILTVLALRDGVIPPTLNLEN 377

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 53747904   390 PNPALHLEqspfFVNTQPLPWESprgpRLAGVSSFGIGGTNAHTLF 435
Cdd:PRK07910  378 LDPEIDLD----VVAGEPRPGNY----RYAINNSFGFGGHNVALAF 415
antibiot_sagB TIGR03605
SagB-type dehydrogenase domain; SagB of Sterptococcus pyogenes participates in the maturation ...
 3299-3460 5.53e-23

SagB-type dehydrogenase domain; SagB of Sterptococcus pyogenes participates in the maturation of streptolysin S from a ribosomally produced precursor polypeptide. Chemically similar systems operate on highly diverse sets of bacteriocin precursors in numerous other bacteria. This model describes a domain within SgaB and homologous regions from other proteins, many of which appear to be involved in biosynthesis of secondary metabolites. While some substrates may be intermediates in non-ribosomal peptide syntheses, others are involved in heterocycle-containing bacteriocin biosynthesis, and can be found near SgaC-like (see TIGR03603, cyclodehydratase) and SgaD-like (see TIGR03604, "docking") proteins. Members of this domain family are heterogeneous in length, as many have a partial second copy of the domain represented here. The incomplete second domain scores below the cutoffs to this model in most cases.


Pssm-ID: 188352  Cd Length: 173  Bit Score: 98.53  E-value: 5.53e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   3299 EQLGRLL---APLREWEV----QGSRRYLYASAGGLYPVQLYLHLKpgRARGLEPGTWYYDPSTHRLVLLSAGAG-LDRR 3370
Cdd:TIGR03605    3 EELSQLLwysAGVRSIKLpyndGILFRRPYPSGGGLYPLEIYLYVK--NIEGLPDGVYHYDPEEHRLILIRAGEEnVDAF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   3371 IHDPHQNQAIFDSAAFSLFLIARMGAVEPVYAEHALHFATLEAGLMTQLLDLGAAPSGLGLCHIGDLDFAQARGLFHLE- 3449
Cdd:TIGR03605   81 LVNALLNAENANPPPVIIFITARFWKNFWKYGNRAYRLALLDVGIIIQNFYLVATALGLGSCAIGGFDDDYIAELLGLDg 160

                          170
                   ....*....|..
gi 53747904   3450 -EEHVLLHSLVG 3460
Cdd:TIGR03605  161 iEEHVVGVFPVG 172
Zn_ADH5 cd08259
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
 1676-1989 8.48e-23

Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. This group contains proteins that share the characteristic catalytic and structural zinc-binding sites of the zinc-dependent alcohol dehydrogenase family. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine (His-51), the ribose of NAD, a serine (Ser-48), then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176220 [Multi-domain]  Cd Length: 332  Bit Score: 102.78  E-value: 8.48e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1676 AVGTPGLLESLGLRRCTRPAPGPRQVEIEVEAAGLNFLDVLGALGMMPALEAEeSVLGRECSGRIAAVGEGVSGLRVGDE 1755
Cdd:cd08259    3 AAILHKPNKPLQIEEVPDPEPGPGEVLIKVKAAGVCYRDLLFWKGFFPRGKYP-LILGHEIVGTVEEVGEGVERFKPGDR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1756 VLAVA----------------------------PGCFRSYVLVDESQVVRRPASLGLAEGAAQMVPFATAYFALHtVGRL 1807
Cdd:cd08259   82 VILYYyipcgkceyclsgeenlcrnraeygeevDGGFAEYVKVPERSLVKLPDNVSDESAALAACVVGTAVHALK-RAGV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1808 RRGERILIHAAAGGLGLAAVQLASRTGAEILATAGSEQKREYLRSLGIAHVLDSRstSFVSEVRERTggrGVDVVLNSLA 1887
Cdd:cd08259  161 KKGDTVLVTGAGGGVGIHAIQLAKALGARVIAVTRSPEKLKILKELGADYVIDGS--KFSEDVKKLG---GADVVIELVG 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1888 GELLLAGLSVLAPHGRFLELGKRDlyaDQQVGLR---TLARGQTFAAidfgpHHPDFRAVLEEVATQLTQGQLEPLPTRL 1964
Cdd:cd08259  236 SPTIEESLRSLNKGGRLVLIGNVT---PDPAPLRpglLILKEIRIIG-----SISATKADVEEALKLVKEGKIKPVIDRV 307

                        330       340
                 ....*....|....*....|....*
gi 53747904 1965 FPARQVAEAFSFMARALHIGRVAVS 1989
Cdd:cd08259  308 VSLEDINEALEDLKSGKVVGRIVLK 332
Mgc45594_like cd08250
Mgc45594 gene product and other MDR family members; Includes Human Mgc45594 gene product of ...
 1684-1988 1.13e-22

Mgc45594 gene product and other MDR family members; Includes Human Mgc45594 gene product of undetermined function. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES.


Pssm-ID: 176212 [Multi-domain]  Cd Length: 329  Bit Score: 102.34  E-value: 1.13e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1684 ESLGLRRCTRPAPGPRQVEIEVEAAGLNFLDVLGALGMMPALEAEESVLGRECSGRIAAVGEGVSGLRVGDEVLAVAPGC 1763
Cdd:cd08250   16 EATSIVDVPVPLPGPGEVLVKNRFVGINASDINFTAGRYDPGVKPPFDCGFEGVGEVVAVGEGVTDFKVGDAVATMSFGA 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1764 FRSYVLVDESQVVRRPASLglAEGAAQMVPFATAYFALHTVGRLRRGERILIHAAAGGLGLAAVQLASRTGAEILATAGS 1843
Cdd:cd08250   96 FAEYQVVPARHAVPVPELK--PEVLPLLVSGLTASIALEEVGEMKSGETVLVTAAAGGTGQFAVQLAKLAGCHVIGTCSS 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1844 EQKREYLRSLGIAHVLDSRSTSfVSEVRERTGGRGVDVVLNSLAGELLLAGLSVLAPHGRFLELGKRDLYADQ------- 1916
Cdd:cd08250  174 DEKAEFLKSLGCDRPINYKTED-LGEVLKKEYPKGVDVVYESVGGEMFDTCVDNLALKGRLIVIGFISGYQSGtgpspvk 252

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 53747904 1917 --QVGLRTLARGQTFAAIdFGPHH-PDFRAVLEEVATQLTQGQLEPL--PTRLFPARQVAEAFSFMARALHIGRVAV 1988
Cdd:cd08250  253 gaTLPPKLLAKSASVRGF-FLPHYaKLIPQHLDRLLQLYQRGKLVCEvdPTRFRGLESVADAVDYLYSGKNIGKVVV 328
ttLC_FACS_AlkK_like cd12119
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
 2752-3127 1.61e-22

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: 105.02  E-value: 1.61e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2752 PPGVQVIAVDEL----EPATEAPPLPprgtpEHLAYVI-YTSGSTGKPKGVAIEHRAA-LNTVVDLNTR-FGVGPEDRVL 2824
Cdd:cd12119  136 PAGVGVLAYEELlaaeSPEYDWPDFD-----ENTAAAIcYTSGTTGNPKGVVYSHRSLvLHAMAALLTDgLGLSESDVVL 210

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2825 -----------GL---SALTFDLSVYdvlgllgaggalvlPAAEAekDPAHWWERLVAGRVTVWNSTPALMLLLVEYAEQ 2890
Cdd:cd12119  211 pvvpmfhvnawGLpyaAAMVGAKLVL--------------PGPYL--DPASLAELIEREGVTFAAGVPTVWQGLLDHLEA 274

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2891 RGLKLPaALRLVMLSGDWIPVALPDRIRALGrdVQVVSLGGATEASiwsiayPIGQVA---PQWKSIPY----------G 2957
Cdd:cd12119  275 NGRDLS-SLRRVVIGGSAVPRSLIEAFEERG--VRVIHAWGMTETS------PLGTVArppSEHSNLSEdeqlalrakqG 345

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2958 MPLANQRFHVLD-------------GRLEARPWWVPGElYIGGEGLAREYWRDEPLtatrfirhprtgerlyRTGDQGRM 3024
Cdd:cd12119  346 RPVPGVELRIVDddgrelpwdgkavGELQVRGPWVTKS-YYKNDEESEALTEDGWL----------------RTGDVATI 408

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3025 LPEGSIEFLGR-EDLqVKVQGFRVELGEIEAALAQHPALSASVVVARGEPRGVRRLVAYAVPRSGQTPAAGELRRYLAER 3103
Cdd:cd12119  409 DEDGYLTITDRsKDV-IKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEGATVTAEELLEFLADK 487

                        410       420
                 ....*....|....*....|....
gi 53747904 3104 LPAYMVPSAFVLLESLPRSRNGKI 3127
Cdd:cd12119  488 VAKWWLPDDVVFVDEIPKTSTGKI 511
KAsynt_C_assoc pfam16197
Ketoacyl-synthetase C-terminal extension; KAsynt_C_assoc represents the very C-terminus of a ...
 390-499 2.45e-22

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: 94.53  E-value: 2.45e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904    390 PNPALH-LEQSPFFVNTQPLPWesPRGprLAGVSSFGIGGTNAHTLFEEAPPPPASGPTRPN--QVLLLSARSTSALEHI 466
Cdd:pfam16197    1 PNPDIPaLLDGRLKVVTEPTPW--PGG--IVGVNSFGFGGANAHVILKSNPKPKIPPESPDNlpRLVLLSGRTEEAVKAL 76

                           90       100       110
                   ....*....|....*....|....*....|...
gi 53747904    467 AGRLAAHLRRHPDLELADVAFTLQvgRARFPYR 499
Cdd:pfam16197   77 LEKLENHLDDAEFLSLLNDIHSLP--ISGHPYR 107
hydroxyacyl_CoA_DH cd08254
6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, ...
 1694-1988 3.21e-22

6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, and other MDR family members; This group contains enzymes of the zinc-dependent alcohol dehydrogenase family, including members (aka MDR) identified as 6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase and N-benzyl-3-pyrrolidinol dehydrogenase. 6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase catalyzes the conversion of 6-Hydroxycyclohex-1-enecarbonyl-CoA and NAD+ to 6-Ketoxycyclohex-1-ene-1-carboxyl-CoA,NADH, and H+. This group displays the characteristic catalytic and structural zinc sites of the zinc-dependent alcohol dehydrogenases. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176216 [Multi-domain]  Cd Length: 338  Bit Score: 101.17  E-value: 3.21e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1694 PAPGPRQVEIEVEAAG-----LNFLDVLGalgmmPALEAEESVLGRECSGRIAAVGEGVSGLRVGDEVLAVAP------- 1761
Cdd:cd08254   22 PEPGPGEVLVKVKAAGvchsdLHILDGGV-----PTLTKLPLTLGHEIAGTVVEVGAGVTNFKVGDRVAVPAVipcgaca 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1762 ---------------------GCFRSYVLVDESQVVRRPASLGLAEGAAQMVPFATAYFALHTVGRLRRGERILI----- 1815
Cdd:cd08254   97 lcrrgrgnlclnqgmpglgidGGFAEYIVVPARALVPVPDGVPFAQAAVATDAVLTPYHAVVRAGEVKPGETVLViglgg 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1816 ---HaaagglglaAVQLASRTGAEILATAGSEQKREYLRSLGIAHVLDSRSTSFVSEVrERTGGRGVDVVLN-SLAGELL 1891
Cdd:cd08254  177 lglN---------AVQIAKAMGAAVIAVDIKEEKLELAKELGADEVLNSLDDSPKDKK-AAGLGGGFDVIFDfVGTQPTF 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1892 LAGLSVLAPHGRFLELGkrdlYADQQVGLRT--LARGQTFAAIDFGPHHPDFRAVLEEVAtqltQGQLEPLPTRLfPARQ 1969
Cdd:cd08254  247 EDAQKAVKPGGRIVVVG----LGRDKLTVDLsdLIARELRIIGSFGGTPEDLPEVLDLIA----KGKLDPQVETR-PLDE 317

                        330
                 ....*....|....*....
gi 53747904 1970 VAEAFSFMARALHIGRVAV 1988
Cdd:cd08254  318 IPEVLERLHKGKVKGRVVL 336
MACS_like_3 cd05971
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
 2682-3132 4.35e-22

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: 102.51  E-value: 4.35e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2682 ELEVQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLDPEQPPLRLHQLLEEGPARVVLTQSSllhtvpwppgvqviavD 2761
Cdd:cd05971   25 EIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVTDGS----------------D 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2762 ELepateapplpprgtpehlAYVIYTSGSTGKPKGVAIEHRAALNTVVDLNTRFGVGPEDRVL-----------GLsalt 2830
Cdd:cd05971   89 DP------------------ALIIYTSGTTGPPKGALHAHRVLLGHLPGVQFPFNLFPRDGDLywtpadwawigGL---- 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2831 FDLSVydvlgllgaggalvlPAaeaekdpAHWWERLVAGRVTVWnSTPALMLLLVEYAEQRGLKLPAALRLVMLSGDwiP 2910
Cdd:cd05971  147 LDVLL---------------PS-------LYFGVPVLAHRMTKF-DPKAALDLMSRYGVTTAFLPPTALKMMRQQGE--Q 201

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2911 VALPD-RIRAL---GRDVQVVSLGGATEASIWSIAYPIGQV--------APQWKSI---PYGMPLANQRFHVLDGRLEAR 2975
Cdd:cd05971  202 LKHAQvKLRAIatgGESLGEELLGWAREQFGVEVNEFYGQTecnlvignCSALFPIkpgSMGKPIPGHRVAIVDDNGTPL 281

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2976 PwwvPGElyIGGEGLAR-------EYWRDEPLTATRFIrhprtGERLyRTGDQGRMLPEGSIEFLGREDLQVKVQGFRVE 3048
Cdd:cd05971  282 P---PGE--VGEIAVELpdpvaflGYWNNPSATEKKMA-----GDWL-LTGDLGRKDSDGYFWYVGRDDDVITSSGYRIG 350

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3049 LGEIEAALAQHPALSASVVVARGEPRGVRRLVAYAVPRSGQTPA---AGELRRYLAERLPAYMVPSAFVLLESLPRSRNG 3125
Cdd:cd05971  351 PAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPSdalAREIQELVKTRLAAHEYPREIEFVNELPRTATG 430


                 ....*..
gi 53747904 3126 KIARDQL 3132
Cdd:cd05971  431 KIRRREL 437
MACS_like cd05972
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ...
 2779-3132 1.28e-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: 100.87  E-value: 1.28e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2779 EHLAYVIYTSGSTGKPKGVAIEHRAALNTVVDLNTRFGVGPEDRVLGLSALTFDLSVYDVLGLLGAGGALVLPAAEAEKD 2858
Cdd:cd05972   81 EDPALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRPDDIHWNIADPGWAKGAWSSFFGPWLLGATVFVYEGPRFD 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2859 PAHWWERLVAGRVTVWNSTP-ALMLLLVEYAEQRGLKlpaALRLVMLSGDWI-PVALPDRIRALGRDVQvvSLGGATEAS 2936
Cdd:cd05972  161 AERILELLERYGVTSFCGPPtAYRMLIKQDLSSYKFS---HLRLVVSAGEPLnPEVIEWWRAATGLPIR--DGYGQTETG 235

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2937 IWSIAYPIGQVAPqwKSIpyGMPLANQRFHVLDGRLEARPWWVPGELYI--GGEGLAREYWRDEPLTATRFirhprtGER 3014
Cdd:cd05972  236 LTVGNFPDMPVKP--GSM--GRPTPGYDVAIIDDDGRELPPGEEGDIAIklPPPGLFLGYVGDPEKTEASI------RGD 305

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3015 LYRTGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPALSASVVVARGEPrgVRRLV--AYAVPRSGQTPA 3092
Cdd:cd05972  306 YYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDP--VRGEVvkAFVVLTSGYEPS 383

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 53747904 3093 ---AGELRRYLAERLPAYMVPSAFVLLESLPRSRNGKIARDQL 3132
Cdd:cd05972  384 eelAEELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRVEL 426
LCL_NRPS-like cd19531
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ...
 2216-2605 2.32e-21

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: 100.12  E-value: 2.32e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2216 LEVERFIQCWRQLLQRHDMLRMV-VLPDG--RQQVLEQVPeYTPEVVELRGLSPQEAESRrlqLRERMAHQVLRS---DR 2289
Cdd:cd19531   36 LDVAALERALNELVARHEALRTTfVEVDGepVQVILPPLP-LPLPVVDLSGLPEAEREAE---AQRLAREEARRPfdlAR 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2290 WPLFELVLcryeggVRI----HmsmdALML-------DAWSSAVLRQDFAQLY----HEPGRPLEPLAITFRDYVLAERR 2354
Cdd:cd19531  112 GPLLRATL------LRLgedeH----VLLLtmhhivsDGWSMGVLLRELAALYaaflAGRPSPLPPLPIQYADYAVWQRE 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2355 LREGEAHERARAYWWARLDTlppppelplvkEPSQLE-------HARFTHREAR----LEPHRWARLQERARAHGLTPSA 2423
Cdd:cd19531  182 WLQGEVLERQLAYWREQLAG-----------APPVLElptdrprPAVQSFRGARvrftLPAELTAALRALARREGATLFM 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2424 ACMAAFAEVLARWS-------------RHprftlnltlfqrlplHPQVDELVGDFTSLVLLEVEAHAASTFAE-----RA 2485
Cdd:cd19531  251 TLLAAFQVLLHRYSgqddivvgtpvagRN---------------RAELEGLIGFFVNTLVLRTDLSGDPTFREllarvRE 315

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2486 SRLQAQlwrdlEHGSVSAVQLIREL--VRTGRRSPgaimpvVFTSILSLDARRGPQGSLSFFEGELVYSISQTPQVWLDH 2563
Cdd:cd19531  316 TALEAY-----AHQDLPFEKLVEALqpERDLSRSP------LFQVMFVLQNAPAAALELPGLTVEPLEVDSGTAKFDLTL 384

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|..
gi 53747904 2564 GVHEEEGALVLAWDSVEALFPPGMVDDMFHAYQRLLGALAEE 2605
Cdd:cd19531  385 SLTETDGGLRGSLEYNTDLFDAATIERMAGHFQTLLEAIVAD 426
FACL_like_1 cd05910
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 2782-3132 2.45e-21

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: 100.61  E-value: 2.45e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2782 AYVIYTSGSTGKPKGVAIEHRAALNTVVDLNTRFGVGPEDRVLGlsalTFDL-SVYDVLGLLGAGGALVLPAAEAEKDPA 2860
Cdd:cd05910   88 AAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEVDLA----TFPLfALFGPALGLTSVIPDMDPTRPARADPQ 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2861 HWWERLVAGRVTVWNSTPALMLLLVEYAEQRGLKLPaALRLVMLSGDWIPVALPDRIR-ALGRDVQVVSLGGATEA-SIW 2938
Cdd:cd05910  164 KLVGAIRQYGVSIVFGSPALLERVARYCAQHGITLP-SLRRVLSAGAPVPIALAARLRkMLSDEAEILTPYGATEAlPVS 242

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2939 SIA-----YPIGQVAPQWKSIPYGMPLANQRFHVL----------DGRLEArPWWVPGELYIGGEGLAREYWRDEplTAT 3003
Cdd:cd05910  243 SIGsrellATTTAATSGGAGTCVGRPIPGVRVRIIeiddepiaewDDTLEL-PRGEIGEITVTGPTVTPTYVNRP--VAT 319

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3004 RFIRHPRTGER-LYRTGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPALSASVVVARGEPRGVRRLVAY 3082
Cdd:cd05910  320 ALAKIDDNSEGfWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGVGKPGCQLPVLCV 399

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 53747904 3083 AVPRSGQTPAAGELR--RYLAERLPAYMVPSAFVLLESLPRS--RNGKIARDQL 3132
Cdd:cd05910  400 EPLPGTITPRARLEQelRALAKDYPHTQRIGRFLIHPSFPVDirHNAKIFREKL 453
PRK07787 PRK07787
acyl-CoA synthetase; Validated
 2655-3132 3.16e-21

acyl-CoA synthetase; Validated


Pssm-ID: 236096 [Multi-domain]  Cd Length: 471  Bit Score: 100.45  E-value: 3.16e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2655 PALLAPERTLSYGELARRAQALAArlrelEVQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLDPEQPPLRLHQLLEEG 2734
Cdd:PRK07787   17 DAVRIGGRVLSRSDLAGAATAVAE-----RVAGARRVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILADS 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2735 PARVVLTQssllhtVPW-PPGVQVIAVDELEPATEAPPLPPrgtPEHLAYVIYTSGSTGKPKGVAIEHRAALNTVVDLNT 2813
Cdd:PRK07787   92 GAQAWLGP------APDdPAGLPHVPVRLHARSWHRYPEPD---PDAPALIVYTSGTTGPPKGVVLSRRAIAADLDALAE 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2814 RFGVGPEDR-------------VLG-LSALTFDLSVydvlgllgAGGALVLPAAEAEKDPAHwwERLVAGRVTVWNSTPA 2879
Cdd:PRK07787  163 AWQWTADDVlvhglplfhvhglVLGvLGPLRIGNRF--------VHTGRPTPEAYAQALSEG--GTLYFGVPTVWSRIAA 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2880 lmlllvEYAEQRGLKlPAALrLVMLSGDwIPVALPDRIRAL-GRdvQVVSLGGATEASIWSIAYPIGQVAPQWksipYGM 2958
Cdd:PRK07787  233 ------DPEAARALR-GARL-LVSGSAA-LPVPVFDRLAALtGH--RPVERYGMTETLITLSTRADGERRPGW----VGL 297

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2959 PLANQRFHVLDGRLEARPWWVP--GELYIGGEGLAREYWRDEPLTATRFirhprTGERLYRTGDQGRMLPEGSIEFLGRE 3036
Cdd:PRK07787  298 PLAGVETRLVDEDGGPVPHDGEtvGELQVRGPTLFDGYLNRPDATAAAF-----TADGWFRTGDVAVVDPDGMHRIVGRE 372

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  3037 --DLqVKVQGFRVELGEIEAALAQHPALSASVVVARGEPRGVRRLVAYAVPRSGqtPAAGELRRYLAERLPAYMVPSAFV 3114
Cdd:PRK07787  373 stDL-IKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGADD--VAADELIDFVAQQLSVHKRPREVR 449

                         490
                  ....*....|....*...
gi 53747904  3115 LLESLPRSRNGKIARDQL 3132
Cdd:PRK07787  450 FVDALPRNAMGKVLKKQL 467
MDR9 cd08274
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 1692-1988 4.97e-21

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176235 [Multi-domain]  Cd Length: 350  Bit Score: 97.75  E-value: 4.97e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1692 TRPAPGPRQVEIEVEAAGLNFLDV---LGALG--MMPALEAEESVL--------------GRECSGRIAAVGEGVSGLRV 1752
Cdd:cd08274   22 PVPTPAPGEVLIRVGACGVNNTDIntrEGWYSteVDGATDSTGAGEagwwggtlsfpriqGADIVGRVVAVGEGVDTARI 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1753 GDEVLaVAP---------------------GCFRSYVLVDESQVVRRPASLGLAEGAAQMVPFATAYFALHTvGRLRRGE 1811
Cdd:cd08274  102 GERVL-VDPsirdppeddpadidyigserdGGFAEYTVVPAENAYPVNSPLSDVELATFPCSYSTAENMLER-AGVGAGE 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1812 RILIHAAAGGLGLAAVQLASRTGAEILATAGSEqKREYLRSLGiAHVLDSRSTSFVSEVRErTGGRGVDVVLNSLAGELL 1891
Cdd:cd08274  180 TVLVTGASGGVGSALVQLAKRRGAIVIAVAGAA-KEEAVRALG-ADTVILRDAPLLADAKA-LGGEPVDVVADVVGGPLF 256

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1892 LAGLSVLAPHGRF----------LELGKRDLYadqqvgLRTLargqTFAAIDFGPhhpdfRAVLEEVATQLTQGQLEPLP 1961
Cdd:cd08274  257 PDLLRLLRPGGRYvtagaiagpvVELDLRTLY------LKDL----TLFGSTLGT-----REVFRRLVRYIEEGEIRPVV 321

                        330       340
                 ....*....|....*....|....*..
gi 53747904 1962 TRLFPARQVAEAFSFMARALHIGRVAV 1988
Cdd:cd08274  322 AKTFPLSEIREAQAEFLEKRHVGKLVL 348
PRK13383 PRK13383
acyl-CoA synthetase; Provisional
 2652-3133 5.09e-21

acyl-CoA synthetase; Provisional


Pssm-ID: 139531 [Multi-domain]  Cd Length: 516  Bit Score: 100.07  E-value: 5.09e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2652 PELPALLAPERTLSYGELARRAQALAARLRELEVQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLDPEQPPLRLHQLL 2731
Cdd:PRK13383   49 PGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAAL 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2732 EEGPARVVLTQSSLLHtvpwppgvQVIAVDE----LEPAT----EAPPLPPRGTPEHLayVIYTSGSTGKPKGV--AIEH 2801
Cdd:PRK13383  129 RAHHISTVVADNEFAE--------RIAGADDavavIDPATagaeESGGRPAVAAPGRI--VLLTSGTTGKPKGVprAPQL 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2802 RAALNTVVDL--NTRFGVG-------PEDRVLGLSALTFDLSVydvlGLLGAGGALVLPAAEAEKDPAHwwerlvagRVT 2872
Cdd:PRK13383  199 RSAVGVWVTIldRTRLRTGsrisvamPMFHGLGLGMLMLTIAL----GGTVLTHRHFDAEAALAQASLH--------RAD 266

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2873 VWNSTPALMLLLVEYAEQRGLKLP-AALRLVMLSGDWIPVALPDRIRALGRDVqVVSLGGATEASIWSIAYPIG-QVAPQ 2950
Cdd:PRK13383  267 AFTAVPVVLARILELPPRVRARNPlPQLRVVMSSGDRLDPTLGQRFMDTYGDI-LYNGYGSTEVGIGALATPADlRDAPE 345

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2951 wksiPYGMPLANQRFHVLDGRLEARPWWVPGELYIGGEgLAREYWRDEPLTATRfirhprtgERLYRTGDQGRMLPEGSI 3030
Cdd:PRK13383  346 ----TVGKPVAGCPVRILDRNNRPVGPRVTGRIFVGGE-LAGTRYTDGGGKAVV--------DGMTSTGDMGYLDNAGRL 412

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  3031 EFLGREDLQVKVQGFRVELGEIEAALAQHPALSASVVVARGEPRGVRRLVAYAVPRSGQTPAAGELRRYLAERLPAYMVP 3110
Cdd:PRK13383  413 FIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSGVDAAQLRDYLKDRVSRFEQP 492

                         490       500
                  ....*....|....*....|...
gi 53747904  3111 SAFVLLESLPRSRNGKIARDQLP 3133
Cdd:PRK13383  493 RDINIVSSIPRNPTGKVLRKELP 515
Zn_ADH9 cd08269
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR) ...
 1679-1980 5.30e-21

Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability.


Pssm-ID: 176230 [Multi-domain]  Cd Length: 312  Bit Score: 96.66  E-value: 5.30e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1679 TPGLLEslgLRRCTRPAPGPRQVEIEVEAAGL--NFLDVLGALGMMPALEAEESVLGRECSGRIAAVGEGVSGLRVGDEV 1756
Cdd:cd08269    3 GPGRFE---VEEHPRPTPGPGQVLVRVEGCGVcgSDLPAFNQGRPWFVYPAEPGGPGHEGWGRVVALGPGVRGLAVGDRV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1757 LAVAPGCFRSYVLVDESQVVRRPASLGLAEGAAQmvPFATAYFALHtVGRLRRGERILIhAAAGGLGLAAVQLASRTGAE 1836
Cdd:cd08269   80 AGLSGGAFAEYDLADADHAVPLPSLLDGQAFPGE--PLGCALNVFR-RGWIRAGKTVAV-IGAGFIGLLFLQLAAAAGAR 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1837 ILATAGSEQKREYL-RSLGIAHVLDSRSTSFVSEVRERTGGRGVDVVLNSLAGELLLAGLSVL-APHGRFLELG-KRDLY 1913
Cdd:cd08269  156 RVIAIDRRPARLALaRELGATEVVTDDSEAIVERVRELTGGAGADVVIEAVGHQWPLDLAGELvAERGRLVIFGyHQDGP 235

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1914 AdqQVGLRTL-ARGQTFAAIDFGPHHPDFRAVLEEVATqLTQGQLEP--LPTRLFPARQVAEAFSFMARA 1980
Cdd:cd08269  236 R--PVPFQTWnWKGIDLINAVERDPRIGLEGMREAVKL-IADGRLDLgsLLTHEFPLEELGDAFEAARRR 302
quinone_oxidoreductase_like_1 cd08243
Quinone oxidoreductase (QOR); NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
 1675-1977 9.64e-21

Quinone oxidoreductase (QOR); NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. The medium chain alcohol dehydrogenase family (MDR) have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.


Pssm-ID: 176205 [Multi-domain]  Cd Length: 320  Bit Score: 96.14  E-value: 9.64e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1675 VAVGTPGLLESLGLRRCTRPAPGPRQVEIEVEAAGLNFLDVLGALGMMPALEAEEsVLGRECSGRIAAVGEGvsGLRVGD 1754
Cdd:cd08243    4 IVIEQPGGPEVLKLREIPIPEPKPGWVLIRVKAFGLNRSEIFTRQGHSPSVKFPR-VLGIEAVGEVEEAPGG--TFTPGQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1755 EVLAVAPGCFRS-------YVLVDESQVVRRPASLGLAEGAAQMVPFATAYFALHTVGRLRRGERILIHAAAGGLGLAAV 1827
Cdd:cd08243   81 RVATAMGGMGRTfdgsyaeYTLVPNEQVYAIDSDLSWAELAALPETYYTAWGSLFRSLGLQPGDTLLIRGGTSSVGLAAL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1828 QLASRTGAEILATAGSEQKREYLRSLGIAHV-LDSRSTSfvSEVRERTGgrGVDVVLNSLAGELLLAGLSVLAPHGRFL- 1905
Cdd:cd08243  161 KLAKALGATVTATTRSPERAALLKELGADEVvIDDGAIA--EQLRAAPG--GFDKVLELVGTATLKDSLRHLRPGGIVCm 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1906 --ELGkrdlyadqqvGLRTLARGQTFAAID-------FGPHHPDFRA-VLEEVATQLTQGQLEPLPTRLFPARQVAEAFS 1975
Cdd:cd08243  237 tgLLG----------GQWTLEDFNPMDDIPsgvnltlTGSSSGDVPQtPLQELFDFVAAGHLDIPPSKVFTFDEIVEAHA 306


                 ..
gi 53747904 1976 FM 1977
Cdd:cd08243  307 YM 308
Zn_ADH6 cd08260
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
 1684-1988 2.14e-20

Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. This group has the characteristic catalytic and structural zinc sites of the zinc-dependent alcohol dehydrogenases. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176221 [Multi-domain]  Cd Length: 345  Bit Score: 95.75  E-value: 2.14e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1684 ESLGLRRCTRPAPGPRQVEIEVEAAGLNFLDVLGALGMmPALEAEESVLGRECSGRIAAVGEGVSGLRVGDEVLA----- 1758
Cdd:cd08260   11 EPLEIREVPDPEPPPDGVVVEVEACGVCRSDWHGWQGH-DPDVTLPHVPGHEFAGVVVEVGEDVSRWRVGDRVTVpfvlg 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1759 -----------------------VAPGCFRSYVLVDESQV--VRRPASLGLAEGAAQMVPFATAYFALHTVGRLRRGERI 1813
Cdd:cd08260   90 cgtcpycragdsnvcehqvqpgfTHPGSFAEYVAVPRADVnlVRLPDDVDFVTAAGLGCRFATAFRALVHQARVKPGEWV 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1814 LIHaAAGGLGLAAVQLASRTGAEILATAGSEQKREYLRSLGIAHVLDSR-STSFVSEVRERTGGrGVDVVLNSlAGELLL 1892
Cdd:cd08260  170 AVH-GCGGVGLSAVMIASALGARVIAVDIDDDKLELARELGAVATVNASeVEDVAAAVRDLTGG-GAHVSVDA-LGIPET 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1893 AGLSV--LAPHGRFLelgkrdlyadqQVGLRTLARGQTFAAIDF---------GPH---HPDFRAVLEEVATqlTQGQLE 1958
Cdd:cd08260  247 CRNSVasLRKRGRHV-----------QVGLTLGEEAGVALPMDRvvareleivGSHgmpAHRYDAMLALIAS--GKLDPE 313

                        330       340       350
                 ....*....|....*....|....*....|
gi 53747904 1959 PLPTRLFPARQVAEAFSFMARALHIGRVAV 1988
Cdd:cd08260  314 PLVGRTISLDEAPDALAAMDDYATAGITVI 343
PRK04319 PRK04319
acetyl-CoA synthetase; Provisional
 2660-3129 2.45e-20

acetyl-CoA synthetase; Provisional


Pssm-ID: 235279 [Multi-domain]  Cd Length: 570  Bit Score: 98.43  E-value: 2.45e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2660 PERTLSYGELARRAQALAARLRELEVQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLDPEQPPLRLHQLLEEGPARVV 2739
Cdd:PRK04319   70 RKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVL 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2740 LTQSSLLHTVPWP--PGVQ-VIAVDE--------------LEPATEAPPLPPrGTPEHLAYVIYTSGSTGKPKGV----- 2797
Cdd:PRK04319  150 ITTPALLERKPADdlPSLKhVLLVGEdveegpgtldfnalMEQASDEFDIEW-TDREDGAILHYTSGSTGKPKGVlhvhn 228

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2798 -AIEHRAALNTVVDLNtrfgvgPEDR---------VLGLSALTFD------LSVYDvlgllgaggalvlpaaEAEKDPAH 2861
Cdd:PRK04319  229 aMLQHYQTGKYVLDLH------EDDVywctadpgwVTGTSYGIFApwlngaTNVID----------------GGRFSPER 286

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2862 WWERLVAGRVTVWNSTPA----LMLLLVEYAEQRGLklpAALRLVMLSGDwiPVAlPDRIRaLGRDVqvvsLG------- 2930
Cdd:PRK04319  287 WYRILEDYKVTVWYTAPTairmLMGAGDDLVKKYDL---SSLRHILSVGE--PLN-PEVVR-WGMKV----FGlpihdnw 355

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2931 GATEASIWSIA-YPIGQVAPqwKSIpyGMPLANQRFHVLDGRLEARPWWVPGELYI--GGEGLAREYWRDEPltatRFIR 3007
Cdd:PRK04319  356 WMTETGGIMIAnYPAMDIKP--GSM--GKPLPGIEAAIVDDQGNELPPNRMGNLAIkkGWPSMMRGIWNNPE----KYES 427

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  3008 HPRTGerLYRTGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPALSASVVVarGEPRGVR--RLVAYAVP 3085
Cdd:PRK04319  428 YFAGD--WYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVI--GKPDPVRgeIIKAFVAL 503

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*..
gi 53747904  3086 RSGQTPA---AGELRRYLAERLPAYMVPSAFVLLESLPRSRNGKIAR 3129
Cdd:PRK04319  504 RPGYEPSeelKEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMR 550
PRK06178 PRK06178
acyl-CoA synthetase; Validated
 2648-3132 3.02e-20

acyl-CoA synthetase; Validated


Pssm-ID: 235724 [Multi-domain]  Cd Length: 567  Bit Score: 98.19  E-value: 3.02e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2648 ARLHPELPALLAPERTLSYGELARRAQALAARLRELEVQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLDPEQPPLRL 2727
Cdd:PRK06178   43 ARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHEL 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2728 HQLLEEGPARVVLTQSSLLH---------------------------TVPWPPGVQ--------VIAVDELEPATEAPPL 2772
Cdd:PRK06178  123 SYELNDAGAEVLLALDQLAPvveqvraetslrhvivtsladvlpaepTLPLPDSLRaprlaaagAIDLLPALRACTAPVP 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2773 PPRGTPEHLAYVIYTSGSTGKPKGVAIEHR-----AALNTVVDLntrfgVGPEDRV--------------LGL-----SA 2828
Cdd:PRK06178  203 LPPPALDALAALNYTGGTTGMPKGCEHTQRdmvytAAAAYAVAV-----VGGEDSVflsflpefwiagenFGLlfplfSG 277

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2829 LTFDLSvydvlgllgaggalvlpaaeaekdpAHWWERLVAGRVTVWNSTPALMLL--LVEYAEQRGLKLP--AALRLVML 2904
Cdd:PRK06178  278 ATLVLL-------------------------ARWDAVAFMAAVERYRVTRTVMLVdnAVELMDHPRFAEYdlSSLRQVRV 332

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2905 SgDWIPVALPD---RIRALGRDVQVVSLGGATE---ASIWSIAYPIGQVAPQWKSIPYGMPLANQRFHVLD---GRLeaR 2975
Cdd:PRK06178  333 V-SFVKKLNPDyrqRWRALTGSVLAEAAWGMTEthtCDTFTAGFQDDDFDLLSQPVFVGLPVPGTEFKICDfetGEL--L 409

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2976 PWWVPGELYIGGEGLAREYWRDEPLTATRFirhpRTGerLYRTGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAA 3055
Cdd:PRK06178  410 PLGAEGEIVVRTPSLLKGYWNKPEATAEAL----RDG--WLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEAL 483

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 53747904  3056 LAQHPALSASVVVARGEPRGVRRLVAYAVPRSGQTPAAGELRRYLAERLPAYMVPSAFVlLESLPRSRNGKIARDQL 3132
Cdd:PRK06178  484 LGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGADLTAAALQAWCRENMAVYKVPEIRI-VDALPMTATGKVRKQDL 559
PRK07798 PRK07798
acyl-CoA synthetase; Validated
 2652-3126 3.42e-20

acyl-CoA synthetase; Validated


Pssm-ID: 236100 [Multi-domain]  Cd Length: 533  Bit Score: 97.65  E-value: 3.42e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2652 PELPALLAPERTLSYGELARRAQALAARLRELEVQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLDPEQPPLRLHQLL 2731
Cdd:PRK07798   17 PDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLL 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2732 EEGPARVVLTQSSLLHTV----PWPPGVQVI--------------AVDELEPATEAPPLPPRGT--PEHLaYVIYTSGST 2791
Cdd:PRK07798   97 DDSDAVALVYEREFAPRVaevlPRLPKLRTLvvvedgsgndllpgAVDYEDALAAGSPERDFGErsPDDL-YLLYTGGTT 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2792 GKPKGVAIEH----RAALN-----------TVVDLNTRFGVGPEDRVL-------------GLSALTFDLSV--YDvlgl 2841
Cdd:PRK07798  176 GMPKGVMWRQedifRVLLGgrdfatgepieDEEELAKRAAAGPGMRRFpapplmhgagqwaAFAALFSGQTVvlLP---- 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2842 lgaggalvlpaaEAEKDPAHWWERLVAGRVTVWNSTPALML--LLVEYAEQRGLKLPAaLRLVMLSGDWIPVALPDRIRA 2919
Cdd:PRK07798  252 ------------DVRFDADEVWRTIEREKVNVITIVGDAMArpLLDALEARGPYDLSS-LFAIASGGALFSPSVKEALLE 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2920 LGRDVQVVSLGGATEASIWSIAYpigqVAPqwKSIPYGMPL--ANQRFHVLDgrlEARPWWVPGElyiGGEG-LARE--- 2993
Cdd:PRK07798  319 LLPNVVLTDSIGSSETGFGGSGT----VAK--GAVHTGGPRftIGPRTVVLD---EDGNPVEPGS---GEIGwIARRghi 386

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2994 ---YWRDEPLTATRFIRHprTGERLYRTGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPALSASVVVAR 3070
Cdd:PRK07798  387 plgYYKDPEKTAETFPTI--DGVRYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGV 464

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 53747904  3071 GEPRGVRRLVAYAVPRSGQTPAAGELRRYLAERLPAYMVPSAFVLLESLPRSRNGK 3126
Cdd:PRK07798  465 PDERWGQEVVAVVQLREGARPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
 2209-2438 4.10e-20

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: 96.12  E-value: 4.10e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2209 FEIESPgLEVERFIQCWRQLLQRHDMLRMVVLPDGRQQ----VLEQVPeyTP-EVVELRGLSPQEAESRRLQLRERMAHQ 2283
Cdd:cd19543   30 ITLEGP-LDPDRFRAAWQAVVDRHPILRTSFVWEGLGEplqvVLKDRK--LPwRELDLSHLSEAEQEAELEALAEEDRER 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2284 VLRSDRWPLFELVLCRYEGG-VRIHMSMDALMLDAWSSAVLRQDFAQLYHEP--GRPLE-PLAITFRDYV--LAERRlre 2357
Cdd:cd19543  107 GFDLARAPLMRLTLIRLGDDrYRLVWSFHHILLDGWSLPILLKELFAIYAALgeGQPPSlPPVRPYRDYIawLQRQD--- 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2358 geaHERARAYWWARLDTLPPPPELPLVKEPSQLEHARFTHREARLEPHRWARLQERARAHGLTPSAACMAAFAEVLARWS 2437
Cdd:cd19543  184 ---KEAAEAYWREYLAGFEEPTPLPKELPADADGSYEPGEVSFELSAELTARLQELARQHGVTLNTVVQGAWALLLSRYS 260


                 .
gi 53747904 2438 R 2438
Cdd:cd19543  261 G 261
PRK03640 PRK03640
o-succinylbenzoate--CoA ligase;
2647-3132 4.37e-20

o-succinylbenzoate--CoA ligase;


Pssm-ID: 235146 [Multi-domain]  Cd Length: 483  Bit Score: 96.96  E-value: 4.37e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2647 QARLHPELPALLAPERTLSYGELARRAQALAARLRELEVQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLDPEQPPLR 2726
Cdd:PRK03640   11 RAFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREE 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2727 LHQLLEEGPARVVLTQSSLLHTVpwpPGVQVIAVDELEPATEAPPLPPrgTPEHL---AYVIYTSGSTGKPKGV------ 2797
Cdd:PRK03640   91 LLWQLDDAEVKCLITDDDFEAKL---IPGISVKFAELMNGPKEEAEIQ--EEFDLdevATIMYTSGTTGKPKGViqtygn 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2798 ----AIEhrAALNtvvdlntrFGVGPEDRVL---------GLSAL----TFDLSVYdvlgllgaggalVLPAAEAEKdpA 2860
Cdd:PRK03640  166 hwwsAVG--SALN--------LGLTEDDCWLaavpifhisGLSILmrsvIYGMRVV------------LVEKFDAEK--I 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2861 HWWerLVAGRVTVWnSTPALML--LLVEYAEQRglkLPAALRLVMLSGDWIPVALPDRIRAlgRDVQVVSLGGATEASIW 2938
Cdd:PRK03640  222 NKL--LQTGGVTII-SVVSTMLqrLLERLGEGT---YPSSFRCMLLGGGPAPKPLLEQCKE--KGIPVYQSYGMTETASQ 293

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2939 SIAYP-------IGQVapqwksipyGMPLANQRFHVLDGRLEARPwWVPGELYIGGEGLAREYWRDEPLTATRFirhpRT 3011
Cdd:PRK03640  294 IVTLSpedaltkLGSA---------GKPLFPCELKIEKDGVVVPP-FEEGEIVVKGPNVTKGYLNREDATRETF----QD 359

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  3012 GerLYRTGDQGRMLPEGSIEFLGRE-DLQVKvQGFRVELGEIEAALAQHPALSASVVVarGEPRGVRRLVAYAVPRSGQT 3090
Cdd:PRK03640  360 G--WFKTGDIGYLDEEGFLYVLDRRsDLIIS-GGENIYPAEIEEVLLSHPGVAEAGVV--GVPDDKWGQVPVAFVVKSGE 434

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|..
gi 53747904  3091 PAAGELRRYLAERLPAYMVPSAFVLLESLPRSRNGKIARDQL 3132
Cdd:PRK03640  435 VTEEELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHEL 476
sugar_DH cd08236
NAD(P)-dependent sugar dehydrogenases; This group contains proteins identified as sorbitol ...
 1693-1979 6.39e-20

NAD(P)-dependent sugar dehydrogenases; This group contains proteins identified as sorbitol dehydrogenases and other sugar dehydrogenases of the medium-chain dehydrogenase/reductase family (MDR), which includes zinc-dependent alcohol dehydrogenase and related proteins. Sorbitol and aldose reductase are NAD(+) binding proteins of the polyol pathway, which interconverts glucose and fructose. Sorbitol dehydrogenase is tetrameric and has a single catalytic zinc per subunit. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Related proteins include threonine dehydrogenase, formaldehyde dehydrogenase, and butanediol dehydrogenase. The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit. Horse liver alcohol dehydrogenase is a dimeric enzyme and each subunit has two domains. The NAD binding domain is in a Rossmann fold and the catalytic domain contains a zinc ion to which substrates bind. There is a cleft between the domains that closes upon formation of the ternary complex.


Pssm-ID: 176198 [Multi-domain]  Cd Length: 343  Bit Score: 94.22  E-value: 6.39e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1693 RPAPGPRQVEIEVEAAGLNFLDVLGALG----MMPAleaeesVLGRECSGRIAAVGEGVSGLRVGDEVlAVAP------- 1761
Cdd:cd08236   19 KPEPGPGEVLVKVKACGICGSDIPRYLGtgayHPPL------VLGHEFSGTVEEVGSGVDDLAVGDRV-AVNPllpcgkc 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1762 ----------------------GCFRSYVLVDESQVVRRPASLGLAEGAaqMV-PFATayfALHTVGR--LRRGERILI- 1815
Cdd:cd08236   92 eyckkgeyslcsnydyigsrrdGAFAEYVSVPARNLIKIPDHVDYEEAA--MIePAAV---ALHAVRLagITLGDTVVVi 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1816 ------HaaagglglAAVQLASRTGAE-ILATAGSEQKREYLRSLGIAHVLDSRSTSfVSEVRERTGGRGVDVVLNSL-A 1887
Cdd:cd08236  167 gagtigL--------LAIQWLKILGAKrVIAVDIDDEKLAVARELGADDTINPKEED-VEKVRELTEGRGADLVIEAAgS 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1888 GELLLAGLSVLAPHGRFLELGkrDLYADQ---QVGLRTLARGQ-----TFAAIDFGPHHPDFRAVLEEVATQLTqgQLEP 1959
Cdd:cd08236  238 PATIEQALALARPGGKVVLVG--IPYGDVtlsEEAFEKILRKEltiqgSWNSYSAPFPGDEWRTALDLLASGKI--KVEP 313

                        330       340
                 ....*....|....*....|
gi 53747904 1960 LPTRLFPARQVAEAFSFMAR 1979
Cdd:cd08236  314 LITHRLPLEDGPAAFERLAD 333
ttLC_FACS_AEE21_like cd12118
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ...
 2648-3127 8.26e-20

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: 96.21  E-value: 8.26e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2648 ARLHPELPALLAPERTLSYGELARRAQALAARLRELEVQPQELVAI------AM---HKGWEQATAVLGVLQAAaaylpL 2718
Cdd:cd12118   14 AAVYPDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVlapntpAMyelHFGVPMAGAVLNALNTR-----L 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2719 DPEQpplrLHQLLEEGPARVVLTQSSLLHTV------PWPPGVQviAVDELEPATeapplpprgtpehlayVIYTSGSTG 2792
Cdd:cd12118   89 DAEE----IAFILRHSEAKVLFVDREFEYEDllaegdPDFEWIP--PADEWDPIA----------------LNYTSGTTG 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2793 KPKGVAIEHRAA-LNTVVDLnTRFGVGPEDRVLGL------SALTFDLSVydvlgllgaggalvlpAAEA-------EKD 2858
Cdd:cd12118  147 RPKGVVYHHRGAyLNALANI-LEWEMKQHPVYLWTlpmfhcNGWCFPWTV----------------AAVGgtnvclrKVD 209

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2859 PAHWWERLVAGRVTVWNSTPALMLLLVEYAEQRGLKLPAALRlVMLSGDWIPVALPDRIRALGRDVQVVSlgGATEAsiw 2938
Cdd:cd12118  210 AKAIYDLIEKHKVTHFCGAPTVLNMLANAPPSDARPLPHRVH-VMTAGAPPPAAVLAKMEELGFDVTHVY--GLTET--- 283

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2939 siaYPIGQVA---PQWKSIP----YGMpLANQ--RFHVLDGRLEARPWW---VP------GELYIGGEGLAREYWRDEPL 3000
Cdd:cd12118  284 ---YGPATVCawkPEWDELPteerARL-KARQgvRYVGLEEVDVLDPETmkpVPrdgktiGEIVFRGNIVMKGYLKNPEA 359

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3001 TATRFirhpRTGerLYRTGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPALSASVVVARGEPRGVRRLV 3080
Cdd:cd12118  360 TAEAF----RGG--WFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPC 433

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*..
gi 53747904 3081 AYAVPRSGQTPAAGELRRYLAERLPAYMVPSAFVLLEsLPRSRNGKI 3127
Cdd:cd12118  434 AFVELKEGAKVTEEEIIAFCREHLAGFMVPKTVVFGE-LPKTSTGKI 479
CAD3 cd08297
Cinnamyl alcohol dehydrogenases (CAD); These alcohol dehydrogenases are related to the ...
 1694-1903 1.16e-19

Cinnamyl alcohol dehydrogenases (CAD); These alcohol dehydrogenases are related to the cinnamyl alcohol dehydrogenases (CAD), members of the medium chain dehydrogenase/reductase family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Cinnamyl alcohol dehydrogenases (CAD) reduce cinnamaldehydes to cinnamyl alcohols in the last step of monolignal metabolism in plant cells walls. CAD binds 2 zinc ions and is NADPH- dependent. CAD family members are also found in non-plant species, e.g. in yeast where they have an aldehyde reductase activity. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176257 [Multi-domain]  Cd Length: 341  Bit Score: 93.37  E-value: 1.16e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1694 PAPGPRQVEIEVEAAGLNFLDVLGALGMMPALEAEESVLGRECSGRIAAVGEGVSGLRVGDEVlAVA------------- 1760
Cdd:cd08297   22 PEPGPGEVLVKLEASGVCHTDLHAALGDWPVKPKLPLIGGHEGAGVVVAVGPGVSGLKVGDRV-GVKwlydacgkceycr 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1761 -----------------PGCFRSYVLVDESQVVRRPASLGLAEGAAQMVPFATAYFALhTVGRLRRGERILI-------- 1815
Cdd:cd08297  101 tgdetlcpnqknsgytvDGTFAEYAIADARYVTPIPDGLSFEQAAPLLCAGVTVYKAL-KKAGLKPGDWVVIsgaggglg 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1816 HAaagglglaAVQLASRTGAEILATAGSEQKREYLRSLGIAHVLDSRSTSFVSEVRERTGGRGVD-VVLNSLAGELLLAG 1894
Cdd:cd08297  180 HL--------GVQYAKAMGLRVIAIDVGDEKLELAKELGADAFVDFKKSDDVEAVKELTGGGGAHaVVVTAVSAAAYEQA 251


                 ....*....
gi 53747904 1895 LSVLAPHGR 1903
Cdd:cd08297  252 LDYLRPGGT 260
AFD_YhfT-like cd17633
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ...
 2780-3129 1.71e-19

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: 92.47  E-value: 1.71e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2780 HLAYVIYTSGSTGKPKGVAIEHRAALNTVVDLNTRFGVGPEDRVLGLSALTFDLSVYDVLGLLGAGGALVLpaaEAEKDP 2859
Cdd:cd17633    1 NPFYIGFTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLFLYGAISALYLGGTFIG---QRKFNP 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2860 AHWWERLVAGRVTVWNSTPALMLLLVeyaeqRGLKLPAALRLVMLSGDWIPVALPDRIRALGRDVQVVSLGGATEASIws 2939
Cdd:cd17633   78 KSWIRKINQYNATVIYLVPTMLQALA-----RTLEPESKIKSIFSSGQKLFESTKKKLKNIFPKANLIEFYGTSELSF-- 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2940 IAYPIGQVAPQWKSIpyGMPLANQRFHVLD------GRLearpwWVPGELYIGGEGLAREYWRDEPLTatrfirhprtge 3013
Cdd:cd17633  151 ITYNFNQESRPPNSV--GRPFPNVEIEIRNadggeiGKI-----FVKSEMVFSGYVRGGFSNPDGWMS------------ 211

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3014 rlyrTGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPALSASVVVarGEPRGVRRLVAYAVpRSGQTPAA 3093
Cdd:cd17633  212 ----VGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVV--GIPDARFGEIAVAL-YSGDKLTY 284

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 53747904 3094 GELRRYLAERLPAYMVPSAFVLLESLPRSRNGKIAR 3129
Cdd:cd17633  285 KQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
FACL_like_5 cd05924
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 2915-3126 4.66e-19

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: 92.06  E-value: 4.66e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2915 DRIRALGRDVQVVSLGGATEASIWSIAYPIGQVAPQWKSIpygmpLANQRFHVLDGRLEARPWWVPGELYIGGEGL-ARE 2993
Cdd:cd05924  152 QGLLELVPNITLVDAFGSSETGFTGSGHSAGSGPETGPFT-----RANPDTVVLDDDGRVVPPGSGGVGWIARRGHiPLG 226

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2994 YWRDEPLTATRFIRhpRTGERLYRTGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPALSASVVVARGEP 3073
Cdd:cd05924  227 YYGDEAKTAETFPE--VDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDE 304

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 53747904 3074 RGVRRLVAYAVPRSGQTPAAGELRRYLAERLPAYMVPSAFVLLESLPRSRNGK 3126
Cdd:cd05924  305 RWGQEVVAVVQLREGAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
iditol_2_DH_like cd08235
L-iditol 2-dehydrogenase; Putative L-iditol 2-dehydrogenase based on annotation of some ...
 1693-1974 4.86e-19

L-iditol 2-dehydrogenase; Putative L-iditol 2-dehydrogenase based on annotation of some members in this subgroup. L-iditol 2-dehydrogenase catalyzes the NAD+-dependent conversion of L-iditol to L-sorbose in fructose and mannose metabolism. This enzyme is related to sorbitol dehydrogenase, alcohol dehydrogenase, and other medium chain dehydrogenase/reductases. The zinc-dependent alcohol dehydrogenase (ADH-Zn)-like family of proteins is a diverse group of proteins related to the first identified member, class I mammalian ADH. This group is also called the medium chain dehydrogenases/reductase family (MDR) to highlight its broad range of activities and to distinguish from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal GroES-like catalytic domain. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176197 [Multi-domain]  Cd Length: 343  Bit Score: 91.50  E-value: 4.86e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1693 RPAPGPRQVEIEVEAAGLNFLDVLGALGMMPALEAEeSVLGRECSGRIAAVGEGVSGLRVGDEVlAVAPGC--------- 1763
Cdd:cd08235   19 VPEPGPGEVLVKVRACGICGTDVKKIRGGHTDLKPP-RILGHEIAGEIVEVGDGVTGFKVGDRV-FVAPHVpcgechycl 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1764 --------------------FRSYVLVDESQVVRR-----PASLGLAEGAaqMV-PFATAYFALHTVGrLRRGERILI-- 1815
Cdd:cd08235   97 rgnenmcpnykkfgnlydggFAEYVRVPAWAVKRGgvlklPDNVSFEEAA--LVePLACCINAQRKAG-IKPGDTVLVig 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1816 -------HaaagglglaaVQLASRTGAE-ILATAGSEQKREYLRSLGIAHVLDSRSTSFVSEVRERTGGRGVDVV-LNSL 1886
Cdd:cd08235  174 agpigllH----------AMLAKASGARkVIVSDLNEFRLEFAKKLGADYTIDAAEEDLVEKVRELTDGRGADVViVATG 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1887 AGELLLAGLSVLAPHGRFLELGKrdLYADQQVGL--RTLARGQ-----TFAAIDfgphhPDFRAVLEEVATqltqGQ--L 1957
Cdd:cd08235  244 SPEAQAQALELVRKGGRILFFGG--LPKGSTVNIdpNLIHYREititgSYAASP-----EDYKEALELIAS----GKidV 312

                        330
                 ....*....|....*..
gi 53747904 1958 EPLPTRLFPARQVAEAF 1974
Cdd:cd08235  313 KDLITHRFPLEDIEEAF 329
crotonyl_coA_red cd08246
crotonyl-CoA reductase; Crotonyl-CoA reductase, a member of the medium chain dehydrogenase ...
 1694-1988 5.02e-19

crotonyl-CoA reductase; Crotonyl-CoA reductase, a member of the medium chain dehydrogenase/reductase family, catalyzes the NADPH-dependent conversion of crotonyl-CoA to butyryl-CoA, a step in (2S)-methylmalonyl-CoA production for straight-chain fatty acid biosynthesis. Like enoyl reductase, another enzyme in fatty acid synthesis, crotonyl-CoA reductase is a member of the zinc-dependent alcohol dehydrogenase-like medium chain dehydrogenase/reductase family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES.


Pssm-ID: 176208 [Multi-domain]  Cd Length: 393  Bit Score: 92.48  E-value: 5.02e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1694 PAPGPRQVEIEVEAAGLNFLDVLGALG--------MMPALEAEE-SVLGRECSGRIAAVGEGVSGLRVGDEVLA------ 1758
Cdd:cd08246   38 PELGPGEVLVAVMAAGVNYNNVWAALGepvstfaaRQRRGRDEPyHIGGSDASGIVWAVGEGVKNWKVGDEVVVhcsvwd 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1759 ------------VAP-----------GCFRSYVLVDESQVVRRPASLGLAEGAAQMVPFATAYFAL-----HTVgrlRRG 1810
Cdd:cd08246  118 gndperaggdpmFDPsqriwgyetnyGSFAQFALVQATQLMPKPKHLSWEEAAAYMLVGATAYRMLfgwnpNTV---KPG 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1811 ERILIHAAAGGLGLAAVQLASRTGAEILATAGSEQKREYLRSLGIAHVLD----------------------SRSTSFVS 1868
Cdd:cd08246  195 DNVLIWGASGGLGSMAIQLARAAGANPVAVVSSEEKAEYCRALGAEGVINrrdfdhwgvlpdvnseaytawtKEARRFGK 274

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1869 EVRERTGGR-GVDVVLNSLAGELLLAGLSVLAPHGRFLELGKRDLYaDQQVGLRTL----ARGQtfaaidfGPHHPDFRA 1943
Cdd:cd08246  275 AIWDILGGReDPDIVFEHPGRATFPTSVFVCDRGGMVVICAGTTGY-NHTYDNRYLwmrqKRIQ-------GSHFANDRE 346

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 53747904 1944 VLEevATQLT-QGQLEPLPTRLFPARQVAEAFSFMAR-ALHIGRVAV 1988
Cdd:cd08246  347 AAE--ANRLVmKGRIDPCLSKVFSLDETPDAHQLMHRnQHHVGNMAV 391
PRK09185 PRK09185
beta-ketoacyl-ACP synthase;
156-439 5.81e-19

beta-ketoacyl-ACP synthase;


Pssm-ID: 236398 [Multi-domain]  Cd Length: 392  Bit Score: 92.21  E-value: 5.81e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   156 GNYPDFLAtrvAYkLNLRGPALGIHTACSTSLVSINMACSALRGFECDMALAGGV-SL-RLParsgyLYeegGVAS---- 229
Cdd:PRK09185  137 GSLADFLR---AY-LGLSGPAYTISTACSSSAKVFASARRLLEAGLCDAAIVGGVdSLcRLT-----LN---GFNSlesl 204

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   230 KDGHCRPFDAR---------ATGtvtgdgvgvvvlkrledALKARDPIHAVirgwALNNDGASRAGF--TAPSVEGQSEV 298
Cdd:PRK09185  205 SPQPCRPFSANrdginigeaAAF-----------------FLLEREDDAAV----ALLGVGESSDAHhmSAPHPEGLGAI 263

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   299 IAL--AHAAAGISARDITYVEAHGTGTPLGDPIEVAALTRAFRAHTAdtafCTlgAVKSNIGHLDAAAGVAGVIKTVQAL 376
Cdd:PRK09185  264 LAMqqALADAGLAPADIGYINLHGTATPLNDAMESRAVAAVFGDGVP----CS--STKGLTGHTLGAAGAVEAAICWLAL 337

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 53747904   377 RHRLIPPTLHFERPNPALHLEqsPFFVNTQPLPwesprgPRLAGVSSFGIGGTNAHTLFEEAP 439
Cdd:PRK09185  338 RHGLPPHGWNTGQPDPALPPL--YLVENAQALA------IRYVLSNSFAFGGNNCSLIFGRAD 392
FAAL cd05931
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...
 2686-3129 7.01e-19

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: 93.84  E-value: 7.01e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2686 QPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLDPEQPPL---RLHQLLEEGPARVVLTQSSLL-------HTVPWPPGV 2755
Cdd:cd05931   46 KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPPTPGRhaeRLAAILADAGPRVVLTTAAALaavrafaASRPAAGTP 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2756 QVIAVDELEPATEAPPLPPRGTPEHLAYVIYTSGSTGKPKGVAIEHRAALNTVVDLNTRFGVGPEDRVLG---------- 2825
Cdd:cd05931  126 RLLVVDLLPDTSAADWPPPSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSwlplyhdmgl 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2826 ----LSALTFDLSVYdvlgllgaggaLVLPAAEAeKDPAHWWERLVAGRVTVwnsTPA------LMLLLVEYAEQRGLKL 2895
Cdd:cd05931  206 igglLTPLYSGGPSV-----------LMSPAAFL-RRPLRWLRLISRYRATI---SAApnfaydLCVRRVRDEDLEGLDL 270

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2896 pAALRLVMLSGDwiPV------ALPDRIRALGRDVQV-------------VSLGGATE---------ASIWSIAYPIGQV 2947
Cdd:cd05931  271 -SSWRVALNGAE--PVrpatlrRFAEAFAPFGFRPEAfrpsyglaeatlfVSGGPPGTgpvvlrvdrDALAGRAVAVAAD 347

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2948 APQWKSIP-YGMPLANQRFHVLD--GRLEARPWWVpGELYIGGEGLAREYWRDEPLTATRFIRHPRTGERLY-RTGDQGR 3023
Cdd:cd05931  348 DPAARELVsCGRPLPDQEVRIVDpeTGRELPDGEV-GEIWVRGPSVASGYWGRPEATAETFGALAATDEGGWlRTGDLGF 426

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3024 MLpEGSIEFLGR-EDLQVkVQGFRVELGEIEAALAQ-HPALSASVVVARG-EPRGVRRLVAYAVPRSGQTPA-----AGE 3095
Cdd:cd05931  427 LH-DGELYITGRlKDLII-VRGRNHYPQDIEATAEEaHPALRPGCVAAFSvPDDGEERLVVVAEVERGADPAdlaaiAAA 504

                        490       500       510
                 ....*....|....*....|....*....|....*.
gi 53747904 3096 LRRYLAERLPayMVPSAFVLLE--SLPRSRNGKIAR 3129
Cdd:cd05931  505 IRAAVAREHG--VAPADVVLVRpgSIPRTSSGKIQR 538
OSB_CoA_lg cd05912
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ...
 2779-3132 7.51e-19

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: 92.02  E-value: 7.51e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2779 EHLAYVIYTSGSTGKPKGVAIEHRAALNTVVDLNTRFGVGPEDRVL---------GLS----ALTFDLSVYdvlgllgag 2845
Cdd:cd05912   77 DDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLTEDDNWLcalplfhisGLSilmrSVIYGMTVY--------- 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2846 galVLPAAEAEKdpAHwwERLVAGRVTVWNSTPALmllLVEYAEQRGLKLPAALRLVMLSGDWIPVALPDRirALGRDVQ 2925
Cdd:cd05912  148 ---LVDKFDAEQ--VL--HLINSGKVTIISVVPTM---LQRLLEILGEGYPNNLRCILLGGGPAPKPLLEQ--CKEKGIP 215

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2926 VVSLGGATEASIWSIAYPIGQVAPQWKSIpyGMPLANQRFHVLDgrlEARPWWVPGELYIGGEGLAREYWRDEPLTATRF 3005
Cdd:cd05912  216 VYQSYGMTETCSQIVTLSPEDALNKIGSA--GKPLFPVELKIED---DGQPPYEVGEILLKGPNVTKGYLNRPDATEESF 290

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3006 irhpRTGerLYRTGDQGRMLPEGSIEFLGR-EDLQVKvQGFRVELGEIEAALAQHPALSASVVVARGEPRGVRRLVAYAV 3084
Cdd:cd05912  291 ----ENG--WFKTGDIGYLDEEGFLYVLDRrSDLIIS-GGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVV 363

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 53747904 3085 prSGQTPAAGELRRYLAERLPAYMVPSAFVLLESLPRSRNGKIARDQL 3132
Cdd:cd05912  364 --SERPISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHEL 409
PRK05605 PRK05605
long-chain-fatty-acid--CoA ligase; Validated
 2748-3134 1.27e-18

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


Pssm-ID: 235531 [Multi-domain]  Cd Length: 573  Bit Score: 93.14  E-value: 1.27e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2748 TVPWPpgvqvIAVDELEPATEAPPLPPRGTPEHLAYVIYTSGSTGKPKGVAIEHR----------AALNTVVDLNTRF-G 2816
Cdd:PRK05605  193 TVPWE-----TLVDAAIGGDGSDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRnlfanaaqgkAWVPGLGDGPERVlA 267

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2817 VGPEDRVLGLS-ALTFDLSVydvlgllgAGGALVLPAAEAE-------KDPAHWwerlVAGrvtvwnsTPALMLLLVEYA 2888
Cdd:PRK05605  268 ALPMFHAYGLTlCLTLAVSI--------GGELVLLPAPDIDlildamkKHPPTW----LPG-------VPPLYEKIAEAA 328

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2889 EQRGLKLpAALRlVMLSGdwiPVALPDRIRALGRDVQ---VVSLGGATEASIWSIAYPIGQVA-PQWKSIPYgmPLANQR 2964
Cdd:PRK05605  329 EERGVDL-SGVR-NAFSG---AMALPVSTVELWEKLTgglLVEGYGLTETSPIIVGNPMSDDRrPGYVGVPF--PDTEVR 401

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2965 FHVLDGRLEARPWWVPGELYIGGEGLAREYWRDEPLTATRFIrhprtgERLYRTGDQGRMLPEGSIEFLGREDLQVKVQG 3044
Cdd:PRK05605  402 IVDPEDPDETMPDGEEGELLVRGPQVFKGYWNRPEETAKSFL------DGWFRTGDVVVMEEDGFIRIVDRIKELIITGG 475

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  3045 FRVELGEIEAALAQHPALSASVVVARGEPRGVRRLVAYAVPRSGQTPAAGELRRYLAERLPAYMVPSAFVLLESLPRSRN 3124
Cdd:PRK05605  476 FNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPGAALDPEGLRAYCREHLTRYKVPRRFYHVDELPRDQL 555

                         410
                  ....*....|
gi 53747904  3125 GKIARDQLPE 3134
Cdd:PRK05605  556 GKVRRREVRE 565
AL_MDR cd08252
Arginate lyase and other MDR family members; This group contains a structure identified as an ...
 1693-1904 1.38e-18

Arginate lyase and other MDR family members; This group contains a structure identified as an arginate lyase. Other members are identified quinone reductases, alginate lyases, and other proteins related to the zinc-dependent dehydrogenases/reductases. QOR catalyzes the conversion of a quinone and NAD(P)H to a hydroquinone and NAD(P+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR acts in the respiratory chains of bacteria and mitochondria, while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family, but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176214 [Multi-domain]  Cd Length: 336  Bit Score: 90.28  E-value: 1.38e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1693 RPAPGPRQVEIEVEAAGLNFLDVlGALGMMPALEAEESVLGRECSGRIAAVGEGVSGLRVGDEVL---AVA-PGCFRSYV 1768
Cdd:cd08252   25 KPVPGGRDLLVRVEAVSVNPVDT-KVRAGGAPVPGQPKILGWDASGVVEAVGSEVTLFKVGDEVYyagDITrPGSNAEYQ 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1769 LVDESQVVRRPASLGLAEGAAQMVPFATAYFALHTVGRLRRGER-----ILIHAAAGGLGLAAVQLASR-TGAEILATAG 1842
Cdd:cd08252  104 LVDERIVGHKPKSLSFAEAAALPLTSLTAWEALFDRLGISEDAEnegktLLIIGGAGGVGSIAIQLAKQlTGLTVIATAS 183

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 53747904 1843 SEQKREYLRSLGIAHVLDSRStSFVSEVRERtGGRGVDVVLN-SLAGELLLAGLSVLAPHGRF 1904
Cdd:cd08252  184 RPESIAWVKELGADHVINHHQ-DLAEQLEAL-GIEPVDYIFClTDTDQHWDAMAELIAPQGHI 244
ABCL cd05958
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ...
 2655-3132 1.51e-18

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: 91.77  E-value: 1.51e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2655 PALLAPERTLSYGELARRA-QALAARLRELEVQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLDPEQPPLRLHQLLEE 2733
Cdd:cd05958    2 TCLRSPEREWTYRDLLALAnRIANVLVGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2734 GPARVVLTQSSLLHTvpwppgvqviavdelepateapplpprgtpEHLAYVIYTSGSTGKPKGVAIEHRAALnTVVDLNT 2813
Cdd:cd05958   82 ARITVALCAHALTAS------------------------------DDICILAFTSGTTGAPKATMHFHRDPL-ASADRYA 130

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2814 R--FGVGPEDRVLGLSAL--TFDLSVYDVLGLLGAGGALVLPAAEAEKdpahwwerlVAG-----RVTVWNSTPALMLLL 2884
Cdd:cd05958  131 VnvLRLREDDRFVGSPPLafTFGLGGVLLFPFGVGASGVLLEEATPDL---------LLSaiaryKPTVLFTAPTAYRAM 201

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2885 VEYAEQRGLKLpAALRLVMLSGDWIPVALPDRIR-ALGrdVQVVSLGGATEASIWSIAYPIGQVAPQwksiPYGMPLANQ 2963
Cdd:cd05958  202 LAHPDAAGPDL-SSLRKCVSAGEALPAALHRAWKeATG--IPIIDGIGSTEMFHIFISARPGDARPG----ATGKPVPGY 274

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2964 RFHVLDGRLEARPWWVPGELYIGGEGLAReyWRDEPLTATRFirhprTGERLYrTGDQGRMLPEGSIEFLGREDLQVKVQ 3043
Cdd:cd05958  275 EAKVVDDEGNPVPDGTIGRLAVRGPTGCR--YLADKRQRTYV-----QGGWNI-TGDTYSRDPDGYFRHQGRSDDMIVSG 346

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3044 GFRVELGEIEAALAQHPALSASVVVARGEPRGVRRLVAYAVPRSGQTPA---AGELRRYLAERLPAYMVPSAFVLLESLP 3120
Cdd:cd05958  347 GYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPGpvlARELQDHAKAHIAPYKYPRAIEFVTELP 426

                        490
                 ....*....|..
gi 53747904 3121 RSRNGKIARDQL 3132
Cdd:cd05958  427 RTATGKLQRFAL 438
ACLS-CaiC cd17637
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ...
 2784-3129 1.64e-18

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: 90.02  E-value: 1.64e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2784 VIYTSGSTGKPKGVAIEHRAALNTVVDLNTRFGVGPEDRVLGL------SALTFDLSVYDVLGLLGAggalvlpaaeAEK 2857
Cdd:cd17637    5 IIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMlplfhiAGLNLALATFHAGGANVV----------MEK 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2858 -DPAHWWERLVAGRVTVWNSTPALMLLLVEYAEQRGLKLpAALRLVmlSGdwipVALPDRIRALGRDV--QVVSLGGATE 2934
Cdd:cd17637   75 fDPAEALELIEEEKVTLMGSFPPILSNLLDAAEKSGVDL-SSLRHV--LG----LDAPETIQRFEETTgaTFWSLYGQTE 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2935 ASIWSIAYPIGQvapqwKSIPYGMPLANQRFHVLDGRLEARPWWVPGELYIGGEGLAREYWRDEPLTATRFirhpRTGer 3014
Cdd:cd17637  148 TSGLVTLSPYRE-----RPGSAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTF----RNG-- 216

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3015 LYRTGDQGRMLPEGSIEFLGR--EDLQVKVQGFRVELGEIEAALAQHPALSASVVVARGEPR---GVRrlvAYAVPRSGQ 3089
Cdd:cd17637  217 WHHTGDLGRFDEDGYLWYAGRkpEKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKwgeGIK---AVCVLKPGA 293

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 53747904 3090 TPAAGELRRYLAERLPAYMVPSAFVLLESLPRSRNGKIAR 3129
Cdd:cd17637  294 TLTADELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
PRK08439 PRK08439
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
 86-435 1.65e-18

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


Pssm-ID: 236265 [Multi-domain]  Cd Length: 406  Bit Score: 90.95  E-value: 1.65e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904    86 SPREASHLDPQQRLLLECSWEALEDAGLRPDQL-PGWVGVYVGAG---------DTSYRFQllrghgdplSGSKDVAGFF 155
Cdd:PRK08439   62 DPKEVKKADRFIQLGLKAAREAMKDAGFLPEELdAERFGVSSASGigglpniekNSIICFE---------KGPRKISPFF 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   156 --GNYPDFLATRVAYKLNLRGPALGIHTACSTSLVSINMA--CSALRGFE-----------CDMALAGGVSLR-LPARSg 219
Cdd:PRK08439  133 ipSALVNMLGGFISIEHGLKGPNLSSVTACAAGTHAIIEAvkTIMLGGADkmlvvgaesaiCPVGIGGFAAMKaLSTRN- 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   220 ylyEEGGVASkdghcRPFDARATGTVTGDGVGVVVLKRLEDALKARDPIHAVIRGWALNNDGASragFTAPSVEGQSEVI 299
Cdd:PRK08439  212 ---DDPKKAS-----RPFDKDRDGFVMGEGAGALVLEEYESAKKRGAKIYAEIIGFGESGDANH---ITSPAPEGPLRAM 280

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   300 ALAHAAAGISarDITYVEAHGTGTPLGDPIEVAALTRAFrahtADTAFCTL-GAVKSNIGH-LDAAAGVAGVIkTVQALR 377
Cdd:PRK08439  281 KAALEMAGNP--KIDYINAHGTSTPYNDKNETAALKELF----GSKEKVPPvSSTKGQIGHcLGAAGAIEAVI-SIMAMR 353

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   378 HRLIPPTLHFERPNPALHLEQSPffvNTqplpwesPRGPRLAGV--SSFGIGGTNAHTLF 435
Cdd:PRK08439  354 DGILPPTINQETPDPECDLDYIP---NV-------ARKAELNVVmsNSFGFGGTNGVVIF 403
FACL_like_2 cd05917
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 2786-3132 1.76e-18

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: 90.03  E-value: 1.76e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2786 YTSGSTGKPKGVAIEHRAALNTVVDLNTRFGVGPEDR-------------VLG-LSALTFDLS-VYdvlgllgaggalvl 2850
Cdd:cd05917    9 FTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRlcipvplfhcfgsVLGvLACLTHGATmVF-------------- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2851 paAEAEKDPAHWWERLVAGRVTVWNSTPALMLLLVEYAEQRGLKLpAALRLVMLSGDWIPVALPDRIRALGRDVQVVSLG 2930
Cdd:cd05917   75 --PSPSFDPLAVLEAIEKEKCTALHGVPTMFIAELEHPDFDKFDL-SSLRTGIMAGAPCPPELMKRVIEVMNMKDVTIAY 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2931 GATEASIWSIAYPIGQVAPQwKSIPYGMPLANQRFHVLD--GRLEArPWWVPGELYIGGEGLAREYWRDEPLTATRFirh 3008
Cdd:cd05917  152 GMTETSPVSTQTRTDDSIEK-RVNTVGRIMPHTEAKIVDpeGGIVP-PVGVPGELCIRGYSVMKGYWNDPEKTAEAI--- 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3009 prTGERLYRTGDQGRMLPEGSIEFLGR-EDLQVKvQGFRVELGEIEAALAQHPALSASVVVARGEPRGVRRLVAYAVPRS 3087
Cdd:cd05917  227 --DGDGWLHTGDLAVMDEDGYCRIVGRiKDMIIR-GGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKE 303

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 53747904 3088 GQTPAAGELRRYLAERLPAYMVPSAFVLLESLPRSRNGKIARDQL 3132
Cdd:cd05917  304 GAELTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKL 348
PRK10754 PRK10754
NADPH:quinone reductase;
1678-1885 1.83e-18

NADPH:quinone reductase;


Pssm-ID: 182701 [Multi-domain]  Cd Length: 327  Bit Score: 89.79  E-value: 1.83e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  1678 GTPGLLESLGLrrcTRPAPGPRQVEIEVEAAGLNFLDVLGALGMMPAlEAEESVLGRECSGRIAAVGEGVSGLRVGDEVL 1757
Cdd:PRK10754   11 GGPEVLQAVEF---TPADPAENEVQVENKAIGINYIDTYIRSGLYPP-PSLPSGLGTEAAGVVSKVGSGVKHIKVGDRVV 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  1758 -AVAP-GCFRSYVLVDESQVVRRPASLGLAEGAAQMVPFATAYFALHTVGRLRRGERILIHAAAGGLGLAAVQLASRTGA 1835
Cdd:PRK10754   87 yAQSAlGAYSSVHNVPADKAAILPDAISFEQAAASFLKGLTVYYLLRKTYEIKPDEQFLFHAAAGGVGLIACQWAKALGA 166

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 53747904  1836 EILATAGSEQKREYLRSLGIAHVLDSRSTSFVSEVRERTGGRGVDVVLNS 1885
Cdd:PRK10754  167 KLIGTVGSAQKAQRAKKAGAWQVINYREENIVERVKEITGGKKVRVVYDS 216
PRK06145 PRK06145
acyl-CoA synthetase; Validated
 2648-3127 1.92e-18

acyl-CoA synthetase; Validated


Pssm-ID: 102207 [Multi-domain]  Cd Length: 497  Bit Score: 91.87  E-value: 1.92e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2648 ARLHPELPALLAPERTLSYGELARRAQALAARLRELEVQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLDPEQPPLRL 2727
Cdd:PRK06145   12 ARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEV 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2728 HQLLEEGPARVVLTQSSLlhTVPWPPGVQVIAVDEL---------EPATEAPPLPPRgTPEHLAYVIYTSGSTGKPKGVA 2798
Cdd:PRK06145   92 AYILGDAGAKLLLVDEEF--DAIVALETPKIVIDAAaqadsrrlaQGGLEIPPQAAV-APTDLVRLMYTSGTTDRPKGVM 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2799 IEHRAALNTVVDLNTRFGVGPEDRVLGLSALtFDLSVYDVLGLLGAGGALVLpAAEAEKDPAHWWERLVAGRVTVWNSTP 2878
Cdd:PRK06145  169 HSYGNLHWKSIDHVIALGLTASERLLVVGPL-YHVGAFDLPGIAVLWVGGTL-RIHREFDPEAVLAAIERHRLTCAWMAP 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2879 ALMLLLVEYAEQRGLKLpAALRLVMLSGDWIPvalPDRIRALGR---DVQVVSLGGATEASIWSIAYPIGQVAPQWKSIp 2955
Cdd:PRK06145  247 VMLSRVLTVPDRDRFDL-DSLAWCIGGGEKTP---ESRIRDFTRvftRARYIDAYGLTETCSGDTLMEAGREIEKIGST- 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2956 yGMPLANQRFHVLDGRLEARPWWVPGELYIGGEGLAREYWRDEPLTATRFIrhprtgERLYRTGDQGRMLPEGSIEFLGR 3035
Cdd:PRK06145  322 -GRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFY------GDWFRSGDVGYLDEEGFLYLTDR 394

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  3036 EDLQVKVQGFRVELGEIEAALAQHPALSASVVVARGEPRGVRRLVAYAVPRSGQTPAAGELRRYLAERLPAYMVPSAFVL 3115
Cdd:PRK06145  395 KKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGATLTLEALDRHCRQRLASFKVPRQLKV 474

                         490
                  ....*....|..
gi 53747904  3116 LESLPRSRNGKI 3127
Cdd:PRK06145  475 RDELPRNPSGKV 486
PRK08316 PRK08316
acyl-CoA synthetase; Validated
 2648-3132 3.91e-18

acyl-CoA synthetase; Validated


Pssm-ID: 181381 [Multi-domain]  Cd Length: 523  Bit Score: 91.15  E-value: 3.91e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2648 ARLHPELPALLAPERTLSYGELARRAQALAARLRELEVQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLDPEQPPLRL 2727
Cdd:PRK08316   21 ARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEEL 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2728 HQLLEEGPARVVLTQSSLL------------HTVPWPPGV-------QVIAVDELEPATEAPPLPPRGTPEHLAYVIYTS 2788
Cdd:PRK08316  101 AYILDHSGARAFLVDPALAptaeaalallpvDTLILSLVLggreapgGWLDFADWAEAGSVAEPDVELADDDLAQILYTS 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2789 GSTGKPKGVAIEHRAAL----NTVVDLntrfGVGPEDRVlgLSAL----TFDLSVYDVLGLLGAGGALVLPAAeaekDPA 2860
Cdd:PRK08316  181 GTESLPKGAMLTHRALIaeyvSCIVAG----DMSADDIP--LHALplyhCAQLDVFLGPYLYVGATNVILDAP----DPE 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2861 HWWERLVAGRV-------TVWNStpalmLLLVEYAEQRGLklpAALRLVMLSGDWIPVALPDRIRALGRDVQVVSLGGAT 2933
Cdd:PRK08316  251 LILRTIEAERItsffappTVWIS-----LLRHPDFDTRDL---SSLRKGYYGASIMPVEVLKELRERLPGLRFYNCYGQT 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2934 E-ASIWSIAYPIGQVApqwKSIPYGMPLANQRFHVLDGRLEARPWWVPGELYIGGEGLAREYWRDEPLTATRFirhpRTG 3012
Cdd:PRK08316  323 EiAPLATVLGPEEHLR---RPGSAGRPVLNVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAF----RGG 395

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  3013 erLYRTGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPALSASVVVARGEPRGVRRLVAYAVPRSGQTPA 3092
Cdd:PRK08316  396 --WFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAGATVT 473

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|
gi 53747904  3093 AGELRRYLAERLPAYMVPSAFVLLESLPRSRNGKIARDQL 3132
Cdd:PRK08316  474 EDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKREL 513
PRK06060 PRK06060
p-hydroxybenzoic acid--AMP ligase FadD22;
2736-3323 8.29e-18

p-hydroxybenzoic acid--AMP ligase FadD22;


Pssm-ID: 180374 [Multi-domain]  Cd Length: 705  Bit Score: 90.86  E-value: 8.29e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2736 ARVVLTQSSLLHTvpWPPGVQVIAVDELEPATEAPPL---PPRGtpEHLAYVIYTSGSTGKPKGvAIEHRAALNTVVDLN 2812
Cdd:PRK06060  103 PALVVTSDALRDR--FQPSRVAEAAELMSEAARVAPGgyePMGG--DALAYATYTSGTTGPPKA-AIHRHADPLTFVDAM 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2813 TR--FGVGPEDrvLGLSA----LTFDL--SVYDVLGLLGAGGALVLP-AAEAEKDPAHWWERlvagrvTVWNSTPALMLL 2883
Cdd:PRK06060  178 CRkaLRLTPED--TGLCSarmyFAYGLgnSVWFPLATGGSAVINSAPvTPEAAAILSARFGP------SVLYGVPNFFAR 249

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2884 LVEYAEQRGLKlpaALRLVMLSGDWIPVALPDRIRALGRDVQVVSLGGATEasiwsiaypIGQV-----APQWKSIPYGM 2958
Cdd:PRK06060  250 VIDSCSPDSFR---SLRCVVSAGEALELGLAERLMEFFGGIPILDGIGSTE---------VGQTfvsnrVDEWRLGTLGR 317

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2959 PLANQRFHVLDGRLEARPWWVPGELYIGGEGLAREYW-RDEPLTatrfirhprTGERLYRTGDQGRMLPEGSIEFLGRED 3037
Cdd:PRK06060  318 VLPPYEIRVVAPDGTTAGPGVEGDLWVRGPAIAKGYWnRPDSPV---------ANEGWLDTRDRVCIDSDGWVTYRCRAD 388

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  3038 LQVKVQGFRVELGEIEAALAQHPALSASVVVARGEPRGVRRLVAYAVPRSGQTPAAGELR---RYLAERLPAYMVPSAFV 3114
Cdd:PRK06060  389 DTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGATIDGSVMRdlhRGLLNRLSAFKVPHRFA 468

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  3115 LLESLPRSRNGKIARD----QLP----------------------EPQQTQGLAAQAAAADPLVERLAALVKEALRL--E 3166
Cdd:PRK06060  469 VVDRLPRTPNGKLVRGalrkQSPtkpiwelsltepgsgvraqrddLSASNMTIAGGNDGGATLRERLVALRQERQRLvvD 548

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  3167 RV---------EPQDSLL-------DLGADSVALIRLINRLEAELQFRPRLADIYENPTVQGLATLhqektksqgeggap 3230
Cdd:PRK06060  549 AVcaeaakmlgEPDPWSVdqdlafsELGFDSQMTVTLCKRLAAVTGLRLPETVGWDYGSISGLAQY-------------- 614

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  3231 rltaprstllpaeewgrFKANRPGLRRFPDgTPEVALPGS-GLAPAPEELTALERRRSVRTYSLEPVSHEQLGRLLAPLR 3309
Cdd:PRK06060  615 -----------------LEAELAGGHGRLK-SAGPVNSGAtGLWAIEEQLNKVEELVAVIADGEKQRVADRLRALLGTIA 676

                         650
                  ....*....|....
gi 53747904  3310 EWEVQGSRRYLYAS 3323
Cdd:PRK06060  677 GSEAGLGKLIQAAS 690
PRK14691 PRK14691
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
 147-436 1.04e-17

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


Pssm-ID: 173154 [Multi-domain]  Cd Length: 342  Bit Score: 87.86  E-value: 1.04e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   147 GSKDVAGFfgNYPDFL----ATRVAYKLNLRGPALGIHTACSTSLVSINMACSALRGFECDMALAGG-------VSLRLP 215
Cdd:PRK14691   53 GPKRLSPF--TVPSFLvnlaAGHVSIKHHFKGPIGAPVTACAAGVQAIGDAVRMIRNNEADVALCGGaeavidtVSLAGF 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   216 ARSGYLYEEGGvASKDGHCRPFDARATGTVTGDGVGVVVLKRLEDALKARDPIHAVIRGWALNNDgASRAGFTAPSVEGQ 295
Cdd:PRK14691  131 AAARALSTHFN-STPEKASRPFDTARDGFVMGEGAGLLIIEELEHALARGAKPLAEIVGYGTSAD-AYHMTSGAEDGDGA 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   296 SEVIALAHAAAGISARDITYVEAHGTGTPLGDPIEVAALTRAFRAHTAdtafCTLGAVKSNIGHLDAAAGVAGVIKTVQA 375
Cdd:PRK14691  209 YRAMKIALRQAGITPEQVQHLNAHATSTPVGDLGEINAIKHLFGESNA----LAITSTKSATGHLLGAAGGLETIFTVLA 284

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 53747904   376 LRHRLIPPTLHFERPNPA---LHLEQSpffvNTQplpwesPRGPRLAGVSSFGIGGTNAHTLFE 436
Cdd:PRK14691  285 LRDQIVPATLNLENPDPAakgLNIIAG----NAQ------PHDMTYALSNGFGFAGVNASILLK 338
Zn_ADH_like2 cd08264
Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol ...
 1683-1916 1.14e-17

Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol dehydrogenases of the medium chain dehydrogenase family. However, this subgroup does not contain the characteristic catalytic zinc site. Also, it contains an atypical structural zinc-binding pattern: DxxCxxCxxxxxxxC. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176225 [Multi-domain]  Cd Length: 325  Bit Score: 87.02  E-value: 1.14e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1683 LESLGLRRCTRPAPGPRQVEIEVEAAGLNFLD--VLGALGM--MPaleaeeSVLGRECSGRIAAVGEGVSGLRVGDEVLA 1758
Cdd:cd08264   11 IENLKVEDVKDPKPGPGEVLIRVKMAGVNPVDynVINAVKVkpMP------HIPGAEFAGVVEEVGDHVKGVKKGDRVVV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1759 ----------------------------VAPGCFRSYVLVDESQVVRRPASLGLAEGAAQMVPFATAYFALHTVGrLRRG 1810
Cdd:cd08264   85 ynrvfdgtcdmclsgnemlcrnggiigvVSNGGYAEYIVVPEKNLFKIPDSISDELAASLPVAALTAYHALKTAG-LGPG 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1811 ERILIHAAAGGLGLAAVQLASRTGAEILATAGseqkREYLRSLGIAHVLDsrSTSFVSEVRERTggRGVDVVLNSLAGEL 1890
Cdd:cd08264  164 ETVVVFGASGNTGIFAVQLAKMMGAEVIAVSR----KDWLKEFGADEVVD--YDEVEEKVKEIT--KMADVVINSLGSSF 235

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 53747904 1891 LLAGLSVLAPHGRFLELGK----------RDLYADQ 1916
Cdd:cd08264  236 WDLSLSVLGRGGRLVTFGTltggevkldlSDLYSKQ 271
butanediol_DH_like cd08233
(2R,3R)-2,3-butanediol dehydrogenase; (2R,3R)-2,3-butanediol dehydrogenase, a zinc-dependent ...
 1694-1883 2.86e-17

(2R,3R)-2,3-butanediol dehydrogenase; (2R,3R)-2,3-butanediol dehydrogenase, a zinc-dependent medium chain alcohol dehydrogenase, catalyzes the NAD(+)-dependent oxidation of (2R,3R)-2,3-butanediol and meso-butanediol to acetoin. BDH functions as a homodimer. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. The medium chain alcohol dehydrogenase family (MDR) have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit. Sorbitol and aldose reductase are NAD(+) binding proteins of the polyol pathway, which interconverts glucose and fructose. Sorbitol dehydrogenase is tetrameric and has a single catalytic zinc per subunit.


Pssm-ID: 176195 [Multi-domain]  Cd Length: 351  Bit Score: 86.44  E-value: 2.86e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1694 PAPGPRQVEIEVEAAGL------------NFLDVLGAlgmmPALEAEES--VLGRECSGRIAAVGEGVSGLRVGDEVlAV 1759
Cdd:cd08233   20 PPVKPGEVKIKVAWCGIcgsdlheyldgpIFIPTEGH----PHLTGETApvTLGHEFSGVVVEVGSGVTGFKVGDRV-VV 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1760 AP------------------------------GCFRSYVLVDESQVVRRPASLGLAEGAaqMV-PFATAYFALhTVGRLR 1808
Cdd:cd08233   95 EPtikcgtcgackrglynlcdslgfiglggggGGFAEYVVVPAYHVHKLPDNVPLEEAA--LVePLAVAWHAV-RRSGFK 171

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 53747904 1809 RGERILIhAAAGGLGLAAVQLASRTGA-EILATAGSEQKREYLRSLGIAHVLDSRSTSFVSEVRERTGGRGVDVVL 1883
Cdd:cd08233  172 PGDTALV-LGAGPIGLLTILALKAAGAsKIIVSEPSEARRELAEELGATIVLDPTEVDVVAEVRKLTGGGGVDVSF 246
ADH_zinc_N pfam00107
Zinc-binding dehydrogenase;
1827-1950 2.93e-17

Zinc-binding dehydrogenase;


Pssm-ID: 395057 [Multi-domain]  Cd Length: 129  Bit Score: 80.73  E-value: 2.93e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   1827 VQLASRTGAEILATAGSEQKREYLRSLGIAHVLDSRSTSFVSEVRERTGGRGVDVVLN-SLAGELLLAGLSVLAPHGRFL 1905
Cdd:pfam00107    7 IQLAKAAGAKVIAVDGSEEKLELAKELGADHVINPKETDLVEEIKELTGGKGVDVVFDcVGSPATLEQALKLLRPGGRVV 86

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 53747904   1906 ELGKrdLYADQQVGLRTLA-RGQTFAAIDFGpHHPDFRAVLEEVAT 1950
Cdd:pfam00107   87 VVGL--PGGPLPLPLAPLLlKELTILGSFLG-SPEEFPEALDLLAS 129
PLN02787 PLN02787
3-oxoacyl-[acyl-carrier-protein] synthase II
 166-439 3.27e-17

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


Pssm-ID: 215421 [Multi-domain]  Cd Length: 540  Bit Score: 88.50  E-value: 3.27e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   166 VAYKLNLRGPALGIHTACSTSLVSI-NMACSALRGfECDMALAGGV-SLRLPARSGYLYEEGGVASKDGH----CRPFDA 239
Cdd:PLN02787  274 LAMDLGWMGPNYSISTACATSNFCIlNAANHIIRG-EADVMLCGGSdAAIIPIGLGGFVACRALSQRNDDptkaSRPWDM 352

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   240 RATGTVTGDGVGVVVLKRLEDALKARDPIHAVIRGWALNNDGASragFTAPSVEGQSEVIAL--AHAAAGISARDITYVE 317
Cdd:PLN02787  353 NRDGFVMGEGAGVLLLEELEHAKKRGANIYAEFLGGSFTCDAYH---MTEPHPEGAGVILCIekALAQSGVSKEDVNYIN 429

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   318 AHGTGTPLGDPIEVAALTRAFRAHTAdtafCTLGAVKSNIGHLDAAAGVAGVIKTVQALRHRLIPPTLHFERPNPAlhle 397
Cdd:PLN02787  430 AHATSTKAGDLKEYQALMRCFGQNPE----LRVNSTKSMIGHLLGAAGAVEAIATVQAIRTGWVHPNINLENPESG---- 501

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 53747904   398 qspffVNTQPLPweSPRGPRL----AGVSSFGIGGTNAHTLFeeAP 439
Cdd:PLN02787  502 -----VDTKVLV--GPKKERLdikvALSNSFGFGGHNSSILF--AP 538
AMP-binding_C pfam13193
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ...
 3051-3126 4.07e-17

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: 78.36  E-value: 4.07e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 53747904   3051 EIEAALAQHPALSASVVVARGEPRGVRRLVAYAVPRSGQTPAAGELRRYLAERLPAYMVPSAFVLLESLPRSRNGK 3126
Cdd:pfam13193    1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
PRK06087 PRK06087
medium-chain fatty-acid--CoA ligase;
2685-3132 5.85e-17

medium-chain fatty-acid--CoA ligase;


Pssm-ID: 180393 [Multi-domain]  Cd Length: 547  Bit Score: 87.50  E-value: 5.85e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2685 VQPQELVAIAMhKGWEQATAV-LGVLQAAAAYLPLDPEQPPLRLHQLLEEGPARVVLTQS------------SLLHTVPW 2751
Cdd:PRK06087   71 IEPGDRVAFQL-PGWCEFTIIyLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFAPTlfkqtrpvdlilPLQNQLPQ 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2752 PPgvQVIAVDELEPATEAPPL------------PPRGTPEHLAYVIYTSGSTGKPKGVAIEHRAALNTVVDLNTRFGVGP 2819
Cdd:PRK06087  150 LQ--QIVGVDKLAPATSSLSLsqiiadyeplttAITTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTW 227

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2820 EDRVLGLSALTFDLSVYDVLGLLGAGGALVlpAAEAEKDPAHWWERLVAGRVT-VWNSTPALMLLLVEyAEQRGLKLPAa 2898
Cdd:PRK06087  228 QDVFMMPAPLGHATGFLHGVTAPFLIGARS--VLLDIFTPDACLALLEQQRCTcMLGATPFIYDLLNL-LEKQPADLSA- 303

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2899 LRLVMLSGDWIPVALPDRirALGRDVQVVSLGGATEASiwsiayPIGQVAP----QWKSIPYGMPLANQRFHVLDgrlEA 2974
Cdd:PRK06087  304 LRFFLCGGTTIPKKVARE--CQQRGIKLLSVYGSTESS------PHAVVNLddplSRFMHTDGYAAAGVEIKVVD---EA 372

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2975 RPWWVPGELyigGEGLARE------YWRDEPLTATRFirhprTGERLYRTGDQGRMLPEGSIEFLGRE-DLQVKvQGFRV 3047
Cdd:PRK06087  373 RKTLPPGCE---GEEASRGpnvfmgYLDEPELTARAL-----DEEGWYYSGDLCRMDEAGYIKITGRKkDIIVR-GGENI 443

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  3048 ELGEIEAALAQHPALSASVVVARGEPRGVRRLVAYAVPRSG-QTPAAGELRRYLAE-RLPAYMVPSAFVLLESLPRSRNG 3125
Cdd:PRK06087  444 SSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVLKAPhHSLTLEEVVAFFSRkRVAKYKYPEHIVVIDKLPRTASG 523


                  ....*..
gi 53747904  3126 KIARDQL 3132
Cdd:PRK06087  524 KIQKFLL 530
PRK13771 PRK13771
putative alcohol dehydrogenase; Provisional
 1676-1990 6.73e-17

putative alcohol dehydrogenase; Provisional


Pssm-ID: 184316 [Multi-domain]  Cd Length: 334  Bit Score: 85.09  E-value: 6.73e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  1676 AVGTPGLLESLGLRRCTRPAPGPRQVEIEVEAAGLNFLDVLGALGMMPALEAEeSVLGRECSGRIAAVGEGVSGLRVGDE 1755
Cdd:PRK13771    3 AVILPGFKQGYRIEEVPDPKPGKDEVVIKVNYAGLCYRDLLQLQGFYPRMKYP-VILGHEVVGTVEEVGENVKGFKPGDR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  1756 VLAV----------------------------APGCFRSYVLVDESQVVRRPAslGLAEGAAQMVPFATA--YFALHTVG 1805
Cdd:PRK13771   82 VASLlyapdgtceycrsgeeaycknrlgygeeLDGFFAEYAKVKVTSLVKVPP--NVSDEGAVIVPCVTGmvYRGLRRAG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  1806 rLRRGERILIHAAAGGLGLAAVQLASRTGAEILATAGSEQKREYLRSlgIA-HVLDSRstSFVSEVReRTGgrGVDVVLN 1884
Cdd:PRK13771  160 -VKKGETVLVTGAGGGVGIHAIQVAKALGAKVIAVTSSESKAKIVSK--YAdYVIVGS--KFSEEVK-KIG--GADIVIE 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  1885 SLAGELLLAGLSVLAPHGRFLELGKRDlyADQQVGLR---TLARGqtfaaIDFGPHHPDFRAVLEEVATQLTQGQLEPLP 1961
Cdd:PRK13771  232 TVGTPTLEESLRSLNMGGKIIQIGNVD--PSPTYSLRlgyIILKD-----IEIIGHISATKRDVEEALKLVAEGKIKPVI 304

                         330       340
                  ....*....|....*....|....*....
gi 53747904  1962 TRLFPARQVAEAFSFMARALHIGRVAVSM 1990
Cdd:PRK13771  305 GAEVSLSEIDKALEELKDKSRIGKILVKP 333
PRK06501 PRK06501
beta-ketoacyl-ACP synthase;
82-431 7.47e-17

beta-ketoacyl-ACP synthase;


Pssm-ID: 235817 [Multi-domain]  Cd Length: 425  Bit Score: 86.22  E-value: 7.47e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904    82 FFGYSPREASHLdpQQRLLLECSWEALEDAGLRPDQLPGwvGVYVGAG----DTSYRFQLlrGHGDPLSGSKDVAGFF-- 155
Cdd:PRK06501   63 FLPESPFGASAL--SEALARLAAEEALAQAGIGKGDFPG--PLFLAAPpvelEWPARFAL--AAAVGDNDAPSYDRLLra 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   156 ---GNYPDF--------LATRVAYKLNLRGPALGIHTACSTSLVSINMACSALRGFECDMALA----GGVSLRLPARSGY 220
Cdd:PRK06501  137 argGRFDALherfqfgsIADRLADRFGTRGLPISLSTACASGATAIQLGVEAIRRGETDRALCiatdGSVSAEALIRFSL 216

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   221 LY------EEGGVASKdghcrPFDARATGTVTGDGVGVVVLKRLEDALKARDPIHAVIRGWALNNDGASRagfTAPSVEG 294
Cdd:PRK06501  217 LSalstqnDPPEKASK-----PFSKDRDGFVMAEGAGALVLESLESAVARGAKILGIVAGCGEKADSFHR---TRSSPDG 288

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   295 qSEVIALAHAA---AGISARDITYVEAHGTGTPLGDPIEVAALTRAFRAHTADTAfctLGAVKSNIGHLDAAAGVAGVIK 371
Cdd:PRK06501  289 -SPAIGAIRAAladAGLTPEQIDYINAHGTSTPENDKMEYLGLSAVFGERLASIP---VSSNKSMIGHTLTAAGAVEAVF 364

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 53747904   372 TVQALRHRLIPPTLHFERPNPALHLEQSPffvNTQplpwespRGPRLAGV--SSFGIGGTNA 431
Cdd:PRK06501  365 SLLTIQTGRLPPTINYDNPDPAIPLDVVP---NVA-------RDARVTAVlsNSFGFGGQNA 416
FadD3 cd17638
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ...
 2784-3129 7.96e-17

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: 84.86  E-value: 7.96e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2784 VIYTSGSTGKPKGVAIEHRAALNTVVDLNTRFGVGPEDRVLGLSALTFDLSVYDVLGLLGAGGALVLPaaEAEKDPAHWW 2863
Cdd:cd17638    5 IMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFFHTFGYKAGIVACLLTGATVVP--VAVFDVDAIL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2864 ERLVAGRVTVWNSTPALMLLLVEYAEQRGLKLpAALRLVMLSGDWIPVALPDRIRA-LGRDVqVVSLGGATEASIWSIAY 2942
Cdd:cd17638   83 EAIERERITVLPGPPTLFQSLLDHPGRKKFDL-SSLRAAVTGAATVPVELVRRMRSeLGFET-VLTAYGLTEAGVATMCR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2943 PigQVAPQWKSIPYGMPLANQRFHVLDgrlearpwwvPGELYIGGEGLAREYWRDEPLTATRFirhprTGERLYRTGDQG 3022
Cdd:cd17638  161 P--GDDAETVATTCGRACPGFEVRIAD----------DGEVLVRGYNVMQGYLDDPEATAEAI-----DADGWLHTGDVG 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3023 RMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPALSASVVVARGEPRGVRRLVAYAVPRSGQTPAAGELRRYLAE 3102
Cdd:cd17638  224 ELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGVTLTEEDVIAWCRE 303

                        330       340
                 ....*....|....*....|....*..
gi 53747904 3103 RLPAYMVPSAFVLLESLPRSRNGKIAR 3129
Cdd:cd17638  304 RLANYKVPRFVRFLDELPRNASGKVMK 330
A_NRPS_TubE_like cd05906
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ...
 2726-3132 2.99e-16

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: 85.41  E-value: 2.99e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2726 RLHQLLEEGparVVLTQSSLLHTV-----PWP-PGVQVIAVDELePATEAPPLPPRGTPEHLAYVIYTSGSTGKPKGVAI 2799
Cdd:cd05906  112 HIWQLLGSP---VVLTDAELVAEFagletLSGlPGIRVLSIEEL-LDTAADHDLPQSRPDDLALLMLTSGSTGFPKAVPL 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2800 EHRAALNTVVDLNTRFGVGPEDRvlGLSALTFD----LSVYDVLGLLGAGGALVLPAAEAEKDPAHWWERLVAGRVTV-W 2874
Cdd:cd05906  188 THRNILARSAGKIQHNGLTPQDV--FLNWVPLDhvggLVELHLRAVYLGCQQVHVPTEEILADPLRWLDLIDRYRVTItW 265

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2875 --NSTPALMLLLVEYAEQRGLKLpAALRLVMLSGDWIPVALPDR-IRAL---GRDVQVVSLG-GATEAS---IWSIAYPI 2944
Cdd:cd05906  266 apNFAFALLNDLLEEIEDGTWDL-SSLRYLVNAGEAVVAKTIRRlLRLLepyGLPPDAIRPAfGMTETCsgvIYSRSFPT 344

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2945 GQVAPQWKSIPYGMPLANQRFHVLDGRLEARPWWVPGELYIGGEGLAREYWRDEPLTATRFirhprTGERLYRTGDQGrM 3024
Cdd:cd05906  345 YDHSQALEFVSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAF-----TEDGWFRTGDLG-F 418

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3025 LPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPALSASVVVA---RGEPRGVRRLVAYAVPRSGQTPAAGEL----R 3097
Cdd:cd05906  419 LDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPSFTAAfavRDPGAETEELAIFFVPEYDLQDALSETlraiR 498

                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 53747904 3098 RYLAERL---PAYMVPsafVLLESLPRSRNGKIARDQL 3132
Cdd:cd05906  499 SVVSREVgvsPAYLIP---LPKEEIPKTSLGKIQRSKL 533
Zn_ADH7 cd08261
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to ...
 1731-1978 3.08e-16

Alcohol dehydrogenases of the MDR family; This group contains members identified as related to zinc-dependent alcohol dehydrogenase and other members of the MDR family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group includes various activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176222 [Multi-domain]  Cd Length: 337  Bit Score: 83.01  E-value: 3.08e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1731 VLGRECSGRIAAVGEGVSGLRVGD---------------------------EVLAV-APGCFRSYVLVDEsQVVRRPASL 1782
Cdd:cd08261   56 ILGHELSGEVVEVGEGVAGLKVGDrvvvdpyiscgecyacrkgrpnccenlQVLGVhRDGGFAEYIVVPA-DALLVPEGL 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1783 GLAEGAaqMV-PFATAYfalHTV--GRLRRGERILIhAAAGGLGLAAVQLASRTGAEILATAGSEQKREYLRSLGIAHVL 1859
Cdd:cd08261  135 SLDQAA--LVePLAIGA---HAVrrAGVTAGDTVLV-VGAGPIGLGVIQVAKARGARVIVVDIDDERLEFARELGADDTI 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1860 DSRSTSFVSEVRERTGGRGVDVVLNSL-AGELLLAGLSVLAPHGR--FLELGKRDL-YADQQVGLRTLA----RGQTfaA 1931
Cdd:cd08261  209 NVGDEDVAARLRELTDGEGADVVIDATgNPASMEEAVELVAHGGRvvLVGLSKGPVtFPDPEFHKKELTilgsRNAT--R 286

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 53747904 1932 IDFgphhpdfravlEEVATQLTQGQLEPLP--TRLFPARQVAEAFSFMA 1978
Cdd:cd08261  287 EDF-----------PDVIDLLESGKVDPEAliTHRFPFEDVPEAFDLWE 324
AACS_like cd05968
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ...
 2662-3129 3.12e-16

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: 85.62  E-value: 3.12e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2662 RTLSYGELARRAQALAARLRELEVQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLDPEQPPLRLHQLLEEGPARVVLT 2741
Cdd:cd05968   90 RTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALIT 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2742 QSSLL-------------HTVPWPPGVQVIAV-------------DELEPATE---APPLPPRGTPEHLAYVIYTSGSTG 2792
Cdd:cd05968  170 ADGFTrrgrevnlkeeadKACAQCPTVEKVVVvrhlgndftpakgRDLSYDEEketAGDGAERTESEDPLMIIYTSGTTG 249

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2793 KPKGVAIEHRA-ALNTVVDLNTRFGVGPEDRVLGLSALTF---------------DLSVYDvlgllgaggalvlpAAEAE 2856
Cdd:cd05968  250 KPKGTVHVHAGfPLKAAQDMYFQFDLKPGDLLTWFTDLGWmmgpwlifgglilgaTMVLYD--------------GAPDH 315

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2857 KDPAHWWERLVAGRVTVWNSTP----ALMLLLVEYAEQRGLKlpaALRLVMLSGD-WIPVALPDRIRALGRD-VQVVSLG 2930
Cdd:cd05968  316 PKADRLWRMVEDHEITHLGLSPtlirALKPRGDAPVNAHDLS---SLRVLGSTGEpWNPEPWNWLFETVGKGrNPIINYS 392

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2931 GATEASIWSIA-YPIGQVAPqwksIPYGMPLANQRFHVLDGrlEARPwwVPGELyigGE--------GLAREYWRDEplt 3001
Cdd:cd05968  393 GGTEISGGILGnVLIKPIKP----SSFNGPVPGMKADVLDE--SGKP--ARPEV---GElvllapwpGMTRGFWRDE--- 458

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3002 aTRFIR-HPRTGERLYRTGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPALSASVVVARGEPRGVRRLV 3080
Cdd:cd05968  459 -DRYLEtYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIV 537

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|..
gi 53747904 3081 AYAVPRSGQTPAAG---ELRRYLAERLPAYMVPSAFVLLESLPRSRNGKIAR 3129
Cdd:cd05968  538 CFVVLKPGVTPTEAlaeELMERVADELGKPLSPERILFVKDLPKTRNAKVMR 589
4CL cd05904
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ...
 2645-3132 3.79e-16

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: 84.59  E-value: 3.79e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2645 FTQARLHPELPALL--APERTLSYGELARRAQALAARLRELEVQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLDPEQ 2722
Cdd:cd05904   12 FLFASAHPSRPALIdaATGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLS 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2723 PPLRLHQLLEEGPARVVLTQSSLLHTVPwPPGVQVIAVDELE-----------PATEAPPLPPRGTPEHLAYVIYTSGST 2791
Cdd:cd05904   92 TPAEIAKQVKDSGAKLAFTTAELAEKLA-SLALPVVLLDSAEfdslsfsdllfEADEAEPPVVVIKQDDVAALLYSSGTT 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2792 GKPKGVAIEHR---AALNTVVDLnTRFGVGPEDRVLGLSAL--TFDLSVYDVLGLLGAGGALVLPAAEAEKdpahwwerL 2866
Cdd:cd05904  171 GRSKGVMLTHRnliAMVAQFVAG-EGSNSDSEDVFLCVLPMfhIYGLSSFALGLLRLGATVVVMPRFDLEE--------L 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2867 VAG----RVTVWNSTPALMLLLVEYAEQRGLKLPaALRLVMLSGDWIPVALPDRIRALGRDVQVVSLGGATEASiwsiay 2942
Cdd:cd05904  242 LAAieryKVTHLPVVPPIVLALVKSPIVDKYDLS-SLRQIMSGAAPLGKELIEAFRAKFPNVDLGQGYGMTEST------ 314

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2943 PIGQV--APQWKSIPY---GMPLANQRFHVLD---GrlEARPWWVPGELYIGGEGLAREYWRDEPLTATRFirhprTGER 3014
Cdd:cd05904  315 GVVAMcfAPEKDRAKYgsvGRLVPNVEAKIVDpetG--ESLPPNQTGELWIRGPSIMKGYLNNPEATAATI-----DKEG 387

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3015 LYRTGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPALSASVVVAR-----GE-PrgvrrlVAYAVPRSG 3088
Cdd:cd05904  388 WLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYpdeeaGEvP------MAFVVRKPG 461

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....
gi 53747904 3089 QTPAAGELRRYLAERLPAYMVPSAFVLLESLPRSRNGKIARDQL 3132
Cdd:cd05904  462 SSLTEDEIMDFVAKQVAPYKKVRKVAFVDAIPKSPSGKILRKEL 505
PRK06839 PRK06839
o-succinylbenzoate--CoA ligase;
2647-3134 4.44e-16

o-succinylbenzoate--CoA ligase;


Pssm-ID: 168698 [Multi-domain]  Cd Length: 496  Bit Score: 84.53  E-value: 4.44e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2647 QARLHPELPALLAPERTLSYGEL-ARRAQALAARLRELEVQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLDPEQPPL 2725
Cdd:PRK06839   11 RAYLHPDRIAIITEEEEMTYKQLhEYVSKVAAYLIYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTEN 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2726 RLHQLLEEGPARVVLTQSSLLHTVPWPPGV----QVIAVDELEPATEAPPLPPRGTPEHLAYVI-YTSGSTGKPKGVAIE 2800
Cdd:PRK06839   91 ELIFQLKDSGTTVLFVEKTFQNMALSMQKVsyvqRVISITSLKEIEDRKIDNFVEKNESASFIIcYTSGTTGKPKGAVLT 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2801 HRA----ALNTVVDLNTRfgvgPEDRVLGLSALtFDLSVYDVLGLLGAGGALVLPAAEaEKDPAHWWERLVAGRVTVWNS 2876
Cdd:PRK06839  171 QENmfwnALNNTFAIDLT----MHDRSIVLLPL-FHIGGIGLFAFPTLFAGGVIIVPR-KFEPTKALSMIEKHKVTVVMG 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2877 TPALMLLLVEYAEQRGLKLpAALRLVMLSGDWIPVALpdrIRALGRDVQVVSLG-GATEASiwSIAYPIGQVAPQWKSIP 2955
Cdd:PRK06839  245 VPTIHQALINCSKFETTNL-QSVRWFYNGGAPCPEEL---MREFIDRGFLFGQGfGMTETS--PTVFMLSEEDARRKVGS 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2956 YGMPLANQRFHVLDGRLEARPWWVPGELYIGGEGLAREYWRDEPLTATRFirhpRTGerLYRTGDQGRMLPEGSIEFLGR 3035
Cdd:PRK06839  319 IGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETI----QDG--WLCTGDLARVDEDGFVYIVGR 392

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  3036 EDLQVKVQGFRVELGEIEAALAQHPALSASVVVARGEPRGVRRLVAYAVPRSGQTPAAGELRRYLAERLPAYMVPSAFVL 3115
Cdd:PRK06839  393 KKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIEKDVIEHCRLFLAKYKIPKEIVF 472

                         490
                  ....*....|....*....
gi 53747904  3116 LESLPRSRNGKIARDQLPE 3134
Cdd:PRK06839  473 LKELPKNATGKIQKAQLVN 491
PRK07967 PRK07967
beta-ketoacyl-ACP synthase I;
106-435 4.73e-16

beta-ketoacyl-ACP synthase I;


Pssm-ID: 181184 [Multi-domain]  Cd Length: 406  Bit Score: 83.57  E-value: 4.73e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   106 EALEDAGLRPDQLPG-WVGVYVGAGDTSYRFQLLRGhgDPLSGSKDVAGFfGNY--PDFLATRVAYKL----NLRGPALG 178
Cdd:PRK07967   81 QAIADAGLSEEQVSNpRTGLIAGSGGGSTRNQVEAA--DAMRGPRGPKRV-GPYavTKAMASTVSACLatpfKIKGVNYS 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   179 IHTACSTSLVSINMACSALRGFECDMALAGGVSlRLPARSGYLYEE-GGVASK-----DGHCRPFDARATGTVTGDGVGV 252
Cdd:PRK07967  158 ISSACATSAHCIGNAVEQIQLGKQDIVFAGGGE-ELDWEMSCLFDAmGALSTKyndtpEKASRAYDANRDGFVIAGGGGV 236

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   253 VVLKRLEDALKARDPIHAVIRGWALNNDGASragFTAPSVEGQseVIALAHAAAGISArDITYVEAHGTGTPLGDPIEVA 332
Cdd:PRK07967  237 VVVEELEHALARGAKIYAEIVGYGATSDGYD---MVAPSGEGA--VRCMQMALATVDT-PIDYINTHGTSTPVGDVKELG 310

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   333 ALTRAFRAHTAdtafcTLGAVKSNIGHLDAAAGVAGVIKTVQALRHRLIPPTLHFERPNPAlhleqspffVNTQPLPWES 412
Cdd:PRK07967  311 AIREVFGDKSP-----AISATKSLTGHSLGAAGVQEAIYSLLMMEHGFIAPSANIEELDPQ---------AAGMPIVTET 376

                         330       340
                  ....*....|....*....|....*
gi 53747904   413 PRGPRLAGV--SSFGIGGTNAHTLF 435
Cdd:PRK07967  377 TDNAELTTVmsNSFGFGGTNATLVF 401
VL_LC_FACS_like cd05907
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ...
 2660-3111 5.58e-16

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: 83.80  E-value: 5.58e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2660 PERTLSYGELARRAQALAARLRELEVQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLDPEQPPLRLHQLLEEGPARVV 2739
Cdd:cd05907    2 VWQPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKAL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2740 LTqssllhtvpwppgvqviavdelepateapplpprGTPEHLAYVIYTSGSTGKPKGVAIEHRAALNTVVDLNTRFGVGP 2819
Cdd:cd05907   82 FV----------------------------------EDPDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATE 127

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2820 EDRVLGLSALtfdlsvydvlgllgaggalvlpaaeaekdpAHWWER-------LVAG-RVTVWNSTPALMLLLVE----- 2886
Cdd:cd05907  128 GDRHLSFLPL------------------------------AHVFERraglyvpLLAGaRIYFASSAETLLDDLSEvrptv 177

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2887 -----------YAEQRGLKLPAALRLVMLSgdwipvALPDRIRAlgrdvqVVSLGGATEASIWSIAYPIGqvapqwksIP 2955
Cdd:cd05907  178 flavprvwekvYAAIKVKAVPGLKRKLFDL------AVGGRLRF------AASGGAPLPAELLHFFRALG--------IP 237

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2956 ----YGM----------PLANQRF----HVLDG---RLEARpwwvpGELYIGGEGLAREYWRDEPLTATRFirhprTGER 3014
Cdd:cd05907  238 vyegYGLtetsavvtlnPPGDNRIgtvgKPLPGvevRIADD-----GEILVRGPNVMLGYYKNPEATAEAL-----DADG 307

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3015 LYRTGDQGRMLPEGSIEFLGR-EDLQVKVQGFRVELGEIEAALAQHPALSASVVVARGEPrgvrRLVAYAVPRSGQtpaa 3093
Cdd:cd05907  308 WLHTGDLGEIDEDGFLHITGRkKDLIITSGGKNISPEPIENALKASPLISQAVVIGDGRP----FLVALIVPDPEA---- 379

                        490
                 ....*....|....*...
gi 53747904 3094 geLRRYLAERLPAYMVPS 3111
Cdd:cd05907  380 --LEAWAEEHGIAYTDVA 395
KR_1_FAS_SDR_x cd08954
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 1, complex (x) SDRs; ...
 1237-1377 5.95e-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: 83.65  E-value: 5.95e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1237 GAEVQVYTADVAeeaAVRSVVEQVHARW--GKIHGVLHAAATFDDGVIQLRTHEQSSRALRTKVRGSMVLHEVLASEG-- 1312
Cdd:cd08954  273 FHFVSVDVSDVS---SLEKAINLILNAPkiGPIGGIFHLAFVLIDKVLEIDTESLFISVNKAKVMGAINLHNQSIKRCwk 349

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 53747904 1313 LDWFALCSSLASALGSFGQADYCAANAFQDAYAHHLRRQGFTGaLALDWGTWRDTGaamrLVART 1377
Cdd:cd08954  350 LDYFVLFSSVSSIRGSAGQCNYVCANSVLDSLSRYRKSIGLPS-IAINWGAIGDVG----FVSRN 409
FAA1 COG1022
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
2644-3073 1.02e-15

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


Pssm-ID: 440645 [Multi-domain]  Cd Length: 603  Bit Score: 84.00  E-value: 1.02e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2644 FFTQARLHPELPALLAPE----RTLSYGELARRAQALAARLRELEVQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLD 2719
Cdd:COG1022   17 LRRRAARFPDRVALREKEdgiwQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVPIY 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2720 PEQPPLRLHQLLEEGPARVVLTQS---------------SLLHTV-----PWPPGVQVIAVDELEPATEAPPLPPR---- 2775
Cdd:COG1022   97 PTSSAEEVAYILNDSGAKVLFVEDqeqldkllevrdelpSLRHIVvldprGLRDDPRLLSLDELLALGREVADPAElear 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2776 ---GTPEHLAYVIYTSGSTGKPKGVAIEHRAALNTVVDLNTRFGVGPEDRVL-------------GLSALTFDLSVYdvl 2839
Cdd:COG1022  177 raaVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLsflplahvfertvSYYALAAGATVA--- 253

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2840 gllgaggalvlpAAEAEKDPA--------HW-------WERLVAG-RVTVWNSTPALMLLL-------VEYAEQR--GLK 2894
Cdd:COG1022  254 ------------FAESPDTLAedlrevkpTFmlavprvWEKVYAGiQAKAEEAGGLKRKLFrwalavgRRYARARlaGKS 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2895 LPAALRLVMLSGDWIpVAlpDRIR-ALGRDVQV-VSLGGATEASI----WSIAYPIGQVapqwksipYGM---------- 2958
Cdd:COG1022  322 PSLLLRLKHALADKL-VF--SKLReALGGRLRFaVSGGAALGPELarffRALGIPVLEG--------YGLtetspvitvn 390

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2959 PLANQRFH----VLDG---RLEARpwwvpGELYIGGEGLAREYWRDEPLTATRFirhprTGERLYRTGDQGRMLPEGSIE 3031
Cdd:COG1022  391 RPGDNRIGtvgpPLPGvevKIAED-----GEILVRGPNVMKGYYKNPEATAEAF-----DADGWLHTGDIGELDEDGFLR 460

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|...
gi 53747904 3032 FLGR-EDLQVKVQGFRVELGEIEAALAQHPALSASVVVARGEP 3073
Cdd:COG1022  461 ITGRkKDLIVTSGGKNVAPQPIENALKASPLIEQAVVVGDGRP 503
arabinose_DH_like cd05284
D-arabinose dehydrogenase; This group contains arabinose dehydrogenase (AraDH) and related ...
 1684-1883 1.29e-15

D-arabinose dehydrogenase; This group contains arabinose dehydrogenase (AraDH) and related alcohol dehydrogenases. AraDH is a member of the medium chain dehydrogenase/reductase family and catalyzes the NAD(P)-dependent oxidation of D-arabinose and other pentoses, the initial step in the metabolism of d-arabinose into 2-oxoglutarate. Like the alcohol dehydrogenases, AraDH binds a zinc in the catalytic cleft as well as a distal structural zinc. AraDH forms homotetramers as a dimer of dimers. AraDH replaces a conserved catalytic His with replace with Arg, compared to the canonical ADH site. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176187 [Multi-domain]  Cd Length: 340  Bit Score: 81.45  E-value: 1.29e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1684 ESLGLRRCTRPAPGPRQVEIEVEAAGLNFLDVL-------GALGMMPALeaeesVLGRECSGRIAAVGEGVSGLRVGDEV 1756
Cdd:cd05284   11 KPLRLEDVPVPEPGPGQVLVRVGGAGVCHSDLHvidgvwgGILPYKLPF-----TLGHENAGWVEEVGSGVDGLKEGDPV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1757 LAVAP-GC---------------------------FRSYVLVDESQVVRRPASLGLAEGAaqmvPFA----TAYFALHT- 1803
Cdd:cd05284   86 VVHPPwGCgtcrycrrgeenycenarfpgigtdggFAEYLLVPSRRLVKLPRGLDPVEAA----PLAdaglTAYHAVKKa 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1804 VGRLRRGERILI-------HAAagglglaaVQLASR-TGAEILATAGSEQKREYLRSLGIAHVLDSRSTSfVSEVRERTG 1875
Cdd:cd05284  162 LPYLDPGSTVVVigvgglgHIA--------VQILRAlTPATVIAVDRSEEALKLAERLGADHVLNASDDV-VEEVRELTG 232


                 ....*...
gi 53747904 1876 GRGVDVVL 1883
Cdd:cd05284  233 GRGADAVI 240
DCL_NRPS-like cd19536
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ...
 2216-2605 1.43e-15

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: 82.11  E-value: 1.43e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2216 LEVERFIQCWRQLLQRHDMLRMVVLPDGRQQ----VLEQVpEYTPEVVELRGLSPQEAESRRLQLRERMAHQVLRSDRWP 2291
Cdd:cd19536   36 LNLDLLLEALQVLIDRHDILRTSFIEDGLGQpvqvVHRQA-QVPVTELDLTPLEEQLDPLRAYKEETKIRRFDLGRAPLV 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2292 LFELVLCRYEGGVRIHMSMDALMLDAWSSAVLRQDFAQLYHEP--GRPLEPL-AITFRDYVLAERRLREGEAHERaraYW 2368
Cdd:cd19536  115 RAALVRKDERERFLLVISDHHSILDGWSLYLLVKEILAVYNQLleYKPLSLPpAQPYRDFVAHERASIQQAASER---YW 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2369 WARLD----TLPPPPELPLVKEPSQleharftHREARLEPHRWARLQERARAHGLTPSAACMAAFAEVLARWSRHPRFTL 2444
Cdd:cd19536  192 REYLAgatlATLPALSEAVGGGPEQ-------DSELLVSVPLPVRSRSLAKRSGIPLSTLLLAAWALVLSRHSGSDDVVF 264

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2445 NLTLFQRLPLHPQVDELVGDFTSLVLLEVEAhAASTFAERASRLQAQLWRDLEHGSVSavqlIRELVRTGRRSPGAIMPV 2524
Cdd:cd19536  265 GTVVHGRSEETTGAERLLGLFLNTLPLRVTL-SEETVEDLLKRAQEQELESLSHEQVP----LADIQRCSEGEPLFDSIV 339

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2525 VFTSILSLDARRGPQGSLSFFEGELVYSISQTPQVWLdhGVHEEEGALVLAWDSVEALFPPGMVDDMFHAYQRLLGALAE 2604
Cdd:cd19536  340 NFRHFDLDFGLPEWGSDEGMRRGLLFSEFKSNYDVNL--SVLPKQDRLELKLAYNSQVLDEEQAQRLAAYYKSAIAELAT 417


                 .
gi 53747904 2605 E 2605
Cdd:cd19536  418 A 418
PRK07470 PRK07470
acyl-CoA synthetase; Validated
 2644-3134 1.62e-15

acyl-CoA synthetase; Validated


Pssm-ID: 180988 [Multi-domain]  Cd Length: 528  Bit Score: 82.78  E-value: 1.62e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2644 FFTQ-ARLHPELPALLAPERTLSYGELARRAQALAARLRELEVQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLDPEQ 2722
Cdd:PRK07470   12 FLRQaARRFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQ 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2723 PPLRLHQLLEEGPARVVLTQS-------SLLHTVPWPPGVQVIAVDELEPATEAPPLPPRGTPEHLAYV--------IYT 2787
Cdd:PRK07470   92 TPDEVAYLAEASGARAMICHAdfpehaaAVRAASPDLTHVVAIGGARAGLDYEALVARHLGARVANAAVdhddpcwfFFT 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2788 SGSTGKPKGVAIEH-RAAL---NTVVDLNTrfGVGPEDRVLGLSALTFDLSVYDVLGLLGAGGALVLPaaeAEK-DPAHW 2862
Cdd:PRK07470  172 SGTTGRPKAAVLTHgQMAFvitNHLADLMP--GTTEQDASLVVAPLSHGAGIHQLCQVARGAATVLLP---SERfDPAEV 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2863 WeRLVAG-RVTVWNSTPALMLLLVEYaeqrglklPAA-------LRLVMLSGdwIPVALPDRIRALGR----DVQVVSLG 2930
Cdd:PRK07470  247 W-ALVERhRVTNLFTVPTILKMLVEH--------PAVdrydhssLRYVIYAG--APMYRADQKRALAKlgkvLVQYFGLG 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2931 GATeASIwSIAYPIGQVA---PQWKSIPYGMPLANQRFHVLDGRLEARPWWVPGELYIGGEGLAREYWRDEPLTATRFir 3007
Cdd:PRK07470  316 EVT-GNI-TVLPPALHDAedgPDARIGTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAF-- 391

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  3008 hpRTGerLYRTGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPALSASVVVARGEPRGVRRLVAYAVPRS 3087
Cdd:PRK07470  392 --RDG--WFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARD 467

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*..
gi 53747904  3088 GQTPAAGELRRYLAERLPAYMVPSAFVLLESLPRSRNGKIARDQLPE 3134
Cdd:PRK07470  468 GAPVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVRE 514
CAD cd08245
Cinnamyl alcohol dehydrogenases (CAD) and related proteins; Cinnamyl alcohol dehydrogenases ...
 1675-1903 2.98e-15

Cinnamyl alcohol dehydrogenases (CAD) and related proteins; Cinnamyl alcohol dehydrogenases (CAD), members of the medium chain dehydrogenase/reductase family, reduce cinnamaldehydes to cinnamyl alcohols in the last step of monolignal metabolism in plant cells walls. CAD binds 2 zinc ions and is NADPH- dependent. CAD family members are also found in non-plant species, e.g. in yeast where they have an aldehyde reductase activity. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes, or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176207 [Multi-domain]  Cd Length: 330  Bit Score: 80.06  E-value: 2.98e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1675 VAVGTPGLLESLGLRRCTRPAPGPRQVEIEVEAAGLNFLDVLGALG-----MMPAleaeesVLGRECSGRIAAVGEGVSG 1749
Cdd:cd08245    1 KAAVVHAAGGPLEPEEVPVPEPGPGEVLIKIEACGVCHTDLHAAEGdwggsKYPL------VPGHEIVGEVVEVGAGVEG 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1750 LRVGDEV----LAVAPGC-------------------------FRSYVLVDESQVVRRPASLGLAEGAAQMVPFATAYFA 1800
Cdd:cd08245   75 RKVGDRVgvgwLVGSCGRceycrrglenlcqkavntgyttqggYAEYMVADAEYTVLLPDGLPLAQAAPLLCAGITVYSA 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1801 LHTVGrLRRGERILI-------HAaagglglaAVQLASRTGAEILATAGSEQKREYLRSLGIAHVLDSRstsfvSEVRER 1873
Cdd:cd08245  155 LRDAG-PRPGERVAVlgigglgHL--------AVQYARAMGFETVAITRSPDKRELARKLGADEVVDSG-----AELDEQ 220

                        250       260       270
                 ....*....|....*....|....*....|.
gi 53747904 1874 TGGRGVDVVLN-SLAGELLLAGLSVLAPHGR 1903
Cdd:cd08245  221 AAAGGADVILVtVVSGAAAEAALGGLRRGGR 251
23DHB-AMP_lg cd05920
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ...
 2870-3132 3.39e-15

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: 81.61  E-value: 3.39e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2870 RVTVWNSTPALMLLLVEYAEQRGLKLPAaLRLVMLSGDWIPVALPDRIRA-LGRDVQVV-----------SLGGATEASI 2937
Cdd:cd05920  229 GVTVTALVPALVSLWLDAAASRRADLSS-LRLLQVGGARLSPALARRVPPvLGCTLQQVfgmaegllnytRLDDPDEVII 307

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2938 WSIAYPIGQ------VAPQWKSIPYGMPlanqrfhvldgrlearpwwvpGELYIGGEGLAREYWRDEPLTATRFirhprT 3011
Cdd:cd05920  308 HTQGRPMSPddeirvVDEEGNPVPPGEE---------------------GELLTRGPYTIRGYYRAPEHNARAF-----T 361

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3012 GERLYRTGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPALSASVVVARGEPRGVRRLVAYAVPRsGQTP 3091
Cdd:cd05920  362 PDGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLR-DPPP 440

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 53747904 3092 AAGELRRYLAER-LPAYMVPSAFVLLESLPRSRNGKIARDQL 3132
Cdd:cd05920  441 SAAQLRRFLRERgLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
PRK06164 PRK06164
acyl-CoA synthetase; Validated
 2646-3134 4.84e-15

acyl-CoA synthetase; Validated


Pssm-ID: 235722 [Multi-domain]  Cd Length: 540  Bit Score: 81.33  E-value: 4.84e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2646 TQARLHPELPALLAPERTLSYGELARRAQALAARLRELEVQPQELVAIAMHK-----GWEQATAVLGVL----------- 2709
Cdd:PRK06164   18 AHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNciewvVLFLACARLGATviavntryrsh 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2710 -------QAAAAYLPLDPEQPPLRLHQLLEEGPARVVLTQSSLL------HTVPWP-PGVQVIAVDELEPATEAPPLPPR 2775
Cdd:PRK06164   98 evahilgRGRARWLVVWPGFKGIDFAAILAAVPPDALPPLRAIAvvddaaDATPAPaPGARVQLFALPDPAPPAAAGERA 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2776 GTPEHLAYVIYTSGSTGKPKGVAieHRAAlnTVVDLNTR----FGVGPEDRVlgLSALTFdLSVYDVLGLLGAGGALVLP 2851
Cdd:PRK06164  178 ADPDAGALLFTTSGTTSGPKLVL--HRQA--TLLRHARAiaraYGYDPGAVL--LAALPF-CGVFGFSTLLGALAGGAPL 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2852 AAEAEKDPAHWWERLVAGRVT-VWNSTPALMLLLVEYAEQRGLklpAALRLVMLsGDWIPVALPDRIRALGRDVQVVSLG 2930
Cdd:PRK06164  251 VCEPVFDAARTARALRRHRVThTFGNDEMLRRILDTAGERADF---PSARLFGF-ASFAPALGELAALARARGVPLTGLY 326

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2931 GATEA----SIWSIAYPigqVAPQWksIPYGMPLANQ-RFHV---LDGRLeaRPWWVPGELYIGGEGLAREYWRDEPLTA 3002
Cdd:PRK06164  327 GSSEVqalvALQPATDP---VSVRI--EGGGRPASPEaRVRArdpQDGAL--LPDGESGEIEIRAPSLMRGYLDNPDATA 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  3003 TRFirhprTGERLYRTGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPALSASVVVArGEPRGVRRLVAY 3082
Cdd:PRK06164  400 RAL-----TDDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVG-ATRDGKTVPVAF 473

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 53747904  3083 AVPRSGQTPAAGELRRYLAERLPAYMVPSAFVLLESLP--RSRNG-KIARDQLPE 3134
Cdd:PRK06164  474 VIPTDGASPDEAGLMAACREALAGFKVPARVQVVEAFPvtESANGaKIQKHRLRE 528
PRK07638 PRK07638
acyl-CoA synthetase; Validated
 2648-3129 6.28e-15

acyl-CoA synthetase; Validated


Pssm-ID: 236071 [Multi-domain]  Cd Length: 487  Bit Score: 80.59  E-value: 6.28e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2648 ARLHPELPALLAPERTLSYGELARRAQALAARLRELEVQPqELVAIAMHKGWEQATAVLGVLQAAAAYLPLDPEQPPLRL 2727
Cdd:PRK07638   11 ASLQPNKIAIKENDRVLTYKDWFESVCKVANWLNEKESKN-KTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDEL 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2728 HQLLEEGPARVVLTQSSLLHTVPWPPGvQVIAVDELEPATE--APPLPPRGTPEHLA-YVIYTSGSTGKPKGVAIEHRAA 2804
Cdd:PRK07638   90 KERLAISNADMIVTERYKLNDLPDEEG-RVIEIDEWKRMIEkyLPTYAPIENVQNAPfYMGFTSGSTGKPKAFLRAQQSW 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2805 LNTVVDLNTRFGVGPEDRVL-------------GLSALTFDLSVYdvlgllgaggalvlpaAEAEKDPAHWWERLVAGRV 2871
Cdd:PRK07638  169 LHSFDCNVHDFHMKREDSVLiagtlvhslflygAISTLYVGQTVH----------------LMRKFIPNQVLDKLETENI 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2872 TVWNSTPALMLLLVEYAEQRGLKLpaalrLVMLSG-DWiPVALPDRIRALGRDVQVVSLGGATEASIWSIAYPigqvaPQ 2950
Cdd:PRK07638  233 SVMYTVPTMLESLYKENRVIENKM-----KIISSGaKW-EAEAKEKIKNIFPYAKLYEFYGASELSFVTALVD-----EE 301

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2951 WKSIPY--GMPLANQRFHVldgRLEARPWWVPGEL-------------YIGGEGLAREYWRDEPLTatrfirhprtgerl 3015
Cdd:PRK07638  302 SERRPNsvGRPFHNVQVRI---CNEAGEEVQKGEIgtvyvkspqffmgYIIGGVLARELNADGWMT-------------- 364

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  3016 yrTGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPALSASVVVARGEPRGVRRLVAYAvprSGQTPAAgE 3095
Cdd:PRK07638  365 --VRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAII---KGSATKQ-Q 438

                         490       500       510
                  ....*....|....*....|....*....|....
gi 53747904  3096 LRRYLAERLPAYMVPSAFVLLESLPRSRNGKIAR 3129
Cdd:PRK07638  439 LKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIAR 472
PrpE cd05967
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ...
 2715-3129 6.60e-15

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: 81.21  E-value: 6.60e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2715 YLPLdpeqpplrLHQLLEEG---PARVVLTQSSLLHTVPWPPGVQVIAVDELEPATEAPPLPPRGTpeHLAYVIYTSGST 2791
Cdd:cd05967  173 YKPL--------LDKALELSghkPHHVLVLNRPQVPADLTKPGRDLDWSELLAKAEPVDCVPVAAT--DPLYILYTSGTT 242

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2792 GKPKGVAIE---HRAALNTVVDlnTRFGVGPEDR---------VLGLSaltfdLSVYDVLGLLGAG-----GALVLPaae 2854
Cdd:cd05967  243 GKPKGVVRDnggHAVALNWSMR--NIYGIKPGDVwwaasdvgwVVGHS-----YIVYGPLLHGATTvlyegKPVGTP--- 312

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2855 aekDPAHWWERLVAGRVTVWNSTPALMLLL------VEYAEQRGLKlpaALRLVMLSGD--------WIPVALPdriral 2920
Cdd:cd05967  313 ---DPGAFWRVIEKYQVNALFTAPTAIRAIrkedpdGKYIKKYDLS---SLRTLFLAGErldpptleWAENTLG------ 380

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2921 grdVQVVSLGGATEaSIWSI-AYPIGQVAPQWKSIPYGMPLANQRFHVLDGRLEARPWWVPGELYIGGE---GLAREYWR 2996
Cdd:cd05967  381 ---VPVIDHWWQTE-TGWPItANPVGLEPLPIKAGSPGKPVPGYQVQVLDEDGEPVGPNELGNIVIKLPlppGCLLTLWK 456

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2997 DEPLTATRFIRHPRTgerLYRTGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPALS-ASVVVARGEPRG 3075
Cdd:cd05967  457 NDERFKKLYLSKFPG---YYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAeCAVVGVRDELKG 533

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 53747904 3076 vRRLVAYAVPRSGQTPAAGELRRYLA----ERLPAYMVPSAFVLLESLPRSRNGKIAR 3129
Cdd:cd05967  534 -QVPLGLVVLKEGVKITAEELEKELValvrEQIGPVAAFRLVIFVKRLPKTRSGKILR 590
PRK05852 PRK05852
fatty acid--CoA ligase family protein;
2648-3134 8.16e-15

fatty acid--CoA ligase family protein;


Pssm-ID: 235625 [Multi-domain]  Cd Length: 534  Bit Score: 80.70  E-value: 8.16e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2648 ARLHPELPALL-APERT-LSYGELARRAQALAARLRELEVQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLDPEQPPL 2725
Cdd:PRK05852   26 ATRLPEAPALVvTADRIaISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIA 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2726 RLHQLLEEGPARVVLTQSSLLH-----TVP-WPPGVQVIAVDELEPATEAP-------PLPPRGTPEHL----AYVIYTS 2788
Cdd:PRK05852  106 EQRVRSQAAGARVVLIDADGPHdraepTTRwWPLTVNVGGDSGPSGGTLSVhldaatePTPATSTPEGLrpddAMIMFTG 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2789 GSTGKPKGVAIEHRAALNTVVDLNTRFGVGPEDRVLGLSALTFDLSVYDVLGLLGAGGALVLPAAEAEKDPAHWWERLVA 2868
Cdd:PRK05852  186 GTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALLATLASGGAVLLPARGRFSAHTFWDDIKA 265

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2869 GRVTVWNSTPALMLLLVEYA-EQRGLKLPAALRLVM-LSGDWIP---VALPDRIRAlgrdvQVVSLGGATEASIWSIAYP 2943
Cdd:PRK05852  266 VGATWYTAVPTIHQILLERAaTEPSGRKPAALRFIRsCSAPLTAetaQALQTEFAA-----PVVCAFGMTEATHQVTTTQ 340

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2944 IGQVA----PQWKSIPYGMPLANQrFHVLDGRLEARPWWVPGELYIGGEGLAREYWRDEPLTATRFIrhprtgERLYRTG 3019
Cdd:PRK05852  341 IEGIGqtenPVVSTGLVGRSTGAQ-IRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANFT------DGWLRTG 413

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  3020 DQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPALSASVVVARGEPRGVRRLVAYAVPRSGQTPAAGELRRY 3099
Cdd:PRK05852  414 DLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPRESAPPTAEELVQF 493

                         490       500       510
                  ....*....|....*....|....*....|....*
gi 53747904  3100 LAERLPAYMVPSAFVLLESLPRSRNGKIARDQLPE 3134
Cdd:PRK05852  494 CRERLAAFEIPASFQEASGLPHTAKGSLDRRAVAE 528
PLN02860 PLN02860
o-succinylbenzoate-CoA ligase
 2723-3132 1.35e-14

o-succinylbenzoate-CoA ligase


Pssm-ID: 215464 [Multi-domain]  Cd Length: 563  Bit Score: 80.23  E-value: 1.35e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2723 PPLRLHQLLEEGPARVVLTQSSLLHTvpwppgvqviavDELEPATEAPPLP-PRGTPEHLAYVIYTSGSTGKPKGVAIEH 2801
Cdd:PLN02860  127 PSLMWQVFLESPSSSVFIFLNSFLTT------------EMLKQRALGTTELdYAWAPDDAVLICFTSGTTGRPKGVTISH 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2802 RAALNTVVDLNTRFGVGPEDRVL---------GLS-ALT-------------FDLSVydvlgllgaggalvlpAAEAEKD 2858
Cdd:PLN02860  195 SALIVQSLAKIAIVGYGEDDVYLhtaplchigGLSsALAmlmvgachvllpkFDAKA----------------ALQAIKQ 258

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2859 pahwwerlvaGRVTVWNSTPALMLLLVEYA-EQRGLKLPAALRLVMLSGDWIPVALPDRIRALGRDVQVVSLGGATEA-- 2935
Cdd:PLN02860  259 ----------HNVTSMITVPAMMADLISLTrKSMTWKVFPSVRKILNGGGSLSSRLLPDAKKLFPNAKLFSAYGMTEAcs 328

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2936 SIWSIAYPIGQVAPQWKSIPYGMPLANQRFHVLDGRLEARPwwVPG-ELYIGGEGLARE-------------YWRDEPLT 3001
Cdd:PLN02860  329 SLTFMTLHDPTLESPKQTLQTVNQTKSSSVHQPQGVCVGKP--APHvELKIGLDESSRVgriltrgphvmlgYWGQNSET 406

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  3002 ATRfirhpRTGERLYRTGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPALSASVVVARGEPRGVRRLVA 3081
Cdd:PLN02860  407 ASV-----LSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVA 481

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 53747904  3082 YAVPRSG------QTPAAG--------ELRRYLAER-LPAYMVPSAFVLLES-LPRSRNGKIARDQL 3132
Cdd:PLN02860  482 CVRLRDGwiwsdnEKENAKknltlsseTLRHHCREKnLSRFKIPKLFVQWRKpFPLTTTGKIRRDEV 548
Nitroreductase pfam00881
Nitroreductase family; The nitroreductase family comprises a group of FMN- or FAD-dependent ...
 3282-3455 1.39e-14

Nitroreductase family; The nitroreductase family comprises a group of FMN- or FAD-dependent and NAD(P)H-dependent enzymes able to metabolize nitrosubstituted compounds.


Pssm-ID: 425926 [Multi-domain]  Cd Length: 168  Bit Score: 74.35  E-value: 1.39e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   3282 LERRRSVRTYSLEPVSHEQLGRLLAplrewevQGSRrylYASAGGLYPVQLYLhLKPGRARglepgtWYYDPSTHRLVLL 3361
Cdd:pfam00881    1 IRQRRSVRKFDPEPVPKEVLEEILE-------AARR---APSAGNLQPWRFYV-VTDGELR------YRLAEAALELLLV 63

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   3362 SAGAGLDRRIHDPHQ----NQAIFDSAAFSLFLIARMGAVEPVYAEHALHFATLEAGLMTQLLDLGAAPSGLGLCHIGDL 3437
Cdd:pfam00881   64 EPAAALLLLLRRDANlkllLQDFLRGAPVLIVITASLSTYLRKAAERAYREALLDAGAAAQNLLLAATSLGLGSCPIGGF 143

                          170
                   ....*....|....*...
gi 53747904   3438 DFAQARGLFHLEEEHVLL 3455
Cdd:pfam00881  144 DAAAVRELLGLPDDERLV 161
AST1_like cd08247
AST1 is a cytoplasmic protein associated with the periplasmic membrane in yeast; This group ...
 1684-1885 1.52e-14

AST1 is a cytoplasmic protein associated with the periplasmic membrane in yeast; This group contains members identified in targeting of yeast membrane proteins ATPase. AST1 is a cytoplasmic protein associated with the periplasmic membrane in yeast, identified as a multicopy suppressor of pma1 mutants which cause temperature sensitive growth arrest due to the inability of ATPase to target to the cell surface. This family is homologous to the medium chain family of dehydrogenases and reductases. Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of an beta-alpha form and an N-terminal catalytic domain with distant homology to GroES.


Pssm-ID: 176209 [Multi-domain]  Cd Length: 352  Bit Score: 78.08  E-value: 1.52e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1684 ESLGLRRCTrpapGPRQVEIEVEAAGLNFLDVLGALGMMPALEAEESVLGRECSGRIAAVGEGV-SGLRVGDEVLAVAP- 1761
Cdd:cd08247   18 IKLPLPNCY----KDNEIVVKVHAAALNPVDLKLYNSYTFHFKVKEKGLGRDYSGVIVKVGSNVaSEWKVGDEVCGIYPh 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1762 -----GCFRSYVLVDESQ----VVRRPASLGLAEGAAQMVPFATAYFALHTVGR-LRRGERILIHAAAGGLGLAAVQLAS 1831
Cdd:cd08247   94 pyggqGTLSQYLLVDPKKdkksITRKPENISLEEAAAWPLVLGTAYQILEDLGQkLGPDSKVLVLGGSTSVGRFAIQLAK 173

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1832 RTGA--EILATAgSEQKREYLRSLGIAHVLDSRSTS---FVSEVRERTGGRG-VDVVLNS 1885
Cdd:cd08247  174 NHYNigTVVGTC-SSRSAELNKKLGADHFIDYDAHSgvkLLKPVLENVKGQGkFDLILDC 232
EntE COG1021
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ...
 2980-3132 1.85e-14

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: 79.42  E-value: 1.85e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2980 PGELYIGGEGLAREYWRDEPLTATRFirhprTGERLYRTGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQH 3059
Cdd:COG1021  380 VGELLTRGPYTIRGYYRAPEHNARAF-----TPDGFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAH 454

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 53747904 3060 PALSASVVVARGEPRGVRRLVAYAVPRsGQTPAAGELRRYLAER-LPAYMVPSAFVLLESLPRSRNGKIARDQL 3132
Cdd:COG1021  455 PAVHDAAVVAMPDEYLGERSCAFVVPR-GEPLTLAELRRFLRERgLAAFKLPDRLEFVDALPLTAVGKIDKKAL 527
PRK06018 PRK06018
putative acyl-CoA synthetase; Provisional
 2786-3134 2.04e-14

putative acyl-CoA synthetase; Provisional


Pssm-ID: 235673 [Multi-domain]  Cd Length: 542  Bit Score: 79.41  E-value: 2.04e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2786 YTSGSTGKPKGVAIEHRA-ALNTVVDLNTrfgvgpedRVLGLSALTFDLSVYDVLGLLGAGGALVLPAA-------EAEK 2857
Cdd:PRK06018  184 YTSGTTGDPKGVLYSHRSnVLHALMANNG--------DALGTSAADTMLPVVPLFHANSWGIAFSAPSMgtklvmpGAKL 255

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2858 DPAHWWERLVAGRVTVWNSTPALMLLLVEYAEQRGLKLPaALRLVMLSGDWIPVALpdrIRA-LGRDVQVVSLGGATEAS 2936
Cdd:PRK06018  256 DGASVYELLDTEKVTFTAGVPTVWLMLLQYMEKEGLKLP-HLKMVVCGGSAMPRSM---IKAfEDMGVEVRHAWGMTEMS 331

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2937 iwsiayPIGQVA---PQWKSIPY----------GMPLANQRFHVLDGRLEARPW--WVPGELYIGGEGLAREYWR--DEP 2999
Cdd:PRK06018  332 ------PLGTLAalkPPFSKLPGdarldvlqkqGYPPFGVEMKITDDAGKELPWdgKTFGRLKVRGPAVAAAYYRvdGEI 405

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  3000 LTATRFirhprtgerlYRTGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPALSASVVVARGEPRGVRRL 3079
Cdd:PRK06018  406 LDDDGF----------FDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERP 475

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 53747904  3080 VAYAVPRSGQTPAAGELRRYLAERLPAYMVPSAFVLLESLPRSRNGKIARDQLPE 3134
Cdd:PRK06018  476 LLIVQLKPGETATREEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALRE 530
MDR4 cd08270
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 1685-1982 2.32e-14

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176231 [Multi-domain]  Cd Length: 305  Bit Score: 77.03  E-value: 2.32e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1685 SLGLRRCTRPAPGPRQVEIEVEAAGLNFldvlGALGMMPALEAEEsVLGRECSGRIAAVGEGVSGLRVGDEVLA-VAPGC 1763
Cdd:cd08270   13 RLRLGEVPDPQPAPHEALVRVAAISLNR----GELKFAAERPDGA-VPGWDAAGVVERAAADGSGPAVGARVVGlGAMGA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1764 FRSYVLVDESQVVRRPASLGLAEGAAQMVPFATAYFALHTVGRLRrGERILIHAAAGGLGLAAVQLASRTGAEILATAGS 1843
Cdd:cd08270   88 WAELVAVPTGWLAVLPDGVSFAQAATLPVAGVTALRALRRGGPLL-GRRVLVTGASGGVGRFAVQLAALAGAHVVAVVGS 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1844 EQKREYLRSLGIAHVldsrstsfVSEVRERTGGRgVDVVLNSLAGELLLAGLSVLAPHGRFLELGKRD-----LYADQQV 1918
Cdd:cd08270  167 PARAEGLRELGAAEV--------VVGGSELSGAP-VDLVVDSVGGPQLARALELLAPGGTVVSVGSSSgepavFNPAAFV 237

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 53747904 1919 GLRTLARGQTFAAIDFGPHHPDFRAVLEEVAtqltQGQLEPLPTRLFPARQVAEAF-SFMARALH 1982
Cdd:cd08270  238 GGGGGRRLYTFFLYDGEPLAADLARLLGLVA----AGRLDPRIGWRGSWTEIDEAAeALLARRFR 298
Zn_ADH4 cd08258
Alcohol dehydrogenases of the MDR family; This group shares the zinc coordination sites of the ...
 1685-1883 2.81e-14

Alcohol dehydrogenases of the MDR family; This group shares the zinc coordination sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of an beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176219 [Multi-domain]  Cd Length: 306  Bit Score: 76.59  E-value: 2.81e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1685 SLGLRRCTRPAPGPRQVEIEVEAAGLNFLDVLgalgmmpALEAEE------SVLGRECSGRIAAVGEGVSGLRVGDEVLA 1758
Cdd:cd08258   13 NVELREVPEPEPGPGEVLIKVAAAGICGSDLH-------IYKGDYdpvetpVVLGHEFSGTIVEVGPDVEGWKVGDRVVS 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1759 VA--------PGC---------------------FRSYVLVDESQVVRRPASLGLaEGAAQMVPFATAYFALHTVGRLRR 1809
Cdd:cd08258   86 ETtfstcgrcPYCrrgdynlcphrkgigtqadggFAEYVLVPEESLHELPENLSL-EAAALTEPLAVAVHAVAERSGIRP 164

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 53747904 1810 GERILIhAAAGGLGLAAVQLASRTGAEILATaGSEQKREYL---RSLGIAHVlDSRSTSFVSEVRERTGGRGVDVVL 1883
Cdd:cd08258  165 GDTVVV-FGPGPIGLLAAQVAKLQGATVVVV-GTEKDEVRLdvaKELGADAV-NGGEEDLAELVNEITDGDGADVVI 238
sorbitol_DH cd05285
Sorbitol dehydrogenase; Sorbitol and aldose reductase are NAD(+) binding proteins of the ...
 1686-1883 3.82e-14

Sorbitol dehydrogenase; Sorbitol and aldose reductase are NAD(+) binding proteins of the polyol pathway, which interconverts glucose and fructose. Sorbitol dehydrogenase is tetrameric and has a single catalytic zinc per subunit. Aldose reductase catalyzes the NADP(H)-dependent conversion of glucose to sorbital, and SDH uses NAD(H) in the conversion of sorbitol to fructose. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. The medium chain alcohol dehydrogenase family (MDR) have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.


Pssm-ID: 176188 [Multi-domain]  Cd Length: 343  Bit Score: 76.76  E-value: 3.82e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1686 LGLRRCTRPAPGPRQVEIEVEAAGLNFLDVL----GALGMMPAleAEESVLGRECSGRIAAVGEGVSGLRVGDEV----- 1756
Cdd:cd05285   10 LRLEERPIPEPGPGEVLVRVRAVGICGSDVHyykhGRIGDFVV--KEPMVLGHESAGTVVAVGSGVTHLKVGDRVaiepg 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1757 ----------------------LAVAP--GCFRSYVLVDESQVVRRPASLGLAEGAaqMV-PFATayfALHTVGR--LRR 1809
Cdd:cd05285   88 vpcrtcefcksgrynlcpdmrfAATPPvdGTLCRYVNHPADFCHKLPDNVSLEEGA--LVePLSV---GVHACRRagVRP 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1810 GERILIhaaagglglaavqlasrTGA-----------------EILATAGSEQKREYLRSLGIAHVLDSRSTS---FVSE 1869
Cdd:cd05285  163 GDTVLV-----------------FGAgpiglltaavakafgatKVVVTDIDPSRLEFAKELGATHTVNVRTEDtpeSAEK 225

                        250
                 ....*....|....
gi 53747904 1870 VRERTGGRGVDVVL 1883
Cdd:cd05285  226 IAELLGGKGPDVVI 239
threonine_DH_like cd08234
L-threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
 1694-1882 3.86e-14

L-threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent formation of 2-amino-3-ketobutyrate from L-threonine, via NAD(H)-dependent oxidation. THD is a member of the zinc-requiring, medium chain NAD(H)-dependent alcohol dehydrogenase family (MDR). MDRs have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit. Sorbitol and aldose reductase are NAD(+) binding proteins of the polyol pathway, which interconverts glucose and fructose.


Pssm-ID: 176196 [Multi-domain]  Cd Length: 334  Bit Score: 76.80  E-value: 3.86e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1694 PAPGPRQVEIEVEAAGLNFLDVL---GALGMMPALeaeesVLGRECSGRIAAVGEGVSGLRVGDEVlAVAP--------- 1761
Cdd:cd08234   20 PEPGPDEVLIKVAACGICGTDLHiyeGEFGAAPPL-----VPGHEFAGVVVAVGSKVTGFKVGDRV-AVDPniycgecfy 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1762 --------------------GCFRSYVLVDESQVVRRPASLGLAEGAaqMV-PFATayfALHTVGRL--RRGERILI--- 1815
Cdd:cd08234   94 crrgrpnlcenltavgvtrnGGFAEYVVVPAKQVYKIPDNLSFEEAA--LAePLSC---AVHGLDLLgiKPGDSVLVfga 168

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 53747904 1816 ------HaaagglglaaVQLASRTGAEILATAG-SEQKREYLRSLGIAHVLDsrSTSFVSEVRERTGGRGVDVV 1882
Cdd:cd08234  169 gpigllL----------AQLLKLNGASRVTVAEpNEEKLELAKKLGATETVD--PSREDPEAQKEDNPYGFDVV 230
PRK12492 PRK12492
long-chain-fatty-acid--CoA ligase; Provisional
 2931-3135 3.91e-14

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


Pssm-ID: 171539 [Multi-domain]  Cd Length: 562  Bit Score: 78.71  E-value: 3.91e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2931 GATEASIWSIAYPIGQVApqwKSIPYGMPLANQRFHVLDGRLEARPWWVPGELYIGGEGLAREYWRDEPLTATRFirhpr 3010
Cdd:PRK12492  366 GLTETSPVASTNPYGELA---RLGTVGIPVPGTALKVIDDDGNELPLGERGELCIKGPQVMKGYWQQPEATAEAL----- 437

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  3011 TGERLYRTGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPALSASVVVARGEPRGVRRLVAYAVPRSGqT 3090
Cdd:PRK12492  438 DAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVVARDP-G 516

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 53747904  3091 PAAGELRRYLAERLPAYMVPSAFVLLESLPRSRNGKIARDQLPEP 3135
Cdd:PRK12492  517 LSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELRDI 561
ADH_zinc_N_2 pfam13602
Zinc-binding dehydrogenase;
1853-1988 4.20e-14

Zinc-binding dehydrogenase;


Pssm-ID: 433341 [Multi-domain]  Cd Length: 131  Bit Score: 71.59  E-value: 4.20e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   1853 LGIAHVLDSRSTSFVsevrERTGGRGVDVVLNSLAGELLLAGLSVLAPHGRFLELGKRDLYADqqVGLRTLAR-GQTFAA 1931
Cdd:pfam13602    1 LGADEVIDYRTTDFV----QATGGEGVDVVLDTVGGEAFEASLRVLPGGGRLVTIGGPPLSAG--LLLPARKRgGRGVKY 74

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 53747904   1932 IDFGPHHPDFRAVLEEVATQLTQGQLEPLPTRLFPARQVAEAFSFMARALHIGRVAV 1988
Cdd:pfam13602   75 LFLFVRPNLGADILQELADLIEEGKLRPVIDRVFPLEEAAEAHRYLESGRARGKIVL 131
AcpA COG3433
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ...
 2938-3216 6.65e-14

Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442659 [Multi-domain]  Cd Length: 295  Bit Score: 75.56  E-value: 6.65e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2938 WSIAYPIGQVAPQWKSIPYGMPLANQRFHVLDGRLEARPWWVPGELYIGGEGLAREYWRDEPLTATRFIRHPRTGERLYR 3017
Cdd:COG3433    1 IAIATPPPAPPTPDEPPPVIPPAIVQARALLLIVDLQGYFGGFGGEGGLLGAGLLLRIRLLAAAARAPFIPVPYPAQPGR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3018 TGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPALSASVVVARGEPRGVRRLVAYAVPRSGQTP-AAGEL 3096
Cdd:COG3433   81 QADDLRLLLRRGLGPGGGLERLVQQVVIRAERGEEEELLLVLRAAAVVRVAVLAALRGAGVGLLLIVGAVAALDgLAAAA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3097 RRYLAERLPAYMVPSAFVLLESLPRSRNGKIARDQLP-----EPQQTQGLAAQAAAADPLVERLAALVKEALRL--ERVE 3169
Cdd:COG3433  161 ALAALDKVPPDVVAASAVVALDALLLLALKVVARAAPalaaaEALLAAASPAPALETALTEEELRADVAELLGVdpEEID 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 53747904 3170 PQDSLLDLGADSVALIRLINRLEAElQFRPRLADIYENPTVQGLATL 3216
Cdd:COG3433  241 PDDNLFDLGLDSIRLMQLVERWRKA-GLDVSFADLAEHPTLAAWWAL 286
FACL_like_4 cd05944
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 2778-3132 6.76e-14

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: 76.37  E-value: 6.76e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2778 PEHLAYVIYTSGSTGKPKGVAIEH--RAALNTVVDLNTRFGvgPEDRVL-GLSALTFDLSVYDVLGLLGAGGALVLPAAE 2854
Cdd:cd05944    1 SDDVAAYFHTGGTTGTPKLAQHTHsnEVYNAWMLALNSLFD--PDDVLLcGLPLFHVNGSVVTLLTPLASGAHVVLAGPA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2855 AEKDPA---HWWERLVAGRVTVWNSTPALMLLLVEYAEQRGLklpAALRLVMLSGDWIPVALPDRIR-ALGrdVQVVSLG 2930
Cdd:cd05944   79 GYRNPGlfdNFWKLVERYRITSLSTVPTVYAALLQVPVNADI---SSLRFAMSGAAPLPVELRARFEdATG--LPVVEGY 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2931 GATEAS-IWSIAYPIGQVAPqwKSIPYGMPLANQRFHVLDG----RLEARPWWVpGELYIGGEGLAREYWRDEpltatrF 3005
Cdd:cd05944  154 GLTEATcLVAVNPPDGPKRP--GSVGLRLPYARVRIKVLDGvgrlLRDCAPDEV-GEICVAGPGVFGGYLYTE------G 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3006 IRHPRTGERLYRTGDQGRMLPEGSIEFLGR-EDLQVKvQGFRVELGEIEAALAQHPALSASVVVARGEPRGVRRLVAYAV 3084
Cdd:cd05944  225 NKNAFVADGWLNTGDLGRLDADGYLFITGRaKDLIIR-GGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQ 303

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 53747904 3085 PRSGQTPAAGELRRYLAERLPAY-MVPSAFVLLESLPRSRNGKIARDQL 3132
Cdd:cd05944  304 LKPGAVVEEEELLAWARDHVPERaAVPKHIEVLEELPVTAVGKVFKPAL 352
PRK05677 PRK05677
long-chain-fatty-acid--CoA ligase; Validated
 2931-3132 1.03e-13

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


Pssm-ID: 168170 [Multi-domain]  Cd Length: 562  Bit Score: 77.11  E-value: 1.03e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2931 GATEASiwsiayPIGQVAP----QWKSIpyGMPLANQRFHVLDGRLEARPWWVPGELYIGGEGLAREYWRDEPLTATRFi 3006
Cdd:PRK05677  359 GMTETS------PVVSVNPsqaiQVGTI--GIPVPSTLCKVIDDDGNELPLGEVGELCVKGPQVMKGYWQRPEATDEIL- 429

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  3007 rhprTGERLYRTGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPALSASVVVARGEPRGVRRLVAYAVPR 3086
Cdd:PRK05677  430 ----DSDGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVK 505

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 53747904  3087 SGQTPAAGELRRYLAERLPAYMVPSAFVLLESLPRSRNGKIARDQL 3132
Cdd:PRK05677  506 PGETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRREL 551
AAS_C cd05909
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ...
 2778-3127 1.25e-13

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: 76.60  E-value: 1.25e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2778 PEHLAYVIYTSGSTGKPKGVAIEHRAALNTVVDLNTRFGVGPEDRVLGlsAL----TFDLSVYDVLGLLGAGGALVLPAA 2853
Cdd:cd05909  146 PDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFG--ALpffhSFGLTGCLWLPLLSGIKVVFHPNP 223

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2854 -EAEKDPAHWWERlvagRVTVWNSTPALMLLLVEYAEQRGLklpAALRLVMLSGDwipvALPDRIRALGRD---VQVVSL 2929
Cdd:cd05909  224 lDYKKIPELIYDK----KATILLGTPTFLRGYARAAHPEDF---SSLRLVVAGAE----KLKDTLRQEFQEkfgIRILEG 292

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2930 GGATEAS-IWSIAYP-----IGQVapqwksipyGMPLANQRFHVLDGR-LEARPWWVPGELYIGGEGLAREYWRDEPLTA 3002
Cdd:cd05909  293 YGTTECSpVISVNTPqspnkEGTV---------GRPLPGMEVKIVSVEtHEEVPIGEGGLLLVRGPNVMLGYLNEPELTS 363

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3003 TRFirhprtGERLYRTGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQH-PALSASVVVA-----RGEprgv 3076
Cdd:cd05909  364 FAF------GDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSvpdgrKGE---- 433

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 53747904 3077 rRLVAYAVPRSgQTPAagELRRYLAE-RLPAYMVPSAFVLLESLPRSRNGKI 3127
Cdd:cd05909  434 -KIVLLTTTTD-TDPS--SLNDILKNaGISNLAKPSYIHQVEEIPLLGTGKP 481
PRK07786 PRK07786
long-chain-fatty-acid--CoA ligase; Validated
 2646-3134 1.56e-13

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


Pssm-ID: 169098 [Multi-domain]  Cd Length: 542  Bit Score: 76.74  E-value: 1.56e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2646 TQARLHPELPALLAPERTLSYGELARRAQALAARLRELEVQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLDPEQPPL 2725
Cdd:PRK07786   25 RHALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPP 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2726 RLHQLLEEGPARVVLTQSSLLHTVpwppgvqvIAVDELEP-----------------------ATEAPPLPPRGTPEHL- 2781
Cdd:PRK07786  105 EIAFLVSDCGAHVVVTEAALAPVA--------TAVRDIVPllstvvvaggssddsvlgyedllAEAGPAHAPVDIPNDSp 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2782 AYVIYTSGSTGKPKGVAIEHRAALNTVVDLNTRFGVGPEDRVLGLSALTFDLSVYDVLGLLGAGGALVLPAAEAEKDPAH 2861
Cdd:PRK07786  177 ALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGADINSDVGFVGVPLFHIAGIGSMLPGLLLGAPTVIYPLGAFDPGQ 256

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2862 WWERLVAGRVTVWNSTPALMLLLVEYAEQRGLKLpaALRLVMLSGDWIPVALPDRIRALGRDVQVVSLGGATEASiwsia 2941
Cdd:PRK07786  257 LLDVLEAEKVTGIFLVPAQWQAVCAEQQARPRDL--ALRVLSWGAAPASDTLLRQMAATFPEAQILAAFGQTEMS----- 329

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2942 yPI-----GQVAPQwKSIPYGMPLANQRFHVLDGRLEARPWWVPGELYIGGEGLAREYWRDEPLTATRFirhprtGERLY 3016
Cdd:PRK07786  330 -PVtcmllGEDAIR-KLGSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAF------AGGWF 401

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  3017 RTGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPALSASVVVARGEPRGVRRLVAYAVPRSGQTP-AAGE 3095
Cdd:PRK07786  402 HSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRNDDAAlTLED 481

                         490       500       510
                  ....*....|....*....|....*....|....*....
gi 53747904  3096 LRRYLAERLPAYMVPSAFVLLESLPRSRNGKIARDQLPE 3134
Cdd:PRK07786  482 LAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTELRE 520
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
1232-1350 1.83e-13

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 72.98  E-value: 1.83e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1232 ELEQLGAEVQVYTADVAEEAAVRSVVEQVHARWGKIHGVLHAAATFDDGVIQLRTHEQSSRALRTKVRGSMVLHEVLA-- 1309
Cdd:COG0300   48 ELRAAGARVEVVALDVTDPDAVAALAEAVLARFGPIDVLVNNAGVGGGGPFEELDLEDLRRVFEVNVFGPVRLTRALLpl 127

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 53747904 1310 --SEGLDWFALCSSLASALGSFGQADYCAANAFQDAYAHHLRR 1350
Cdd:COG0300  128 mrARGRGRIVNVSSVAGLRGLPGMAAYAASKAALEGFSESLRA 170
PRK12467 PRK12467
peptide synthase; Provisional
 2083-2468 5.17e-13

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 75.97  E-value: 5.17e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2083 PPSSLEQLIEQVWRKHLGVERVQPTDSFFQLGGDSLLGIQVAADLRRHlGVELPTATLFSHPTLAALAAALRARQGeaaa 2162
Cdd:PRK12467 2094 PQSELEQRLAAIWQDVLGLEQVGLHDNFFELGGDSIISIQVVSRARQA-GIRFTPKDLFQHQTVQSLAAVAQEGDG---- 2168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2163 ptapapALVPDPAARFEPFPLTDVQEAYwvgrrsaFELGGVAAHGYFE--IESPG--LEVERFIQCWRQLLQRHDMLRMV 2238
Cdd:PRK12467 2169 ------TVSIDQGPVTGDLPLLPIQQMF-------FADDIPERHHWNQsvLLEPReaLDAELLEAALQALLVHHDALRLG 2235

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2239 -VLPDGRQQVleqvpEYTPEVVELRGLSPQEAESRRLQLrERMAHQVLRS---DRWPLFELVLCRY-EGGVRIHMSMDAL 2313
Cdd:PRK12467 2236 fVQEDGGWSA-----MHRAPEQERRPLLWQVVVADKEEL-EALCEQAQRSldlEEGPLLRAVLATLpDGSQRLLLVIHHL 2309

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2314 MLDAWSSAVLRQDFAQLYHE--PGRPLEPLAIT--FRDYvlAERRlrEGEAHERA----RAYWWARLDTLPPPPELPLVK 2385
Cdd:PRK12467 2310 VVDGVSWRILLEDLQTAYRQlqGGQPVKLPAKTsaFKAW--AERL--QTYAASAAladeLGYWQAQLQGASTELPCDHPQ 2385

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2386 EPSQLEHARF--THREARlephrWAR--LQERARAHGLTPSAACMAAFAEVLARWSRHPRFTLNLTLFQRLPLHPQVD-- 2459
Cdd:PRK12467 2386 GGLQRRHAASvtTHLDSE-----WTRrlLQEAPAAYRTQVNDLLLTALARVIARWTGQASTLIQLEGHGREDLFDEIDlt 2460


                  ....*....
gi 53747904  2460 ELVGDFTSL 2468
Cdd:PRK12467 2461 RTVGWFTSL 2469
PKS_DH smart00826
Dehydratase domain in polyketide synthase (PKS) enzymes;
1400-1534 7.24e-13

Dehydratase domain in polyketide synthase (PKS) enzymes;


Pssm-ID: 214837  Cd Length: 167  Bit Score: 69.18  E-value: 7.24e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904    1400 EPGGTHWLGlTLRGGEDWVVDEHRLQGVPTLPGVAYLELARAACAQALGAEAVELAELLLLEPLTVPRGESRQVRVVLQP 1479
Cdd:smart00826   12 DGGGVVLTG-RLSLRTHPWLADHRVGGTVVLPGAAYVELALAAADEVGGGAPARLEELTLEAPLVLPEDGAVRVQVVVGA 90

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 53747904    1480 EGQAH--ALRVESRSEEARGWNEHARGRVRAVPRLAERIQPELLRAACEHEQPVPGE 1534
Cdd:smart00826   91 PDEDGrrTFTVYSRPDGDGPWTRHATGTLRPAAAAPAAPAADLAAWPPAGAEPVDVD 147
THR_DH_like cd08239
L-threonine dehydrogenase (TDH)-like; MDR/AHD-like proteins, including a protein annotated as ...
 1694-1979 7.54e-13

L-threonine dehydrogenase (TDH)-like; MDR/AHD-like proteins, including a protein annotated as a threonine dehydrogenase. L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent formation of 2-amino-3-ketobutyrate from L-threonine via NAD(H)-dependent oxidation. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Zinc-dependent ADHs are medium chain dehydrogenase/reductase type proteins (MDRs) and have a NAD(P)(H)-binding domain in a Rossmann fold of an beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. In addition to alcohol dehydrogenases, this group includes quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176201 [Multi-domain]  Cd Length: 339  Bit Score: 72.74  E-value: 7.54e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1694 PAPGPRQVEIEVEAAGLNFLDVLGALGMMPALEAEESVLGRECSGRIAAVGEGVSGLRVGDEVLAV-------------- 1759
Cdd:cd08239   20 PVPGPGEVLLRVKASGLCGSDLHYYYHGHRAPAYQGVIPGHEPAGVVVAVGPGVTHFRVGDRVMVYhyvgcgacrncrrg 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1760 ---------------APGCFRSYVLVDESQVVRRPASLGLAEGAAQMVPFATAYFALHTVGRLRRGeRILIHAAAGGLGL 1824
Cdd:cd08239  100 wmqlctskraaygwnRDGGHAEYMLVPEKTLIPLPDDLSFADGALLLCGIGTAYHALRRVGVSGRD-TVLVVGAGPVGLG 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1825 AAVQLASRTGAEILATAGSEQKREYLRSLGIAHVLDSRSTSfVSEVRERTGGRGVDVVLN-SLAGELLLAGLSVLAPHGR 1903
Cdd:cd08239  179 ALMLARALGAEDVIGVDPSPERLELAKALGADFVINSGQDD-VQEIRELTSGAGADVAIEcSGNTAARRLALEAVRPWGR 257

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1904 FLELGK---------RDLYADQqvglRTLARGQTFAAidfgphhPDFRAVLEEVATQLTqgQLEPLPTRLFPARQVAEAF 1974
Cdd:cd08239  258 LVLVGEggeltievsNDLIRKQ----RTLIGSWYFSV-------PDMEECAEFLARHKL--EVDRLVTHRFGLDQAPEAY 324


                 ....*
gi 53747904 1975 SFMAR 1979
Cdd:cd08239  325 ALFAQ 329
PRK09116 PRK09116
beta-ketoacyl-ACP synthase;
107-394 7.99e-13

beta-ketoacyl-ACP synthase;


Pssm-ID: 181657 [Multi-domain]  Cd Length: 405  Bit Score: 73.48  E-value: 7.99e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   107 ALEDAGLRPDQL--PGWVGVYVG--AGDTsyrfQLLRGHGDPLSgSKDVAGFFGN-Y----PDFLATRVAYKLNLRGPAL 177
Cdd:PRK09116   84 ALEDAGLLGDPIltDGRMGIAYGssTGST----DPIGAFGTMLL-EGSMSGITATtYvrmmPHTTAVNVGLFFGLKGRVI 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   178 GIHTACSTSLVSINMACSALRGFECDMALAGGVSLRLPARSGY---LYeegGVASKDGHC----RPFDARATGTVTGDGV 250
Cdd:PRK09116  159 PTSSACTSGSQGIGYAYEAIKYGYQTVMLAGGAEELCPTEAAVfdtLF---ATSTRNDAPeltpRPFDANRDGLVIGEGA 235

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   251 GVVVLKRLEDAlKARD-PIHAVIRGWALNNDGASragFTAPSVEGQSEVIALAHAAAGISARDITYVEAHGTGTPLGDPI 329
Cdd:PRK09116  236 GTLVLEELEHA-KARGaTIYAEIVGFGTNSDGAH---VTQPQAETMQIAMELALKDAGLAPEDIGYVNAHGTATDRGDIA 311

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 53747904   330 EVAALTRAFRAHTAdtafctLGAVKSNIGHLDAAAGVAGVIKTVQALRHRLIPPTLHFERPNPAL 394
Cdd:PRK09116  312 ESQATAAVFGARMP------ISSLKSYFGHTLGACGALEAWMSIEMMNEGWFAPTLNLTQVDPAC 370
PRK06710 PRK06710
long-chain-fatty-acid--CoA ligase; Validated
 2778-3134 9.16e-13

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


Pssm-ID: 180666 [Multi-domain]  Cd Length: 563  Bit Score: 74.30  E-value: 9.16e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2778 PEH-LAYVIYTSGSTGKPKGVAIEHRAAL-NTVVDLNTRFG-VGPEDRVLGLsaLTFdLSVYDVLGLLGAGGALVLPAAE 2854
Cdd:PRK06710  204 PENdLALLQYTGGTTGFPKGVMLTHKNLVsNTLMGVQWLYNcKEGEEVVLGV--LPF-FHVYGMTAVMNLSIMQGYKMVL 280

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2855 AEK-DPAHWWERLVAGRVTVWNSTPALMLLLVEYAEQRGLKLpAALRLVMLSGDWIPVALPDRIRALGRDvQVVSLGGAT 2933
Cdd:PRK06710  281 IPKfDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDI-SSIRACISGSAPLPVEVQEKFETVTGG-KLVEGYGLT 358

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2934 EAS-------IWSIAYPiGQVAPQWksipygmPLANQRFHVLDGRLEARPWWVpGELYIGGEGLAREYWRDEPLTATRFi 3006
Cdd:PRK06710  359 ESSpvthsnfLWEKRVP-GSIGVPW-------PDTEAMIMSLETGEALPPGEI-GEIVVKGPQIMKGYWNKPEETAAVL- 428

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  3007 rhprtGERLYRTGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPALSASVVVARGEPRGVRRLVAYAVPR 3086
Cdd:PRK06710  429 -----QDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLK 503

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 53747904  3087 SGQTPAAGELRRYLAERLPAYMVPSAFVLLESLPRSRNGKIARDQLPE 3134
Cdd:PRK06710  504 EGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVLIE 551
PRK06155 PRK06155
crotonobetaine/carnitine-CoA ligase; Provisional
 2636-3134 1.05e-12

crotonobetaine/carnitine-CoA ligase; Provisional


Pssm-ID: 235719 [Multi-domain]  Cd Length: 542  Bit Score: 74.02  E-value: 1.05e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2636 PSGRLEEGFFT-QARLHPELPALLAPERTLSYGELARRAQALAARLRELEVQPQELVAIAMHKGWEQATAVLGVLQAAAA 2714
Cdd:PRK06155   18 PSERTLPAMLArQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAI 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2715 YLPLDPEQPPLRLHQLLEEGPARVVLTQSSLLHTV-PWPPGV----QVIAVDElEPATEAP------PLPPRG------- 2776
Cdd:PRK06155   98 AVPINTALRGPQLEHILRNSGARLLVVEAALLAALeAADPGDlplpAVWLLDA-PASVSVPagwstaPLPPLDapapaaa 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2777 -TPEHLAYVIYTSGSTGKPKGVAIEHRA----ALNTVVDLntrfGVGPEDRVLGlsalTFDLSVYDVLGLLGAGGALVLP 2851
Cdd:PRK06155  177 vQPGDTAAILYTSGTTGPSKGVCCPHAQfywwGRNSAEDL----EIGADDVLYT----TLPLFHTNALNAFFQALLAGAT 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2852 AAEAEKDPAH-WWERLVAGRVTVWNSTPALMLLLV---EYAEQRGLKLPAALrlvmlsGDWIPVALPDRIRA-LGrdVQV 2926
Cdd:PRK06155  249 YVLEPRFSASgFWPAVRRHGATVTYLLGAMVSILLsqpARESDRAHRVRVAL------GPGVPAALHAAFRErFG--VDL 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2927 VSLGGATEASiwsiaYPIGQVAPQWKsiPYGMPLANQRFH--VLDGRLEARPWWVPGELyiggegLAREywrDEPLT-AT 3003
Cdd:PRK06155  321 LDGYGSTETN-----FVIAVTHGSQR--PGSMGRLAPGFEarVVDEHDQELPDGEPGEL------LLRA---DEPFAfAT 384

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  3004 RFIRHPRTGERLYR-----TGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPALSASVVVARGEPRGVRR 3078
Cdd:PRK06155  385 GYFGMPEKTVEAWRnlwfhTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDE 464

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 53747904  3079 LVAYAVPRSGQTPAAGELRRYLAERLPAYMVPSAFVLLESLPRSRNGKIARDQLPE 3134
Cdd:PRK06155  465 VMAAVVLRDGTALEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLRE 520
PRK09274 PRK09274
peptide synthase; Provisional
 2761-3132 1.47e-12

peptide synthase; Provisional


Pssm-ID: 236443 [Multi-domain]  Cd Length: 552  Bit Score: 73.39  E-value: 1.47e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2761 DELEPATEAPPLPPRGTPEH-LAYVIYTSGSTGKPKGVAIEHRAALNTVVDLNTRFGVGPEDRVLGlsalTFDL-SVYDV 2838
Cdd:PRK09274  155 ATLLRDGAAAPFPMADLAPDdMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDLP----TFPLfALFGP 230

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2839 LGLLGAGGALVLPAAEAEKDPAHWWERLVAGRVTVWNSTPALMLLLVEYAEQRGLKLPaALRLVMLSGDWIPVALPDRIR 2918
Cdd:PRK09274  231 ALGMTSVIPDMDPTRPATVDPAKLFAAIERYGVTNLFGSPALLERLGRYGEANGIKLP-SLRRVISAGAPVPIAVIERFR 309

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2919 A-LGRDVQVVSLGGATEA----SIWS------------------IAYPIGQVapQWKSIpygmPLANQRFHVLDGRLEAR 2975
Cdd:PRK09274  310 AmLPPDAEILTPYGATEAlpisSIESreilfatraatdngagicVGRPVDGV--EVRII----AISDAPIPEWDDALRLA 383

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2976 PWWVpGELYIGGEGLAREY-WRDEpltATRF--IRHPRTGERlYRTGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEI 3052
Cdd:PRK09274  384 TGEI-GEIVVAGPMVTRSYyNRPE---ATRLakIPDGQGDVW-HRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPC 458

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  3053 EAALAQHPALSASVVVARGEPRGVRRLVAYAvPRSGQTPAAGELR---RYLAERLPAYMVPSAFVLLESLP---RsRNGK 3126
Cdd:PRK09274  459 ERIFNTHPGVKRSALVGVGVPGAQRPVLCVE-LEPGVACSKSALYqelRALAAAHPHTAGIERFLIHPSFPvdiR-HNAK 536


                  ....*.
gi 53747904  3127 IARDQL 3132
Cdd:PRK09274  537 IFREKL 542
CLF cd00832
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ...
 94-431 1.53e-12

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: 72.39  E-value: 1.53e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   94 DPQQRLLLECSWEALEDAGLRPDQLPGW-VGVYVGAGDTSYRF-----QLLRGHGDP-LSGSKDVAGFFGNYPDFLATRv 166
Cdd:cd00832   69 DRMTRLALAAADWALADAGVDPAALPPYdMGVVTASAAGGFEFgqrelQKLWSKGPRhVSAYQSFAWFYAVNTGQISIR- 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  167 aykLNLRGPALGIHTACSTSLVSINMACSALRGfECDMALAGGVSLRLPARSGYLYEEGGVASKDGH----CRPFDARAT 242
Cdd:cd00832  148 ---HGMRGPSGVVVAEQAGGLDALAQARRLVRR-GTPLVVSGGVDSALCPWGWVAQLSSGRLSTSDDparaYLPFDAAAA 223

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  243 GTVTGDGVGVVVLKRLEDALKARDPIHAVIRGWALNNDGASRAGftapSVEGQSEVIALAHAAAGISARDITYVEAHGTG 322
Cdd:cd00832  224 GYVPGEGGAILVLEDAAAARERGARVYGEIAGYAATFDPPPGSG----RPPGLARAIRLALADAGLTPEDVDVVFADAAG 299

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  323 TPLGDPIEVAALTRAFRAHTADTAfctlgAVKSNIGHLDAAAGVAGVIKTVQALRHRLIPPTLHFERPNPALHLEqspfF 402
Cdd:cd00832  300 VPELDRAEAAALAAVFGPRGVPVT-----APKTMTGRLYAGGAPLDVATALLALRDGVIPPTVNVTDVPPAYGLD----L 370

                        330       340
                 ....*....|....*....|....*....
gi 53747904  403 VNTQPLPWEsprgPRLAGVSSFGIGGTNA 431
Cdd:cd00832  371 VTGRPRPAA----LRTALVLARGRGGFNS 395
Zn_ADH_class_III cd08279
Class III alcohol dehydrogenase; Glutathione-dependent formaldehyde dehydrogenases (FDHs, ...
 1694-1883 1.73e-12

Class III alcohol dehydrogenase; Glutathione-dependent formaldehyde dehydrogenases (FDHs, Class III ADH) are members of the zinc-dependent/medium chain alcohol dehydrogenase family. FDH converts formaldehyde and NAD(P) to formate and NAD(P)H. The initial step in this process the spontaneous formation of a S-(hydroxymethyl)glutathione adduct from formaldehyde and glutathione, followed by FDH-mediated oxidation (and detoxification) of the adduct to S-formylglutathione. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. Class III ADH are also known as glutathione-dependent formaldehyde dehydrogenase (FDH), which convert aldehydes to corresponding carboxylic acid and alcohol. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of an beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding.


Pssm-ID: 176240 [Multi-domain]  Cd Length: 363  Bit Score: 72.19  E-value: 1.73e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1694 PAPGPRQVEIEVEAAGL-----NFLDvlGALG-MMPAleaeesVLGRECSGRIAAVGEGVSGLRVGDEV-LAVAPGC--- 1763
Cdd:cd08279   21 DDPGPGEVLVRIAAAGLchsdlHVVT--GDLPaPLPA------VLGHEGAGVVEEVGPGVTGVKPGDHVvLSWIPACgtc 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1764 --------------------------------------------FRSYVLVDESQVVRRPASLGLAEGAAQMVPFATAYF 1799
Cdd:cd08279   93 rycsrgqpnlcdlgagilggqlpdgtrrftadgepvgamcglgtFAEYTVVPEASVVKIDDDIPLDRAALLGCGVTTGVG 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1800 ALHTVGRLRRGERILIhaaaggLGLAAVQLASRTGAEIlATAG-------SEQKREYLRSLGIAHVLDSRSTSFVSEVRE 1872
Cdd:cd08279  173 AVVNTARVRPGDTVAV------IGCGGVGLNAIQGARI-AGASriiavdpVPEKLELARRFGATHTVNASEDDAVEAVRD 245

                        250
                 ....*....|.
gi 53747904 1873 RTGGRGVDVVL 1883
Cdd:cd08279  246 LTDGRGADYAF 256
ACS cd05966
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ...
 2731-3129 1.82e-12

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: 73.36  E-value: 1.82e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2731 LEEGPA-RVVLTQSSLLHTVPWPPGVQVIAVDELE-PATEAPPLPPrgTPEHLAYVIYTSGSTGKPKGVaiEHRAA---L 2805
Cdd:cd05966  183 LEKCPSvEKVLVVKRTGGEVPMTEGRDLWWHDLMAkQSPECEPEWM--DSEDPLFILYTSGSTGKPKGV--VHTTGgylL 258

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2806 NTVVDLNTRFGVGPEDRV---------------------LGLSALTFDlsvydvlgllgaggalvlpAAEAEKDPAHWWE 2864
Cdd:cd05966  259 YAATTFKYVFDYHPDDIYwctadigwitghsyivygplaNGATTVMFE-------------------GTPTYPDPGRYWD 319

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2865 RLVAGRVTVWnstpalmlllveYAEqrglklPAALRLVMLSGDWIPVALpDR--IRALG--------------------R 2922
Cdd:cd05966  320 IVEKHKVTIF------------YTA------PTAIRALMKFGDEWVKKH-DLssLRVLGsvgepinpeawmwyyevigkE 380

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2923 DVQVVS--------------LGGATEASIWSIAYPIGQVAPQwksI--PYGMPLANQRfhvlDGRLEA-RPWwvPGelyi 2985
Cdd:cd05966  381 RCPIVDtwwqtetggimitpLPGATPLKPGSATRPFFGIEPA---IldEEGNEVEGEV----EGYLVIkRPW--PG---- 447

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2986 ggegLAREYWRDEpltaTRFIR---HPRTGerLYRTGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPAL 3062
Cdd:cd05966  448 ----MARTIYGDH----ERYEDtyfSKFPG--YYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAV 517

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3063 SASVVVARGEPRGVRRLVAYAVPRSGQTPA---AGELRRYLAERLPAYMVPSAFVLLESLPRSRNGKIAR 3129
Cdd:cd05966  518 AEAAVVGRPHDIKGEAIYAFVTLKDGEEPSdelRKELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMR 587
CAD_like cd08296
Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the ...
 1694-1908 2.20e-12

Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the medium chain dehydrogenase/reductase family, reduce cinnamaldehydes to cinnamyl alcohols in the last step of monolignal metabolism in plant cells walls. CAD binds 2 zinc ions and is NADPH- dependent. CAD family members are also found in non-plant species, e.g. in yeast where they have an aldehyde reductase activity. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADHs), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176256 [Multi-domain]  Cd Length: 333  Bit Score: 71.51  E-value: 2.20e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1694 PAPGPRQVEIEVEAAGLNFLDVLGALGMMPALEaEESVLGRECSGRIAAVGEGVSGLRVGDEVlAVA------------- 1760
Cdd:cd08296   21 PLPGPGEVLIKVEACGVCHSDAFVKEGAMPGLS-YPRVPGHEVVGRIDAVGEGVSRWKVGDRV-GVGwhgghcgtcdacr 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1761 -----------------PGCFRSYVLVDESQVVRRPASLGLAEGAAQMVPFATAYFALHTVGrLRRGERILI-------H 1816
Cdd:cd08296   99 rgdfvhcengkvtgvtrDGGYAEYMLAPAEALARIPDDLDAAEAAPLLCAGVTTFNALRNSG-AKPGDLVAVqgigglgH 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1817 AaagglglaAVQLASRTGAEILATAGSEQKREYLRSLGIAHVLDSRSTSFVSEVRErTGgrGVDVVLNSLAGELL-LAGL 1895
Cdd:cd08296  178 L--------AVQYAAKMGFRTVAISRGSDKADLARKLGAHHYIDTSKEDVAEALQE-LG--GAKLILATAPNAKAiSALV 246

                        250
                 ....*....|...
gi 53747904 1896 SVLAPHGRFLELG 1908
Cdd:cd08296  247 GGLAPRGKLLILG 259
PRK08308 PRK08308
acyl-CoA synthetase; Validated
 3010-3133 2.20e-12

acyl-CoA synthetase; Validated


Pssm-ID: 236231 [Multi-domain]  Cd Length: 414  Bit Score: 72.38  E-value: 2.20e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  3010 RTGERLYRTGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPALSASVVVARGEPRGVRRLVAYAVPRSGQ 3089
Cdd:PRK08308  287 KMGDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVISHEEI 366

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 53747904  3090 TPAagELRRYLAERLPAYMVPSAFVLLESLPRSRNGKIARDQLP 3133
Cdd:PRK08308  367 DPV--QLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLLE 408
PRK06188 PRK06188
acyl-CoA synthetase; Validated
 2651-3132 2.48e-12

acyl-CoA synthetase; Validated


Pssm-ID: 235731 [Multi-domain]  Cd Length: 524  Bit Score: 72.71  E-value: 2.48e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2651 HPELPALLAPERTLSYGELARRAQALAARLRELEVQPQELVAI--------------AMHKGWeQATAV--LGVLQ---- 2710
Cdd:PRK06188   25 YPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALlslnrpevlmaigaAQLAGL-RRTALhpLGSLDdhay 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2711 ----AAAAYLPLDPEQPPLRLHQLLEEGParvvltqsSLLHTVPWPPGVqvIAVDELEPATEAPPLP--PRGTPEHLAYV 2784
Cdd:PRK06188  104 vledAGISTLIVDPAPFVERALALLARVP--------SLKHVLTLGPVP--DGVDLLAAAAKFGPAPlvAAALPPDIAGL 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2785 IYTSGSTGKPKGVAIEHRAALNTVVDLNTRFGVGPEDRVLGLSALTFDLSVYDVLGLLGAGGALVLPAAeaekDPAHWWE 2864
Cdd:PRK06188  174 AYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSHAGGAFFLPTLLRGGTVIVLAKF----DPAEVLR 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2865 RLVAGRVTVWNSTPALMLLLVEYAEQRGLKLPAaLRLVMLSGDWI-PVALPDRIRALGrdvQVVS-LGGATEAsiwsiAY 2942
Cdd:PRK06188  250 AIEEQRITATFLVPTMIYALLDHPDLRTRDLSS-LETVYYGASPMsPVRLAEAIERFG---PIFAqYYGQTEA-----PM 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2943 PIGQVAPQ--WKSIPY-----GMPLANQRFHVLDGRLEARPWWVPGELYIGGEGLAREYWRDEPLTATRFirhpRTGerL 3015
Cdd:PRK06188  321 VITYLRKRdhDPDDPKrltscGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAF----RDG--W 394

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  3016 YRTGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPALSASVVVARGEPRGVRRLVAYAVPRSGQTPAAGE 3095
Cdd:PRK06188  395 LHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPGAAVDAAE 474

                         490       500       510
                  ....*....|....*....|....*....|....*..
gi 53747904  3096 LRRYLAERLPAYMVPSAFVLLESLPRSRNGKIARDQL 3132
Cdd:PRK06188  475 LQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKAL 511
TDH cd05281
Threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
 1694-1883 3.84e-12

Threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent formation of 2-amino-3-ketobutyrate from L-threonine via NAD(H)- dependent oxidation. THD is a member of the zinc-requiring, medium chain NAD(H)-dependent alcohol dehydrogenase family (MDR). MDRs have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria) and have 2 tightly bound zinc atoms per subunit. Sorbitol and aldose reductase are NAD(+) binding proteins of the polyol pathway, which interconverts glucose and fructose.


Pssm-ID: 176184 [Multi-domain]  Cd Length: 341  Bit Score: 70.73  E-value: 3.84e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1694 PAPGPRQVEIEVEAAGLNFLDV-------LGALGMMPALeaeesVLGRECSGRIAAVGEGVSGLRVGD------------ 1754
Cdd:cd05281   21 PKPGPGEVLIKVLAASICGTDVhiyewdeWAQSRIKPPL-----IFGHEFAGEVVEVGEGVTRVKVGDyvsaethivcgk 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1755 ---------------EVLAV-APGCFRSYVLVDESQVVRRPASLGLaEGAAQMVPFATAyfaLHTV--GRLRrGERILIh 1816
Cdd:cd05281   96 cyqcrtgnyhvcqntKILGVdTDGCFAEYVVVPEENLWKNDKDIPP-EIASIQEPLGNA---VHTVlaGDVS-GKSVLI- 169

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 53747904 1817 AAAGGLGLAAVQLASRTGAE-ILATAGSEQKREYLRSLGIAHVLDSRSTSfVSEVRERTGGRGVDVVL 1883
Cdd:cd05281  170 TGCGPIGLMAIAVAKAAGASlVIASDPNPYRLELAKKMGADVVINPREED-VVEVKSVTDGTGVDVVL 236
PRK07824 PRK07824
o-succinylbenzoate--CoA ligase;
2782-3132 6.00e-12

o-succinylbenzoate--CoA ligase;


Pssm-ID: 236108 [Multi-domain]  Cd Length: 358  Bit Score: 70.46  E-value: 6.00e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2782 AYVIYTSGSTGKPKGvAIEHRAALNTVVDLNTRFGVGPEDRVLGLSA-------------------LTFDLSvydvlgll 2842
Cdd:PRK07824   38 ALVVATSGTTGTPKG-AMLTAAALTASADATHDRLGGPGQWLLALPAhhiaglqvlvrsviagsepVELDVS-------- 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2843 GAGGALVLPAAEAEKDPAHWWERLVAgrvtvwnstpalMLLLVEYAEQRGLKLPAALRLVMLSGDWIPVALPDRIRALGr 2922
Cdd:PRK07824  109 AGFDPTALPRAVAELGGGRRYTSLVP------------MQLAKALDDPAATAALAELDAVLVGGGPAPAPVLDAAAAAG- 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2923 dVQVVSLGGATEASIwsiaypiGQVapqwksipY-GMPLANQRFHVLDGRLEarpwwvpgelyIGGEGLAREYwRDEPlt 3001
Cdd:PRK07824  176 -INVVRTYGMSETSG-------GCV--------YdGVPLDGVRVRVEDGRIA-----------LGGPTLAKGY-RNPV-- 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  3002 atrfIRHPRTGERLYRTGDQGrMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPALSASVVVARGEPRGVRRLVA 3081
Cdd:PRK07824  226 ----DPDPFAEPGWFRTDDLG-ALDDGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVA 300

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 53747904  3082 YAVPRSGQTPAAGELRRYLAERLPAYMVPSAFVLLESLPRSRNGKIARDQL 3132
Cdd:PRK07824  301 AVVGDGGPAPTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRAL 351
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
 2083-2145 1.21e-11

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: 62.95  E-value: 1.21e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 53747904 2083 PPSSLEQLIEQVWRKHLGV--ERVQPTDSFFQ-LGGDSLLGIQVAADLRRHLGVELPTATLFSHPT 2145
Cdd:COG0236    2 PREELEERLAEIIAEVLGVdpEEITPDDSFFEdLGLDSLDAVELIAALEEEFGIELPDTELFEYPT 67
starter-C_NRPS cd19533
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ...
 2182-2518 1.22e-11

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: 70.09  E-value: 1.22e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2182 PLTDVQEAYWVGRRSAFELGGVAAHGYFEIESPgLEVERFIQCWRQLLQRHDMLRM--VVLPDGRQQVLEQVPEYTPEVV 2259
Cdd:cd19533    3 PLTSAQRGVWFAEQLDPEGSIYNLAEYLEITGP-VDLAVLERALRQVIAEAETLRLrfTEEEGEPYQWIDPYTPVPIRHI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2260 ELRGLSPQEAESRRLqLRERMAHQVLRSDRwPLFELVLCRYEGG-----VRIHMsmdaLMLDAWSSAVLRQDFAQLYHE- 2333
Cdd:cd19533   82 DLSGDPDPEGAAQQW-MQEDLRKPLPLDND-PLFRHALFTLGDNrhfwyQRVHH----IVMDGFSFALFGQRVAEIYTAl 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2334 -PGRPLEPLAIT-FRDYVLAERRLREGEAHERARAYWwarLDTLPPPPELPLVKEPSQLEHARFTHREARLEPHRWARLQ 2411
Cdd:cd19533  156 lKGRPAPPAPFGsFLDLVEEEQAYRQSERFERDRAFW---TEQFEDLPEPVSLARRAPGRSLAFLRRTAELPPELTRTLL 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2412 ERARAHGLTPSAACMAAFAEVLARWSRHPRFTLNLTLFQRlpLHPQVDELVGDFTSLVLLEVEAHAASTFAERASRLQAQ 2491
Cdd:cd19533  233 EAAEAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGR--LGAAARQTPGMVANTLPLRLTVDPQQTFAELVAQVSRE 310

                        330       340
                 ....*....|....*....|....*..
gi 53747904 2492 LWRDLEHGSVSAVQLIRELVRTGRRSP 2518
Cdd:cd19533  311 LRSLLRHQRYRYEDLRRDLGLTGELHP 337
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
 2089-2145 1.30e-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: 62.20  E-value: 1.30e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 53747904   2089 QLIEQVWRKHLGV--ERVQPTDSFFQLGGDSLLGIQVAADLRRHLGVELPTATLFSHPT 2145
Cdd:pfam00550    1 ERLRELLAEVLGVpaEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPT 59
PRK07788 PRK07788
acyl-CoA synthetase; Validated
 2752-3134 1.50e-11

acyl-CoA synthetase; Validated


Pssm-ID: 236097 [Multi-domain]  Cd Length: 549  Bit Score: 70.34  E-value: 1.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2752 PPGVQVIAVDELEPATEAPPLPPRGTPEHLayVIYTSGSTGKPKGVAIEHRAALNTVVDLNTR--FGVG-------PEDR 2822
Cdd:PRK07788  182 PSGSTDETLDDLIAGSSTAPLPKPPKPGGI--VILTSGTTGTPKGAPRPEPSPLAPLAGLLSRvpFRAGettllpaPMFH 259

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2823 VLGLSALTFDLSVYDVLGLLGAGgalvlpaaeaekDPAHWWERLVAGRVTVWNSTPaLMLllveyaeQRGLKLPA----- 2897
Cdd:PRK07788  260 ATGWAHLTLAMALGSTVVLRRRF------------DPEATLEDIAKHKATALVVVP-VML-------SRILDLGPevlak 319

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2898 ----ALRLVMLSGDWIPVALPDRIRALGRDVqVVSLGGATEASIWSIAYPI------GQVAPqwksIPYGMPLAnqrfhV 2967
Cdd:PRK07788  320 ydtsSLKIIFVSGSALSPELATRALEAFGPV-LYNLYGSTEVAFATIATPEdlaeapGTVGR----PPKGVTVK-----I 389

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2968 LDGRLEARPWWVPGELYIGGEGLAREYwrdeplTATRfirHPRTGERLYRTGDQGRMLPEGSIEFLGREDLQVKVQGFRV 3047
Cdd:PRK07788  390 LDENGNEVPRGVVGRIFVGNGFPFEGY------TDGR---DKQIIDGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENV 460

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  3048 ELGEIEAALAQHPALSASVVVARGEPRGVRRLVAYAVPRSGQTPAAGELRRYLAERLPAYMVPSAFVLLESLPRSRNGKI 3127
Cdd:PRK07788  461 FPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPGAALDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKV 540


                  ....*..
gi 53747904  3128 ARDQLPE 3134
Cdd:PRK07788  541 LKRELRE 547
MDR_TM0436_like cd08231
Hypothetical enzyme TM0436 resembles the zinc-dependent alcohol dehydrogenases (ADH); This ...
 1694-1988 1.59e-11

Hypothetical enzyme TM0436 resembles the zinc-dependent alcohol dehydrogenases (ADH); This group contains the hypothetical TM0436 alcohol dehydrogenase from Thermotoga maritima, proteins annotated as 5-exo-alcohol dehydrogenase, and other members of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family. MDR, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability.


Pssm-ID: 176193 [Multi-domain]  Cd Length: 361  Bit Score: 69.21  E-value: 1.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1694 PAPGPRQVEIEVEAAGLNFLDV---LGALGMMPAleaeESVLGRECSGRIAAVGEGVS------GLRVGDEV-------- 1756
Cdd:cd08231   21 PDLEPGAVLVRVRLAGVCGSDVhtvAGRRPRVPL----PIILGHEGVGRVVALGGGVTtdvagePLKVGDRVtwsvgapc 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1757 ------------------------LAVAP---GCFRSYVLVDESQ-VVRRPASLGLAEGAAQMVPFATAYFALHTVGRLR 1808
Cdd:cd08231   97 grcyrclvgdptkcenrkkygheaSCDDPhlsGGYAEHIYLPPGTaIVRVPDNVPDEVAAPANCALATVLAALDRAGPVG 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1809 RGERILIHAAAGGLGLAAVQLASRTGAEILATAGSEQKREYLRSLGIAHVLDSRSTSFVSE---VRERTGGRGVDVVLN- 1884
Cdd:cd08231  177 AGDTVVVQGAGPLGLYAVAAAKLAGARRVIVIDGSPERLELAREFGADATIDIDELPDPQRraiVRDITGGRGADVVIEa 256

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1885 SLAGELLLAGLSVLAPHGRFLELGKRDLYADQQVGLRTLARGQ-TFAaidfGPHHPDFRAVLEEVATQLTQGQLEP---L 1960
Cdd:cd08231  257 SGHPAAVPEGLELLRRGGTYVLVGSVAPAGTVPLDPERIVRKNlTII----GVHNYDPSHLYRAVRFLERTQDRFPfaeL 332

                        330       340
                 ....*....|....*....|....*...
gi 53747904 1961 PTRLFPARQVAEAFSFMaRALHIGRVAV 1988
Cdd:cd08231  333 VTHRYPLEDINEALELA-ESGTALKVVI 359
ETR_like_2 cd08292
2-enoyl thioester reductase (ETR) like proteins, child 2; 2-enoyl thioester reductase (ETR) ...
 1693-1908 2.02e-11

2-enoyl thioester reductase (ETR) like proteins, child 2; 2-enoyl thioester reductase (ETR) like proteins. ETR catalyzes the NADPH-dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the 2-enoyl thioester reductase (ETR) like proteins. ETR catalyzes the NADPH-dependent dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains, at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. Candida tropicalis enoyl thioester reductase (Etr1p) catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis. Etr1p forms homodimers, with each subunit containing a nucleotide-binding Rossmann fold domain and a catalytic domain.


Pssm-ID: 176252 [Multi-domain]  Cd Length: 324  Bit Score: 68.13  E-value: 2.02e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1693 RPAPGPRQVEIEVEAAGLNFLDVL---GALGMMPALEAeesVLGRECSGRIAAVGEGVSGLRVGDEVlAVAP--GCFRSY 1767
Cdd:cd08292   23 KPTPGAGEVLVRTTLSPIHNHDLWtirGTYGYKPELPA---IGGSEAVGVVDAVGEGVKGLQVGQRV-AVAPvhGTWAEY 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1768 VLVDESQVVRRPASLGLaEGAAQMV--PFaTAYFALHTVGrLRRGERILIHAAAGGLGLAAVQLASRTGAEILATAGSEQ 1845
Cdd:cd08292   99 FVAPADGLVPLPDGISD-EVAAQLIamPL-SALMLLDFLG-VKPGQWLIQNAAGGAVGKLVAMLAAARGINVINLVRRDA 175

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 53747904 1846 KREYLRSLGIAHVLDSRSTSFVSEVRERTGGRGVDVVLNSLAGELLLAGLSVLAPHGRFLELG 1908
Cdd:cd08292  176 GVAELRALGIGPVVSTEQPGWQDKVREAAGGAPISVALDSVGGKLAGELLSLLGEGGTLVSFG 238
ETR cd08290
2-enoyl thioester reductase (ETR); 2-enoyl thioester reductase (ETR) catalyzes the ...
 1694-1811 2.19e-11

2-enoyl thioester reductase (ETR); 2-enoyl thioester reductase (ETR) catalyzes the NADPH-dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains, at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. Candida tropicalis enoyl thioester reductase (Etr1p) catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis. Etr1p forms homodimers, with each subunit containing a nucleotide-binding Rossmann fold domain and a catalytic domain.


Pssm-ID: 176250 [Multi-domain]  Cd Length: 341  Bit Score: 68.40  E-value: 2.19e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1694 PAPGPRQVEIEVEAAGLNFLDVL---GALGMMPALEAE-ESVLGRECSGRIAAVGEGVSGLRVGDEVLAVAPGC--FRSY 1767
Cdd:cd08290   25 PPGPPNEVLVKMLAAPINPADINqiqGVYPIKPPTTPEpPAVGGNEGVGEVVKVGSGVKSLKPGDWVIPLRPGLgtWRTH 104

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 53747904 1768 VLVDESQVVRRPASLGLAEGAAQMVPFATAYFALHTVGRLRRGE 1811
Cdd:cd08290  105 AVVPADDLIKVPNDVDPEQAATLSVNPCTAYRLLEDFVKLQPGD 148
PRK13382 PRK13382
bile acid CoA ligase;
2643-3135 2.84e-11

bile acid CoA ligase;


Pssm-ID: 172019 [Multi-domain]  Cd Length: 537  Bit Score: 69.40  E-value: 2.84e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2643 GFFTQARLHPELPALLAPERTLSYGELARRAQALAARLRELEVQPQELVAIAM--HKGWEQATAVLGVLQAAAAYLPLDP 2720
Cdd:PRK13382   48 GFAIAAQRCPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCrnHRGFVEALLAANRIGADILLLNTSF 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2721 EQPPLRlhQLLEEGPARVVLTQSSLLHTVP--------------WPPGVQVIAVDEL--EPATEAPPlpprGTPEHLAYV 2784
Cdd:PRK13382  128 AGPALA--EVVTREGVDTVIYDEEFSATVDraladcpqatrivaWTDEDHDLTVEVLiaAHAGQRPE----PTGRKGRVI 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2785 IYTSGSTGKPKGVaieHRAALNTVVDLN------------TRFGVGPEDRVLGLSALTFDLSVydvlgllgaggalVLPA 2852
Cdd:PRK13382  202 LLTSGTTGTPKGA---RRSGPGGIGTLKaildrtpwraeePTVIVAPMFHAWGFSQLVLAASL-------------ACTI 265

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2853 AEAEK-DPAHWWERLVAGRVTVWNSTPALMLLLVEYAEQ-------RGLKLPAAlrlvmlSGDWIPvalPDRIRALGR-- 2922
Cdd:PRK13382  266 VTRRRfDPEATLDLIDRHRATGLAVVPVMFDRIMDLPAEvrnrysgRSLRFAAA------SGSRMR---PDVVIAFMDqf 336

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2923 -DVqVVSLGGATEASIWSIAYPIG-QVAPQwksiPYGMPLANQRFHVLDGRLEARPWWVPGELYIGGEGLAREYwrdEPL 3000
Cdd:PRK13382  337 gDV-IYNNYNATEAGMIATATPADlRAAPD----TAGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGY---TSG 408

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  3001 TATRFIrhprtgERLYRTGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPALSASVVVARGEPRGVRRLV 3080
Cdd:PRK13382  409 STKDFH------DGFMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLA 482

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 53747904  3081 AYAVPRSGQTPAAGELRRYLAERLPAYMVPSAFVLLESLPRSRNGKIARDQLPEP 3135
Cdd:PRK13382  483 AFVVLKPGASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQAR 537
PRK07867 PRK07867
acyl-CoA synthetase; Validated
 2736-3132 2.92e-11

acyl-CoA synthetase; Validated


Pssm-ID: 236120 [Multi-domain]  Cd Length: 529  Bit Score: 69.32  E-value: 2.92e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2736 ARVVLTQSSLLHTV-PWPPGVQVIAVD------ELEPATEAPPLPPRGTPEHLAYVIYTSGSTGKPKGVAIEHRAALNTV 2808
Cdd:PRK07867  102 CQLVLTESAHAELLdGLDPGVRVINVDspawadELAAHRDAEPPFRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVASAG 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2809 VDLNTRFGVGPEDrVLGLSaltfdlsvydvlgllgaggalvLPAAEAEKDPAHWWERLVAG-------RVTVWNSTPALM 2881
Cdd:PRK07867  182 VMLAQRFGLGPDD-VCYVS----------------------MPLFHSNAVMAGWAVALAAGasialrrKFSASGFLPDVR 238

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2882 LLLVEYAEQRG------LKLPAA-------LRLVMlsGDwipVALPDRIRALGR--DVQVVSLGGATEASI---WSIAYP 2943
Cdd:PRK07867  239 RYGATYANYVGkplsyvLATPERpddadnpLRIVY--GN---EGAPGDIARFARrfGCVVVDGFGSTEGGVaitRTPDTP 313

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2944 IGQVAPQWKSIPY-----GMPLANQRFHVlDGRLEARPwwVPGELY-IGGEGLAREYWRDEPLTATRfIRHPRtgerlYR 3017
Cdd:PRK07867  314 PGALGPLPPGVAIvdpdtGTECPPAEDAD-GRLLNADE--AIGELVnTAGPGGFEGYYNDPEADAER-MRGGV-----YW 384

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  3018 TGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPALSASVVVARGEPRGVRRLVAYAVPRSGQTPAAGELR 3097
Cdd:PRK07867  385 SGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALVLAPGAKFDPDAFA 464

                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 53747904  3098 RYLAER--LPAYMVPSAFVLLESLPRSRNGKIARDQL 3132
Cdd:PRK07867  465 EFLAAQpdLGPKQWPSYVRVCAELPRTATFKVLKRQL 501
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 1232-1362 3.32e-11

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: 66.35  E-value: 3.32e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1232 ELEQLGAEVQVYTADVAEEAAVRSVVEQVHARWGKIHGVLHAAATFDDGVIQLRTHEQSSRALRTKVRGSMVL-HEVL-- 1308
Cdd:COG1028   49 ELRAAGGRALAVAADVTDEAAVEALVAAAVAAFGRLDILVNNAGITPPGPLEELTEEDWDRVLDVNLKGPFLLtRAALph 128

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 53747904 1309 ---ASEGLdwFALCSSLASALGSFGQADYCAANAFQDayahhlrrqGFTGALALDWG 1362
Cdd:COG1028  129 mreRGGGR--IVNISSIAGLRGSPGQAAYAASKAAVV---------GLTRSLALELA 174
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
 3149-3216 3.41e-11

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: 61.41  E-value: 3.41e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 53747904 3149 DPLVERLAALVKEALRL--ERVEPQDSLL-DLGADSVALIRLINRLEAELQFRPRLADIYENPTVQGLATL 3216
Cdd:COG0236    4 EELEERLAEIIAEVLGVdpEEITPDDSFFeDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADY 74
FrmA COG1062
Zn-dependent alcohol/formaldehyde dehydrogenase [Energy production and conversion];
1694-1883 3.64e-11

Zn-dependent alcohol/formaldehyde dehydrogenase [Energy production and conversion];


Pssm-ID: 440682 [Multi-domain]  Cd Length: 355  Bit Score: 67.80  E-value: 3.64e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1694 PAPGPRQVEIEVEAAG-----LNFLDvlGALGM-MPAleaeesVLGRECSGRIAAVGEGVSGLRVGDEV-LAVAPGC--- 1763
Cdd:COG1062   12 DEPRPGEVLVRIVAAGlchsdLHVRD--GDLPVpLPA------VLGHEGAGVVEEVGPGVTGVAPGDHVvLSFIPSCghc 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1764 ----------------------------------------------FRSYVLVDESQVVRRPASLGLAEGAaqmvPFA-- 1795
Cdd:COG1062   84 rycasgrpalceagaalngkgtlpdgtsrlssadgepvghffgqssFAEYAVVPERSVVKVDKDVPLELAA----LLGcg 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1796 --TAYFALHTVGRLRRGERILIhaaagglglaaVQLASRTGA-EILATAGSEQKREYLRSLGIAHVLDSRSTSFVSEVRE 1872
Cdd:COG1062  160 vqTGAGAVLNTAKVRPGDTVAVfglgg-vglsaVQGARIAGAsRIIAVDPVPEKLELARELGATHTVNPADEDAVEAVRE 238

                        250
                 ....*....|.
gi 53747904 1873 RTGGrGVDVVL 1883
Cdd:COG1062  239 LTGG-GVDYAF 248
MACS_euk cd05928
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ...
 3016-3132 3.64e-11

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: 69.03  E-value: 3.64e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3016 YRTGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPALSASVVVARGEP-RG--VRRLVAYAVPRSGQTPA 3092
Cdd:cd05928  404 YLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPiRGevVKAFVVLAPQFLSHDPE 483

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 53747904 3093 A--GELRRYLAERLPAYMVPSAFVLLESLPRSRNGKIARDQL 3132
Cdd:cd05928  484 QltKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNEL 525
PRK05691 PRK05691
peptide synthase; Validated
 2684-3241 6.05e-11

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 69.43  E-value: 6.05e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2684 EVQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLDPEQPPLRLHQ-----LLEEGPARVVLTQSSL------LHTVPWP 2752
Cdd:PRK05691   60 RASFGDRAVLLFPSGPDYVAAFFGCLYAGVIAVPAYPPESARRHHQerllsIIADAEPRLLLTVADLrdsllqMEELAAA 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2753 PGVQVIAVDELEPATEAPPLPPRGTPEHLAYVIYTSGSTGKPKGVAIEHRAALNTVVDLNTRFG--VGPEDRVLGLSALT 2830
Cdd:PRK05691  140 NAPELLCVDTLDPALAEAWQEPALQPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGidLNPDDVIVSWLPLY 219

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2831 FDLSVYDVLGLLGAGGA---LVLPAAEAEKdPAHWWERLVAGRVTVWNSTPALMLLLVEYAEQrglklpAALRLVMLSGd 2907
Cdd:PRK05691  220 HDMGLIGGLLQPIFSGVpcvLMSPAYFLER-PLRWLEAISEYGGTISGGPDFAYRLCSERVSE------SALERLDLSR- 291

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2908 WiPVAL----PDRIRALGRDVQVVSLGGATEASIWSiAYPIGQV------APQWKSIPY----GMPLANQRFHVLDG--- 2970
Cdd:PRK05691  292 W-RVAYsgsePIRQDSLERFAEKFAACGFDPDSFFA-SYGLAEAtlfvsgGRRGQGIPAleldAEALARNRAEPGTGsvl 369

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2971 ------------------RLEARPWWVPGELYIGGEGLAREYWRDEPLTATRFIRHprTGERLYRTGDQGrMLPEGSIEF 3032
Cdd:PRK05691  370 mscgrsqpghavlivdpqSLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTFVEH--DGRTWLRTGDLG-FLRDGELFV 446

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  3033 LGREDLQVKVQGFRVELGEIEAALAQHPAlsasvVVARGeprgvrRLVAYAVPRSGQTP--AAGELRRYLAERLPA---- 3106
Cdd:PRK05691  447 TGRLKDMLIVRGHNLYPQDIEKTVEREVE-----VVRKG------RVAAFAVNHQGEEGigIAAEISRSVQKILPPqali 515

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  3107 -----------YMVPSAFVLLE--SLPRSRNGKIARD---------------QLPEpQQTQGLAAQAAAADPLVERLAAL 3158
Cdd:PRK05691  516 ksirqavaeacQEAPSVVLLLNpgALPKTSSGKLQRSacrlrladgsldsyaLFPA-LQAVEAAQTAASGDELQARIAAI 594

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  3159 VKEALRLERVEPQDSLLDLGADSVALIRLINRLEAELQFRPRLADIYENPTVQGLATL--HQEKTKSQGEGGAPRLtaPR 3236
Cdd:PRK05691  595 WCEQLKVEQVAADDHFFLLGGNSIAATQVVARLRDELGIDLNLRQLFEAPTLAAFSAAvaRQLAGGGAAQAAIARL--PR 672


                  ....*
gi 53747904  3237 STLLP 3241
Cdd:PRK05691  673 GQALP 677
FUM14_C_NRPS-like cd19545
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ...
 2181-2604 6.57e-11

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: 67.32  E-value: 6.57e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2181 FPLTDVQE-----------AYwVGRRsAFELggvaahgyfeieSPGLEVERFIQCWRQLLQRHDMLR--MVVLPDGR-QQ 2246
Cdd:cd19545    2 YPCTPLQEglmaltarqpgAY-VGQR-VFEL------------PPDIDLARLQAAWEQVVQANPILRtrIVQSDSGGlLQ 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2247 VleQVPEYTPEVVELRGLS--PQEAESRRLQLRERMAHQVLRSDRWPLFELVLCryeggvrIHMSmdalMLDAWSSAVLR 2324
Cdd:cd19545   68 V--VVKESPISWTESTSLDeyLEEDRAAPMGLGGPLVRLALVEDPDTERYFVWT-------IHHA----LYDGWSLPLIL 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2325 QDFAQLYHepGRPLEPLAiTFRDYVlaeRRLREGEaHERARAYWWARLdtlppppelplvKEPSQLEHARFTHreARLEP 2404
Cdd:cd19545  135 RQVLAAYQ--GEPVPQPP-PFSRFV---KYLRQLD-DEAAAEFWRSYL------------AGLDPAVFPPLPS--SRYQP 193

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2405 HRWARLQERARA-----HGLTPSAACMAAFAEVLARWSRHPRFTLNLTLFQR-LPLhPQVDELVGDFTSLVLLEVEAHAA 2478
Cdd:cd19545  194 RPDATLEHSISLpssasSGVTLATVLRAAWALVLSRYTGSDDVVFGVTLSGRnAPV-PGIEQIVGPTIATVPLRVRIDPE 272

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2479 STFAERASRLQAQLWRDLEHGSvSAVQLIRELvrtgrrSPGAIMPVVFTSILSLDARRGPQGSLSFFEGelVYSISQTPQ 2558
Cdd:cd19545  273 QSVEDFLQTVQKDLLDMIPFEH-TGLQNIRRL------GPDARAACNFQTLLVVQPALPSSTSESLELG--IEEESEDLE 343

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|..
gi 53747904 2559 VWLDHGVHEE----EGALVL--AWDSVeaLFPPGMVDDMFHAYQRLLGALAE 2604
Cdd:cd19545  344 DFSSYGLTLEcqlsGSGLRVraRYDSS--VISEEQVERLLDQFEHVLQQLAS 393
PRK09029 PRK09029
O-succinylbenzoic acid--CoA ligase; Provisional
 2648-3132 7.22e-11

O-succinylbenzoic acid--CoA ligase; Provisional


Pssm-ID: 236363 [Multi-domain]  Cd Length: 458  Bit Score: 67.59  E-value: 7.22e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2648 ARLHPELPALLAPERTLSYGELARRAQALAARLRELEVQPQELVAIamhKGWEQATAV---LGVLQAAAAYLPLDPEQPP 2724
Cdd:PRK09029   13 AQVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVAL---RGKNSPETLlayLALLQCGARVLPLNPQLPQ 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2725 LRLHQLLEEGPARVVLTqsslLHTVPWPPGVQVIAVDELEPATEAPPLPPRgtpehLAYVIYTSGSTGKPKGVAIEHRAA 2804
Cdd:PRK09029   90 PLLEELLPSLTLDFALV----LEGENTFSALTSLHLQLVEGAHAVAWQPQR-----LATMTLTSGSTGLPKAAVHTAQAH 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2805 LNTVVDLNTRFGVGPEDRVLgLSALTFDLS----VydvlgllgaggalvlpaaeaekdpahwWERLVAG-RVTVWNSTP- 2878
Cdd:PRK09029  161 LASAEGVLSLMPFTAQDSWL-LSLPLFHVSgqgiV---------------------------WRWLYAGaTLVVRDKQPl 212

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2879 ALMLLLVEYAE------QRGLK---LPAALRLVMLSGDWIPVALPDRIRALGrdvqVVS-LG-GATE-ASiwsiaypigQ 2946
Cdd:PRK09029  213 EQALAGCTHASlvptqlWRLLDnrsEPLSLKAVLLGGAAIPVELTEQAEQQG----IRCwCGyGLTEmAS---------T 279

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2947 V-APQWKSIP-YGMPLANQRFhvldgRLearpwwVPGELYIGGEGLAREYWRDEPLTatrfirhPRTGER-LYRTGDQGR 3023
Cdd:PRK09029  280 VcAKRADGLAgVGSPLPGREV-----KL------VDGEIWLRGASLALGYWRQGQLV-------PLVNDEgWFATRDRGE 341

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  3024 MLpEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPALSASVVVARGEPRGVRRLVAYAVPRSGQTPAAgeLRRYLAER 3103
Cdd:PRK09029  342 WQ-NGELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADAEFGQRPVAVVESDSEAAVVN--LAEWLQDK 418

                         490       500
                  ....*....|....*....|....*....
gi 53747904  3104 LPAYMVPSAFVLLESLPRSRNGKIARDQL 3132
Cdd:PRK09029  419 LARFQQPVAYYLLPPELKNGGIKISRQAL 447
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
 3153-3211 8.03e-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: 59.88  E-value: 8.03e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 53747904   3153 ERLAALVKEALRL--ERVEPQDSLLDLGADSVALIRLINRLEAELQFRPRLADIYENPTVQ 3211
Cdd:pfam00550    1 ERLRELLAEVLGVpaEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLA 61
PRK12467 PRK12467
peptide synthase; Provisional
 2083-2145 8.65e-11

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 68.65  E-value: 8.65e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 53747904  2083 PPSSLEQLIEQVWRKHLGVERVQPTDSFFQLGGDSLLGIQVAADLRRHLGVELPTATLFSHPT 2145
Cdd:PRK12467 3602 PRSEVEQQLAAIWADVLGVEQVGVTDNFFELGGDSLLALQVLSRIRQSLGLKLSLRDLMSAPT 3664
LC_FACL_like cd05914
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ...
 2663-3129 9.71e-11

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: 67.47  E-value: 9.71e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2663 TLSYGELARRAQALAARLRELEVQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLDPEQPPLRLHQLLEEGPARVVLTq 2742
Cdd:cd05914    7 PLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFV- 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2743 ssllhtvpwppgvqviavdelepateapplpprGTPEHLAYVIYTSGSTGKPKGVAIEHRAALNTVVDLNTRFGVGPEDR 2822
Cdd:cd05914   86 ---------------------------------SDEDDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGKGDK 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2823 VLGL------SALTFDLsVYDVLGLLGAGGALVLPAAEAEKdpahwwERLVAGRVTVWNSTPALMLLLVEYAEQRGLKLP 2896
Cdd:cd05914  133 ILSIlplhhiYPLTFTL-LLPLLNGAHVVFLDKIPSAKIIA------LAFAQVTPTLGVPVPLVIEKIFKMDIIPKLTLK 205

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2897 AALRLVMlsgdwIPVaLPDRIR---------ALGRDVQVVSLGGA-----TEASIWSIAYPIgqvapqwkSIPYGM---- 2958
Cdd:cd05914  206 KFKFKLA-----KKI-NNRKIRklafkkvheAFGGNIKEFVIGGAkinpdVEEFLRTIGFPY--------TIGYGMteta 271

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2959 ------PLANQRF----HVLDGrLEAR-----PWWVPGELYIGGEGLAREYWRDEPLTATRFirhprTGERLYRTGDQGR 3023
Cdd:cd05914  272 piisysPPNRIRLgsagKVIDG-VEVRidspdPATGEGEIIVRGPNVMKGYYKNPEATAEAF-----DKDGWFHTGDLGK 345

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3024 MLPEGSIEFLGR-EDLQVKVQGFRVELGEIEAALAQHPALSASVVVARgEPRGVrrLVAYAVPRSGQTPAAG-------- 3094
Cdd:cd05914  346 IDAEGYLYIRGRkKEMIVLSSGKNIYPEEIEAKINNMPFVLESLVVVQ-EKKLV--ALAYIDPDFLDVKALKqrniidai 422

                        490       500       510
                 ....*....|....*....|....*....|....*...
gi 53747904 3095 --ELRRYLAERLPAYMVPSAFVLL-ESLPRSRNGKIAR 3129
Cdd:cd05914  423 kwEVRDKVNQKVPNYKKISKVKIVkEEFEKTPKGKIKR 460
E_NRPS cd19534
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
 2180-2494 1.08e-10

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: 66.89  E-value: 1.08e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2180 PFPLTDVQEAYwvgrrsaFELGGVAAHGY-----FEIeSPGLEVERFIQCWRQLLQRHDMLRMVVL-PDGR-QQVLEQVP 2252
Cdd:cd19534    1 EVPLTPIQRWF-------FEQNLAGRHHFnqsvlLRV-PQGLDPDALRQALRALVEHHDALRMRFRrEDGGwQQRIRGDV 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2253 E--YTPEVVELRGLSPQEAesrrlqLRERM--AHQVLRSDRWPLFELVLC-RYEGGVRIHMSMDALMLDAWSSAVLRQDF 2327
Cdd:cd19534   73 EelFRLEVVDLSSLAQAAA------IEALAaeAQSSLDLEEGPLLAAALFdGTDGGDRLLLVIHHLVVDGVSWRILLEDL 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2328 AQLYH--EPGRPLE-PLAITFRDYVLAERRLREGEAHERARAYWWARLDTLPPPPELPLVKepsqlEHARFTHREARLEP 2404
Cdd:cd19534  147 EAAYEqaLAGEPIPlPSKTSFQTWAELLAEYAQSPALLEELAYWRELPAADYWGLPKDPEQ-----TYGDARTVSFTLDE 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2405 HRWARL-QERARAHGLTPSAACMAAFAEVLARWSRHPRFTLNLTLFQRLPLHPQVD--ELVGDFTSL--VLLEVEahAAS 2479
Cdd:cd19534  222 EETEALlQEANAAYRTEINDLLLAALALAFQDWTGRAPPAIFLEGHGREEIDPGLDlsRTVGWFTSMypVVLDLE--ASE 299

                        330
                 ....*....|....*
gi 53747904 2480 TFAERASRLQAQLWR 2494
Cdd:cd19534  300 DLGDTLKRVKEQLRR 314
PRK07769 PRK07769
long-chain-fatty-acid--CoA ligase; Validated
 2686-2831 1.22e-10

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


Pssm-ID: 181109 [Multi-domain]  Cd Length: 631  Bit Score: 67.45  E-value: 1.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2686 QPQELVAIAMHKGWEQATAVLGVLQAAAAYLPL-DPEQPPL--RLHQLLEEGPARVVLTQSS-------LLHTVPWPPGV 2755
Cdd:PRK07769   77 KPGDRVAILAPQNLDYLIAFFGALYAGRIAVPLfDPAEPGHvgRLHAVLDDCTPSAILTTTDsaegvrkFFRARPAKERP 156

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 53747904  2756 QVIAVDELEPATEAPPLPPRGTPEHLAYVIYTSGSTGKPKGVAIEHRAALNTVVDLNTRFGVGPEDRvlGLSALTF 2831
Cdd:PRK07769  157 RVIAVDAVPDEVGATWVPPEANEDTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEGQEGDR--GVSWLPF 230
Zn_ADH10 cd08263
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
 1694-1989 1.28e-10

Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176224 [Multi-domain]  Cd Length: 367  Bit Score: 66.24  E-value: 1.28e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1694 PAPGPRQVEIEVEAAGLNFLDVLGALGMMPAleAEESVLGRECSGRIAAVGEGV---SGLRVGDEVLA--VAP------- 1761
Cdd:cd08263   21 PRPKEGEILIRVAACGVCHSDLHVLKGELPF--PPPFVLGHEISGEVVEVGPNVenpYGLSVGDRVVGsfIMPcgkcryc 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1762 -----------------------------------------GCFRSYVLVDESQVVRRPASLGLAEGAAQMVPFATAYFA 1800
Cdd:cd08263   99 argkenlcedffaynrlkgtlydgttrlfrldggpvymysmGGLAEYAVVPATALAPLPESLDYTESAVLGCAGFTAYGA 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1801 LHTVGRLRRGERILIhAAAGGLGLAAVQLASRTGA-EILATAGSEQKREYLRSLGIAHVLDSRSTSFVSEVRERTGGRGV 1879
Cdd:cd08263  179 LKHAADVRPGETVAV-IGVGGVGSSAIQLAKAFGAsPIIAVDVRDEKLAKAKELGATHTVNAAKEDAVAAIREITGGRGV 257

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1880 DVVLNSL-AGELLLAGLSVLAPHGRFLELGKRDLYADQQVGLRTLARGQTFAAIDFGpHHPdfRAVLEEVATQLTQGQLE 1958
Cdd:cd08263  258 DVVVEALgKPETFKLALDVVRDGGRAVVVGLAPGGATAEIPITRLVRRGIKIIGSYG-ARP--RQDLPELVGLAASGKLD 334

                        330       340       350
                 ....*....|....*....|....*....|...
gi 53747904 1959 P--LPTRLFPARQVAEAFSFMARALHIGRVAVS 1989
Cdd:cd08263  335 PeaLVTHKYKLEEINEAYENLRKGLIHGRAIVE 367
PLN02330 PLN02330
4-coumarate--CoA ligase-like 1
 2662-3134 1.73e-10

4-coumarate--CoA ligase-like 1


Pssm-ID: 215189 [Multi-domain]  Cd Length: 546  Bit Score: 66.93  E-value: 1.73e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2662 RTLSYGELARRAQALAARLRELEVQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLDPEQPPLRLHQLLEEGPARVVLT 2741
Cdd:PLN02330   54 KAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVT 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2742 QSSLLHTVPwPPGVQVIAVDE--LEPATEAPPLPPRG-----TPEH-------LAYVIYTSGSTGKPKGVAIEHRaalNT 2807
Cdd:PLN02330  134 NDTNYGKVK-GLGLPVIVLGEekIEGAVNWKELLEAAdragdTSDNeeilqtdLCALPFSSGTTGISKGVMLTHR---NL 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2808 VVDL-NTRFGVGPE--DRVLGLSALTFdLSVYDVLGLLGAGGALVLPAAEAEK-DPAHWWERLVAGRVTVWNSTPALMLL 2883
Cdd:PLN02330  210 VANLcSSLFSVGPEmiGQVVTLGLIPF-FHIYGITGICCATLRNKGKVVVMSRfELRTFLNALITQEVSFAPIVPPIILN 288

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2884 LVE--YAEQRGL-KLpaALRLVMLSGdwIPVAlPDRIRALGR---DVQVVSLGGATEASIWSIAY---PIGQVAPQWKSI 2954
Cdd:PLN02330  289 LVKnpIVEEFDLsKL--KLQAIMTAA--APLA-PELLTAFEAkfpGVQVQEAYGLTEHSCITLTHgdpEKGHGIAKKNSV 363

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2955 PYGMPLANQRFHVLDGRLeARPWWVPGELYIGGEGLAREYWRDEPLTAtrfirhpRTGER--LYRTGDQGRMLPEGSIEF 3032
Cdd:PLN02330  364 GFILPNLEVKFIDPDTGR-SLPKNTPGELCVRSQCVMQGYYNNKEETD-------RTIDEdgWLHTGDIGYIDDDGDIFI 435

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  3033 LGREDLQVKVQGFRVELGEIEAALAQHPALSASVVVARGEPRGVRRLVAYAVPRSGQTPAAGELRRYLAERLPAYMVPSA 3112
Cdd:PLN02330  436 VDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVINPKAKESEEDILNFVAANVAHYKKVRV 515

                         490       500
                  ....*....|....*....|..
gi 53747904  3113 FVLLESLPRSRNGKIARDQLPE 3134
Cdd:PLN02330  516 VQFVDSIPKSLSGKIMRRLLKE 537
PRK05691 PRK05691
peptide synthase; Validated
 2083-2498 1.80e-10

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 67.50  E-value: 1.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2083 PPSSLEQLIEQVWRKHLGVERVQPTDSFFQLGGDSLLGIQVAADLRRhLGVELPTATLFSHPTLAALAAALRARQgeaaa 2162
Cdd:PRK05691 2706 PRSELEQQLAQIWREVLNVERVGLGDNFFELGGDSILSIQVVSRARQ-LGIHFSPRDLFQHQTVQTLAAVATHSE----- 2779

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2163 ptapapALVPDPAARFEPFPLTDVQeaywvgrrsafelggvaaHGYFEIESP---------------GLEVERFIQCWRQ 2227
Cdd:PRK05691 2780 ------AAQAEQGPLQGASGLTPIQ------------------HWFFDSPVPqpqhwnqallleprqALDPALLEQALQA 2835

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2228 LLQRHDMLRMVV-----------LPDGRQQVLEQVPeyTPEVVELRGLSPQEAESRRLQlrermahqvlrsdRWPLFELV 2296
Cdd:PRK05691 2836 LVEHHDALRLRFsqadgrwqaeyRAVTAQELLWQVT--VADFAECAALFADAQRSLDLQ-------------QGPLLRAL 2900

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2297 LCR-YEGGVRIHMSMDALMLDAWSSAVLRQDFAQLYH--EPGRPLEPLAIT--FRDYVLAERRLREGEAHERARAYWWAR 2371
Cdd:PRK05691 2901 LVDgPQGQQRLLLAIHHLVVDGVSWRVLLEDLQALYRqlSAGAEPALPAKTsaFRDWAARLQAYAGSESLREELGWWQAQ 2980

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2372 LDTLPPPPELPLVKEPSQLEHARFThrEARLEPHRWARLQERARAHGLTP-SAACMAAFAEVLARWSRHPRFTLNLTLFQ 2450
Cdd:PRK05691 2981 LGGPRAELPCDRPQGGNLNRHAQTV--SVRLDAERTRQLLQQAPAAYRTQvNDLLLTALARVLCRWSGQPSVLVQLEGHG 3058

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 53747904  2451 RLPLHPQVD--ELVGDFTSLVLLEVEAHAASTFAERAS--RLQAQLwRDLEH 2498
Cdd:PRK05691 3059 REALFDDIDltRSVGWFTSAYPLRLTPAPGDDAARGESikAIKEQL-RAVPH 3109
PLN02574 PLN02574
4-coumarate--CoA ligase-like
 2704-3132 1.84e-10

4-coumarate--CoA ligase-like


Pssm-ID: 215312 [Multi-domain]  Cd Length: 560  Bit Score: 66.79  E-value: 1.84e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2704 AVLGVLQAAAAYLPLDPEQPPLRLHQlleegpaRVVLTQSSLLHTVP------WPPGVQVIAVDEL----EPATEAPPL- 2772
Cdd:PLN02574  108 IFLAVLSLGGIVTTMNPSSSLGEIKK-------RVVDCSVGLAFTSPenveklSPLGVPVIGVPENydfdSKRIEFPKFy 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2773 ------------PPRGTpEHLAYVIYTSGSTGKPKGVAIEHRAALNTVvDLNTRF---------------GVGPEDRVLG 2825
Cdd:PLN02574  181 elikedfdfvpkPVIKQ-DDVAAIMYSSGTTGASKGVVLTHRNLIAMV-ELFVRFeasqyeypgsdnvylAALPMFHIYG 258

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2826 LSALTFDLsvydVLGLLGAGGALVLPAAEAEKDPAHWwerlvagRVTVWNSTPALMLLLVEYAEQRGLKLPAALRLVM-- 2903
Cdd:PLN02574  259 LSLFVVGL----LSLGSTIVVMRRFDASDMVKVIDRF-------KVTHFPVVPPILMALTKKAKGVCGEVLKSLKQVScg 327

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2904 ---LSGDWIPvalpDRIRALGRdVQVVSLGGATEASIWSIAYPIGQVAPQWKSIpyGMPLANQRFHVLDgrLEARPWWVP 2980
Cdd:PLN02574  328 aapLSGKFIQ----DFVQTLPH-VDFIQGYGMTESTAVGTRGFNTEKLSKYSSV--GLLAPNMQAKVVD--WSTGCLLPP 398

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2981 G---ELYIGGEGLAREYWRDEPLTATRFIRhprtgERLYRTGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALA 3057
Cdd:PLN02574  399 GncgELWIQGPGVMKGYLNNPKATQSTIDK-----DGWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLI 473

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 53747904  3058 QHPALSASVVVARGEPRGVRRLVAYAVPRSGQTPAAGELRRYLAERLPAYMVPSAFVLLESLPRSRNGKIARDQL 3132
Cdd:PLN02574  474 SHPEIIDAAVTAVPDKECGEIPVAFVVRRQGSTLSQEAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRREL 548
Ac_CoA_lig_AcsA TIGR02188
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ...
 2778-3129 2.26e-10

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: 66.50  E-value: 2.26e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   2778 PEHLAYVIYTSGSTGKPKGVAieHRAA---LNTVVDLNTRFGVGPEDR---------VLGLSALtfdlsVYdvlgllgag 2845
Cdd:TIGR02188  236 SEDPLFILYTSGSTGKPKGVL--HTTGgylLYAAMTMKYVFDIKDGDIfwctadvgwITGHSYI-----VY--------- 299

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   2846 galvLPAAE-----------AEKDPAHWWERLVAGRVTVWNSTPALMLLLVEYAEQ--RGLKLpAALRLVMLSGDWI-PV 2911
Cdd:TIGR02188  300 ----GPLANgattvmfegvpTYPDPGRFWEIIEKHKVTIFYTAPTAIRALMRLGDEwvKKHDL-SSLRLLGSVGEPInPE 374

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   2912 ALPDRIRALGR-DVQVVS--------------LGGATEASIWSIAYPIGQVAPQwksipygmpLANQRFHVLDGRLE--- 2973
Cdd:TIGR02188  375 AWMWYYKVVGKeRCPIVDtwwqtetggimitpLPGATPTKPGSATLPFFGIEPA---------VVDEEGNPVEGPGEggy 445

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   2974 ---ARPWwvPgelyiggeGLAREYWRDEpltaTRFIR-HPRTGERLYRTGDQGRMLPEGSIEFLGREDLQVKVQGFRVEL 3049
Cdd:TIGR02188  446 lviKQPW--P--------GMLRTIYGDH----ERFVDtYFSPFPGYYFTGDGARRDKDGYIWITGRVDDVINVSGHRLGT 511

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   3050 GEIEAALAQHPALSASVVVARGEPRGVRRLVAYAVPRSGQTPAAG---ELRRYLAERLPAYMVPSAFVLLESLPRSRNGK 3126
Cdd:TIGR02188  512 AEIESALVSHPAVAEAAVVGIPDDIKGQAIYAFVTLKDGYEPDDElrkELRKHVRKEIGPIAKPDKIRFVPGLPKTRSGK 591


                   ...
gi 53747904   3127 IAR 3129
Cdd:TIGR02188  592 IMR 594
AACS cd05943
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ...
 2738-3127 2.39e-10

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: 66.53  E-value: 2.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2738 VVLTQSSLLHTVPWPPGVQVIAVDELEPATEAPPLPPRGTP-EHLAYVIYTSGSTGKPK-------GVAIEHRAALNTVV 2809
Cdd:cd05943  207 VVVPYTVAAGQPDLSKIAKALTLEDFLATGAAGELEFEPLPfDHPLYILYSSGTTGLPKcivhgagGTLLQHLKEHILHC 286

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2810 DLntrfgvGPEDRVL-------------------GLSALTFDLSvydvlgllgaggalvlPAAEAekdpAHWWERLVAG- 2869
Cdd:cd05943  287 DL------RPGDRLFyyttcgwmmwnwlvsglavGATIVLYDGS----------------PFYPD----TNALWDLADEe 340

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2870 RVTVWNSTPALMLLLveyaEQRGLKLPA-----ALRLVMLSG--------DWIPvalpdriRALGRDVQVVSLGGATE-A 2935
Cdd:cd05943  341 GITVFGTSAKYLDAL----EKAGLKPAEthdlsSLRTILSTGsplkpesfDYVY-------DHIKPDVLLASISGGTDiI 409

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2936 SIWSIAYPIgqvAPQWKS----IPYGMPLAnqrfhVLDGrlEARPWW-VPGELYI--GGEGLAREYWRDEPLT---ATRF 3005
Cdd:cd05943  410 SCFVGGNPL---LPVYRGeiqcRGLGMAVE-----AFDE--EGKPVWgEKGELVCtkPFPSMPVGFWNDPDGSryrAAYF 479

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3006 IRHPRtgerLYRTGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPALSASVVVARGEPRGVRRLVAYAVP 3085
Cdd:cd05943  480 AKYPG----VWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKL 555

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 53747904 3086 RSGQT---PAAGELRRYLAERLPAYMVPSAFVLLESLPRSRNGKI 3127
Cdd:cd05943  556 REGVElddELRKRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGKK 600
2-desacetyl-2-hydroxyethyl_bacteriochlorophyllide_ cd08255
2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup ...
 1731-1974 2.42e-10

2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family has members identified as 2-desacetyl-2-hydroxyethyl bacteriochlorophyllide A dehydrogenase and alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability.


Pssm-ID: 176217 [Multi-domain]  Cd Length: 277  Bit Score: 64.21  E-value: 2.42e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1731 VLGRECSGRIAAVGEGVSGLRVGDEVlaVAPGCFRSYVLVDESQVVRRPASLGLAEGaaqmVPFATAYFALHTV--GRLR 1808
Cdd:cd08255   23 PPGYSSVGRVVEVGSGVTGFKPGDRV--FCFGPHAERVVVPANLLVPLPDGLPPERA----ALTALAATALNGVrdAEPR 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1809 RGERILIhaaagglglaaV----------QLASRTGA-EILATAGSEQKREYLRSLGIAHVLdsrstsfVSEVRERTGGR 1877
Cdd:cd08255   97 LGERVAV-----------VglglvgllaaQLAKAAGArEVVGVDPDAARRELAEALGPADPV-------AADTADEIGGR 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1878 GVDVVLN-SLAGELLLAGLSVLAPHGRFLELGKrdlyadqqVGLRTLARGQTF---------------AAIDFGPHHPDF 1941
Cdd:cd08255  159 GADVVIEaSGSPSALETALRLLRDRGRVVLVGW--------YGLKPLLLGEEFhfkrlpirssqvygiGRYDRPRRWTEA 230

                        250       260       270
                 ....*....|....*....|....*....|...
gi 53747904 1942 RAvLEEVATQLTQGQLEPLPTRLFPARQVAEAF 1974
Cdd:cd08255  231 RN-LEEALDLLAEGRLEALITHRVPFEDAPEAY 262
PRK12316 PRK12316
peptide synthase; Provisional
 2083-2145 2.49e-10

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 67.29  E-value: 2.49e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 53747904  2083 PPSSLEQLIEQVWRKHLGVERVQPTDSFFQLGGDSLLGIQVAADLRRHLGVELPTATLFSHPT 2145
Cdd:PRK12316 5069 PRSELEQQVAAIWAEVLQLERVGLDDNFFELGGHSLLAIQVTSRIQLELGLELPLRELFQTPT 5131
PRK12406 PRK12406
long-chain-fatty-acid--CoA ligase; Provisional
 2656-3135 2.67e-10

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


Pssm-ID: 183506 [Multi-domain]  Cd Length: 509  Bit Score: 66.26  E-value: 2.67e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2656 ALLAPERTLSYGELARRAQALAARLRELEVQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLDPEQPPLRLHQLLEEGP 2735
Cdd:PRK12406    4 TIISGDRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2736 ARVVLTQSSLLHTVP--WPPGVQVIAVD---------ELEPATEAPPL-------------PPRGTP-EHLAYVIYTSGS 2790
Cdd:PRK12406   84 ARVLIAHADLLHGLAsaLPAGVTVLSVPtppeiaaayRISPALLTPPAgaidwegwlaqqePYDGPPvPQPQSMIYTSGT 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2791 TGKPKGV-----AIEHRAALNTVVDLNtrFGVGPEDRVL-------------GLSALTFDLSVydvlgllgaggalvlpA 2852
Cdd:PRK12406  164 TGHPKGVrraapTPEQAAAAEQMRALI--YGLKPGIRALltgplyhsapnayGLRAGRLGGVL----------------V 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2853 AEAEKDPAHWWERLVAGRVTVWNSTPALMLllveyaeqRGLKLPAA---------LRLVMLSGDWIPVALPDRIRALGRD 2923
Cdd:PRK12406  226 LQPRFDPEELLQLIERHRITHMHMVPTMFI--------RLLKLPEEvrakydvssLRHVIHAAAPCPADVKRAMIEWWGP 297

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2924 VqVVSLGGATEASIWSIAypigqVAPQWKSIP--YGMPLANQRFHVLDGRLEARPWWVPGELYIGGEGLAREYW--RDEP 2999
Cdd:PRK12406  298 V-IYEYYGSTESGAVTFA-----TSEDALSHPgtVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDFTYhnKPEK 371

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  3000 LTATRfirhpRTGerLYRTGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPALSASVVVARGEPRGVRRL 3079
Cdd:PRK12406  372 RAEID-----RGG--FITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEAL 444

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 53747904  3080 VAYAVPRSGQTPAAGELRRYLAERLPAYMVPSAFVLLESLPRSRNGKIARDQLPEP 3135
Cdd:PRK12406  445 MAVVEPQPGATLDEADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLRDP 500
PRK08633 PRK08633
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
 2777-3127 3.19e-10

2-acyl-glycerophospho-ethanolamine acyltransferase; Validated


Pssm-ID: 236315 [Multi-domain]  Cd Length: 1146  Bit Score: 66.49  E-value: 3.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2777 TPEHLAYVIYTSGSTGKPKGVAIEHRAALNTVVDLNTRFGVGPEDRVL---------GLSALTFdlsvydvlgllgagga 2847
Cdd:PRK08633  780 KPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILsslpffhsfGLTVTLW---------------- 843

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2848 lvLPAAEAEK-----DP--AHWWERLVAG-RVTVWNSTPALMLLlveYAeqRGLKLP----AALRLVMLSGDwipvALPD 2915
Cdd:PRK08633  844 --LPLLEGIKvvyhpDPtdALGIAKLVAKhRATILLGTPTFLRL---YL--RNKKLHplmfASLRLVVAGAE----KLKP 912

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2916 RIRALGRD---VQVVSLGGATEAS-IWSIAYP---IGQVAPQWKSIP--YGMPLANQRFHVLD-GRLEARPWWVPGELYI 2985
Cdd:PRK08633  913 EVADAFEEkfgIRILEGYGATETSpVASVNLPdvlAADFKRQTGSKEgsVGMPLPGVAVRIVDpETFEELPPGEDGLILI 992

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2986 GGEGLAREYWRDEPLTAtRFIRHPrTGERLYRTGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPALSAS 3065
Cdd:PRK08633  993 GGPQVMKGYLGDPEKTA-EVIKDI-DGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKALGGEEV 1070

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 53747904  3066 VVVARG---EPRGVRRLVAYAvprSGQTPAAgELRRYLAE-RLPAYMVPSAFVLLESLPRSRNGKI 3127
Cdd:PRK08633 1071 VFAVTAvpdEKKGEKLVVLHT---CGAEDVE-ELKRAIKEsGLPNLWKPSRYFKVEALPLLGSGKL 1132
PLN03102 PLN03102
acyl-activating enzyme; Provisional
 2786-3132 3.28e-10

acyl-activating enzyme; Provisional


Pssm-ID: 215576 [Multi-domain]  Cd Length: 579  Bit Score: 65.81  E-value: 3.28e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2786 YTSGSTGKPKGVAIEHRAALNTVVD--LNTRFGVGP----EDRVLGLSALTFDLSVYDVLGLLGAGGALVLPAAeaekdp 2859
Cdd:PLN03102  193 YTSGTTADPKGVVISHRGAYLSTLSaiIGWEMGTCPvylwTLPMFHCNGWTFTWGTAARGGTSVCMRHVTAPEI------ 266

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2860 ahwWERLVAGRVTVWNSTPALMLLLVEyAEQRGLKLPAALRLVMLSGDWIPVALPDRIRALGrdVQVVSLGGATEASiws 2939
Cdd:PLN03102  267 ---YKNIEMHNVTHMCCVPTVFNILLK-GNSLDLSPRSGPVHVLTGGSPPPAALVKKVQRLG--FQVMHAYGLTEAT--- 337

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2940 iaYPI--GQVAPQWKSIPYGMPL---ANQRFHVL-----DGRLEARPWWVP------GELYIGGEGLAREYWRDEPLTAT 3003
Cdd:PLN03102  338 --GPVlfCEWQDEWNRLPENQQMelkARQGVSILgladvDVKNKETQESVPrdgktmGEIVIKGSSIMKGYLKNPKATSE 415

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  3004 RFiRHPrtgerLYRTGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPALSASVVVARGEPRGVRRLVAYA 3083
Cdd:PLN03102  416 AF-KHG-----WLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFV 489

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 53747904  3084 VPRSGQTPAA----------GELRRYLAERLPAYMVPSAFVLLESLPRSRNGKIARDQL 3132
Cdd:PLN03102  490 VLEKGETTKEdrvdklvtreRDLIEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKL 548
PRK12316 PRK12316
peptide synthase; Provisional
 2083-2492 3.63e-10

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 66.52  E-value: 3.63e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2083 PPSSLEQLIEQVWRKHLGVERVQPTDSFFQLGGDSLLGIQVAADLRRHlGVELPTATLFSHPTLAALAAALRARQGEAAA 2162
Cdd:PRK12316 1015 PRNALERTLAAIWQDVLGVERVGLDDNFFELGGDSIVSIQVVSRARQA-GIQLSPRDLFQHQTIRSLALVAKAGQATAAD 1093

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2163 PtapapalvpDPAArfEPFPLTDVQeaywvgrRSAFELGGVAAHGY-----FEIESPgLEVERFIQCWRQLLQRHDMLRM 2237
Cdd:PRK12316 1094 Q---------GPAS--GEVALAPVQ-------RWFFEQAIPQRQHWnqsllLQARQP-LDPDRLGRALERLVAHHDALRL 1154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2238 -VVLPDGRQQVLEQVPEYTpEVVELRGLSPQEAesrrLQLRERMAHQVLRSDRWPLFELVLCRY-EGGVRIHMSMDALML 2315
Cdd:PRK12316 1155 rFREEDGGWQQAYAAPQAG-EVLWQRQAASEEE----LLALCEEAQRSLDLEQGPLLRALLVDMaDGSQRLLLVIHHLVV 1229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2316 DAWSSAVLRQDFAQLYHEPGRPLEPLAITFRDYvlAERRLREGEAHERARAYWWARLDTLPPPPELPLVKEPSQLEHARf 2395
Cdd:PRK12316 1230 DGVSWRILLEDLQRAYADLDADLPARTSSYQAW--ARRLHEHAGARAEELDYWQAQLEDAPHELPCENPDGALENRHER- 1306

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2396 tHREARLEPHRWAR-LQERARAHGLTPSAACMAAFAEVLARWSRHPRFTLNLTLFQRLPLHPQVD--ELVGDFTSlvLLE 2472
Cdd:PRK12316 1307 -KLELRLDAERTRQlLQEAPAAYRTQVNDLLLTALARVTCRWSGQASVLVQLEGHGREDLFEDIDlsRTVGWFTS--LFP 1383

                         410       420
                  ....*....|....*....|
gi 53747904  2473 VEAHAASTFAERASRLQAQL 2492
Cdd:PRK12316 1384 VRLTPAADLGESIKAIKEQL 1403
C_PKS-NRPS cd19532
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
 2208-2604 3.76e-10

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: 65.17  E-value: 3.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2208 YFEIESPgLEVERFIQCWRQLLQRHDMLRM---VVLPDGR--QQVLEQVPeytPEVVELRGLSPQEAEsrrlQLRERMAH 2282
Cdd:cd19532   29 SYRLTGP-LDVARLERAVRAVGQRHEALRTcffTDPEDGEpmQGVLASSP---LRLEHVQISDEAEVE----EEFERLKN 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2283 QVLRSDRWPLFELVLCRYEGGVRI------HMSMDAlmldaWSSAVLRQDFAQLYHepGRPLEPLAITFRDYVLAERRLR 2356
Cdd:cd19532  101 HVYDLESGETMRIVLLSLSPTEHYlifgyhHIAMDG-----VSFQIFLRDLERAYN--GQPLLPPPLQYLDFAARQRQDY 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2357 EGEAHERARAYWWARLDTLppppelplvkePSQLE-------HAR------FTHR-EARLEPHRWARLQERARAHGLTPS 2422
Cdd:cd19532  174 ESGALDEDLAYWKSEFSTL-----------PEPLPllpfakvKSRppltryDTHTaERRLDAALAARIKEASRKLRVTPF 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2423 AACMAAFAEVLARWSRHPRFTLNLTLFQRlpLHPQVDELVGDFTSLVLLEVEAHAASTFAE--RASR---LQAqlwrdLE 2497
Cdd:cd19532  243 HFYLAALQVLLARLLDVDDICIGIADANR--TDEDFMETIGFFLNLLPLRFRRDPSQTFADvlKETRdkaYAA-----LA 315

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2498 HGSVSAVQLIRELVRTgrRSPGAiMPV--VFtsilsLDARRGPQGSLSFFEGELV---YSISQTPQ-VWLDhgVHE-EEG 2570
Cdd:cd19532  316 HSRVPFDVLLDELGVP--RSATH-SPLfqVF-----INYRQGVAESRPFGDCELEgeeFEDARTPYdLSLD--IIDnPDG 385

                        410       420       430
                 ....*....|....*....|....*....|....
gi 53747904 2571 ALVLAWDSVEALFPPGMVDDMFHAYQRLLGALAE 2604
Cdd:cd19532  386 DCLLTLKVQSSLYSEEDAELLLDSYVNLLEAFAR 419
PtmA cd17636
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ...
 2964-3125 4.81e-10

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: 64.25  E-value: 4.81e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2964 RFHVLDGRLEARPWWVPGELYIGGEGLAREYWRDEPLTATRFirhpRTGerLYRTGDQGRMLPEGSIEFLGREDLQVKVQ 3043
Cdd:cd17636  173 QVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRT----RGG--WHHTNDLGRREPDGSLSFVGPKTRMIKSG 246

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3044 GFRVELGEIEAALAQHPALSASVVVARGEPRGVRRLVAYAVPRSGQTPAAGELRRYLAERLPAYMVPSAFVLLESLPRSR 3123
Cdd:cd17636  247 AENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGASVTEAELIEHCRARIASYKKPKSVEFADALPRTA 326


                 ..
gi 53747904 3124 NG 3125
Cdd:cd17636  327 GG 328
MACS_AAE_MA_like cd05970
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ...
 2989-3129 5.25e-10

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: 65.21  E-value: 5.25e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2989 GLAREYWRDEPLTATRFirhprtGERLYRTGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPALSASVVV 3068
Cdd:cd05970  393 GLFGGYYKDAEKTAEVW------HDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVT 466

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 53747904 3069 arGEPRGVRRLV--AYAVPRSGQTPA---AGELRRYLAERLPAYMVPSAFVLLESLPRSRNGKIAR 3129
Cdd:cd05970  467 --GVPDPIRGQVvkATIVLAKGYEPSeelKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRR 530
caiC PRK08008
putative crotonobetaine/carnitine-CoA ligase; Validated
 2764-3132 8.80e-10

putative crotonobetaine/carnitine-CoA ligase; Validated


Pssm-ID: 181195 [Multi-domain]  Cd Length: 517  Bit Score: 64.32  E-value: 8.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2764 EPAT--EAPPLPPRGTPEhlayVIYTSGSTGKPKGVAIEHraalntvvdLNTRFG---------VGPEDRVLG-LSALTF 2831
Cdd:PRK08008  160 QPATlcYAPPLSTDDTAE----ILFTSGTTSRPKGVVITH---------YNLRFAgyysawqcaLRDDDVYLTvMPAFHI 226

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2832 DLSVydvlgllgaggALVLPAAEA-------EKDPAH-WWERLVAGRVTVWNSTP----ALMLLLVEYAEQRglklpAAL 2899
Cdd:PRK08008  227 DCQC-----------TAAMAAFSAgatfvllEKYSARaFWGQVCKYRATITECIPmmirTLMVQPPSANDRQ-----HCL 290

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2900 RLVMLsgdWIPVALPDRIRALGR-DVQVVSLGGATEASIWSIAYPIGQvAPQWKSIpyGMPLANQRFHVLDGRLEARPWW 2978
Cdd:PRK08008  291 REVMF---YLNLSDQEKDAFEERfGVRLLTSYGMTETIVGIIGDRPGD-KRRWPSI--GRPGFCYEAEIRDDHNRPLPAG 364

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2979 VPGELYIGGE---GLAREYWRDEPLTATRFirhprTGERLYRTGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAA 3055
Cdd:PRK08008  365 EIGEICIKGVpgkTIFKEYYLDPKATAKVL-----EADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENI 439

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 53747904  3056 LAQHPALSASVVVarGEPRGVR--RLVAYAVPRSGQTPAAGELRRYLAERLPAYMVPSAFVLLESLPRSRNGKIARDQL 3132
Cdd:PRK08008  440 IATHPKIQDIVVV--GIKDSIRdeAIKAFVVLNEGETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNL 516
PRK07008 PRK07008
long-chain-fatty-acid--CoA ligase; Validated
 2786-3134 8.96e-10

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


Pssm-ID: 235908 [Multi-domain]  Cd Length: 539  Bit Score: 64.34  E-value: 8.96e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2786 YTSGSTGKPKGVAIEHR--------AALNTVVDLNTRFGVGPEDRVLGLSALTFDLSVydvlGLLGAGGALVLPAAeaek 2857
Cdd:PRK07008  183 YTSGTTGNPKGALYSHRstvlhaygAALPDAMGLSARDAVLPVVPMFHVNAWGLPYSA----PLTGAKLVLPGPDL---- 254

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2858 DPAHWWERLVAGRVTVWNSTPALMLLLVEYAEQRGLKLpAALRLVMLSGDWIPvalPDRIRALGRD--VQVVSLGGATEA 2935
Cdd:PRK07008  255 DGKSLYELIEAERVTFSAGVPTVWLGLLNHMREAGLRF-STLRRTVIGGSACP---PAMIRTFEDEygVEVIHAWGMTEM 330

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2936 SiwsiayPIGQVA-PQWKSIpyGMPLANQR--------------FHVLDGRLEARPW--WVPGELYIGGEGLAREYWRDE 2998
Cdd:PRK07008  331 S------PLGTLCkLKWKHS--QLPLDEQRkllekqgrviygvdMKIVGDDGRELPWdgKAFGDLQVRGPWVIDRYFRGD 402

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2999 --PLTATRFirhPrtgerlyrTGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPALSASVVVARGEPRGV 3076
Cdd:PRK07008  403 asPLVDGWF---P--------TGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWD 471

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 53747904  3077 RRLVAYAVPRSGQTPAAGELRRYLAERLPAYMVPSAFVLLESLPRSRNGKIARDQLPE 3134
Cdd:PRK07008  472 ERPLLVVVKRPGAEVTREELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLRE 529
E-C_NRPS cd19544
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ...
 2218-2435 1.03e-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: 63.61  E-value: 1.03e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2218 VERFIQCWRQLLQRHDMLRMVVLPDGRQQ----VLEQVPeytpevVELRGLSPQEAESRRLQLRERMAHQVLRSD--RWP 2291
Cdd:cd19544   38 LDAFLAALQQVIDRHDILRTAILWEGLSEpvqvVWRQAE------LPVEELTLDPGDDALAQLRARFDPRRYRLDlrQAP 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2292 LFELVLCRYEGGVRIHMSMDA--LMLDAWSSAVLRQDF-AQLYHEPGRPLEPLAitFRDYVLaerRLREGEAHERARAYW 2368
Cdd:cd19544  112 LLRAHVAEDPANGRWLLLLLFhhLISDHTSLELLLEEIqAILAGRAAALPPPVP--YRNFVA---QARLGASQAEHEAFF 186

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 53747904 2369 WARLDTlppppelplVKEPS--------QLEHARFTHREARLEPHRWARLQERARAHGLTPSAACMAAFAEVLAR 2435
Cdd:cd19544  187 REMLGD---------VDEPTapfglldvQGDGSDITEARLALDAELAQRLRAQARRLGVSPASLFHLAWALVLAR 252
LC_FACS_bac cd05932
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ...
 2769-3104 1.06e-09

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: 64.03  E-value: 1.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2769 APPL---PPRGtPEHLAYVIYTSGSTGKPKGVAIEHRAALNTVVDLNTRFGVGPEDRVLGLSALTfdlSVYDVLGLLGAG 2845
Cdd:cd05932  125 HPPLeerPTRF-PEQLATLIYTSGTTGQPKGVMLTFGSFAWAAQAGIEHIGTEENDRMLSYLPLA---HVTERVFVEGGS 200

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2846 GALVLPAAEAEKDPAhWWERLVAGRVTVWNSTPALMLLLveyaeQRGL--KLPAALRLVMLSgdwIPV--ALPDR--IRA 2919
Cdd:cd05932  201 LYGGVLVAFAESLDT-FVEDVQRARPTLFFSVPRLWTKF-----QQGVqdKIPQQKLNLLLK---IPVvnSLVKRkvLKG 271

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2920 LGRDVQVVSLGGATEAS----IW--SIAYPIGQVapqwksipYGMPlANQRFHVLDGRLEARPWWV-------------P 2980
Cdd:cd05932  272 LGLDQCRLAGCGSAPVPpallEWyrSLGLNILEA--------YGMT-ENFAYSHLNYPGRDKIGTVgnagpgvevriseD 342

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2981 GELYIGGEGLAREYWRDEPLTATRFirhprTGERLYRTGDQGRMLPEGSIEFLGR-EDLQVKVQGFRVELGEIEAALAQH 3059
Cdd:cd05932  343 GEILVRSPALMMGYYKDPEATAEAF-----TADGFLRTGDKGELDADGNLTITGRvKDIFKTSKGKYVAPAPIENKLAEH 417

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 53747904 3060 PALSASVVVARGEPRGVRRLVAYAVPRSGQTPAA-GELRRYLAERL 3104
Cdd:cd05932  418 DRVEMVCVIGSGLPAPLALVVLSEEARLRADAFArAELEASLRAHL 463
FADD10 cd17635
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ...
 2779-3129 1.27e-09

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: 63.05  E-value: 1.27e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2779 EHLAYVIYTSGSTGKPKGVAIEHRAALNTVVDLNTR-FGVGPEDRVLGLSALTFDLSVYdvLGLLGAGGALVLPAAEAEK 2857
Cdd:cd17635    1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEgLNWVVGDVTYLPLPATHIGGLW--WILTCLIHGGLCVTGGENT 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2858 DPAHWWERLVAGRVTVWNSTPALMLLLV-EYAEQrgLKLPAALRLVMLSGDWiPVALPDRIRALGRDVQVVSLGGATEAS 2936
Cdd:cd17635   79 TYKSLFKILTTNAVTTTCLVPTLLSKLVsELKSA--NATVPSLRLIGYGGSR-AIAADVRFIEATGLTNTAQVYGLSETG 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2937 IwSIAYPIGQVAPQWKSIpyGMPLANQRFHVLDGRLEARPWWVPGELYIGGEGLAREYWRDEPLTATRFIrhprtGERLY 3016
Cdd:cd17635  156 T-ALCLPTDDDSIEINAV--GRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLI-----DGWVN 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3017 rTGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPALSASVVVA-----RGEprgvrrLVAYAVPRSGQ-- 3089
Cdd:cd17635  228 -TGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEisdeeFGE------LVGLAVVASAEld 300

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 53747904 3090 TPAAGELRRYLAERLPAYMVPSAFVLLESLPRSRNGKIAR 3129
Cdd:cd17635  301 ENAIRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
idonate-5-DH cd08232
L-idonate 5-dehydrogenase; L-idonate 5-dehydrogenase (L-ido 5-DH ) catalyzes the conversion of ...
 1694-1986 1.29e-09

L-idonate 5-dehydrogenase; L-idonate 5-dehydrogenase (L-ido 5-DH ) catalyzes the conversion of L-lodonate to 5-ketogluconate in the metabolism of L-Idonate to 6-P-gluconate. In E. coli, this GntII pathway is a subsidiary pathway to the canonical GntI system, which also phosphorylates and transports gluconate. L-ido 5-DH is found in an operon with a regulator indR, transporter idnT, 5-keto-D-gluconate 5-reductase, and Gnt kinase. L-ido 5-DH is a zinc-dependent alcohol dehydrogenase-like protein. The alcohol dehydrogenase ADH-like family of proteins is a diverse group of proteins related to the first identified member, class I mammalian ADH. This group is also called the medium chain dehydrogenases/reductase family (MDR) which displays a broad range of activities and are distinguished from the smaller short chain dehydrogenases(~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal GroES-like catalytic domain. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176194 [Multi-domain]  Cd Length: 339  Bit Score: 63.02  E-value: 1.29e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1694 PAPGPRQVEIEVEAAGLNFLDVL----GALGmmPALEAEESVLGRECSGRIAAVGEGVSGLRVGDEVlAVAP-------- 1761
Cdd:cd08232   17 PEPGPGEVRVRVAAGGICGSDLHyyqhGGFG--TVRLREPMVLGHEVSGVVEAVGPGVTGLAPGQRV-AVNPsrpcgtcd 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1762 --------------------------GCFRSYVLVDESQVVRRPASLGLAEGA-AQmvPFATAYFALHTVGRLRrGERIL 1814
Cdd:cd08232   94 ycragrpnlclnmrflgsamrfphvqGGFREYLVVDASQCVPLPDGLSLRRAAlAE--PLAVALHAVNRAGDLA-GKRVL 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1815 IHAAAGGLGLAAVQLASRTGAEILATAGSEQKREYLRSLGIAHVLDSRSTSFVsevRERTGGRGVDVVLN-SLAGELLLA 1893
Cdd:cd08232  171 VTGAGPIGALVVAAARRAGAAEIVATDLADAPLAVARAMGADETVNLARDPLA---AYAADKGDFDVVFEaSGAPAALAS 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1894 GLSVLAPHGRFLELGKrdLYADQQVGLRTL-ARGQTFAAidfgphhpDFRAVLE--EVATQLTQGQLEPLP--TRLFPAR 1968
Cdd:cd08232  248 ALRVVRPGGTVVQVGM--LGGPVPLPLNALvAKELDLRG--------SFRFDDEfaEAVRLLAAGRIDVRPliTAVFPLE 317

                        330
                 ....*....|....*...
gi 53747904 1969 QVAEAFSFMARALHIGRV 1986
Cdd:cd08232  318 EAAEAFALAADRTRSVKV 335
PRK08974 PRK08974
long-chain-fatty-acid--CoA ligase FadD;
2931-3132 2.71e-09

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


Pssm-ID: 236359 [Multi-domain]  Cd Length: 560  Bit Score: 63.15  E-value: 2.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2931 GATEASIWSIAYPIgQVAPQWKSIpyGMPLANQRFHVLDGRLEARPWWVPGELYIGGEGLAREYWRdepltatrfiRHPR 3010
Cdd:PRK08974  358 GLTECSPLVSVNPY-DLDYYSGSI--GLPVPSTEIKLVDDDGNEVPPGEPGELWVKGPQVMLGYWQ----------RPEA 424

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  3011 TGERL----YRTGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPALSASVVVarGEPRGVR-RLVAYAVP 3085
Cdd:PRK08974  425 TDEVIkdgwLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAV--GVPSEVSgEAVKIFVV 502

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 53747904  3086 RSGQTPAAGELRRYLAERLPAYMVPSAFVLLESLPRSRNGKIARDQL 3132
Cdd:PRK08974  503 KKDPSLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRREL 549
ADH_N pfam08240
Alcohol dehydrogenase GroES-like domain; This is the catalytic domain of alcohol ...
 1700-1776 3.99e-09

Alcohol dehydrogenase GroES-like domain; This is the catalytic domain of alcohol dehydrogenases. Many of them contain an inserted zinc binding domain. This domain has a GroES-like structure.


Pssm-ID: 400513 [Multi-domain]  Cd Length: 106  Bit Score: 56.46  E-value: 3.99e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   1700 QVEIEVEAAGLNFLDVLGALGMMPALEAEeSVLGRECSGRIAAVGEGVSGLRVGDEVLAVA------------------- 1760
Cdd:pfam08240    2 EVLVKVKAAGICGSDLHIYKGGNPPVKLP-LILGHEFAGEVVEVGPGVTGLKVGDRVVVEPlipcgkceycregrynlcp 80

                           90       100
                   ....*....|....*....|....*
gi 53747904   1761 ---------PGCFRSYVLVDESQVV 1776
Cdd:pfam08240   81 ngrflgydrDGGFAEYVVVPERNLV 105
PRK07529 PRK07529
AMP-binding domain protein; Validated
 2648-3132 1.04e-08

AMP-binding domain protein; Validated


Pssm-ID: 236043 [Multi-domain]  Cd Length: 632  Bit Score: 61.12  E-value: 1.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2648 ARLHPELPAL--------LAPERTLSYGELARRAQALAARLRELEVQPQELVAIAMHKGWEQATAVLGVlQAAAAYLPLD 2719
Cdd:PRK07529   35 AARHPDAPALsflldadpLDRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGG-EAAGIANPIN 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2720 PEQPPLRLHQLLEEGPARVVLTQSSLLHTVPWP---------PGVQ-VIAVDELE----PATEAPPL------------- 2772
Cdd:PRK07529  114 PLLEPEQIAELLRAAGAKVLVTLGPFPGTDIWQkvaevlaalPELRtVVEVDLARylpgPKRLAVPLirrkaharildfd 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2773 -------------PPRGTPEHLAYVIYTSGSTGKPKGVAIEHRaalNTVVD---LNTRFGVGPEDRVL------------ 2824
Cdd:PRK07529  194 aelarqpgdrlfsGRPIGPDDVAAYFHTGGTTGMPKLAQHTHG---NEVANawlGALLLGLGPGDTVFcglplfhvnall 270

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2825 --GLSALTFDLSVydvlgllgaggalVLPAAEAEKDP---AHWWERLVAGRVTVWNSTPALMLLLveyaeqrgLKLPAA- 2898
Cdd:PRK07529  271 vtGLAPLARGAHV-------------VLATPQGYRGPgviANFWKIVERYRINFLSGVPTVYAAL--------LQVPVDg 329

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2899 -----LRLVMLSGDWIPVALPDRI-RALGrdVQVVSLGGATEA-SIWSIAYPIGQVAPQWKSIPygMPLANQRFHVLDgr 2971
Cdd:PRK07529  330 hdissLRYALCGAAPLPVEVFRRFeAATG--VRIVEGYGLTEAtCVSSVNPPDGERRIGSVGLR--LPYQRVRVVILD-- 403

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2972 lEARPWWVP------GELYIGGEGLAREYwrdeplTATRFIRHPRTGERLYRTGDQGRMLPEGSIEFLGR-EDLQVKvQG 3044
Cdd:PRK07529  404 -DAGRYLRDcavdevGVLCIAGPNVFSGY------LEAAHNKGLWLEDGWLNTGDLGRIDADGYFWLTGRaKDLIIR-GG 475

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  3045 FRVELGEIEAALAQHPALSASVVVARGEPRGVRRLVAYAVPRSGQTPAAGELRRYLAERLP---AymVPSAFVLLESLPR 3121
Cdd:PRK07529  476 HNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYVQLKPGASATEAELLAFARDHIAeraA--VPKHVRILDALPK 553

                         570
                  ....*....|.
gi 53747904  3122 SRNGKIARDQL 3132
Cdd:PRK07529  554 TAVGKIFKPAL 564
liver_ADH_like1 cd08281
Zinc-dependent alcohol dehydrogenases (ADH) and class III ADG (AKA formaldehyde dehydrogenase); ...
 1692-1883 1.72e-08

Zinc-dependent alcohol dehydrogenases (ADH) and class III ADG (AKA formaldehyde dehydrogenase); NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. This group contains members identified as zinc dependent alcohol dehydrogenases (ADH), and class III ADG (aka formaldehyde dehydrogenase, FDH). Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. Class III ADH are also know as glutathione-dependent formaldehyde dehydrogenase (FDH), which convert aldehydes to the corresponding carboxylic acid and alcohol. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176241 [Multi-domain]  Cd Length: 371  Bit Score: 59.70  E-value: 1.72e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1692 TRPAPGPRQVEIEVEAAGLNFLDVLGALGMMPalEAEESVLGRECSGRIAAVGEGVSGLRVGDEVLAV-APGC------- 1763
Cdd:cd08281   27 ELDPPGPGEVLVKIAAAGLCHSDLSVINGDRP--RPLPMALGHEAAGVVVEVGEGVTDLEVGDHVVLVfVPSCghcrpca 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1764 -----------------------------------------FRSYVLVDESQVVRRPASLGLAEGAAQMVPFATAYFALH 1802
Cdd:cd08281  105 egrpalcepgaaangagtllsggrrlrlrggeinhhlgvsaFAEYAVVSRRSVVKIDKDVPLEIAALFGCAVLTGVGAVV 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1803 TVGRLRRGERILIhaaaggLGLAAVQLASRTGA------EILATAGSEQKREYLRSLGIAHVLDSRSTSFVSEVRERTGG 1876
Cdd:cd08281  185 NTAGVRPGQSVAV------VGLGGVGLSALLGAvaagasQVVAVDLNEDKLALARELGATATVNAGDPNAVEQVRELTGG 258


                 ....*..
gi 53747904 1877 rGVDVVL 1883
Cdd:cd08281  259 -GVDYAF 264
NfnB COG0778
Nitroreductase [Energy production and conversion]; Nitroreductase is part of the Pathway ...
 3279-3455 2.18e-08

Nitroreductase [Energy production and conversion]; Nitroreductase is part of the Pathway/BioSystem: Pyrimidine degradation


Pssm-ID: 440541 [Multi-domain]  Cd Length: 163  Bit Score: 56.01  E-value: 2.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3279 LTALERRRSVRTYSLEPVSHEQLGRLL-----APlrewevqgsrrylyaSAGGLYPvqlylhlkpgrarglepgtWyydp 3353
Cdd:COG0778    2 LELLLTRRSVRKFTDKPVSDEELEELLeaarlAP---------------SAGNLQP-------------------W---- 43

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3354 sthRLVLLSaGAGLDRRIHD--PHQNQAIFDSAAFSLFLIARMGAvepvYAEHALHFATLEAGLMTQLLDLGAAPSGLGL 3431
Cdd:COG0778   44 ---RFVVVR-DPELRERLAEalAEANQEWVADAPVLIVVCADPDR----SEKVPERYALLDAGIAAQNLLLAARALGLGT 115

                        170       180
                 ....*....|....*....|....
gi 53747904 3432 CHIGDLDFAQARGLFHLEEEHVLL 3455
Cdd:COG0778  116 CWIGGFDPEKVRELLGLPEGEEPV 139
PGDH cd05288
Prostaglandin dehydrogenases; Prostaglandins and related eicosanoids are metabolized by the ...
 1742-1988 2.27e-08

Prostaglandin dehydrogenases; Prostaglandins and related eicosanoids are metabolized by the oxidation of the 15(S)-hydroxyl group of the NAD+-dependent (type I 15-PGDH) 15-prostaglandin dehydrogenase (15-PGDH) followed by reduction by NADPH/NADH-dependent (type II 15-PGDH) delta-13 15-prostaglandin reductase (13-PGR) to 15-keto-13,14,-dihydroprostaglandins. 13-PGR is a bifunctional enzyme, since it also has leukotriene B(4) 12-hydroxydehydrogenase activity. These 15-PGDH and related enzymes are members of the medium chain dehydrogenase/reductase family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES.


Pssm-ID: 176190 [Multi-domain]  Cd Length: 329  Bit Score: 59.03  E-value: 2.27e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1742 AVGEGV----SGLRVGDEVLAVAPgcFRSYVLVDESQVVRR-----PASLGLAEGAAQMVPFaTAYFALHTVGRLRRGER 1812
Cdd:cd05288   72 GVGEVVesrsPDFKVGDLVSGFLG--WQEYAVVDGASGLRKldpslGLPLSAYLGVLGMTGL-TAYFGLTEIGKPKPGET 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1813 ILIHAAAGGLGLAAVQLASRTGAEILATAGSEQKREYLRS-LGIAHVLDSRSTSFVSEVRERTGGrGVDV---------- 1881
Cdd:cd05288  149 VVVSAAAGAVGSVVGQIAKLLGARVVGIAGSDEKCRWLVEeLGFDAAINYKTPDLAEALKEAAPD-GIDVyfdnvggeil 227

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1882 --VLNslagelllaglsVLAPHGRFLELGKRDLY-ADQQVGLRTLA---------RGqtFAAIDFGPHHPDFravLEEVA 1949
Cdd:cd05288  228 daALT------------LLNKGGRIALCGAISQYnATEPPGPKNLGniitkrltmQG--FIVSDYADRFPEA---LAELA 290

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 53747904 1950 TQLTQGQLEPLPTRLFPARQVAEAFSFMARALHIGRVAV 1988
Cdd:cd05288  291 KWLAEGKLKYREDVVEGLENAPEAFLGLFTGKNTGKLVV 329
PRK07059 PRK07059
Long-chain-fatty-acid--CoA ligase; Validated
 2957-3132 2.33e-08

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


Pssm-ID: 235923 [Multi-domain]  Cd Length: 557  Bit Score: 60.03  E-value: 2.33e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2957 GMPLANQRFHVLDGRLEARPWWVPGELYIGGEGLAREYWRDEPLTAtRFIrhprTGERLYRTGDQGRMLPEGSIEFLGRE 3036
Cdd:PRK07059  383 GLPLPSTEVSIRDDDGNDLPLGEPGEICIRGPQVMAGYWNRPDETA-KVM----TADGFFRTGDVGVMDERGYTKIVDRK 457

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  3037 DLQVKVQGFRVELGEIEAALAQHPALSASVVVARGEPRGVRRLVAYAVpRSGQTPAAGELRRYLAERLPAYMVPSAFVLL 3116
Cdd:PRK07059  458 KDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFVV-KKDPALTEEDVKAFCKERLTNYKRPKFVEFR 536

                         170
                  ....*....|....*.
gi 53747904  3117 ESLPRSRNGKIARDQL 3132
Cdd:PRK07059  537 TELPKTNVGKILRREL 552
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
 2079-2145 2.35e-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: 53.79  E-value: 2.35e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 53747904    2079 PQALPPSSLEQLIEQVWRKHLGV-------ERVQPTDSFFQLGGDSLLGIQVAADLRRHLGVELPTATLFSHPT 2145
Cdd:smart00823    1 LAALPPAERRRLLLDLVREQVAAvlghaaaEAIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPT 74
MACS_like_1 cd05974
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
 2786-3132 2.59e-08

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: 59.50  E-value: 2.59e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2786 YTSGSTGKPKGVaiEHRAALNTVVDLNTRFGVG--PEDRVLGLSALTFDLSVYDVLGLLGAGGALVLPAAEAEKDPAHWW 2863
Cdd:cd05974   92 FTSGTTSKPKLV--EHTHRSYPVGHLSTMYWIGlkPGDVHWNISSPGWAKHAWSCFFAPWNAGATVFLFNYARFDAKRVL 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2864 ERLVAGRVTVWNSTPALMLLLVEyaeQRGLKLPAALRLVMLSGDWIPVALPDRIRAL-GRDVQvvSLGGATEASIWSIAY 2942
Cdd:cd05974  170 AALVRYGVTTLCAPPTVWRMLIQ---QDLASFDVKLREVVGAGEPLNPEVIEQVRRAwGLTIR--DGYGQTETTALVGNS 244

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2943 PiGQVApqwKSIPYGMPLANQRFHVLDGrlEARPWwVPGE--LYIGGE---GLAREYWRDEPLTATRFirhprtGERLYR 3017
Cdd:cd05974  245 P-GQPV---KAGSMGRPLPGYRVALLDP--DGAPA-TEGEvaLDLGDTrpvGLMKGYAGDPDKTAHAM------RGGYYR 311

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3018 TGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPALSASVVVARGEPRGVRRLVAYAVPRSGQTPA---AG 3094
Cdd:cd05974  312 TGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGYEPSpetAL 391

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 53747904 3095 ELRRYLAERLPAYMVPSAFVLLEsLPRSRNGKIARDQL 3132
Cdd:cd05974  392 EIFRFSRERLAPYKRIRRLEFAE-LPKTISGKIRRVEL 428
LC-FACS_euk cd05927
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ...
 2753-2822 2.60e-08

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: 59.92  E-value: 2.60e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 53747904 2753 PGVQVIAVDELEP-ATEAPPLPPRGTPEHLAYVIYTSGSTGKPKGVAIEHRAALNTVVDLNT----RFGVGPEDR 2822
Cdd:cd05927   87 AGVKVYSLEEFEKlGKKNKVPPPPPKPEDLATICYTSGTTGNPKGVMLTHGNIVSNVAGVFKileiLNKINPTDV 161
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 1222-1362 2.73e-08

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: 57.29  E-value: 2.73e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1222 RTQHRIRCLLELEQLGAEVQVYTADVAEEAAVRSVVEQVHARWGKIHGVLHAAATFDDGVIQLRTHEQSSRALRTKVRGS 1301
Cdd:cd05233   30 RNEEALAELAAIEALGGNAVAVQADVSDEEDVEALVEEALEEFGRLDILVNNAGIARPGPLEELTDEDWDRVLDVNLTGV 109

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 53747904 1302 M-VLHEVLAsegldwfALC----------SSLASALGSFGQADYCAANAFQDayahhlrrqGFTGALALDWG 1362
Cdd:cd05233  110 FlLTRAALP-------HMKkqgggrivniSSVAGLRPLPGQAAYAASKAALE---------GLTRSLALELA 165
CAD1 cd05283
Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the ...
 1692-1908 2.91e-08

Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the medium chain dehydrogenase/reductase family, reduce cinnamaldehydes to cinnamyl alcohols in the last step of monolignal metabolism in plant cells walls. CAD binds 2 zinc ions and is NADPH- dependent. CAD family members are also found in non-plant species, e.g. in yeast where they have an aldehyde reductase activity. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176186 [Multi-domain]  Cd Length: 337  Bit Score: 58.66  E-value: 2.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1692 TRPAPGPRQVEIEVEAAGLNFLDVL---GALGMMPAleaeESVLGRECSGRIAAVGEGVSGLRVGDEVlAVapGCFR--- 1765
Cdd:cd05283   18 ERRPLGPDDVDIKITYCGVCHSDLHtlrNEWGPTKY----PLVPGHEIVGIVVAVGSKVTKFKVGDRV-GV--GCQVdsc 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1766 ------------------------------------SYVLVDESQVVRRPASLGLAEGAaqmvPF----ATAYFALHTVG 1805
Cdd:cd05283   91 gtceqcksgeeqycpkgvvtyngkypdgtitqggyaDHIVVDERFVFKIPEGLDSAAAA----PLlcagITVYSPLKRNG 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1806 rLRRGERI-------LIHAaagglglaAVQLASRTGAEILATAGSEQKREYLRSLGIAHVLDSRSTSFVSEVRertggRG 1878
Cdd:cd05283  167 -VGPGKRVgvvgiggLGHL--------AVKFAKALGAEVTAFSRSPSKKEDALKLGADEFIATKDPEAMKKAA-----GS 232

                        250       260       270
                 ....*....|....*....|....*....|.
gi 53747904 1879 VDVVLNSLAGELLLAG-LSVLAPHGRFLELG 1908
Cdd:cd05283  233 LDLIIDTVSASHDLDPyLSLLKPGGTLVLVG 263
6_hydroxyhexanoate_dh_like cd08240
6-hydroxyhexanoate dehydrogenase; 6-hydroxyhexanoate dehydrogenase, an enzyme of the ...
 1693-1883 3.05e-08

6-hydroxyhexanoate dehydrogenase; 6-hydroxyhexanoate dehydrogenase, an enzyme of the zinc-dependent alcohol dehydrogenase-like family of medium chain dehydrogenases/reductases catalyzes the conversion of 6-hydroxyhexanoate and NAD(+) to 6-oxohexanoate + NADH and H+. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains, at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176202 [Multi-domain]  Cd Length: 350  Bit Score: 58.78  E-value: 3.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1693 RPAPGPRQVEIEVEAAGL---------NFLDvLGALGMMPALEAEES---VLGRECSGRIAAVGEGVSGLRVGDEVLA-- 1758
Cdd:cd08240   20 TPKPPGTEVLVKVTACGVchsdlhiwdGGYD-LGGGKTMSLDDRGVKlplVLGHEIVGEVVAVGPDAADVKVGDKVLVyp 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1759 --------------------------VAPGCFRSYVLVDESQVVRRPASLGLAEGAAQMVPFATAYFALHTVGRLRRGER 1812
Cdd:cd08240   99 wigcgecpvclagdenlcakgralgiFQDGGYAEYVIVPHSRYLVDPGGLDPALAATLACSGLTAYSAVKKLMPLVADEP 178

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 53747904 1813 ILIhAAAGGLGLAAVQLASRTG-AEILATAGSEQKREYLRSLGIAHVLDSRSTSFVSEVRERTGGrGVDVVL 1883
Cdd:cd08240  179 VVI-IGAGGLGLMALALLKALGpANIIVVDIDEAKLEAAKAAGADVVVNGSDPDAAKRIIKAAGG-GVDAVI 248
ETR_like_1 cd08291
2-enoyl thioester reductase (ETR) like proteins, child 1; 2-enoyl thioester reductase (ETR) ...
 1676-1872 4.04e-08

2-enoyl thioester reductase (ETR) like proteins, child 1; 2-enoyl thioester reductase (ETR) like proteins. ETR catalyzes the NADPH-dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the 2-enoyl thioester reductase (ETR) like proteins. ETR catalyzes the NADPH-dependent dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. Candida tropicalis enoyl thioester reductase (Etr1p) catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis. Etr1p forms homodimers, with each subunit containing a nucleotide-binding Rossmann fold domain and a catalytic domain.


Pssm-ID: 176251 [Multi-domain]  Cd Length: 324  Bit Score: 58.00  E-value: 4.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1676 AVGTPGLLESLGLRRCTRPAPGPRQVEIEVEAAGLNFLDVL---GALGMMPALEAeesVLGRECSGRIAAVGEG-VSGLR 1751
Cdd:cd08291    8 EYGKPLEVKELSLPEPEVPEPGPGEVLIKVEAAPINPSDLGflkGQYGSTKALPV---PPGFEGSGTVVAAGGGpLAQSL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1752 VGDEVLAVAP--GCFRSYVLVDESQVVRRPASLGLAEGAAQMV-PFaTAYFALHTVgrLRRGERILIHAAAGGLG-LAAV 1827
Cdd:cd08291   85 IGKRVAFLAGsyGTYAEYAVADAQQCLPLPDGVSFEQGASSFVnPL-TALGMLETA--REEGAKAVVHTAAASALgRMLV 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 53747904 1828 QLASRTGAEILATAGSEQKREYLRSLGIAHVLDSRSTSFVSEVRE 1872
Cdd:cd08291  162 RLCKADGIKVINIVRRKEQVDLLKKIGAEYVLNSSDPDFLEDLKE 206
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 1234-1351 4.76e-08

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: 56.73  E-value: 4.76e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1234 EQLGAEVQVYTADVAEEAAVRSVVEQVHARWGKIHGVLHAAATFDDGVIQLRTHEQSSRALRTKVRGSM-VLHEVL---- 1308
Cdd:COG4221   47 AELGGRALAVPLDVTDEAAVEAAVAAAVAEFGRLDVLVNNAGVALLGPLEELDPEDWDRMIDVNVKGVLyVTRAALpamr 126

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 53747904 1309 -ASEGLdwFALCSSLASALGSFGQADYCAANAFQDAYAHHLRRQ 1351
Cdd:COG4221  127 aRGSGH--IVNISSIAGLRPYPGGAVYAATKAAVRGLSESLRAE 168
PLN02246 PLN02246
4-coumarate--CoA ligase
 2662-3132 5.66e-08

4-coumarate--CoA ligase


Pssm-ID: 215137 [Multi-domain]  Cd Length: 537  Bit Score: 58.45  E-value: 5.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2662 RTLSYGELARRAQALAARLRELEVQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLDPEQPPLRLHQLLEEGPARVVLT 2741
Cdd:PLN02246   49 RVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLIIT 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2742 QSSLLHTVP---WPPGVQVIAVD----------ELEPATEAPPLPPRGTPEHLAYVIYTSGSTGKPKGVAIEHRAALNTV 2808
Cdd:PLN02246  129 QSCYVDKLKglaEDDGVTVVTIDdppegclhfsELTQADENELPEVEISPDDVVALPYSSGTTGLPKGVMLTHKGLVTSV 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2809 ---VD-LNTRFGVGPEDRVL-----------------GL---SALT----FDLsvydvlgllgaggalvlpAAEAEKDPA 2860
Cdd:PLN02246  209 aqqVDgENPNLYFHSDDVILcvlpmfhiyslnsvllcGLrvgAAILimpkFEI------------------GALLELIQR 270

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2861 HwwerlvagRVTVWNSTPALMLLLVE--YAEQRGLklpAALRLVMlSGdwipvALP------DRIRAlgRDVQVVsLG-- 2930
Cdd:PLN02246  271 H--------KVTIAPFVPPIVLAIAKspVVEKYDL---SSIRMVL-SG-----AAPlgkeleDAFRA--KLPNAV-LGqg 330

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2931 -GATEAS---IWSIAY-----PIgqvapqwKSIPYGMPLANQRFHVLD---GrlEARPWWVPGELYIGGEGLAREYWRDE 2998
Cdd:PLN02246  331 yGMTEAGpvlAMCLAFakepfPV-------KSGSCGTVVRNAELKIVDpetG--ASLPRNQPGEICIRGPQIMKGYLNDP 401

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2999 PLTAtrfirhprtgerlyRTGDQGRMLPEGSIEFLGRED-------LQ--VKVQGFRVELGEIEAALAQHPALSASVVVA 3069
Cdd:PLN02246  402 EATA--------------NTIDKDGWLHTGDIGYIDDDDelfivdrLKelIKYKGFQVAPAELEALLISHPSIADAAVVP 467

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 53747904  3070 RGEPRGVRRLVAYAVPRSGQTPAAGELRRYLAERLPAYMVPSAFVLLESLPRSRNGKIARDQL 3132
Cdd:PLN02246  468 MKDEVAGEVPVAFVVRSNGSEITEDEIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDL 530
LC_FACS_euk1 cd17639
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ...
 2776-3069 9.39e-08

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: 58.00  E-value: 9.39e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2776 GTPEHLAYVIYTSGSTGKPKGVAIEHRAALNTVVDLNTRFG--VGPEDRVLGL-------------------------SA 2828
Cdd:cd17639   85 GKPDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRVPelLGPDDRYLAYlplahifelaaenvclyrggtigygSP 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2829 LTF----------DLSVYdvlgllGAGGALVLPAAeaekdpahwWERLVAGRVTVWNSTPALMLLLVEYAEQRGLKlpaA 2898
Cdd:cd17639  165 RTLtdkskrgckgDLTEF------KPTLMVGVPAI---------WDTIRKGVLAKLNPMGGLKRTLFWTAYQSKLK---A 226

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2899 LRLVMLSGDWIPVALpDRIR-ALGRDVQVVSLGGA-----TEASIWSIAYPIGQ-------VA-------PQWKSIPYGM 2958
Cdd:cd17639  227 LKEGPGTPLLDELVF-KKVRaALGGRLRYMLSGGAplsadTQEFLNIVLCPVIQgygltetCAggtvqdpGDLETGRVGP 305

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2959 PLANQRFHVLD----GRLEARPwwVP-GELYIGGEGLAREYWRDEPLTATRFirhprTGERLYRTGDQGRMLPEGSIEFL 3033
Cdd:cd17639  306 PLPCCEIKLVDweegGYSTDKP--PPrGEILIRGPNVFKGYYKNPEKTKEAF-----DGDGWFHTGDIGEFHPDGTLKII 378

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 53747904 3034 GR-EDLqVKVQ-GFRVELGEIEAALAQHPALSASVVVA 3069
Cdd:cd17639  379 DRkKDL-VKLQnGEYIALEKLESIYRSNPLVNNICVYA 415
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
 2072-2145 1.02e-07

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: 58.54  E-value: 1.02e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 53747904   2072 GRAAAAEPQALppSSLEQLIEQVWRKHL--GVERVQPTDSFFQLGGDSLLGIQVAADLRRHLGVELPTATLFSHPT 2145
Cdd:TIGR03443  836 NRSASAADEEF--TETEREIRDLWLELLpnRPATISPDDSFFDLGGHSILATRMIFELRKKLNVELPLGLIFKSPT 909
PRK05850 PRK05850
acyl-CoA synthetase; Validated
 2691-2802 1.17e-07

acyl-CoA synthetase; Validated


Pssm-ID: 235624 [Multi-domain]  Cd Length: 578  Bit Score: 57.64  E-value: 1.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2691 VAIAMHKGWEQATAVLGVLQAAAAYLPLDPEQPPL---RLHQLLEEGPARVVLTQSSLLHTV-------PWPPGVQVIAV 2760
Cdd:PRK05850   62 AVILAPQGLEYIVAFLGALQAGLIAVPLSVPQGGAhdeRVSAVLRDTSPSVVLTTSAVVDDVteyvapqPGQSAPPVIEV 141

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 53747904  2761 DELEPATEAPPLPPRGTPEHLAYVIYTSGSTGKPKGVAIEHR 2802
Cdd:PRK05850  142 DLLDLDSPRGSDARPRDLPSTAYLQYTSGSTRTPAGVMVSHR 183
PRK08162 PRK08162
acyl-CoA synthetase; Validated
 2786-3134 1.30e-07

acyl-CoA synthetase; Validated


Pssm-ID: 236169 [Multi-domain]  Cd Length: 545  Bit Score: 57.65  E-value: 1.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2786 YTSGSTGKPKGVAIEHR-AALNTVVDLnTRFGVGPedRVLGLSAL--------TFDLSVydvlgllgaggalvlpAAEA- 2855
Cdd:PRK08162  189 YTSGTTGNPKGVVYHHRgAYLNALSNI-LAWGMPK--HPVYLWTLpmfhcngwCFPWTV----------------AARAg 249

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2856 ------EKDPAHWWERLVAGRVTVWNSTPALMLLLV--EYAEQRGLKLPAAlrlVMLSGDWIPVALPDRIRALGRDVQVV 2927
Cdd:PRK08162  250 tnvclrKVDPKLIFDLIREHGVTHYCGAPIVLSALInaPAEWRAGIDHPVH---AMVAGAAPPAAVIAKMEEIGFDLTHV 326

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2928 SlgGATEasiwsiAY-PIGQVA--PQWKSipygMPLANQ---------RFHVLDG-------RLEARPW--WVPGELYIG 2986
Cdd:PRK08162  327 Y--GLTE------TYgPATVCAwqPEWDA----LPLDERaqlkarqgvRYPLQEGvtvldpdTMQPVPAdgETIGEIMFR 394

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2987 GEGLAREYWRDEPLTATRFirhpRTGerLYRTGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPALSASV 3066
Cdd:PRK08162  395 GNIVMKGYLKNPKATEEAF----AGG--WFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAA 468

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 53747904  3067 VVARGEPRGVRRLVAYAVPRSGQTPAAGELRRYLAERLPAYMVPSAFVLLEsLPRSRNGKIARDQLPE 3134
Cdd:PRK08162  469 VVAKPDPKWGEVPCAFVELKDGASATEEEIIAHCREHLAGFKVPKAVVFGE-LPKTSTGKIQKFVLRE 535
tdh PRK05396
L-threonine 3-dehydrogenase; Validated
 1694-1883 1.44e-07

L-threonine 3-dehydrogenase; Validated


Pssm-ID: 180054 [Multi-domain]  Cd Length: 341  Bit Score: 56.37  E-value: 1.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  1694 PAPGPRQVEIEVEAAGLNFLDV------LGALGMMPAleaeESVLGRECSGRIAAVGEGVSGLRVGDEV----------- 1756
Cdd:PRK05396   21 PEPGPNDVLIKVKKTAICGTDVhiynwdEWAQKTIPV----PMVVGHEFVGEVVEVGSEVTGFKVGDRVsgeghivcghc 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  1757 ----------------LAV-APGCFRSYVLVDESQVVRRPASLGLAEGAAQMvPFATAyfaLHTV--GRLRrGERILIha 1817
Cdd:PRK05396   97 rncragrrhlcrntkgVGVnRPGAFAEYLVIPAFNVWKIPDDIPDDLAAIFD-PFGNA---VHTAlsFDLV-GEDVLI-- 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  1818 aagglglaavqlasrTGA-----------------EILATAGSEQKREYLRSLGIAHVLDSRSTSFVSEVRERTGGRGVD 1880
Cdd:PRK05396  170 ---------------TGAgpigimaaavakhvgarHVVITDVNEYRLELARKMGATRAVNVAKEDLRDVMAELGMTEGFD 234


                  ...
gi 53747904  1881 VVL 1883
Cdd:PRK05396  235 VGL 237
PLN02479 PLN02479
acetate-CoA ligase
 3016-3132 1.73e-07

acetate-CoA ligase


Pssm-ID: 178097 [Multi-domain]  Cd Length: 567  Bit Score: 57.16  E-value: 1.73e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  3016 YRTGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPALSASVVVARGEPRGVRRLVAYAVPRSG-----QT 3090
Cdd:PLN02479  432 FHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFVTLKPGvdksdEA 511

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 53747904  3091 PAAGELRRYLAERLPAYMVPSAfVLLESLPRSRNGKIARDQL 3132
Cdd:PLN02479  512 ALAEDIMKFCRERLPAYWVPKS-VVFGPLPKTATGKIQKHVL 552
PRK13390 PRK13390
acyl-CoA synthetase; Provisional
 2646-3132 1.76e-07

acyl-CoA synthetase; Provisional


Pssm-ID: 139538 [Multi-domain]  Cd Length: 501  Bit Score: 56.94  E-value: 1.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2646 TQARLHPELPALLAPE--RTLSYGELARRAQALAARLRELEVQPQELVAIaMHKGWEQATAVLGVLQAAAAYL-PLDPEQ 2722
Cdd:PRK13390    5 THAQIAPDRPAVIVAEtgEQVSYRQLDDDSAALARVLYDAGLRTGDVVAL-LSDNSPEALVVLWAALRSGLYItAINHHL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2723 PPLRLHQLLEEGPARVVLTQSSL---LHTVPWPPGVQVIAVDELE-----PATEAPPLPPRGTPEHLAYVIYTSGSTGKP 2794
Cdd:PRK13390   84 TAPEADYIVGDSGARVLVASAALdglAAKVGADLPLRLSFGGEIDgfgsfEAALAGAGPRLTEQPCGAVMLYSSGTTGFP 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2795 KGVAiehraalntvVDLNTRFGVGPEDRVLGLSALTFDLSVYDvlgllgaGGALVLPAAEAEkdPAHWW----------- 2863
Cdd:PRK13390  164 KGIQ----------PDLPGRDVDAPGDPIVAIARAFYDISESD-------IYYSSAPIYHAA--PLRWCsmvhalggtvv 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2864 --ERLVAG---------RVTVWNSTPALMLLLVEY-AEQRGLKLPAALRLVMLSGDWIPV----ALPDRIRALgrdvqVV 2927
Cdd:PRK13390  225 laKRFDAQatlghveryRITVTQMVPTMFVRLLKLdADVRTRYDVSSLRAVIHAAAPCPVdvkhAMIDWLGPI-----VY 299

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2928 SLGGATEASIWSIAYpigqvAPQWKSIP--YGMPLANQrFHVLDGRLEARPWWVPGELYIGGEGLAREYWRDEPLTATrf 3005
Cdd:PRK13390  300 EYYSSTEAHGMTFID-----SPDWLAHPgsVGRSVLGD-LHICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAA-- 371

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  3006 IRHPrtGERLYRT-GDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPALSASVVVARGEP---RGVRRLVA 3081
Cdd:PRK13390  372 AQHP--AHPFWTTvGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPemgEQVKAVIQ 449

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 53747904  3082 YAVPRSGQTPAAGELRRYLAERLPAYMVPSAFVLLESLPRSRNGKIARDQL 3132
Cdd:PRK13390  450 LVEGIRGSDELARELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLL 500
FCS cd05921
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ...
 2648-3107 1.77e-07

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: 57.06  E-value: 1.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2648 ARLHPELPALLAPE-----RTLSYGELARRAQALAARLRELEVQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLDPE- 2721
Cdd:cd05921    5 ARQAPDRTWLAEREgnggwRRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPAy 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2722 ----QPPLRLHQLLEEGPARVVLTQS----------------SLLHTVPWPPGVQVIAVDEL---EPATEAPPLPPRGTP 2778
Cdd:cd05921   85 slmsQDLAKLKHLFELLKPGLVFAQDaapfaralaaifplgtPLVVSRNAVAGRGAISFAELaatPPTAAVDAAFAAVGP 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2779 EHLAYVIYTSGSTGKPKGVAIEHRA-ALNTVVDLNTRFGVGPEDRVL----------GLSAlTFDLSVYDVLGLLGAgga 2847
Cdd:cd05921  165 DTVAKFLFTSGSTGLPKAVINTQRMlCANQAMLEQTYPFFGEEPPVLvdwlpwnhtfGGNH-NFNLVLYNGGTLYID--- 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2848 lvlpaaEAEKDPAHWWERLVAGR---VTVWNSTPALMLLLVEYAEQ-RGL--KLPAALRLVMLSGDWIPVALPDRIRAL- 2920
Cdd:cd05921  241 ------DGKPMPGGFEETLRNLReisPTVYFNVPAGWEMLVAALEKdEALrrRFFKRLKLMFYAGAGLSQDVWDRLQALa 314

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2921 ----GRDVQVVSLGGATEASIWSiaypIGQVAPQWKSIPYGMPLANQRFHVL--DGRLEAR---PWWVPGelyiggegla 2991
Cdd:cd05921  315 vatvGERIPMMAGLGATETAPTA----TFTHWPTERSGLIGLPAPGTELKLVpsGGKYEVRvkgPNVTPG---------- 380

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2992 reYWRDEPLTATRFirhprTGERLYRTGDQGRML----PEGSIEFLGR--EDLQVKvQGFRVELGEIEAAL--AQHPALS 3063
Cdd:cd05921  381 --YWRQPELTAQAF-----DEEGFYCLGDAAKLAdpddPAKGLVFDGRvaEDFKLA-SGTWVSVGPLRARAvaACAPLVH 452

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....
gi 53747904 3064 ASVVVARGE----------PRGVRRLVAYAVPRSGQTPAAGELRRYLAERLPAY 3107
Cdd:cd05921  453 DAVVAGEDRaevgalvfpdLLACRRLVGLQEASDAEVLRHAKVRAAFRDRLAAL 506
Zn_ADH1 cd05279
Liver alcohol dehydrogenase and related zinc-dependent alcohol dehydrogenases; NAD(P)(H) ...
 1676-1880 2.02e-07

Liver alcohol dehydrogenase and related zinc-dependent alcohol dehydrogenases; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. There are 7 vertebrate ADH 7 classes, 6 of which have been identified in humans. Class III, glutathione-dependent formaldehyde dehydrogenase, has been identified as the primordial form and exists in diverse species, including plants, micro-organisms, vertebrates, and invertebrates. Class I, typified by liver dehydrogenase, is an evolving form. Gene duplication and functional specialization of ADH into ADH classes and subclasses created numerous forms in vertebrates. For example, the A, B and C (formerly alpha, beta, gamma) human class I subunits have high overall structural similarity, but differ in the substrate binding pocket and therefore in substrate specificity. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine (His-51), the ribose of NAD, a serine (Ser-48), then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of an beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding.


Pssm-ID: 176182 [Multi-domain]  Cd Length: 365  Bit Score: 56.29  E-value: 2.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1676 AVGTPGLLESLGLRrctrpAPGPRQVEIEVEAAGLNFLDVLGALGMMPALEAeeSVLGRECSGRIAAVGEGVSGLRVGDE 1755
Cdd:cd05279    8 EKGKPLSIEEIEVA-----PPKAGEVRIKVVATGVCHTDLHVIDGKLPTPLP--VILGHEGAGIVESIGPGVTTLKPGDK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1756 VLAV-APGC------------------------------------------------FRSYVLVDESQVVRRPASLGLAE 1786
Cdd:cd05279   81 VIPLfGPQCgkckqclnprpnlcsksrgtngrglmsdgtsrftckgkpihhflgtstFAEYTVVSEISLAKIDPDAPLEK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1787 GAAQMVPFATAYFALHTVGRLRRGERILIhaaaggLGLAAVQLASRTGAE------ILATAGSEQKREYLRSLGIAHVLD 1860
Cdd:cd05279  161 VCLIGCGFSTGYGAAVNTAKVTPGSTCAV------FGLGGVGLSVIMGCKaagasrIIAVDINKDKFEKAKQLGATECIN 234

                        250       260
                 ....*....|....*....|..
gi 53747904 1861 SRSTSF-VSEV-RERTGGrGVD 1880
Cdd:cd05279  235 PRDQDKpIVEVlTEMTDG-GVD 255
LC_FACS_like cd17640
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ...
 2777-3085 2.84e-07

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: 56.21  E-value: 2.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2777 TPEHLAYVIYTSGSTGKPKGVAIEHRAALNTVVDLNTRFGVGPEDRVLGLsaltfdLSVYDVLGLLGAGGALVLPAAEAE 2856
Cdd:cd17640   86 DSDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQPGDRFLSI------LPIWHSYERSAEYFIFACGCSQAY 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2857 KDPAHWWERLVAGRVTVWNSTPALMLLLVEYAEQRGLKLPAALRLV---MLSGDWIPV------ALPDRI----RALGRD 2923
Cdd:cd17640  160 TSIRTLKDDLKRVKPHYIVSVPRLWESLYSGIQKQVSKSSPIKQFLflfFLSGGIFKFgisgggALPPHVdtffEAIGIE 239

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2924 VQVvslG-GATEASiwsiayPIGQVAPQWKSI--PYGMPLANQRFHVLD--GRlEARPWWVPGELYIGGEGLAREYWRDe 2998
Cdd:cd17640  240 VLN---GyGLTETS------PVVSARRLKCNVrgSVGRPLPGTEIKIVDpeGN-VVLPPGEKGIVWVRGPQVMKGYYKN- 308

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2999 PLTATRFIrhprTGERLYRTGDQGRMLPEGSIEFLGRE-DLQVKVQGFRVELGEIEAALAQHPALSASVVVARGEprgvR 3077
Cdd:cd17640  309 PEATSKVL----DSDGWFNTGDLGWLTCGGELVLTGRAkDTIVLSNGENVEPQPIEEALMRSPFIEQIMVVGQDQ----K 380


                 ....*...
gi 53747904 3078 RLVAYAVP 3085
Cdd:cd17640  381 RLGALIVP 388
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
1232-1362 3.67e-07

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 54.40  E-value: 3.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  1232 ELEQLGAEVQVYTADVAEEAAVRSVVEQVHARWGKIHGVLHAAATFDDGVIQLRTHEQSSRALRTKVRGSM-VLHEVLAS 1310
Cdd:PRK05653   48 ELRAAGGEARVLVFDVSDEAAVRALIEAAVEAFGALDILVNNAGITRDALLPRMSEEDWDRVIDVNLTGTFnVVRAALPP 127

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 53747904  1311 ---EGLDWFALCSSLASALGSFGQADYCAANAFQdayahhlrrQGFTGALALDWG 1362
Cdd:PRK05653  128 mikARYGRIVNISSVSGVTGNPGQTNYSAAKAGV---------IGFTKALALELA 173
MDR_yhdh_yhfp cd05280
Yhdh and yhfp-like putative quinone oxidoreductases; Yhdh and yhfp-like putative quinone ...
 1685-1860 4.04e-07

Yhdh and yhfp-like putative quinone oxidoreductases; Yhdh and yhfp-like putative quinone oxidoreductases (QOR). QOR catalyzes the conversion of a quinone + NAD(P)H to a hydroquinone + NAD(P)+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR actin the respiratory chains of bacteria and mitochondria, while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family, but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176183 [Multi-domain]  Cd Length: 325  Bit Score: 54.86  E-value: 4.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1685 SLGLRRCTRPAPGPRQVEIEVEAAGLNFLDVLGALGMMPALEAEESVLGRECSGRIAAVGEGvsGLRVGDEVLAVA---- 1760
Cdd:cd05280   14 SLFLRTLPLDDLPEGDVLIRVHYSSLNYKDALAATGNGGVTRNYPHTPGIDAAGTVVSSDDP--RFREGDEVLVTGydlg 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1761 ---PGCFRSYVLVDESQVVRRPASLGLAEGAAqmvpFATAYFA--------LHTVGRLRRGErILIHAAAGGLGLAAVQL 1829
Cdd:cd05280   92 mntDGGFAEYVRVPADWVVPLPEGLSLREAMI----LGTAGFTaalsvhrlEDNGQTPEDGP-VLVTGATGGVGSIAVAI 166

                        170       180       190
                 ....*....|....*....|....*....|.
gi 53747904 1830 ASRTGAEILATAGSEQKREYLRSLGIAHVLD 1860
Cdd:cd05280  167 LAKLGYTVVALTGKEEQADYLKSLGASEVLD 197
PRK00174 PRK00174
acetyl-CoA synthetase; Provisional
 3016-3129 5.70e-07

acetyl-CoA synthetase; Provisional


Pssm-ID: 234677 [Multi-domain]  Cd Length: 637  Bit Score: 55.53  E-value: 5.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  3016 YRTGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPALSASVVVAR-----GEprGVrrlVAYAVPRSGQT 3090
Cdd:PRK00174  485 YFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRpddikGQ--GI---YAFVTLKGGEE 559

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 53747904  3091 PAAG---ELRRYLAERLPAYMVPSAFVLLESLPRSRNGKIAR 3129
Cdd:PRK00174  560 PSDElrkELRNWVRKEIGPIAKPDVIQFAPGLPKTRSGKIMR 601
prpE PRK10524
propionyl-CoA synthetase; Provisional
 2995-3129 5.82e-07

propionyl-CoA synthetase; Provisional


Pssm-ID: 182517 [Multi-domain]  Cd Length: 629  Bit Score: 55.34  E-value: 5.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2995 WRDEpltaTRFIRH--PRTGERLYRTGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPALSASVVVARGE 3072
Cdd:PRK10524  456 WGDD----DRFVKTywSLFGRQVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKD 531

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 53747904  3073 PRGVRRLVAYAVPRSG---QTPAA-----GELRRYLAERLPAYMVPSAFVLLESLPRSRNGKIAR 3129
Cdd:PRK10524  532 ALKGQVAVAFVVPKDSdslADREArlaleKEIMALVDSQLGAVARPARVWFVSALPKTRSGKLLR 596
Zn_ADH8 cd08262
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR) ...
 1694-1883 6.76e-07

Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176223 [Multi-domain]  Cd Length: 341  Bit Score: 54.62  E-value: 6.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1694 PAPGPRQVEIEVEAAG-----LNFLD-----VLGALGMMPALEAEESVLGRECSGRIAAVGEGVSG-LRVGDEVLAV--- 1759
Cdd:cd08262   19 PEPGPGQVLVKVLACGicgsdLHATAhpeamVDDAGGPSLMDLGADIVLGHEFCGEVVDYGPGTERkLKVGTRVTSLpll 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1760 ---------------APGCFRSYVLVDESQVVRRPASLGLAEgAAQMVPFATAYFALhTVGRLRRGERILIHAAAGGLGL 1824
Cdd:cd08262   99 lcgqgascgiglspeAPGGYAEYMLLSEALLLRVPDGLSMED-AALTEPLAVGLHAV-RRARLTPGEVALVIGCGPIGLA 176

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 53747904 1825 AAVQLASRTGAEILATAGSEQKREYLRSLGIAHVLDSRSTS---FVSEVRERTGGRGVDVVL 1883
Cdd:cd08262  177 VIAALKARGVGPIVASDFSPERRALALAMGADIVVDPAADSpfaAWAAELARAGGPKPAVIF 238
PRK08276 PRK08276
long-chain-fatty-acid--CoA ligase; Validated
 2966-3135 1.13e-06

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


Pssm-ID: 236215 [Multi-domain]  Cd Length: 502  Bit Score: 54.52  E-value: 1.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2966 HVLDGRLEARPWWVPGELYIGGEGLAREYWRDEplTATRFIRHPRTgerLYRTGDQGRMLPEGSIEFLGREDLQVKVQGF 3045
Cdd:PRK08276  326 RILDEDGNELPPGEIGTVYFEMDGYPFEYHNDP--EKTAAARNPHG---WVTVGDVGYLDEDGYLYLTDRKSDMIISGGV 400

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  3046 RVELGEIEAALAQHPA-LSASVVVARGEPRGvRRLVAYAVPRSGQTPA---AGELRRYLAERLPAYMVPSAFVLLESLPR 3121
Cdd:PRK08276  401 NIYPQEIENLLVTHPKvADVAVFGVPDEEMG-ERVKAVVQPADGADAGdalAAELIAWLRGRLAHYKCPRSIDFEDELPR 479

                         170
                  ....*....|....
gi 53747904  3122 SRNGKIARDQLPEP 3135
Cdd:PRK08276  480 TPTGKLYKRRLRDR 493
PRK07514 PRK07514
malonyl-CoA synthase; Validated
 2652-2824 1.24e-06

malonyl-CoA synthase; Validated


Pssm-ID: 181011 [Multi-domain]  Cd Length: 504  Bit Score: 54.11  E-value: 1.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2652 PELPALLAPE-RTLSYGELARRAQALAARLRELEVQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLDPEQPPLRLHQL 2730
Cdd:PRK07514   16 RDAPFIETPDgLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYF 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2731 LEE-GPARVVLTQSSL--LHTVPWPPGVQ-VIAVDE------LEPATEAPPL---PPRGtPEHLAYVIYTSGSTGKPKGV 2797
Cdd:PRK07514   96 IGDaEPALVVCDPANFawLSKIAAAAGAPhVETLDAdgtgslLEAAAAAPDDfetVPRG-ADDLAAILYTSGTTGRSKGA 174

                         170       180
                  ....*....|....*....|....*..
gi 53747904  2798 AIEHRAALNTVVDLNTRFGVGPEDRVL 2824
Cdd:PRK07514  175 MLSHGNLLSNALTLVDYWRFTPDDVLI 201
entE PRK10946
(2,3-dihydroxybenzoyl)adenylate synthase;
3016-3132 2.04e-06

(2,3-dihydroxybenzoyl)adenylate synthase;


Pssm-ID: 236803 [Multi-domain]  Cd Length: 536  Bit Score: 53.46  E-value: 2.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  3016 YRTGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPALSASVVVARGEPRGVRRLVAYAVPRSGQTPAAge 3095
Cdd:PRK10946  411 YCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVVKEPLKAVQ-- 488

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 53747904  3096 LRRYLAERLPA-YMVPSAFVLLESLPRSRNGKIARDQL 3132
Cdd:PRK10946  489 LRRFLREQGIAeFKLPDRVECVDSLPLTAVGKVDKKQL 526
X-Domain_NRPS cd19546
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ...
 2179-2489 2.22e-06

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: 53.25  E-value: 2.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2179 EPFPLTDVQEAYWvgRRSAFELGGVAAHGYFEIESPG-LEVERFIQCWRQLLQRHDMLRmVVLPDGRQQVLEQVPEYTPE 2257
Cdd:cd19546    3 DEVPATAGQLRTW--LLARLDEETRGRHLSVALRLRGrLDRDALEAALGDVAARHEILR-TTFPGDGGDVHQRILDADAA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2258 VVELRGLSPQEAESRRLqLRERMAHQ--VLRSDRW--PLFELVlcryEGGVRIHMSMDALMLDAWSSAVLRQDFAQLY-- 2331
Cdd:cd19546   80 RPELPVVPATEEELPAL-LADRAAHLfdLTRETPWrcTLFALS----DTEHVLLLVVHRIAADDESLDVLVRDLAAAYga 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2332 HEPGRPLE--PLAITFRDYVLAERRLREGEAHERAR-----AYWWARLDTLPPPPELPLVKEPSQLEHARFTHREARLEP 2404
Cdd:cd19546  155 RREGRAPEraPLPLQFADYALWERELLAGEDDRDSLigdqiAYWRDALAGAPDELELPTDRPRPVLPSRRAGAVPLRLDA 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2405 HRWARLQERARAHGLTPSAACMAAFAEVLARWSRHPRFTLNlTLFQRLPLHPQVDELVGDFTSLVLLEVEAHAASTFAER 2484
Cdd:cd19546  235 EVHARLMEAAESAGATMFTVVQAALAMLLTRLGAGTDVTVG-TVLPRDDEEGDLEGMVGPFARPLALRTDLSGDPTFREL 313


                 ....*
gi 53747904 2485 ASRLQ 2489
Cdd:cd19546  314 LGRVR 318
PRK13388 PRK13388
acyl-CoA synthetase; Provisional
 2981-3132 2.49e-06

acyl-CoA synthetase; Provisional


Pssm-ID: 237374 [Multi-domain]  Cd Length: 540  Bit Score: 53.49  E-value: 2.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2981 GELY-IGGEGLAREYWRDEPLTATRfIRHPRtgerlYRTGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQH 3059
Cdd:PRK13388  352 GELVnTAGAGFFEGYYNNPEATAER-MRHGM-----YWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRH 425

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 53747904  3060 PALSASVVVARGEPRGVRRLVAYAVPRSGQTPAAGELRRYLAER--LPAYMVPSAFVLLESLPRSRNGKIARDQL 3132
Cdd:PRK13388  426 PAINRVAVYAVPDERVGDQVMAALVLRDGATFDPDAFAAFLAAQpdLGTKAWPRYVRIAADLPSTATNKVLKREL 500
PLN02736 PLN02736
long-chain acyl-CoA synthetase
 2704-2802 2.71e-06

long-chain acyl-CoA synthetase


Pssm-ID: 178337 [Multi-domain]  Cd Length: 651  Bit Score: 53.18  E-value: 2.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2704 AVLGVLQAAAAYLPLDPEQPPLRLhqlleegpARVVLTQSSLLHTVPWPPGVQVIAVDELEP---ATEAPPLPPRgtPEH 2780
Cdd:PLN02736  153 AIFCVPQTLNTLLSCLSEIPSVRL--------IVVVGGADEPLPSLPSGTGVEIVTYSKLLAqgrSSPQPFRPPK--PED 222

                          90       100
                  ....*....|....*....|..
gi 53747904  2781 LAYVIYTSGSTGKPKGVAIEHR 2802
Cdd:PLN02736  223 VATICYTSGTTGTPKGVVLTHG 244
NADP_ADH cd08285
NADP(H)-dependent alcohol dehydrogenases; This group is predominated by atypical alcohol ...
 1673-1883 3.06e-06

NADP(H)-dependent alcohol dehydrogenases; This group is predominated by atypical alcohol dehydrogenases; they exist as tetramers and exhibit specificity for NADP(H) as a cofactor in the interconversion of alcohols and aldehydes, or ketones. Like other zinc-dependent alcohol dehydrogenases (ADH) of the medium chain alcohol dehydrogenase/reductase family (MDR), tetrameric ADHs have a catalytic zinc that resides between the catalytic and NAD(H)binding domains; however, they do not have and a structural zinc in a lobe of the catalytic domain. The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.


Pssm-ID: 176245 [Multi-domain]  Cd Length: 351  Bit Score: 52.24  E-value: 3.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1673 VEVAVGTPGLLESlglrrcTRPAPGPRQVEIEVEAAGLNFLDVLGALGMMPAlEAEESVLGRECSGRIAAVGEGVSGLRV 1752
Cdd:cd08285    5 AMLGIGKVGWIEK------PIPVCGPNDAIVRPTAVAPCTSDVHTVWGGAPG-ERHGMILGHEAVGVVEEVGSEVKDFKP 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1753 GDEVL--AVAP-----------------------------GCFRSYVLVDESQVVRRPASLGLAEGAAQMVP-FATAYFA 1800
Cdd:cd08285   78 GDRVIvpAITPdwrsvaaqrgypsqsggmlggwkfsnfkdGVFAEYFHVNDADANLAPLPDGLTDEQAVMLPdMMSTGFH 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1801 LHTVGRLRRGERILIhaaaggLGLAAVQLASRTGAE------ILATAGSEQKREYLRSLGIAHVLDSRSTSFVSEVRERT 1874
Cdd:cd08285  158 GAELANIKLGDTVAV------FGIGPVGLMAVAGARlrgagrIIAVGSRPNRVELAKEYGATDIVDYKNGDVVEQILKLT 231


                 ....*....
gi 53747904 1875 GGRGVDVVL 1883
Cdd:cd08285  232 GGKGVDAVI 240
PRK12583 PRK12583
acyl-CoA synthetase; Provisional
 2786-3134 3.06e-06

acyl-CoA synthetase; Provisional


Pssm-ID: 237145 [Multi-domain]  Cd Length: 558  Bit Score: 53.24  E-value: 3.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2786 YTSGSTGKPKGVAIEHRAALNTVVDLNTRFGVGPEDRVLGLSAL--TFDLsVYDVLGLLGAGGALVLPAAEAekDPAHWW 2863
Cdd:PRK12583  208 YTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPVPLyhCFGM-VLANLGCMTVGACLVYPNEAF--DPLATL 284

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2864 ERLVAGRVTVWNSTPALMLLLVEYAEQRGLKLpAALRLVMLSGDWIPVALPDRIRALGRDVQVVSLGGATEASiwsiayP 2943
Cdd:PRK12583  285 QAVEEERCTALYGVPTMFIAELDHPQRGNFDL-SSLRTGIMAGAPCPIEVMRRVMDEMHMAEVQIAYGMTETS------P 357

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2944 IGQVAPQWKSIP-----YGMPLANQRFHVLDGRLEARPWWVPGELYIGGEGLAREYWRDEPLTATRFirhprTGERLYRT 3018
Cdd:PRK12583  358 VSLQTTAADDLErrvetVGRTQPHLEVKVVDPDGATVPRGEIGELCTRGYSVMKGYWNNPEATAESI-----DEDGWMHT 432

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  3019 GDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPALSASVVVARGEPRGVRRLVAYAVPRSGQTPAAGELRR 3098
Cdd:PRK12583  433 GDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHPGHAASEEELRE 512

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 53747904  3099 YLAERLPAYMVPSAFVLLESLPRSRNGKIARDQLPE 3134
Cdd:PRK12583  513 FCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMRE 548
FDH_like_2 cd08284
Glutathione-dependent formaldehyde dehydrogenase related proteins, child 2; ...
 1692-1883 3.46e-06

Glutathione-dependent formaldehyde dehydrogenase related proteins, child 2; Glutathione-dependent formaldehyde dehydrogenases (FDHs) are members of the zinc-dependent/medium chain alcohol dehydrogenase family. Formaldehyde dehydrogenase (FDH) is a member of the zinc-dependent/medium chain alcohol dehydrogenase family. FDH converts formaldehyde and NAD to formate and NADH. The initial step in this process the spontaneous formation of a S-(hydroxymethyl)glutathione adduct from formaldehyde and glutathione, followed by FDH-mediated oxidation (and detoxification) of the adduct to S-formylglutathione. These tetrameric FDHs have a catalytic zinc that resides between the catalytic and NAD(H)binding domains and a structural zinc in a lobe of the catalytic domain. The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.


Pssm-ID: 176244 [Multi-domain]  Cd Length: 344  Bit Score: 52.26  E-value: 3.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1692 TRPAP---GPRQVEIEVEAAGLNFLDVLGALGMMPalEAEESVLGRECSGRIAAVGEGVSGLRVGDEVLAVA-------P 1761
Cdd:cd08284   16 EVPIPqiqDPTDAIVKVTAAAICGSDLHIYRGHIP--STPGFVLGHEFVGEVVEVGPEVRTLKVGDRVVSPFtiacgecF 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1762 GCFRSYV-LVDESQVVRRPASLGLAEGAAQM--VPFA------------------------TAYFALHTvGRLRRGERIL 1814
Cdd:cd08284   94 YCRRGQSgRCAKGGLFGYAGSPNLDGAQAEYvrVPFAdgtllklpdglsdeaalllgdilpTGYFGAKR-AQVRPGDTVA 172

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 53747904 1815 IHAAAGGLGLAAVQLASRTGAEILATAGSEQKREYLRSLGiAHVLDSRSTSFVSEVRERTGGRGVDVVL 1883
Cdd:cd08284  173 VIGCGPVGLCAVLSAQVLGAARVFAVDPVPERLERAAALG-AEPINFEDAEPVERVREATEGRGADVVL 240
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
 3149-3214 3.53e-06

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: 47.63  E-value: 3.53e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 53747904    3149 DPLVERLAALVKEALRL---ERVEPQDSLLDLGADSVALIRLINRLEAELQFRPRLADIYENPTVQGLA 3214
Cdd:smart00823   11 RLLLDLVREQVAAVLGHaaaEAIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALA 79
PRK08751 PRK08751
long-chain fatty acid--CoA ligase;
2957-3132 3.81e-06

long-chain fatty acid--CoA ligase;


Pssm-ID: 181546 [Multi-domain]  Cd Length: 560  Bit Score: 52.57  E-value: 3.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2957 GMPLANQRFHVLDGRLEARPWWVPGELYIGGEGLAREYWRDEPLTAtrfirHPRTGERLYRTGDQGRMLPEGSIEFLGRE 3036
Cdd:PRK08751  385 GLPIPSTDACIKDDAGTVLAIGEIGELCIKGPQVMKGYWKRPEETA-----KVMDADGWLHTGDIARMDEQGFVYIVDRK 459

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  3037 DLQVKVQGFRVELGEIEAALAQHPA-LSASVVVARGEPRGvrRLVAYAVPRSGQTPAAGELRRYLAERLPAYMVPSAFVL 3115
Cdd:PRK08751  460 KDMILVSGFNVYPNEIEDVIAMMPGvLEVAAVGVPDEKSG--EIVKVVIVKKDPALTAEDVKAHARANLTGYKQPRIIEF 537

                         170
                  ....*....|....*..
gi 53747904  3116 LESLPRSRNGKIARDQL 3132
Cdd:PRK08751  538 RKELPKTNVGKILRREL 554
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
 1270-1370 3.86e-06

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: 50.21  E-value: 3.86e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1270 VLHAAATFDDGVIQLRTHEQSSRALRTKVRGSMVLHE----VLASEGLDWFALCSSLASALGSFGQADYCAANAFQDAYA 1345
Cdd:cd02266   35 VVHNAAILDDGRLIDLTGSRIERAIRANVVGTRRLLEaareLMKAKRLGRFILISSVAGLFGAPGLGGYAASKAALDGLA 114

                         90       100
                 ....*....|....*....|....*...
gi 53747904 1346 HHLRRQGFTGAL---ALDWGTWRDTGAA 1370
Cdd:cd02266  115 QQWASEGWGNGLpatAVACGTWAGSGMA 142
CurA COG2130
NADPH-dependent curcumin reductase CurA [Secondary metabolites biosynthesis, transport and ...
 1741-1957 4.13e-06

NADPH-dependent curcumin reductase CurA [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];


Pssm-ID: 441733 [Multi-domain]  Cd Length: 333  Bit Score: 51.98  E-value: 4.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1741 AAVGEGV----SGLRVGDEVLAVAPgcFRSYVLVDESQVVR---RPASLGLAEGAAQMVPFaTAYFALHTVGRLRRGERI 1813
Cdd:COG2130   74 GAVGEVVesrhPDFAVGDLVLGMLG--WQDYAVSDGAGLRKvdpSLAPLSAYLGVLGMPGL-TAYFGLLDIGKPKAGETV 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1814 LihaaagglglaaV------------QLASRTGAEILATAGSEQKREYLRS-LGIAHVLDSRSTSFVSEVRERTGGrGVD 1880
Cdd:COG2130  151 V------------VsaaagavgsvvgQIAKLKGCRVVGIAGGAEKCRYLVEeLGFDAAIDYKAGDLAAALAAACPD-GID 217

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1881 V------------VLNslagelllaglsVLAPHGRFLELGKRDLY--ADQQVGLRTL-------ARGQTFAAIDFGPHHP 1939
Cdd:COG2130  218 VyfdnvggeildaVLP------------LLNTFARIAVCGAISQYnaTEPPPGPRNLgqllvkrLRMQGFIVFDHADRFP 285

                        250
                 ....*....|....*...
gi 53747904 1940 DFravLEEVATQLTQGQL 1957
Cdd:COG2130  286 EF---LAELAGWVAEGKL 300
FATP_chFAT1_like cd05937
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ...
 2980-3132 5.76e-06

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: 52.05  E-value: 5.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2980 PGE----LYIGGEGLAREYWRDEPLTATRFIRHP-RTGERLYRTGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEA 3054
Cdd:cd05937  299 PGEmlgrVPFKNREAFQGYLHNEDATESKLVRDVfRKGDIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVAD 378

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3055 ALAQHPALSASVVVARGEPR--GVRRLVAYAVPRSGQTPAA---GELRRYLAERLPAYMVPSAFVLLESLPRSRNGKIAR 3129
Cdd:cd05937  379 VLGAHPDIAEANVYGVKVPGhdGRAGCAAITLEESSAVPTEftkSLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQK 458


                 ...
gi 53747904 3130 DQL 3132
Cdd:cd05937  459 GVL 461
PaaK COG1541
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ...
 2787-3129 5.84e-06

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


Pssm-ID: 441150 [Multi-domain]  Cd Length: 423  Bit Score: 51.69  E-value: 5.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2787 TSGSTGKPKGVAIEhRAALNTVVDLNTRF----GVGPEDRVL-----GL--SALTFDLSvydvlgllgaggalvlpaaeA 2855
Cdd:COG1541   91 SSGTTGKPTVVGYT-RKDLDRWAELFARSlraaGVRPGDRVQnafgyGLftGGLGLHYG--------------------A 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2856 EK-----------DPAHWWERLVAGRVTVWNSTPALMLLLVEYAEQRGLKLPA-ALRLVMLSGDWIPVALPDRI-RALGr 2922
Cdd:COG1541  150 ERlgatvipagggNTERQLRLMQDFGPTVLVGTPSYLLYLAEVAEEEGIDPRDlSLKKGIFGGEPWSEEMRKEIeERWG- 228

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2923 dVQVVSLGGATEASIWsIAY--PIGQvapqwksipyGMPLANQRFHV--LD-GRLEARPwwvPGELyigGE----GLARE 2993
Cdd:COG1541  229 -IKAYDIYGLTEVGPG-VAYecEAQD----------GLHIWEDHFLVeiIDpETGEPVP---EGEE---GElvvtTLTKE 290

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2994 -YwrdePLtatrfIRhprtgerlYRTGDQGRMLPEGS--------IEF-LGREDLQVKVQGFRVELGEIEAALAQHPALS 3063
Cdd:COG1541  291 aM----PL-----IR--------YRTGDLTRLLPEPCpcgrthprIGRiLGRADDMLIIRGVNVFPSQIEEVLLRIPEVG 353

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3064 AS--VVVARGEPRGVRRLVAYAVPRSGQTPAAGELRRYLAERLpayMVPSAFVLLE--SLPRSrNGKIAR 3129
Cdd:COG1541  354 PEyqIVVDREGGLDELTVRVELAPGASLEALAEAIAAALKAVL---GLRAEVELVEpgSLPRS-EGKAKR 419
BACL_like cd05929
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ...
 2763-3129 7.17e-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: 51.61  E-value: 7.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2763 LEPATEAPPLPPrgtPEHLA---YVIYTSGSTGKPKGVAIEHRAALN---TVVDLNTRFGVGPEDRVLglsaltfdlsvy 2836
Cdd:cd05929  109 YEAAEGGSPETP---IEDEAagwKMLYSGGTTGRPKGIKRGLPGGPPdndTLMAAALGFGPGADSVYL------------ 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2837 dvlgllgaggalvLPAAEAEKDPAHW-------------WERLVAG---------RVTVWNSTPALMlllveyaeQRGLK 2894
Cdd:cd05929  174 -------------SPAPLYHAAPFRWsmtalfmggtlvlMEKFDPEeflrlieryRVTFAQFVPTMF--------VRLLK 232

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2895 LP---------AALRLVMLSGDWIPVALPDRIRALGRDVqVVSLGGATEASIWSIAYpigqvAPQWKSIP--YGMPLANq 2963
Cdd:cd05929  233 LPeavrnaydlSSLKRVIHAAAPCPPWVKEQWIDWGGPI-IWEYYGGTEGQGLTIIN-----GEEWLTHPgsVGRAVLG- 305

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2964 RFHVLDGRLEARPWWVPGELYIGGeGLAREYWRDEPLTAtrfirhPRTGERLYRT-GDQGRMLPEGSIEFLGREDLQVKV 3042
Cdd:cd05929  306 KVHILDEDGNEVPPGEIGEVYFAN-GPGFEYTNDPEKTA------AARNEGGWSTlGDVGYLDEDGYLYLTDRRSDMIIS 378

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3043 QGFRVELGEIEAALAQHPALSASVVVARGEPRGVRRLVAYAVPRSGQTPA---AGELRRYLAERLPAYMVPSAFVLLESL 3119
Cdd:cd05929  379 GGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQPAPGADAGtalAEELIAFLRDRLSRYKCPRSIEFVAEL 458

                        410
                 ....*....|
gi 53747904 3120 PRSRNGKIAR 3129
Cdd:cd05929  459 PRDDTGKLYR 468
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1232-1339 7.77e-06

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 50.34  E-value: 7.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  1232 ELEQLGAEVQVYTADVAEEAAVRSVVEQVHARWGKIHGVLHAAATFDDGV-IQLRTHEQSSRalrtkvrgsMVLHE---V 1307
Cdd:PRK08217   48 ECGALGTEVRGYAANVTDEEDVEATFAQIAEDFGQLNGLINNAGILRDGLlVKAKDGKVTSK---------MSLEQfqsV 118

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 53747904  1308 LASEGLDWFaLC--------------------SSLASAlGSFGQADYCAANA 1339
Cdd:PRK08217  119 IDVNLTGVF-LCgreaaakmiesgskgviiniSSIARA-GNMGQTNYSASKA 168
PRK12476 PRK12476
putative fatty-acid--CoA ligase; Provisional
 2685-2809 9.47e-06

putative fatty-acid--CoA ligase; Provisional


Pssm-ID: 171527 [Multi-domain]  Cd Length: 612  Bit Score: 51.67  E-value: 9.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2685 VQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPL-DPEQP--PLRLHQLLEEGPARVVLTQS-------SLLHTVPWPPG 2754
Cdd:PRK12476   89 AGPGDRVAILAPQGIDYVAGFFAAIKAGTIAVPLfAPELPghAERLDTALRDAEPTVVLTTTaaaeaveGFLRNLPRLRR 168

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 53747904  2755 VQVIAVDELEPATEAPPLPPRGTPEHLAYVIYTSGSTGKPKGVAIEHRAALNTVV 2809
Cdd:PRK12476  169 PRVIAIDAIPDSAGESFVPVELDTDDVSHLQYTSGSTRPPVGVEITHRAVGTNLV 223
PLN02387 PLN02387
long-chain-fatty-acid-CoA ligase family protein
 2756-3060 1.06e-05

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


Pssm-ID: 215217 [Multi-domain]  Cd Length: 696  Bit Score: 51.27  E-value: 1.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2756 QVIAVDELEPATEAPPLPPR-GTPEHLAYVIYTSGSTGKPKGVAIEHRAALNTVVDLNTRF-GVGPEDRVLGLSALTFDL 2833
Cdd:PLN02387  226 TVSSFSEVEKLGKENPVDPDlPSPNDIAVIMYTSGSTGLPKGVMMTHGNIVATVAGVMTVVpKLGKNDVYLAYLPLAHIL 305

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2834 SVYDVLGLLGAGGALVLPAAEAEKDPAHWWERLVAGRVTVWNST-----PALM-------LLLVEyaEQRGL-----KLP 2896
Cdd:PLN02387  306 ELAAESVMAAVGAAIGYGSPLTLTDTSNKIKKGTKGDASALKPTlmtavPAILdrvrdgvRKKVD--AKGGLakklfDIA 383

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2897 AALRLVMLSGDWIPVALPDR----------IRA-LGRDVQVVSLGGA-----TEASIwSIAY--PIGQvapqwksiPYGM 2958
Cdd:PLN02387  384 YKRRLAAIEGSWFGAWGLEKllwdalvfkkIRAvLGGRIRFMLSGGAplsgdTQRFI-NICLgaPIGQ--------GYGL 454

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2959 --PLANQRFHVLD----GRLEArPwwVP-----------------------GELYIGGEGLAREYWRDEPLTATRFIRHP 3009
Cdd:PLN02387  455 teTCAGATFSEWDdtsvGRVGP-P--LPccyvklvsweeggylisdkpmprGEIVIGGPSVTLGYFKNQEKTDEVYKVDE 531

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 53747904  3010 RtGERLYRTGDQGRMLPEGSIEFLGREDLQVKVQ-GFRVELGEIEAALAQHP 3060
Cdd:PLN02387  532 R-GMRWFYTGDIGQFHPDGCLEIIDRKKDIVKLQhGEYVSLGKVEAALSVSP 582
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 1234-1275 1.41e-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: 49.35  E-value: 1.41e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 53747904   1234 EQLGAEVqvYTADVAEEAAVRSVVEQVHARWGKIHGVLHAAA 1275
Cdd:pfam13561   41 EELGAAV--LPCDVTDEEQVEALVAAAVEKFGRLDILVNNAG 80
CAD2 cd08298
Cinnamyl alcohol dehydrogenases (CAD); These alcohol dehydrogenases are related to the ...
 1679-1861 1.51e-05

Cinnamyl alcohol dehydrogenases (CAD); These alcohol dehydrogenases are related to the cinnamyl alcohol dehydrogenases (CAD), members of the medium chain dehydrogenase/reductase family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Cinnamyl alcohol dehydrogenases (CAD) reduce cinnamaldehydes to cinnamyl alcohols in the last step of monolignal metabolism in plant cells walls. CAD binds 2 zinc ions and is NADPH- dependent. CAD family members are also found in non-plant species, e.g. in yeast where they have an aldehyde reductase activity. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176258 [Multi-domain]  Cd Length: 329  Bit Score: 50.26  E-value: 1.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1679 TPGLLES--LGLRRCTRPAPGPRQVEIEVEAAGLNFLDVLGALGMMPALeAEESVLGRECSGRIAAVGEGVSGLRVGDEV 1756
Cdd:cd08298    8 KPGPIEEnpLRLTEVPVPEPGPGEVLIKVEACGVCRTDLHIVEGDLPPP-KLPLIPGHEIVGRVEAVGPGVTRFSVGDRV 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1757 lAVAP------------------------------GCFRSYVLVDESQVVRRPASLGLAEGAAQMVPFATAYFALHTVGr 1806
Cdd:cd08298   87 -GVPWlgstcgecrycrsgrenlcdnarftgytvdGGYAEYMVADERFAYPIPEDYDDEEAAPLLCAGIIGYRALKLAG- 164

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 53747904 1807 LRRGERILI-------HAAagglglaaVQLASRTGAEILATAGSEQKREYLRSLGIAHVLDS 1861
Cdd:cd08298  165 LKPGQRLGLygfgasaHLA--------LQIARYQGAEVFAFTRSGEHQELARELGADWAGDS 218
C_PKS-NRPS cd20483
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
 2218-2469 1.85e-05

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: 50.34  E-value: 1.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2218 VERFIQCWRQLLQRHDMLRMVVL---PDGRQQVLEQvPEYTPEVVELRGLSPQEAESRRL--QLRE-----------RMA 2281
Cdd:cd20483   38 VNLLQKALSELVRRHEVLRTAYFegdDFGEQQVLDD-PSFHLIVIDLSEAADPEAALDQLvrNLRRqeldieegeviRGW 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2282 HQVLRSDRWPLFelvlcryeggVRIHMsmdaLMLDAWSSAVLRQDFAQLY-----HEPGRPLEPLAITFRDYVLAERRLR 2356
Cdd:cd20483  117 LVKLPDEEFALV----------LASHH----IAWDRGSSKSIFEQFTALYdalraGRDLATVPPPPVQYIDFTLWHNALL 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2357 EGEAHERARAYWWARLDTLPPPPEL---PLVKEPSQLEHARFTHrEARLEPHRWARLQERARAHGLTPSAACMAAFAEVL 2433
Cdd:cd20483  183 QSPLVQPLLDFWKEKLEGIPDASKLlpfAKAERPPVKDYERSTV-EATLDKELLARMKRICAQHAVTPFMFLLAAFRAFL 261

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 53747904 2434 ARWSRHPRFTLNLTLFQRlPlHPQVDELVGDFTSLV 2469
Cdd:cd20483  262 YRYTEDEDLTIGMVDGDR-P-HPDFDDLVGFFVNML 295
Firefly_Luc cd17642
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ...
 2981-3134 2.78e-05

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: 49.83  E-value: 2.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2981 GELYIGGEGLAREYWRDEPLTATRFIRhprtgERLYRTGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHP 3060
Cdd:cd17642  382 GELCVKGPMIMKGYVNNPEATKALIDK-----DGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHP 456

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 53747904 3061 ALSASVVVARGEPRGVRRLVAYAVPRSGQTPAAGELRRYLAERL-PAYMVPSAFVLLESLPRSRNGKIARDQLPE 3134
Cdd:cd17642  457 KIFDAGVAGIPDEDAGELPAAVVVLEAGKTMTEKEVMDYVASQVsTAKRLRGGVKFVDEVPKGLTGKIDRRKIRE 531
LC_FACS_bac1 cd17641
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ...
 2775-3074 3.29e-05

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: 49.73  E-value: 3.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2775 RGTPEHLAYVIYTSGSTGKPKGVAIEHRAALNTVVDLNTRFGVGPEDRVLGLSALTFDLS-VYDVLGLLGAGGALVLP-- 2851
Cdd:cd17641  154 AGKGEDVAVLCTTSGTTGKPKLAMLSHGNFLGHCAAYLAADPLGPGDEYVSVLPLPWIGEqMYSVGQALVCGFIVNFPee 233

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2852 AAEAEKD-----------PAHWWERLVAG-RVTVWNSTP-------ALMLLLVEYAEQ--RGLKLPAALRLVMLSGDWIP 2910
Cdd:cd17641  234 PETMMEDlreigptfvllPPRVWEGIAADvRARMMDATPfkrfmfeLGMKLGLRALDRgkRGRPVSLWLRLASWLADALL 313

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2911 V-ALPDRI------------RALGRD---------VQVVSLGGATEASIWSIAYPIGQVAPQwksiPYGMPLANQRFHVL 2968
Cdd:cd17641  314 FrPLRDRLgfsrlrsaatggAALGPDtfrffhaigVPLKQLYGQTELAGAYTVHRDGDVDPD----TVGVPFPGTEVRID 389

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2969 DgrlearpwwvPGELYIGGEGLAREYWRDEPLTATRFirhprTGERLYRTGDQGRMLPEGSIEFLGR-EDLQVKVQGFRV 3047
Cdd:cd17641  390 E----------VGEILVRSPGVFVGYYKNPEATAEDF-----DEDGWLHTGDAGYFKENGHLVVIDRaKDVGTTSDGTRF 454

                        330       340
                 ....*....|....*....|....*..
gi 53747904 3048 ELGEIEAALAQHPALSASVVVARGEPR 3074
Cdd:cd17641  455 SPQFIENKLKFSPYIAEAVVLGAGRPY 481
A_NRPS_MycA_like cd05908
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ...
 2778-2833 3.70e-05

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: 49.41  E-value: 3.70e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 53747904 2778 PEHLAYVIYTSGSTGKPKGVAIEHRAALNTVVDLNTRFGVGPEDRVLGLSALTFDL 2833
Cdd:cd05908  105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDM 160
AcpA COG3433
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ...
 2020-2145 5.20e-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: 5.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2020 AGGISSEEGAEAFLRALEQGAPQLIISPQDFSSLLRGLGGSQGVREKERLVTGR----AAAAEPQALPPSSLEQLIEQVW 2095
Cdd:COG3433  149 AVAALDGLAAAAALAALDKVPPDVVAASAVVALDALLLLALKVVARAAPALAAAeallAAASPAPALETALTEEELRADV 228

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 53747904 2096 RKHLGV--ERVQPTDSFFQLGGDSLLGIQVAADLRRHlGVELPTATLFSHPT 2145
Cdd:COG3433  229 AELLGVdpEEIDPDDNLFDLGLDSIRLMQLVERWRKA-GLDVSFADLAEHPT 279
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
 1232-1392 5.58e-05

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: 47.38  E-value: 5.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1232 ELEQLGAEVQVYTADVAEEAAVRSVVEQVHARWGKIHGVLHAAATFDDGVIQLRTHEQSSRALRTK----VRGSMVLHEV 1307
Cdd:cd05360   43 EVRELGGEAIAVVADVADAAQVERAADTAVERFGRIDTWVNNAGVAVFGRFEDVTPEEFRRVFDVNylghVYGTLAALPH 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1308 LASEGLDWFALCSSLASALGSFGQADYCAAN----AFQDAYAHHLRRQGFTGALALDWGTWRDTGAAMRlvARTRRGGHE 1383
Cdd:cd05360  123 LRRRGGGALINVGSLLGYRSAPLQAAYSASKhavrGFTESLRAELAHDGAPISVTLVQPTAMNTPFFGH--ARSYMGKKP 200


                 ....*....
gi 53747904 1384 KPPTPLTHP 1392
Cdd:cd05360  201 KPPPPIYQP 209
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
2083-2145 5.79e-05

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 49.27  E-value: 5.79e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 53747904  2083 PPSSLEQLIEQVWRKHLGVERVQPTDSFFQLGGDSLLGIQVAADLRRHLGVELPTATLFSHPT 2145
Cdd:PRK10252  975 PKTGTETIIAAAFSSLLGCDVVDADADFFALGGHSLLAMKLAAQLSRQFARQVTPGQVMVAST 1037
PRK07445 PRK07445
O-succinylbenzoic acid--CoA ligase; Reviewed
 2981-3134 6.03e-05

O-succinylbenzoic acid--CoA ligase; Reviewed


Pssm-ID: 236019 [Multi-domain]  Cd Length: 452  Bit Score: 48.84  E-value: 6.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2981 GELYIGGEGLAREYWrdePltatrfirHPRTGERLYRTGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHP 3060
Cdd:PRK07445  302 GNITIQAQSLALGYY---P--------QILDSQGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATG 370

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 53747904  3061 ALSASVVVARGEPRGVRRLVAYAVPRSGQtPAAGELRRYLAERLPAYMVPSAFVLLESLPRSRNGKIARDQLPE 3134
Cdd:PRK07445  371 LVQDVCVLGLPDPHWGEVVTAIYVPKDPS-ISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQ 443
B4_12hDH TIGR02825
leukotriene B4 12-hydroxydehydrogenase/15-oxo-prostaglandin 13-reductase; Leukotriene B4 ...
 1748-1880 6.50e-05

leukotriene B4 12-hydroxydehydrogenase/15-oxo-prostaglandin 13-reductase; Leukotriene B4 12-hydroxydehydrogenase is an NADP-dependent enzyme of arachidonic acid metabolism, responsible for converting leukotriene B4 to the much less active metabolite 12-oxo-leukotriene B4. The BRENDA database lists leukotriene B4 12-hydroxydehydrogenase as one of the synonyms of 2-alkenal reductase (EC 1.3.1.74), while 1.3.1.48 is 15-oxoprostaglandin 13-reductase.


Pssm-ID: 131872 [Multi-domain]  Cd Length: 325  Bit Score: 48.07  E-value: 6.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   1748 SGLRVGDEVLAvAPGcFRSYVLVDESQVVRRPAS------LGLAEGAAQMvPFATAYFALHTVGRLRRGERILIHAAAGG 1821
Cdd:TIGR02825   74 VALPKGTIVLA-SPG-WTSHSISDGKDLEKLLTEwpdtlpLSLALGTVGM-PGLTAYFGLLEICGVKGGETVMVNAAAGA 150

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 53747904   1822 LGLAAVQLASRTGAEILATAGSEQKREYLRSLGIAHVLDSRSTSFVSEVRERTGGRGVD 1880
Cdd:TIGR02825  151 VGSVVGQIAKLKGCKVVGAAGSDEKVAYLKKLGFDVAFNYKTVKSLEETLKKASPDGYD 209
PRK07514 PRK07514
malonyl-CoA synthase; Validated
 2994-3131 7.69e-05

malonyl-CoA synthase; Validated


Pssm-ID: 181011 [Multi-domain]  Cd Length: 504  Bit Score: 48.33  E-value: 7.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2994 YWRDEPLTATRFirhprTGERLYRTGDQGRMLPEGSIEFLGRE-DLqVKVQGFRVELGEIEAALAQHPALSASVVVAR-- 3070
Cdd:PRK07514  362 YWRMPEKTAEEF-----RADGFFITGDLGKIDERGYVHIVGRGkDL-IISGGYNVYPKEVEGEIDELPGVVESAVIGVph 435

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 53747904  3071 ---GEprGVrrlVAYAVPRSGQTPAAGELRRYLAERLPAYMVPSAFVLLESLPRSRNGK----IARDQ 3131
Cdd:PRK07514  436 pdfGE--GV---TAVVVPKPGAALDEAAILAALKGRLARFKQPKRVFFVDELPRNTMGKvqknLLREQ 498
benzyl_alcohol_DH cd08278
Benzyl alcohol dehydrogenase; Benzyl alcohol dehydrogenase is similar to liver alcohol ...
 1676-1883 9.86e-05

Benzyl alcohol dehydrogenase; Benzyl alcohol dehydrogenase is similar to liver alcohol dehydrogenase, but has some amino acid substitutions near the active site, which may determine the enzyme's specificity of oxidizing aromatic substrates. Also known as aryl-alcohol dehydrogenases, they catalyze the conversion of an aromatic alcohol + NAD+ to an aromatic aldehyde + NADH + H+. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176239 [Multi-domain]  Cd Length: 365  Bit Score: 47.88  E-value: 9.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1676 AVGTPGLLESLGLRrctrpAPGPRQVEIEVEAAGLNFLDVLGALGMMPA-LEAeesVLGRECSGRIAAVGEGVSGLRVGD 1754
Cdd:cd08278   10 EPGGPFVLEDVELD-----DPRPDEVLVRIVATGICHTDLVVRDGGLPTpLPA---VLGHEGAGVVEAVGSAVTGLKPGD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1755 EVLAVAPGC--------------------------------------------------FRSYVLVDESQVVRRPASL-- 1782
Cdd:cd08278   82 HVVLSFASCgecanclsghpaycenffplnfsgrrpdgstplslddgtpvhghffgqssFATYAVVHERNVVKVDKDVpl 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1783 --------GLAEGAAqmvpfatayfALHTVGRLRRGERILIhaaaggLGLAAVQLASRTGA------EILATAGSEQKRE 1848
Cdd:cd08278  162 ellaplgcGIQTGAG----------AVLNVLKPRPGSSIAV------FGAGAVGLAAVMAAkiagctTIIAVDIVDSRLE 225

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 53747904 1849 YLRSLGIAHVLDSRSTSFVSEVRERTGGrGVDVVL 1883
Cdd:cd08278  226 LAKELGATHVINPKEEDLVAAIREITGG-GVDYAL 259
PRK05691 PRK05691
peptide synthase; Validated
 2083-2141 1.01e-04

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 48.63  E-value: 1.01e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 53747904  2083 PPSSLEQLIEQVWRKHLGVERVQPTDSFFQLGGDSLLGIQVAADLRRHLGVELPTATLF 2141
Cdd:PRK05691 4238 PRNELEQTLATIWADVLKVERVGVHDNFFELGGHSLLATQIASRVQKALQRNVPLRAMF 4296
PRK09192 PRK09192
fatty acyl-AMP ligase;
2753-2822 1.20e-04

fatty acyl-AMP ligase;


Pssm-ID: 236403 [Multi-domain]  Cd Length: 579  Bit Score: 48.08  E-value: 1.20e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 53747904  2753 PGVQVIAVDELEpATEAPPLP-PRGTPEHLAYVIYTSGSTGKPKGVAIEHRAALNTVVDLnTRFG--VGPEDR 2822
Cdd:PRK09192  150 PLLHVLSHAWFK-ALPEADVAlPRPTPDDIAYLQYSSGSTRFPRGVIITHRALMANLRAI-SHDGlkVRPGDR 220
PLN02654 PLN02654
acetate-CoA ligase
 3016-3129 1.28e-04

acetate-CoA ligase


Pssm-ID: 215353 [Multi-domain]  Cd Length: 666  Bit Score: 47.97  E-value: 1.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  3016 YRTGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHP-ALSASVVVARGEPRGvRRLVAYAVPRSGqTPAAG 3094
Cdd:PLN02654  515 YFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPqCAEAAVVGIEHEVKG-QGIYAFVTLVEG-VPYSE 592

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 53747904  3095 ELRRYLA----ERLPAYMVPSAFVLLESLPRSRNGKIAR 3129
Cdd:PLN02654  593 ELRKSLIltvrNQIGAFAAPDKIHWAPGLPKTRSGKIMR 631
PRK12582 PRK12582
acyl-CoA synthetase; Provisional
 2648-2802 1.42e-04

acyl-CoA synthetase; Provisional


Pssm-ID: 237144 [Multi-domain]  Cd Length: 624  Bit Score: 47.73  E-value: 1.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2648 ARLHPELPALL------APERTLSYGELARRAQALAARLRELEVQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLDP- 2720
Cdd:PRK12582   59 AAEAPDRPWLAqrepghGQWRKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVSPa 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2721 ----EQPPLRLHQLLEEGPARVVLTQS----------------SLLHTVPWPPGVQVIAVDEL---EPATEAPPLPPRGT 2777
Cdd:PRK12582  139 yslmSHDHAKLKHLFDLVKPRVVFAQSgapfaralaaldlldvTVVHVTGPGEGIASIAFADLaatPPTAAVAAAIAAIT 218

                         170       180
                  ....*....|....*....|....*
gi 53747904  2778 PEHLAYVIYTSGSTGKPKGVAIEHR 2802
Cdd:PRK12582  219 PDTVAKYLFTSGSTGMPKAVINTQR 243
ttLC_FACS_like cd05915
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
 2786-3132 1.99e-04

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: 47.04  E-value: 1.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2786 YTSGSTGKPKGVAIEHRAA-LN-TVVDLNTRFGVGPEDRVLgLSALTFDLSVYDVLGLLGAGGALVLPAAEAEKDPAhWW 2863
Cdd:cd05915  160 YTTGTTGLPKGVVYSHRALvLHsLAASLVDGTALSEKDVVL-PVVPMFHVNAWCLPYAATLVGAKQVLPGPRLDPAS-LV 237

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2864 ERLVAGRVTVWNSTPALMLLLVEYAEQRGLKLPAALRLvmLSGDWIPVALPDRIRALGRDVQVVSLG-----GATEASIW 2938
Cdd:cd05915  238 ELFDGEGVTFTAGVPTVWLALADYLESTGHRLKTLRRL--VVGGSAAPRSLIARFERMGVEVRQGYGltetsPVVVQNFV 315

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2939 siaypigqvAPQWKSIPYGMPLanqRFHVLDGR---------LEARPWWVPGE------LYIGGEGLAREYWRDEPLTAT 3003
Cdd:cd05915  316 ---------KSHLESLSEEEKL---TLKAKTGLpiplvrlrvADEEGRPVPKDgkalgeVQLKGPWITGGYYGNEEATRS 383

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 3004 RFIRHPrtgerLYRTGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPALSASVVVARGEPRGVRRLVAYA 3083
Cdd:cd05915  384 ALTPDG-----FFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVV 458

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 53747904 3084 VPRSGQTPAAgELRRYLAERLPAY-MVPSAFVLLESLPRSRNGKIARDQL 3132
Cdd:cd05915  459 VPRGEKPTPE-ELNEHLLKAGFAKwQLPDAYVFAEEIPRTSAGKFLKRAL 507
PRK08279 PRK08279
long-chain-acyl-CoA synthetase; Validated
 2613-2806 2.14e-04

long-chain-acyl-CoA synthetase; Validated


Pssm-ID: 236217 [Multi-domain]  Cd Length: 600  Bit Score: 47.18  E-value: 2.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2613 LPELLPPAQRELLARYNATQAPRPSGR-----LEEgfftQARLHPELPALLAPERTLSYGELARRAQALAARLRELEVQP 2687
Cdd:PRK08279   11 LPRRLPDLPGILRGLKRTALITPDSKRslgdvFEE----AAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGK 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2688 QELVAIAMHKGWEQATAVLGV--LQAAAAYL-------PL--------------DPEqpplrLHQLLEEGPARVVLTQSS 2744
Cdd:PRK08279   87 GDVVALLMENRPEYLAAWLGLakLGAVVALLntqqrgaVLahslnlvdakhlivGEE-----LVEAFEEARADLARPPRL 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 53747904  2745 LLH---TVPWPPGVQVIAVDELEPATEAPPLPPRGTPEHLAYVIYTSGSTGKPKGVAIEHRAALN 2806
Cdd:PRK08279  162 WVAggdTLDDPEGYEDLAAAAAGAPTTNPASRSGVTAKDTAFYIYTSGTTGLPKAAVMSHMRWLK 226
PRK05857 PRK05857
fatty acid--CoA ligase;
2642-3132 2.23e-04

fatty acid--CoA ligase;


Pssm-ID: 180293 [Multi-domain]  Cd Length: 540  Bit Score: 46.93  E-value: 2.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2642 EGFFTQARLHPELPALLAPERT--LSYGELARRAQALAARLRELEVQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLD 2719
Cdd:PRK05857   18 DRVFEQARQQPEAIALRRCDGTsaLRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMAD 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2720 PEQPPLRLHQLLE-EGPARVVLTQSSLLHTVPWPPG---VQVIAVDELEPATEAPPLPPR---------GTPEHLAyVIY 2786
Cdd:PRK05857   98 GNLPIAAIERFCQiTDPAAALVAPGSKMASSAVPEAlhsIPVIAVDIAAVTRESEHSLDAaslagnadqGSEDPLA-MIF 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2787 TSGSTGKPKGVAIEHRaalntvvdlnTRFGVGPEDRVLGLSALTFdlsvydvlgllgaggalvlPAAEAEKDP---AH-- 2861
Cdd:PRK05857  177 TSGTTGEPKAVLLANR----------TFFAVPDILQKEGLNWVTW-------------------VVGETTYSPlpaTHig 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2862 --WW----------------------ERLVAGRVTVWNSTPALMLLLVEYAEQRGLKLPaALRLVMLSGDwipvalpdri 2917
Cdd:PRK05857  228 glWWiltclmhgglcvtggenttsllEILTTNAVATTCLVPTLLSKLVSELKSANATVP-SLRLVGYGGS---------- 296

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2918 RALGRDVQVVSLGGATEASIWSIAyPIGQVApqwksipYGMPLANQRFHVLDGRLEARPWwvPG-ELYIGGEGLAREYWR 2996
Cdd:PRK05857  297 RAIAADVRFIEATGVRTAQVYGLS-ETGCTA-------LCLPTDDGSIVKIEAGAVGRPY--PGvDVYLAATDGIGPTAP 366

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2997 DEPLTA---TRFIRHP-----------RTGERL----YRTGDQGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQ 3058
Cdd:PRK05857  367 GAGPSAsfgTLWIKSPanmlgywnnpeRTAEVLidgwVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEG 446

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  3059 HPALSASVVVARGEPRgVRRLVAYAVPRSGQTPAAG--ELRRYLAERL----PAYMVPSAFVLLESLPRSRNGKIARDQL 3132
Cdd:PRK05857  447 VSGVREAACYEIPDEE-FGALVGLAVVASAELDESAarALKHTIAARFrresEPMARPSTIVIVTDIPRTQSGKVMRASL 525
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1232-1339 2.62e-04

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 45.63  E-value: 2.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  1232 ELEQLGAEVQVYTADVAEEAAVRSVVEQVHARWGKIHGVLHAAATFDDGVIQLRTHEQSSRALRTKVRGSM-VLHEVL-- 1308
Cdd:PRK12825   50 AVEALGRRAQAVQADVTDKAALEAAVAAAVERFGRIDILVNNAGIFEDKPLADMSDDEWDEVIDVNLSGVFhLLRAVVpp 129

                          90       100       110
                  ....*....|....*....|....*....|..
gi 53747904  1309 -ASEGLDWFALCSSLASALGSFGQADYCAANA 1339
Cdd:PRK12825  130 mRKQRGGRIVNISSVAGLPGWPGRSNYAAAKA 161
SCP-x_thiolase cd00829
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ...
 99-210 5.41e-04

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: 45.33  E-value: 5.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904   99 LLLECSWEALEDAGLRPDQLPgwvGVYVGAGDTsyrfqllrghgdplsgskdvagffGNYPDFLATRVAYKLNLRG-PAL 177
Cdd:cd00829   19 LAAEAARAALDDAGLEPADID---AVVVGNAAG------------------------GRFQSFPGALIAEYLGLLGkPAT 71

                         90       100       110
                 ....*....|....*....|....*....|...
gi 53747904  178 GIHTACSTSLVSINMACSALRGFECDMALAGGV 210
Cdd:cd00829   72 RVEAAGASGSAAVRAAAAAIASGLADVVLVVGA 104
LCL_NRPS-like cd19540
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ...
 2316-2483 5.67e-04

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: 45.49  E-value: 5.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2316 DAWSSAVLRQDFAQLY------HEPGRPlePLAITFRDYVLAERRLREGEAHERAR-----AYWWARLDTLppppelplv 2384
Cdd:cd19540  134 DGWSMAPLARDLATAYaarragRAPDWA--PLPVQYADYALWQRELLGDEDDPDSLaarqlAYWRETLAGL--------- 202

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2385 kePSQLE-------HARFTHR----EARLEPHRWARLQERARAHGLTPSAACMAAFAEVLARWSRHprftlnltlfQRLP 2453
Cdd:cd19540  203 --PEELElptdrprPAVASYRggtvEFTIDAELHARLAALAREHGATLFMVLHAALAVLLSRLGAG----------DDIP 270

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 53747904 2454 L--------HPQVDELVGDFTSLVLLEVEAHAASTFAE 2483
Cdd:cd19540  271 IgtpvagrgDEALDDLVGMFVNTLVLRTDVSGDPTFAE 308
FabI COG0623
Enoyl-[acyl-carrier-protein] reductase FabI [Lipid transport and metabolism]; Enoyl- ...
 1234-1275 6.56e-04

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: 44.24  E-value: 6.56e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 53747904 1234 EQLGAEVqVYTADVAEEAAVRSVVEQVHARWGKIHGVLHAAA 1275
Cdd:COG0623   52 EELGSAL-VLPCDVTDDEQIDALFDEIKEKWGKLDFLVHSIA 92
liver_alcohol_DH_like cd08277
Liver alcohol dehydrogenase; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
 1696-1763 7.33e-04

Liver alcohol dehydrogenase; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. There are 7 vertebrate ADH 7 classes, 6 of which have been identified in humans. Class III, glutathione-dependent formaldehyde dehydrogenase, has been identified as the primordial form and exists in diverse species, including plants, micro-organisms, vertebrates, and invertebrates. Class I, typified by liver dehydrogenase, is an evolving form. Gene duplication and functional specialization of ADH into ADH classes and subclasses created numerous forms in vertebrates. For example, the A, B and C (formerly alpha, beta, gamma) human class I subunits have high overall structural similarity, but differ in the substrate binding pocket and therefore in substrate specificity. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine (His-51), the ribose of NAD, a serine (Ser-48) , then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of an beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding.


Pssm-ID: 176238 [Multi-domain]  Cd Length: 365  Bit Score: 45.02  E-value: 7.33e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 53747904 1696 PGPRQVEIEVEAAGLNFLDVLGALGMMPALEAEesVLGRECSGRIAAVGEGVSGLRVGDEVLAV-APGC 1763
Cdd:cd08277   25 PKANEVRIKMLATSVCHTDILAIEGFKATLFPV--ILGHEGAGIVESVGEGVTNLKPGDKVIPLfIGQC 91
PRK06814 PRK06814
acyl-[ACP]--phospholipid O-acyltransferase;
2774-2823 9.06e-04

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


Pssm-ID: 235865 [Multi-domain]  Cd Length: 1140  Bit Score: 45.34  E-value: 9.06e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 53747904  2774 PRGTPEHLAYVIYTSGSTGKPKGVAIEHRAALNTVVDLNTRFGVGPEDRV 2823
Cdd:PRK06814  788 CNRDPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPEDKV 837
PRK12826 PRK12826
SDR family oxidoreductase;
1233-1354 1.06e-03

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 43.75  E-value: 1.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  1233 LEQLGAEVQVYTADVAEEAAVRSVVEQVHARWGKIHGVLHAAATFDDGVIQLRTHEQSSRALRTKVRGSMVLHEVLaseg 1312
Cdd:PRK12826   50 VEAAGGKARARQVDVRDRAALKAAVAAGVEDFGRLDILVANAGIFPLTPFAEMDDEQWERVIDVNLTGTFLLTQAA---- 125

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 53747904  1313 LDWF--------ALCSSLA-SALGSFGQADYCAA----NAFQDAYAHHLRRQGFT 1354
Cdd:PRK12826  126 LPALiragggriVLTSSVAgPRVGYPGLAHYAASkaglVGFTRALALELAARNIT 180
PRK05620 PRK05620
long-chain fatty-acid--CoA ligase;
2745-3132 1.15e-03

long-chain fatty-acid--CoA ligase;


Pssm-ID: 180167 [Multi-domain]  Cd Length: 576  Bit Score: 44.77  E-value: 1.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2745 LLHTVPWPPGVQVIAVDEL-EPATEAPP----------LPPRGT-------PEHLAYVI-YTSGSTGKPKGVAIEHRAAL 2805
Cdd:PRK05620  128 ILKECPCVRAVVFIGPSDAdSAAAHMPEgikvysyealLDGRSTvydwpelDETTAAAIcYSTGTTGAPKGVVYSHRSLY 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2806 NTVVDLNT--RFGVGPEDRVLGLSALTFDLSVYDVLGLLGAGGALVLPAAEAekDPAHWWERLVAGRVTVWNSTPAL-ML 2882
Cdd:PRK05620  208 LQSLSLRTtdSLAVTHGESFLCCVPIYHVLSWGVPLAAFMSGTPLVFPGPDL--SAPTLAKIIATAMPRVAHGVPTLwIQ 285

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2883 LLVEYAEQRGLKLpaALRLVMLSGDWIPVALPDRIRA-LGrdVQVVSLGGATEAS-IWSIAYPIGQVAPQ--WK-SIPYG 2957
Cdd:PRK05620  286 LMVHYLKNPPERM--SLQEIYVGGSAVPPILIKAWEErYG--VDVVHVWGMTETSpVGTVARPPSGVSGEarWAyRVSQG 361

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2958 MPLANQRFHVLD------------GRLEARPWWVPGELY---IGGEGLAREYWRDEPL--TATRFirhprTGERLYRTGD 3020
Cdd:PRK05620  362 RFPASLEYRIVNdgqvmestdrneGEIQVRGNWVTASYYhspTEEGGGAASTFRGEDVedANDRF-----TADGWLRTGD 436

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  3021 QGRMLPEGSIEFLGREDLQVKVQGFRVELGEIEAALAQHPALSASVVVARGEPRGVRR-----LVAYAVPRSGQTpaAGE 3095
Cdd:PRK05620  437 VGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERplavtVLAPGIEPTRET--AER 514

                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 53747904  3096 LRRYLAERLPAYMVPSAFVLLESLPRSRNGKIARDQL 3132
Cdd:PRK05620  515 LRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDL 551
PTZ00342 PTZ00342
acyl-CoA synthetase; Provisional
 2778-2811 1.29e-03

acyl-CoA synthetase; Provisional


Pssm-ID: 240370 [Multi-domain]  Cd Length: 746  Bit Score: 44.71  E-value: 1.29e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 53747904  2778 PEHLAYVIYTSGSTGKPKGVAIEHRAALNTVVDL 2811
Cdd:PTZ00342  303 PDFITSIVYTSGTSGKPKGVMLSNKNLYNTVVPL 336
AFD_CAR-like cd17632
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ...
 2623-2802 1.73e-03

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: 43.98  E-value: 1.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2623 ELLARYNATQAPRPS-GRLEEGFFTQARLHPELPALLAPERTLSYGEL-ARRAQALAARLRELEVQPQELVAIAMHKGWE 2700
Cdd:cd17632   26 QIIATVMTGYADRPAlGQRATELVTDPATGRTTLRLLPRFETITYAELwERVGAVAAAHDPEQPVRPGDFVAVLGFTSPD 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2701 QATAVLGVLQAAAAYLPLDPEQPPLRLHQLLEE------------------------GPARVVL---------TQSSL-- 2745
Cdd:cd17632  106 YATVDLALTRLGAVSVPLQAGASAAQLAPILAEteprllavsaehldlaveavleggTPPRLVVfdhrpevdaHRAALes 185

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 53747904 2746 ----LHTVPWPPGVQVIAVDELEPATEAPPLPPRGTPEHLAYVIYTSGSTGKPKGVAIEHR 2802
Cdd:cd17632  186 arerLAAVGIPVTTLTLIAVRGRDLPPAPLFRPEPDDDPLALLIYTSGSTGTPKGAMYTER 246
PRK07768 PRK07768
long-chain-fatty-acid--CoA ligase; Validated
 2754-2802 1.97e-03

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


Pssm-ID: 236091 [Multi-domain]  Cd Length: 545  Bit Score: 43.83  E-value: 1.97e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 53747904  2754 GVQVIAVDELEPATEAPPLPPrgTPEHLAYVIYTSGSTGKPKGVAIEHR 2802
Cdd:PRK07768  129 GIRVLTVADLLAADPIDPVET--GEDDLALMQLTSGSTGSPKAVQITHG 175
FDH_like_ADH2 cd08286
formaldehyde dehydrogenase (FDH)-like; This group is related to formaldehyde dehydrogenase ...
 1731-1883 2.01e-03

formaldehyde dehydrogenase (FDH)-like; This group is related to formaldehyde dehydrogenase (FDH), which is a member of the zinc-dependent/medium chain alcohol dehydrogenase family. This family uses NAD(H) as a cofactor in the interconversion of alcohols and aldehydes, or ketones. Another member is identified as a dihydroxyacetone reductase. Like the zinc-dependent alcohol dehydrogenases (ADH) of the medium chain alcohol dehydrogenase/reductase family (MDR), tetrameric FDHs have a catalytic zinc that resides between the catalytic and NAD(H)binding domains and a structural zinc in a lobe of the catalytic domain. Unlike ADH, where NAD(P)(H) acts as a cofactor, NADH in FDH is a tightly bound redox cofactor (similar to nicotinamide proteins). The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.


Pssm-ID: 176246 [Multi-domain]  Cd Length: 345  Bit Score: 43.39  E-value: 2.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1731 VLGRECSGRIAAVGEGVSGLRVGDEVL-------AVAPGCFRS---------YVL---VDESQV--VRRP---ASL---- 1782
Cdd:cd08286   57 ILGHEGVGVVEEVGSAVTNFKVGDRVLiscisscGTCGYCRKGlyshcesggWILgnlIDGTQAeyVRIPhadNSLyklp 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1783 -GLAEGAAQMVP--FATAYFALHTVGRLRRGERILIhaaaggLGLAAVQLAS------RTGAEILATAGSEQKREYLRSL 1853
Cdd:cd08286  137 eGVDEEAAVMLSdiLPTGYECGVLNGKVKPGDTVAI------VGAGPVGLAAlltaqlYSPSKIIMVDLDDNRLEVAKKL 210

                        170       180       190
                 ....*....|....*....|....*....|
gi 53747904 1854 GIAHVLDSRSTSFVSEVRERTGGRGVDVVL 1883
Cdd:cd08286  211 GATHTVNSAKGDAIEQVLELTDGRGVDVVI 240
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
 2369-2912 2.38e-03

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


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 44.09  E-value: 2.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2369 WARLDTLPPPpelplvkEPSQLEHARFTHREARLEPHRWARLQERARAHGLTPSAACMAAFAEVLARWSRHPRFTLNLTL 2448
Cdd:COG3321  849 WSALYPGRGR-------RRVPLPTYPFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALAL 921

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2449 FQRLPLHPQVDELVGDFTSLVLLEVEAHAASTFAERASRLQAQLWRDLEHGSVSAVQLIRELVRTGRRSPGAIMPVVFTS 2528
Cdd:COG3321  922 AAAALAALLALVALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAA 1001

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2529 ILSLDARRGPQGSLSFFEGELVYSISQTPQVWLDHGVHEEEGALVLAWDSVEALFPPGMVDDMFHAYQRLLGALAEEEQA 2608
Cdd:COG3321 1002 LALLAAAALLLAAAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAA 1081

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2609 WEGELPELLPPAQRELLARYNATQAPRPSGRLEEGFFTQARLHPELPALLAPERTLSYGELARRAQALAARLRELEVQPQ 2688
Cdd:COG3321 1082 AALALAAALAAAALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAA 1161

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2689 ELVAIAMHKGWEQATAVLGVLQAAAAYLPLDPEQPPLRLHQLLEEGPARVVLTQSSLLHTVPWPPGVQVIAVDELEPATE 2768
Cdd:COG3321 1162 ALAAALLAAAALLLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAA 1241

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 2769 APPLPPRGTPEHLAYVIYTSGSTGKPKGVAIEHRAALNTVVDLNTRFGVGPEDRVLGLSALTFDLSVYDVLGLLGAGGAL 2848
Cdd:COG3321 1242 AAAVAALAAAAAALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAAL 1321

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 53747904 2849 VLPAAEAEKDPAHWWERLVAGRVTVWNSTPALMLLLVEYAEQRGLKLPAALRLVMLSGDWIPVA 2912
Cdd:COG3321 1322 AAALLAAALAALAAAVAAALALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALALAALAAAV 1385
PLN02702 PLN02702
L-idonate 5-dehydrogenase
 1694-1765 3.07e-03

L-idonate 5-dehydrogenase


Pssm-ID: 215378 [Multi-domain]  Cd Length: 364  Bit Score: 42.84  E-value: 3.07e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 53747904  1694 PAPGPRQVEIEVEAAGLNFLDV--LGALGMMPALEAEESVLGRECSGRIAAVGEGVSGLRVGDEVlAVAPG--CFR 1765
Cdd:PLN02702   37 PPLGPHDVRVRMKAVGICGSDVhyLKTMRCADFVVKEPMVIGHECAGIIEEVGSEVKHLVVGDRV-ALEPGisCWR 111
MDR_yhdh cd08288
Yhdh putative quinone oxidoreductases; Yhdh putative quinone oxidoreductases (QOR). QOR ...
 1687-1882 3.95e-03

Yhdh putative quinone oxidoreductases; Yhdh putative quinone oxidoreductases (QOR). QOR catalyzes the conversion of a quinone + NAD(P)H to a hydroquinone + NAD(P)+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR actin the respiratory chains of bacteria and mitochondria, while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family, but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176248 [Multi-domain]  Cd Length: 324  Bit Score: 42.52  E-value: 3.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1687 GLRRCTRPAPGPRQVEIEVEAAGLNFLDVLGALGMMPALEAEESVLGrecsgrIAAVGEGVS----GLRVGDEVLA---- 1758
Cdd:cd08288   16 ELRELDESDLPEGDVTVEVHYSTLNYKDGLAITGKGGIVRTFPLVPG------IDLAGTVVEssspRFKPGDRVVLtgwg 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904 1759 ---VAPGCFRSYVLVDESQVVRRPASLGLAEGAAqmvpFATAYF-------ALHTVGRLRRGERILIHAAAGGLGLAAVQ 1828
Cdd:cd08288   90 vgeRHWGGYAQRARVKADWLVPLPEGLSARQAMA----IGTAGFtamlcvmALEDHGVTPGDGPVLVTGAAGGVGSVAVA 165

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 53747904 1829 LASRTGAEILATAGSEQKREYLRSLGIAHVLDsRSTsFVSEVR----ERTGGrGVDVV 1882
Cdd:cd08288  166 LLARLGYEVVASTGRPEEADYLRSLGASEIID-RAE-LSEPGRplqkERWAG-AVDTV 220
ENR_SDR cd05372
Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ...
 1233-1293 4.15e-03

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: 41.80  E-value: 4.15e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 53747904 1233 LEQLGAEVQVYTADVAEEAAVRSVVEQVHARWGKIHGVLHAAAtFDDGVIQLRTHEQSSRA 1293
Cdd:cd05372   47 AERLGESALVLPCDVSNDEEIKELFAEVKKDWGKLDGLVHSIA-FAPKVQLKGPFLDTSRK 106
PRK13391 PRK13391
acyl-CoA synthetase; Provisional
 2966-3127 4.32e-03

acyl-CoA synthetase; Provisional


Pssm-ID: 184022 [Multi-domain]  Cd Length: 511  Bit Score: 42.76  E-value: 4.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2966 HVLDGRLEARPWWVPGELYIGGeGLAREYWRDEPLTATRfiRHPRTGerLYRTGDQGRMLPEGSIEFLGREDLQVKVQGF 3045
Cdd:PRK13391  339 HILDDDGAELPPGEPGTIWFEG-GRPFEYLNDPAKTAEA--RHPDGT--WSTVGDIGYVDEDGYLYLTDRAAFMIISGGV 413

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  3046 RVELGEIEAALAQHP-ALSASVVVARGEPRG-VRRLVAYAVPRSGQTPA-AGELRRYLAERLPAYMVPSAFVLLESLPRS 3122
Cdd:PRK13391  414 NIYPQEAENLLITHPkVADAAVFGVPNEDLGeEVKAVVQPVDGVDPGPAlAAELIAFCRQRLSRQKCPRSIDFEDELPRL 493


                  ....*
gi 53747904  3123 RNGKI 3127
Cdd:PRK13391  494 PTGKL 498
PRK00174 PRK00174
acetyl-CoA synthetase; Provisional
 2779-2797 4.57e-03

acetyl-CoA synthetase; Provisional


Pssm-ID: 234677 [Multi-domain]  Cd Length: 637  Bit Score: 42.82  E-value: 4.57e-03
                          10
                  ....*....|....*....
gi 53747904  2779 EHLAYVIYTSGSTGKPKGV 2797
Cdd:PRK00174  245 EDPLFILYTSGSTGKPKGV 263
PRK08180 PRK08180
feruloyl-CoA synthase; Reviewed
 2648-2802 6.07e-03

feruloyl-CoA synthase; Reviewed


Pssm-ID: 236175 [Multi-domain]  Cd Length: 614  Bit Score: 42.56  E-value: 6.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2648 ARLHPELPAL-----LAPERTLSYGELARRAQALAARLRELEVQPQELVAIAMHKGWEQATAVLGVLQAAAAYLPLDPE- 2721
Cdd:PRK08180   49 AQEAPDRVFLaergaDGGWRRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMYAGVPYAPVSPAy 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53747904  2722 ----QPPLRLHQLLE----------EGPA------RVVLTQSSLLHTVPWPPGVQVIAVDELEPATEAPPLP---PRGTP 2778
Cdd:PRK08180  129 slvsQDFGKLRHVLElltpglvfadDGAAfaralaAVVPADVEVVAVRGAVPGRAATPFAALLATPPTAAVDaahAAVGP 208

                         170       180
                  ....*....|....*....|....
gi 53747904  2779 EHLAYVIYTSGSTGKPKGVAIEHR 2802
Cdd:PRK08180  209 DTIAKFLFTSGSTGLPKAVINTHR 232
PRK08628 PRK08628
SDR family oxidoreductase;
1232-1281 8.86e-03

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 41.10  E-value: 8.86e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 53747904  1232 ELEQLGAEVQVYTADVAEEAAVRSVVEQVHARWGKIHGVLHAAATfDDGV 1281
Cdd:PRK08628   49 ELRALQPRAEFVQVDLTDDAQCRDAVEQTVAKFGRIDGLVNNAGV-NDGV 97
hsFATP4_like cd05939
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ...
 2767-2823 9.50e-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: 41.64  E-value: 9.50e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 53747904 2767 TEAPPLPPRGTPEHLAYvIYTSGSTGKPKGVAIEHRAALNTVVDLNTRFGVGPEDRV 2823
Cdd:cd05939   93 TEPPSQDDVNFRDKLFY-IYTSGTTGLPKAAVIVHSRYYRIAAGAYYAFGMRPEDVV 148
PRK06198 PRK06198
short chain dehydrogenase; Provisional
 1232-1282 9.57e-03

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 40.76  E-value: 9.57e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 53747904  1232 ELEQLGAEVQVYTADVAEEAAVRSVVEQVHARWGKIHGVLHAAATFDDGVI 1282
Cdd:PRK06198   50 ELEALGAKAVFVQADLSDVEDCRRVVAAADEAFGRLDALVNAAGLTDRGTI 100
 
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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