|
Name |
Accession |
Description |
Interval |
E-value |
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
801-1698 |
0e+00 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 963.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 801 PLVRVMSFSRSEQEHFLLVVIHHLIFDGVSSVTFIHSLFDTYQLLLKGQQPEIAVSPAIYHDFAAWEKNMLAGKDGVKHR 880
Cdd:COG1020 129 PLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLLLAELLRLYLAAYAGAPLPLPPLPIQYADYALWQREWLQGEELARQL 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 881 TYWQKQLSGTLPNLQLP-KVSASSVSEFREDTYTRRLSSGFMNQVRMFAKEHSVNVTTVFLSCYMMLLGRYTGQKEQIVG 959
Cdd:COG1020 209 AYWRQQLAGLPPLLELPtDRPRPAVQSYRGARVSFRLPAELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVG 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 960 MPAMVRPEERFDDAIGHFLNMLPIRSELNPADTFSSFISKLQLTILDGLDHAAYPFPKMVRDLNIPRSQAGSPVFQTAFF 1039
Cdd:COG1020 289 TPVAGRPRPELEGLVGFFVNTLPLRVDLSGDPSFAELLARVRETLLAAYAHQDLPFERLVEELQPERDLSRNPLFQVMFV 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1040 YQNFLQSGsyqsllsryADF--FSVDYVEYIHQEGEYELVFELWETEEKMELNIKYNTGLFDAASISAMFDHFVYVTEQA 1117
Cdd:COG1020 369 LQNAPADE---------LELpgLTLEPLELDSGTAKFDLTLTVVETGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEAL 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1118 MLNPSQPLKEYSLLPEAEKQMILKTWNATGKTYP-YITFHELFEQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQ 1196
Cdd:COG1020 440 AADPDQPLGDLPLLTAAERQQLLAEWNATAAPYPaDATLHELFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLR 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1197 AHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLEDSEVFITLTTSELVNTLSWNGVTTALLDQ 1276
Cdd:COG1020 520 ALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYMLEDAGARLVLTQSALAARLPELGVPVLALDA 599
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1277 dwDEIAQTASDRkvLTRTVTPENLAYVIYTSGSTGKPKGVMIPHKALTNFLVSMGETPGLTAEDKMLAVTTYCFDIAALE 1356
Cdd:COG1020 600 --LALAAEPATN--PPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFDASVWE 675
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1357 LFLPLIKGAHCYICQTEHTKDVEKLKRDIRTIKPTVMQATPATWKMLFYSGWENEENVK-ILCGGEALPETLKRYFLDTG 1435
Cdd:COG1020 676 IFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLLRALLDAAPEALPSLRlVLVGGEALPPELVRRWRARL 755
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1436 SEA--WNMFGPTETTIWSAVQRINDECSRA---TIGRPIANTQIYITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELT 1510
Cdd:COG1020 756 PGArlVNLYGPTETTVDSTYYEVTPPDADGgsvPIGRPIANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELT 835
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1511 DSRFIDNPF-EPGSKLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMDN-----L 1584
Cdd:COG1020 836 AERFVADPFgFPGARLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDApgdkrL 915
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1585 AAYYTAkHANASLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLKNIDLSGEQlkQRQTSPKNIQDTVFT 1664
Cdd:COG1020 916 VAYVVP-EAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAAAAAA--AAAAPPAEEEEEEAA 992
|
890 900 910
....*....|....*....|....*....|....
gi 1776025254 1665 IWQEVLKTSDIEWDDGFFDVGGDSLLAVTVADRI 1698
Cdd:COG1020 993 LALLLLLVVVVGDDDFFFFGGGLGLLLLLALARA 1026
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
20-561 |
0e+00 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 866.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 20 PLHISEKQPATIPEVLYRtAAELGDTKGIIYLQPDGTEVYQSYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNSQLLP 99
Cdd:cd05906 1 PLHRPEGAPRTLLELLLR-AAERGPTKGITYIDADGSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 100 AFWGCVLTGVVPAPLAVPPTYAESSSGTQKLKDAWTLLDKPAVITDRGMHQEMLDWAKEQGLEGFRAIIVEDLLSAEADT 179
Cdd:cd05906 80 AFWACVLAGFVPAPLTVPPTYDEPNARLRKLRHIWQLLGSPVVLTDAELVAEFAGLETLSGLPGIRVLSIEELLDTAADH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 180 DWHQSSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDHVGGIGMLHLRDVYLGCQEIN 259
Cdd:cd05906 160 DLPQSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHVGGLVELHLRAVYLGCQQVH 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 260 VSSETILMEPLKWLDWIDHYRASVTWAPNFAFGLVTDFAEEIKDRKWDLSSMRYMLNGGEAMVAKVGRRILELLEPHGLP 339
Cdd:cd05906 240 VPTEEILADPLRWLDLIDRYRVTITWAPNFAFALLNDLLEEIEDGTWDLSSLRYLVNAGEAVVAKTIRRLLRLLEPYGLP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 340 ADAIRPAWGMSETSSGVIFSHEFTRAGTSDDDHFVEIGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGYYQRPD 419
Cdd:cd05906 320 PDAIRPAFGMTETCSGVIYSRSFPTYDHSQALEFVSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 420 LNESVFTEDGWFETGDLGFLRNGRLTITGRTKDAIIINGINYYSHAIESAVEELSEIETSYTAACAVRLGQNSTDQLAIF 499
Cdd:cd05906 400 ANAEAFTEDGWFRTGDLGFLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPSFTAAFAVRDPGAETEELAIF 479
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1776025254 500 FVTSAKLNDeQMSQLLRNIQSHVSQVIGVTPEYLLPVQKEEIPKTAIGKIQRTQLKTSFENG 561
Cdd:cd05906 480 FVPEYDLQD-ALSETLRAIRSVVSREVGVSPAYLIPLPKEEIPKTSLGKIQRSKLKAAFEAG 540
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
185-1737 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 845.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 185 SPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDI-----TFN-----WMPFDHVGGIGMLHLRDvylg 254
Cdd:PRK12467 654 DPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSmlmvsTFAfdlgvTELFGALASGATLHLLP---- 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 255 cqeinvssETILMEPLKWLDWIDHYRASVTWAPNFAFGLVTDFAEEIKDRkwdlsSMRYMLNGGEAMVAKVGRRILELLe 334
Cdd:PRK12467 730 --------PDCARDAEAFAALMADQGVTVLKIVPSHLQALLQASRVALPR-----PQRALVCGGEALQVDLLARVRALG- 795
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 335 phglPADAIRPAWGMSETSSGVIFsheFTRAGTSDDDHFVEIGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGY 414
Cdd:PRK12467 796 ----PGARLINHYGPTETTVGVST---YELSDEERDFGNVPIGQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGY 868
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 415 YQRPDLNESVFTEDGW-------FETGDLGFLR-NGRLTITGRTKDAIIINGINYyshaiesaveELSEIETSYTAACAV 486
Cdd:PRK12467 869 HRRPALTAERFVPDPFgadggrlYRTGDLARYRaDGVIEYLGRMDHQVKIRGFRI----------ELGEIEARLLAQPGV 938
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 487 R------LGQNSTDQLAIFFVTSAKLNDEQMSQLLRNIQSHVSQVIgvtPEYLLP---VQKEEIPKTAIGKIQRTQLKts 557
Cdd:PRK12467 939 ReavvlaQPGDAGLQLVAYLVPAAVADGAEHQATRDELKAQLRQVL---PDYMVPahlLLLDSLPLTPNGKLDRKALP-- 1013
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 558 fengefdhllhKPnrmnDAVQDEEMQQADhvkrvREEIQEHLLTCLTEELHVSRdwVEPNANIQSLGVNSIKMMKLIRSI 637
Cdd:PRK12467 1014 -----------KP----DASAVQATFVAP-----QTELEKRLAAIWADVLKVER--VGLTDNFFELGGHSLLATQVISRV 1071
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 638 EKNYHIKLTAREIHQYPTIERLASYLSehedlssssADKKGTDTYKTEPERSQAtfQPLSEVQKGLWTLQKMSPEKSAYH 717
Cdd:PRK12467 1072 RQRLGIQVPLRTLFEHQTLAGFAQAVA---------AQQQGAQPALPDVDRDQP--LPLSYAQERQWFLWQLEPGSAAYH 1140
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 718 VPLCFKFSSGLHLETLQQAFGLVLNQHPILKHVIQEKDGVPILKNEPALS--IEIKTENISSMKESDIPAFLRKKVKEPY 795
Cdd:PRK12467 1141 IPQALRLKGPLDIEALERSFDALVARHESLRTTFVQEDGRTRQVIHPVGSltLEEPLLLAADKDEAQLKVYVEAEARQPF 1220
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 796 VKENSPLVRVMSFSRSEQEHFLLVVIHHLIFDGVSSVTFIHSLFDTYQLLLKGQQPEIAVSPAIYHDFAAWEKNMLAGKD 875
Cdd:PRK12467 1221 DLEQGPLLRVGLLRLAADEHVLVLTLHHIVSDGWSMQVLVDELVALYAAYSQGQSLQLPALPIQYADYAVWQRQWMDAGE 1300
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 876 GVKHRTYWQKQLSGTLPNLQLP-KVSASSVSEFREDTYTRRLSSGFMNQVRMFAKEHSVNVTTVFLSCYMMLLGRYTGQK 954
Cdd:PRK12467 1301 RARQLAYWKAQLGGEQPVLELPtDRPRPAVQSHRGARLAFELPPALAEGLRALARREGVTLFMLLLASFQTLLHRYSGQD 1380
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 955 EQIVGMPAMVRPEERFDDAIGHFLNMLPIRSELNPADTFSSFISKLQLTILDGLDHAAYPFPKMVRDLNIPRSQAGSPVF 1034
Cdd:PRK12467 1381 DIRVGVPIANRNRAETEGLIGFFVNTQVLRAEVDGQASFQQLLQQVKQAALEAQAHQDLPFEQLVEALQPERSLSHSPLF 1460
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1035 QTAFFYQNFLQSGSYQsllsryADFFSVDYVEYIHQEGEYELVFELWETEEKMELNIKYNTGLFDAASISAMFDHFVYVT 1114
Cdd:PRK12467 1461 QVMFNHQRDDHQAQAQ------LPGLSVESLSWESQTAQFDLTLDTYESSEGLQASLTYATDLFEASTIERLAGHWLNLL 1534
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1115 EQAMLNPSQPLKEYSLLPEAEKQMILKTWNATGKTYPY-ITFHELFEQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAI 1193
Cdd:PRK12467 1535 QGLVADPERRLGELDLLDEAERRQILEGWNATHTGYPLaRLVHQLIEDQAAATPEAVALVFGEQELTYGELNRRANRLAH 1614
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1194 YLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLEDSEVFITLTTSELVNTL-SWNGVTTA 1272
Cdd:PRK12467 1615 RLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQSHLQARLpLPDGLRSL 1694
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1273 LLDQ--DWDEiAQTASDRKVltrTVTPENLAYVIYTSGSTGKPKGVMIPHKALTNFLVSMGETPGLTAEDKMLAVTTYCF 1350
Cdd:PRK12467 1695 VLDQedDWLE-GYSDSNPAV---NLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFAF 1770
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1351 DIAALELFLPLIKGAHCYICQTEHTKDVEKLKRDIRTIKPTVMQATPATWKMlFYSGWENEENV----KILCGGEALPET 1426
Cdd:PRK12467 1771 DVSVWELFWPLINGARLVIAPPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQ-LLQMDEQVEHPlslrRVVCGGEALEVE 1849
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1427 LKRYFL----DTGseAWNMFGPTETTI----WSAvqRINDECSRAT--IGRPIANTQIYITDSQLAPVPAGVPGELCIAG 1496
Cdd:PRK12467 1850 ALRPWLerlpDTG--LFNLYGPTETAVdvthWTC--RRKDLEGRDSvpIGQPIANLSTYILDASLNPVPIGVAGELYLGG 1925
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1497 DGVAKGYYKKEELTDSRFIDNPF-EPGSKLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILEC 1575
Cdd:PRK12467 1926 VGLARGYLNRPALTAERFVADPFgTVGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREA 2005
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1576 VVVA-DMDN---LAAYYTAKHA-------NASLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLKNIDLS 1644
Cdd:PRK12467 2006 VVIAqDGANgkqLVAYVVPTDPglvdddeAQVALRAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKALPAPDAS 2085
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1645 geQLKQRQTSPKN-IQDTVFTIWQEVLKTSDIEWDDGFFDVGGDSLLAVTVADRIKHElSCEFSVTDLFEYSTIKNISQY 1723
Cdd:PRK12467 2086 --ELQQAYVAPQSeLEQRLAAIWQDVLGLEQVGLHDNFFELGGDSIISIQVVSRARQA-GIRFTPKDLFQHQTVQSLAAV 2162
|
1610
....*....|....
gi 1776025254 1724 ITEQRMGNASDHMP 1737
Cdd:PRK12467 2163 AQEGDGTVSIDQGP 2176
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
3339-3881 |
0e+00 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 814.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3339 EPVAIVGISGRFPGAMDIDEFWKNLEEGKDSITEVPKDRWDWREHYGNPDTDVNKTDIKWGGFIDGVAEFDPLFFGISPR 3418
Cdd:COG3321 4 EPIAIIGMACRFPGADDPEEFWRNLRAGRDAITEVPADRWDADAYYDPDPDAPGKTYVRWGGFLDDVDEFDALFFGISPR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3419 EADYVDPQQRLLMTYVWKALEDAGCPPQSLSGTGTGIFIGTGNTGYKDLFHRANLPIEGHAATGhMIPSVGPNRMSYFLN 3498
Cdd:COG3321 84 EAEAMDPQQRLLLEVAWEALEDAGYDPESLAGSRTGVFVGASSNDYALLLLADPEAIDAYALTG-NAKSVLAGRISYKLD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3499 IHGPSEPVETACSSSLVAIHRAVTAMQNGDCEMAIAGGVNTILTEEAHISYSKAGMLSKDGRCKTFSADANGYVRGEGVG 3578
Cdd:COG3321 163 LRGPSVTVDTACSSSLVAVHLACQSLRSGECDLALAGGVNLMLTPESFILFSKGGMLSPDGRCRAFDADADGYVRGEGVG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3579 MVMLKKLEDAERDGNHIYGVIRGTAENHGGRANTLTSPNPKAQADLLVRAYRQAGIDPSTVTYIEAHGTGTELGDPIEIN 3658
Cdd:COG3321 243 VVVLKRLSDALRDGDRIYAVIRGSAVNQDGRSNGLTAPNGPAQAAVIRRALADAGVDPATVDYVEAHGTGTPLGDPIEAA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3659 GLKAAFKELsnmRGESQPdvpdhrCGIGSVKSNIGHLELAAGISGLIKVLLQMKHKTLVKSLHCETLNPYLQLTDSPFYI 3738
Cdd:COG3321 323 ALTAAFGQG---RPADQP------CAIGSVKSNIGHLEAAAGVAGLIKAVLALRHGVLPPTLHFETPNPHIDFENSPFYV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3739 VQEKQEWKSvtdcdgNELPRRAGISSFGIGGVNAHIVIEEYMPKANSEHTATEQPNVIVLSAKNKSRLIDRASQLLEAIR 3818
Cdd:COG3321 394 NTELRPWPA------GGGPRRAGVSSFGFGGTNAHVVLEEAPAAAPAAAAAARPPQLLVLSAKTEEALRALAARLAAFLE 467
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1776025254 3819 NKkyTDQGLHRIAYTLQVGREEMDERLACVAGTMQELEEKLQAFVDGKEETDEFFRGQSHRNK 3881
Cdd:COG3321 468 AH--PDLDLADVAYTLATGRAHFEHRLAVVASSREELAAKLRALAAGEAAPGVVTGAAAAAPK 528
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
28-1715 |
0e+00 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 807.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 28 PATIPEVLYRTAAELGDTKGIIYLQPDGTE-VYQSYRRLwDDGLRIVKGLRQSGLKAKQSVILQLGDNSQLLPAFWGCVL 106
Cdd:PRK05691 8 PLTLVQALQRRAAQTPDRLALRFLADDPGEgVVLSYRDL-DLRARTIAAALQARASFGDRAVLLFPSGPDYVAAFFGCLY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 107 TGVVPAPlAVPPtyaESSSGTQK------LKDAWTLLdkpaVITDRGMHQEMldwakeQGLEGFRA------IIVEDLLS 174
Cdd:PRK05691 87 AGVIAVP-AYPP---ESARRHHQerllsiIADAEPRL----LLTVADLRDSL------LQMEELAAanapelLCVDTLDP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 175 AEADtDWH--QSSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIiqMQGF----TREDITFNWMPFDH-VGGIGMLh 247
Cdd:PRK05691 153 ALAE-AWQepALQPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLI--RHGFgidlNPDDVIVSWLPLYHdMGLIGGL- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 248 LRDVYLGCQEINVSSETILMEPLKWLDWIDHYRASVTWAPNFAFGLVTDFAEEIKDRKWDLSSMRYMLNGGEAMVAKVGR 327
Cdd:PRK05691 229 LQPIFSGVPCVLMSPAYFLERPLRWLEAISEYGGTISGGPDFAYRLCSERVSESALERLDLSRWRVAYSGSEPIRQDSLE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 328 RILELLEPHGLPADAIRPAWGMSETSSGV--------IFSHEF-------TRAGTSDDDHFVEIGSPIPGFSMRIVN-DH 391
Cdd:PRK05691 309 RFAEKFAACGFDPDSFFASYGLAEATLFVsggrrgqgIPALELdaealarNRAEPGTGSVLMSCGRSQPGHAVLIVDpQS 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 392 NELVEEGEIGRFQVSGLSVTSGYYQRPDLNESVFTE-DG--WFETGDLGFLRNGRLTITGRTKDAIIINGINYYSHAIES 468
Cdd:PRK05691 389 LEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTFVEhDGrtWLRTGDLGFLRDGELFVTGRLKDMLIVRGHNLYPQDIEK 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 469 AVE-ELSEIETSYTAACAVRlgQNSTDQLAIFFVTSAKLNDEQMSQ-LLRNIQSHVSQVIGVTPEYLLPVQKEEIPKTAI 546
Cdd:PRK05691 469 TVErEVEVVRKGRVAAFAVN--HQGEEGIGIAAEISRSVQKILPPQaLIKSIRQAVAEACQEAPSVVLLLNPGALPKTSS 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 547 GKIQRTQLKTSFENGEFDHLLHKPNrmNDAVQDEEMQQADhvkrvrEEIQEHLLTCLTEELHVSRdwVEPNANIQSLGVN 626
Cdd:PRK05691 547 GKLQRSACRLRLADGSLDSYALFPA--LQAVEAAQTAASG------DELQARIAAIWCEQLKVEQ--VAADDHFFLLGGN 616
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 627 SIKMMKLIRSIEKNYHIKLTAREIHQYPTIERLASYLSEHEdlssssADKKGTDTYKTEPERSQATfqPLSEVQKGLWTL 706
Cdd:PRK05691 617 SIAATQVVARLRDELGIDLNLRQLFEAPTLAAFSAAVARQL------AGGGAAQAAIARLPRGQAL--PQSLAQNRLWLL 688
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 707 QKMSPEKSAYHVPlcfkfsSGLHL------ETLQQAFGLVLNQHPILKHVIQEKDGVPILKNEPALSIEIKTENISSMKE 780
Cdd:PRK05691 689 WQLDPQSAAYNIP------GGLHLrgeldeAALRASFQRLVERHESLRTRFYERDGVALQRIDAQGEFALQRIDLSDLPE 762
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 781 SDIPAFLRK----KVKEPYVKENSPLVRVMSFSRSEQEHFLLVVIHHLIFDGVSSVTFIHSLFDTYQLLLKGQQPEIAVS 856
Cdd:PRK05691 763 AEREARAAQireeEARQPFDLEKGPLLRVTLVRLDDEEHQLLVTLHHIVADGWSLNILLDEFSRLYAAACQGQTAELAPL 842
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 857 PAIYHDFAAWEKNMLAGKDGVKHRTYWQKQLSGTLPNLQLP-KVSASSVSEFREDTYTRRLSSGFMNQVRMFAKEHSVNV 935
Cdd:PRK05691 843 PLGYADYGAWQRQWLAQGEAARQLAYWKAQLGDEQPVLELAtDHPRSARQAHSAARYSLRVDASLSEALRGLAQAHQATL 922
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 936 TTVFLSCYMMLLGRYTGQKEQIVGMPAMVRPEERFDDAIGHFLNMLPIRSELNPADTFSSFISKLQLTILDGLDHAAYPF 1015
Cdd:PRK05691 923 FMVLLAAFQALLHRYSGQGDIRIGVPNANRPRLETQGLVGFFINTQVLRAQLDGRLPFTALLAQVRQATLGAQAHQDLPF 1002
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1016 PKMVRDLNIPRSQAgspVFQTAFFYQnflqsgsyQSLLS--RYADFFSVDYVEYIHQEGEYELvfELWETEE---KMELN 1090
Cdd:PRK05691 1003 EQLVEALPQAREQG---LFQVMFNHQ--------QRDLSalRRLPGLLAEELPWHSREAKFDL--QLHSEEDrngRLTLS 1069
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1091 IKYNTGLFDAASISAMFDHFVYVTEQAMLNPSQPLKEYSLLPEAEKQMiLKTWNATGKTYPYITFHELFEQQAKKTPDRA 1170
Cdd:PRK05691 1070 FDYAAELFDAATIERLAEHFLALLEQVCEDPQRALGDVQLLDAAERAQ-LAQWGQAPCAPAQAWLPELLNEQARQTPERI 1148
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1171 AVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLEDSE 1250
Cdd:PRK05691 1149 ALVWDGGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSG 1228
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1251 VFITLTTSELVNTL-SWNGVTTALLDQ-DWDEIAQTASdrkvlTRTVTPENLAYVIYTSGSTGKPKGVMIPHKALTNFLV 1328
Cdd:PRK05691 1229 VELLLTQSHLLERLpQAEGVSAIALDSlHLDSWPSQAP-----GLHLHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQ 1303
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1329 SMGETPGLTAEDKMLAVTTYCFDIAALELFLPLIKGAHCYICQTEHTKDVEKLKRDIRTIKPTVMQATPATWKMLFYSGW 1408
Cdd:PRK05691 1304 WMQATYALDDSDVLMQKAPISFDVSVWECFWPLITGCRLVLAGPGEHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEPL 1383
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1409 ENEENV--KILCGGEALPETLKRYFLDT--GSEAWNMFGPTETTI----WsavQRINDECSRATIGRPIANTQIYITDSQ 1480
Cdd:PRK05691 1384 AAACTSlrRLFSGGEALPAELRNRVLQRlpQVQLHNRYGPTETAInvthW---QCQAEDGERSPIGRPLGNVLCRVLDAE 1460
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1481 LAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPF-EPGSKLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIEL 1559
Cdd:PRK05691 1461 LNLLPPGVAGELCIGGAGLARGYLGRPALTAERFVPDPLgEDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEP 1540
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1560 GDIESRLSEHPGILECVVV----ADMDNLAAYYTAKhANASLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDR 1635
Cdd:PRK05691 1541 EEIQARLLAQPGVAQAAVLvregAAGAQLVGYYTGE-AGQEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDR 1619
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1636 NSLKNidlsgEQLKQRQ-TSPKN-IQDTVFTIWQEVLKTSDIEWDDGFFDVGGDSLLAVTVADRIKHELSCEFSVTDLFE 1713
Cdd:PRK05691 1620 RALPE-----PVWQQREhVEPRTeLQQQIAAIWREVLGLPRVGLRDDFFALGGHSLLATQIVSRTRQACDVELPLRALFE 1694
|
..
gi 1776025254 1714 YS 1715
Cdd:PRK05691 1695 AS 1696
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
61-1722 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 794.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 61 SYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNSQLLPAFWGCVLTGVVPAPLavPPTYAesssgTQKLkdAWTLLDKP 140
Cdd:PRK12316 2030 SYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPL--DPNYP-----AERL--AYMLEDSG 2100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 141 A--VITDRGMHQEMLdwaKEQGLEgfraiivedLLSAEADTDWH---------QSSPEDLALLLLTSGSTGTPKAVMLNH 209
Cdd:PRK12316 2101 AalLLTQRHLLERLP---LPAGVA---------RLPLDRDAEWAdypdtapavQLAGENLAYVIYTSGSTGLPKGVAVSH 2168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 210 RNIMSMVKGIIQMQGFTREDITFNWMPFDHVGGI-----GMLHLRDVYLGCQEINVSSETI-LMEplkwldwidhyRASV 283
Cdd:PRK12316 2169 GALVAHCQAAGERYELSPADCELQFMSFSFDGAHeqwfhPLLNGARVLIRDDELWDPEQLYdEME-----------RHGV 2237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 284 TWApNFAFGLVTDFAEEIKDRKWDLSSMRYMLnGGEAMVAKVGRRILEllephGLPADAIRPAWGMSETSsgVIFSHEFT 363
Cdd:PRK12316 2238 TIL-DFPPVYLQQLAEHAERDGRPPAVRVYCF-GGEAVPAASLRLAWE-----ALRPVYLFNGYGPTEAV--VTPLLWKC 2308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 364 RAGTSDDDHFVEIGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGYYQRPDLNESVFTEDGW-------FETGDL 436
Cdd:PRK12316 2309 RPQDPCGAAYVPIGRALGNRRAYILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFsasgerlYRTGDL 2388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 437 GFLR-NGRLTITGRTKDAIIINGINYyshaiesaveELSEIETSYTAACAVR----LGQN--STDQLAIFFVTsaklnDE 509
Cdd:PRK12316 2389 ARYRaDGVVEYLGRIDHQVKIRGFRI----------ELGEIEARLQAHPAVReavvVAQDgaSGKQLVAYVVP-----DD 2453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 510 QMSQLLRNIQSHVSQVIgvtPEYLLP---VQKEEIPKTAIGKIQRTQLKtsfengefdhllhkpnrmndAVQDEEMQQAD 586
Cdd:PRK12316 2454 AAEDLLAELRAWLAARL---PAYMVPahwVVLERLPLNPNGKLDRKALP--------------------KPDVSQLRQAY 2510
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 587 HVKRvrEEIQEHLLTCLTEELHVSRdwVEPNANIQSLGVNSIKMMKLIRSIEKNYHIKLTAREIHQYPTIERLAsylseh 666
Cdd:PRK12316 2511 VAPQ--EGLEQRLAAIWQAVLKVEQ--VGLDDHFFELGGHSLLATQVVSRVRQDLGLEVPLRILFERPTLAAFA------ 2580
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 667 edlssssADKKGTDTYKTEPERSQATFQPL--SEVQKGLWTLQKMSPEKSAYHVPLCFKFSSGLHLETLQQAFGLVLNQH 744
Cdd:PRK12316 2581 -------ASLESGQTSRAPVLQKVTRVQPLplSHAQQRQWFLWQLEPESAAYHLPSALHLRGVLDQAALEQAFDALVLRH 2653
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 745 PILKHVIQEKDGVPILKNEPALSIEIKTENISSMKESDIPAFLRKKVKEPYVKENSPLVRVMSFSRSEQEHFLLVVIHHL 824
Cdd:PRK12316 2654 ETLRTRFVEVGEQTRQVILPNMSLRIVLEDCAGVADAAIRQRVAEEIQRPFDLARGPLLRVRLLALDGQEHVLVITQHHI 2733
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 825 IFDGVSSVTFIHSLFDTYQLLLKGQQPEIAVSPAIYHDFAAWEKNMLAGKDGVKHRTYWQKQLSGTLPNLQLPKVSAS-S 903
Cdd:PRK12316 2734 VSDGWSMQVMVDELVQAYAGARRGEQPTLPPLPLQYADYAAWQRAWMDSGEGARQLDYWRERLGGEQPVLELPLDRPRpA 2813
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 904 VSEFREDTYTRRLSSGFMNQVRMFAKEHSVNVTTVFLSCYMMLLGRYTGQKEQIVGMPAMVRPEERFDDAIGHFLNMLPI 983
Cdd:PRK12316 2814 LQSHRGARLDVALDVALSRELLALARREGVTLFMLLLASFQVLLHRYSGQSDIRVGVPIANRNRAETERLIGFFVNTQVL 2893
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 984 RSELNPADTFSSFISKLQLTILDGLDHAAYPFPKMVRDLNIPRSQAGSPVFQTAFFYQNFLQSGSYQSLLsryaDFFSVD 1063
Cdd:PRK12316 2894 RAQVDAQLAFRDLLGQVKEQALGAQAHQDLPFEQLVEALQPERSLSHSPLFQVMYNHQSGERAAAQLPGL----HIESFA 2969
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1064 YVEYIHQegeYELVFELWETEEKMELNIKYNTGLFDAASISAMFDHFVYVTEQAMLNPSQPLKEYSLLPEAEKQMILKTW 1143
Cdd:PRK12316 2970 WDGAATQ---FDLALDTWESAEGLGASLTYATDLFDARTVERLARHWQNLLRGMVENPQRSVDELAMLDAEERGQLLEAW 3046
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1144 NATGKTYPY-ITFHELFEQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLA 1222
Cdd:PRK12316 3047 NATAAEYPLeRGVHRLFEEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLA 3126
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1223 ILKAGGAYVPLDPSYPAERLEYMLEDSEVFITLTTSELVNTLSwNGVTTALLDQDWDEIAQTASDRKVltrtvTPENLAY 1302
Cdd:PRK12316 3127 ILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQSHLRLPLA-QGVQVLDLDRGDENYAEANPAIRT-----MPENLAY 3200
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1303 VIYTSGSTGKPKGVMIPHKALTNFLVSMGETPGLTAEDKMLAVTTYCFDIAALELFLPLIKGAHCYICQTEHTKDVEKLK 1382
Cdd:PRK12316 3201 VIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDPALLV 3280
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1383 RDIRTIKPTVMQATPATWKMLFYSGWENEENV--KILCGGEALPETLKRYFLdTGSEAWNMFGPTETTIWSAVQRINDEC 1460
Cdd:PRK12316 3281 ELINSEGVDVLHAYPSMLQAFLEEEDAHRCTSlkRIVCGGEALPADLQQQVF-AGLPLYNLYGPTEATITVTHWQCVEEG 3359
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1461 -SRATIGRPIANTQIYITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPFEPGSKLYRTGDMARWLPGGR 1539
Cdd:PRK12316 3360 kDAVPIGRPIANRACYILDGSLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPFVPGERLYRTGDLARYRADGV 3439
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1540 IEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMDNLAAYYTAKHANASLTARELRHFVKNALPAYMVPSYF 1619
Cdd:PRK12316 3440 IEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAVDGRQLVAYVVPEDEAGDLREALKAHLKASLPEYMVPAHL 3519
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1620 IQLDHMPLTPNGKIDRNSLKNIDLSgeQLKQRQTSPKN-IQDTVFTIWQEVLKTSDIEWDDGFFDVGGDSLLAVTVADRI 1698
Cdd:PRK12316 3520 LFLERMPLTPNGKLDRKALPRPDAA--LLQQDYVAPVNeLERRLAAIWADVLKLEQVGLTDNFFELGGDSIISLQVVSRA 3597
|
1690 1700
....*....|....*....|....
gi 1776025254 1699 KhELSCEFSVTDLFEYSTIKNISQ 1722
Cdd:PRK12316 3598 R-QAGIRFTPKDLFQHQTIQGLAR 3620
|
|
| C_PKS-NRPS_PksJ-like |
cd20484 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
693-1121 |
0e+00 |
|
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs), similar to Bacillus subtilis PksJ; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily have the typical C-domain HHxxxD motif. PksJ is involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is important in secondary metabolism. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380472 [Multi-domain] Cd Length: 430 Bit Score: 789.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 693 FQPLSEVQKGLWTLQKMSPEKSAYHVPLCFKFSSGLHLETLQQAFGLVLNQHPILKHVIQEKDGVPILKNEPALSIEIKT 772
Cdd:cd20484 1 RSPLSEGQKGLWMLQKMSPEMSAYNVPLCFRFSSKLDVEKFKQACQFVLEQHPILKSVIEEEDGVPFQKIEPSKPLSFQE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 773 ENISSMKESDIPAFLRKKVKEPYVKENSPLVRVMSFSRSEQEHFLLVVIHHLIFDGVSSVTFIHSLFDTYQLLLKGQQPE 852
Cdd:cd20484 81 EDISSLKESEIIAYLREKAKEPFVLENGPLMRVHLFSRSEQEHFVLITIHHIIFDGSSSLTLIHSLLDAYQALLQGKQPT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 853 IAVSPAIYHDFAAWEKNMLAGKDGVKHRTYWQKQLSGTLPNLQLPKVSA-SSVSEFREDTYTRRLSSGFMNQVRMFAKEH 931
Cdd:cd20484 161 LASSPASYYDFVAWEQDMLAGAEGEEHRAYWKQQLSGTLPILELPADRPrSSAPSFEGQTYTRRLPSELSNQIKSFARSQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 932 SVNVTTVFLSCYMMLLGRYTGQKEQIVGMPAMVRPEERFDDAIGHFLNMLPIRSELNPADTFSSFISKLQLTILDGLDHA 1011
Cdd:cd20484 241 SINLSTVFLGIFKLLLHRYTGQEDIIVGMPTMGRPEERFDSLIGYFINMLPIRSRILGEETFSDFIRKLQLTVLDGLDHA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1012 AYPFPKMVRDLNIPRSQAGSPVFQTAFFYQNFLQSGSYQSLLSRYADFFSVDYVEYIHQEGEYELVFELWETEEKMELNI 1091
Cdd:cd20484 321 AYPFPAMVRDLNIPRSQANSPVFQVAFFYQNFLQSTSLQQFLAEYQDVLSIEFVEGIHQEGEYELVLEVYEQEDRFTLNI 400
|
410 420 430
....*....|....*....|....*....|
gi 1776025254 1092 KYNTGLFDAASISAMFDHFVYVTEQAMLNP 1121
Cdd:cd20484 401 KYNPDLFDASTIERMMEHYVKLAEELIANP 430
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
688-1733 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 788.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 688 RSQATFQPLSEVQKGLWTLQKMSPEKSAYHVPLCFKFSSGLHLETLQQAFGLVLNQHPILKHVIQEKDGVPILKNEPALS 767
Cdd:PRK12467 44 RSAFERIPLSYAQERQWFLWQLDPDSAAYNIPTALRLRGELDVSALRRAFDALVARHESLRTRFVQDEEGFRQVIDASLS 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 768 IEIKTENISSM----KESDIPAFLRKKVKEPYVKENSPLVRVMSFSRSEQEHFLLVVIHHLIFDGVSSVTFIHSLFDTYQ 843
Cdd:PRK12467 124 LTIPLDDLANEqgraRESQIEAYINEEVARPFDLANGPLLRVRLLRLADDEHVLVVTLHHIISDGWSMRVLVEELVQLYS 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 844 LLLKGQQPEIAVSPAIYHDFAAWEKNMLAGKDGVKHRTYWQKQLSGTLPNLQLP-KVSASSVSEFREDTYTRRLSSGFMN 922
Cdd:PRK12467 204 AYSQGREPSLPALPIQYADYAIWQRSWLEAGERERQLAYWQEQLGGEHTVLELPtDRPRPAVPSYRGARLRVDLPQALSA 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 923 QVRMFAKEHSVNVTTVFLSCYMMLLGRYTGQKEQIVGMPAMVRPEERFDDAIGHFLNMLPIRSELNPADTFSSFISKLQL 1002
Cdd:PRK12467 284 GLKALAQREGVTLFMVLLASFQTLLHRYSGQSDIRIGVPNANRNRVETERLIGFFVNTQVLKAEVDPQASFLELLQQVKR 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1003 TILDGLDHAAYPFPKMVRDLNIPRSQAGSPVFQTAFFYQNfLQSGSYQSLLSRYADFfSVDYVEYIHQEGEYELVFELWE 1082
Cdd:PRK12467 364 TALGAQAHQDLPFEQLVEALQPERSLSHSPLFQVMFNHQN-TATGGRDREGAQLPGL-TVEELSWARHTAQFDLALDTYE 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1083 TEEKMELNIKYNTGLFDAASISAMFDHFVYVTEQAMLNPSQPLKEYSLLPEAEKQMILKTWNATGKTYPYITFHELFEQQ 1162
Cdd:PRK12467 442 SAQGLWAAFTYATDLFEATTIERLATHWRNLLEAIVAEPRRRLGELPLLDAEERARELVRWNAPATEYAPDCVHQLIEAQ 521
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1163 AKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERL 1242
Cdd:PRK12467 522 ARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRL 601
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1243 EYMLEDSEVFITLTTSELVNTLSW-NGVTTALLDQDWDEIAQTASDRKVLtrTVTPENLAYVIYTSGSTGKPKGVMIPHK 1321
Cdd:PRK12467 602 AYMLDDSGVRLLLTQSHLLAQLPVpAGLRSLCLDEPADLLCGYSGHNPEV--ALDPDNLAYVIYTSGSTGQPKGVAISHG 679
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1322 ALTNFLVSMGETPGLTAEDKMLAVTTYCFDIAALELFLPLIKGAHCYICQTEHTKDVEKLKRDIRTIKPTVMQATPATWK 1401
Cdd:PRK12467 680 ALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPDCARDAEAFAALMADQGVTVLKIVPSHLQ 759
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1402 MLFYSGWENE--ENVKILCGGEALPETLKRYFLDTGSEA--WNMFGPTETTIWSAVQRINDE---CSRATIGRPIANTQI 1474
Cdd:PRK12467 760 ALLQASRVALprPQRALVCGGEALQVDLLARVRALGPGArlINHYGPTETTVGVSTYELSDEerdFGNVPIGQPLANLGL 839
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1475 YITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPFEP-GSKLYRTGDMARWLPGGRIEYIGRIDNQVKIR 1553
Cdd:PRK12467 840 YILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDPFGAdGGRLYRTGDLARYRADGVIEYLGRMDHQVKIR 919
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1554 GFRIELGDIESRLSEHPGILECVVVA---DMDN-LAAY----YTAKHANASLTARELRHFVKNALPAYMVPSYFIQLDHM 1625
Cdd:PRK12467 920 GFRIELGEIEARLLAQPGVREAVVLAqpgDAGLqLVAYlvpaAVADGAEHQATRDELKAQLRQVLPDYMVPAHLLLLDSL 999
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1626 PLTPNGKIDRNSLKNIDLSgeQLKQRQTSPKN-IQDTVFTIWQEVLKTSDIEWDDGFFDVGGDSLLAVTVADRIKHELSC 1704
Cdd:PRK12467 1000 PLTPNGKLDRKALPKPDAS--AVQATFVAPQTeLEKRLAAIWADVLKVERVGLTDNFFELGGHSLLATQVISRVRQRLGI 1077
|
1050 1060
....*....|....*....|....*....
gi 1776025254 1705 EFSVTDLFEYSTIKNISQYITEQRMGNAS 1733
Cdd:PRK12467 1078 QVPLRTLFEHQTLAGFAQAVAAQQQGAQP 1106
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
1167-1638 |
0e+00 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 766.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1167 PDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYML 1246
Cdd:cd12116 1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1247 EDSEVFITLTTSELVNTLSWNGVTTALLdqdwdeIAQTASDRKVLTRTVTPENLAYVIYTSGSTGKPKGVMIPHKALTNF 1326
Cdd:cd12116 81 EDAEPALVLTDDALPDRLPAGLPVLLLA------LAAAAAAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1327 LVSMGETPGLTAEDKMLAVTTYCFDIAALELFLPLIKGAHCYICQTEHTKDVEKLKRDIRTIKPTVMQATPATWKMLFYS 1406
Cdd:cd12116 155 LHSMRERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSITVMQATPATWRMLLDA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1407 GWENEENVKILCGGEALPETLKRYFLDTGSEAWNMFGPTETTIWSAVQRINDECSRATIGRPIANTQIYITDSQLAPVPA 1486
Cdd:cd12116 235 GWQGRAGLTALCGGEALPPDLAARLLSRVGSLWNLYGPTETTIWSTAARVTAAAGPIPIGRPLANTQVYVLDAALRPVPP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1487 GVPGELCIAGDGVAKGYYKKEELTDSRFIDNPF-EPGSKLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESR 1565
Cdd:cd12116 315 GVPGELYIGGDGVAQGYLGRPALTAERFVPDPFaGPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAA 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1776025254 1566 LSEHPGILECVVVADMDN----LAAYYTAKHAnASLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSL 1638
Cdd:cd12116 395 LAAHPGVAQAAVVVREDGgdrrLVAYVVLKAG-AAPDAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
686-1740 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 732.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 686 PERSQATFQPLSEVQKGLWTLQKMSPEKSAYHVPLCFKFSSGLHLETLQQAFGLVLNQHPILKHVIQEKDGVPILKNEPA 765
Cdd:PRK12316 42 AGVSSAERDRLSYAQQRMWFLWQLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADDSLAQVPLD 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 766 LSIEIKTENISSMKESDIPAFLRKKVK----EPYVKENSPLVRVMSFSRSEQEHFLLVVIHHLIFDGVSSVTFIHSLFDT 841
Cdd:PRK12316 122 RPLEVEFEDCSGLPEAEQEARLRDEAQreslQPFDLCEGPLLRVRLLRLGEEEHVLLLTLHHIVSDGWSMNVLIEEFSRF 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 842 YQLLLKGQQPEIAVSPAIYHDFAAWEKNMLAGKDGVKHRTYWQKQLSGTLPNLQLP-KVSASSVSEFREDTYTRRLSSGF 920
Cdd:PRK12316 202 YSAYATGAEPGLPALPIQYADYALWQRSWLEAGEQERQLEYWRAQLGEEHPVLELPtDHPRPAVPSYRGSRYEFSIDPAL 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 921 MNQVRMFAKEHSVNVTTVFLSCYMMLLGRYTGQKEQIVGMPAMVRPEERFDDAIGHFLNMLPIRSELNPADTFSSFISKL 1000
Cdd:PRK12316 282 AEALRGTARRQGLTLFMLLLGAFNVLLHRYSGQTDIRVGVPIANRNRAEVEGLIGFFVNTQVLRSVFDGRTRVATLLAGV 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1001 QLTILDGLDHAAYPFPKMVRDLNIPRSQAGSPVFQTAFFYQNFLQSGSYQSLLSRyadfFSVDYVEYIHQEGEYELVFEL 1080
Cdd:PRK12316 362 KDTVLGAQAHQDLPFERLVEALKVERSLSHSPLFQVMYNHQPLVADIEALDTVAG----LEFGQLEWKSRTTQFDLTLDT 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1081 WETEEKMELNIKYNTGLFDAASISAMFDHFVYVTEQAMLNPSQPLKEYSLLPEAEKQMILKTWNATGKTYPYIT-FHELF 1159
Cdd:PRK12316 438 YEKGGRLHAALTYATDLFEARTVERMARHWQNLLRGMVENPQARVDELPMLDAEERGQLVEGWNATAAEYPLQRgVHRLF 517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1160 EQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPA 1239
Cdd:PRK12316 518 EEQVERTPEAPALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPA 597
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1240 ERLEYMLEDSEVFITLTTSELVNTLSWN-GVTTALLDQDWDEIAqTASDRKVLTRtVTPENLAYVIYTSGSTGKPKGVMI 1318
Cdd:PRK12316 598 ERLAYMLEDSGVQLLLSQSHLGRKLPLAaGVQVLDLDRPAAWLE-GYSEENPGTE-LNPENLAYVIYTSGSTGKPKGAGN 675
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1319 PHKALTNFLVSMGETPGLTAEDKMLAVTTYCFDIAALELFLPLIKGAHCYICQTEHTKDVEKLKRDIRTIKPTVMQATPA 1398
Cdd:PRK12316 676 RHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPS 755
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1399 twkMLfySGWENEENV-------KILCGGEALPETLKR--YFLDTGSEAWNMFGPTETTI----WSAVQRINDECSratI 1465
Cdd:PRK12316 756 ---ML--QAFLQDEDVasctslrRIVCSGEALPADAQEqvFAKLPQAGLYNLYGPTEAAIdvthWTCVEEGGDSVP---I 827
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1466 GRPIANTQIYITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPFEPGSKLYRTGDMARWLPGGRIEYIGR 1545
Cdd:PRK12316 828 GRPIANLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFVPSPFVAGERMYRTGDLARYRADGVIEYAGR 907
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1546 IDNQVKIRGFRIELGDIESRLSEHPGILECVVVA-DMDNLAAYYTAKHANASLtaRE-LRHFVKNALPAYMVPSYFIQLD 1623
Cdd:PRK12316 908 IDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAvDGKQLVGYVVLESEGGDW--REaLKAHLAASLPEYMVPAQWLALE 985
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1624 HMPLTPNGKIDRNSLKNIDLSGEQlkQRQTSPKN-IQDTVFTIWQEVLKTSDIEWDDGFFDVGGDSLLAVTVADRIKHEl 1702
Cdd:PRK12316 986 RLPLTPNGKLDRKALPAPEASVAQ--QGYVAPRNaLERTLAAIWQDVLGVERVGLDDNFFELGGDSIVSIQVVSRARQA- 1062
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|...
gi 1776025254 1703 SCEFSVTDLFEYSTIKNISQYI-----TEQRMGNASDHMPTDP 1740
Cdd:PRK12316 1063 GIQLSPRDLFQHQTIRSLALVAkagqaTAADQGPASGEVALAP 1105
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
647-1736 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 711.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 647 AREIHQYPTIERLA-SYLSE------------HEDLSSSSADKKGTDTYKTE----PERSQATFQPLSEVQKGLWTLQKM 709
Cdd:PRK12316 4039 SREMFEEATIQRLAdDYAAEltalvehccdaeRHGVTPSDFPLAGLDQARLDalplPLGEIEDIYPLSPMQQGMLFHSLY 4118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 710 SPEKSAYHVPLCFKFSsGLHLETLQQAFGLVLNQHPILKH--VIQEKDGVPILKNEPALSIEIKTENISSMK--ESDIPA 785
Cdd:PRK12316 4119 EQEAGDYINQMRVDVQ-GLDVERFRAAWQAALDRHDVLRSgfVWQGELGRPLQVVHKQVSLPFAELDWRGRAdlQAALDA 4197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 786 FLRKKVKEPYVKENSPLVRVMSFSRSEQEHFLLVVIHHLIFDGVSSVTFIHSLFDTYqlllKGQQPeiAVSPAIYHDFAA 865
Cdd:PRK12316 4198 LAAAERERGFDLQRAPLLRLVLVRTAEGRHHLIYTNHHILMDGWSNSQLLGEVLERY----SGRPP--AQPGGRYRDYIA 4271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 866 WeknmLAGKDGVKHRTYWQKQLSgtlpNLQLPKVSASSVSEFREDT------YTRRLSSGFMNQVRMFAKEHSVNVTTVF 939
Cdd:PRK12316 4272 W----LQRQDAAASEAFWREQLA----ALDEPTRLAQAIARADLRSangygeHVRELDATATARLREFARTQRVTLNTLV 4343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 940 LSCYMMLLGRYTGQKEQIVGMPAMVRPEER--FDDAIGHFLNMLPIRSELNPADTFSSFISKLQLTILDGLDHAAYPFPK 1017
Cdd:PRK12316 4344 QAAWLLLLQRYTGQDTVAFGATVAGRPAELpgIEGQIGLFINTLPVIATPRAQQSVVEWLQQVQRQNLALREHEHTPLYE 4423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1018 MVRDlnipRSQAGSPVFQTAFFYQNF-----LQSGSYQSLlsRYADFFSvdyveyiHQEGEYELVFELwETEEKMELNIK 1092
Cdd:PRK12316 4424 IQRW----AGQGGEALFDSLLVFENYpvseaLQQGAPGGL--RFGEVTN-------HEQTNYPLTLAV-GLGETLSLQFS 4489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1093 YNTGLFDAASISAMFDHFVYVTEQAMLNPSQPLKEYSLLPEAEKQMILKTWNATGKTYPY-ITFHELFEQQAKKTPDRAA 1171
Cdd:PRK12316 4490 YDRGHFDAATIERLARHLTNLLEAMAEDPQRRLGELQLLEKAEQQRIVALWNRTDAGYPAtRCVHQLVAERARMTPDAVA 4569
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1172 VSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLEDSEV 1251
Cdd:PRK12316 4570 VVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGA 4649
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1252 FITLTTSELVNTL-SWNGVTTALLDQ--DWDEIAQTASDRKvltrtVTPENLAYVIYTSGSTGKPKGVMIPHKALTNFLV 1328
Cdd:PRK12316 4650 ALLLTQSHLLQRLpIPDGLASLALDRdeDWEGFPAHDPAVR-----LHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLH 4724
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1329 SMGETPGLTAEDKMLAVTTYCFDIAALELFLPLIKGAHCYICQTEHTkDVEKLKRDIRTIKPTVMQATPATWKMLFySGW 1408
Cdd:PRK12316 4725 ATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVIRDDSLW-DPERLYAEIHEHRVTVLVFPPVYLQQLA-EHA 4802
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1409 ENEENV----KILCGGEALPETLKRYFLDTGSEA--WNMFGPTETTIWSAVQRI--NDECSRAT--IGRPIANTQIYITD 1478
Cdd:PRK12316 4803 ERDGEPpslrVYCFGGEAVAQASYDLAWRALKPVylFNGYGPTETTVTVLLWKArdGDACGAAYmpIGTPLGNRSGYVLD 4882
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1479 SQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPF-EPGSKLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRI 1557
Cdd:PRK12316 4883 GQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgAPGGRLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRI 4962
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1558 ELGDIESRLSEHPGILECVVVAD----MDNLAAYY---TAKHANASLTARELRHFVKNAL----PAYMVPSYFIQLDHMP 1626
Cdd:PRK12316 4963 ELGEIEARLREHPAVREAVVIAQegavGKQLVGYVvpqDPALADADEAQAELRDELKAALrerlPEYMVPAHLVFLARMP 5042
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1627 LTPNGKIDRNSLKNIDLSgeQLKQRQTSPKN-IQDTVFTIWQEVLKTSDIEWDDGFFDVGGDSLLAVTVADRIKHELSCE 1705
Cdd:PRK12316 5043 LTPNGKLDRKALPQPDAS--LLQQAYVAPRSeLEQQVAAIWAEVLQLERVGLDDNFFELGGHSLLAIQVTSRIQLELGLE 5120
|
1130 1140 1150
....*....|....*....|....*....|.
gi 1776025254 1706 FSVTDLFEYSTIKNISQYITEQRMGNASDHM 1736
Cdd:PRK12316 5121 LPLRELFQTPTLAAFVELAAAAGSGDDEKFD 5151
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
3339-3776 |
0e+00 |
|
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different products, called polyketides, by successive decarboxylating Claisen condensations. PKSs can be divided into 2 groups, modular type I PKSs consisting of one or more large multifunctional proteins and iterative type II PKSs, complexes of several monofunctional subunits.
Pssm-ID: 238429 [Multi-domain] Cd Length: 421 Bit Score: 663.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3339 EPVAIVGISGRFPGAMDIDEFWKNLEEGKDSITEVPKDRWDWREHYGNPDTDvNKTDIKWGGFIDGVAEFDPLFFGISPR 3418
Cdd:cd00833 1 EPIAIVGMACRFPGAADPDEFWENLLEGRDAISEIPEDRWDADGYYPDPGKP-GKTYTRRGGFLDDVDAFDAAFFGISPR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3419 EADYVDPQQRLLMTYVWKALEDAGCPPQSLSGTGTGIFIGTGNTGYKDLFHRANLPIEGHAATGHMIpSVGPNRMSYFLN 3498
Cdd:cd00833 80 EAEAMDPQQRLLLEVAWEALEDAGYSPESLAGSRTGVFVGASSSDYLELLARDPDEIDAYAATGTSR-AFLANRISYFFD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3499 IHGPSEPVETACSSSLVAIHRAVTAMQNGDCEMAIAGGVNTILTEEAHISYSKAGMLSKDGRCKTFSADANGYVRGEGVG 3578
Cdd:cd00833 159 LRGPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLSPDGRCRPFDADADGYVRGEGVG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3579 MVMLKKLEDAERDGNHIYGVIRGTAENHGGRANTLTSPNPKAQADLLVRAYRQAGIDPSTVTYIEAHGTGTELGDPIEIN 3658
Cdd:cd00833 239 VVVLKRLSDALRDGDRIYAVIRGSAVNQDGRTKGITAPSGEAQAALIRRAYARAGVDPSDIDYVEAHGTGTPLGDPIEVE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3659 GLKAAFkelsnmrgeSQPDVPDHRCGIGSVKSNIGHLELAAGISGLIKVLLQMKHKTLVKSLHCETLNPYLQLTDSPFYI 3738
Cdd:cd00833 319 ALAKVF---------GGSRSADQPLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKIDFEESPLRV 389
|
410 420 430
....*....|....*....|....*....|....*...
gi 1776025254 3739 VQEKQEWKSvtdcdgNELPRRAGISSFGIGGVNAHIVI 3776
Cdd:cd00833 390 PTEARPWPA------PAGPRRAGVSSFGFGGTNAHVIL 421
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
160-1725 |
0e+00 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 658.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 160 GLEGFRAIIVEDLLSAEADTdWHQSSP------EDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFN 233
Cdd:PRK05691 1241 RLPQAEGVSAIALDSLHLDS-WPSQAPglhlhgDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQ 1319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 234 WMP--FDhvggigmLHLRDVYL----GCQEInVSSETILMEPLKWLDWIDHYRASVTwapNFAFGLVTDFAEEikDRKWD 307
Cdd:PRK05691 1320 KAPisFD-------VSVWECFWplitGCRLV-LAGPGEHRDPQRIAELVQQYGVTTL---HFVPPLLQLFIDE--PLAAA 1386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 308 LSSMRYMLNGGEAMVAKVGRRILELLephglPADAIRPAWGMSETSSGVifSHEFTRAgtsDDDHFVEIGSPIPGFSMRI 387
Cdd:PRK05691 1387 CTSLRRLFSGGEALPAELRNRVLQRL-----PQVQLHNRYGPTETAINV--THWQCQA---EDGERSPIGRPLGNVLCRV 1456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 388 VNDHNELVEEGEIGRFQVSGLSVTSGYYQRPDLNESVFT-----EDG--WFETGDLG-FLRNGRLTITGRTKDAIIINGI 459
Cdd:PRK05691 1457 LDAELNLLPPGVAGELCIGGAGLARGYLGRPALTAERFVpdplgEDGarLYRTGDRArWNADGALEYLGRLDQQVKLRGF 1536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 460 NYYSHAIESAVEELSEIETsytAACAVRLGQNSTdQLaIFFVTSAKLNDEQMSQLLRNIQSHVsqvigvtPEYLLPVQ-- 537
Cdd:PRK05691 1537 RVEPEEIQARLLAQPGVAQ---AAVLVREGAAGA-QL-VGYYTGEAGQEAEAERLKAALAAEL-------PEYMVPAQli 1604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 538 -KEEIPKTAIGKIQRTqlktsfengefdhllhkpnrmndAVQDEEMQQADHVKRvREEIQEHLLTCLTEELHVSRdwVEP 616
Cdd:PRK05691 1605 rLDQMPLGPSGKLDRR-----------------------ALPEPVWQQREHVEP-RTELQQQIAAIWREVLGLPR--VGL 1658
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 617 NANIQSLGVNSIKMMKLIRSIEKNYHIKLTAREIHQYptiERLASYLSEHEDLSSSSADKKGTDTYKTEpeRSQATfqPL 696
Cdd:PRK05691 1659 RDDFFALGGHSLLATQIVSRTRQACDVELPLRALFEA---SELGAFAEQVARIQAAGERNSQGAIARVD--RSQPV--PL 1731
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 697 SEVQKGLWTLQKMSPEKSAYHVPLCFKFSSGLHLETLQQAFGLVLNQHPILKHVIQEKDGVPILKNEPALSIEIKTENIS 776
Cdd:PRK05691 1732 SYSQQRMWFLWQMEPDSPAYNVGGMARLSGVLDVDRFEAALQALILRHETLRTTFPSVDGVPVQQVAEDSGLRMDWQDFS 1811
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 777 SM----KESDIPAFLRKKVKEPYVKENSPLVRVMSFSRSEQEHFLLVVIHHLIFDGVSSVTFIHSLFDTYQLLLKGQQPE 852
Cdd:PRK05691 1812 ALpadaRQQRLQQLADSEAHQPFDLERGPLLRACLVKAAEREHYFVLTLHHIVTEGWAMDIFARELGALYEAFLDDRESP 1891
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 853 IAVSPAIYHDFAAWEKNMLAGKDGVKHRTYWQKQLSGTLPNLQLP-KVSASSVSEFREDTYTRRLSSGFMNQVRMFAKEH 931
Cdd:PRK05691 1892 LEPLPVQYLDYSVWQRQWLESGERQRQLDYWKAQLGNEHPLLELPaDRPRPPVQSHRGELYRFDLSPELAARVRAFNAQR 1971
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 932 SVNVTTVFLSCYMMLLGRYTGQKEQIVGMPAM--VRPEErfDDAIGHFLNMLPIRSELNPADTFSSFISKLQLTILDGLD 1009
Cdd:PRK05691 1972 GLTLFMTMTATLAALLYRYSGQRDLRIGAPVAnrIRPES--EGLIGAFLNTQVLRCQLDGQMSVSELLEQVRQTVIEGQS 2049
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1010 HAAYPFPKMVRDLNIPRSQAGSPVFQTAFFYQNFlqsgSYQSllSRYADFFSVDYVEYIHQEGEYELVFELWETEEKMEL 1089
Cdd:PRK05691 2050 HQDLPFDHLVEALQPPRSAAYNPLFQVMCNVQRW----EFQQ--SRQLAGMTVEYLVNDARATKFDLNLEVTDLDGRLGC 2123
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1090 NIKYNTGLFDAASISAMFDHFVYVTEQAMLNPSQPLKEYSLLPEAEKQMILKTWNAT-GKTYPYITFHELFEQQAKKTPD 1168
Cdd:PRK05691 2124 CLTYSRDLFDEPRIARMAEHWQNLLEALLGDPQQRLAELPLLAAAEQQQLLDSLAGEaGEARLDQTLHGLFAAQAARTPQ 2203
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1169 RAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLED 1248
Cdd:PRK05691 2204 APALTFAGQTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIED 2283
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1249 SEVFITLTTSELVNTLSW--NGVTTALLDQDWDEIAQTASDRkvLTRTVTPENLAYVIYTSGSTGKPKGVMIPHKALTNF 1326
Cdd:PRK05691 2284 SGIGLLLSDRALFEALGElpAGVARWCLEDDAAALAAYSDAP--LPFLSLPQHQAYLIYTSGSTGKPKGVVVSHGEIAMH 2361
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1327 LVSMGETPGLTAEDKMLAVTTYCFDIAALELFLPLIKGAHCyICQTEHTKDVEKLKRDIRTIKPTVMQATPATWKMLF-Y 1405
Cdd:PRK05691 2362 CQAVIERFGMRADDCELHFYSINFDAASERLLVPLLCGARV-VLRAQGQWGAEEICQLIREQQVSILGFTPSYGSQLAqW 2440
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1406 SGWENEENVKILC--GGEAL-PETLKRYFLDTGSEA-WNMFGPTETTIWS----AVQRINDECSRATIGRPIANTQIYIT 1477
Cdd:PRK05691 2441 LAGQGEQLPVRMCitGGEALtGEHLQRIRQAFAPQLfFNAYGPTETVVMPlaclAPEQLEEGAASVPIGRVVGARVAYIL 2520
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1478 DSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPFEP-GSKLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFR 1556
Cdd:PRK05691 2521 DADLALVPQGATGELYVGGAGLAQGYHDRPGLTAERFVADPFAAdGGRLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFR 2600
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1557 IELGDIESRLSEHPGILECVVVAdMDN-----LAAYYTAKHANASLTA----RE-LRHFVKNALPAYMVPSYFIQLDHMP 1626
Cdd:PRK05691 2601 IELGEIESRLLEHPAVREAVVLA-LDTpsgkqLAGYLVSAVAGQDDEAqaalREaLKAHLKQQLPDYMVPAHLILLDSLP 2679
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1627 LTPNGKIDRNSLKNIDLsgEQLKQRQTSPKN-IQDTVFTIWQEVLKTSDIEWDDGFFDVGGDSLLAVTVADRIKhELSCE 1705
Cdd:PRK05691 2680 LTANGKLDRRALPAPDP--ELNRQAYQAPRSeLEQQLAQIWREVLNVERVGLGDNFFELGGDSILSIQVVSRAR-QLGIH 2756
|
1610 1620
....*....|....*....|
gi 1776025254 1706 FSVTDLFEYSTIKNISQYIT 1725
Cdd:PRK05691 2757 FSPRDLFQHQTVQTLAAVAT 2776
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
1759-2291 |
0e+00 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 644.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1759 DDSVAIIGISCEFPGAKNHDEFWENLRDGKESIAFFNKEEL--QRFGISKEIAENADYVPAKASIEGKDRFDPSFFQISP 1836
Cdd:COG3321 3 DEPIAIIGMACRFPGADDPEEFWRNLRAGRDAITEVPADRWdaDAYYDPDPDAPGKTYVRWGGFLDDVDEFDALFFGISP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1837 KDAEFMDPQLRMLLTHSWKAIEDAGYAAGQIP--QTSVFMSASNNSYRALLPSDttesLETPDGYVSWVLAQSgTIPTMI 1914
Cdd:COG3321 83 REAEAMDPQQRLLLEVAWEALEDAGYDPESLAgsRTGVFVGASSNDYALLLLAD----PEAIDAYALTGNAKS-VLAGRI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1915 SHKLGLRGPSYFVHANCSSSLIGLHSAYKSLLSAESDYALVGGATLHTESNIGYVHQPGLNFSSDGHIKAFDASADGMIG 1994
Cdd:COG3321 158 SYKLDLRGPSVTVDTACSSSLVAVHLACQSLRSGECDLALAGGVNLMLTPESFILFSKGGMLSPDGRCRAFDADADGYVR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1995 GEGVAVVLLKKAADAVKDGDHIYALLRGIGVNNDGADKvGFYAPSVKGQADVVQQVMNQTKIHPESICYVEAHGTGTKLG 2074
Cdd:COG3321 238 GEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRSN-GLTAPNGPAQAAVIRRALADAGVDPATVDYVEAHGTGTPLG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2075 DPIELAALTNVYRQYTNKTQFCGIGSVKTNIGHLDTAAGLAGCIKVVMSLYHQELAPSINYKEPNPNTDLASSPFYVVDQ 2154
Cdd:COG3321 317 DPIEAAALTAAFGQGRPADQPCAIGSVKSNIGHLEAAAGVAGLIKAVLALRHGVLPPTLHFETPNPHIDFENSPFYVNTE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2155 KKTLSREIQTHRAALSSFGLGGTNTHAIFEQF--KRDSDKGKIDGTCIVPISAKNKERLQEYAEDILAYLERRGLENsqL 2232
Cdd:COG3321 397 LRPWPAGGGPRRAGVSSFGFGGTNAHVVLEEApaAAPAAAAAARPPQLLVLSAKTEEALRALAARLAAFLEAHPDLD--L 474
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1776025254 2233 PDFAYTLQVGREAMEHRVVFIADHVNELKQRLTDFINGKTAiEGCFQGSKHNAREVSWL 2291
Cdd:COG3321 475 ADVAYTLATGRAHFEHRLAVVASSREELAAKLRALAAGEAA-PGVVTGAAAAAPKVAFL 532
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
1167-1638 |
0e+00 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341253 [Multi-domain] Cd Length: 444 Bit Score: 599.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1167 PDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYML 1246
Cdd:cd05930 1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1247 EDSEVFITLTTselvntlswngvttalldqdwdeiaqtasdrkvltrtvtPENLAYVIYTSGSTGKPKGVMIPHKALTNF 1326
Cdd:cd05930 81 EDSGAKLVLTD---------------------------------------PDDLAYVIYTSGSTGKPKGVMVEHRGLVNL 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1327 LVSMGETPGLTAEDKMLAVTTYCFDIAALELFLPLIKGAHCYICQTEHTKDVEKLKRDIRTIKPTVMQATPATWKMLF-Y 1405
Cdd:cd05930 122 LLWMQEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLRLLLqE 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1406 SGWENEENVKIL-CGGEALPETLKRYFLDTGSEA--WNMFGPTETTIWSAVQRINDEC---SRATIGRPIANTQIYITDS 1479
Cdd:cd05930 202 LELAALPSLRLVlVGGEALPPDLVRRWRELLPGArlVNLYGPTEATVDATYYRVPPDDeedGRVPIGRPIPNTRVYVLDE 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1480 QLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPFEPGSKLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIEL 1559
Cdd:cd05930 282 NLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIEL 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1560 GDIESRLSEHPGILECVVVADMDN-----LAAYYTAKHANAsLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKID 1634
Cdd:cd05930 362 GEIEAALLAHPGVREAAVVAREDGdgekrLVAYVVPDEGGE-LDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVD 440
|
....
gi 1776025254 1635 RNSL 1638
Cdd:cd05930 441 RKAL 444
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
1157-1638 |
1.27e-178 |
|
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341310 [Multi-domain] Cd Length: 490 Bit Score: 559.25 E-value: 1.27e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1157 ELFEQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPS 1236
Cdd:cd17655 1 ELFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1237 YPAERLEYMLEDSEVFITLTTSELVNTLSWNGVTTALLDQDWDEiaQTASDrkvLTRTVTPENLAYVIYTSGSTGKPKGV 1316
Cdd:cd17655 81 YPEERIQYILEDSGADILLTQSHLQPPIAFIGLIDLLDEDTIYH--EESEN---LEPVSKSDDLAYVIYTSGSTGKPKGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1317 MIPHKALTNFLVSMGETPGLTAEDKMLAVTTYCFDIAALELFLPLIKGAHCYICQTEHTKDVEKLKRDIRTIKPTVMQAT 1396
Cdd:cd17655 156 MIEHRGVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQALTQYIRQNRITIIDLT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1397 PATWKMLFYSGWENEENVK-ILCGGEALPETLKRYFLD---TGSEAWNMFGPTETTIWSAVQRINDECSRAT---IGRPI 1469
Cdd:cd17655 236 PAHLKLLDAADDSEGLSLKhLIVGGEALSTELAKKIIElfgTNPTITNAYGPTETTVDASIYQYEPETDQQVsvpIGKPL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1470 ANTQIYITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPFEPGSKLYRTGDMARWLPGGRIEYIGRIDNQ 1549
Cdd:cd17655 316 GNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVPGERMYRTGDLARWLPDGNIEFLGRIDHQ 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1550 VKIRGFRIELGDIESRLSEHPGILECVVVA--DMDN---LAAYYTakhANASLTARELRHFVKNALPAYMVPSYFIQLDH 1624
Cdd:cd17655 396 VKIRGYRIELGEIEARLLQHPDIKEAVVIArkDEQGqnyLCAYIV---SEKELPVAQLREFLARELPDYMIPSYFIKLDE 472
|
490
....*....|....
gi 1776025254 1625 MPLTPNGKIDRNSL 1638
Cdd:cd17655 473 IPLTPNGKVDRKAL 486
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
1157-1638 |
5.54e-178 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.
Pssm-ID: 341282 [Multi-domain] Cd Length: 483 Bit Score: 557.20 E-value: 5.54e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1157 ELFEQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPS 1236
Cdd:cd12117 1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1237 YPAERLEYMLEDSEVFITLTTSELVNTLSwNGVTTALLDQDWDeiaqtASDRKVLTRTVTPENLAYVIYTSGSTGKPKGV 1316
Cdd:cd12117 81 LPAERLAFMLADAGAKVLLTDRSLAGRAG-GLEVAVVIDEALD-----AGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1317 MIPHKALTNfLVSMGETPGLTAEDKMLAVTTYCFDIAALELFLPLIKGAHCYICQTEHTKDVEKLKRDIRTIKPTVMQAT 1396
Cdd:cd12117 155 AVTHRGVVR-LVKNTNYVTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPDALGALIAEEGVTVLWLT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1397 PATWKMLFysgwenEENV-------KILCGGEALPETLKRYFLDT--GSEAWNMFGPTETTIWSAVQRINDECSRAT--- 1464
Cdd:cd12117 234 AALFNQLA------DEDPecfaglrELLTGGEVVSPPHVRRVLAAcpGLRLVNGYGPTENTTFTTSHVVTELDEVAGsip 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1465 IGRPIANTQIYITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPFEPGSKLYRTGDMARWLPGGRIEYIG 1544
Cdd:cd12117 308 IGRPIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFGPGERLYRTGDLARWLPDGRLEFLG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1545 RIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMDN-----LAAYYTAKHAnasLTARELRHFVKNALPAYMVPSYF 1619
Cdd:cd12117 388 RIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAggdkrLVAYVVAEGA---LDAAELRAFLRERLPAYMVPAAF 464
|
490
....*....|....*....
gi 1776025254 1620 IQLDHMPLTPNGKIDRNSL 1638
Cdd:cd12117 465 VVLDELPLTANGKVDRRAL 483
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
1760-2182 |
1.36e-171 |
|
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different products, called polyketides, by successive decarboxylating Claisen condensations. PKSs can be divided into 2 groups, modular type I PKSs consisting of one or more large multifunctional proteins and iterative type II PKSs, complexes of several monofunctional subunits.
Pssm-ID: 238429 [Multi-domain] Cd Length: 421 Bit Score: 535.99 E-value: 1.36e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1760 DSVAIIGISCEFPGAKNHDEFWENLRDGKESIAFFNKEELQRFGI-SKEIAENADYVPAKASIEGKDRFDPSFFQISPKD 1838
Cdd:cd00833 1 EPIAIVGMACRFPGAADPDEFWENLLEGRDAISEIPEDRWDADGYyPDPGKPGKTYTRRGGFLDDVDAFDAAFFGISPRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1839 AEFMDPQLRMLLTHSWKAIEDAGYAAGQIP--QTSVFMSASNNSYRALLPSDttesLETPDGYVSWVLAQSgTIPTMISH 1916
Cdd:cd00833 81 AEAMDPQQRLLLEVAWEALEDAGYSPESLAgsRTGVFVGASSSDYLELLARD----PDEIDAYAATGTSRA-FLANRISY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1917 KLGLRGPSYFVHANCSSSLIGLHSAYKSLLSAESDYALVGGATLHTESNIGYVHQPGLNFSSDGHIKAFDASADGMIGGE 1996
Cdd:cd00833 156 FFDLRGPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLSPDGRCRPFDADADGYVRGE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1997 GVAVVLLKKAADAVKDGDHIYALLRGIGVNNDGADKVGfYAPSVKGQADVVQQVMNQTKIHPESICYVEAHGTGTKLGDP 2076
Cdd:cd00833 236 GVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRTKGI-TAPSGEAQAALIRRAYARAGVDPSDIDYVEAHGTGTPLGDP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2077 IELAALTNVYRQYTNKTQFCGIGSVKTNIGHLDTAAGLAGCIKVVMSLYHQELAPSINYKEPNPNTDLASSPFYVVDQKK 2156
Cdd:cd00833 315 IEVEALAKVFGGSRSADQPLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKIDFEESPLRVPTEAR 394
|
410 420
....*....|....*....|....*.
gi 1776025254 2157 TLSREIQTHRAALSSFGLGGTNTHAI 2182
Cdd:cd00833 395 PWPAPAGPRRAGVSSFGFGGTNAHVI 420
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
695-1739 |
1.53e-171 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 601.18 E-value: 1.53e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 695 PLSEVQKGLWTLQKMSPEKSAY----HVPLCfkfssGLHLETLQQAFGLVLNQHPILKHVIQEKDGVP----ILKNEPAL 766
Cdd:PRK12316 1558 PLSPMQQGMLFHSLYEQEAGDYinqlRVDVQ-----GLDPDRFRAAWQATVDRHEILRSGFLWQDGLEqplqVIHKQVEL 1632
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 767 SIEIKTENISSMKESDIPAFLRKKVKEPYVKENSPLVRVMSFSRSEQEHFLLVVIHHLIFDGVSSVTFIHSLFDTYqlll 846
Cdd:PRK12316 1633 PFAELDWRGREDLGQALDALAQAERQKGFDLTRAPLLRLVLVRTGEGRHHLIYTNHHILMDGWSNAQLLGEVLQRY---- 1708
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 847 KGQQPEIAVSPaiYHDFAAWeknmLAGKDGVKHRTYWQKQLSGTLPNLQLPKVSASSVSEFREDTYTRRLSSGFMNQVRM 926
Cdd:PRK12316 1709 AGQPVAAPGGR--YRDYIAW----LQRQDAAASEAFWKEQLAALEEPTRLAQAARTEDGQVGYGDHQQLLDPAQTRALAE 1782
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 927 FAKEHSVNVTTVFLSCYMMLLGRYTGQKEQIVGMPAMVRPEER--FDDAIGHFLNMLPIRSELNPADTFSSFISKLQLTI 1004
Cdd:PRK12316 1783 FARAQKVTLNTLVQAAWLLLLQRYTGQETVAFGATVAGRPAELpgIEQQIGLFINTLPVIAAPRPDQSVADWLQEVQALN 1862
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1005 LDGLDHAAYPFpkmvrdLNIPR--SQAGSPVFQTAFFYQNF-----LQSGSYQSL-LSRYADffsvdyveyiHQEGEYEL 1076
Cdd:PRK12316 1863 LALREHEHTPL------YDIQRwaGQGGEALFDSLLVFENYpvaeaLKQGAPAGLvFGRVSN----------HEQTNYPL 1926
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1077 VFELwETEEKMELNIKYNTGLFDAASISAMFDHFVYVTEQAMLNPSQPLKEYSLLPEAEKQMILKTWNATGKTYPY-ITF 1155
Cdd:PRK12316 1927 TLAV-TLGETLSLQYSYDRGHFDAAAIERLDRHLLHLLEQMAEDAQAALGELALLDAGERQRILADWDRTPEAYPRgPGV 2005
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1156 HELFEQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDP 1235
Cdd:PRK12316 2006 HQRIAEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDP 2085
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1236 SYPAERLEYMLEDSEVFITLTTSELVNTLSW-NGVTTALLDQ--DWDEIAQTASDRKvltrtVTPENLAYVIYTSGSTGK 1312
Cdd:PRK12316 2086 NYPAERLAYMLEDSGAALLLTQRHLLERLPLpAGVARLPLDRdaEWADYPDTAPAVQ-----LAGENLAYVIYTSGSTGL 2160
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1313 PKGVMIPHKALTNFLVSMGETPGLTAEDKMLAVTTYCFDIAALELFLPLIKGAHCYICQTEHtKDVEKLKRDIRTIKPTV 1392
Cdd:PRK12316 2161 PKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAHEQWFHPLLNGARVLIRDDEL-WDPEQLYDEMERHGVTI 2239
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1393 MQATPATWKMLFysgwENEE------NVKILC-GGEALP-ETLKRYFLDTGSEAW-NMFGPTETTI----WSAvqRINDE 1459
Cdd:PRK12316 2240 LDFPPVYLQQLA----EHAErdgrppAVRVYCfGGEAVPaASLRLAWEALRPVYLfNGYGPTEAVVtpllWKC--RPQDP 2313
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1460 CSRAT--IGRPIANTQIYITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPFE-PGSKLYRTGDMARWLP 1536
Cdd:PRK12316 2314 CGAAYvpIGRALGNRRAYILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFSaSGERLYRTGDLARYRA 2393
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1537 GGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADM----DNLAAYYTAKHAnASLTARELRHFVKNALPA 1612
Cdd:PRK12316 2394 DGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQDgasgKQLVAYVVPDDA-AEDLLAELRAWLAARLPA 2472
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1613 YMVPSYFIQLDHMPLTPNGKIDRNSLKNIDLSgeQLKQRQTSPKN-IQDTVFTIWQEVLKTSDIEWDDGFFDVGGDSLLA 1691
Cdd:PRK12316 2473 YMVPAHWVVLERLPLNPNGKLDRKALPKPDVS--QLRQAYVAPQEgLEQRLAAIWQAVLKVEQVGLDDHFFELGGHSLLA 2550
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|....*...
gi 1776025254 1692 VTVADRIKHELSCEFSVTDLFEYSTIKNISQYITEQRMGNASDHMPTD 1739
Cdd:PRK12316 2551 TQVVSRVRQDLGLEVPLRILFERPTLAAFAASLESGQTSRAPVLQKVT 2598
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
727-1724 |
2.66e-170 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 596.37 E-value: 2.66e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 727 GLHLETLQQAFGLVLNQHPILK-------------HVIQEKDGVPIL----KNEPALSIEIKTENISSMKESdipaflrk 789
Cdd:PRK12467 2679 GLDVERFRTAWQAVIDRHEILRsgflwdgeleeplQVVYKQARLPFSrldwRDRADLEQALDALAAADRQQG-------- 2750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 790 kvkepYVKENSPLVRVMSFSRSEQEHFLLVVIHHLIFDGVSSVTFIHSLFDTYqlllKGQQPeiAVSPAIYHDFAAWekn 869
Cdd:PRK12467 2751 -----FDLLSAPLLRLTLVRTGEDRHHLIYTNHHILMDGWSGSQLLGEVLQRY----FGQPP--PAREGRYRDYIAW--- 2816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 870 mLAGKDGVKHRTYWQKQLSgtlpNLQLPKVSASSVS-------EFREDTYtRRLSSGFMNQVRMFAKEHSVNVTTVFLSC 942
Cdd:PRK12467 2817 -LQAQDAEASEAFWKEQLA----ALEEPTRLARALYpapaeavAGHGAHY-LHLDATQTRQLIEFARRHRVTLNTLVQGA 2890
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 943 YMMLLGRYTGQKEQIVGMPAMVRPEER--FDDAIGHFLNMLPIRSELNPADTFSSFISKLQLTILDGLDHAAYPFpkmvr 1020
Cdd:PRK12467 2891 WLLLLQRFTGQDTVCFGATVAGRPAQLrgAEQQLGLFINTLPVIASPRAEQTVSDWLQQVQAQNLALREFEHTPL----- 2965
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1021 dLNIPR--SQAGSPVFQTAFFYQNF-----LQSGSYQSLlsRYADFFSVDYVEYihqegEYELVFELWETeekMELNIKY 1093
Cdd:PRK12467 2966 -ADIQRwaGQGGEALFDSILVFENYpiseaLKQGAPSGL--RFGAVSSREQTNY-----PLTLAVGLGDT---LELEFSY 3034
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1094 NTGLFDAASISAMFDHFVYVTEQAMLNPSQPLKEYSLLPEAEKQMILKTWNATGKTYP-YITFHELFEQQAKKTPDRAAV 1172
Cdd:PRK12467 3035 DRQHFDAAAIERLAESFDRLLQAMLNNPAARLGELPTLAAHERRQVLHAWNATAAAYPsERLVHQLIEAQVARTPEAPAL 3114
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1173 SYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLEDSEVF 1252
Cdd:PRK12467 3115 VFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVK 3194
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1253 ITLTTSELVNTLSW-NGVTTALLDQD--WDEiaqtaSDRKVLTRtVTPENLAYVIYTSGSTGKPKGVMIPHKALTNFLVS 1329
Cdd:PRK12467 3195 LLLTQAHLLEQLPApAGDTALTLDRLdlNGY-----SENNPSTR-VMGENLAYVIYTSGSTGKPKGVGVRHGALANHLCW 3268
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1330 MGETPGLTAEDKMLAVTTYCFDIAALELFLPLIKGAhCYICQTEHTKDVEKLKRDIRTIKPTVMQATPATWKML--FYSG 1407
Cdd:PRK12467 3269 IAEAYELDANDRVLLFMSFSFDGAQERFLWTLICGG-CLVVRDNDLWDPEELWQAIHAHRISIACFPPAYLQQFaeDAGG 3347
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1408 WENEENVKILCGGEALP----ETLKRYFLDTGseAWNMFGPTETTI----WSAVQRINDECSRATIGRPIANTQIYITDS 1479
Cdd:PRK12467 3348 ADCASLDIYVFGGEAVPpaafEQVKRKLKPRG--LTNGYGPTEAVVtvtlWKCGGDAVCEAPYAPIGRPVAGRSIYVLDG 3425
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1480 QLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPFE-PGSKLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIE 1558
Cdd:PRK12467 3426 QLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVADPFSgSGGRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIE 3505
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1559 LGDIESRLSEHPGILECVVVA-DMDN---LAAYYTAKHANASLtARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKID 1634
Cdd:PRK12467 3506 LGEIEARLLQHPSVREAVVLArDGAGgkqLVAYVVPADPQGDW-RETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVD 3584
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1635 RNSLKNIDLsgeQLKQRQTSPKN-IQDTVFTIWQEVLKTSDIEWDDGFFDVGGDSLLAVTVADRIKHELSCEFSVTDLFE 1713
Cdd:PRK12467 3585 RKALPDPDA---KGSREYVAPRSeVEQQLAAIWADVLGVEQVGVTDNFFELGGDSLLALQVLSRIRQSLGLKLSLRDLMS 3661
|
1050
....*....|.
gi 1776025254 1714 YSTIKNISQYI 1724
Cdd:PRK12467 3662 APTIAELAGYS 3672
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
1156-1638 |
2.72e-169 |
|
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341301 [Multi-domain] Cd Length: 488 Bit Score: 532.24 E-value: 2.72e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1156 HELFEQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDP 1235
Cdd:cd17646 1 HALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1236 SYPAERLEYMLEDSEVFITLTTSELVNTLSwnGVTTALLDQDWDEIAQTASDRKVLTRtvtPENLAYVIYTSGSTGKPKG 1315
Cdd:cd17646 81 GYPADRLAYMLADAGPAVVLTTADLAARLP--AGGDVALLGDEALAAPPATPPLVPPR---PDNLAYVIYTSGSTGRPKG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1316 VMIPHKALTNFLVSMGETPGLTAEDKMLAVTTYCFDIAALELFLPLIKGAHCYICQTEHTKDVEKLKRDIRTIKPTVMQA 1395
Cdd:cd17646 156 VMVTHAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDPAYLAALIREHGVTTCHF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1396 TPAtwkML--FY-----SGWENEENVkiLCGGEALP-ETLKRYFLDTGSEAWNMFGPTETTI----WSAvqRINDECSRA 1463
Cdd:cd17646 236 VPS---MLrvFLaepaaGSCASLRRV--FCSGEALPpELAARFLALPGAELHNLYGPTEAAIdvthWPV--RGPAETPSV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1464 TIGRPIANTQIYITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPFEPGSKLYRTGDMARWLPGGRIEYI 1543
Cdd:cd17646 309 PIGRPVPNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFGPGSRMYRTGDLARWRPDGALEFL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1544 GRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMDN-----LAAYYTAKHANASLTARELRHFVKNALPAYMVPSY 1618
Cdd:cd17646 389 GRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPagaarLVGYVVPAAGAAGPDTAALRAHLAERLPEYMVPAA 468
|
490 500
....*....|....*....|
gi 1776025254 1619 FIQLDHMPLTPNGKIDRNSL 1638
Cdd:cd17646 469 FVVLDALPLTANGKLDRAAL 488
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
695-1727 |
1.29e-165 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 551.57 E-value: 1.29e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 695 PLSEVQKGLWTLQKMSPEKSAYHVPLCFKFSSGLHLETLQQAFGLVLNQHPILKHVIQEKDGVPILKNEPALSIEikTEN 774
Cdd:PRK10252 9 PLVAAQPGIWMAEKLSPLPSAWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFTEDNGEVWQWVDPALTFP--LPE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 775 ISSMKESDIP-----AFLRKKVKEPY-VKENSPLVRVMSFSRSEQEHFLLVVIHHLIFDGVSSVTFIHSLFDTYQLLLKG 848
Cdd:PRK10252 87 IIDLRTQPDPhaaaqALMQADLQQDLrVDSGKPLVFHQLIQLGDNRWYWYQRYHHLLVDGFSFPAITRRIAAIYCAWLRG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 849 QQ-PEIAVSP--AIYHDFAAWEKNMLAGKDGvkhrTYWQKQLSGTLPNLQL---PKVSASSVSEFREDTytRRLSSGFMn 922
Cdd:PRK10252 167 EPtPASPFTPfaDVVEEYQRYRASEAWQRDA----AFWAEQRRQLPPPASLspaPLPGRSASADILRLK--LEFTDGAF- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 923 qVRMFAKEHSVNVTTVFLSCYMMLLGRYTGQKEQIVGMPAMVRPEERFDDAIGHFLNMLPIRSELNPADTFSSFISKLQL 1002
Cdd:PRK10252 240 -RQLAAQASGVQRPDLALALVALWLGRLCGRMDYAAGFIFMRRLGSAALTATGPVLNVLPLRVHIAAQETLPELATRLAA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1003 TILDGLDHAAYPFPKMVRDLNipRSQAGSPVFQTAFFYQNFlqsgSYQsllsryADFFSVDYVEYIHQEG---EYELVFE 1079
Cdd:PRK10252 319 QLKKMRRHQRYDAEQIVRDSG--RAAGDEPLFGPVLNIKVF----DYQ------LDFPGVQAQTHTLATGpvnDLELALF 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1080 LwETEEKMELNIKYNTGLFDAASISAMFDHFVYVTEQAMLNPSQPLKEYSLLPEAEKQMiLKTWNATGKTYPYITFHELF 1159
Cdd:PRK10252 387 P-DEHGGLSIEILANPQRYDEATLIAHAERLKALIAQFAADPALLCGDVDILLPGEYAQ-LAQVNATAVEIPETTLSALV 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1160 EQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPA 1239
Cdd:PRK10252 465 AQQAAKTPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPD 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1240 ERLEYMLEDSEVFITLTTSELVNTLSWNGVTTALLDQDWdeiaQTASDRKVLTRTvTPENLAYVIYTSGSTGKPKGVMIP 1319
Cdd:PRK10252 545 DRLKMMLEDARPSLLITTADQLPRFADVPDLTSLCYNAP----LAPQGAAPLQLS-QPHHTAYIIFTSGSTGRPKGVMVG 619
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1320 HKALTNFLVSMGETPGLTAEDKMLAVTTYCFDIAALELFLPLIKGAHCYICQTEHTKDVEKLKRDIRTIKPTVMQATPAt 1399
Cdd:PRK10252 620 QTAIVNRLLWMQNHYPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTTHFVPS- 698
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1400 wkML--FYSGWENEENVK-------ILCGGEALPETLKRYFLD-TGSEAWNMFGPTET----TIWSAVQRINDECSRAT- 1464
Cdd:PRK10252 699 --MLaaFVASLTPEGARQscaslrqVFCSGEALPADLCREWQQlTGAPLHNLYGPTEAavdvSWYPAFGEELAAVRGSSv 776
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1465 -IGRPIANTQIYITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPFEPGSKLYRTGDMARWLPGGRIEYI 1543
Cdd:PRK10252 777 pIGYPVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPGERMYRTGDVARWLDDGAVEYL 856
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1544 GRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVA-----------DMDNLAAYYTAkHANASLTARELRHFVKNALPA 1612
Cdd:PRK10252 857 GRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVTHAcvinqaaatggDARQLVGYLVS-QSGLPLDTSALQAQLRERLPP 935
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1613 YMVPSYFIQLDHMPLTPNGKIDRNSLKNIDLSGeQLKQRqtSPKNIQDT-VFTIWQEVLKTSDIEWDDGFFDVGGDSLLA 1691
Cdd:PRK10252 936 HMVPVVLLQLDQLPLSANGKLDRKALPLPELKA-QVPGR--APKTGTETiIAAAFSSLLGCDVVDADADFFALGGHSLLA 1012
|
1050 1060 1070
....*....|....*....|....*....|....*.
gi 1776025254 1692 VTVADRIKHELSCEFSVTDLFEYSTIKNISQYITEQ 1727
Cdd:PRK10252 1013 MKLAAQLSRQFARQVTPGQVMVASTVAKLATLLDAE 1048
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
1154-1638 |
3.94e-159 |
|
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341299 [Multi-domain] Cd Length: 465 Bit Score: 502.35 E-value: 3.94e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1154 TFHELFEQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPL 1233
Cdd:cd17644 1 CIHQLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1234 DPSYPAERLEYMLEDSEVFITLTTselvntlswngvttalldqdwdeiaqtasdrkvltrtvtPENLAYVIYTSGSTGKP 1313
Cdd:cd17644 81 DPNYPQERLTYILEDAQISVLLTQ---------------------------------------PENLAYVIYTSGSTGKP 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1314 KGVMIPHKALTNFLVSMGETPGLTAEDKMLAVTTYCFDIAALELFLPLIKGAHCYICQTEHTKDVEKLKRDIRTIKPTVM 1393
Cdd:cd17644 122 KGVMIEHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEDFVQYIQQWQLTVL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1394 QATPATWKMLFYSGWENEENV-----KILCGGEA-LPETLKRYFLDTGS--EAWNMFGPTETTIWSAVQRINDECSRA-- 1463
Cdd:cd17644 202 SLPPAYWHLLVLELLLSTIDLpsslrLVIVGGEAvQPELVRQWQKNVGNfiQLINVYGPTEATIAATVCRLTQLTERNit 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1464 --TIGRPIANTQIYITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPFE--PGSKLYRTGDMARWLPGGR 1539
Cdd:cd17644 282 svPIGRPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNssESERLYKTGDLARYLPDGN 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1540 IEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMDN-----LAAYYTAkHANASLTARELRHFVKNALPAYM 1614
Cdd:cd17644 362 IEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQpgnkrLVAYIVP-HYEESPSTVELRQFLKAKLPDYM 440
|
490 500
....*....|....*....|....
gi 1776025254 1615 VPSYFIQLDHMPLTPNGKIDRNSL 1638
Cdd:cd17644 441 IPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
3341-3778 |
4.30e-157 |
|
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the thiolase family and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.
Pssm-ID: 214836 [Multi-domain] Cd Length: 298 Bit Score: 488.76 E-value: 4.30e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3341 VAIVGISGRFPGAMDIDEFWKNLEEGkdsitevpkdrwdwrehygnpdtdvnktdikwggfIDGVAEFDPLFFGISPREA 3420
Cdd:smart00825 1 IAIVGMSCRFPGADDPEEFWDLLLAG-----------------------------------LDDVDLFDAAFFGISPREA 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3421 DYVDPQQRLLMTYVWKALEDAGCPPQSLSGTGTGIFIGTGNTGYkdlfhranlpieghaatghmipsvgpnrmsyflnih 3500
Cdd:smart00825 46 EAMDPQQRLLLEVAWEALEDAGIDPESLRGSRTGVFVGVSSSDY------------------------------------ 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3501 gpSEPVETACSSSLVAIHRAVTAMQNGDCEMAIAGGVNTILTEEAHISYSKAGMLSKDGRCKTFSADANGYVRGEGVGMV 3580
Cdd:smart00825 90 --SVTVDTACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLSPDGRCKTFDASADGYVRGEGVGVV 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3581 MLKKLEDAERDGNHIYGVIRGTAENHGGRANTLTSPNPKAQadllvrayrqagidpstvtyieahgtgtelgdpieingl 3660
Cdd:smart00825 168 VLKRLSDALRDGDPILAVIRGSAVNQDGRSNGITAPSGPAQ--------------------------------------- 208
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3661 kaafkelsnmrgesqpdvpdhrCGIGSVKSNIGHLELAAGISGLIKVLLQMKHKTLVKSLHCETLNPYLQLTDSPFYIVQ 3740
Cdd:smart00825 209 ----------------------LLIGSVKSNIGHLEAAAGVAGLIKVVLALKHGVIPPTLHFETPNPHIDLEESPLRVPT 266
|
410 420 430
....*....|....*....|....*....|....*...
gi 1776025254 3741 EKQEWksvtdcDGNELPRRAGISSFGIGGVNAHIVIEE 3778
Cdd:smart00825 267 ELTPW------PPPGRPRRAGVSSFGFGGTNAHVILEE 298
|
|
| Condensation |
pfam00668 |
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ... |
690-1140 |
8.04e-157 |
|
Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.
Pssm-ID: 395541 [Multi-domain] Cd Length: 454 Bit Score: 494.93 E-value: 8.04e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 690 QATFQPLSEVQKGLWTLQKMSPEKSAYHVPLCFKFSSGLHLETLQQAFGLVLNQHPILKHVIQEK-DGVPILKNEPALSI 768
Cdd:pfam00668 1 VQDEYPLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRQeNGEPVQVILEERPF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 769 EIKTENIS----SMKESDIPAFLRKKVKEPYVKENSPLVRVMSFSRSEQEHFLLVVIHHLIFDGVSSVTFIHSLFDTYQL 844
Cdd:pfam00668 81 ELEIIDISdlseSEEEEAIEAFIQRDLQSPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 845 LLKGQQPEIAVSPAiYHDFAAWEKNMLAGKDGVKHRTYWQKQLSGTLPNLQLPKVSASS-VSEFREDTYTRRLSSGFMNQ 923
Cdd:pfam00668 161 LLKGEPLPLPPKTP-YKDYAEWLQQYLQSEDYQKDAAYWLEQLEGELPVLQLPKDYARPaDRSFKGDRLSFTLDEDTEEL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 924 VRMFAKEHSVNVTTVFLSCYMMLLGRYTGQKEQIVGMPAMVRPEERFDDAIGHFLNMLPIRSELNPADTFSSFISKLQLT 1003
Cdd:pfam00668 240 LRKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSPDIERMVGMFVNTLPLRIDPKGGKTFSELIKRVQED 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1004 ILDGLDHAAYPFPKMVRDLNIPRSQAGSPVFQTAFFYQNFLQSGSYQSLLSRYADFFSVDYVeyIHQEGEYELVFELWET 1083
Cdd:pfam00668 320 LLSAEPHQGYPFGDLVNDLRLPRDLSRHPLFDPMFSFQNYLGQDSQEEEFQLSELDLSVSSV--IEEEAKYDLSLTASER 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1776025254 1084 EEKMELNIKYNTGLFDAASISAMFDHFVYVTEQAMLNPSQPLKEYSLLPEAEKQMIL 1140
Cdd:pfam00668 398 GGGLTIKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLSDAEKQKLL 454
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
1159-1638 |
1.04e-153 |
|
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341306 [Multi-domain] Cd Length: 491 Bit Score: 487.62 E-value: 1.04e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1159 FEQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYP 1238
Cdd:cd17651 1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1239 AERLEYMLEDSEVFITLTTSELVNTLSwnGVTTALLDQDWDEIAQTASDRkvLTRTVTPENLAYVIYTSGSTGKPKGVMI 1318
Cdd:cd17651 81 AERLAFMLADAGPVLVLTHPALAGELA--VELVAVTLLDQPGAAAGADAE--PDPALDADDLAYVIYTSGSTGRPKGVVM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1319 PHKALTNFLVSMGETPGLTAEDKMLAVTTYCFDIAALELFLPLIKGAhCYICQTEHTK-DVEKLKRDIRTIKPTVMQATP 1397
Cdd:cd17651 157 PHRSLANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGA-TLVLPPEEVRtDPPALAAWLDEQRISRVFLPT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1398 ATWKMLFYSGWENEENV----KILCGGEALP--ETLKRYFLDTGSEAW-NMFGPTETTIWSAVQRINDEC---SRATIGR 1467
Cdd:cd17651 236 VALRALAEHGRPLGVRLaalrYLLTGGEQLVltEDLREFCAGLPGLRLhNHYGPTETHVVTALSLPGDPAawpAPPPIGR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1468 PIANTQIYITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPFEPGSKLYRTGDMARWLPGGRIEYIGRID 1547
Cdd:cd17651 316 PIDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVPGARMYRTGDLARWLPDGELEFLGRAD 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1548 NQVKIRGFRIELGDIESRLSEHPGILECVVVADMDN-----LAAYYTAkHANASLTARELRHFVKNALPAYMVPSYFIQL 1622
Cdd:cd17651 396 DQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRpgekrLVAYVVG-DPEAPVDAAELRAALATHLPEYMVPSAFVLL 474
|
490
....*....|....*.
gi 1776025254 1623 DHMPLTPNGKIDRNSL 1638
Cdd:cd17651 475 DALPLTPNGKLDRRAL 490
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
1180-1577 |
3.66e-153 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 482.54 E-value: 3.66e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1180 TYRELDERSTQLAIYLQA-HGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLEDSEVFITLTTS 1258
Cdd:TIGR01733 1 TYRELDERANRLARHLRAaGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1259 ELVNTLSWNGVTTALLDQDWDEIAQTASDRKVLTRTVTPENLAYVIYTSGSTGKPKGVMIPHKALTNFLVSMGETPGLTA 1338
Cdd:TIGR01733 81 ALASRLAGLVLPVILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1339 EDKMLAVTTYCFDIAALELFLPLIKGAHCYICQTEHTKDVEKLKRD-IRTIKPTVMQATPATWKMLFYSGWENEENVKIL 1417
Cdd:TIGR01733 161 DDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLAAlIAEHPVTVLNLTPSLLALLAAALPPALASLRLV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1418 C-GGEALPETLKRYFLDTGSEA--WNMFGPTETTIWSAVQRI----NDECSRATIGRPIANTQIYITDSQLAPVPAGVPG 1490
Cdd:TIGR01733 241 IlGGEALTPALVDRWRARGPGArlINLYGPTETTVWSTATLVdpddAPRESPVPIGRPLANTRLYVLDDDLRPVPVGVVG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1491 ELCIAGDGVAKGYYKKEELTDSRFIDNPF--EPGSKLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSE 1568
Cdd:TIGR01733 321 ELYIGGPGVARGYLNRPELTAERFVPDPFagGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLR 400
|
....*....
gi 1776025254 1569 HPGILECVV 1577
Cdd:TIGR01733 401 HPGVREAVV 409
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
1167-1638 |
7.65e-149 |
|
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).
Pssm-ID: 341307 [Multi-domain] Cd Length: 436 Bit Score: 471.35 E-value: 7.65e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1167 PDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYML 1246
Cdd:cd17652 1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1247 EDSEVFITLTTselvntlswngvttalldqdwdeiaqtasdrkvltrtvtPENLAYVIYTSGSTGKPKGVMIPHKALTNF 1326
Cdd:cd17652 81 ADARPALLLTT---------------------------------------PDNLAYVIYTSGSTGRPKGVVVTHRGLANL 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1327 LVSMGETPGLTAEDKMLAVTTYCFDIAALELFLPLIKGAHCYICQTEHTKDVEKLKRDIRTIKPTVMQATPATWKMLfyS 1406
Cdd:cd17652 122 AAAQIAAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREHRITHVTLPPAALAAL--P 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1407 GWENEENVKILCGGEALP-ETLKRYflDTGSEAWNMFGPTETTIWSAVQRINDECSRATIGRPIANTQIYITDSQLAPVP 1485
Cdd:cd17652 200 PDDLPDLRTLVVAGEACPaELVDRW--APGRRMINAYGPTETTVCATMAGPLPGGGVPPIGRPVPGTRVYVLDARLRPVP 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1486 AGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPF-EPGSKLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIES 1564
Cdd:cd17652 278 PGVPGELYIAGAGLARGYLNRPGLTAERFVADPFgAPGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEA 357
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1776025254 1565 RLSEHPGILECVVVADMDN-----LAAYYTAKhANASLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSL 1638
Cdd:cd17652 358 ALTEHPGVAEAVVVVRDDRpgdkrLVAYVVPA-PGAAPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
1167-1639 |
1.92e-147 |
|
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341304 [Multi-domain] Cd Length: 450 Bit Score: 468.00 E-value: 1.92e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1167 PDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYML 1246
Cdd:cd17649 1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1247 EDSEVFITLTTselvntlswngvttalldqdwdeiaqtasdrkvltrtvTPENLAYVIYTSGSTGKPKGVMIPHKALTNF 1326
Cdd:cd17649 81 EDSGAGLLLTH--------------------------------------HPRQLAYVIYTSGSTGTPKGVAVSHGPLAAH 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1327 LVSMGETPGLTAEDKMLAVTTYCFDIAALELFLPLIKGAHCYICQTEHTKDVEKLKRDIRTIKPTVMQATPATWKMLF-- 1404
Cdd:cd17649 123 CQATAERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVTVLDLPPAYLQQLAee 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1405 --YSGWENEENVKILC-GGEAL-PETLKRYFldTGSEAW-NMFGPTETTI----WSAVQRINDECSRATIGRPIANTQIY 1475
Cdd:cd17649 203 adRTGDGRPPSLRLYIfGGEALsPELLRRWL--KAPVRLfNAYGPTEATVtplvWKCEAGAARAGASMPIGRPLGGRSAY 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1476 ITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPF-EPGSKLYRTGDMARWLPGGRIEYIGRIDNQVKIRG 1554
Cdd:cd17649 281 ILDADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFgAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRG 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1555 FRIELGDIESRLSEHPGILECVVVA-DMD---NLAAYYTAKHANA-SLTARELRHFVKNALPAYMVPSYFIQLDHMPLTP 1629
Cdd:cd17649 361 FRIELGEIEAALLEHPGVREAAVVAlDGAggkQLVAYVVLRAAAAqPELRAQLRTALRASLPDYMVPAHLVFLARLPLTP 440
|
490
....*....|
gi 1776025254 1630 NGKIDRNSLK 1639
Cdd:cd17649 441 NGKLDRKALP 450
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
1156-1638 |
9.31e-147 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.
Pssm-ID: 341280 [Multi-domain] Cd Length: 447 Bit Score: 465.64 E-value: 9.31e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1156 HELFEQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDP 1235
Cdd:cd12115 2 HDLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1236 SYPAERLEYMLEDSEVFITLTTselvntlswngvttalldqdwdeiaqtasdrkvltrtvtPENLAYVIYTSGSTGKPKG 1315
Cdd:cd12115 82 AYPPERLRFILEDAQARLVLTD---------------------------------------PDDLAYVIYTSGSTGRPKG 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1316 VMIPHKALTNFLVSMGETpgLTAED--KMLAVTTYCFDIAALELFLPLIKGAHCYICQT-EHTKDVEKLKRD--IRTIkP 1390
Cdd:cd12115 123 VAIEHRNAAAFLQWAAAA--FSAEElaGVLASTSICFDLSVFELFGPLATGGKVVLADNvLALPDLPAAAEVtlINTV-P 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1391 TVMQ------ATPATWKMLfysgweneeNVkilcGGEALPETLKR--YFLDTGSEAWNMFGPTETTIWSAVQRINDECSR 1462
Cdd:cd12115 200 SAAAellrhdALPASVRVV---------NL----AGEPLPRDLVQrlYARLQVERVVNLYGPSEDTTYSTVAPVPPGASG 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1463 A-TIGRPIANTQIYITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPFEPGSKLYRTGDMARWLPGGRIE 1541
Cdd:cd12115 267 EvSIGRPLANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGPGARLYRTGDLVRWRPDGLLE 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1542 YIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMD-----NLAAYYTAKHANASLTArELRHFVKNALPAYMVP 1616
Cdd:cd12115 347 FLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDaagerRLVAYIVAEPGAAGLVE-DLRRHLGTRLPAYMVP 425
|
490 500
....*....|....*....|..
gi 1776025254 1617 SYFIQLDHMPLTPNGKIDRNSL 1638
Cdd:cd12115 426 SRFVRLDALPLTPNGKIDRSAL 447
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
1167-1638 |
8.04e-145 |
|
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341298 [Multi-domain] Cd Length: 450 Bit Score: 460.24 E-value: 8.04e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1167 PDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYML 1246
Cdd:cd17643 1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1247 EDSEVFITLTTselvntlswngvttalldqdwdeiaqtasdrkvltrtvtPENLAYVIYTSGSTGKPKGVMIPHKALTNF 1326
Cdd:cd17643 81 ADSGPSLLLTD---------------------------------------PDDLAYVIYTSGSTGRPKGVVVSHANVLAL 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1327 LVSMGETPGLTAEDKMLAVTTYCFDIAALELFLPLIKGAHCYICQTEHTKDVEKLKRDIRTIKPTVMQATPATWKMLFYS 1406
Cdd:cd17643 122 FAATQRWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGVTVLNQTPSAFYQLVEA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1407 GWENEENVK----ILCGGEAL-PETLKRY---FLDTGSEAWNMFGPTETTIWSAVQRIN----DECSRATIGRPIANTQI 1474
Cdd:cd17643 202 ADRDGRDPLalryVIFGGEALeAAMLRPWagrFGLDRPQLVNMYGITETTVHVTFRPLDaadlPAAAASPIGRPLPGLRV 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1475 YITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPF-EPGSKLYRTGDMARWLPGGRIEYIGRIDNQVKIR 1553
Cdd:cd17643 282 YVLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFgGPGSRMYRTGDLARRLPDGELEYLGRADEQVKIR 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1554 GFRIELGDIESRLSEHPGILECVVVADMDN-----LAAYYTAKhANASLTARELRHFVKNALPAYMVPSYFIQLDHMPLT 1628
Cdd:cd17643 362 GFRIELGEIEAALATHPSVRDAAVIVREDEpgdtrLVAYVVAD-DGAAADIAELRALLKELLPDYMVPARYVPLDALPLT 440
|
490
....*....|
gi 1776025254 1629 PNGKIDRNSL 1638
Cdd:cd17643 441 VNGKLDRAAL 450
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
1166-1638 |
1.74e-141 |
|
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341311 [Multi-domain] Cd Length: 479 Bit Score: 451.93 E-value: 1.74e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1166 TPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYM 1245
Cdd:cd17656 1 TPDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1246 LEDSEVFITLTTSELVNTLSWNGVTTALldqDWDEIAQtaSDRKVLTRTVTPENLAYVIYTSGSTGKPKGVMIPHKALTN 1325
Cdd:cd17656 81 MLDSGVRVVLTQRHLKSKLSFNKSTILL---EDPSISQ--EDTSNIDYINNSDDLLYIIYTSGTTGKPKGVQLEHKNMVN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1326 FLVSMGETPGLTAEDKMLAVTTYCFDIAALELFLPLIKGAHCYICQTEHTKDVEKLKRDIRTIKPTVMQATPATWKMLFY 1405
Cdd:cd17656 156 LLHFEREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNIEVVFLPVAFLKFIFS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1406 S-GWENE--ENVK-ILCGGEAL--PETLKRYFLDTGSEAWNMFGPTETTIWSAVqRINDECSRAT---IGRPIANTQIYI 1476
Cdd:cd17656 236 ErEFINRfpTCVKhIITAGEQLviTNEFKEMLHEHNVHLHNHYGPSETHVVTTY-TINPEAEIPElppIGKPISNTWIYI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1477 TDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPFEPGSKLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFR 1556
Cdd:cd17656 315 LDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYR 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1557 IELGDIESRLSEHPGILECVVVADMDN-----LAAYYTAKHAnasLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNG 1631
Cdd:cd17656 395 IELGEIEAQLLNHPGVSEAVVLDKADDkgekyLCAYFVMEQE---LNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNG 471
|
....*..
gi 1776025254 1632 KIDRNSL 1638
Cdd:cd17656 472 KVDRKAL 478
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
4588-4989 |
4.14e-135 |
|
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different products, called polyketides, by successive decarboxylating Claisen condensations. PKSs can be divided into 2 groups, modular type I PKSs consisting of one or more large multifunctional proteins and iterative type II PKSs, complexes of several monofunctional subunits.
Pssm-ID: 238429 [Multi-domain] Cd Length: 421 Bit Score: 431.21 E-value: 4.14e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4588 EGIAVVGLSCRFPGAETLESYWSLLSEGRSSIGPIPAERWGCKTPY------------YAGVIDGVSYFDPDFFLLHEED 4655
Cdd:cd00833 1 EPIAIVGMACRFPGAADPDEFWENLLEGRDAISEIPEDRWDADGYYpdpgkpgktytrRGGFLDDVDAFDAAFFGISPRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4656 VRAMDPQALLVLEECLKLLYHAGYTPEEIKGKPVGVYIGGRS---QHKPDEDSLDHAKNPIVTVGQNYLAANLSQFFDVR 4732
Cdd:cd00833 81 AEAMDPQQRLLLEVAWEALEDAGYSPESLAGSRTGVFVGASSsdyLELLARDPDEIDAYAATGTSRAFLANRISYFFDLR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4733 GPSVVVDTACSSALVGMNMAIQALRGGDIQSAIVGGVSLLSSDASHRLFDRRGILSKHSSFHVFDERADGVVLGEGVGMV 4812
Cdd:cd00833 161 GPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLSPDGRCRPFDADADGYVRGEGVGVV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4813 MLKTVKQALEDGDTIYAVVKAASVNNDGRTAGPATPNLEAQKEVMKDALFKSGKKPEDISYLEANGSGSIVTDLLELKAI 4892
Cdd:cd00833 241 VLKRLSDALRDGDRIYAVIRGSAVNQDGRTKGITAPSGEAQAALIRRAYARAGVDPSDIDYVEAHGTGTPLGDPIEVEAL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4893 QSVYRSGHS--SPLSLGSIKPNIGHPLCAEGIASFIKVVLMLKERRFVPFLSGEKEMAHFDQQKANITFSRALEKW-TDS 4969
Cdd:cd00833 321 AKVFGGSRSadQPLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKIDFEESPLRVPTEARPWpAPA 400
|
410 420
....*....|....*....|.
gi 1776025254 4970 QP-TAAINCFADGGTNVHVIV 4989
Cdd:cd00833 401 GPrRAGVSSFGFGGTNAHVIL 421
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
1156-1638 |
7.74e-135 |
|
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.
Pssm-ID: 341300 [Multi-domain] Cd Length: 440 Bit Score: 431.21 E-value: 7.74e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1156 HELFEQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDP 1235
Cdd:cd17645 1 HQLFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1236 SYPAERLEYMLEDSEVFITLTTselvntlswngvttalldqdwdeiaqtasdrkvltrtvtPENLAYVIYTSGSTGKPKG 1315
Cdd:cd17645 81 DYPGERIAYMLADSSAKILLTN---------------------------------------PDDLAYVIYTSGSTGLPKG 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1316 VMIPHKALTNFLVSMGETPGLTAEDKMLAVTTYCFDIAALELFLPLIKGAHCYICQTEHTKDVEKLKRDIRTIKPTV-MQ 1394
Cdd:cd17645 122 VMIEHHNLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDLDALNDYFNQEGITIsFL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1395 ATPATWKmlfYSGWENEENVKILCGGEALpetlkRYFLDTGSEAWNMFGPTETTIWSAVQRINDECSRATIGRPIANTQI 1474
Cdd:cd17645 202 PTGAAEQ---FMQLDNQSLRVLLTGGDKL-----KKIERKGYKLVNNYGPTENTVVATSFEIDKPYANIPIGKPIDNTRV 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1475 YITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPFEPGSKLYRTGDMARWLPGGRIEYIGRIDNQVKIRG 1554
Cdd:cd17645 274 YILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRG 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1555 FRIELGDIESRLSEHPGILECVVVADMDN-----LAAYYTAKhanASLTARELRHFVKNALPAYMVPSYFIQLDHMPLTP 1629
Cdd:cd17645 354 YRIEPGEIEPFLMNHPLIELAAVLAKEDAdgrkyLVAYVTAP---EEIPHEELREWLKNDLPDYMIPTYFVHLKALPLTA 430
|
....*....
gi 1776025254 1630 NGKIDRNSL 1638
Cdd:cd17645 431 NGKVDRKAL 439
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
1167-1638 |
6.83e-134 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 428.81 E-value: 6.83e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1167 PDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYML 1246
Cdd:cd17650 1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1247 EDSEVFITLTTselvntlswngvttalldqdwdeiaqtasdrkvltrtvtPENLAYVIYTSGSTGKPKGVMIPHKALTNF 1326
Cdd:cd17650 81 EDSGAKLLLTQ---------------------------------------PEDLAYVIYTSGTTGKPKGVMVEHRNVAHA 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1327 LVSMGETPGLTAED-KMLAVTTYCFDIAALELFLPLIKGAHCYICQTEHTKDVEKLKRDIRTIKPTVMQATPATWKMLF- 1404
Cdd:cd17650 122 AHAWRREYELDSFPvRLLQMASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRITLMESTPALIRPVMa 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1405 YSGWENE--ENVKILCGGEAL-----PETLKRYFLdTGSEAWNMFGPTETTIWSAVQRIND--ECSRAT--IGRPIANTQ 1473
Cdd:cd17650 202 YVYRNGLdlSAMRLLIVGSDGckaqdFKTLAARFG-QGMRIINSYGVTEATIDSTYYEEGRdpLGDSANvpIGRPLPNTA 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1474 IYITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPFEPGSKLYRTGDMARWLPGGRIEYIGRIDNQVKIR 1553
Cdd:cd17650 281 MYVLDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIR 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1554 GFRIELGDIESRLSEHPGILECVVVADMDN-----LAAYYTAKHanaSLTARELRHFVKNALPAYMVPSYFIQLDHMPLT 1628
Cdd:cd17650 361 GFRIELGEIESQLARHPAIDEAVVAVREDKggearLCAYVVAAA---TLNTAELRAFLAKELPSYMIPSYYVQLDALPLT 437
|
490
....*....|
gi 1776025254 1629 PNGKIDRNSL 1638
Cdd:cd17650 438 PNGKVDRRAL 447
|
|
| KR_2_SDR_x |
cd08953 |
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ... |
2672-3082 |
9.55e-130 |
|
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes both KR domains of the Bacillus subtilis Pks J,-L, and PksM, and all three KR domains of PksN, components of the megacomplex bacillaene synthase, which synthesizes the antibiotic bacillaene. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.
Pssm-ID: 187656 [Multi-domain] Cd Length: 436 Bit Score: 416.38 E-value: 9.55e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2672 LEPVWEKQNEEREDEDLSYTEHIIVLFETERSVTDSIASHMKDARvitlneavghiaeryQCYMQNIFELLQ-SKVRELS 2750
Cdd:cd08953 36 LQPVWAPAALASAFLALAYEAALLGLAAAEAALLDALSALDPAAA---------------LQLLESLQRLLKaGLLAARA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2751 AGRIIIQAIVPLEKEKQL------FAGVSGLLKTAEIEFSKLTAQVIEIEKPEEMID-LHLKLKDDSQRPFDKQIRYEAG 2823
Cdd:cd08953 101 SGRALLQVVTGLPGALGLdaldpaGAGLAGLLRTLAQEYPGLTCRLIDLDAGEASAEaLARELAAELAAPGAAEVRYRDG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2824 HRFVKGWREMVLPSADTLHMPWRDEGVYLITGGAGSLGLLFAKEIANRTGRsTIVLTGRSVLSEDKENE---LEALRSIG 2900
Cdd:cd08953 181 LRYVQTLEPLPLPAGAAASAPLKPGGVYLVTGGAGGIGRALARALARRYGA-RLVLLGRSPLPPEEEWKaqtLAALEALG 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2901 AEVVYREADVSDQHAVHHLFEEIKERYGTLNGIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSGLLHVDECSKDFPLDFFI 2980
Cdd:cd08953 260 ARVLYISADVTDAAAVRRLLEKVRERYGAIDGVIHAAGVLRDALLAQKTAEDFEAVLAPKVDGLLNLAQALADEPLDFFV 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2981 FFSSVSGCLGNAGQADYAAANSFMDAFAEYRRSLAAskkrFGSTISFNWPLWEEGGMQVGAEDEkRMLKTTGMVPMPTDS 3060
Cdd:cd08953 340 LFSSVSAFFGGAGQADYAAANAFLDAFAAYLRQRGP----QGRVLSINWPAWREGGMAADLGAR-ELLARAGLLPIEPEE 414
|
410 420
....*....|....*....|..
gi 1776025254 3061 GLKAFYQGIASDKPQVFVMEGQ 3082
Cdd:cd08953 415 GLQALEQALSSDLPQVLVSPGD 436
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
1156-1641 |
9.14e-129 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 415.40 E-value: 9.14e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1156 HELFEQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDP 1235
Cdd:cd05918 2 HDLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1236 SYPAERLEYMLEDSEVFITLTTselvntlswngvttalldqdwdeiaqtasdrkvltrtvTPENLAYVIYTSGSTGKPKG 1315
Cdd:cd05918 82 SHPLQRLQEILQDTGAKVVLTS--------------------------------------SPSDAAYVIFTSGSTGKPKG 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1316 VMIPHKALTNFLVSMGETPGLTAEDKMLAVTTYCFDIAALELFLPLIKGAhCyIC-QTEHTKdVEKLKRDIRTIKPTVMQ 1394
Cdd:cd05918 124 VVIEHRALSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGG-C-LCiPSEEDR-LNDLAGFINRLRVTWAF 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1395 ATPATWKMLfysGWENEENVKILC-GGEALPETLKRYFLDtGSEAWNMFGPTETTIWSAVQRINDECSRATIGRPIANTq 1473
Cdd:cd05918 201 LTPSVARLL---DPEDVPSLRTLVlGGEALTQSDVDTWAD-RVRLINAYGPAECTIAATVSPVVPSTDPRNIGRPLGAT- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1474 IYITD--SQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNP-------FEPGSKLYRTGDMARWLPGGRIEYIG 1544
Cdd:cd05918 276 CWVVDpdNHDRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPawlkqegSGRGRRLYRTGDLVRYNPDGSLEYVG 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1545 RIDNQVKIRGFRIELGDIESRLSEH-PGILECVVVA-------DMDNLAAYYTAK----------------HANASLTAR 1600
Cdd:cd05918 356 RKDTQVKIRGQRVELGEIEHHLRQSlPGAKEVVVEVvkpkdgsSSPQLVAFVVLDgsssgsgdgdslflepSDEFRALVA 435
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1776025254 1601 ELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLKNI 1641
Cdd:cd05918 436 ELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRALREL 476
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
1167-1635 |
8.87e-128 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.
Pssm-ID: 341279 [Multi-domain] Cd Length: 477 Bit Score: 412.43 E-value: 8.87e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1167 PDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYML 1246
Cdd:cd12114 1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1247 EDSEVFITLTTSELVNTLSWNGVTTALLDQdwdeiAQTASDRkVLTRTVTPENLAYVIYTSGSTGKPKGVMIPHKALTNF 1326
Cdd:cd12114 81 ADAGARLVLTDGPDAQLDVAVFDVLILDLD-----ALAAPAP-PPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1327 LVSMGETPGLTAEDKMLAVTTYCFDIAALELFLPLIKGAHCYICQTEHTKDVEKLKRDIRTIKPTVMQATPATWKMLF-Y 1405
Cdd:cd12114 155 ILDINRRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDPAHWAELIERHGVTLWNSVPALLEMLLdV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1406 SGWENEENVK---ILCGGE----ALPETLKRYFldTGSEAWNMFGPTETTIWSAVQRIND-ECSRATI--GRPIANTQIY 1475
Cdd:cd12114 235 LEAAQALLPSlrlVLLSGDwiplDLPARLRALA--PDARLISLGGATEASIWSIYHPIDEvPPDWRSIpyGRPLANQRYR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1476 ITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPfePGSKLYRTGDMARWLPGGRIEYIGRIDNQVKIRGF 1555
Cdd:cd12114 313 VLDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHP--DGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGY 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1556 RIELGDIESRLSEHPGILECVVVADMD----NLAAYYTAKHANASLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNG 1631
Cdd:cd12114 391 RIELGEIEAALQAHPGVARAVVVVLGDpggkRLAAFVVPDNDGTPIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANG 470
|
....
gi 1776025254 1632 KIDR 1635
Cdd:cd12114 471 KVDR 474
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
1157-1640 |
3.53e-125 |
|
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341308 [Multi-domain] Cd Length: 433 Bit Score: 403.23 E-value: 3.53e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1157 ELFEQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPS 1236
Cdd:cd17653 1 DAFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1237 YPAERLEYMLEDSEVFITLTTSelvntlswngvttalldqdwdeiaqtasdrkvltrtvTPENLAYVIYTSGSTGKPKGV 1316
Cdd:cd17653 81 LPSARIQAILRTSGATLLLTTD-------------------------------------SPDDLAYIIFTSGSTGIPKGV 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1317 MIPHKALTNFLVSMGETPGLTAEDKMLAVTTYCFDIAALELFLPLIKGAHcyICQTEHTKDVEKLKR--DIRTIKPTVMQ 1394
Cdd:cd17653 124 MVPHRGVLNYVSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGT--LVLADPSDPFAHVARtvDALMSTPSILS 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1395 ATPATwkmlfysgweNEENVK-ILCGGEALPETLKRYFLDtGSEAWNMFGPTETTIWSAVQRINDEcSRATIGRPIANTQ 1473
Cdd:cd17653 202 TLSPQ----------DFPNLKtIFLGGEAVPPSLLDRWSP-GRRLYNAYGPTECTISSTMTELLPG-QPVTIGKPIPNST 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1474 IYITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPFEPGSKLYRTGDMARWLPGGRIEYIGRIDNQVKIR 1553
Cdd:cd17653 270 CYILDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFWPGSRMYRTGDYGRWTEDGGLEFLGREDNQVKVR 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1554 GFRIELGDIESR-LSEHPGILECVVVADMDNLAAYYTAkhanASLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGK 1632
Cdd:cd17653 350 GFRINLEEIEEVvLQSQPEVTQAAAIVVNGRLVAFVTP----ETVDVDGLRSELAKHLPSYAVPDRIIALDSFPLTANGK 425
|
....*...
gi 1776025254 1633 IDRNSLKN 1640
Cdd:cd17653 426 VDRKALRE 433
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
695-1736 |
7.57e-123 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 439.99 E-value: 7.57e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 695 PLSEVQKGLWTLQKMSPEKSAYHVPLCFKFSSGLHLETLQQAFGLVLNQHPILK------------HVI----------Q 752
Cdd:PRK05691 3259 PLTPMQEGLLLHTLLEPGTGLYYMQDRYRINSALDPERFAQAWQAVVARHEALRasfswnagetmlQVIhkpgrtpidyL 3338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 753 EKDGVPILKNEPALSIEIKTENISSMKESDIPAF-LRkkvkepyvkenspLVRVmsfsrSEQEHFLLVVIHHLIFDGVSS 831
Cdd:PRK05691 3339 DWRGLPEDGQEQRLQALHKQEREAGFDLLNQPPFhLR-------------LIRV-----DEARYWFMMSNHHILIDAWCR 3400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 832 VTFIHSLFDTYQLLLKGQQPEIAVSPAiYHDFAAWeknmLAGKDGVKHRTYWQKQLSGtlpnLQLPKVSASSVSEFRE-- 909
Cdd:PRK05691 3401 SLLMNDFFEIYTALGEGREAQLPVPPR-YRDYIGW----LQRQDLAQARQWWQDNLRG----FERPTPIPSDRPFLREha 3471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 910 ---------DTYTRrLSSGFMNQVRMFAKEHSVNVTTVFLSCYMMLLGRYTGQKEQI---------VGMPAMVRpeerfd 971
Cdd:PRK05691 3472 gdsggmvvgDCYTR-LDAADGARLRELAQAHQLTVNTFAQAAWALVLRRYSGDRDVLfgvtvagrpVSMPQMQR------ 3544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 972 dAIGHFLNMLPIRSELnPAD----TFSSFISKLQLTILDGLDHAAYPFPKMVRDLNIPRsqaGSPVFQTAFFYQNF---- 1043
Cdd:PRK05691 3545 -TVGLFINSIALRVQL-PAAgqrcSVRQWLQGLLDSNMELREYEYLPLVAIQECSELPK---GQPLFDSLFVFENApvev 3619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1044 -----LQSGSYQSLLSRYADFFSVDYVEYihqegeyelvfelweTEEKMELNIKYNTGLFDAASISAMFDHFVYVTEQAM 1118
Cdd:PRK05691 3620 svldrAQSLNASSDSGRTHTNFPLTAVCY---------------PGDDLGLHLSYDQRYFDAPTVERLLGEFKRLLLALV 3684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1119 LNPSQPLKEYSLLPEAEKQMILKTWNATGKTYP----YItfhELFEQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIY 1194
Cdd:PRK05691 3685 QGFHGDLSELPLLGEQERDFLLDGCNRSERDYPleqsYV---RLFEAQVAAHPQRIAASCLDQQWSYAELNRAANRLGHA 3761
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1195 LQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLEDSEvfitltTSELVNTLSWNGVTTALL 1274
Cdd:PRK05691 3762 LRAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGLPAQRLQRIIELSR------TPVLVCSAACREQARALL 3835
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1275 DQ----------DWDEIAQTASDRKVLTRTVTPENLAYVIYTSGSTGKPKGVMIPHKALTNFLVSMGETPGLTAEDKMLA 1344
Cdd:PRK05691 3836 DElgcanrprllVWEEVQAGEVASHNPGIYSGPDNLAYVIYTSGSTGLPKGVMVEQRGMLNNQLSKVPYLALSEADVIAQ 3915
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1345 VTTYCFDIAALElFL--PLIkGAHCYICQTEHTKDVEKLKRDIRTIKPTVMQATPATWKMLFYSGWENEENVK-ILCGGE 1421
Cdd:PRK05691 3916 TASQSFDISVWQ-FLaaPLF-GARVEIVPNAIAHDPQGLLAHVQAQGITVLESVPSLIQGMLAEDRQALDGLRwMLPTGE 3993
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1422 ALPETLKRYFLDTGSEAW--NMFGPTETTIWSAVQRINDECSRAT---IGRPIANTQIYITDSQLAPVPAGVPGELCIAG 1496
Cdd:PRK05691 3994 AMPPELARQWLQRYPQIGlvNAYGPAECSDDVAFFRVDLASTRGSylpIGSPTDNNRLYLLDEALELVPLGAVGELCVAG 4073
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1497 DGVAKGYYKKEELTDSRFIDNPF-EPGSKLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILEC 1575
Cdd:PRK05691 4074 TGVGRGYVGDPLRTALAFVPHPFgAPGERLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREA 4153
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1576 VVV----ADMDNLAAYYTAKHANASLTAR--ELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLKNIDLSGEQlK 1649
Cdd:PRK05691 4154 AVAvqegVNGKHLVGYLVPHQTVLAQGALleRIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKALPALDIGQLQ-S 4232
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1650 QRQTSPKN-IQDTVFTIWQEVLKTSDIEWDDGFFDVGGDSLLAVTVADRIKHELSCEFSVTDLFEYSTIKNISQYI---- 1724
Cdd:PRK05691 4233 QAYLAPRNeLEQTLATIWADVLKVERVGVHDNFFELGGHSLLATQIASRVQKALQRNVPLRAMFECSTVEELAEYIegla 4312
|
1130
....*....|....*.
gi 1776025254 1725 ----TEQRMGNASDHM 1736
Cdd:PRK05691 4313 gsaiDEQKVDRLSDLM 4328
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
1762-2185 |
1.13e-120 |
|
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the thiolase family and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.
Pssm-ID: 214836 [Multi-domain] Cd Length: 298 Bit Score: 384.37 E-value: 1.13e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1762 VAIIGISCEFPGAKNHDEFWENLRDGkesiaffnkeelqrfgiskeiaenadyvpakasIEGKDRFDPSFFQISPKDAEF 1841
Cdd:smart00825 1 IAIVGMSCRFPGADDPEEFWDLLLAG---------------------------------LDDVDLFDAAFFGISPREAEA 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1842 MDPQLRMLLTHSWKAIEDAGYAAGQIP--QTSVFMSASNNSYrallpsdttesletpdgyvswvlaqsgtiptmishklg 1919
Cdd:smart00825 48 MDPQQRLLLEVAWEALEDAGIDPESLRgsRTGVFVGVSSSDY-------------------------------------- 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1920 lrgpSYFVHANCSSSLIGLHSAYKSLLSAESDYALVGGATLHTESNIGYVHQPGLNFSSDGHIKAFDASADGMIGGEGVA 1999
Cdd:smart00825 90 ----SVTVDTACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLSPDGRCKTFDASADGYVRGEGVG 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2000 VVLLKKAADAVKDGDHIYALLRGIGVNNDGADKvGFYAPSVKGQadvvqqvmnqtkihpesicyveahgtgtklgdpiel 2079
Cdd:smart00825 166 VVVLKRLSDALRDGDPILAVIRGSAVNQDGRSN-GITAPSGPAQ------------------------------------ 208
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2080 aaltnvyrqytnktqfCGIGSVKTNIGHLDTAAGLAGCIKVVMSLYHQELAPSINYKEPNPNTDLASSPFYVVDQKKTLS 2159
Cdd:smart00825 209 ----------------LLIGSVKSNIGHLEAAAGVAGLIKVVLALKHGVIPPTLHFETPNPHIDLEESPLRVPTELTPWP 272
|
410 420
....*....|....*....|....*.
gi 1776025254 2160 REIQTHRAALSSFGLGGTNTHAIFEQ 2185
Cdd:smart00825 273 PPGRPRRAGVSSFGFGGTNAHVILEE 298
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
4587-5010 |
1.38e-118 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 413.50 E-value: 1.38e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4587 AEGIAVVGLSCRFPGAETLESYWSLLSEGRSSIGPIPAERWGCKTPY-------------YAGVIDGVSYFDPDFFLLHE 4653
Cdd:COG3321 3 DEPIAIIGMACRFPGADDPEEFWRNLRAGRDAITEVPADRWDADAYYdpdpdapgktyvrWGGFLDDVDEFDALFFGISP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4654 EDVRAMDPQALLVLEECLKLLYHAGYTPEEIKGKPVGVYIGG-------RSQHKPDEDSLDHAknpiVTVGQNYLAANLS 4726
Cdd:COG3321 83 REAEAMDPQQRLLLEVAWEALEDAGYDPESLAGSRTGVFVGAssndyalLLLADPEAIDAYAL----TGNAKSVLAGRIS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4727 QFFDVRGPSVVVDTACSSALVGMNMAIQALRGGDIQSAIVGGVSLLSSDASHRLFDRRGILSKHSSFHVFDERADGVVLG 4806
Cdd:COG3321 159 YKLDLRGPSVTVDTACSSSLVAVHLACQSLRSGECDLALAGGVNLMLTPESFILFSKGGMLSPDGRCRAFDADADGYVRG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4807 EGVGMVMLKTVKQALEDGDTIYAVVKAASVNNDGRTAGPATPNLEAQKEVMKDALFKSGKKPEDISYLEANGSGSIVTDL 4886
Cdd:COG3321 239 EGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRSNGLTAPNGPAQAAVIRRALADAGVDPATVDYVEAHGTGTPLGDP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4887 LELKAIQSVYRSGHS--SPLSLGSIKPNIGHPLCAEGIASFIKVVLMLKERRFVPFLsgekemaHFDQQKANITFS---- 4960
Cdd:COG3321 319 IEAAALTAAFGQGRPadQPCAIGSVKSNIGHLEAAAGVAGLIKAVLALRHGVLPPTL-------HFETPNPHIDFEnspf 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1776025254 4961 ---RALEKW-TDSQP-TAAINCFADGGTNVHVIVEAWEKDEKHAikRSPKSPPQL 5010
Cdd:COG3321 392 yvnTELRPWpAGGGPrRAGVSSFGFGGTNAHVVLEEAPAAAPAA--AAAARPPQL 444
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
1167-1638 |
8.02e-115 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 374.04 E-value: 8.02e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1167 PDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVG-PDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYM 1245
Cdd:cd17648 1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAEIrPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1246 LEDSEVFITLTTselvntlswngvttalldqdwdeiaqtasdrkvltrtvtPENLAYVIYTSGSTGKPKGVMIPHKALTN 1325
Cdd:cd17648 81 LEDTGARVVITN---------------------------------------STDLAYAIYTSGTTGKPKGVLVEHGSVVN 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1326 FLVSMGETPGLTAED--KMLAVTTYCFDIAALELFLPLIKGAHCYICQTEHTKDVEKLKRDIRTIKPTVMQATPATWKML 1403
Cdd:cd17648 122 LRTSLSERYFGRDNGdeAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPDRFYAYINREKVTYLSGTPSVLQQY 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1404 FYSGWENEEnvKILCGGEALP----ETLKRYFldtGSEAWNMFGPTETTIWSAVQRI-NDECSRATIGRPIANTQIYITD 1478
Cdd:cd17648 202 DLARLPHLK--RVDAAGEEFTapvfEKLRSRF---AGLIINAYGPTETTVTNHKRFFpGDQRFDKSLGRPVRNTKCYVLN 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1479 SQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPFEP--------GSKLYRTGDMARWLPGGRIEYIGRIDNQV 1550
Cdd:cd17648 277 DAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFQTeqerargrNARLYKTGDLVRWLPSGELEYLGRNDFQV 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1551 KIRGFRIELGDIESRLSEHPGILECVVVADMDN----------LAAYYTAkhANASLTARELRHFVKNALPAYMVPSYFI 1620
Cdd:cd17648 357 KIRGQRIEPGEVEAALASYPGVRECAVVAKEDAsqaqsriqkyLVGYYLP--EPGHVPESDLLSFLRAKLPRYMVPARLV 434
|
490
....*....|....*...
gi 1776025254 1621 QLDHMPLTPNGKIDRNSL 1638
Cdd:cd17648 435 RLEGIPVTINGKLDVRAL 452
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
1155-1639 |
2.38e-114 |
|
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440087 [Multi-domain] Cd Length: 452 Bit Score: 372.61 E-value: 2.38e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1155 FHELFEQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLD 1234
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1235 PSYPAERLEYMLEDSEVfitlttselvntlswngvttalldqdwdeiaqtasdrKVLtrtVTpenlAYVIYTSGSTGKPK 1314
Cdd:COG0318 81 PRLTAEELAYILEDSGA-------------------------------------RAL---VT----ALILYTSGTTGRPK 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1315 GVMIPHKALTNFLVSMGETPGLTAEDKMLAVTTYCFDIA-ALELFLPLIKGAHCYIcqteHTK-DVEKLKRDIRTIKPTV 1392
Cdd:COG0318 117 GVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGlTVGLLAPLLAGATLVL----LPRfDPERVLELIERERVTV 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1393 MQATPATWKMLFYSGWENEENVK----ILCGGEALPETLKRYFLD-TGSEAWNMFGPTETTIWSAVQRINDECSR-ATIG 1466
Cdd:COG0318 193 LFGVPTMLARLLRHPEFARYDLSslrlVVSGGAPLPPELLERFEErFGVRIVEGYGLTETSPVVTVNPEDPGERRpGSVG 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1467 RPIANTQIYITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNpfepgskLYRTGDMARWLPGGRIEYIGRI 1546
Cdd:COG0318 273 RPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFRDG-------WLRTGDLGRLDEDGYLYIVGRK 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1547 DNQVKIRGFRIELGDIESRLSEHPGILECVVVADMDN-----LAAYYTAKhANASLTARELRHFVKNALPAYMVPSYFIQ 1621
Cdd:COG0318 346 KDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEkwgerVVAFVVLR-PGAELDAEELRAFLRERLARYKVPRRVEF 424
|
490
....*....|....*...
gi 1776025254 1622 LDHMPLTPNGKIDRNSLK 1639
Cdd:COG0318 425 VDELPRTASGKIDRRALR 442
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
1163-1638 |
3.41e-114 |
|
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341267 [Multi-domain] Cd Length: 449 Bit Score: 372.35 E-value: 3.41e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1163 AKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERL 1242
Cdd:cd05945 1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1243 EYMLEDSEVfitlttselvntlswngvtTALLdqdwdeiaqtasdrkvltrtVTPENLAYVIYTSGSTGKPKGVMIPHKA 1322
Cdd:cd05945 81 REILDAAKP-------------------ALLI--------------------ADGDDNAYIIFTSGSTGRPKGVQISHDN 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1323 LTNFLVSMGETPGLTAEDKMLAVTTYCFDIAALELFLPLIKGAHCYICQTEHTKDVEKLKRDIRTIKPTVMQATPATWKM 1402
Cdd:cd05945 122 LVSFTNWMLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADPKQLFRFLAEHGITVWVSTPSFAAM 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1403 LFYSGWENEENVK-----ILCGgEALP----ETLKRYFldTGSEAWNMFGPTETTIWSAVQRINDECS----RATIGRPI 1469
Cdd:cd05945 202 CLLSPTFTPESLPslrhfLFCG-EVLPhktaRALQQRF--PDARIYNTYGPTEATVAVTYIEVTPEVLdgydRLPIGYAK 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1470 ANTQIYITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPFEPGsklYRTGDMARWLPGGRIEYIGRIDNQ 1549
Cdd:cd05945 279 PGAKLVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDEGQRA---YRTGDLVRLEADGLLFYRGRLDFQ 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1550 VKIRGFRIELGDIESRLSEHPGILECVVVADMDN-----LAAYYTAKHANASLTARELRHFVKNALPAYMVPSYFIQLDH 1624
Cdd:cd05945 356 VKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGekvteLIAFVVPKPGAEAGLTKAIKAELAERLPPYMIPRRFVYLDE 435
|
490
....*....|....
gi 1776025254 1625 MPLTPNGKIDRNSL 1638
Cdd:cd05945 436 LPLNANGKIDRKAL 449
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
1159-1553 |
4.72e-114 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 370.49 E-value: 4.72e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1159 FEQQAKKTPDRAAVS-YEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSY 1237
Cdd:pfam00501 1 LERQAARTPDKTALEvGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1238 PAERLEYMLEDSE--VFITLTTSELVNTLSW-----NGVTTALLDQDW-------DEIAQTASDRKVLTRTVTPENLAYV 1303
Cdd:pfam00501 81 PAEELAYILEDSGakVLITDDALKLEELLEAlgkleVVKLVLVLDRDPvlkeeplPEEAKPADVPPPPPPPPDPDDLAYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1304 IYTSGSTGKPKGVMIPHKALTNFLVSMGETP----GLTAEDKMLAVTTYCFDIA-ALELFLPLIKGAHCYICQTEHTKDV 1378
Cdd:pfam00501 161 IYTSGTTGKPKGVMLTHRNLVANVLSIKRVRprgfGLGPDDRVLSTLPLFHDFGlSLGLLGPLLAGATVVLPPGFPALDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1379 EKLKRDIRTIKPTVMQATPATWKMLFYSGWENEENVK----ILCGGEALPETLKRYFLD-TGSEAWNMFGPTETTIWSA- 1452
Cdd:pfam00501 241 AALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSslrlVLSGGAPLPPELARRFRElFGGALVNGYGLTETTGVVTt 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1453 -VQRINDECSRATIGRPIANTQIYITD-SQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPFepgsklYRTGD 1530
Cdd:pfam00501 321 pLPLDEDLRSLGSVGRPLPGTEVKIVDdETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDEDGW------YRTGD 394
|
410 420
....*....|....*....|...
gi 1776025254 1531 MARWLPGGRIEYIGRIDNQVKIR 1553
Cdd:pfam00501 395 LGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| KR_2_SDR_x |
cd08953 |
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ... |
4029-4401 |
1.70e-109 |
|
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes both KR domains of the Bacillus subtilis Pks J,-L, and PksM, and all three KR domains of PksN, components of the megacomplex bacillaene synthase, which synthesizes the antibiotic bacillaene. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.
Pssm-ID: 187656 [Multi-domain] Cd Length: 436 Bit Score: 358.22 E-value: 1.70e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4029 DWKEFDGLVDVIGCGWDDeGRLDWIEWVQRLVEF----GHKEGLRLLCVTKGLESFQNTS-VRMAGASRAGLYRMLQCEY 4103
Cdd:cd08953 61 LAAAEAALLDALSALDPA-AALQLLESLQRLLKAgllaARASGRALLQVVTGLPGALGLDaLDPAGAGLAGLLRTLAQEY 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4104 SHLISRHMDAEEVTDHP-RLAKLIADEfYSESYDAEVCYRDGLRYQSFLKAHPETGKATeQSAVFPKDHVLLITGGTRGI 4182
Cdd:cd08953 140 PGLTCRLIDLDAGEASAeALARELAAE-LAAPGAAEVRYRDGLRYVQTLEPLPLPAGAA-ASAPLKPGGVYLVTGGAGGI 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4183 GLLCARHFAECYGvKKLVLTGREQLPPREEWARfktsntslaekiQAVRELEAKGVQVEMLSLTLSDDAQVEQTLQHIKR 4262
Cdd:cd08953 218 GRALARALARRYG-ARLVLLGRSPLPPEEEWKA------------QTLAALEALGARVLYISADVTDAAAVRRLLEKVRE 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4263 TLGPIGGVIHCAGLTDMDTLafIRKTSDDIQRVMEPKVSGLTTLYRHVCNEPLQFFVLFSSVSAIIPelSAGQADYAMAN 4342
Cdd:cd08953 285 RYGAIDGVIHAAGVLRDALL--AQKTAEDFEAVLAPKVDGLLNLAQALADEPLDFFVLFSSVSAFFG--GAGQADYAAAN 360
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1776025254 4343 SYMDYFAEAHQK---HVPIISVQWPNWKETGMGEV--TNQAYRESGLFSITNSEGLRFLDQIVS 4401
Cdd:cd08953 361 AFLDAFAAYLRQrgpQGRVLSINWPAWREGGMAADlgARELLARAGLLPIEPEEGLQALEQALS 424
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
3339-3588 |
2.31e-108 |
|
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains. The N-terminal domain contains most of the structures involved in dimer formation and also the active site cysteine.
Pssm-ID: 425468 [Multi-domain] Cd Length: 251 Bit Score: 346.93 E-value: 2.31e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3339 EPVAIVGISGRFPGAMDIDEFWKNLEEGKDSITEVPKDRWDWREHYGNPDTDVNKTDIKWGGfIDGVAEFDPLFFGISPR 3418
Cdd:pfam00109 1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIPADRWDPDKLYDPPSRIAGKIYTKWGG-LDDIFDFDPLFFGISPR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3419 EADYVDPQQRLLMTYVWKALEDAGCPPQSLSGTGTGIFIGTGNTGYKDL--FHRANLPIEGHAATGHMIPSVGPNRMSYF 3496
Cdd:pfam00109 80 EAERMDPQQRLLLEAAWEALEDAGITPDSLDGSRTGVFIGSGIGDYAALllLDEDGGPRRGSPFAVGTMPSVIAGRISYF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3497 LNIHGPSEPVETACSSSLVAIHRAVTAMQNGDCEMAIAGGVNTILTEEAHISYSKAGMLSKDGRCKTFSADANGYVRGEG 3576
Cdd:pfam00109 160 LGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSPDGPCKAFDPFADGFVRGEG 239
|
250
....*....|..
gi 1776025254 3577 VGMVMLKKLEDA 3588
Cdd:pfam00109 240 VGAVVLKRLSDA 251
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
46-563 |
4.76e-105 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 347.94 E-value: 4.76e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 46 KGIIYLQPDGTEVYQSYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNSQLLPAFWGCVLTGVVPaplaVPPTYAESSS 125
Cdd:cd05908 2 EGIIFILGDKKEKFVSYRHLREEALGYLGALQELGIKPGQEVVFQITHNNKFLYLFWACLLGGMIA----VPVSIGSNEE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 126 GTQKLKDAWTLLDKPAVITDRGMHQEMldwakeqglegfraiivedllsaeadtdwhqssPEDLALLLLTSGSTGTPKAV 205
Cdd:cd05908 78 HKLKLNKVWNTLKNPYLITEEEVLCEL---------------------------------ADELAFIQFSSGSTGDPKGV 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 206 MLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDHVGGIGMLHLRDVYLGCQEINVSSETILMEPLKWLDWIDHYRASVTW 285
Cdd:cd05908 125 MLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMPTRLFIRRPILWLKKASEHKATIVS 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 286 APNFAFGLVTDFAEEIKDRKWDLSSMRYMLNGGEAMVAKVGRRILELLEPHGLPADAIRPAWGMSETSSGVIFS------ 359
Cdd:cd05908 205 SPNFGYKYFLKTLKPEKANDWDLSSIRMILNGAEPIDYELCHEFLDHMSKYGLKRNAILPVYGLAEASVGASLPkaqspf 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 360 ------HEFTRAG-----TSDDDH----FVEIGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGYYQRPDLNESV 424
Cdd:cd05908 285 ktitlgRRHVTHGepepeVDKKDSecltFVEVGKPIDETDIRICDEDNKILPDGYIGHIQIRGKNVTPGYYNNPEATAKV 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 425 FTEDGWFETGDLGFLRNGRLTITGRTKDAIIINGINYYSHAIESAVEELSEIETSYTAACAVRLGQNSTDQLAIFFVTSA 504
Cdd:cd05908 365 FTDDGWLKTGDLGFIRNGRLVITGREKDIIFVNGQNVYPHDIERIAEELEGVELGRVVACGVNNSNTRNEEIFCFIEHRK 444
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1776025254 505 KLNDeqMSQLLRNIQSHVSQVIGVTPEYLLPVQKeeIPKTAIGKIQRTQLKTSFENGEF 563
Cdd:cd05908 445 SEDD--FYPLGKKIKKHLNKRGGWQINEVLPIRR--IPKTTSGKVKRYELAQRYQSGEF 499
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
4590-4991 |
5.41e-104 |
|
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the thiolase family and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.
Pssm-ID: 214836 [Multi-domain] Cd Length: 298 Bit Score: 336.61 E-value: 5.41e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4590 IAVVGLSCRFPGAETLESYWSLLSEGrssigpipaerwgcktpyyagvIDGVSYFDPDFFLLHEEDVRAMDPQALLVLEE 4669
Cdd:smart00825 1 IAIVGMSCRFPGADDPEEFWDLLLAG----------------------LDDVDLFDAAFFGISPREAEAMDPQQRLLLEV 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4670 CLKLLYHAGYTPEEIKGKPVGVYIGGRSQHkpdedsldhaknpivtvgqnYlaanlsqffdvrgpSVVVDTACSSALVGM 4749
Cdd:smart00825 59 AWEALEDAGIDPESLRGSRTGVFVGVSSSD--------------------Y--------------SVTVDTACSSSLVAL 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4750 NMAIQALRGGDIQSAIVGGVSLLSSDASHRLFDRRGILSKHSSFHVFDERADGVVLGEGVGMVMLKTVKQALEDGDTIYA 4829
Cdd:smart00825 105 HLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLSPDGRCKTFDASADGYVRGEGVGVVVLKRLSDALRDGDPILA 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4830 VVKAASVNNDGRTAGPATPNLEAQkevmkdalfksgkkpedisyleangsgsivtdllelkaiqsvyrsghsspLSLGSI 4909
Cdd:smart00825 185 VIRGSAVNQDGRSNGITAPSGPAQ--------------------------------------------------LLIGSV 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4910 KPNIGHPLCAEGIASFIKVVLMLKERRFVPFLSGEKEMAHFDQQKANITFSRALEKW--TDSQPTAAINCFADGGTNVHV 4987
Cdd:smart00825 215 KSNIGHLEAAAGVAGLIKVVLALKHGVIPPTLHFETPNPHIDLEESPLRVPTELTPWppPGRPRRAGVSSFGFGGTNAHV 294
|
....
gi 1776025254 4988 IVEA 4991
Cdd:smart00825 295 ILEE 298
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
37-560 |
6.09e-97 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 326.12 E-value: 6.09e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 37 RTAAELGDTKGIIYL-QPDGTEVYQSYRRLWDDGLRIVKGLRQSGlKAKQSVILQLGDNSQLLPAFWGCVLTGVVPAPLA 115
Cdd:cd05931 1 RRAAARPDRPAYTFLdDEGGREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 116 VPptyaESSSGTQKLKDAwtLLD-KP-AVITDRGMHQEMLDWAKEQGLEGFRAIIVEDLLSAEADTDWH--QSSPEDLAL 191
Cdd:cd05931 80 PP----TPGRHAERLAAI--LADaGPrVVLTTAAALAAVRAFAASRPAAGTPRLLVVDLLPDTSAADWPppSPDPDDIAY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 192 LLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDH-VGGIGMLhLRDVYLGCQEINVSSETILMEPL 270
Cdd:cd05931 154 LQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHdMGLIGGL-LTPLYSGGPSVLMSPAAFLRRPL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 271 KWLDWIDHYRASVTWAPNFAFGLVTDFAEEIKDRKWDLSSMRYMLNGGEAMVAKVGRRILELLEPHGLPADAIRPAWGMS 350
Cdd:cd05931 233 RWLRLISRYRATISAAPNFAYDLCVRRVRDEDLEGLDLSSWRVALNGAEPVRPATLRRFAEAFAPFGFRPEAFRPSYGLA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 351 ETSSGVIFS---------------HEFTRAGTSDDDH----FVEIGSPIPGFSMRIVN-DHNELVEEGEIGRFQVSGLSV 410
Cdd:cd05931 313 EATLFVSGGppgtgpvvlrvdrdaLAGRAVAVAADDPaareLVSCGRPLPDQEVRIVDpETGRELPDGEVGEIWVRGPSV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 411 TSGYYQRPDLNESVF------TEDGWFETGDLGFLRNGRLTITGRTKDAIIINGINYYSHAIESAVEELSE-IETSYTAA 483
Cdd:cd05931 393 ASGYWGRPEATAETFgalaatDEGGWLRTGDLGFLHDGELYITGRLKDLIIVRGRNHYPQDIEATAEEAHPaLRPGCVAA 472
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1776025254 484 CAVrlGQNSTDQLAIFFVTSAKLNDEQMSQLLRNIQSHVSQVIGVTPEYLLPVQKEEIPKTAIGKIQRTQLKTSFEN 560
Cdd:cd05931 473 FSV--PDDGEERLVVVAEVERGADPADLAAIAAAIRAAVAREHGVAPADVVLVRPGSIPRTSSGKIQRRACRAAYLD 547
|
|
| LCL_NRPS-like |
cd19531 |
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ... |
695-1121 |
3.83e-92 |
|
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.
Pssm-ID: 380454 [Multi-domain] Cd Length: 427 Bit Score: 307.74 E-value: 3.83e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 695 PLSEVQKGLWTLQKMSPEKSAYHVPLCFKFSSGLHLETLQQAFGLVLNQHPILKHVIQEKDGVPILKNEPALSIEIKTEN 774
Cdd:cd19531 3 PLSFAQQRLWFLDQLEPGSAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFVEVDGEPVQVILPPLPLPLPVVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 775 ISSM----KESDIPAFLRKKVKEPYVKENSPLVRVMSFSRSEQEHFLLVVIHHLIFDGVSSVTFIHSLFDTYQLLLKGQQ 850
Cdd:cd19531 83 LSGLpeaeREAEAQRLAREEARRPFDLARGPLLRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYAAFLAGRP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 851 PEIAVSPAIYHDFAAWEKNMLAGKDGVKHRTYWQKQLSGTLPNLQLPkvsA----SSVSEFREDTYTRRLSSGFMNQVRM 926
Cdd:cd19531 163 SPLPPLPIQYADYAVWQREWLQGEVLERQLAYWREQLAGAPPVLELP---TdrprPAVQSFRGARVRFTLPAELTAALRA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 927 FAKEHsvNVT--TVFLSCYMMLLGRYTGQKEQIVGMPAMVRPEERFDDAIGHFLNMLPIRSELNPADTFSSFISKLQLTI 1004
Cdd:cd19531 240 LARRE--GATlfMTLLAAFQVLLHRYSGQDDIVVGTPVAGRNRAELEGLIGFFVNTLVLRTDLSGDPTFRELLARVRETA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1005 LDGLDHAAYPFPKMVRDLNIPRSQAGSPVFQTAFFYQNFLQSGSYQSLLsryadffSVDYVEYIHQEGEYELVFELWETE 1084
Cdd:cd19531 318 LEAYAHQDLPFEKLVEALQPERDLSRSPLFQVMFVLQNAPAAALELPGL-------TVEPLEVDSGTAKFDLTLSLTETD 390
|
410 420 430
....*....|....*....|....*....|....*..
gi 1776025254 1085 EKMELNIKYNTGLFDAASISAMFDHFVYVTEQAMLNP 1121
Cdd:cd19531 391 GGLRGSLEYNTDLFDAATIERMAGHFQTLLEAIVADP 427
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
31-564 |
4.87e-91 |
|
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440087 [Multi-domain] Cd Length: 452 Bit Score: 305.58 E-value: 4.87e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 31 IPEVLYRTAAELGDTKGIIYlqpDGTEVyqSYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNSQLLPAFWGCVLTGVV 110
Cdd:COG0318 1 LADLLRRAAARHPDRPALVF---GGRRL--TYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 111 PAPlaVPPTYAEsssgtQKLKDAWTLLDKPAVITdrgmhqemldwakeqglegfraiivedllsaeadtdwhqsspedlA 190
Cdd:COG0318 76 VVP--LNPRLTA-----EELAYILEDSGARALVT---------------------------------------------A 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 191 LLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDHVGGIGMLHLRDVYLGCQeinvsseTILME-- 268
Cdd:COG0318 104 LILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGAT-------LVLLPrf 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 269 -PLKWLDWIDHYRASV-TWAPNFAFGLvtdfAEEIKDRKWDLSSMRYMLNGGEAMVAKVGRRILELLEPhglpadAIRPA 346
Cdd:COG0318 177 dPERVLELIERERVTVlFGVPTMLARL----LRHPEFARYDLSSLRLVVSGGAPLPPELLERFEERFGV------RIVEG 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 347 WGMSETSSGVIFsheftRAGTSDDDHFVEIGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGYYQRPDLNESVFt 426
Cdd:COG0318 247 YGLTETSPVVTV-----NPEDPGERRPGSVGRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAF- 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 427 EDGWFETGDLGFLR-NGRLTITGRTKDAIIINGINYYSHAIESAVEELSEIetsytAACAV------RLGQnstdQLAIF 499
Cdd:COG0318 321 RDGWLRTGDLGRLDeDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGV-----AEAAVvgvpdeKWGE----RVVAF 391
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1776025254 500 FVTS--AKLNDEQMSQLLRniqSHVSQvIGVtPEYLLPVqkEEIPKTAIGKIQRTQLKTSFENGEFD 564
Cdd:COG0318 392 VVLRpgAELDAEELRAFLR---ERLAR-YKV-PRRVEFV--DELPRTASGKIDRRALRERYAAGALE 451
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
1157-1640 |
3.38e-86 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 293.34 E-value: 3.38e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1157 ELFEQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPS 1236
Cdd:PRK04813 6 ETIEEFAQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVDVS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1237 YPAERLEYMLEDSEVFITLTTSELVNTLSwnGVTTALLDQDWDEIAQTASdrKVLTRTVTPENLAYVIYTSGSTGKPKGV 1316
Cdd:PRK04813 86 SPAERIEMIIEVAKPSLIIATEELPLEIL--GIPVITLDELKDIFATGNP--YDFDHAVKGDDNYYIIFTSGTTGKPKGV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1317 MIPHKAL---TNFLVSMGETPgltAEDKMLAVTTYCFDIAALELFLPLIKGAHCYICQTEHTKDVEKLKRDIRTIKPTVM 1393
Cdd:PRK04813 162 QISHDNLvsfTNWMLEDFALP---EGPQFLNQAPYSFDLSVMDLYPTLASGGTLVALPKDMTANFKQLFETLPQLPINVW 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1394 QATPATWKMLFYSGWENEEN-----VKILCGgEALP----ETLKRYFLDtgSEAWNMFGPTETTIwsAV------QRIND 1458
Cdd:PRK04813 239 VSTPSFADMCLLDPSFNEEHlpnltHFLFCG-EELPhktaKKLLERFPS--ATIYNTYGPTEATV--AVtsieitDEMLD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1459 ECSRATIGRPIANTQIYITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDnpfEPGSKLYRTGDMARwLPGG 1538
Cdd:PRK04813 314 QYKRLPIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFFT---FDGQPAYHTGDAGY-LEDG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1539 RIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADM-----DNLAAYYTAKH----ANASLTaRELRHFVKNA 1609
Cdd:PRK04813 390 LLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYNkdhkvQYLIAYVVPKEedfeREFELT-KAIKKELKER 468
|
490 500 510
....*....|....*....|....*....|.
gi 1776025254 1610 LPAYMVPSYFIQLDHMPLTPNGKIDRNSLKN 1640
Cdd:PRK04813 469 LMEYMIPRKFIYRDSLPLTPNGKIDRKALIE 499
|
|
| omega_3_PfaA |
TIGR02813 |
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ... |
3340-3881 |
3.42e-85 |
|
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this alignment are involved in omega-3 polyunsaturated fatty acid biosynthesis, such as the protein PfaA from the eicosapentaenoic acid biosynthesis operon in Photobacterium profundum strain SS9. PfaA is encoded together with PfaB, PfaC, and PfaD, and the functions of the individual polypeptides have not yet been described. More distant homologs of PfaA, also included with the reach of this model, appear to be involved in polyketide-like biosynthetic mechanisms of polyunsaturated fatty acid biosynthesis, an alternative to the more familiar iterated mechanism of chain extension and desaturation, and in most cases are encoded near genes for homologs of PfaB, PfaC, and/or PfaD.
Pssm-ID: 274311 [Multi-domain] Cd Length: 2582 Bit Score: 315.02 E-value: 3.42e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3340 PVAIVGISGRFPGAMDIDEFWKNLEEGKDSITEVPKDRWDWREHYGNPDTDVNKTDIKWGGFIDGVaEFDPLFFGISPRE 3419
Cdd:TIGR02813 8 PIAIVGMASIFANSRYLNKFWDLIFEKIDAITDVPSDHWAKDDYYDSDKSEADKSYCKRGGFLPEV-DFNPMEFGLPPNI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3420 ADYVDPQQRLLMTYVWKALEDAGCPpQSLSGTGTGIFIGTG-----------------------NTGYKDL--------F 3468
Cdd:TIGR02813 87 LELTDISQLLSLVVAKEVLNDAGLP-DGYDRDKIGITLGVGggqkqssslnarlqypvlkkvfkASGVEDEdsemlikkF 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3469 HRANLPIEGHAATGhMIPSVGPNRMSYFLNIHGPSEPVETACSSSLVAIHRAVTAMQNGDCEMAIAGGVNTILTEEAHIS 3548
Cdd:TIGR02813 166 QDQYIHWEENSFPG-SLGNVISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGGVCTDNSPFMYMS 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3549 YSKAGMLSKDGRCKTFSADANGYVRGEGVGMVMLKKLEDAERDGNHIYGVIRGTAENHGGRANTLTSPNPKAQADLLVRA 3628
Cdd:TIGR02813 245 FSKTPAFTTNEDIQPFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGKFKSIYAPRPEGQAKALKRA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3629 YRQAGIDPSTVTYIEAHGTGTELGDPIEINGLKAAFkelsnmrgeSQPDVPDHRCGIGSVKSNIGHLELAAGISGLIKVL 3708
Cdd:TIGR02813 325 YDDAGFAPHTCGLIEAHGTGTAAGDVAEFGGLVSVF---------SQDNDQKQHIALGSVKSQIGHTKSTAGTAGMIKAV 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3709 LQMKHKTLVKSLHCETLNPYLQLTDSPFYIVQEKQEWKSVTDcdgnELPRRAGISSFGIGGVNAHIVIEEYMPKA--NSE 3786
Cdd:TIGR02813 396 LALHHKVLPPTINVDQPNPKLDIENSPFYLNTETRPWMQRED----GTPRRAGISSFGFGGTNFHMVLEEYSPKHqrDDQ 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3787 HTATEQPNVIVLSAKNKSRLIDRASQLLEAIrNKKYTDQGLHRIAYTLQVGREEMD---ERLACVAGTMQELEEKL-QAF 3862
Cdd:TIGR02813 472 YRQRAVAQTLLFTAANEKALVSSLKDWKNKL-SAKADDQPYAFNALAVENTLRTIAvalARLGFVAKNADELITMLeQAI 550
|
570 580
....*....|....*....|..
gi 1776025254 3863 VDGKEETDEFFR---GQSHRNK 3881
Cdd:TIGR02813 551 TQLEAKSCEEWQlpsGISYRKS 572
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
4588-4820 |
7.44e-79 |
|
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains. The N-terminal domain contains most of the structures involved in dimer formation and also the active site cysteine.
Pssm-ID: 425468 [Multi-domain] Cd Length: 251 Bit Score: 262.57 E-value: 7.44e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4588 EGIAVVGLSCRFPGAETLESYWSLLSEGRSSIGPIPAERWGCKTPYY------------AGVIDGVSYFDPDFFLLHEED 4655
Cdd:pfam00109 1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIPADRWDPDKLYDppsriagkiytkWGGLDDIFDFDPLFFGISPRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4656 VRAMDPQALLVLEECLKLLYHAGYTPEEIKGKPVGVYIGGRSQHKPDEDSLDHAKNP------IVTVGQNYLAANLSQFF 4729
Cdd:pfam00109 81 AERMDPQQRLLLEAAWEALEDAGITPDSLDGSRTGVFIGSGIGDYAALLLLDEDGGPrrgspfAVGTMPSVIAGRISYFL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4730 DVRGPSVVVDTACSSALVGMNMAIQALRGGDIQSAIVGGVSLLSSDASHRLFDRRGILSKHSSFHVFDERADGVVLGEGV 4809
Cdd:pfam00109 161 GLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSPDGPCKAFDPFADGFVRGEGV 240
|
250
....*....|.
gi 1776025254 4810 GMVMLKTVKQA 4820
Cdd:pfam00109 241 GAVVLKRLSDA 251
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
1760-2009 |
5.80e-77 |
|
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains. The N-terminal domain contains most of the structures involved in dimer formation and also the active site cysteine.
Pssm-ID: 425468 [Multi-domain] Cd Length: 251 Bit Score: 256.79 E-value: 5.80e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1760 DSVAIIGISCEFPGAKNHDEFWENLRDGKESIAFFNKE--ELQRFGISKEIAENADYVPAKAsIEGKDRFDPSFFQISPK 1837
Cdd:pfam00109 1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIPADrwDPDKLYDPPSRIAGKIYTKWGG-LDDIFDFDPLFFGISPR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1838 DAEFMDPQLRMLLTHSWKAIEDAGYAAGQI--PQTSVFMSASNNSYRALLPSDTTESLEtpDGYVSWVLAQSGTIPTMIS 1915
Cdd:pfam00109 80 EAERMDPQQRLLLEAAWEALEDAGITPDSLdgSRTGVFIGSGIGDYAALLLLDEDGGPR--RGSPFAVGTMPSVIAGRIS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1916 HKLGLRGPSYFVHANCSSSLIGLHSAYKSLLSAESDYALVGGATLHTESNIGYVHQPGLNFSSDGHIKAFDASADGMIGG 1995
Cdd:pfam00109 158 YFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSPDGPCKAFDPFADGFVRG 237
|
250
....*....|....
gi 1776025254 1996 EGVAVVLLKKAADA 2009
Cdd:pfam00109 238 EGVGAVVLKRLSDA 251
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
188-550 |
6.52e-75 |
|
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341228 [Multi-domain] Cd Length: 336 Bit Score: 254.52 E-value: 6.52e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 188 DLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDHVGGIGmLHLRDVYLGCQeinvsseTILM 267
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLF-GLLGALLAGGT-------VVLL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 268 E---PLKWLDWIDHYRASVTWAPNFAFGLVTDFAEEikdRKWDLSSMRYMLNGGEAMVAKVGRRILELLEPhglpadAIR 344
Cdd:cd04433 73 PkfdPEAALELIEREKVTILLGVPTLLARLLKAPES---AGYDLSSLRALVSGGAPLPPELLERFEEAPGI------KLV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 345 PAWGMSETSSGVIFSheftrAGTSDDDHFVEIGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGYYQRPDLNESV 424
Cdd:cd04433 144 NGYGLTETGGTVATG-----PPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 425 FtEDGWFETGDLGFLR-NGRLTITGRTKDAIIINGINYYSHAIESAVEELSEIetsytAACAV------RLGQnstdQLA 497
Cdd:cd04433 219 D-EDGWYRTGDLGRLDeDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGV-----AEAAVvgvpdpEWGE----RVV 288
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1776025254 498 IFFVTsaklnDEQMSQLLRNIQSHVSQVIG--VTPEYLLPVqkEEIPKTAIGKIQ 550
Cdd:cd04433 289 AVVVL-----RPGADLDAEELRAHVRERLApyKVPRRVVFV--DALPRTASGKID 336
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
909-1775 |
8.90e-74 |
|
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.
Pssm-ID: 274582 [Multi-domain] Cd Length: 1389 Bit Score: 274.63 E-value: 8.90e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 909 EDTYTRRLSSgfmnqvRMFAKEHSVNVTTVFLSCYMMLLGRYTGQKEQIVGmpamVRPEERFDDAIghflnmlpIRSELN 988
Cdd:TIGR03443 28 EATYSLQLPS------AEVTAGGGSTPFIILLAAFAALVYRLTGDEDIVLG----TSSNKSGRPFV--------LRLNIT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 989 PADTFSSFISKLQLTILDGLDHAAYPFPKMVRDLNIP-RSQAGSPVFQTAFFYQNFLQSgsyqsllSRYADFFSVDYVEY 1067
Cdd:TIGR03443 90 PELSFLQLYAKVSEEEKEGASDIGVPFDELSEHIQAAkKLERTPPLFRLAFQDAPDNQQ-------TTYSTGSTTDLTVF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1068 IHQEGEyelvfelweteeKMELNIKYNTGLFDAASISAMFDHFVYVTEQAMLNPSQPLKEYSLLPEAEKQMI------LK 1141
Cdd:TIGR03443 163 LTPSSP------------ELELSIYYNSLLFSSDRITIVADQLAQLLSAASSNPDEPIGKVSLITPSQKSLLpdptkdLD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1142 TWNATGktypyiTFHELFEQQAKKTPDRAAV---------SYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDR 1212
Cdd:TIGR03443 231 WSGFRG------AIHDIFADNAEKHPDRTCVvetpsfldpSSKTRSFTYKQINEASNILAHYLLKTGIKRGDVVMIYAYR 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1213 SLDMLVGLLAILKAGGAYVPLDPSYPAER--------------------------LEYMLEDSEVFITLTTSELVNTLSw 1266
Cdd:TIGR03443 305 GVDLVVAVMGVLKAGATFSVIDPAYPPARqtiylsvakpraliviekagtldqlvRDYIDKELELRTEIPALALQDDGS- 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1267 ngVTTALLDQDWDEIAQTASDRKVlTRT---VTPENLAYVIYTSGSTGKPKGVMIPHKALTNFLVSMGETPGLTAEDKML 1343
Cdd:TIGR03443 384 --LVGGSLEGGETDVLAPYQALKD-TPTgvvVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFGLSENDKFT 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1344 AVTTYCFDIAALELFLPLIKGAHCYICQTEHTKDVEKLKRDIRTIKPTVMQATPATWKML--------------FYSGwe 1409
Cdd:TIGR03443 461 MLSGIAHDPIQRDMFTPLFLGAQLLVPTADDIGTPGRLAEWMAKYGATVTHLTPAMGQLLsaqattpipslhhaFFVG-- 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1410 neenvKILcggealpetLKRYFLDTGSEA-----WNMFGPTETTiwSAVQ------RINDECSRATI------GRPIANT 1472
Cdd:TIGR03443 539 -----DIL---------TKRDCLRLQTLAenvciVNMYGTTETQ--RAVSyfeipsRSSDSTFLKNLkdvmpaGKGMKNV 602
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1473 QIYITD----SQLAPVpaGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPF-EPGS---------------------KLY 1526
Cdd:TIGR03443 603 QLLVVNrndrTQTCGV--GEVGEIYVRAGGLAEGYLGLPELNAEKFVNNWFvDPSHwidldkennkperefwlgprdRLY 680
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1527 RTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECV--VVADMDN---LAAYYTAKHANASLTA-- 1599
Cdd:TIGR03443 681 RTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVtlVRRDKDEeptLVSYIVPQDKSDELEEfk 760
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1600 -----------------------RELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLKNIDLSGEQLKQRQTSPk 1656
Cdd:TIGR03443 761 sevddeessdpvvkglikyrkliKDIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKPALPFPDTAQLAAVAKNRSA- 839
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1657 NIQDTVFT--------IWQEVL--KTSDIEWDDGFFDVGGDSLLAVTVADRIKHELSCEFSVTDLFEYSTIKNISQYITE 1726
Cdd:TIGR03443 840 SAADEEFTetereirdLWLELLpnRPATISPDDSFFDLGGHSILATRMIFELRKKLNVELPLGLIFKSPTIKGFAKEVDR 919
|
970 980 990 1000 1010
....*....|....*....|....*....|....*....|....*....|.
gi 1776025254 1727 -QRMGNASDHMPTdppahIEDQSTEMSDLpDYYDDSVAII-GISCEFPGAK 1775
Cdd:TIGR03443 920 lKKGEELADEGDS-----EIEEEETVLEL-DYAKDAKTLVdSLPKSYPSRK 964
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
33-553 |
1.22e-73 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 258.39 E-value: 1.22e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 33 EVLYRTAAelGDTKGIIYLQPDGtEVYQSYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNSQLLPAFWGCVLTGVV-- 110
Cdd:PRK07768 6 EKMYANAR--TSPRGMVTGEPDA-PVRHTWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASlt 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 111 ----PAPLAVPPTYAESSsgtqklKDAWTLLDKPAVITDrgmhqEMLDWAKEQgLE--GFRAIIVEDLLSAEAdTDWHQS 184
Cdd:PRK07768 83 mlhqPTPRTDLAVWAEDT------LRVIGMIGAKAVVVG-----EPFLAAAPV-LEekGIRVLTVADLLAADP-IDPVET 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 185 SPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTRE-DITFNWMPFDH-VGGIGMLHLrDVYLGCQEINVSS 262
Cdd:PRK07768 150 GEDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVEtDVMVSWLPLFHdMGMVGFLTV-PMYFGAELVKVTP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 263 ETILMEPLKWLDWIDHYRASVTWAPNFAFGLVTD-FAEEIKDRKWDLSSMRYMLNGGEAMVAKVGRRILELLEPHGLPAD 341
Cdd:PRK07768 229 MDFLRDPLLWAELISKYRGTMTAAPNFAYALLARrLRRQAKPGAFDLSSLRFALNGAEPIDPADVEDLLDAGARFGLRPE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 342 AIRPAWGMSETSSGVIFSHEFT----------------RAGTSDDDH---FVEIGSPIPGFSMRIVNDHNELVEEGEIGR 402
Cdd:PRK07768 309 AILPAYGMAEATLAVSFSPCGAglvvdevdadllaalrRAVPATKGNtrrLATLGPPLPGLEVRVVDEDGQVLPPRGVGV 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 403 FQVSGLSVTSGYYQrPDLNESVFTEDGWFETGDLGFL-RNGRLTITGRTKDAIIINGINYYSHAIESAVEELSEIETSyt 481
Cdd:PRK07768 389 IELRGESVTPGYLT-MDGFIPAQDADGWLDTGDLGYLtEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVRPG-- 465
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1776025254 482 AACAVRL-GQNSTDQLAIFFVTSAKLNDEQMSQLLRNIQSHVSQVIGVTPEYLLPVQKEEIPKTAIGKIQRTQ 553
Cdd:PRK07768 466 NAVAVRLdAGHSREGFAVAVESNAFEDPAEVRRIRHQVAHEVVAEVGVRPRNVVVLGPGSIPKTPSGKLRRAN 538
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
1157-1639 |
8.95e-72 |
|
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341259 [Multi-domain] Cd Length: 468 Bit Score: 250.17 E-value: 8.95e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1157 ELFEQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGP-DRLAgIYVDRSLDMLVGLLAILKAGGAYVPLDP 1235
Cdd:cd05936 3 DLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPgDRVA-LMLPNCPQFPIAYFGALKAGAVVVPLNP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1236 SYPAERLEYMLEDSevfitlttselvntlswnGVTTALLDQDWDEIAQTASdRKVLTRTVTPENLAYVIYTSGSTGKPKG 1315
Cdd:cd05936 82 LYTPRELEHILNDS------------------GAKALIVAVSFTDLLAAGA-PLGERVALTPEDVAVLQYTSGTTGVPKG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1316 VMIPHKALT-NFLVSMG-ETPGLTAEDKMLAVT----TYCFDIAaleLFLPLIKGAHCYIcqtEHTKDVEKLKRDIRTIK 1389
Cdd:cd05936 143 AMLTHRNLVaNALQIKAwLEDLLEGDDVVLAALplfhVFGLTVA---LLLPLALGATIVL---IPRFRPIGVLKEIRKHR 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1390 PTVMQATPATWKMLFYSGWENEENVK----ILCGGEALPETLKRYFLD-TGSEAWNMFGPTETTIWSAVQRINDECSRAT 1464
Cdd:cd05936 217 VTIFPGVPTMYIALLNAPEFKKRDFSslrlCISGGAPLPVEVAERFEElTGVPIVEGYGLTETSPVVAVNPLDGPRKPGS 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1465 IGRPIANTQIYITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPFepgsklyRTGDMARWLPGGRIEYIG 1544
Cdd:cd05936 297 IGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVDGWL-------RTGDIGYMDEDGYFFIVD 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1545 RIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMDNLA-----AYYTAKHaNASLTARELRHFVKNALPAYMVPSYF 1619
Cdd:cd05936 370 RKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSgeavkAFVVLKE-GASLTEEEIIAFCREQLAGYKVPRQV 448
|
490 500
....*....|....*....|
gi 1776025254 1620 IQLDHMPLTPNGKIDRNSLK 1639
Cdd:cd05936 449 EFRDELPKSAVGKILRRELR 468
|
|
| KR |
pfam08659 |
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ... |
2849-3034 |
6.18e-70 |
|
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.
Pssm-ID: 430138 [Multi-domain] Cd Length: 180 Bit Score: 233.99 E-value: 6.18e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2849 GVYLITGGAGSLGLLFAKEIANRtGRSTIVLTGRSVLS-EDKENELEALRSIGAEVVYREADVSDQHAVHHLFEEIKERY 2927
Cdd:pfam08659 1 GTYLITGGLGGLGRELARWLAER-GARHLVLLSRSAAPrPDAQALIAELEARGVEVVVVACDVSDPDAVAALLAEIKAEG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2928 GTLNGIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSGLLHVDECSKDFPLDFFIFFSSVSGCLGNAGQADYAAANSFMDAF 3007
Cdd:pfam08659 80 PPIRGVIHAAGVLRDALLENMTDEDWRRVLAPKVTGTWNLHEATPDEPLDFFVLFSSIAGLLGSPGQANYAAANAFLDAL 159
|
170 180
....*....|....*....|....*..
gi 1776025254 3008 AEYRRSLAAskkrfgSTISFNWPLWEE 3034
Cdd:pfam08659 160 AEYRRSQGL------PATSINWGPWAE 180
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
1167-1638 |
1.44e-69 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 243.15 E-value: 1.44e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1167 PDRAAVS-YEGQ---TLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERL 1242
Cdd:cd17654 1 PDRPALIiDQTTsdtTVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1243 EYMLEDSEVFITLTTSELVNTlswngvttalldqdwdeiAQTASDRKVLTRTVTPENLAYVIYTSGSTGKPKGVMIPHKA 1322
Cdd:cd17654 81 LTVMKKCHVSYLLQNKELDNA------------------PLSFTPEHRHFNIRTDECLAYVIHTSGTTGTPKIVAVPHKC 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1323 LTNFLVSMGETPGLTAEDKMLAVTTYCFDIAALELFLPLIKGAHCYICQTEHTKDVEKLKRDIRTI-KPTVMQATPATWK 1401
Cdd:cd17654 143 ILPNIQHFRSLFNITSEDILFLTSPLTFDPSVVEIFLSLSSGATLLIVPTSVKVLPSKLADILFKRhRITVLQATPTLFR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1402 MLFYSGWENE-----ENVKILC-GGEALP-----ETLKRYFLDTgsEAWNMFGPTETTIWSAVQRINDECSRATIGRPIA 1470
Cdd:cd17654 223 RFGSQSIKSTvlsatSSLRVLAlGGEPFPslvilSSWRGKGNRT--RIFNIYGITEVSCWALAYKVPEEDSPVQLGSPLL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1471 NTQIYITDSQlapvPAGVPGELciAGDGVAKGYYKKEELTdsrfidnpfEPGSKLYRTGDMARwLPGGRIEYIGRIDNQV 1550
Cdd:cd17654 301 GTVIEVRDQN----GSEGTGQV--FLGGLNRVCILDDEVT---------VPKGTMRATGDFVT-VKDGELFFLGRKDSQI 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1551 KIRGFRIELGDIESRLSEHPGILECVV-VADMDNLAAYYTAKhanaSLTARELRHFVKNALPAYMVPSYFIQLDHMPLTP 1629
Cdd:cd17654 365 KRRGKRINLDLIQQVIESCLGVESCAVtLSDQQRLIAFIVGE----SSSSRIHKELQLTLLSSHAIPDTFVQIDKLPLTS 440
|
....*....
gi 1776025254 1630 NGKIDRNSL 1638
Cdd:cd17654 441 HGKVDKSEL 449
|
|
| PKS_KR |
smart00822 |
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ... |
2849-3034 |
5.13e-69 |
|
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.
Pssm-ID: 214833 [Multi-domain] Cd Length: 180 Bit Score: 231.22 E-value: 5.13e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2849 GVYLITGGAGSLGLLFAKEIANRTGRsTIVLTGRSVLSEDKENEL-EALRSIGAEVVYREADVSDQHAVHHLFEEIKERY 2927
Cdd:smart00822 1 GTYLITGGLGGLGRALARWLAERGAR-RLVLLSRSGPDAPGAAALlAELEAAGARVTVVACDVADRDALAAVLAAIPAVE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2928 GTLNGIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSGLLHVDECSKDFPLDFFIFFSSVSGCLGNAGQADYAAANSFMDAF 3007
Cdd:smart00822 80 GPLTGVIHAAGVLDDGVLASLTPERFAAVLAPKAAGAWNLHELTADLPLDFFVLFSSIAGVLGSPGQANYAAANAFLDAL 159
|
170 180
....*....|....*....|....*..
gi 1776025254 3008 AEYRRSLAaskkrfGSTISFNWPLWEE 3034
Cdd:smart00822 160 AEYRRARG------LPALSIAWGAWAE 180
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
1300-1634 |
3.01e-68 |
|
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341228 [Multi-domain] Cd Length: 336 Bit Score: 235.26 E-value: 3.01e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1300 LAYVIYTSGSTGKPKGVMIPHKALTNFLVSMGETPGLTAEDKMLAVTTYCFDIAALELFLPLIKGAHCYIcqtEHTKDVE 1379
Cdd:cd04433 2 PALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVL---LPKFDPE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1380 KLKRDIRTIKPTVMQATPATWKMLFYSGWENEEN----VKILCGGEALPETLKRYFLD-TGSEAWNMFGPTETTIWSAVQ 1454
Cdd:cd04433 79 AALELIEREKVTILLGVPTLLARLLKAPESAGYDlsslRALVSGGAPLPPELLERFEEaPGIKLVNGYGLTETGGTVATG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1455 RINDECSRA-TIGRPIANTQIYITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNpfepgskLYRTGDMAR 1533
Cdd:cd04433 159 PPDDDARKPgSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVDEDG-------WYRTGDLGR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1534 WLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVA----DMDNLAAYYTAKHANASLTARELRHFVKNA 1609
Cdd:cd04433 232 LDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGvpdpEWGERVVAVVVLRPGADLDAEELRAHVRER 311
|
330 340
....*....|....*....|....*
gi 1776025254 1610 LPAYMVPSYFIQLDHMPLTPNGKID 1634
Cdd:cd04433 312 LAPYKVPRRVVFVDALPRTASGKID 336
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
3340-3776 |
5.20e-63 |
|
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible for the elongation steps in fatty acid biosynthesis. KASIII catalyses the initial condensation and KAS I and II catalyze further elongation steps by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP.
Pssm-ID: 238430 [Multi-domain] Cd Length: 406 Bit Score: 222.80 E-value: 5.20e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3340 PVAIVGISGRFPGAMDIDEFWKNLEEGKDSITEVPKDrwdwrehygnpdtDVNKTDIKWGGFIDGVAEFDPlffgISPRE 3419
Cdd:cd00834 2 RVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRF-------------DASGFPSRIAGEVPDFDPEDY----LDRKE 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3420 ADYVDPQQRLLMTYVWKALEDAGCPPQSLSGTGTGIFIGTGNTGYKDL--FHRANLPIEGHAATGHMIPSVGPNRMSYF- 3496
Cdd:cd00834 65 LRRMDRFAQFALAAAEEALADAGLDPEELDPERIGVVIGSGIGGLATIeeAYRALLEKGPRRVSPFFVPMALPNMAAGQv 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3497 ---LNIHGPSEPVETACSSSLVAIHRAVTAMQNGDCEMAIAGGVNTILTEEAHISYSKAGMLSKDG-----RCKTFSADA 3568
Cdd:cd00834 145 airLGLRGPNYTVSTACASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALRALSTRNddpekASRPFDKDR 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3569 NGYVRGEGVGMVMLKKLEDAERDGNHIYGVIRGTAENhgGRANTLTSPNPKAQADLLV--RAYRQAGIDPSTVTYIEAHG 3646
Cdd:cd00834 225 DGFVLGEGAGVLVLESLEHAKARGAKIYAEILGYGAS--SDAYHITAPDPDGEGAARAmrAALADAGLSPEDIDYINAHG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3647 TGTELGDPIEINGLKAAFkelsnmrGESQPDVPdhrcgIGSVKSNIGHLELAAGISGLIKVLLQMKHKTLVKSLHCETLN 3726
Cdd:cd00834 303 TSTPLNDAAESKAIKRVF-------GEHAKKVP-----VSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPD 370
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1776025254 3727 PYLQLTdspfYIVQEKQEWksvtdcdgnelPRRAGIS-SFGIGGVNAHIVI 3776
Cdd:cd00834 371 PECDLD----YVPNEAREA-----------PIRYALSnSFGFGGHNASLVF 406
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
1150-1639 |
6.19e-63 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 226.22 E-value: 6.19e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1150 YPYITFHELFEQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGP-DRLAgiYVDR-SLDMLVGLLAILKAG 1227
Cdd:PRK06187 3 DYPLTIGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKgDRVA--VFDWnSHEYLEAYFAVPKIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1228 GAYVPLDPSYPAERLEYMLEDSEVFITLTTSELVNTLS-----------------WNGVTTALLDQDWDEIAQTASDRKV 1290
Cdd:PRK06187 81 AVLHPINIRLKPEEIAYILNDAEDRVVLVDSEFVPLLAailpqlptvrtvivegdGPAAPLAPEVGEYEELLAAASDTFD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1291 lTRTVTPENLAYVIYTSGSTGKPKGVMIPHKALTNFLVSMGETPGLTAEDKMLAVTTyCFDIAALEL-FLPLIKGA---- 1365
Cdd:PRK06187 161 -FPDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVP-MFHVHAWGLpYLALMAGAkqvi 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1366 -HCYicqtehtkDVEKLKRDIRTIKPTVMQATPATWKMLF---------YSGWEneenvKILCGGEALPETLKRYFLDTG 1435
Cdd:PRK06187 239 pRRF--------DPENLLDLIETERVTFFFAVPTIWQMLLkaprayfvdFSSLR-----LVIYGGAALPPALLREFKEKF 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1436 S----EAWNMfgpTETTIWSAVQRINDECS-----RATIGRPIANTQIYITDSQLAPVPA--GVPGELCIAGDGVAKGYY 1504
Cdd:PRK06187 306 GidlvQGYGM---TETSPVVSVLPPEDQLPgqwtkRRSAGRPLPGVEARIVDDDGDELPPdgGEVGEIIVRGPWLMQGYW 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1505 KKEELTDSRFIDNpfepgskLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMDNL 1584
Cdd:PRK06187 383 NRPEATAETIDGG-------WLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEK 455
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1585 A-----AYYTAKhANASLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLK 1639
Cdd:PRK06187 456 WgerpvAVVVLK-PGATLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLR 514
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
1159-1635 |
2.13e-62 |
|
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.
Pssm-ID: 341286 [Multi-domain] Cd Length: 435 Bit Score: 222.10 E-value: 2.13e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1159 FEQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGP-DRLAgIYVDRSLDMLVGLLAILKAGGAYVPLDPSY 1237
Cdd:cd17631 1 LRRRARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKgDRVA-VLSKNSPEFLELLFAAARLGAVFVPLNFRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1238 PAERLEYMLEDSEvfitlttselvntlswngvTTALLDQdwdeiaqtasdrkvltrtvtpenLAYVIYTSGSTGKPKGVM 1317
Cdd:cd17631 80 TPPEVAYILADSG-------------------AKVLFDD-----------------------LALLMYTSGTTGRPKGAM 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1318 IPHKALTNFLVSMGETPGLTAEDKMLAVTTYcFDIAALELFLP--LIKGAHCYICqteHTKDVEKLKRDIRTIKPTVMQA 1395
Cdd:cd17631 118 LTHRNLLWNAVNALAALDLGPDDVLLVVAPL-FHIGGLGVFTLptLLRGGTVVIL---RKFDPETVLDLIERHRVTSFFL 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1396 TPATWKMLFYSGWENEENV----KILCGGEALPETLKRYFLDTGSEAWNMFGPTETTIWSAVQRINDECSRA-TIGRPIA 1470
Cdd:cd17631 194 VPTMIQALLQHPRFATTDLsslrAVIYGGAPMPERLLRALQARGVKFVQGYGMTETSPGVTFLSPEDHRRKLgSAGRPVF 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1471 NTQIYITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPFepgsklyRTGDMARWLPGGRIEYIGRIDNQV 1550
Cdd:cd17631 274 FVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFRDGWF-------HTGDLGRLDEDGYLYIVDRKKDMI 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1551 KIRGFRIELGDIESRLSEHPGILECVVVADMDNL-----AAYYTAKhANASLTARELRHFVKNALPAYMVPSYFIQLDHM 1625
Cdd:cd17631 347 ISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKwgeavVAVVVPR-PGAELDEDELIAHCRERLARYKIPKSVEFVDAL 425
|
490
....*....|
gi 1776025254 1626 PLTPNGKIDR 1635
Cdd:cd17631 426 PRNATGKILK 435
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
3341-3779 |
9.93e-62 |
|
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism]; 3-oxoacyl-(acyl-carrier-protein) synthase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440073 [Multi-domain] Cd Length: 409 Bit Score: 219.20 E-value: 9.93e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3341 VAIVGISGRFPGAMDIDEFWKNLEEGKDSITEVPKDrwdwrehygnpdtDVNKTDIKWGGFIDGvaeFDPLFFgISPREA 3420
Cdd:COG0304 3 VVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITRF-------------DASGLPVRIAGEVKD---FDPEEY-LDRKEL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3421 DYVDPQQRLLMTYVWKALEDAGCPPQSLSGTGTGIFIGTGNTG-------YKDLFHRANLPIEGHAATGhMIPSVGPNRM 3493
Cdd:COG0304 66 RRMDRFTQYALAAAREALADAGLDLDEVDPDRTGVIIGSGIGGldtleeaYRALLEKGPRRVSPFFVPM-MMPNMAAGHV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3494 SYFLNIHGPSEPVETACSSSLVAIHRAVTAMQNGDCEMAIAGGVNTILTEEAHISYSKAGMLSK-----DGRCKTFSADA 3568
Cdd:COG0304 145 SIRFGLKGPNYTVSTACASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLAGFDALGALSTrnddpEKASRPFDKDR 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3569 NGYVRGEGVGMVMLKKLEDAERDGNHIYGVIRGTAENHGGRANTLTSPNPKAQADLLVRAYRQAGIDPSTVTYIEAHGTG 3648
Cdd:COG0304 225 DGFVLGEGAGVLVLEELEHAKARGAKIYAEVVGYGASSDAYHITAPAPDGEGAARAMRAALKDAGLSPEDIDYINAHGTS 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3649 TELGDPIEINGLKAAFkelsnmrGESQPDVPdhrcgIGSVKSNIGHLELAAGISGLIKVLLQMKHKTLVKSLHCETLNPY 3728
Cdd:COG0304 305 TPLGDAAETKAIKRVF-------GDHAYKVP-----VSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPE 372
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1776025254 3729 LQLTdspfYIVQEKQewksvtdcdgnELPRRAGIS-SFGIGGVNAHIVIEEY 3779
Cdd:COG0304 373 CDLD----YVPNEAR-----------EAKIDYALSnSFGFGGHNASLVFKRY 409
|
|
| PS-DH |
pfam14765 |
Polyketide synthase dehydratase; This is the dehydratase domain of polyketide synthases. ... |
2373-2658 |
1.08e-61 |
|
Polyketide synthase dehydratase; This is the dehydratase domain of polyketide synthases. Structural analysis shows these DH domains are double hotdogs in which the active site contains a histidine from the N-terminal hotdog and an aspartate from the C-terminal hotdog. Studies have uncovered that a substrate tunnel formed between the DH domains may be essential for loading substrates and unloading products.
Pssm-ID: 434191 Cd Length: 296 Bit Score: 214.93 E-value: 1.08e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2373 HPLL-HQNTS-DFSEQKFSSVFTGDEF-FLRDHVVRGKPVLPGVAYLEMAYAAINQAAGSEIG---QDVRIRlnhtvwvQ 2446
Cdd:pfam14765 1 HPLLgSRVPSpSDLEPVWRNRLRLADLpWLRDHRVGGTVVLPGAGYLEMALEAARQLFGGSGAvalRDVSIL-------K 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2447 PVVVDRHSA-QVDISLFPEEDG---KITFDIYSTQEDGDDPVIHSQGSAELASAAETPVADLTEISRRC----GKGKMSP 2518
Cdd:pfam14765 74 ALVLPEDDPvEVQTSLTPEEDGadsWWEFEIFSRAGGGWEWTLHATGTVRLAPGEPAAPVDLESLPARCaqpaDPRSVSS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2519 DQFYEEGRSRGMFHGPAFQGIKNVNIGNREVLAQLQLPEIVSGTNEQFVLHPSIMDSALQT-ATICIMQELTDQKLILPF 2597
Cdd:pfam14765 154 AEFYERLAARGLFYGPAFQGLRRIWRGDGEALAEARLPEAAAGGESPYLLHPALLDAALQLlGAALPAEAEHADQAYLPV 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1776025254 2598 ALEELEVIKG--CSSSMWAYARLSDSDHSGGVvqkADIDVIDESGSVCVRIKGFSTRVLEGEV 2658
Cdd:pfam14765 234 GIERLRIYRSlpPGEPLWVHARLERRGGRTIV---GDLTLVDEDGRVVARIEGLRLRRVEREA 293
|
|
| KR_2_FAS_SDR_x |
cd08955 |
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 2, complex (x); ... |
2817-3079 |
1.36e-60 |
|
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 2, complex (x); Ketoreductase, a module of the multidomain polyketide synthase, has 2 subdomains, each corresponding to a short-chain dehydrogenases/reductase (SDR) family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerizes but is composed of 2 subdomains, each resembling an SDR monomer. In some instances, as in porcine FAS, an enoyl reductase (a Rossman fold NAD binding domain of the MDR family) module is inserted between the sub-domains. The active site resembles that of typical SDRs, except that the usual positions of the catalytic asparagine and tyrosine are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular polyketide synthases are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) fatty acid synthase. In some instances, such as porcine FAS , an enoyl reductase module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consists of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthesis uses dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-ketoacyl reductase (KR), forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-enoyl reductase (ER). Polyketide syntheses also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes the KR domain of the Lyngbya majuscule Jam J, -K, and #L which are encoded on the jam gene cluster and are involved in the synthesis of the Jamaicamides (neurotoxins); Lyngbya majuscule Jam P belongs to a different KR_FAS_SDR_x subfamily. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.
Pssm-ID: 187658 [Multi-domain] Cd Length: 376 Bit Score: 214.84 E-value: 1.36e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2817 QIRYEAGHRFV---KGWRemvlpsadtlHMPWRDEGVYLITGGAGSLGLLFAKEIANRtGRSTIVLTGRSVLSEDKENEL 2893
Cdd:cd08955 125 QVALRGGARYVarlVRAP----------ARPLRPDATYLITGGLGGLGLLVAEWLVER-GARHLVLTGRRAPSAAARQAI 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2894 EALRSIGAEVVYREADVSDQHAVHHLFEEIKERYGTLNGIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSGLLHVDECSKD 2973
Cdd:cd08955 194 AALEEAGAEVVVLAADVSDRDALAAALAQIRASLPPLRGVIHAAGVLDDGVLANQDWERFRKVLAPKVQGAWNLHQLTQD 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2974 FPLDFFIFFSSVSGCLGNAGQADYAAANSFMDAFAEYRRS--LAAskkrfgstISFNWPLWEEGGMQVGAEDEKRmLKTT 3051
Cdd:cd08955 274 LPLDFFVLFSSVASLLGSPGQANYAAANAFLDALAHYRRArgLPA--------LSINWGPWAEVGMAASLARQAR-LEAR 344
|
250 260
....*....|....*....|....*...
gi 1776025254 3052 GMVPMPTDSGLKAFYQGIASDKPQVFVM 3079
Cdd:cd08955 345 GVGAISPAAGLQALGQLLRTGSTQVGVA 372
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
35-456 |
5.94e-60 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 214.10 E-value: 5.94e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 35 LYRTAAELGDTkgiIYLQPDGTEVYqSYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNSQLLPAFWGCVLTGVVPAPl 114
Cdd:pfam00501 1 LERQAARTPDK---TALEVGEGRRL-TYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVP- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 115 aVPPTYAESSSGTQkLKDAwtllDKPAVITDRGMHQEMLDWAKEQGLEGFRAIIV--------EDLLSAEADTDWHQS-- 184
Cdd:pfam00501 76 -LNPRLPAEELAYI-LEDS----GAKVLITDDALKLEELLEALGKLEVVKLVLVLdrdpvlkeEPLPEEAKPADVPPPpp 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 185 ---SPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQ----GFTREDITFNWMPFDHVGGIGMLHLRDVYLGCQe 257
Cdd:pfam00501 150 pppDPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRprgfGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGAT- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 258 INVSSETILMEPLKWLDWIDHYRASVTWAPNFAFGLVTDFAEEikdRKWDLSSMRYMLNGGEAMVAKVGRRILELLephg 337
Cdd:pfam00501 229 VVLPPGFPALDPAALLELIERYKVTVLYGVPTLLNMLLEAGAP---KRALLSSLRLVLSGGAPLPPELARRFRELF---- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 338 lpADAIRPAWGMSETSSGVIFS----HEFTRAGTsdddhfveIGSPIPGFSMRIVNDH-NELVEEGEIGRFQVSGLSVTS 412
Cdd:pfam00501 302 --GGALVNGYGLTETTGVVTTPlpldEDLRSLGS--------VGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMK 371
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1776025254 413 GYYQRPDLNESVFTEDGWFETGDLG-FLRNGRLTITGRTKDAIII 456
Cdd:pfam00501 372 GYLNDPELTAEAFDEDGWYRTGDLGrRDEDGYLEIVGRKKDQIKL 416
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
1157-1639 |
3.82e-59 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 215.15 E-value: 3.82e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1157 ELFEQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGP-DRLAgIYVDRSLDMLVGLLAILKAGGAYVPLDP 1235
Cdd:PRK07656 9 ELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKgDRVA-IWAPNSPHWVIAALGALKAGAVVVPLNT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1236 SYPAERLEYMLEDSEVFITLTTSEL-----------------VNTLSWNGVTTALLDQDWDEIAQTASDRKVlTRTVTPE 1298
Cdd:PRK07656 88 RYTADEAAYILARGDAKALFVLGLFlgvdysattrlpalehvVICETEEDDPHTEKMKTFTDFLAAGDPAER-APEVDPD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1299 NLAYVIYTSGSTGKPKGVMIPHKALTNFLVSMGETPGLTAEDKMLAVT----TYCFDIAALElflPLIKGAHCYIcqtEH 1374
Cdd:PRK07656 167 DVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAANpffhVFGYKAGVNA---PLMRGATILP---LP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1375 TKDVEKLKRDIRTIKPTVMQATPATWKMLFYSGWENEENVKILC----GGEALPETLKRYF-----LDTGSEAwnmFGPT 1445
Cdd:PRK07656 241 VFDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRlavtGAASMPVALLERFeselgVDIVLTG---YGLS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1446 ETTIWSAVQRIND--ECSRATIGRPIANTQIYITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTdSRFIDnpfePGS 1523
Cdd:PRK07656 318 EASGVTTFNRLDDdrKTVAGTIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEAT-AAAID----ADG 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1524 KLYrTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVV--VADmDNLA----AYYTAKHAnASL 1597
Cdd:PRK07656 393 WLH-TGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVigVPD-ERLGevgkAYVVLKPG-AEL 469
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1776025254 1598 TARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLK 1639
Cdd:PRK07656 470 TEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRALR 511
|
|
| KR_FAS_SDR_x |
cd05274 |
ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of ... |
2770-3079 |
6.42e-59 |
|
ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. In some instances, such as porcine FAS, an enoyl reductase (ER) module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consist of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthase uses a dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-KR, forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-ER. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.
Pssm-ID: 187582 [Multi-domain] Cd Length: 375 Bit Score: 209.93 E-value: 6.42e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2770 AGVSGLLKTAEIEFSKLTAQVIEIEKPEEMIDLHLKLKDDSQRPFDKQIRYEAGHRFVKGWREMVLPSADTLHMPWRDEG 2849
Cdd:cd05274 72 AALWGLLRVLALEHPELWGGLVDLDAADAADEAAALAALLAGAPGEDELALRGGQRLVPRLVRAPAAALELAAAPGGLDG 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGLLFAKEIANRTGRsTIVLTGRSVLSEDKENELEALRSIGAEVVYREADVSDQHAVHHLFEEIkERYGT 2929
Cdd:cd05274 152 TYLITGGLGGLGLLVARWLAARGAR-HLVLLSRRGPAPRAAARAALLRAGGARVSVVRCDVTDPAALAALLAEL-AAGGP 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2930 LNGIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSGLLHVDECSKDFPLDFFIFFSSVSGCLGNAGQADYAAANSFMDAFAE 3009
Cdd:cd05274 230 LAGVIHAAGVLRDALLAELTPAAFAAVLAAKVAGALNLHELTPDLPLDFFVLFSSVAALLGGAGQAAYAAANAFLDALAA 309
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3010 YRRSLAaskkrfGSTISFNWPLWEEGGMqVGAEDEKRMLKTTGMVPMPTDSGLKAFYQGIASDKPQVFVM 3079
Cdd:cd05274 310 QRRRRG------LPATSVQWGAWAGGGM-AAAAALRARLARSGLGPLAPAEALEALEALLASDAPQAVVA 372
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
1156-1653 |
1.30e-58 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 214.98 E-value: 1.30e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1156 HELFEQQAKKTPDRAAVSYEG-----QTLTYRELDERSTQLAIYLQAHGVGP-DRLAgIYVDRSLDMLVGLLAILKAGGA 1229
Cdd:COG0365 12 YNCLDRHAEGRGDKVALIWEGedgeeRTLTYAELRREVNRFANALRALGVKKgDRVA-IYLPNIPEAVIAMLACARIGAV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1230 YVPLDPSYPAERLEYMLEDSE--VFIT---------------------LTTSELVNTLSWNGVTTALL---DQDWDEIAQ 1283
Cdd:COG0365 91 HSPVFPGFGAEALADRIEDAEakVLITadgglrggkvidlkekvdealEELPSLEHVIVVGRTGADVPmegDLDWDELLA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1284 TASDrkvltrTVTPENL-----AYVIYTSGSTGKPKGVMIPHKA-LTNFLVSMGETPGLTAEDKMLAVTT--------YC 1349
Cdd:COG0365 171 AASA------EFEPEPTdaddpLFILYTSGTTGKPKGVVHTHGGyLVHAATTAKYVLDLKPGDVFWCTADigwatghsYI 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1350 fdiaaleLFLPLIKGAHCYICQ-TEHTKDVEKLKRDIRTIKPTVMQATPATWKMLFYSGwenEENVK---------ILCG 1419
Cdd:COG0365 245 -------VYGPLLNGATVVLYEgRPDFPDPGRLWELIEKYGVTVFFTAPTAIRALMKAG---DEPLKkydlsslrlLGSA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1420 GEAL-PETLKRYFLDTGSEAWNMFGPTETT-IWSAVQRInDECSRATIGRPIANTQIYITDSQLAPVPAGVPGELCIAGD 1497
Cdd:COG0365 315 GEPLnPEVWEWWYEAVGVPIVDGWGQTETGgIFISNLPG-LPVKPGSMGKPVPGYDVAVVDEDGNPVPPGEEGELVIKGP 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1498 --GVAKGYYKKEEltdsRFIDNPFEPGSKLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILEC 1575
Cdd:COG0365 394 wpGMFRGYWNDPE----RYRETYFGRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEA 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1576 VVVA--DMDNLA---AYYTAK---HANASLtARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLKNIDLsGEQ 1647
Cdd:COG0365 470 AVVGvpDEIRGQvvkAFVVLKpgvEPSDEL-AKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKIAE-GRP 547
|
....*.
gi 1776025254 1648 LKQRQT 1653
Cdd:COG0365 548 LGDTST 553
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
56-563 |
2.26e-58 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 214.48 E-value: 2.26e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 56 TEVYqSYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNSQLLPAFWGCVLTGVVPAPLAVPPTYAESSSGTQKLKDAWT 135
Cdd:PRK09192 47 EEAL-PYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPLPMGFGGRESYIAQLRGMLA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 136 LLDKPAVITDrgmhQEMLDWAKE--QGLEGFRAIIVEDL-LSAEADTDWHQSSPEDLALLLLTSGSTGTPKAVMLNHRNI 212
Cdd:PRK09192 126 SAQPAAIITP----DELLPWVNEatHGNPLLHVLSHAWFkALPEADVALPRPTPDDIAYLQYSSGSTRFPRGVIITHRAL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 213 MSMVKGIIQMQGFTRE-DITFNWMPFDH-VGGIGMLHlrdVYLGCQeINV---SSETILMEPLKWLDWIDHYRASVTWAP 287
Cdd:PRK09192 202 MANLRAISHDGLKVRPgDRCVSWLPFYHdMGLVGFLL---TPVATQ-LSVdylPTRDFARRPLQWLDLISRNRGTISYSP 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 288 NFAFGLVTDFAEEIKDRKWDLSSMRYMLNGGEAMVAKVGRRILELLEPHGLPADAIRPAWGMSETSSGVIFS-------- 359
Cdd:PRK09192 278 PFGYELCARRVNSKDLAELDLSCWRVAGIGADMIRPDVLHQFAEAFAPAGFDDKAFMPSYGLAEATLAVSFSplgsgivv 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 360 HEFTRAGTSDDDH-------------FVEIGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGYYQRPDlNESVFT 426
Cdd:PRK09192 358 EEVDRDRLEYQGKavapgaetrrvrtFVNCGKALPGHEIEIRNEAGMPLPERVVGHICVRGPSLMSGYFRDEE-SQDVLA 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 427 EDGWFETGDLGFLRNGRLTITGRTKDAIIINGINYYSHAIESAVEELSEIETSYTAACAVrlgqNSTDQLAIFFVTSAKL 506
Cdd:PRK09192 437 ADGWLDTGDLGYLLDGYLYITGRAKDLIIINGRNIWPQDIEWIAEQEPELRSGDAAAFSI----AQENGEKIVLLVQCRI 512
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1776025254 507 NDEQMSQLLRN-IQSHVSQVIGVTPEYLLpVQKEEIPKTAIGKIQRTQLKTSFENGEF 563
Cdd:PRK09192 513 SDEERRGQLIHaLAALVRSEFGVEAAVEL-VPPHSLPRTSSGKLSRAKAKKRYLSGAF 569
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
1154-1639 |
2.34e-58 |
|
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.
Pssm-ID: 211788 [Multi-domain] Cd Length: 517 Bit Score: 212.72 E-value: 2.34e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1154 TFHELFEQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPL 1233
Cdd:TIGR03098 1 LLHHLLEDAAARLPDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1234 DPSYPAERLEYMLEDSEVFITLTTSELVNTLSWNGVTTALLDQ--------------------DWDEiAQTASDRKVLTR 1293
Cdd:TIGR03098 81 NPLLKAEQVAHILADCNVRLLVTSSERLDLLHPALPGCHDLRTliivgdpahaseghpgeepaSWPK-LLALGDADPPHP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1294 tVTPENLAYVIYTSGSTGKPKGVMIPHKALTNFLVSMGETPGLTAEDKMLAVTTYCFDIAALELFLPLIKGAHCYICQTE 1373
Cdd:TIGR03098 160 -VIDSDMAAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPLSFDYGFNQLTTAFYVGATVVLHDYL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1374 HTKDVEKL--KRDIrtikpTVMQATPATWKMLFYSGWENE--ENVKILC--GGEALPET---LKRYFLDTgsEAWNMFGP 1444
Cdd:TIGR03098 239 LPRDVLKAleKHGI-----TGLAAVPPLWAQLAQLDWPESaaPSLRYLTnsGGAMPRATlsrLRSFLPNA--RLFLMYGL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1445 TE----TTIWSA-VQRINDecsraTIGRPIANTQIYITD---SQLAPvpaGVPGELCIAGDGVAKGYYKKEELTDSRFID 1516
Cdd:TIGR03098 312 TEafrsTYLPPEeVDRRPD-----SIGKAIPNAEVLVLRedgSECAP---GEEGELVHRGALVAMGYWNDPEKTAERFRP 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1517 NP-FEPGSKLYRT----GDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMD-----NLAA 1586
Cdd:TIGR03098 384 LPpFPGELHLPELavwsGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAFGVPDptlgqAIVL 463
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1776025254 1587 YYTAKhANASLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLK 1639
Cdd:TIGR03098 464 VVTPP-GGEELDRAALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKALA 515
|
|
| PKS_KR |
smart00822 |
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ... |
4172-4368 |
1.32e-57 |
|
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.
Pssm-ID: 214833 [Multi-domain] Cd Length: 180 Bit Score: 198.48 E-value: 1.32e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4172 VLLITGGTRGIGLLCARHFAECyGVKKLVLTGREQLPPREEWArfktsntslaekiqAVRELEAKGVQVEMLSLTLSDDA 4251
Cdd:smart00822 2 TYLITGGLGGLGRALARWLAER-GARRLVLLSRSGPDAPGAAA--------------LLAELEAAGARVTVVACDVADRD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4252 QVEQTLQHIKRTLGPIGGVIHCAGLTDMDTLAfiRKTSDDIQRVMEPKVSGLTTLYRHVCNEPLQFFVLFSSVSAIIPel 4331
Cdd:smart00822 67 ALAAVLAAIPAVEGPLTGVIHAAGVLDDGVLA--SLTPERFAAVLAPKAAGAWNLHELTADLPLDFFVLFSSIAGVLG-- 142
|
170 180 190
....*....|....*....|....*....|....*...
gi 1776025254 4332 SAGQADYAMANSYMDYFAEAHQKHV-PIISVQWPNWKE 4368
Cdd:smart00822 143 SPGQANYAAANAFLDALAEYRRARGlPALSIAWGAWAE 180
|
|
| KR_FAS_SDR_x |
cd05274 |
ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of ... |
4056-4411 |
3.01e-56 |
|
ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. In some instances, such as porcine FAS, an enoyl reductase (ER) module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consist of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthase uses a dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-KR, forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-ER. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.
Pssm-ID: 187582 [Multi-domain] Cd Length: 375 Bit Score: 202.23 E-value: 3.01e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4056 VQRLVEFGHKEGLRLLCVTKGLESFQNTSVRMAGASR-AGLYRMLQCEYSHLISRHMDAEEVTDHPRLAKLiADEFYSES 4134
Cdd:cd05274 37 VAALLAAYASTGPPLWLVTRGAEAVSADDVAALAQAAlWGLLRVLALEHPELWGGLVDLDAADAADEAAAL-AALLAGAP 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4135 YDAEVCYRDGLRYQSFLKAHPETGkATEQSAVFPKDHVLLITGGTRGIGLLCARHFAECyGVKKLVLTGREQLPPREEWA 4214
Cdd:cd05274 116 GEDELALRGGQRLVPRLVRAPAAA-LELAAAPGGLDGTYLITGGLGGLGLLVARWLAAR-GARHLVLLSRRGPAPRAAAR 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4215 rfktsntslaekiqaVRELEAKGVQVEMLSLTLSDDAQVEQTLQHIkRTLGPIGGVIHCAGLTDMDTLAFIrkTSDDIQR 4294
Cdd:cd05274 194 ---------------AALLRAGGARVSVVRCDVTDPAALAALLAEL-AAGGPLAGVIHAAGVLRDALLAEL--TPAAFAA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4295 VMEPKVSGLTTLYRHVCNEPLQFFVLFSSVSAIIpeLSAGQADYAMANSYMDYFAEA-HQKHVPIISVQWPNWKETGMG- 4372
Cdd:cd05274 256 VLAAKVAGALNLHELTPDLPLDFFVLFSSVAALL--GGAGQAAYAAANAFLDALAAQrRRRGLPATSVQWGAWAGGGMAa 333
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1776025254 4373 -EVTNQAYRESGLFSITNSEGLRFLDQIVSKMFG-PVVLPA 4411
Cdd:cd05274 334 aAALRARLARSGLGPLAPAEALEALEALLASDAPqAVVASV 374
|
|
| C_PKS-NRPS |
cd20483 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
695-1111 |
9.56e-56 |
|
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHXXXD motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380471 [Multi-domain] Cd Length: 430 Bit Score: 202.49 E-value: 9.56e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 695 PLSEVQKGLWTLQKMSPEKSAYHVPLCFKFSSGLHLETLQQAFGLVLNQHPILKHVIQEKDGVPILKNEPALSIEIKTEN 774
Cdd:cd20483 3 PMSTFQRRLWFLHNFLEDKTFLNLLLVCHIKGKPDVNLLQKALSELVRRHEVLRTAYFEGDDFGEQQVLDDPSFHLIVID 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 775 ISSMK--ESDIPAFLRKKVKEPYVKENSPLVRVMSFSRSEQEHFLLVVIHHLIFDGVSSVTFIHSLFDTYQLLLKgQQPE 852
Cdd:cd20483 83 LSEAAdpEAALDQLVRNLRRQELDIEEGEVIRGWLVKLPDEEFALVLASHHIAWDRGSSKSIFEQFTALYDALRA-GRDL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 853 IAVSP--AIYHDFAAWEKNMLAGKDGVKHRTYWQKQLSG---TLPNLQLPKVSASSVSEFREDTYTRRLSSGFMNQVRMF 927
Cdd:cd20483 162 ATVPPppVQYIDFTLWHNALLQSPLVQPLLDFWKEKLEGipdASKLLPFAKAERPPVKDYERSTVEATLDKELLARMKRI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 928 AKEHSVnvtTVF---LSCYMMLLGRYTGQKEQIVGMPAMVRPEERFDDAIGHFLNMLPIRSELNPADTFSSFISKLQLTI 1004
Cdd:cd20483 242 CAQHAV---TPFmflLAAFRAFLYRYTEDEDLTIGMVDGDRPHPDFDDLVGFFVNMLPIRCRMDCDMSFDDLLESTKTTC 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1005 LDGLDHAAYPFPKMVRDLNIPRSQAGSPVFQTAFFYQnflQSGSYQSllSRYADFfsvDYVEYIHQEGE--YELVFELWE 1082
Cdd:cd20483 319 LEAYEHSAVPFDYIVDALDVPRSTSHFPIGQIAVNYQ---VHGKFPE--YDTGDF---KFTDYDHYDIPtaCDIALEAEE 390
|
410 420 430
....*....|....*....|....*....|
gi 1776025254 1083 TEEK-MELNIKYNTGLFDAASISAMFDHFV 1111
Cdd:cd20483 391 DPDGgLDLRLEFSTTLYDSADMERFLDNFV 420
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
31-555 |
8.75e-55 |
|
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341259 [Multi-domain] Cd Length: 468 Bit Score: 200.87 E-value: 8.75e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 31 IPEVLYRTAAELGDTKGIIylqpdGTEVYQSYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNSQLLPAFWGCVLTGVV 110
Cdd:cd05936 1 LADLLEEAARRFPDKTALI-----FMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 111 PAPLAvpPTYaesssgtqklkdawtlldkpaviTDRGMHQEMLDwakeqglEGFRAIIV----EDLLSAEADTD-WHQSS 185
Cdd:cd05936 76 VVPLN--PLY-----------------------TPRELEHILND-------SGAKALIVavsfTDLLAAGAPLGeRVALT 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 186 PEDLALLLLTSGSTGTPKAVMLNHRNIMS---MVKGIIQmQGFTREDITFNWMPFDHVGGIGMLHLRDVYLGCQEINVSS 262
Cdd:cd05936 124 PEDVAVLQYTSGTTGVPKGAMLTHRNLVAnalQIKAWLE-DLLEGDDVVLAALPLFHVFGLTVALLLPLALGATIVLIPR 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 263 etilMEPLKWLDWIDHYRASV-TWAPNFAFGLVTDFAeeikDRKWDLSSMRYMLNGGEAMVAKVGRRILELLephGLPad 341
Cdd:cd05936 203 ----FRPIGVLKEIRKHRVTIfPGVPTMYIALLNAPE----FKKRDFSSLRLCISGGAPLPVEVAERFEELT---GVP-- 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 342 aIRPAWGMSETSSGVIFSH--EFTRAGTsdddhfveIGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGYYQRPD 419
Cdd:cd05936 270 -IVEGYGLTETSPVVAVNPldGPRKPGS--------IGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPE 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 420 LNESVFTeDGWFETGDLGFL-RNGRLTITGRTKDAIIINGINYYSHAIESAVEELSEIetsytAACAVrLG---QNSTDQ 495
Cdd:cd05936 341 ETAEAFV-DGWLRTGDIGYMdEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAV-----AEAAV-VGvpdPYSGEA 413
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1776025254 496 LAIFFV--TSAKLNDEQMSQLLRniqSHVsqvigvtPEYLLPVQ---KEEIPKTAIGKIQRTQLK 555
Cdd:cd05936 414 VKAFVVlkEGASLTEEEIIAFCR---EQL-------AGYKVPRQvefRDELPKSAVGKILRRELR 468
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
61-550 |
4.64e-54 |
|
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341237 [Multi-domain] Cd Length: 486 Bit Score: 199.36 E-value: 4.64e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 61 SYRRLWDDGLRIVKGLRQSGLKaKQSVILQLGDNS-QLLPAFWGCVLTGVVPAPLAvpPTYAESSSGTQkLKDAwtlldK 139
Cdd:cd05911 12 TYAQLRTLSRRLAAGLRKLGLK-KGDVVGIISPNStYYPPVFLGCLFAGGIFSAAN--PIYTADELAHQ-LKIS-----K 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 140 P-AVITDRGMHQEMLDWAKEQG---------LEGFRAIIVEDLLSAEA-DTDWHQ-----SSPEDLALLLLTSGSTGTPK 203
Cdd:cd05911 83 PkVIFTDPDGLEKVKEAAKELGpkdkiivldDKPDGVLSIEDLLSPTLgEEDEDLppplkDGKDDTAAILYSSGTTGLPK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 204 AVMLNHRNIMSMvkgIIQMQGFT-----REDITFNWMPFDHVGGIGMLHLRdVYLGCqeinvssETILM---EPLKWLDW 275
Cdd:cd05911 163 GVCLSHRNLIAN---LSQVQTFLygndgSNDVILGFLPLYHIYGLFTTLAS-LLNGA-------TVIIMpkfDSELFLDL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 276 IDHYRASVTWA--PNFAFglvtdFAEEIKDRKWDLSSMRYMLNGGeamvAKVGRRILELLEPHgLPADAIRPAWGMSETS 353
Cdd:cd05911 232 IEKYKITFLYLvpPIAAA-----LAKSPLLDKYDLSSLRVILSGG----APLSKELQELLAKR-FPNATIKQGYGMTETG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 354 SGVIFSHEFtragtsdDDHFVEIGSPIPGFSMRIVNDH-NELVEEGEIGRFQVSGLSVTSGYYQRPDLNESVFTEDGWFE 432
Cdd:cd05911 302 GILTVNPDG-------DDKPGSVGRLLPNVEAKIVDDDgKDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGWLH 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 433 TGDLGFLR-NGRLTITGRTKDAIIINGINYYSHAIESAVEELSEIETsytaACAVRLGQNSTDQLAIFFVTSAKlnDEQM 511
Cdd:cd05911 375 TGDIGYFDeDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVAD----AAVIGIPDEVSGELPRAYVVRKP--GEKL 448
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1776025254 512 S--QLLRNIQSHVSQ-------VIGVtpeyllpvqkEEIPKTAIGKIQ 550
Cdd:cd05911 449 TekEVKDYVAKKVASykqlrggVVFV----------DEIPKSASGKIL 486
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
1762-2183 |
9.95e-54 |
|
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible for the elongation steps in fatty acid biosynthesis. KASIII catalyses the initial condensation and KAS I and II catalyze further elongation steps by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP.
Pssm-ID: 238430 [Multi-domain] Cd Length: 406 Bit Score: 195.84 E-value: 9.95e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1762 VAIIGISCEFPGAKNHDEFWENLRDGKESIAffnkeELQRFGISKEIAENADYVPAkasiegkdrFDPSFFqISPKDAEF 1841
Cdd:cd00834 3 VVITGLGAVTPLGNGVEEFWEALLAGRSGIR-----PITRFDASGFPSRIAGEVPD---------FDPEDY-LDRKELRR 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1842 MDPQLRMLLTHSWKAIEDAGYAAGQIPQ--TSVFMSASNNSYRALLPSDTTeSLETPDGYVSWVL---AQSGTIPTMISH 1916
Cdd:cd00834 68 MDRFAQFALAAAEEALADAGLDPEELDPerIGVVIGSGIGGLATIEEAYRA-LLEKGPRRVSPFFvpmALPNMAAGQVAI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1917 KLGLRGPSYFVHANCSSSLIGLHSAYKSLLSAESDYALVGGA-TLHTESNIGyvhqpglNFSS--------DGHIKA--- 1984
Cdd:cd00834 147 RLGLRGPNYTVSTACASGAHAIGDAARLIRLGRADVVIAGGAeALITPLTLA-------GFAAlralstrnDDPEKAsrp 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1985 FDASADGMIGGEGVAVVLLKKAADAVKDGDHIYALLRGIGVNNDGADKVgfyAPSV--KGQADVVQQVMNQTKIHPESIC 2062
Cdd:cd00834 220 FDKDRDGFVLGEGAGVLVLESLEHAKARGAKIYAEILGYGASSDAYHIT---APDPdgEGAARAMRAALADAGLSPEDID 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2063 YVEAHGTGTKLGDPIELAALTNVYRQYTNKTQFCgigSVKTNIGHLDTAAGLAGCIKVVMSLYHQELAPSINYKEPNPNT 2142
Cdd:cd00834 297 YINAHGTSTPLNDAAESKAIKRVFGEHAKKVPVS---STKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPEC 373
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1776025254 2143 DLAsspfYVVDQkktlSREIQThRAALS-SFGLGGTNTHAIF 2183
Cdd:cd00834 374 DLD----YVPNE----AREAPI-RYALSnSFGFGGHNASLVF 406
|
|
| LCL_NRPS |
cd19538 |
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ... |
695-1121 |
2.66e-53 |
|
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.
Pssm-ID: 380461 [Multi-domain] Cd Length: 432 Bit Score: 195.56 E-value: 2.66e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 695 PLSEVQKGLWTLQKMSPEKSAYHVPLCFKFSSGLHLETLQQAFGLVLNQHPILKHVIQEKDGVP---ILkNEPALSIEIK 771
Cdd:cd19538 3 PLSFAQRRLWFLHQLEGPSATYNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVFPEEDGVPyqlIL-EEDEATPKLE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 772 TENISsmkESDIPAFLRKKVKEPYVKENSPLVRVMSFSRSEQEHFLLVVIHHLIFDGVSSVTFIHSLFDTYQLLLKGQQP 851
Cdd:cd19538 82 IKEVD---EEELESEINEAVRYPFDLSEEPPFRATLFELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYRARCKGEAP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 852 EIAVSPAIYHDFAAWEKNMLAGKDGVKHR-----TYWQKQLSGtLPN-LQLPK-VSASSVSEFREDTYTRRLSSGFMNQV 924
Cdd:cd19538 159 ELAPLPVQYADYALWQQELLGDESDPDSLiarqlAYWKKQLAG-LPDeIELPTdYPRPAESSYEGGTLTFEIDSELHQQL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 925 RMFAKEHSVNVTTVFLSCYMMLLGRYTGQKEQIVGMPAMVRPEERFDDAIGHFLNMLPIRSEL--NPadTFSSFISKLQL 1002
Cdd:cd19538 238 LQLAKDNNVTLFMVLQAGFAALLTRLGAGTDIPIGSPVAGRNDDSLEDLVGFFVNTLVLRTDTsgNP--SFRELLERVKE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1003 TILDGLDHAAYPFPKMVRDLNIPRSQAGSPVFQTAFFYQNFLQSgsyqSLlsryaDFFSVDYVEYIHQEG--EYELVFEL 1080
Cdd:cd19538 316 TNLEAYEHQDIPFERLVEALNPTRSRSRHPLFQIMLALQNTPQP----SL-----DLPGLEAKLELRTVGsaKFDLTFEL 386
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1776025254 1081 WE-----TEEKMELNIKYNTGLFDAASISAMFDHFVYVTEQAMLNP 1121
Cdd:cd19538 387 REqyndgTPNGIEGFIEYRTDLFDHETIEALAQRYLLLLESAVENP 432
|
|
| COG4908 |
COG4908 |
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ... |
696-939 |
2.78e-53 |
|
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];
Pssm-ID: 443936 [Multi-domain] Cd Length: 243 Bit Score: 188.71 E-value: 2.78e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 696 LSEVQKGLWtlqKMSPEKSAYHVPLCFKFSSGLHLETLQQAFGLVLNQHPILKHVIQEKDGVPILKNEPALSIEIKTENI 775
Cdd:COG4908 1 LSPAQKRFL---FLEPGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEEDGEPVQRIDPDADLPLEVVDL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 776 SSM----KESDIPAFLRKKVKEPYVKENSPLVRVMSFSRSEQEHFLLVVIHHLIFDGVSSVTFIHSLFDTYQLLLKGQQP 851
Cdd:COG4908 78 SALpepeREAELEELVAEEASRPFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALLEGEPP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 852 EIAVSPAIYHDFAAWEKNMLAGKDGVKHRTYWQKQLSGTLPNLQLPK-VSASSVSEFREDTYTRRLSSGFMNQVRMFAKE 930
Cdd:COG4908 158 PLPELPIQYADYAAWQRAWLQSEALEKQLEYWRQQLAGAPPVLELPTdRPRPAVQTFRGATLSFTLPAELTEALKALAKA 237
|
....*....
gi 1776025254 931 HSvnvTTVF 939
Cdd:COG4908 238 HG---ATVN 243
|
|
| omega_3_PfaA |
TIGR02813 |
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ... |
1759-2193 |
5.13e-53 |
|
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this alignment are involved in omega-3 polyunsaturated fatty acid biosynthesis, such as the protein PfaA from the eicosapentaenoic acid biosynthesis operon in Photobacterium profundum strain SS9. PfaA is encoded together with PfaB, PfaC, and PfaD, and the functions of the individual polypeptides have not yet been described. More distant homologs of PfaA, also included with the reach of this model, appear to be involved in polyketide-like biosynthetic mechanisms of polyunsaturated fatty acid biosynthesis, an alternative to the more familiar iterated mechanism of chain extension and desaturation, and in most cases are encoded near genes for homologs of PfaB, PfaC, and/or PfaD.
Pssm-ID: 274311 [Multi-domain] Cd Length: 2582 Bit Score: 208.71 E-value: 5.13e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1759 DDSVAIIGISCEFPGAKNHDEFWENLRDGKESIaffnkeelqrfgisKEIAEN----ADYVPAKASIEGKD--------- 1825
Cdd:TIGR02813 6 DMPIAIVGMASIFANSRYLNKFWDLIFEKIDAI--------------TDVPSDhwakDDYYDSDKSEADKSyckrggflp 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1826 --RFDPSFFQISPKDAEFMDPQLRMLLTHSWKAIEDA---------------GYAAGQIPQTSVFMSASNNSYRALLPSD 1888
Cdd:TIGR02813 72 evDFNPMEFGLPPNILELTDISQLLSLVVAKEVLNDAglpdgydrdkigitlGVGGGQKQSSSLNARLQYPVLKKVFKAS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1889 TTESLETP-------DGYVSWvlaQSGTIPTM--------ISHKLGLRGPSYFVHANCSSSLIGLHSAYKSLLSAESDYA 1953
Cdd:TIGR02813 152 GVEDEDSEmlikkfqDQYIHW---EENSFPGSlgnvisgrIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMM 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1954 LVGGATLHTESNIGYVHQPGLNFSSDGHIKAFDASADGMIGGEGVAVVLLKKAADAVKDGDHIYALLRGIGVNNDGADKv 2033
Cdd:TIGR02813 229 ITGGVCTDNSPFMYMSFSKTPAFTTNEDIQPFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGKFK- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2034 GFYAPSVKGQADVVQQVMNQTKIHPESICYVEAHGTGTKLGDPIELAALTNVYRQYTNKTQFCGIGSVKTNIGHLDTAAG 2113
Cdd:TIGR02813 308 SIYAPRPEGQAKALKRAYDDAGFAPHTCGLIEAHGTGTAAGDVAEFGGLVSVFSQDNDQKQHIALGSVKSQIGHTKSTAG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2114 LAGCIKVVMSLYHQELAPSINYKEPNPNTDLASSPFYVVDQKKT-LSREIQT-HRAALSSFGLGGTNTHAIFEQFKRDSD 2191
Cdd:TIGR02813 388 TAGMIKAVLALHHKVLPPTINVDQPNPKLDIENSPFYLNTETRPwMQREDGTpRRAGISSFGFGGTNFHMVLEEYSPKHQ 467
|
..
gi 1776025254 2192 KG 2193
Cdd:TIGR02813 468 RD 469
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
1762-2186 |
1.21e-52 |
|
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism]; 3-oxoacyl-(acyl-carrier-protein) synthase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440073 [Multi-domain] Cd Length: 409 Bit Score: 192.62 E-value: 1.21e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1762 VAIIGISCEFPGAKNHDEFWENLRDGKESIAFfnkeeLQRFGISKeiaenadyVPAKASIEGKDrFDPSFFqISPKDAEF 1841
Cdd:COG0304 3 VVITGLGAVSPLGNGVEEFWEALLAGRSGIRP-----ITRFDASG--------LPVRIAGEVKD-FDPEEY-LDRKELRR 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1842 MDPQLRMLLTHSWKAIEDAGYAAGQI--PQTSVFMSASNNSYRALLPSDTTESLETPDgYVS--WVLAQ-SGTIPTMISH 1916
Cdd:COG0304 68 MDRFTQYALAAAREALADAGLDLDEVdpDRTGVIIGSGIGGLDTLEEAYRALLEKGPR-RVSpfFVPMMmPNMAAGHVSI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1917 KLGLRGPSYFVHANCSSSLIGLHSAYKSLLSAESDYALVGGAtlhtESNIgyvHQPGLN-FSSdghIKA----------- 1984
Cdd:COG0304 147 RFGLKGPNYTVSTACASGAHAIGEAYRLIRRGRADVMIAGGA----EAAI---TPLGLAgFDA---LGAlstrnddpeka 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1985 ---FDASADGMIGGEGVAVVLLKKAADAVKDGDHIYALLRGIGVNNDGADKVGfYAPSVKGQADVVQQVMNQTKIHPESI 2061
Cdd:COG0304 217 srpFDKDRDGFVLGEGAGVLVLEELEHAKARGAKIYAEVVGYGASSDAYHITA-PAPDGEGAARAMRAALKDAGLSPEDI 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2062 CYVEAHGTGTKLGDPIELAALTNVYRQYTNKTQfcgIGSVKTNIGHLDTAAGLAGCIKVVMSLYHQELAPSINYKEPNPN 2141
Cdd:COG0304 296 DYINAHGTSTPLGDAAETKAIKRVFGDHAYKVP---VSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPE 372
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1776025254 2142 TDLAsspfYVVDQkktlSREIQThRAALS-SFGLGGTNTHAIFEQF 2186
Cdd:COG0304 373 CDLD----YVPNE----AREAKI-DYALSnSFGFGGHNASLVFKRY 409
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
3426-3776 |
3.17e-52 |
|
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new carbon-carbon bond by a decarboxylating Claisen-like condensation reaction. Members are involved in the synthesis of fatty acids and polyketides, a diverse group of natural products. Both pathways are an iterative series of additions of small carbon units, usually acetate, to a nascent acyl group. There are 2 classes of decarboxylating condensing enzymes, which can be distinguished by sequence similarity, type of active site residues and type of primer units (acetyl CoA or acyl carrier protein (ACP) linked units).
Pssm-ID: 238421 [Multi-domain] Cd Length: 332 Bit Score: 189.00 E-value: 3.17e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3426 QQRLLMTYVWKALEDAGCPPQSLSGTGTGIFIGTGNTGYKDLFHRAN--LPIEGHAATGHMIPSVGpNRMSYFLNIHGPS 3503
Cdd:cd00825 11 VSILGFEAAERAIADAGLSREYQKNPIVGVVVGTGGGSPRFQVFGADamRAVGPYVVTKAMFPGAS-GQIATPLGIHGPA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3504 EPVETACSSSLVAIHRAVTAMQNGDCEMAIAGGVNTILTEEAHISYSKAGMLSKDGRCKTFSADANGYVRGEGVGMVMLK 3583
Cdd:cd00825 90 YDVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAPMDCEFDAMGALSTPEKASRTFDAAADGFVFGDGAGALVVE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3584 KLEDAERDGNHIYGVIRGTAENHGGRANTLTSPNPKAQADLLVRAYRQAGIDPSTVTYIEAHGTGTELGDPIEINGLKAA 3663
Cdd:cd00825 170 ELEHALARGAHIYAEIVGTAATIDGAGMGAFAPSAEGLARAAKEALAVAGLTVWDIDYLVAHGTGTPIGDVKELKLLRSE 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3664 FKelsnmrgesqpdvpDHRCGIGSVKSNIGHLELAAGISGLIKVLLQMKHKTLVKSLHCETLNPYLQLTdspfyivqekq 3743
Cdd:cd00825 250 FG--------------DKSPAVSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPPSIHIEELDEAGLNI----------- 304
|
330 340 350
....*....|....*....|....*....|...
gi 1776025254 3744 ewksVTDCDGNElPRRAGISSFGIGGVNAHIVI 3776
Cdd:cd00825 305 ----VTETTPRE-LRTALLNGFGLGGTNATLVL 332
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
1167-1638 |
3.44e-52 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 194.66 E-value: 3.44e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1167 PDRAAV-------SYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPA 1239
Cdd:cd17647 2 PERTCVvetpslnSSKTRSFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1240 ERleymledSEVFITLTTSELVNTLSWNGVTtalldqdwdeiaqtasdrkvltrtVTPENLAYVIYTSGSTGKPKGVMIP 1319
Cdd:cd17647 82 AR-------QNIYLGVAKPRGLIVIRAAGVV------------------------VGPDSNPTLSFTSGSEGIPKGVLGR 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1320 HKALTNFLVSMGETPGLTAEDKMLAVTTYCFDIAALELFLPLIKGAHCYICQTEHTKDVEKLKRDIRTIKPTVMQATPAT 1399
Cdd:cd17647 131 HFSLAYYFPWMAKRFNLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTQDDIGTPGRLAEWMAKYGATVTHLTPAM 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1400 WKMLfySGWENEENVKILCG---GEALpetLKRYFLDTGSEA-----WNMFGPTET----TIWSAVQRINDEC----SRA 1463
Cdd:cd17647 211 GQLL--TAQATTPFPKLHHAffvGDIL---TKRDCLRLQTLAenvriVNMYGTTETqravSYFEVPSRSSDPTflknLKD 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1464 TI--GRPIANTQIYITD----SQLAPVpaGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPF-EPG-------------- 1522
Cdd:cd17647 286 VMpaGRGMLNVQLLVVNrndrTQICGI--GEVGEIYVRAGGLAEGYRGLPELNKEKFVNNWFvEPDhwnyldkdnnepwr 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1523 -------SKLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECV--VVADMDN---LAAYYTA 1590
Cdd:cd17647 364 qfwlgprDRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENItlVRRDKDEeptLVSYIVP 443
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1776025254 1591 KHANASLTA----------------------RELRH----FVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSL 1638
Cdd:cd17647 444 RFDKPDDESfaqedvpkevstdpivkgligyRKLIKdireFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKL 517
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
1154-1580 |
5.43e-52 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 196.09 E-value: 5.43e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1154 TFHELFEQQAKKTPDRAAVSY----EGQTLTYRELDERSTQLAIYLQAHGVGP-DRLAgIYVDRSLDMLVGLLAILKAGG 1228
Cdd:COG1022 12 TLPDLLRRRAARFPDRVALREkedgIWQSLTWAEFAERVRALAAGLLALGVKPgDRVA-ILSDNRPEWVIADLAILAAGA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1229 AYVPLDPSYPAERLEYMLEDSEV-FITLTTSELVNTLSwngvttALLDQ----------------------DWDEI---- 1281
Cdd:COG1022 91 VTVPIYPTSSAEEVAYILNDSGAkVLFVEDQEQLDKLL------EVRDElpslrhivvldprglrddprllSLDELlalg 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1282 AQTASDRKVLTR--TVTPENLAYVIYTSGSTGKPKGVMIPHKALTNFLVSMGETPGLTAEDKMLavttycfdiaaleLFL 1359
Cdd:COG1022 165 REVADPAELEARraAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTL-------------SFL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1360 PLikgAH------CYIC-----QTEHTKDVEKLKRDIRTIKPTVMQATPATW------------------KMLFYS---- 1406
Cdd:COG1022 232 PL---AHvfertvSYYAlaagaTVAFAESPDTLAEDLREVKPTFMLAVPRVWekvyagiqakaeeagglkRKLFRWalav 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1407 GWENEE---------------------------------NVKIL-CGGEALPETLKRYFLDTG---SEAWnmfGPTETTI 1449
Cdd:COG1022 309 GRRYARarlagkspslllrlkhaladklvfsklrealggRLRFAvSGGAALGPELARFFRALGipvLEGY---GLTETSP 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1450 WSAVQRiNDECSRATIGRPIANTQIYITDSqlapvpagvpGELCIAGDGVAKGYYKKEELTDSRFIDNPFepgsklYRTG 1529
Cdd:COG1022 386 VITVNR-PGDNRIGTVGPPLPGVEVKIAED----------GEILVRGPNVMKGYYKNPEATAEAFDADGW------LHTG 448
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1776025254 1530 DMARWLPGGRIEYIGRIDNQVKIR-GFRIELGDIESRLSEHPGILECVVVAD 1580
Cdd:COG1022 449 DIGELDEDGFLRITGRKKDLIVTSgGKNVAPQPIENALKASPLIEQAVVVGD 500
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
1169-1639 |
6.73e-51 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 188.44 E-value: 6.73e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1169 RAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLED 1248
Cdd:cd05919 1 KTAFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1249 SEvfitlttselvntlswngvtTALLDQDWDEIAqtasdrkvltrtvtpenlaYVIYTSGSTGKPKGVMIPHKALTNFLV 1328
Cdd:cd05919 81 CE--------------------ARLVVTSADDIA-------------------YLLYSSGTTGPPKGVMHAHRDPLLFAD 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1329 SMG-ETPGLTAEDKMLAVTTYCFDIA-ALELFLPLIKGAHCYICQTehTKDVEKLKRDIRTIKPTVMQATPATWKMLFYS 1406
Cdd:cd05919 122 AMArEALGLTPGDRVFSSAKMFFGYGlGNSLWFPLAVGASAVLNPG--WPTAERVLATLARFRPTVLYGVPTFYANLLDS 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1407 G-WENEENVKILC---GGEALPETLKRYFLDT-GSEAWNMFGPTETTIWSAVQRInDECSRATIGRPIANTQIYITDSQL 1481
Cdd:cd05919 200 CaGSPDALRSLRLcvsAGEALPRGLGERWMEHfGGPILDGIGATEVGHIFLSNRP-GAWRLGSTGRPVPGYEIRLVDEEG 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1482 APVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNpfepgskLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGD 1561
Cdd:cd05919 279 HTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFNGG-------WYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVE 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1562 IESRLSEHPGILECVVVA-----DMDNLAAYYTAK--HANASLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKID 1634
Cdd:cd05919 352 VESLIIQHPAVAEAAVVAvpestGLSRLTAFVVLKspAAPQESLARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQ 431
|
....*
gi 1776025254 1635 RNSLK 1639
Cdd:cd05919 432 RFKLR 436
|
|
| Ketoacyl-synt_C |
pfam02801 |
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
3596-3723 |
8.28e-51 |
|
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.
Pssm-ID: 426989 Cd Length: 118 Bit Score: 176.60 E-value: 8.28e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3596 YGVIRGTAENHGGRANTLTSPNPKAQADLLVRAYRQAGIDPSTVTYIEAHGTGTELGDPIEINGLKAAFkelsnmrgesQ 3675
Cdd:pfam02801 1 YAVIKGSAVNHDGRHNGLTAPNGEGQARAIRRALADAGVDPEDVDYVEAHGTGTPLGDPIEAEALKRVF----------G 70
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1776025254 3676 PDVPDHRCGIGSVKSNIGHLELAAGISGLIKVLLQMKHKTLVKSLHCE 3723
Cdd:pfam02801 71 SGARKQPLAIGSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLNLE 118
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
27-562 |
9.25e-51 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 190.40 E-value: 9.25e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 27 QPATIPEVLYRTAAELGDTKgIIYlqPDGTEVyqSYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNSQLLPAFWGCVL 106
Cdd:PRK06187 4 YPLTIGRILRHGARKHPDKE-AVY--FDGRRT--TYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 107 TGVVPAPLAVpptyaesssgtqKLKD---AWTLLDKPA--VITDRGmHQEMLDWAKEQgLEGFRAIIV------------ 169
Cdd:PRK06187 79 IGAVLHPINI------------RLKPeeiAYILNDAEDrvVLVDSE-FVPLLAAILPQ-LPTVRTVIVegdgpaaplape 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 170 ----EDLLSAEADT-DWHQSSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDHVGGIG 244
Cdd:PRK06187 145 vgeyEELLAAASDTfDFPDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPMFHVHAWG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 245 MLHLRdVYLGCQEINVSSetilMEPLKWLDWIDHYRasVTwapnFAFG---LVTDFAEEIKDRKWDLSSMRYMLNGG--- 318
Cdd:PRK06187 225 LPYLA-LMAGAKQVIPRR----FDPENLLDLIETER--VT----FFFAvptIWQMLLKAPRAYFVDFSSLRLVIYGGaal 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 319 -----EAMVAKVGRRILEllephglpadairpAWGMSETSSGVIFSH-------EFTRAGTSdddhfveiGSPIPGFSMR 386
Cdd:PRK06187 294 ppallREFKEKFGIDLVQ--------------GYGMTETSPVVSVLPpedqlpgQWTKRRSA--------GRPLPGVEAR 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 387 IVNDH-NEL-VEEGEIGRFQVSGLSVTSGYYQRPDLNESVFtEDGWFETGDLGFL-RNGRLTITGRTKDAIIINGINYYS 463
Cdd:PRK06187 352 IVDDDgDELpPDGGEVGEIIVRGPWLMQGYWNRPEATAETI-DGGWLHTGDVGYIdEDGYLYITDRIKDVIISGGENIYP 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 464 HAIESAVEELSEIetsytAACAVrLGQnsTDQ------LAifFVTSAKlnDEQMSQllRNIQSHVSQVIgvtPEYLLPVQ 537
Cdd:PRK06187 431 RELEDALYGHPAV-----AEVAV-IGV--PDEkwgerpVA--VVVLKP--GATLDA--KELRAFLRGRL---AKFKLPKR 493
|
570 580
....*....|....*....|....*...
gi 1776025254 538 ---KEEIPKTAIGKIQRTQLKTSFENGE 562
Cdd:PRK06187 494 iafVDELPRTSVGKILKRVLREQYAEGK 521
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
1168-1640 |
1.94e-50 |
|
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.
Pssm-ID: 341264 [Multi-domain] Cd Length: 442 Bit Score: 187.50 E-value: 1.94e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1168 DRAAVSYEGQTLTYRELDERSTQLAIYLQAHG-VGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYML 1246
Cdd:cd05941 1 DRIAIVDDGDSITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1247 EDSEVfitlttselvntlswngvtTALLDqdwdeiaqtasdrkvltrtvtpenLAYVIYTSGSTGKPKGVMIPHKALTNF 1326
Cdd:cd05941 81 TDSEP-------------------SLVLD------------------------PALILYTSGTTGRPKGVVLTHANLAAN 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1327 LVSMGETPGLTAEDKMLAVttycfdiaaLELF----------LPLIKGAHCyICQTEHTKDVEKLKRDIRTIK-----PT 1391
Cdd:cd05941 118 VRALVDAWRWTEDDVLLHV---------LPLHhvhglvnallCPLFAGASV-EFLPKFDPKEVAISRLMPSITvfmgvPT 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1392 V----MQATPATWKMLFYSGWENEENVKIL-CGGEALPE-TLKRYFLDTGSEAWNMFGPTETTIwSAVQRINDECSRATI 1465
Cdd:cd05941 188 IytrlLQYYEAHFTDPQFARAAAAERLRLMvSGSAALPVpTLEEWEAITGHTLLERYGMTEIGM-ALSNPLDGERRPGTV 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1466 GRPIANTQIYITDSQLA-PVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPFepgsklYRTGDMARWLPGGRIEYIG 1544
Cdd:cd05941 267 GMPLPGVQARIVDEETGePLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGW------FKTGDLGVVDEDGYYWILG 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1545 RI-DNQVKIRGFRIELGDIESRLSEHPGILECVVV--ADMD---NLAAYYTAKHANASLTARELRHFVKNALPAYMVPSY 1618
Cdd:cd05941 341 RSsVDIIKSGGYKVSALEIERVLLAHPGVSECAVIgvPDPDwgeRVVAVVVLRAGAAALSLEELKEWAKQRLAPYKRPRR 420
|
490 500
....*....|....*....|..
gi 1776025254 1619 FIQLDHMPLTPNGKIDRNSLKN 1640
Cdd:cd05941 421 LILVDELPRNAMGKVNKKELRK 442
|
|
| C_NRPS-like |
cd19066 |
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ... |
695-1121 |
2.68e-50 |
|
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long, with various activities such as antibiotic, antifungal, antitumor and immunosuppression. There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380453 [Multi-domain] Cd Length: 427 Bit Score: 186.46 E-value: 2.68e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 695 PLSEVQKGLWTLQKMSPEKSAYHVPLCFKFSSGLHLETLQQAFGLVLNQHPILKHVIQEKDGVP---ILKNEPALSIEIK 771
Cdd:cd19066 3 PLSPMQRGMWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEEAGRYeqvVLDKTVRFRIEII 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 772 TENISSMKESDIPAFLRKKVKEPYVKENSPLVRVMSFSRSEQEHFLLVVIHHLIFDGVSSVTFIHSLFDTYQLLLKgQQP 851
Cdd:cd19066 83 DLRNLADPEARLLELIDQIQQTIYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDAAER-QKP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 852 EIAVSPAIYHDFAAWEKNMLAGKDGVKHRTYWQKQLSGTLPNLQLPKVSASSvsefREDTYTRR-----LSSGFMNQVRM 926
Cdd:cd19066 162 TLPPPVGSYADYAAWLEKQLESEAAQADLAYWTSYLHGLPPPLPLPKAKRPS----QVASYEVLtleffLRSEETKRLRE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 927 FAKEHSVNVTTVFLSCYMMLLGRYTGQKEQIVGMPAMVRPEERFDDAIGHFLNMLPIRSELNPADTFSSFISKLQLTILD 1006
Cdd:cd19066 238 VARESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDEAVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKEQSRE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1007 GLDHAAYPFPKMVRDLNIPRSQAGSPVFQTAF-FYQNFLQSGSYQSllsryadfFSVDYVEYIHQEG-EYELVFELWETE 1084
Cdd:cd19066 318 AIEHQRVPFIELVRHLGVVPEAPKHPLFEPVFtFKNNQQQLGKTGG--------FIFTTPVYTSSEGtVFDLDLEASEDP 389
|
410 420 430
....*....|....*....|....*....|....*...
gi 1776025254 1085 EK-MELNIKYNTGLFDAASISAMFDHFVYVTEQAMLNP 1121
Cdd:cd19066 390 DGdLLLRLEYSRGVYDERTIDRFAERYMTALRQLIENP 427
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1176-1639 |
4.60e-50 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 185.57 E-value: 4.60e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1176 GQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLEDSEVFITL 1255
Cdd:cd05934 1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1256 TTselvntlswngvttalldqdwdeiaqtasdrkvltrtvtpenLAYVIYTSGSTGKPKGVMIPHKALTNFLVSMGETPG 1335
Cdd:cd05934 81 VD------------------------------------------PASILYTSGTTGPPKGVVITHANLTFAGYYSARRFG 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1336 LTAEDKMLAVTTYcFDIAALEL-FLP-LIKGAHCYICQTEHTKdveKLKRDIRTIKPTVMQATPATWKMLfYSGWENEEN 1413
Cdd:cd05934 119 LGEDDVYLTVLPL-FHINAQAVsVLAaLSVGATLVLLPRFSAS---RFWSDVRRYGATVTNYLGAMLSYL-LAQPPSPDD 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1414 ----VKILCGGEALPETLKRYFLDTGSEAWNMFGPTETTIwsAVQRINDECSRA-TIGRPIANTQIYITDSQLAPVPAGV 1488
Cdd:cd05934 194 rahrLRAAYGAPNPPELHEEFEERFGVRLLEGYGMTETIV--GVIGPRDEPRRPgSIGRPAPGYEVRIVDDDGQELPAGE 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1489 PGELCI---AGDGVAKGYYKKEELTDSRFIDNpfepgskLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESR 1565
Cdd:cd05934 272 PGELVIrglRGWGFFKGYYNMPEATAEAMRNG-------WFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERA 344
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1776025254 1566 LSEHPGILECVVVADMDNL-----AAYYTAKHAnASLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLK 1639
Cdd:cd05934 345 ILRHPAVREAAVVAVPDEVgedevKAVVVLRPG-ETLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
1175-1633 |
5.24e-50 |
|
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341237 [Multi-domain] Cd Length: 486 Bit Score: 187.42 E-value: 5.24e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1175 EGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLEDSEVFIT 1254
Cdd:cd05911 7 TGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1255 LTTSEL----------------VNTLSWNGVTTALLDQDWDEIAQTASDRKVLTRTVTPENLAYVIYTSGSTGKPKGVMI 1318
Cdd:cd05911 87 FTDPDGlekvkeaakelgpkdkIIVLDDKPDGVLSIEDLLSPTLGEEDEDLPPPLKDGKDDTAAILYSSGTTGLPKGVCL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1319 PHKALTN--FLVSMGETPGLTAEDKMLAVTT----YCFDIAaleLFLPLiKGAHCYICqtehTK-DVEKLKRDIRTIKPT 1391
Cdd:cd05911 167 SHRNLIAnlSQVQTFLYGNDGSNDVILGFLPlyhiYGLFTT---LASLL-NGATVIIM----PKfDSELFLDLIEKYKIT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1392 VMQATPATWKMLFYSGWENEENVK----ILCGG----EALPETLKRYFLDTG-SEAWNMfgpTETTIWSAVQRINDEcSR 1462
Cdd:cd05911 239 FLYLVPPIAAALAKSPLLDKYDLSslrvILSGGaplsKELQELLAKRFPNATiKQGYGM---TETGGILTVNPDGDD-KP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1463 ATIGRPIANTQIYI----TDSQLAPvpaGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPFepgsklYRTGDMARWLPGG 1538
Cdd:cd05911 315 GSVGRLLPNVEAKIvdddGKDSLGP---NEPGEICVRGPQVMKGYYNNPEATKETFDEDGW------LHTGDIGYFDEDG 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1539 RIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVV----ADMDNLAAYYTAKHANASLTARELRHFVKNALPAYM 1614
Cdd:cd05911 386 YLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIgipdEVSGELPRAYVVRKPGEKLTEKEVKDYVAKKVASYK 465
|
490 500
....*....|....*....|....
gi 1776025254 1615 -----VpsYFIqlDHMPLTPNGKI 1633
Cdd:cd05911 466 qlrggV--VFV--DEIPKSASGKI 485
|
|
| SgcC5_NRPS-like |
cd19539 |
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ... |
695-1121 |
8.55e-50 |
|
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- bond forming activity and similar C-domains of modular NRPSs; SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. This subfamily also includes similar C-domains of modular NRPSs such as Penicillium chrysogenum N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase PCBAB. Condensation (C) domains of NRPSs normally catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380462 [Multi-domain] Cd Length: 427 Bit Score: 184.89 E-value: 8.55e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 695 PLSEVQKGLWTLQKMSPEKSAYHVPLCFKFSSGLHLETLQQAFGLVLNQHPILKHVIQEKDG-----VPILKNEPAL-SI 768
Cdd:cd19539 3 PLSFAQERLWFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDGgvprqEILPPGPAPLeVR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 769 EIKTENisSMKESDIPAFLRKKVKEPYVKENSPLVRVMSFSRSEQEHFLLVVIHHLIFDGVSSVTFIHSLFDTYQLLLKG 848
Cdd:cd19539 83 DLSDPD--SDRERRLEELLRERESRGFDLDEEPPIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAARRKG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 849 QQPEIAVSPAIYHDFAAWEKNMLAGKDGVKHRTYWQKQLSGTLPnLQLP-KVSASSVSEFREDTYTRRLSSGFMNQVRMF 927
Cdd:cd19539 161 PAAPLPELRQQYKEYAAWQREALAAPRAAELLDFWRRRLRGAEP-TALPtDRPRPAGFPYPGADLRFELDAELVAALREL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 928 AKEHSVNVTTVFLSCYMMLLGRYTGQKEQIVGMPAMVRPEERFDDAIGHFLNMLPIRSELNPADTFSSFISKLQLTILDG 1007
Cdd:cd19539 240 AKRARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNHPRFESTVGFFVNLLPLRVDVSDCATFRDLIARVRKALVDA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1008 LDHAAYPFPKMVRDLNIPRSQAGSPVFQTAFFYQNFLQSGsyqsllSRYADFFSVDYVEYIHQEGEYELVFELWETEEKM 1087
Cdd:cd19539 320 QRHQELPFQQLVAELPVDRDAGRHPLVQIVFQVTNAPAGE------LELAGGLSYTEGSDIPDGAKFDLNLTVTEEGTGL 393
|
410 420 430
....*....|....*....|....*....|....
gi 1776025254 1088 ELNIKYNTGLFDAASISAMFDHFVYVTEQAMLNP 1121
Cdd:cd19539 394 RGSLGYATSLFDEETIQGFLADYLQVLRQLLANP 427
|
|
| C_PKS-NRPS |
cd19532 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
695-1040 |
6.40e-49 |
|
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHxxxD motif, a few such as Monascus pilosus lovastatin nonaketide synthase MokA have a non-canonical HRxxxD motif in the C-domain and are unable to catalyze amide-bond formation. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380455 [Multi-domain] Cd Length: 421 Bit Score: 182.27 E-value: 6.40e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 695 PLSEVQKGLWTLQKMSPEKSAYHVPLCFKFSSGLHLETLQQAFGLVLNQHPILK--HVIQEKDGVP---ILKnEPALSIE 769
Cdd:cd19532 3 PMSFGQSRFWFLQQYLEDPTTFNVTFSYRLTGPLDVARLERAVRAVGQRHEALRtcFFTDPEDGEPmqgVLA-SSPLRLE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 770 IKTenISSmkESDIPAFLRKKVKEPYVKENSPLVRVMSFSRSEQEHFLLVVIHHLIFDGVSSVTFIHSLFDTYQlllkGQ 849
Cdd:cd19532 82 HVQ--ISD--EAEVEEEFERLKNHVYDLESGETMRIVLLSLSPTEHYLIFGYHHIAMDGVSFQIFLRDLERAYN----GQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 850 QPeiavSPAI--YHDFAAWEKNMLAGKDGVKHRTYWQKQLSG---TLPNLQLPKVSA-SSVSEFREDTYTRRLSSGFMNQ 923
Cdd:cd19532 154 PL----LPPPlqYLDFAARQRQDYESGALDEDLAYWKSEFSTlpePLPLLPFAKVKSrPPLTRYDTHTAERRLDAALAAR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 924 VRMFAKEHSVNVTTVFLSCYMMLLGRYTGQKEQIVGMPAMVRPEERFDDAIGHFLNMLPIRSELNPADTFSSFISKLQLT 1003
Cdd:cd19532 230 IKEASRKLRVTPFHFYLAALQVLLARLLDVDDICIGIADANRTDEDFMETIGFFLNLLPLRFRRDPSQTFADVLKETRDK 309
|
330 340 350
....*....|....*....|....*....|....*..
gi 1776025254 1004 ILDGLDHAAYPFPKMVRDLNIPRSQAGSPVFQTAFFY 1040
Cdd:cd19532 310 AYAALAHSRVPFDVLLDELGVPRSATHSPLFQVFINY 346
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
187-486 |
6.78e-49 |
|
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.
Pssm-ID: 341286 [Multi-domain] Cd Length: 435 Bit Score: 182.81 E-value: 6.78e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 187 EDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDHVGGIGMLHLRDVYLGcqeinvsSETIL 266
Cdd:cd17631 98 DDLALLMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRG-------GTVVI 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 267 M---EPLKWLDWIDHYRASVTWA-PNFAFGLVT--DFAEeikdrkWDLSSMRYMLNGGEAMVAkvgrRILELLEPHGLpa 340
Cdd:cd17631 171 LrkfDPETVLDLIERHRVTSFFLvPTMIQALLQhpRFAT------TDLSSLRAVIYGGAPMPE----RLLRALQARGV-- 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 341 dAIRPAWGMSETSSGVIF-SHEFTRAgtsdddHFVEIGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGYYQRPD 419
Cdd:cd17631 239 -KFVQGYGMTETSPGVTFlSPEDHRR------KLGSAGRPVFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPE 311
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1776025254 420 LNESVFtEDGWFETGDLGFL-RNGRLTITGRTKDAIIINGINYYSHAIESAVEELSEIetsytAACAV 486
Cdd:cd17631 312 ATAAAF-RDGWFHTGDLGRLdEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAV-----AEVAV 373
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
166-561 |
2.06e-48 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 183.81 E-value: 2.06e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 166 AIIVEDLLSAEA---DTDWHQSSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTR-EDITFNWMPFDHVG 241
Cdd:PRK05851 128 SVTVHDLATAAHtnrSASLTPPDSGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVGLDAaTDVGCSWLPLYHDM 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 242 GIGMLhLRDVYLGCQEINVSSETILMEPLKWLDWIDHYRASVTWAPNFAFGLVTDFAEEIKDrkWDLSSMRYMLNGGEAM 321
Cdd:PRK05851 208 GLAFL-LTAALAGAPLWLAPTTAFSASPFRWLSWLSDSRATLTAAPNFAYNLIGKYARRVSD--VDLGALRVALNGGEPV 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 322 VAKVGRRILELLEPHGLPADAIRPAWGMSETS---------SGVIFSHEFTRAGTSDDDHFVeIGSPIPGFSMRIV-NDH 391
Cdd:PRK05851 285 DCDGFERFATAMAPFGFDAGAAAPSYGLAESTcavtvpvpgIGLRVDEVTTDDGSGARRHAV-LGNPIPGMEVRISpGDG 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 392 NELVEEGEIGRFQVSGLSVTSGYyqrpdLNESVFTEDGWFETGDLGFLRNGRLTITGRTKDAIIINGINYYSHAIESAVE 471
Cdd:PRK05851 364 AAGVAGREIGEIEIRGASMMSGY-----LGQAPIDPDDWFPTGDLGYLVDGGLVVCGRAKELITVAGRNIFPTEIERVAA 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 472 ELSEIETSytAACAVRLGQNSTDQ---LAIFFVTSaklnDEQMSQllRNIQSHVSQVIGVTPEYLLPVQKEEIPKTAIGK 548
Cdd:PRK05851 439 QVRGVREG--AVVAVGTGEGSARPglvIAAEFRGP----DEAGAR--SEVVQRVASECGVVPSDVVFVAPGSLPRTSSGK 510
|
410
....*....|...
gi 1776025254 549 IQRTQLKTSFENG 561
Cdd:PRK05851 511 LRRLAVKRSLEAA 523
|
|
| KR_2_FAS_SDR_x |
cd08955 |
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 2, complex (x); ... |
4056-4418 |
4.61e-48 |
|
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 2, complex (x); Ketoreductase, a module of the multidomain polyketide synthase, has 2 subdomains, each corresponding to a short-chain dehydrogenases/reductase (SDR) family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerizes but is composed of 2 subdomains, each resembling an SDR monomer. In some instances, as in porcine FAS, an enoyl reductase (a Rossman fold NAD binding domain of the MDR family) module is inserted between the sub-domains. The active site resembles that of typical SDRs, except that the usual positions of the catalytic asparagine and tyrosine are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular polyketide synthases are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) fatty acid synthase. In some instances, such as porcine FAS , an enoyl reductase module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consists of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthesis uses dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-ketoacyl reductase (KR), forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-enoyl reductase (ER). Polyketide syntheses also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes the KR domain of the Lyngbya majuscule Jam J, -K, and #L which are encoded on the jam gene cluster and are involved in the synthesis of the Jamaicamides (neurotoxins); Lyngbya majuscule Jam P belongs to a different KR_FAS_SDR_x subfamily. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.
Pssm-ID: 187658 [Multi-domain] Cd Length: 376 Bit Score: 178.25 E-value: 4.61e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4056 VQRLVEFGHKEGLRLLCVTKGLESF--QNTSVRMAGASRAGLYRMLQCEYSHLISRHMDAEEVTDHPRLAKLIADEFYSE 4133
Cdd:cd08955 41 VQALSKAGLRRAPRLWLVTRGAQSVlaDGEPVSPAQAPLWGLGRVIALEHPELRCGLVDLDPEATAAEEAEALLAELLAA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4134 SYDAEVCYRDGLRYQSFLKAHPetgkATEQSAvfpkDHVLLITGGTRGIGLLCARHFAEcYGVKKLVLTGREQLPpreew 4213
Cdd:cd08955 121 DAEDQVALRGGARYVARLVRAP----ARPLRP----DATYLITGGLGGLGLLVAEWLVE-RGARHLVLTGRRAPS----- 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4214 arfktsntslAEKIQAVRELEAKGVQVEMLSLTLSDDAQVEQTLQHIKRTLGPIGGVIHCAGLTDMDTLAfiRKTSDDIQ 4293
Cdd:cd08955 187 ----------AAARQAIAALEEAGAEVVVLAADVSDRDALAAALAQIRASLPPLRGVIHAAGVLDDGVLA--NQDWERFR 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4294 RVMEPKVSGLTTLYRHVCNEPLQFFVLFSSVSAIIPelSAGQADYAMANSYMDYFAEAHQ-KHVPIISVQWPNWKETGM- 4371
Cdd:cd08955 255 KVLAPKVQGAWNLHQLTQDLPLDFFVLFSSVASLLG--SPGQANYAAANAFLDALAHYRRaRGLPALSINWGPWAEVGMa 332
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1776025254 4372 GEVTNQAY-RESGLFSITNSEGLRFLDQIVSKmfGPVVLPAManQTNW 4418
Cdd:cd08955 333 ASLARQARlEARGVGAISPAAGLQALGQLLRT--GSTQVGVA--PVDW 376
|
|
| Ketoacyl-synt_C |
pfam02801 |
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
2017-2136 |
4.70e-48 |
|
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.
Pssm-ID: 426989 Cd Length: 118 Bit Score: 168.52 E-value: 4.70e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2017 YALLRGIGVNNDGADkVGFYAPSVKGQADVVQQVMNQTKIHPESICYVEAHGTGTKLGDPIELAALTNVYRQYTNKtQFC 2096
Cdd:pfam02801 1 YAVIKGSAVNHDGRH-NGLTAPNGEGQARAIRRALADAGVDPEDVDYVEAHGTGTPLGDPIEAEALKRVFGSGARK-QPL 78
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1776025254 2097 GIGSVKTNIGHLDTAAGLAGCIKVVMSLYHQELAPSINYK 2136
Cdd:pfam02801 79 AIGSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLNLE 118
|
|
| KR |
pfam08659 |
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ... |
4174-4368 |
8.60e-48 |
|
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.
Pssm-ID: 430138 [Multi-domain] Cd Length: 180 Bit Score: 170.44 E-value: 8.60e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4174 LITGGTRGIGLLCARHFAEcYGVKKLVLTGReqlppreewarfktSNTSLAEKIQAVRELEAKGVQVEMLSLTLSDDAQV 4253
Cdd:pfam08659 4 LITGGLGGLGRELARWLAE-RGARHLVLLSR--------------SAAPRPDAQALIAELEARGVEVVVVACDVSDPDAV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4254 EQTLQHIKRTLGPIGGVIHCAGLTDmDTLaFIRKTSDDIQRVMEPKVSGLTTLYRHVCNEPLQFFVLFSSVSAIIPelSA 4333
Cdd:pfam08659 69 AALLAEIKAEGPPIRGVIHAAGVLR-DAL-LENMTDEDWRRVLAPKVTGTWNLHEATPDEPLDFFVLFSSIAGLLG--SP 144
|
170 180 190
....*....|....*....|....*....|....*.
gi 1776025254 4334 GQADYAMANSYMDYFAEA-HQKHVPIISVQWPNWKE 4368
Cdd:pfam08659 145 GQANYAAANAFLDALAEYrRSQGLPATSINWGPWAE 180
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
1847-2182 |
1.10e-47 |
|
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new carbon-carbon bond by a decarboxylating Claisen-like condensation reaction. Members are involved in the synthesis of fatty acids and polyketides, a diverse group of natural products. Both pathways are an iterative series of additions of small carbon units, usually acetate, to a nascent acyl group. There are 2 classes of decarboxylating condensing enzymes, which can be distinguished by sequence similarity, type of active site residues and type of primer units (acetyl CoA or acyl carrier protein (ACP) linked units).
Pssm-ID: 238421 [Multi-domain] Cd Length: 332 Bit Score: 175.90 E-value: 1.10e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1847 RMLLTHSWKAIEDAGYAAGQI--PQTSVFMSASNNSYRALLPSDTTESLETPDGYVSWVLAQSGTiptMISHKLGLRGPS 1924
Cdd:cd00825 13 ILGFEAAERAIADAGLSREYQknPIVGVVVGTGGGSPRFQVFGADAMRAVGPYVVTKAMFPGASG---QIATPLGIHGPA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1925 YFVHANCSSSLIGLHSAYKSLLSAESDYALVGGATLHTESNIGYVHQPGLNFSSDGHIKAFDASADGMIGGEGVAVVLLK 2004
Cdd:cd00825 90 YDVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAPMDCEFDAMGALSTPEKASRTFDAAADGFVFGDGAGALVVE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2005 KAADAVKDGDHIYALLRGIGVNNDGADKVGFyAPSVKGQADVVQQVMNQTKIHPESICYVEAHGTGTKLGDPIELAALTN 2084
Cdd:cd00825 170 ELEHALARGAHIYAEIVGTAATIDGAGMGAF-APSAEGLARAAKEALAVAGLTVWDIDYLVAHGTGTPIGDVKELKLLRS 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2085 VYrqytnKTQFCGIGSVKTNIGHLDTAAGLAGCIKVVMSLYHQELAPSINYKEPNPNTDLASSpfyvvdqkKTLSREIQT 2164
Cdd:cd00825 249 EF-----GDKSPAVSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPPSIHIEELDEAGLNIVT--------ETTPRELRT 315
|
330
....*....|....*...
gi 1776025254 2165 hrAALSSFGLGGTNTHAI 2182
Cdd:cd00825 316 --ALLNGFGLGGTNATLV 331
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
4590-4992 |
3.56e-47 |
|
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism]; 3-oxoacyl-(acyl-carrier-protein) synthase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440073 [Multi-domain] Cd Length: 409 Bit Score: 176.82 E-value: 3.56e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4590 IAVVGLSCRFPGAETLESYWSLLSEGRSSIGPIP---AERWGCKtpyYAGVIDGvsyFDPDFFLlHEEDVRAMDPQ---A 4663
Cdd:COG0304 3 VVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITrfdASGLPVR---IAGEVKD---FDPEEYL-DRKELRRMDRFtqyA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4664 LLVLEECLKllyHAGYTPEEIKGKPVGVYIG-GRSQHKPDEDSLD--HAKNP-------IVTVGQNYLAANLSQFFDVRG 4733
Cdd:COG0304 76 LAAAREALA---DAGLDLDEVDPDRTGVIIGsGIGGLDTLEEAYRalLEKGPrrvspffVPMMMPNMAAGHVSIRFGLKG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4734 PSVVVDTACSSALVGMNMAIQALRGGDIQSAIVGGVSLLSSDASHRLFDRRGILS------KHSSfHVFDERADGVVLGE 4807
Cdd:COG0304 153 PNYTVSTACASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLAGFDALGALStrnddpEKAS-RPFDKDRDGFVLGE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4808 GVGMVMLKTVKQALEDGDTIYAVVKAASVNNDG-RTAGPAtPNLEAQKEVMKDALFKSGKKPEDISYLEANGSGSIVTDL 4886
Cdd:COG0304 232 GAGVLVLEELEHAKARGAKIYAEVVGYGASSDAyHITAPA-PDGEGAARAMRAALKDAGLSPEDIDYINAHGTSTPLGDA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4887 LELKAIQSVYrSGHSSPLSLGSIKPNIGHPLCA----EGIASfikvVLMLKERRFVPflsgekeMAHFDQQ----KANIT 4958
Cdd:COG0304 311 AETKAIKRVF-GDHAYKVPVSSTKSMTGHLLGAagaiEAIAS----VLALRDGVIPP-------TINLENPdpecDLDYV 378
|
410 420 430
....*....|....*....|....*....|....
gi 1776025254 4959 FSRALEKwtdSQPTAAINCFADGGTNVHVIVEAW 4992
Cdd:COG0304 379 PNEAREA---KIDYALSNSFGFGGHNASLVFKRY 409
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
1177-1580 |
1.16e-45 |
|
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341233 [Multi-domain] Cd Length: 452 Bit Score: 173.55 E-value: 1.16e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1177 QTLTYRELDERSTQLAIYLQAHGVGP-DRLAgIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLEDSEVfitl 1255
Cdd:cd05907 4 QPITWAEFAEEVRALAKGLIALGVEPgDRVA-ILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEA---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1256 ttselvntlswngvtTALLdqdwdeiaqtasdrkvltrTVTPENLAYVIYTSGSTGKPKGVMIPHKALTNFLVSMGETPG 1335
Cdd:cd05907 79 ---------------KALF-------------------VEDPDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLP 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1336 LTAEDKMLavttycfdiaaleLFLPLikgAHC-------YIC-----QTEHTKDVEKLKRDIRTIKPTVMQATPATWKML 1403
Cdd:cd05907 125 ATEGDRHL-------------SFLPL---AHVferraglYVPllagaRIYFASSAETLLDDLSEVRPTVFLAVPRVWEKV 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1404 fYSG---------------WENEENVK-ILCGGEALPETLKRYFLDTGSEAWNMFGPTETTIWSAVQRINDEcSRATIGR 1467
Cdd:cd05907 189 -YAAikvkavpglkrklfdLAVGGRLRfAASGGAPLPAELLHFFRALGIPVYEGYGLTETSAVVTLNPPGDN-RIGTVGK 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1468 PIANTQIYITDSqlapvpagvpGELCIAGDGVAKGYYKKEELTDSRFIDNPFepgsklYRTGDMARWLPGGRIEYIGRID 1547
Cdd:cd05907 267 PLPGVEVRIADD----------GEILVRGPNVMLGYYKNPEATAEALDADGW------LHTGDLGEIDEDGFLHITGRKK 330
|
410 420 430
....*....|....*....|....*....|....
gi 1776025254 1548 N-QVKIRGFRIELGDIESRLSEHPGILECVVVAD 1580
Cdd:cd05907 331 DlIITSGGKNISPEPIENALKASPLISQAVVIGD 364
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
1179-1643 |
1.16e-45 |
|
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.
Pssm-ID: 341273 [Multi-domain] Cd Length: 442 Bit Score: 173.46 E-value: 1.16e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1179 LTYRELDERSTQLAIYLQAHGVGP-DRLAgIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLEDSEVFITLTT 1257
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKgDRVF-VLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1258 SELVntlswngvttalldqdwdeiaqtasdrkvltRTVTPENLAYVIYTSGSTGKPKGVMIPHKALTNFLVSMGETPGLT 1337
Cdd:cd05969 80 EELY-------------------------------ERTDPEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLH 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1338 AEDKM--------LAVTTYcfdiaalELFLPLIKGAHCYICQTEHtkDVEKLKRDIRTIKPTVMQATPATWKMLFYSGWE 1409
Cdd:cd05969 129 PDDIYwctadpgwVTGTVY-------GIWAPWLNGVTNVVYEGRF--DAESWYGIIERVKVTVWYTAPTAIRMLMKEGDE 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1410 -----NEENVKILC-GGEAL-PETLKryfldTGSEAWNM-----FGPTETtiwSAVQRINDECSRA---TIGRPIANTQI 1474
Cdd:cd05969 200 larkyDLSSLRFIHsVGEPLnPEAIR-----WGMEVFGVpihdtWWQTET---GSIMIANYPCMPIkpgSMGKPLPGVKA 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1475 YITDSQLAPVPAGVPGELCIAGD--GVAKGYYKKEELTDSRFIDNpfepgskLYRTGDMARWLPGGRIEYIGRIDNQVKI 1552
Cdd:cd05969 272 AVVDENGNELPPGTKGILALKPGwpSMFRGIWNDEERYKNSFIDG-------WYLTGDLAYRDEDGYFWFVGRADDIIKT 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1553 RGFRIELGDIESRLSEHPGILECVVVADMDNL-----AAYYTAK--HANASLTARELRHFVKNALPAYMVPSYFIQLDHM 1625
Cdd:cd05969 345 SGHRVGPFEVESALMEHPAVAEAGVIGKPDPLrgeiiKAFISLKegFEPSDELKEEIINFVRQKLGAHVAPREIEFVDNL 424
|
490
....*....|....*...
gi 1776025254 1626 PLTPNGKIDRNSLKNIDL 1643
Cdd:cd05969 425 PKTRSGKIMRRVLKAKEL 442
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
27-477 |
1.23e-45 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 177.21 E-value: 1.23e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 27 QPATIPEVLYRTAAELGDTKGIIYLQpDGTEVYQSYRRLWDDGLRIVKGLRQSGLKAKQSVILqLGDNS-QLLPAFWGCV 105
Cdd:COG1022 9 PADTLPDLLRRRAARFPDRVALREKE-DGIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAI-LSDNRpEWVIADLAIL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 106 LTGVVPAPLavpptYAESS----------SGT-----------QKLKDAW---TLLDKPAVITDRGMHQE--MLDWAK-- 157
Cdd:COG1022 87 AAGAVTVPI-----YPTSSaeevayilndSGAkvlfvedqeqlDKLLEVRdelPSLRHIVVLDPRGLRDDprLLSLDEll 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 158 EQGlegfRAIIVEDLLSAEadtdWHQSSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPF 237
Cdd:COG1022 162 ALG----REVADPAELEAR----RAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFLPL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 238 DHVGG-IGMLHLrdVYLGCQeINV--SSETIL----------------------------MEPLKWL-----DW-----I 276
Cdd:COG1022 234 AHVFErTVSYYA--LAAGAT-VAFaeSPDTLAedlrevkptfmlavprvwekvyagiqakAEEAGGLkrklfRWalavgR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 277 DHYRASVT-WAPNFAFGLVTDFAEEIKDRKW-DL--SSMRYMLNGGEAMvakvGRRILELLEPHGLPadaIRPAWGMSET 352
Cdd:COG1022 311 RYARARLAgKSPSLLLRLKHALADKLVFSKLrEAlgGRLRFAVSGGAAL----GPELARFFRALGIP---VLEGYGLTET 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 353 SsGVIFSHEF--TRAGTsdddhfveIGSPIPGFSMRIVndhnelvEEGEIgrfQVSGLSVTSGYYQRPDLNESVFTEDGW 430
Cdd:COG1022 384 S-PVITVNRPgdNRIGT--------VGPPLPGVEVKIA-------EDGEI---LVRGPNVMKGYYKNPEATAEAFDADGW 444
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1776025254 431 FETGDLGFLR-NGRLTITGRTKDaIII--NGINYYSHAIESAVEELSEIE 477
Cdd:COG1022 445 LHTGDIGELDeDGFLRITGRKKD-LIVtsGGKNVAPQPIENALKASPLIE 493
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
1157-1639 |
1.87e-45 |
|
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.
Pssm-ID: 341269 [Multi-domain] Cd Length: 508 Bit Score: 174.48 E-value: 1.87e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1157 ELFEQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGP-DRLAGIYVDrSLDMLVGLLAILKAGGAYVPLDP 1235
Cdd:cd05959 8 LVDLNLNEGRGDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKReERVLLIMLD-TVDFPTAFLGAIRAGIVPVPVNT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1236 SYPAERLEYMLEDSEVFITLTTSELVNTL--SWNGVTTALLDQDWDEIAQTASDRKVLTRTVT------------PENLA 1301
Cdd:cd05959 87 LLTPDDYAYYLEDSRARVVVVSGELAPVLaaALTKSEHTLVVLIVSGGAGPEAGALLLAELVAaeaeqlkpaathADDPA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1302 YVIYTSGSTGKPKGVMIPHKALTNFLVSMGE-TPGLTAEDKmlavttyCFDIAAL--------ELFLPLIKGAHCyICQT 1372
Cdd:cd05959 167 FWLYSSGSTGRPKGVVHLHADIYWTAELYARnVLGIREDDV-------CFSAAKLffayglgnSLTFPLSVGATT-VLMP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1373 EHTKDVEKLKRdIRTIKPTVMQATPATW-KMLFYSGWENEENVKI-LC--GGEALPETLKRYFLD-TGSEAWNMFGPTET 1447
Cdd:cd05959 239 ERPTPAAVFKR-IRRYRPTVFFGVPTLYaAMLAAPNLPSRDLSSLrLCvsAGEALPAEVGERWKArFGLDILDGIGSTEM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1448 T---IWSAVQRINDECSratiGRPIANTQIYITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIdnpfepGSk 1524
Cdd:cd05959 318 LhifLSNRPGRVRYGTT----GKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQ------GE- 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1525 LYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVA--DMDNL---AAYYTAK---HANAS 1596
Cdd:cd05959 387 WTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGveDEDGLtkpKAFVVLRpgyEDSEA 466
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1776025254 1597 LtARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLK 1639
Cdd:cd05959 467 L-EEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1186-1639 |
8.96e-45 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 171.08 E-value: 8.96e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1186 ERSTQLAIYLQAHG-VGPDRLAgIYVDRSLDMLVGLLAILKAGGA----YVPLDPSYPAERLEYMLEDSEVFITLTTSEL 1260
Cdd:cd05922 1 LGVSAAASALLEAGgVRGERVV-LILPNRFTYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRIVLADAGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1261 VNTLSWNGVTTALLDQDWDEIAQTASDRKVLTRTVTPENLAYVIYTSGSTGKPKGVMIPHKALTNFLVSMGETPGLTAED 1340
Cdd:cd05922 80 ADRLRDALPASPDPGTVLDADGIRAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1341 KMLAVTTYCFDIAALELFLPLIKGAHCYIcqTEHTKDVEKLKRDIRTIKPTVMQATPATWKMLFYSGWENEE--NVKIL- 1417
Cdd:cd05922 160 RALTVLPLSYDYGLSVLNTHLLRGATLVL--TNDGVLDDAFWEDLREHGATGLAGVPSTYAMLTRLGFDPAKlpSLRYLt 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1418 -CGGEALPETLKRYF-LDTGSEAWNMFGPTETTIWSAV---QRINDECSraTIGRPIANTQIYITDSQLAPVPAGVPGEL 1492
Cdd:cd05922 238 qAGGRLPQETIARLReLLPGAQVYVMYGQTEATRRMTYlppERILEKPG--SIGLAIPGGEFEILDDDGTPTPPGEPGEI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1493 CIAGDGVAKGYYKkeeltDSRFIDNPFEPGSKLYrTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGI 1572
Cdd:cd05922 316 VHRGPNVMKGYWN-----DPPYRRKEGRGGGVLH-TGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLI 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1776025254 1573 LECVVVAD----MDNLAAYYTAKhanASLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLK 1639
Cdd:cd05922 390 IEAAAVGLpdplGEKLALFVTAP---DKIDPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
3339-3776 |
2.96e-44 |
|
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, including beta-ketoacyl [ACP] synthase, type I and II and polyketide synthases.They are characterized by the utlization of acyl carrier protein (ACP) thioesters as primer substrates, as well as the nature of their active site residues.
Pssm-ID: 238424 [Multi-domain] Cd Length: 407 Bit Score: 168.39 E-value: 2.96e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3339 EPVAIVGISGRFP---GAMDIDEFWKNLEEGKDSITEVPKDRWDWREHY-GNPDTdvnktdikwgGFIDGvaefdplffG 3414
Cdd:cd00828 1 SRVVITGIGVVSPhgeGCDEVEEFWEALREGRSGIAPVARLKSRFDRGVaGQIPT----------GDIPG---------W 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3415 ISPREADyVDPQQRLLMTYVWKALEDAGC-PPQSLSGTGTGIFIGTGnTGYKDLFHRANLP----IEGHAATGHM--IPS 3487
Cdd:cd00828 62 DAKRTGI-VDRTTLLALVATEEALADAGItDPYEVHPSEVGVVVGSG-MGGLRFLRRGGKLdaraVNPYVSPKWMlsPNT 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3488 VGPNRMSYFLNIHGPSEPVETACSSSLVAIHRAVTAMQNGDCEMAIAGGVNTILTEEAhISYSKAGMLSKD-----GRCK 3562
Cdd:cd00828 140 VAGWVNILLLSSHGPIKTPVGACATALEALDLAVEAIRSGKADIVVVGGVEDPLEEGL-SGFANMGALSTAeeepeEMSR 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3563 TFSADANGYVRGEGVGMVMLKKLEDAERDGNHIYGVIRGTAENHGGRANTLTSPNPkAQADLLVRAYRQAGIDPSTVTYI 3642
Cdd:cd00828 219 PFDETRDGFVEAEGAGVLVLERAELALARGAPIYGRVAGTASTTDGAGRSVPAGGK-GIARAIRTALAKAGLSLDDLDVI 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3643 EAHGTGTELGDPIEINGLKAAFKELsnmrGESQPdvpdhrcgIGSVKSNIGHLELAAGISGLIKVLLQMKHKTLVKSLHC 3722
Cdd:cd00828 298 SAHGTSTPANDVAESRAIAEVAGAL----GAPLP--------VTAQKALFGHSKGAAGALQLIGALQSLEHGLIPPTANL 365
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1776025254 3723 ETLNPYLQLTdspfYIVQEKQEWksvtdcdgNELPRRAGISSFGIGGVNAHIVI 3776
Cdd:cd00828 366 DDVDPDVEHL----SVVGLSRDL--------NLKVRAALVNAFGFGGSNAALVL 407
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
61-556 |
1.06e-43 |
|
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.
Pssm-ID: 341229 [Multi-domain] Cd Length: 437 Bit Score: 167.56 E-value: 1.06e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 61 SYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNSQLLPAFWGCVLTGVVPAPlaVPPTYAEsssgtQKLkdAWTLLDKP 140
Cdd:cd05903 3 TYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNP--ILPFFRE-----HEL--AFILRRAK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 141 A---VITDRgmhqemldwakeqgLEGFRaiivedllsaeadtdwHQSSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVK 217
Cdd:cd05903 74 AkvfVVPER--------------FRQFD----------------PAAMPDAVALLLFTSGTTGEPKGVMHSHNTLSASIR 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 218 GIIQMQGFTREDItfNWM--PFDHVGGIGMLHLRDVYLGcqeinvsSETILME---PLKWLDWIDHYRASVTW-APNFAF 291
Cdd:cd05903 124 QYAERLGLGPGDV--FLVasPMAHQTGFVYGFTLPLLLG-------APVVLQDiwdPDKALALMREHGVTFMMgATPFLT 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 292 GLVTdfAEEIKDRkwDLSSMRYMLNGGEAMVAKVGRRILELLEPHglpadaIRPAWGMSETSS--GVIFSHEFTRAGTSD 369
Cdd:cd05903 195 DLLN--AVEEAGE--PLSRLRTFVCGGATVPRSLARRAAELLGAK------VCSAYGSTECPGavTSITPAPEDRRLYTD 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 370 ddhfveiGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGYYQRPDLNeSVFTEDGWFETGDLGFL-RNGRLTITG 448
Cdd:cd05903 265 -------GRPLPGVEIKVVDDTGATLAPGVEGELLSRGPSVFLGYLDRPDLT-ADAAPEGWFRTGDLARLdEDGYLRITG 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 449 RTKDAIIINGINYYSHAIESA-VEELSEIETSYTAACAVRLGQNStdqlAIFFVTS--AKLNDEQMSQLLRNiQSHVSQV 525
Cdd:cd05903 337 RSKDIIIRGGENIPVLEVEDLlLGHPGVIEAAVVALPDERLGERA----CAVVVTKsgALLTFDELVAYLDR-QGVAKQY 411
|
490 500 510
....*....|....*....|....*....|.
gi 1776025254 526 IgvtPEYLlpVQKEEIPKTAIGKIQRTQLKT 556
Cdd:cd05903 412 W---PERL--VHVDDLPRTPSGKVQKFRLRE 437
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
61-470 |
5.06e-43 |
|
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341233 [Multi-domain] Cd Length: 452 Bit Score: 165.85 E-value: 5.06e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 61 SYRRLWDDGLRIVKGLRQSGLKaKQSVILQLGDNSqllPAFW----GCVLTGVVPAPLavpptYAESSSGTQklkdAWTL 136
Cdd:cd05907 7 TWAEFAEEVRALAKGLIALGVE-PGDRVAILSRNR---PEWTiadlAILAIGAVPVPI-----YPTSSAEQI----AYIL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 137 LDKPAvitdrgmhqemldwakeqglegfRAIIVEDllsaeadtdwhqssPEDLALLLLTSGSTGTPKAVMLNHRNIMSMV 216
Cdd:cd05907 74 NDSEA-----------------------KALFVED--------------PDDLATIIYTSGTTGRPKGVMLSHRNILSNA 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 217 KGIIQMQGFTREDITFNWMPFDHVGGIGMLHLRDVYLGCQEINVSSETILMEPLKWLDwiDHYRASV--TWAPNFAFGLV 294
Cdd:cd05907 117 LALAERLPATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFASSAETLLDDLSEVR--PTVFLAVprVWEKVYAAIKV 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 295 TDfAEEIKDRKWDL---SSMRYMLNGGeamvAKVGRRILELLEPHGLPadaIRPAWGMSETSSGVIFSHEFT-RAGTsdd 370
Cdd:cd05907 195 KA-VPGLKRKLFDLavgGRLRFAASGG----APLPAELLHFFRALGIP---VYEGYGLTETSAVVTLNPPGDnRIGT--- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 371 dhfveIGSPIPGFSMRIVNDhnelveeGEIgrfQVSGLSVTSGYYQRPDLNESVFTEDGWFETGDLG-FLRNGRLTITGR 449
Cdd:cd05907 264 -----VGKPLPGVEVRIADD-------GEI---LVRGPNVMLGYYKNPEATAEALDADGWLHTGDLGeIDEDGFLHITGR 328
|
410 420
....*....|....*....|...
gi 1776025254 450 TKDaIIIN--GINYYSHAIESAV 470
Cdd:cd05907 329 KKD-LIITsgGKNISPEPIENAL 350
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
30-557 |
1.21e-42 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 167.15 E-value: 1.21e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 30 TIPEVLYRTAAELGDTKGIIYLQPDGTEVYQ-SYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNSQLLPAFWGCVLTG 108
Cdd:PRK13295 25 TINDDLDACVASCPDKTAVTAVRLGTGAPRRfTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 109 VVPAPLavPPTYAESS-SGTQKLKDAwTLLDKPAVItdRGM-HQEML-----DWAKEQ--------GLEGFRAIIVEDLL 173
Cdd:PRK13295 105 AVLNPL--MPIFRERElSFMLKHAES-KVLVVPKTF--RGFdHAAMArrlrpELPALRhvvvvggdGADSFEALLITPAW 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 174 SAEADT----DWHQSSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDHVGGIGMLHLR 249
Cdd:PRK13295 180 EQEPDApailARLRPGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPMAHQTGFMYGLMM 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 250 DVYLGcqeinvsSETILM---EPLKWLDWIDHYRASVTWApnfAFGLVTDFAEEIKDRKWDLSSMRYMLNGGEAMVAKVG 326
Cdd:PRK13295 260 PVMLG-------ATAVLQdiwDPARAAELIRTEGVTFTMA---STPFLTDLTRAVKESGRPVSSLRTFLCAGAPIPGALV 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 327 RRILELLEPHglpadaIRPAWGMSETS--SGVIFSHEFTRAGTSDddhfveiGSPIPGFSMRIVNDHNELVEEGEIGRFQ 404
Cdd:PRK13295 330 ERARAALGAK------IVSAWGMTENGavTLTKLDDPDERASTTD-------GCPLPGVEVRVVDADGAPLPAGQIGRLQ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 405 VSGLSVTSGYYQRPDLNESVFteDGWFETGDLGFL-RNGRLTITGRTKDAIIINGINYYSHAIESAVEELSEIETsyTAA 483
Cdd:PRK13295 397 VRGCSNFGGYLKRPQLNGTDA--DGWFDTGDLARIdADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQ--VAI 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 484 CAV---RLGQNstdqlAIFFVT---SAKLNDEQMSQLLRNiQSHVSQVIgvtPEYLlpVQKEEIPKTAIGKIQ----RTQ 553
Cdd:PRK13295 473 VAYpdeRLGER-----ACAFVVprpGQSLDFEEMVEFLKA-QKVAKQYI---PERL--VVRDALPRTPSGKIQkfrlREM 541
|
....
gi 1776025254 554 LKTS 557
Cdd:PRK13295 542 LRGE 545
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
100-566 |
1.23e-42 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 167.81 E-value: 1.23e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 100 AFWGCVLTGVVPAPLAVPPTYAESSSGTQKLKDAwtlldKPAVI-TDRGMHQEMLDWAKEQGLEGFRAIIVEDLL--SAE 176
Cdd:PRK05850 75 AFLGALQAGLIAVPLSVPQGGAHDERVSAVLRDT-----SPSVVlTTSAVVDDVTEYVAPQPGQSAPPVIEVDLLdlDSP 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 177 ADTDWHQSSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIiqMQGFTRE-------DITF-NWMPFDHVGGIgMLHL 248
Cdd:PRK05850 150 RGSDARPRDLPSTAYLQYTSGSTRTPAGVMVSHRNVIANFEQL--MSDYFGDtggvpppDTTVvSWLPFYHDMGL-VLGV 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 249 -RDVYLGCQEINVSSETILMEPLKWLDWIDHYRASVTWAPNFAFGLVTdfaeeikdRK--------WDLSSMRYMLNGGE 319
Cdd:PRK05850 227 cAPILGGCPAVLTSPVAFLQRPARWMQLLASNPHAFSAAPNFAFELAV--------RKtsdddmagLDLGGVLGIISGSE 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 320 AMVAKVGRRILELLEPHGLPADAIRPAWGMSE------------TSSGVIFSHEF----------TRAGTSdddhFVEIG 377
Cdd:PRK05850 299 RVHPATLKRFADRFAPFNLRETAIRPSYGLAEatvyvatrepgqPPESVRFDYEKlsaghakrceTGGGTP----LVSYG 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 378 SPIPGfSMRIVnDHNELVE--EGEIGRFQVSGLSVTSGYYQRPDLNESVF----------TEDG-WFETGDLGFLRNGRL 444
Cdd:PRK05850 375 SPRSP-TVRIV-DPDTCIEcpAGTVGEIWVHGDNVAAGYWQKPEETERTFgatlvdpspgTPEGpWLRTGDLGFISEGEL 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 445 TITGRTKDAIIINGINYYSHAIESAVEelsEIETSYTAACAVrlGQNSTDQLaiffVTSAKLN-----DEQMSQLL---- 515
Cdd:PRK05850 453 FIVGRIKDLLIVDGRNHYPDDIEATIQ---EITGGRVAAISV--PDDGTEKL----VAIIELKkrgdsDEEAMDRLrtvk 523
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1776025254 516 RNIQSHVSQVIGVTPEYLLPVQKEEIPKTAIGKIQRTQLKTSFENGEFDHL 566
Cdd:PRK05850 524 REVTSAISKSHGLSVADLVLVAPGSIPITTSGKIRRAACVEQYRQDEFTRL 574
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
1179-1639 |
1.82e-42 |
|
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.
Pssm-ID: 341276 [Multi-domain] Cd Length: 428 Bit Score: 163.66 E-value: 1.82e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1179 LTYRELDERSTQLAIYLQAHGVGP-DRLAGIyVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLEDSEVFITLTT 1257
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKgDRVAVL-LPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1258 SElvntlswngvttalldqdwdeiaqtasdrkvltrtvtpeNLAYVIYTSGSTGKPKGVMIPHKALTNFLVSMGETPGLT 1337
Cdd:cd05972 80 AE---------------------------------------DPALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLR 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1338 AEDKMLAVTTYCFDIAAL-ELFLPLIKGAHCYICqTEHTKDVEKLKRDIRTIKPTVMQATPATWKMLFYSGWE--NEENV 1414
Cdd:cd05972 121 PDDIHWNIADPGWAKGAWsSFFGPWLLGATVFVY-EGPRFDAERILELLERYGVTSFCGPPTAYRMLIKQDLSsyKFSHL 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1415 KIL-CGGEAL-PETLKRYFLDTGSEAWNMFGPTETTIWSAVQRINDeCSRATIGRPIANTQIYITDSQLAPVPAGVPGEL 1492
Cdd:cd05972 200 RLVvSAGEPLnPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMP-VKPGSMGRPTPGYDVAIIDDDGRELPPGEEGDI 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1493 CI--AGDGVAKGYYKKEELTDSRFIDNpfepgskLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHP 1570
Cdd:cd05972 279 AIklPPPGLFLGYVGDPEKTEASIRGD-------YYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHP 351
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1776025254 1571 GILECVVVADMDNL------AAYYTAKHANAS-LTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLK 1639
Cdd:cd05972 352 AVAEAAVVGSPDPVrgevvkAFVVLTSGYEPSeELAEELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRVELR 427
|
|
| starter-C_NRPS |
cd19533 |
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ... |
693-1121 |
2.17e-42 |
|
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. While standard C-domains catalyze peptide bond formation between two amino acids, an initial, ('starter') C-domain may instead acylate an amino acid with a fatty acid. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380456 [Multi-domain] Cd Length: 419 Bit Score: 162.92 E-value: 2.17e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 693 FQPLSEVQKGLWTLQKMSPEKSAYHVPLCFKFSSGLHLETLQQAFGLVLNQHPILKHVIQEKDGVPILKNEPALSIEIKT 772
Cdd:cd19533 1 RLPLTSAQRGVWFAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEEEGEPYQWIDPYTPVPIRH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 773 ENISSMK--ESDIPAFLRKKVKEPYVKENSPLVRVMSFSRSEQEHFLLVVIHHLIFDGVSSVTFIHSLFDTYQLLLKGQQ 850
Cdd:cd19533 81 IDLSGDPdpEGAAQQWMQEDLRKPLPLDNDPLFRHALFTLGDNRHFWYQRVHHIVMDGFSFALFGQRVAEIYTALLKGRP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 851 PeiavSPAIYHDFAAW---EKNMLAGKDGVKHRTYWQKQLSGTLPNLQL-PKVSASSVSEFREdtyTRRLSSGFMNQVRM 926
Cdd:cd19533 161 A----PPAPFGSFLDLveeEQAYRQSERFERDRAFWTEQFEDLPEPVSLaRRAPGRSLAFLRR---TAELPPELTRTLLE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 927 FAKEHSVNVTTVFLSCYMMLLGRYTGQKEQIVGMPAMVRPEERFDDAIGHFLNMLPIRSELNPADTFSSFISKLQLTILD 1006
Cdd:cd19533 234 AAEAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRLGAAARQTPGMVANTLPLRLTVDPQQTFAELVAQVSRELRS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1007 GLDHAAYPFPKMVRDLNipRSQAGSPVFQTAFFYQNFlqsgSYQsllsryADFFSVDYVEYIHQEG---EYEL-VFELWe 1082
Cdd:cd19533 314 LLRHQRYRYEDLRRDLG--LTGELHPLFGPTVNYMPF----DYG------LDFGGVVGLTHNLSSGptnDLSIfVYDRD- 380
|
410 420 430
....*....|....*....|....*....|....*....
gi 1776025254 1083 TEEKMELNIKYNTGLFDAASISAMFDHFVYVTEQAMLNP 1121
Cdd:cd19533 381 DESGLRIDFDANPALYSGEDLARHQERLLRLLEEAAADP 419
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
1163-1633 |
2.43e-42 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 165.49 E-value: 2.43e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1163 AKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGP-DRLAgIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAER 1241
Cdd:PRK08316 21 ARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKgDRVA-ALGHNSDAYALLWLACARAGAVHVPVNFMLTGEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1242 LEYMLEDSEVFITLTTSELVNT----------------LSWNGVTTALLDQDWDEIAQTASDRKVLTRtVTPENLAYVIY 1305
Cdd:PRK08316 100 LAYILDHSGARAFLVDPALAPTaeaalallpvdtlilsLVLGGREAPGGWLDFADWAEAGSVAEPDVE-LADDDLAQILY 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1306 TSGSTGKPKGVMIPHKALTNFLVSMGETPGLTAEDKML-AVTTY-CfdiAALELFLplikGAHCYICQTEH---TKDVEK 1380
Cdd:PRK08316 179 TSGTESLPKGAMLTHRALIAEYVSCIVAGDMSADDIPLhALPLYhC---AQLDVFL----GPYLYVGATNVildAPDPEL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1381 LKRDIRTIKPTVMQATPATWKMLFYSGWENEENVKILCGG---------EALPETLKRYfldTGSEAWNMFGPTETTIWS 1451
Cdd:PRK08316 252 ILRTIEAERITSFFAPPTVWISLLRHPDFDTRDLSSLRKGyygasimpvEVLKELRERL---PGLRFYNCYGQTEIAPLA 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1452 AVQRINDECSRA-TIGRPIANTQIYITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPFepgsklyRTGD 1530
Cdd:PRK08316 329 TVLGPEEHLRRPgSAGRPVLNVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAFRGGWF-------HSGD 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1531 MARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMDN-----LAAYYTAKhANASLTARELRHF 1605
Cdd:PRK08316 402 LGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPkwieaVTAVVVPK-AGATVTEDELIAH 480
|
490 500
....*....|....*....|....*...
gi 1776025254 1606 VKNALPAYMVPSYFIQLDHMPLTPNGKI 1633
Cdd:PRK08316 481 CRARLAGFKVPKRVIFVDELPRNPSGKI 508
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
1158-1640 |
6.04e-42 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.
Pssm-ID: 341284 [Multi-domain] Cd Length: 518 Bit Score: 164.34 E-value: 6.04e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1158 LFEQQAKKTPDRAAVSYEGQ----TLTYRELDERSTQLAIYLQAHGVGP-DRLAgiyvdrSLDM-----LVGLLAILKAG 1227
Cdd:cd12119 1 LLEHAARLHGDREIVSRTHEgevhRYTYAEVAERARRLANALRRLGVKPgDRVA------TLAWnthrhLELYYAVPGMG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1228 GAYVPLDPSYPAERLEYMLEDSE---VFI-------------TLTTSELVNTLSWNG---VTTALLDQDWDEIAQTASDR 1288
Cdd:cd12119 75 AVLHTINPRLFPEQIAYIINHAEdrvVFVdrdflplleaiapRLPTVEHVVVMTDDAampEPAGVGVLAYEELLAAESPE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1289 KVLTrtVTPENLAYVI-YTSGSTGKPKGVMIPHKALtnFLVSMG----ETPGLTAEDKMLAVT------TYCFDIAAL-- 1355
Cdd:cd12119 155 YDWP--DFDENTAAAIcYTSGTTGNPKGVVYSHRSL--VLHAMAalltDGLGLSESDVVLPVVpmfhvnAWGLPYAAAmv 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1356 --ELFLPlikGAHcyicqtehtKDVEKLKRDIRTIKPTVMQATPATWKMLFYSGWENEENV----KILCGGEALPETLKR 1429
Cdd:cd12119 231 gaKLVLP---GPY---------LDPASLAELIEREGVTFAAGVPTVWQGLLDHLEANGRDLsslrRVVIGGSAVPRSLIE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1430 YFLDTGSE---AWNMfgpTETTIWSAVQRINDECS----------RATIGRPIANTQIYITDSQLAPVPA-GVP-GELCI 1494
Cdd:cd12119 299 AFEERGVRvihAWGM---TETSPLGTVARPPSEHSnlsedeqlalRAKQGRPVPGVELRIVDDDGRELPWdGKAvGELQV 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1495 AGDGVAKGYYKKEELTDSRFIDNPFepgsklyRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILE 1574
Cdd:cd12119 376 RGPWVTKSYYKNDEESEALTEDGWL-------RTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAE 448
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1776025254 1575 CVVVADMDN------LAayYTAKHANASLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLKN 1640
Cdd:cd12119 449 AAVIGVPHPkwgerpLA--VVVLKEGATVTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
3-1040 |
6.08e-42 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 172.45 E-value: 6.08e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3 NNDNIRILANPSVSHGEPLHISEKQPATIPEVLYRTAAELGDTKGIIYL-------QPDGTEVY-----QSYRRLWDDGL 70
Cdd:PRK12316 3014 QNLLRGMVENPQRSVDELAMLDAEERGQLLEAWNATAAEYPLERGVHRLfeeqverTPDAVALAfgeqrLSYAELNRRAN 3093
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 71 RIVKGLRQSGLKAKQSVILQLGDNSQLLPAFWGCVLTGVVPAPLavPPTYAESssgtqklKDAWTLLDKPAvitDRGMHQ 150
Cdd:PRK12316 3094 RLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPL--DPEYPEE-------RLAYMLEDSGA---QLLLSQ 3161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 151 EMLDWAKEQGLEGFrAIIVEDLLSAEADTDWHqSSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDI 230
Cdd:PRK12316 3162 SHLRLPLAQGVQVL-DLDRGDENYAEANPAIR-TMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDR 3239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 231 TFNWMPFDHVGGIGMLHLrdvylgcqEINVSSETILMEPLKWLD---WIDHYRASVTWAPNFAFGLVTDFAEEIKDRkwD 307
Cdd:PRK12316 3240 VLQFTTFSFDVFVEELFW--------PLMSGARVVLAGPEDWRDpalLVELINSEGVDVLHAYPSMLQAFLEEEDAH--R 3309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 308 LSSMRYMLNGGEAMVAKVGRRILellephglpadAIRPAWGMSETSSGVIFSHEFTRAGTSDDDHFveIGSPIPGFSMRI 387
Cdd:PRK12316 3310 CTSLKRIVCGGEALPADLQQQVF-----------AGLPLYNLYGPTEATITVTHWQCVEEGKDAVP--IGRPIANRACYI 3376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 388 VNDHNELVEEGEIGRFQVSGLSVTSGYYQRPDLNESVFTEDGW------FETGDLGFLR-NGRLTITGRTKDAIIINGIN 460
Cdd:PRK12316 3377 LDGSLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPFvpgerlYRTGDLARYRaDGVIEYIGRVDHQVKIRGFR 3456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 461 YyshaiesaveELSEIETSYTAACAVR---LGQNSTDQLAIFFVTSAKLNDeqmsqLLRNIQSHVSQVIgvtPEYLLPVQ 537
Cdd:PRK12316 3457 I----------ELGEIEARLLEHPWVReavVLAVDGRQLVAYVVPEDEAGD-----LREALKAHLKASL---PEYMVPAH 3518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 538 ---KEEIPKTAIGKIQRtqlktsfengefdHLLHKPnrmndavqDEEMQQADHVKRVrEEIQEHLLTCLTEELHVSRdwV 614
Cdd:PRK12316 3519 llfLERMPLTPNGKLDR-------------KALPRP--------DAALLQQDYVAPV-NELERRLAAIWADVLKLEQ--V 3574
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 615 EPNANIQSLGVNSIKMMKLIrSIEKNYHIKLTAREIHQYPTIERLAsylsehedlsssSADKKGTDTYKTEPERSQATfq 694
Cdd:PRK12316 3575 GLTDNFFELGGDSIISLQVV-SRARQAGIRFTPKDLFQHQTIQGLA------------RVARVGGGVAVDQGPVSGET-- 3639
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 695 PLSEVQKGLwtLQKMSPEKSAYHVPLCFKFSSGLHLETLQQAFGLVLNQHPILKHVIQEKDGVPILKNEPAL---SIEIK 771
Cdd:PRK12316 3640 LLLPIQQQF--FEEPVPERHHWNQSLLLKPREALDAAALEAALQALVEHHDALRLRFVEDAGGWTAEHLPVElggALLWR 3717
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 772 TENIS-SMKESdipafLRKKVKEPYVKENSPLVRVMSFSRSEQEHFLLVVIHHLIFDGVSSVTFIHSLFDTYQLLLKGQQ 850
Cdd:PRK12316 3718 AELDDaEELER-----LGEEAQRSLDLADGPLLRALLATLADGSQRLLLVIHHLVVDGVSWRILLEDLQQAYQQLLQGEA 3792
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 851 PEIAVSPAIYHDFAAWEKNMLAGKDGVKHRTYWQKQLSGTLPNL-------QLPKVSASSVSEFREDTYTRRLssgfmnq 923
Cdd:PRK12316 3793 PRLPAKTSSFKAWAERLQEHARGEALKAELAYWQEQLQGVSSELpcdhpqgALQNRHAASVQTRLDRELTRRL------- 3865
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 924 VRMFAKEHSVNVTTVFLSCYMMLLGRYTGQKEQIVGMPAMVRpEERFDD-----AIGHFLNMLPIRseLNPADTFSSFIS 998
Cdd:PRK12316 3866 LQQAPAAYRTQVNDLLLTALARVVCRWTGEASALVQLEGHGR-EDLFADidlsrTVGWFTSLFPVR--LSPVEDLGASIK 3942
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|....
gi 1776025254 999 --KLQLTILDGlDHAAYPFPKMVRDLNIPRSQAGSPVFQTAFFY 1040
Cdd:PRK12316 3943 aiKEQLRAIPN-KGIGFGLLRYLGDEESRRTLAGLPVPRITFNY 3985
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
4590-4989 |
6.60e-42 |
|
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible for the elongation steps in fatty acid biosynthesis. KASIII catalyses the initial condensation and KAS I and II catalyze further elongation steps by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP.
Pssm-ID: 238430 [Multi-domain] Cd Length: 406 Bit Score: 161.17 E-value: 6.60e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4590 IAVVGLSCRFPGAETLESYWSLLSEGRSSIGPIPAERWGCKTPYYAGVIDGvsyFDPDFFLLhEEDVRAMDPQALLVL-- 4667
Cdd:cd00834 3 VVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRFDASGFPSRIAGEVPD---FDPEDYLD-RKELRRMDRFAQFALaa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4668 -EECLKllyHAGYTPEEIKGKPVGVYIGG--------RSQHKPDEDSLDHAKNP--IVTVGQNYLAANLSQFFDVRGPSV 4736
Cdd:cd00834 79 aEEALA---DAGLDPEELDPERIGVVIGSgigglatiEEAYRALLEKGPRRVSPffVPMALPNMAAGQVAIRLGLRGPNY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4737 VVDTACSSALVGMNMAIQALRGGDIQSAIVGGVSLLSSDASHRLFDRRGILSKHSSFHV-----FDERADGVVLGEGVGM 4811
Cdd:cd00834 156 TVSTACASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALRALSTRNDDPEkasrpFDKDRDGFVLGEGAGV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4812 VMLKTVKQALEDGDTIYAVVKAASVNNDGR--TAgPAtPNLEAQKEVMKDALFKSGKKPEDISYLEANGSGSIVTDLLEL 4889
Cdd:cd00834 236 LVLESLEHAKARGAKIYAEILGYGASSDAYhiTA-PD-PDGEGAARAMRAALADAGLSPEDIDYINAHGTSTPLNDAAES 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4890 KAIQSVYrSGHSSPLSLGSIKPNIGHPLCAEGIASFIKVVLMLKERRFVPflsgekeMAHFDQQKA----NITFSRAlek 4965
Cdd:cd00834 314 KAIKRVF-GEHAKKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPP-------TINLEEPDPecdlDYVPNEA--- 382
|
410 420
....*....|....*....|....*
gi 1776025254 4966 wTDSQPTAAINC-FADGGTNVHVIV 4989
Cdd:cd00834 383 -REAPIRYALSNsFGFGGHNASLVF 406
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
1167-1640 |
8.25e-42 |
|
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.
Pssm-ID: 341249 [Multi-domain] Cd Length: 493 Bit Score: 163.25 E-value: 8.25e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1167 PDRAAVSYEGQT--LTYRELDERSTQLAIYLQAHGVGP-DRLAgIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLE 1243
Cdd:cd05926 1 PDAPALVVPGSTpaLTYADLAELVDDLARQLAALGIKKgDRVA-IALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1244 YMLEDSEVFITLTTSELVNTLSWNGVTT--ALLDQDWD-----------EIAQTASDRKVLTRT--VTPENLAYVIYTSG 1308
Cdd:cd05926 80 FYLADLGSKLVLTPKGELGPASRAASKLglAILELALDvgvlirapsaeSLSNLLADKKNAKSEgvPLPDDLALILHTSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1309 STGKPKGVMIPHkalTNFLVSM---GETPGLTAEDKMLAVTTYcFDIAAL--ELFLPLIKGAhCYICQteHTKDVEKLKR 1383
Cdd:cd05926 160 TTGRPKGVPLTH---RNLAASAtniTNTYKLTPDDRTLVVMPL-FHVHGLvaSLLSTLAAGG-SVVLP--PRFSASTFWP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1384 DIRTIKPTVMQATPATWKMLFYSGWENEENVK-----ILCGGEALPET----LKRYFLDTGSEAWNMfgpTETTIWSAVQ 1454
Cdd:cd05926 233 DVRDYNATWYTAVPTIHQILLNRPEPNPESPPpklrfIRSCSASLPPAvleaLEATFGAPVLEAYGM---TEAAHQMTSN 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1455 RINDECSRA-TIGRPiANTQIYITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPFepgsklYRTGDMAR 1533
Cdd:cd05926 310 PLPPGPRKPgSVGKP-VGVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGW------FRTGDLGY 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1534 WLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMD-----NLAAYYTAKhANASLTARELRHFVKN 1608
Cdd:cd05926 383 LDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDekygeEVAAAVVLR-EGASVTEEELRAFCRK 461
|
490 500 510
....*....|....*....|....*....|..
gi 1776025254 1609 ALPAYMVPSYFIQLDHMPLTPNGKIDRNSLKN 1640
Cdd:cd05926 462 HLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
1180-1639 |
1.03e-41 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 161.83 E-value: 1.03e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1180 TYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLEDSEvfitlttse 1259
Cdd:cd05971 8 TFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSG--------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1260 lvntlswngvTTALLdqdwdeiaqtasdrkvltrTVTPENLAYVIYTSGSTGKPKGVMIPHKALtnflvsMGETPGLTAE 1339
Cdd:cd05971 79 ----------ASALV-------------------TDGSDDPALIIYTSGTTGPPKGALHAHRVL------LGHLPGVQFP 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1340 DKMLAVTTYCFDIAA--------LELFLP-LIKGAHCYICQTEHTkDVEKLKRDIRTIKPTVMQATPATWKMLFYSGWEN 1410
Cdd:cd05971 124 FNLFPRDGDLYWTPAdwawigglLDVLLPsLYFGVPVLAHRMTKF-DPKAALDLMSRYGVTTAFLPPTALKMMRQQGEQL 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1411 EE---NVK-ILCGGEALPETL----KRYFLDTGSEAwnmFGPTETTIW----SAVQRINDecsrATIGRPIANTQIYITD 1478
Cdd:cd05971 203 KHaqvKLRaIATGGESLGEELlgwaREQFGVEVNEF---YGQTECNLVigncSALFPIKP----GSMGKPIPGHRVAIVD 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1479 SQLAPVPAGVPGELCIA-GDGVAK-GYYKKEELTDSRFIdnpfepgSKLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFR 1556
Cdd:cd05971 276 DNGTPLPPGEVGEIAVElPDPVAFlGYWNNPSATEKKMA-------GDWLLTGDLGRKDSDGYFWYVGRDDDVITSSGYR 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1557 IELGDIESRLSEHPGILECVVVADMDN-----LAAYYtakHANASLT-----ARELRHFVKNALPAYMVPSYFIQLDHMP 1626
Cdd:cd05971 349 IGPAEIEECLLKHPAVLMAAVVGIPDPirgeiVKAFV---VLNPGETpsdalAREIQELVKTRLAAHEYPREIEFVNELP 425
|
490
....*....|...
gi 1776025254 1627 LTPNGKIDRNSLK 1639
Cdd:cd05971 426 RTATGKIRRRELR 438
|
|
| LCL_NRPS-like |
cd19540 |
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ... |
695-1117 |
1.58e-41 |
|
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.
Pssm-ID: 380463 [Multi-domain] Cd Length: 433 Bit Score: 161.05 E-value: 1.58e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 695 PLSEVQKGLWTLQKMSPEKSAYHVPLCFKFSSGLHLETLQQAFGLVLNQHPILKHVIQEKDGVP---ILKNEPAlSIEIK 771
Cdd:cd19540 3 PLSFAQQRLWFLNRLDGPSAAYNIPLALRLTGALDVDALRAALADVVARHESLRTVFPEDDGGPyqvVLPAAEA-RPDLT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 772 TENISsmkESDIPAFLRKKVKEPY-VKENSPLvRVMSFSRSEQEHFLLVVIHHLIFDGVSSVTFIHSLFDTYQLLLKGQQ 850
Cdd:cd19540 82 VVDVT---EDELAARLAEAARRGFdLTAELPL-RARLFRLGPDEHVLVLVVHHIAADGWSMAPLARDLATAYAARRAGRA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 851 PEIAVSPAIYHDFAAWEKNMLAGKD---GVKHR--TYWQKQLSGtLPN-LQLPkvsA----SSVSEFREDTYTRRLSSGF 920
Cdd:cd19540 158 PDWAPLPVQYADYALWQRELLGDEDdpdSLAARqlAYWRETLAG-LPEeLELP---TdrprPAVASYRGGTVEFTIDAEL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 921 MNQVRMFAKEHSVNVTTVFLSCYMMLLGRYTGQKEQIVGMPAMVRPEERFDDAIGHFLNMLPIRSELNPADTFSSFISKL 1000
Cdd:cd19540 234 HARLAALAREHGATLFMVLHAALAVLLSRLGAGDDIPIGTPVAGRGDEALDDLVGMFVNTLVLRTDVSGDPTFAELLARV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1001 QLTILDGLDHAAYPFPKMVRDLNIPRSQAGSPVFQTAFFYQNFLQSGsyqsllsryADF--FSVDYVEYIHQEGEYELVF 1078
Cdd:cd19540 314 RETDLAAFAHQDVPFERLVEALNPPRSTARHPLFQVMLAFQNTAAAT---------LELpgLTVEPVPVDTGVAKFDLSF 384
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1776025254 1079 ELWETEEK------MELNIKYNTGLFDAASISAMFDHFVYVTEQA 1117
Cdd:cd19540 385 TLTERRDAdgapagLTGELEYATDLFDRSTAERLADRFVRVLEAV 429
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
186-554 |
2.51e-41 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341253 [Multi-domain] Cd Length: 444 Bit Score: 160.77 E-value: 2.51e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 186 PEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMP--FDhvggigmLHLRDVYL-----GCQEI 258
Cdd:cd05930 92 PDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAYPLTPGDRVLQFTSfsFD-------VSVWEIFGallagATLVV 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 259 nVSSETILmEPLKWLDWIDHYRASVTWAPNFAFGLVTDFAEEikdrkWDLSSMRYMLNGGEAMVAKVGRRILELLEPHgl 338
Cdd:cd05930 165 -LPEEVRK-DPEALADLLAEEGITVLHLTPSLLRLLLQELEL-----AALPSLRLVLVGGEALPPDLVRRWRELLPGA-- 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 339 padAIRPAWGMSETSsgvIFSHEFTRAGTSDDDHFVEIGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGYYQRP 418
Cdd:cd05930 236 ---RLVNLYGPTEAT---VDATYYRVPPDDEEDGRVPIGRPIPNTRVYVLDENLRPVPPGVPGELYIGGAGLARGYLNRP 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 419 DLNESVFTEDGWFE------TGDLG-FLRNGRLTITGRTKDAIIINGinyysH-----AIESAVEELSEIEtsyTAACAV 486
Cdd:cd05930 310 ELTAERFVPNPFGPgermyrTGDLVrWLPDGNLEFLGRIDDQVKIRG-----YrielgEIEAALLAHPGVR---EAAVVA 381
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1776025254 487 RLGQNSTDQLAIFFVTsaklnDEQMSQLLRNIQSHVSQVIgvtPEYLLP---VQKEEIPKTAIGKIQRTQL 554
Cdd:cd05930 382 REDGDGEKRLVAYVVP-----DEGGELDEEELRAHLAERL---PDYMVPsafVVLDALPLTPNGKVDRKAL 444
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
1177-1586 |
4.04e-41 |
|
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341295 [Multi-domain] Cd Length: 468 Bit Score: 160.60 E-value: 4.04e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1177 QTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLEDSEVfitlt 1256
Cdd:cd17640 4 KRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSES----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1257 tselvntlswngvTTALLDQDwdeiaqtasdrkvltrtvtPENLAYVIYTSGSTGKPKGVMIPHKALTNFLVSMGETPGL 1336
Cdd:cd17640 79 -------------VALVVEND-------------------SDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPP 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1337 TAEDKMLAVTT--YCFDIAAlELFLpLIKGAhcyicqTEHTKDVEKLKRDIRTIKPTVMQATPATWKMLfYSGWENE--- 1411
Cdd:cd17640 127 QPGDRFLSILPiwHSYERSA-EYFI-FACGC------SQAYTSIRTLKDDLKRVKPHYIVSVPRLWESL-YSGIQKQvsk 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1412 ---------------ENVKI-LCGGEALPETLKRYFLDTGSEAWNMFGPTETTIWSAVQRInDECSRATIGRPIANTQIY 1475
Cdd:cd17640 198 sspikqflflfflsgGIFKFgISGGGALPPHVDTFFEAIGIEVLNGYGLTETSPVVSARRL-KCNVRGSVGRPLPGTEIK 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1476 ITDSQL-APVPAGVPGELCIAGDGVAKGYYKKEELTdSRFIDNpfepgSKLYRTGDMARWLPGGRIEYIGRI-DNQVKIR 1553
Cdd:cd17640 277 IVDPEGnVVLPPGEKGIVWVRGPQVMKGYYKNPEAT-SKVLDS-----DGWFNTGDLGWLTCGGELVLTGRAkDTIVLSN 350
|
410 420 430
....*....|....*....|....*....|....
gi 1776025254 1554 GFRIELGDIESRLSEHPGILECVVVA-DMDNLAA 1586
Cdd:cd17640 351 GENVEPQPIEEALMRSPFIEQIMVVGqDQKRLGA 384
|
|
| DCL_NRPS |
cd19543 |
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ... |
695-1121 |
4.13e-41 |
|
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor; The DCL-type Condensation (C) domain catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. This domain is D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains in addition to the LCL- and DCL-types such as starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380465 [Multi-domain] Cd Length: 423 Bit Score: 159.29 E-value: 4.13e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 695 PLSEVQKGLWTLQKMSPEKSAYHVPLCFKFSSGLHLETLQQAFGLVLNQHPILK-HVIQEKDGVP---ILKNEPalsIEI 770
Cdd:cd19543 3 PLSPMQEGMLFHSLLDPGSGAYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRtSFVWEGLGEPlqvVLKDRK---LPW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 771 KTENISSM----KESDIPAFLRKKVKEPYVKENSPLVRVMSFSRSEQEHFLLVVIHHLIFDGVSSVTFIHSLFDTYQLLL 846
Cdd:cd19543 80 RELDLSHLseaeQEAELEALAEEDRERGFDLARAPLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAALG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 847 KGQQPEIAVSPAiYHDFAAWeknmLAGKDGVKHRTYWQKQLSG-----TLPNLQLpkvsASSVSEFREDTYTRRLSSGFM 921
Cdd:cd19543 160 EGQPPSLPPVRP-YRDYIAW----LQRQDKEAAEAYWREYLAGfeeptPLPKELP----ADADGSYEPGEVSFELSAELT 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 922 NQVRMFAKEHSVNVTTVFLSCYMMLLGRYTGQKEQIVGMPAMVRPEER--FDDAIGHFLNMLPIRSELNPADTFSSFISK 999
Cdd:cd19543 231 ARLQELARQHGVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGRPAELpgIETMVGLFINTLPVRVRLDPDQTVLELLKD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1000 LQLTILDGLDHAAYPFPKMVRdlnipRSQAGSPVFQTAFFYQNFLQSGSyqSLLSRYADFFSVDYVEyIHQEGEYELVFE 1079
Cdd:cd19543 311 LQAQQLELREHEYVPLYEIQA-----WSEGKQALFDHLLVFENYPVDES--LEEEQDEDGLRITDVS-AEEQTNYPLTVV 382
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1776025254 1080 LWETEEkMELNIKYNTGLFDAASISAMFDHFVYVTEQAMLNP 1121
Cdd:cd19543 383 AIPGEE-LTIKLSYDAEVFDEATIERLLGHLRRVLEQVAANP 423
|
|
| KR_3_FAS_SDR_x |
cd08956 |
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 3, complex (x); ... |
2836-3076 |
6.83e-41 |
|
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 3, complex (x); Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. In some instances, such as porcine FAS, an enoyl reductase (ER) module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consists of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthesis uses a dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-KR, forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta- ER. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes KR domains found in many multidomain PKSs, including six of seven Sorangium cellulosum PKSs (encoded by spiDEFGHIJ) which participate in the synthesis of the polyketide scaffold of the cytotoxic spiroketal polyketide spirangien. These seven PKSs have either a single PKS module (SpiF), two PKR modules (SpiD,-E,-I,-J), or three PKS modules (SpiG,-H). This subfamily includes the second KR domains of SpiE,-G, I, and -J, both KR domains of SpiD, and the third KR domain of SpiH. The single KR domain of SpiF, the first and second KR domains of SpiH, the first KR domains of SpiE,-G,- I, and -J, and the third KR domain of SpiG, belong to a different KR_FAS_SDR subfamily. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.
Pssm-ID: 187659 [Multi-domain] Cd Length: 448 Bit Score: 159.35 E-value: 6.83e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2836 PSADTLHMPWRDEGVYLITGGAGSLGLLFAKEIANRTGRSTIVLTGRSVLSEDKENELEA-LRSIGAEVVYREADVSDQH 2914
Cdd:cd08956 181 ATLPPVPRPLDPDGTVLITGGTGTLGALLARHLVTEHGVRHLLLVSRRGPDAPGAAELVAeLAALGAEVTVAACDVADRA 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2915 AVHHLFEEI-KERygTLNGIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSGLLHVDECSKDFPLDFFIFFSSVSGCLGNAG 2993
Cdd:cd08956 261 ALAALLAAVpADH--PLTAVVHAAGVLDDGVLTSLTPERLDAVLRPKVDAAWHLHELTRDLDLAAFVLFSSAAGVLGSPG 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2994 QADYAAANSFMDAFAEYRRS--LAASkkrfgstiSFNWPLWEEGGM---QVGAEDEKRMlKTTGMVPMPTDSGLKAFYQG 3068
Cdd:cd08956 339 QANYAAANAFLDALAQHRRArgLPAT--------SLAWGLWAQASGmtaHLSDADLARL-ARGGLRPLSAEEGLALFDAA 409
|
....*...
gi 1776025254 3069 IASDKPQV 3076
Cdd:cd08956 410 LAADEPVL 417
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
61-554 |
9.50e-41 |
|
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 162605 [Multi-domain] Cd Length: 436 Bit Score: 158.77 E-value: 9.50e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 61 SYRRLWDDGLRIVKGLRQSGLKaKQSVILQLGDNS-QLLPAFWGCVLTGVVPAPLAvpPTYAESSSGTQkLKDawtlLDK 139
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIR-SGSRVALVGQNSiEMVLLLHACLLLGAEIAMLN--TRLTENERTNQ-LED----LDV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 140 PAVITDrgmhqEMLDwakeqgLEGFRAIIVEDL-LSAEADTDWHQSSP-EDLALLLLTSGSTGTPKAVMLNHRNIMSMVK 217
Cdd:TIGR01923 73 QLLLTD-----SLLE------EKDFQADSLDRIeAAGRYETSLSASFNmDQIATLMFTSGTTGKPKAVPHTFRNHYASAV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 218 GIIQMQGFTREDitfNWM---PFDHVGGIGMLhLRDVYLGCQEINVSSETILMEPLKwldwidhyRASVTWApnfafGLV 294
Cdd:TIGR01923 142 GSKENLGFTEDD---NWLlslPLYHISGLSIL-FRWLIEGATLRIVDKFNQLLEMIA--------NERVTHI-----SLV 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 295 TDFAEEIKDRKWDLSSMRYMLNGGEAMVAKVGRRILELlephGLPadaIRPAWGMSETSSGVI-FSHEFTRAGTSdddhf 373
Cdd:TIGR01923 205 PTQLNRLLDEGGHNENLRKILLGGSAIPAPLIEEAQQY----GLP---IYLSYGMTETCSQVTtATPEMLHARPD----- 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 374 veIGSPIPGFSMRIVNDhnELVEEGEIgrfQVSGLSVTSGYYQRPDLNESVFtEDGWFETGDLGFLRN-GRLTITGRTKD 452
Cdd:TIGR01923 273 --VGRPLAGREIKIKVD--NKEGHGEI---MVKGANLMKGYLYQGELTPAFE-QQGWFNTGDIGELDGeGFLYVLGRRDD 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 453 AIIINGINYYSHAIESAVEELSEIETsytaaCAVRLGQNST-DQLAIFFVTSAklNDEQMSQLLRNIQSHVSQVigVTPE 531
Cdd:TIGR01923 345 LIISGGENIYPEEIETVLYQHPGIQE-----AVVVPKPDAEwGQVPVAYIVSE--SDISQAKLIAYLTEKLAKY--KVPI 415
|
490 500
....*....|....*....|...
gi 1776025254 532 YLLPVQkeEIPKTAIGKIQRTQL 554
Cdd:TIGR01923 416 AFEKLD--ELPYNASGKILRNQL 436
|
|
| Ketoacyl-synt_C |
pfam02801 |
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
4828-4944 |
3.33e-40 |
|
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.
Pssm-ID: 426989 Cd Length: 118 Bit Score: 146.17 E-value: 3.33e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4828 YAVVKAASVNNDGRTAGPATPNLEAQKEVMKDALFKSGKKPEDISYLEANGSGSIVTDLLELKAIQSVYRSGH-SSPLSL 4906
Cdd:pfam02801 1 YAVIKGSAVNHDGRHNGLTAPNGEGQARAIRRALADAGVDPEDVDYVEAHGTGTPLGDPIEAEALKRVFGSGArKQPLAI 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 1776025254 4907 GSIKPNIGHPLCAEGIASFIKVVLMLKERRFVPFLSGE 4944
Cdd:pfam02801 81 GSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLNLE 118
|
|
| omega_3_PfaA |
TIGR02813 |
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ... |
4590-5009 |
4.06e-40 |
|
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this alignment are involved in omega-3 polyunsaturated fatty acid biosynthesis, such as the protein PfaA from the eicosapentaenoic acid biosynthesis operon in Photobacterium profundum strain SS9. PfaA is encoded together with PfaB, PfaC, and PfaD, and the functions of the individual polypeptides have not yet been described. More distant homologs of PfaA, also included with the reach of this model, appear to be involved in polyketide-like biosynthetic mechanisms of polyunsaturated fatty acid biosynthesis, an alternative to the more familiar iterated mechanism of chain extension and desaturation, and in most cases are encoded near genes for homologs of PfaB, PfaC, and/or PfaD.
Pssm-ID: 274311 [Multi-domain] Cd Length: 2582 Bit Score: 166.33 E-value: 4.06e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4590 IAVVGLSCRFPGAETLESYWSLLSEGRSSIGPIPAERWGcKTPYY--------------AGVIDGVSyFDPDFFLLHEED 4655
Cdd:TIGR02813 9 IAIVGMASIFANSRYLNKFWDLIFEKIDAITDVPSDHWA-KDDYYdsdkseadksyckrGGFLPEVD-FNPMEFGLPPNI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4656 VRAMDPQALLVLEECLKLLYHAGyTPEEIKGKPVGVYIG---GRSQHKP--------------------DEDS------- 4705
Cdd:TIGR02813 87 LELTDISQLLSLVVAKEVLNDAG-LPDGYDRDKIGITLGvggGQKQSSSlnarlqypvlkkvfkasgveDEDSemlikkf 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4706 ----LDHAKNPIVTVGQNYLAANLSQFFDVRGPSVVVDTACSSALVGMNMAIQALRGGDIQSAIVGGVSLLSSDASHRLF 4781
Cdd:TIGR02813 166 qdqyIHWEENSFPGSLGNVISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGGVCTDNSPFMYMSF 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4782 DRRGILSKHSSFHVFDERADGVVLGEGVGMVMLKTVKQALEDGDTIYAVVKAASVNNDGRTAGPATPNLEAQKEVMKDAL 4861
Cdd:TIGR02813 246 SKTPAFTTNEDIQPFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGKFKSIYAPRPEGQAKALKRAY 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4862 FKSGKKPEDISYLEANGSGSIVTDLLELKAIQSVYRSGHSSP--LSLGSIKPNIGHPLCAEGIASFIKVVLMLKERRFVP 4939
Cdd:TIGR02813 326 DDAGFAPHTCGLIEAHGTGTAAGDVAEFGGLVSVFSQDNDQKqhIALGSVKSQIGHTKSTAGTAGMIKAVLALHHKVLPP 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1776025254 4940 FLSGEKEMAHFDQQKANITFSRALEKW---TDSQP-TAAINCFADGGTNVHVIVEAWEKDEKHAIKRSPKSPPQ 5009
Cdd:TIGR02813 406 TINVDQPNPKLDIENSPFYLNTETRPWmqrEDGTPrRAGISSFGFGGTNFHMVLEEYSPKHQRDDQYRQRAVAQ 479
|
|
| KR_1_SDR_x |
cd08952 |
ketoreductase (KR), subgroup 1, complex (x) SDRs; Ketoreductase, a module of the multidomain ... |
2836-3078 |
4.80e-40 |
|
ketoreductase (KR), subgroup 1, complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes KR domains found in many multidomain PKSs, including six of seven Sorangium cellulosum PKSs (encoded by spiDEFGHIJ) which participate in the synthesis of the polyketide scaffold of the cytotoxic spiroketal polyketide spirangien. These seven PKSs have either a single PKS module (SpiF), two PKR modules (SpiD,-E,-I,-J), or three PKS modules (SpiG,-H). This subfamily includes the single KR domain of SpiF, the first KR domains of SpiE,-G,H,-I,and #J, the third KR domain of SpiG, and the second KR domain of SpiH. The second KR domains of SpiE,-G, I, and #J, and the KR domains of SpiD, belong to a different KR_FAS_SDR subfamily. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.
Pssm-ID: 187655 [Multi-domain] Cd Length: 480 Bit Score: 157.72 E-value: 4.80e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2836 PSADTLHMPWRDEGVYLITGGAGSLGLLFAKEIAnRTGRSTIVLTGRSVLSEDKENELEA-LRSIGAEVVYREADVSDQH 2914
Cdd:cd08952 218 PAPAPAARPWRPRGTVLVTGGTGALGAHVARWLA-RRGAEHLVLTSRRGPDAPGAAELVAeLTALGARVTVAACDVADRD 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2915 AVHHLFEEIKERYgTLNGIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSGLLHVDECSKDFPLDFFIFFSSVSGCLGNAGQ 2994
Cdd:cd08952 297 ALAALLAALPAGH-PLTAVVHAAGVLDDGPLDDLTPERLAEVLRAKVAGARHLDELTRDRDLDAFVLFSSIAGVWGSGGQ 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2995 ADYAAANSFMDAFAEYRRS--LAASkkrfgstiSFNWPLWEEGGMqVGAEDEKRmLKTTGMVPMPTDSGLKAFYQGIASD 3072
Cdd:cd08952 376 GAYAAANAYLDALAERRRArgLPAT--------SVAWGPWAGGGM-AAGAAAER-LRRRGLRPMDPELALAALRRALDHD 445
|
....*.
gi 1776025254 3073 KPQVFV 3078
Cdd:cd08952 446 ETAVVV 451
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
54-554 |
1.01e-39 |
|
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341267 [Multi-domain] Cd Length: 449 Bit Score: 155.87 E-value: 1.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 54 DGTEVYQSYRRLWDDGLRIVKGLRQSGLKAKQSVILqLGDNSQL-LPAFWGCVLTG--VVPAPLAVPPtyaessSGTQKL 130
Cdd:cd05945 11 VEGGRTLTYRELKERADALAAALASLGLDAGDPVVV-YGHKSPDaIAAFLAALKAGhaYVPLDASSPA------ERIREI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 131 KDAwtllDKPAVItdrgmhqemldwakeqglegfraIIVEDllsaeadtdwhqsspeDLALLLLTSGSTGTPKAVMLNHR 210
Cdd:cd05945 84 LDA----AKPALL-----------------------IADGD----------------DNAYIIFTSGSTGRPKGVQISHD 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 211 NIMSMVKGIIQMQGFTREDITFNWMP--FDhvggigmLHLRDVYL-----GCqeINVSSETILMEPLKWLDWIDHYRASV 283
Cdd:cd05945 121 NLVSFTNWMLSDFPLGPGDVFLNQAPfsFD-------LSVMDLYPalasgAT--LVPVPRDATADPKQLFRFLAEHGITV 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 284 tW--APNFAFGLVTD--FAEEikdrkwDLSSMRYMLNGGEAMVAKVGRRILELLephglPADAIRPAWGMSETSSGVIfS 359
Cdd:cd05945 192 -WvsTPSFAAMCLLSptFTPE------SLPSLRHFLFCGEVLPHKTARALQQRF-----PDARIYNTYGPTEATVAVT-Y 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 360 HEFTRAGTSDDDHfVEIGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGYYQRPDLNESVFTED---GWFETGDL 436
Cdd:cd05945 259 IEVTPEVLDGYDR-LPIGYAKPGAKLVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDegqRAYRTGDL 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 437 GFLRN-GRLTITGRTKDAIIINGINYYSHAIESAVEELSEIEtsytAACAVRLGQNSTDQLAIFFVTsakLNDEQMSQLL 515
Cdd:cd05945 338 VRLEAdGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVK----EAVVVPKYKGEKVTELIAFVV---PKPGAEAGLT 410
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1776025254 516 RNIQSHVSQVIgvtPEYLLP---VQKEEIPKTAIGKIQRTQL 554
Cdd:cd05945 411 KAIKAELAERL---PPYMIPrrfVYLDELPLNANGKIDRKAL 449
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
1178-1633 |
1.41e-39 |
|
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.
Pssm-ID: 341229 [Multi-domain] Cd Length: 437 Bit Score: 155.23 E-value: 1.41e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1178 TLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLEDSEVFITLTT 1257
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1258 SElvntlsWNGVTTALLdqdwdeiaqtasdrkvltrtvtPENLAYVIYTSGSTGKPKGVMIPHKALTNFLVSMGETPGLT 1337
Cdd:cd05903 81 ER------FRQFDPAAM----------------------PDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLG 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1338 AEDKMLAVTTYCFDIAALELF-LPLIKGAHCYICQTEHTKDVEKLkrdIRTIKPTVMQATPATWKMLFYSGWENEENV-- 1414
Cdd:cd05903 133 PGDVFLVASPMAHQTGFVYGFtLPLLLGAPVVLQDIWDPDKALAL---MREHGVTFMMGATPFLTDLLNAVEEAGEPLsr 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1415 --KILCGGEALPETLKRYFLDTG----SEAWNMfgpTETTiwSAVQRINDECSRA---TIGRPIANTQIYITDSQLAPVP 1485
Cdd:cd05903 210 lrTFVCGGATVPRSLARRAAELLgakvCSAYGS---TECP--GAVTSITPAPEDRrlyTDGRPLPGVEIKVVDDTGATLA 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1486 AGVPGELCIAGDGVAKGYYKKEELTdSRFIDNPFepgsklYRTGDMARWLPGGRIEYIGRIDNqVKIR-GFRIELGDIES 1564
Cdd:cd05903 285 PGVEGELLSRGPSVFLGYLDRPDLT-ADAAPEGW------FRTGDLARLDEDGYLRITGRSKD-IIIRgGENIPVLEVED 356
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1776025254 1565 RLSEHPGILECVVVADMD-----NLAAYYTAKhANASLTARELR-HFVKNALPAYMVPSYFIQLDHMPLTPNGKI 1633
Cdd:cd05903 357 LLLGHPGVIEAAVVALPDerlgeRACAVVVTK-SGALLTFDELVaYLDRQGVAKQYWPERLVHVDDLPRTPSGKV 430
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
1163-1638 |
1.66e-39 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 157.90 E-value: 1.66e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1163 AKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGP-DRLAgIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAER 1241
Cdd:PRK06178 43 ARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAgDRVA-VFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1242 LEYMLEDS--EVFITL-------------TTSELVNTLSWNGVTTA--------------LLDQDWDEI--AQTASDRKV 1290
Cdd:PRK06178 122 LSYELNDAgaEVLLALdqlapvveqvraeTSLRHVIVTSLADVLPAeptlplpdslraprLAAAGAIDLlpALRACTAPV 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1291 LTRTVTPENLAYVIYTSGSTGKPKGVMIPHK-----ALTNFLVSMGETPGltaeDKMLAVTTYcFDIAA--LELFLPLIK 1363
Cdd:PRK06178 202 PLPPPALDALAALNYTGGTTGMPKGCEHTQRdmvytAAAAYAVAVVGGED----SVFLSFLPE-FWIAGenFGLLFPLFS 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1364 GA------------------HCYICQTEHTKD--VEKL------KRDIRTikptvMQATPAtwkMLFysgweneenVKIL 1417
Cdd:PRK06178 277 GAtlvllarwdavafmaaveRYRVTRTVMLVDnaVELMdhprfaEYDLSS-----LRQVRV---VSF---------VKKL 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1418 CggealPETLKRYFLDTGS----EAWNMfgpTET----TIWSAVQRIN-DECSRAT-IGRPIANTQIYITDSQL-APVPA 1486
Cdd:PRK06178 340 N-----PDYRQRWRALTGSvlaeAAWGM---TEThtcdTFTAGFQDDDfDLLSQPVfVGLPVPGTEFKICDFETgELLPL 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1487 GVPGELCIAGDGVAKGYYKKEELTDSRFIDNpfepgskLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRL 1566
Cdd:PRK06178 412 GAEGEIVVRTPSLLKGYWNKPEATAEALRDG-------WLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALL 484
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1776025254 1567 SEHPGILECVVVADMDN-----LAAYYTAKhANASLTARELRHFVKNALPAYMVPSYFIqLDHMPLTPNGKIDRNSL 1638
Cdd:PRK06178 485 GQHPAVLGSAVVGRPDPdkgqvPVAFVQLK-PGADLTAAALQAWCRENMAVYKVPEIRI-VDALPMTATGKVRKQDL 559
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
31-555 |
2.46e-39 |
|
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.
Pssm-ID: 341269 [Multi-domain] Cd Length: 508 Bit Score: 156.37 E-value: 2.46e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 31 IPEVLYRTAAELGDTKGIIYlqPDGTevyQSYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNSQLLPAFWGCVLTGVV 110
Cdd:cd05959 6 ATLVDLNLNEGRGDKTAFID--DAGS---LTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 111 PAP---LAVPPTYAE--SSSGTQKLKDAWTLLDK-PAVITDRGMHQEMLDWAKEQGLEGFRAIIVEDLLSAEADTDWHQS 184
Cdd:cd05959 81 PVPvntLLTPDDYAYylEDSRARVVVVSGELAPVlAAALTKSEHTLVVLIVSGGAGPEAGALLLAELVAAEAEQLKPAAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 185 SPEDLALLLLTSGSTGTPKAVMLNHRNIMSM----VKGIIqmqGFTREDITFNWMPFDHVGGIGmlhlRDVYLgcqEINV 260
Cdd:cd05959 161 HADDPAFWLYSSGSTGRPKGVVHLHADIYWTaelyARNVL---GIREDDVCFSAAKLFFAYGLG----NSLTF---PLSV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 261 SSETILM----EPLKWLDWIDHYRasvtwaPNFAFGLVTDFAEEIKDRKW---DLSSMRYMLNGGEAMVAKVGRRI---- 329
Cdd:cd05959 231 GATTVLMperpTPAAVFKRIRRYR------PTVFFGVPTLYAAMLAAPNLpsrDLSSLRLCVSAGEALPAEVGERWkarf 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 330 -LELLEphglpadairpawGMSETSSGVIFSHEFTRA---GTSdddhfveiGSPIPGFSMRIVNDHNELVEEGEIGRFQV 405
Cdd:cd05959 305 gLDILD-------------GIGSTEMLHIFLSNRPGRvryGTT--------GKPVPGYEVELRDEDGGDVADGEPGELYV 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 406 SGLSVTSGYYQRPDLNESVFtEDGWFETGDlGFLRN--GRLTITGRTKDAIIINGINYYSHAIESAVEELSEIetsytAA 483
Cdd:cd05959 364 RGPSSATMYWNNRDKTRDTF-QGEWTRTGD-KYVRDddGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAV-----LE 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 484 CAVrLGQNSTDQL---AIFFVtsakLNDEQMSQ--LLRNIQSHVSQVIgvtPEYLLPVQKE---EIPKTAIGKIQRTQLK 555
Cdd:cd05959 437 AAV-VGVEDEDGLtkpKAFVV----LRPGYEDSeaLEEELKEFVKDRL---APYKYPRWIVfvdELPKTATGKIQRFKLR 508
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
167-561 |
4.17e-39 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 157.97 E-value: 4.17e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 167 IIVEDLLSAEADTDWHQSSP--EDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDHvgGIG 244
Cdd:PRK07769 158 VIAVDAVPDEVGATWVPPEAneDTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEGQEGDRGVSWLPFFH--DMG 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 245 MLHLRDVYLGCQEINV-SSETILMEPLKWLDWI----DHYRASVTWAPNFAF------GLVTDfaeeiKDRKWDLSSMRY 313
Cdd:PRK07769 236 LITVLLPALLGHYITFmSPAAFVRRPGRWIRELarkpGGTGGTFSAAPNFAFehaaarGLPKD-----GEPPLDLSNVKG 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 314 MLNGGEAMVAKVGRRILELLEPHGLPADAIRPAWGMSETSSGV--IFSHEFTRAGTSDDD-----HFVEIGSPIP----- 381
Cdd:PRK07769 311 LLNGSEPVSPASMRKFNEAFAPYGLPPTAIKPSYGMAEATLFVstTPMDEEPTVIYVDRDelnagRFVEVPADAPnavaq 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 382 ---GFSMR-----IVnDHNELVE--EGEIGRFQVSGLSVTSGYYQRPDLNESVF----------------TEDG-WFETG 434
Cdd:PRK07769 391 vsaGKVGVsewavIV-DPETASElpDGQIGEIWLHGNNIGTGYWGKPEETAATFqnilksrlseshaegaPDDAlWVRTG 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 435 DLGFLRNGRLTITGRTKDAIIINGINYYSHAIESAVEELSE-IETSYTAACAVRLGQ------------------NSTDQ 495
Cdd:PRK07769 470 DYGVYFDGELYITGRVKDLVIIDGRNHYPQDLEYTAQEATKaLRTGYVAAFSVPANQlpqvvfddshaglkfdpeDTSEQ 549
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1776025254 496 LAIFFVTSAKLNDEQMSQLLRNIQSHVSQVIGVTPEYLLPVQKEEIPKTAIGKIQRTQLKTSFENG 561
Cdd:PRK07769 550 LVIVAERAPGAHKLDPQPIADDIRAAIAVRHGVTVRDVLLVPAGSIPRTSSGKIARRACRAAYLDG 615
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
1179-1640 |
5.20e-39 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 153.83 E-value: 5.20e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1179 LTYRELDERSTQLAIYLQAHGVGP-DRLAGIyVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLEDSEVFITLTt 1257
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPgDVVAGL-LPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVT- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1258 selvntlswngvttalldqDWDEIAQTASDRKVLtrtvtpenlayvIYTSGSTGKPKGVMIPHKALTNFLVSMGETPGLT 1337
Cdd:cd05973 79 -------------------DAANRHKLDSDPFVM------------MFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLR 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1338 AEDKMlavttycFDIA----ALELFL----PLIKGAHCYICQTEHTkdVEKLKRDIRTIKPTVMQATPATWKMLFYSGWE 1409
Cdd:cd05973 128 PEDSF-------WNAAdpgwAYGLYYaitgPLALGHPTILLEGGFS--VESTWRVIERLGVTNLAGSPTAYRLLMAAGAE 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1410 NEENVK-----ILCGGEALPETLKRYFLDT-GSEAWNMFGPTETTIWSAVQR-INDECSRATIGRPIANTQIYITDSQLA 1482
Cdd:cd05973 199 VPARPKgrlrrVSSAGEPLTPEVIRWFDAAlGVPIHDHYGQTELGMVLANHHaLEHPVHAGSAGRAMPGWRVAVLDDDGD 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1483 PVPAGVPGELCIAGDGVA----KGYYKKEELTdsrfidnpfePGSKLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIE 1558
Cdd:cd05973 279 ELGPGEPGRLAIDIANSPlmwfRGYQLPDTPA----------IDGGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIG 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1559 LGDIESRLSEHPGILECVVVADMDN-----LAAY--YTAKHANASLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNG 1631
Cdd:cd05973 349 PFDVESALIEHPAVAEAAVIGVPDPertevVKAFvvLRGGHEGTPALADELQLHVKKRLSAHAYPRTIHFVDELPKTPSG 428
|
....*....
gi 1776025254 1632 KIDRNSLKN 1640
Cdd:cd05973 429 KIQRFLLRR 437
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
33-554 |
2.17e-38 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.
Pssm-ID: 341282 [Multi-domain] Cd Length: 483 Bit Score: 152.74 E-value: 2.17e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 33 EVLYRTAAELGDTKGIIYlqpDGTEVyqSYRRLWDDGLRIVKGLRQSGLkAKQSVILQLGDNS-QLLPAFWGCVLTG--V 109
Cdd:cd12117 1 ELFEEQAARTPDAVAVVY---GDRSL--TYAELNERANRLARRLRAAGV-GPGDVVGVLAERSpELVVALLAVLKAGaaY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 110 VPAPLAVPPTYAESSsgtqkLKDAwtllDKPAVITDRGMhqemldwAKEQGLEGFRAIIVEDLLSAEADTDWHQSSPEDL 189
Cdd:cd12117 75 VPLDPELPAERLAFM-----LADA----GAKVLLTDRSL-------AGRAGGLEVAVVIDEALDAGPAGNPAVPVSPDDL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 190 ALLLLTSGSTGTPKAVMLNHRNIMSMVKGiiqmQGFTRED----------ITFNWMPFDHVGGI---GMLHLrdvylgcq 256
Cdd:cd12117 139 AYVMYTSGSTGRPKGVAVTHRGVVRLVKN----TNYVTLGpddrvlqtspLAFDASTFEIWGALlngARLVL-------- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 257 einVSSETILmEPLKWLDWIDHYRASVTWAPNFAFGLVTDFAEEIkdrkwdLSSMRYMLNGGEAMVAKVGRRILElleph 336
Cdd:cd12117 207 ---APKGTLL-DPDALGALIAEEGVTVLWLTAALFNQLADEDPEC------FAGLRELLTGGEVVSPPHVRRVLA----- 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 337 GLPADAIRPAWGMSETSsgvIFSHEFTRAGTSDDDHFVEIGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGYYQ 416
Cdd:cd12117 272 ACPGLRLVNGYGPTENT---TFTTSHVVTELDEVAGSIPIGRPIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLN 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 417 RPDLNESVFTEDGW------FETGDL-GFLRNGRLTITGRTKDAIIINGINYYSHAIESAVEELSEIEtsyTAACAVRLG 489
Cdd:cd12117 349 RPALTAERFVADPFgpgerlYRTGDLaRWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVR---EAVVVVRED 425
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1776025254 490 QNSTDQLAIFFVTSAKLNDEQmsqllrnIQSHVSQVIgvtPEYLLP---VQKEEIPKTAIGKIQRTQL 554
Cdd:cd12117 426 AGGDKRLVAYVVAEGALDAAE-------LRAFLRERL---PAYMVPaafVVLDELPLTANGKVDRRAL 483
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
1149-1633 |
2.19e-38 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 154.35 E-value: 2.19e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1149 TYPYITFHELFEQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAH-GVGP-DRLAgIYVDRSLDMLVGLLAILKA 1226
Cdd:PRK08314 6 TLPETSLFHNLEVSARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQQEcGVRKgDRVL-LYMQNSPQFVIAYYAILRA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1227 GGAYVPLDPSYPAERLEYMLEDSEVFITLTTSELVN---------TLSWNGVTT---ALLDQ------DWDEIA---QTA 1285
Cdd:PRK08314 85 NAVVVPVNPMNREEELAHYVTDSGARVAIVGSELAPkvapavgnlRLRHVIVAQysdYLPAEpeiavpAWLRAEpplQAL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1286 SDRKVLT-------------RTVTPENLAYVIYTSGSTGKPKGVMIPHKALTNFLVSMGETPGLTAEDKMLAVTTYcFDI 1352
Cdd:PRK08314 165 APGGVVAwkealaaglapppHTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPL-FHV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1353 AALELFL--PLIKGAHCYICqtehTK-DVEKLKRDIRTIKPTVMQATPATWKMLFYSGWENEENVKILC----GGEALPE 1425
Cdd:PRK08314 244 TGMVHSMnaPIYAGATVVLM----PRwDREAAARLIERYRVTHWTNIPTMVVDFLASPGLAERDLSSLRyiggGGAAMPE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1426 TLKRYFLD-TGSEAWNMFGPTET---TIWSAVQRINDECsratIGRPIANTQIYITDSQ-LAPVPAGVPGELCIAGDGVA 1500
Cdd:PRK08314 320 AVAERLKElTGLDYVEGYGLTETmaqTHSNPPDRPKLQC----LGIPTFGVDARVIDPEtLEELPPGEVGEIVVHGPQVF 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1501 KGYYKKEELTDSRFIDnpFEpGSKLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVAD 1580
Cdd:PRK08314 396 KGYWNRPEATAEAFIE--ID-GKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIAT 472
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1776025254 1581 MDnlaAYY--TAK-------HANASLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKI 1633
Cdd:PRK08314 473 PD---PRRgeTVKavvvlrpEARGKTTEEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKI 531
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
28-556 |
2.73e-38 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 153.14 E-value: 2.73e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 28 PATIPEVLYRTAAELGDTKGIIYlqpDGTEVyqSYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNSQLLPAFWGCVLT 107
Cdd:PRK07656 4 WMTLPELLARAARRFGDKEAYVF---GDQRL--TYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 108 G--VVPaplaVPPTY--AESS-----SGTQKLKDAWTLL--DKPA--------------VITDRGMHQEMLDWAK--EQG 160
Cdd:PRK07656 79 GavVVP----LNTRYtaDEAAyilarGDAKALFVLGLFLgvDYSAttrlpalehvviceTEEDDPHTEKMKTFTDflAAG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 161 LEGFRAIIVedllsaeadtdwhqsSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDHV 240
Cdd:PRK07656 155 DPAERAPEV---------------DPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAANPFFHV 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 241 GGigmlhLRDVYLGCQeinVSSETILME----PLKWLDWIDHYRASVTWAP----NFAFGLVtdfaeeiKDRKWDLSSMR 312
Cdd:PRK07656 220 FG-----YKAGVNAPL---MRGATILPLpvfdPDEVFRLIETERITVLPGPptmyNSLLQHP-------DRSAEDLSSLR 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 313 YMLNGGEAM-VAKVgRRILELLephglPADAIRPAWGMSEtSSGVIfshEFTRAGTSDDDHFVEIGSPIPGFSMRIVNDH 391
Cdd:PRK07656 285 LAVTGAASMpVALL-ERFESEL-----GVDIVLTGYGLSE-ASGVT---TFNRLDDDRKTVAGTIGTAIAGVENKIVNEL 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 392 NELVEEGEIGRFQVSGLSVTSGYYQRPDLNESVFTEDGWFETGDLGFL-RNGRLTITGRTKDAIIINGINYYSHAIESAV 470
Cdd:PRK07656 355 GEEVPVGEVGELLVRGPNVMKGYYDDPEATAAAIDADGWLHTGDLGRLdEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVL 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 471 EELSEIetsytAACAV------RLGqnstdQLAIFFVT---SAKLNDEqmsQLLRNIQSH-----VSQVIgvtpEYLlpv 536
Cdd:PRK07656 435 YEHPAV-----AEAAVigvpdeRLG-----EVGKAYVVlkpGAELTEE---ELIAYCREHlakykVPRSI----EFL--- 494
|
570 580
....*....|....*....|
gi 1776025254 537 qkEEIPKTAIGKIQRTQLKT 556
Cdd:PRK07656 495 --DELPKNATGKVLKRALRE 512
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
4588-4989 |
2.74e-38 |
|
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, including beta-ketoacyl [ACP] synthase, type I and II and polyketide synthases.They are characterized by the utlization of acyl carrier protein (ACP) thioesters as primer substrates, as well as the nature of their active site residues.
Pssm-ID: 238424 [Multi-domain] Cd Length: 407 Bit Score: 150.67 E-value: 2.74e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4588 EGIAVVGLSCRFP---GAETLESYWSLLSEGRSSIGPIPAErwgcKTPYYAGVIDGVSYFDPDffllhEEDVRA---MDP 4661
Cdd:cd00828 1 SRVVITGIGVVSPhgeGCDEVEEFWEALREGRSGIAPVARL----KSRFDRGVAGQIPTGDIP-----GWDAKRtgiVDR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4662 QALLVLEECLKLLYHAGYT-PEEIKGKPVGVYIG-----GRSQH---KPDEDSLDHAKNPIVTVGQNYLAANLSQFFDV- 4731
Cdd:cd00828 72 TTLLALVATEEALADAGITdPYEVHPSEVGVVVGsgmggLRFLRrggKLDARAVNPYVSPKWMLSPNTVAGWVNILLLSs 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4732 RGPSVVVDTACSSALVGMNMAIQALRGGDIQSAIVGGVSLLSSDASH------RLFDRRGILSKHSSFhvFDERADGVVL 4805
Cdd:cd00828 152 HGPIKTPVGACATALEALDLAVEAIRSGKADIVVVGGVEDPLEEGLSgfanmgALSTAEEEPEEMSRP--FDETRDGFVE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4806 GEGVGMVMLKTVKQALEDGDTIYAVVKAASVNNDGRTAGpATPNLEAQKEVMKDALFKSGKKPEDISYLEANGSGSIVTD 4885
Cdd:cd00828 230 AEGAGVLVLERAELALARGAPIYGRVAGTASTTDGAGRS-VPAGGKGIARAIRTALAKAGLSLDDLDVISAHGTSTPAND 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4886 LLELKAIQSVYRsGHSSPLSLGSIKPNIGHPLCAEGIASFIKVVLMLkERRFVPflsGEKEMAHFDQQKANITFSRALEK 4965
Cdd:cd00828 309 VAESRAIAEVAG-ALGAPLPVTAQKALFGHSKGAAGALQLIGALQSL-EHGLIP---PTANLDDVDPDVEHLSVVGLSRD 383
|
410 420
....*....|....*....|....
gi 1776025254 4966 WTDSQPTAAINCFADGGTNVHVIV 4989
Cdd:cd00828 384 LNLKVRAALVNAFGFGGSNAALVL 407
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
1161-1655 |
4.77e-38 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 153.36 E-value: 4.77e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1161 QQAKKTPDRAAVSYE-GQTLTYRELDERSTQLAIYLQAHGVGP-DRLAgIYVDRSLDMLVGLLAILKAGGAYVPLDPSYP 1238
Cdd:PRK06087 31 QTARAMPDKIAVVDNhGASYTYSALDHAASRLANWLLAKGIEPgDRVA-FQLPGWCEFTIIYLACLKVGAVSVPLLPSWR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1239 AERLEYMLE--DSEVFITLTTSELVNTLSW-----NGVTT----ALLDQ-----DWDEIAQTASDRKVLTR--TVTPENL 1300
Cdd:PRK06087 110 EAELVWVLNkcQAKMFFAPTLFKQTRPVDLilplqNQLPQlqqiVGVDKlapatSSLSLSQIIADYEPLTTaiTTHGDEL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1301 AYVIYTSGSTGKPKGVMIPHkalTNFLVS---MGETPGLTAEDKM-----LAVTTYCFDiaalELFLPLIKGAHCYICQT 1372
Cdd:PRK06087 190 AAVLFTSGTEGLPKGVMLTH---NNILASeraYCARLNLTWQDVFmmpapLGHATGFLH----GVTAPFLIGARSVLLDI 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1373 -EHTKDVEKLKRDIRTikpTVMQATPATWKML--------------FYsgweneenvkiLCGGEALPETLKRYFLDTGSE 1437
Cdd:PRK06087 263 fTPDACLALLEQQRCT---CMLGATPFIYDLLnllekqpadlsalrFF-----------LCGGTTIPKKVARECQQRGIK 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1438 AWNMFGPTETtIWSAVQRINDECSR--ATIGRPIANTQIYITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDsRFI 1515
Cdd:PRK06087 329 LLSVYGSTES-SPHAVVNLDDPLSRfmHTDGYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTA-RAL 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1516 DNpfepgSKLYRTGDMARWLPGGRIEYIGRiDNQVKIRGFR-IELGDIESRLSEHPGILECVVVADMDN-----LAAYYT 1589
Cdd:PRK06087 407 DE-----EGWYYSGDLCRMDEAGYIKITGR-KKDIIVRGGEnISSREVEDILLQHPKIHDACVVAMPDErlgerSCAYVV 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1776025254 1590 AKHANASLTAREL-RHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLKNiDLSgEQLKQRQTSP 1655
Cdd:PRK06087 481 LKAPHHSLTLEEVvAFFSRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRK-DIM-RRLTQDVCEE 545
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
61-555 |
4.91e-38 |
|
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.
Pssm-ID: 341264 [Multi-domain] Cd Length: 442 Bit Score: 150.90 E-value: 4.91e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 61 SYRRLWDDGLRIVKGLRQSGLKAK-QSVILQLGDNSQLLPAFWGCVLTGVVPAPLAVPPTYAESSSgtqklkdawtlldk 139
Cdd:cd05941 13 TYADLVARAARLANRLLALGKDLRgDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEY-------------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 140 paVITDRGMhqemldwakeqglegfrAIIVedllsaeadtdwhqsspeDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGI 219
Cdd:cd05941 79 --VITDSEP-----------------SLVL------------------DPALILYTSGTTGRPKGVVLTHANLAANVRAL 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 220 IQMQGFTREDITFNWMPFDHVGGIGMLHLRDVYLGcqeinvsSETILM---EPLKWLDWIDHYRASVTWA-PNFAFGLV- 294
Cdd:cd05941 122 VDAWRWTEDDVLLHVLPLHHVHGLVNALLCPLFAG-------ASVEFLpkfDPKEVAISRLMPSITVFMGvPTIYTRLLq 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 295 ---TDFAEEIKDRKWDLSSMRYMLNGGEAM--------VAKVGRRILEllephglpadaiRpaWGMSETssGVIFS---H 360
Cdd:cd05941 195 yyeAHFTDPQFARAAAAERLRLMVSGSAALpvptleewEAITGHTLLE------------R--YGMTEI--GMALSnplD 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 361 EFTRAGTsdddhfveIGSPIPGFSMRIV-NDHNELVEEGEIGRFQVSGLSVTSGYYQRPDLNESVFTEDGWFETGDLGFL 439
Cdd:cd05941 259 GERRPGT--------VGMPLPGVQARIVdEETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGWFKTGDLGVV 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 440 R-NGRLTITGRTKDAII-INGINYYSHAIESAVEELSEIetsytAACAV------RLGQNstdqlaiffVTSA-KLNDEQ 510
Cdd:cd05941 331 DeDGYYWILGRSSVDIIkSGGYKVSALEIERVLLAHPGV-----SECAVigvpdpDWGER---------VVAVvVLRAGA 396
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1776025254 511 MSQLLRNIQSHVSQVIGVT--PEYLLPVqkEEIPKTAIGKIQRTQLK 555
Cdd:cd05941 397 AALSLEELKEWAKQRLAPYkrPRRLILV--DELPRNAMGKVNKKELR 441
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
1179-1638 |
5.32e-38 |
|
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.
Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 150.32 E-value: 5.32e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1179 LTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLEDSEVFITLTTS 1258
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1259 ELvntlswngvttalldqdwdeiaqtasdrkvltrtvtpENLAYVIYTSGSTGKPKGVMIPHKALTNFLVSMGETPGLTA 1338
Cdd:cd05935 82 EL-------------------------------------DDLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTP 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1339 EDKMLAVTTYcFDIAALE--LFLPLIKGAHcYICQTEHtkDVEKLKRDIRTIKPTVMQATPaTWKMLFYSGWENEE---- 1412
Cdd:cd05935 125 SDVILACLPL-FHVTGFVgsLNTAVYVGGT-YVLMARW--DRETALELIEKYKVTFWTNIP-TMLVDLLATPEFKTrdls 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1413 NVKILCGGEA-LPETLKRYFLD-TGSEAWNMFGPTETTIWSAV---QRINDECsratIGRPIANTQIYITD-SQLAPVPA 1486
Cdd:cd05935 200 SLKVLTGGGApMPPAVAEKLLKlTGLRFVEGYGLTETMSQTHTnppLRPKLQC----LGIP*FGVDARVIDiETGRELPP 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1487 GVPGELCIAGDGVAKGYYKKEELTDSRFIDnpfEPGSKLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRL 1566
Cdd:cd05935 276 NEVGEIVVRGPQIFKGYWNRPEETEESFIE---IKGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKL 352
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1776025254 1567 SEHPGILECVVVADMDNLA-----AYYTAKHA-NASLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSL 1638
Cdd:cd05935 353 YKHPAI*EVCVISVPDERVgeevkAFIVLRPEyRGKVTEEDIIEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
1160-1641 |
7.83e-38 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 151.55 E-value: 7.83e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1160 EQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAH-GVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYP 1238
Cdd:PRK06839 9 EKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1239 AERLEYMLEDSEVFITLTTSELVNTLSWNGVTTALLDQDWDEIAQTASDRKVLTRTVTPENLAYVI-YTSGSTGKPKGVM 1317
Cdd:PRK06839 89 ENELIFQLKDSGTTVLFVEKTFQNMALSMQKVSYVQRVISITSLKEIEDRKIDNFVEKNESASFIIcYTSGTTGKPKGAV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1318 IPHK-----ALTNFLvsmgeTPGLTAEDKMLaVTTYCFDIAALELF-LP-LIKGAHCYICQtehTKDVEKLKRDIRTIKP 1390
Cdd:PRK06839 169 LTQEnmfwnALNNTF-----AIDLTMHDRSI-VLLPLFHIGGIGLFaFPtLFAGGVIIVPR---KFEPTKALSMIEKHKV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1391 TVMQATPATWKMLFYS---GWENEENVKIL-CGGEALPETLKRYFLDTGSEAWNMFGPTETTiwSAVQRINDECSR---A 1463
Cdd:PRK06839 240 TVVMGVPTIHQALINCskfETTNLQSVRWFyNGGAPCPEELMREFIDRGFLFGQGFGMTETS--PTVFMLSEEDARrkvG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1464 TIGRPIANTQIYITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPFepgsklyRTGDMARWLPGGRIEYI 1543
Cdd:PRK06839 318 SIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETIQDGWL-------CTGDLARVDEDGFVYIV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1544 GRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMD----NLAAYYTAKHANASLTARELRHFVKNALPAYMVPSYF 1619
Cdd:PRK06839 391 GRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHvkwgEIPIAFIVKKSSSVLIEKDVIEHCRLFLAKYKIPKEI 470
|
490 500
....*....|....*....|..
gi 1776025254 1620 IQLDHMPLTPNGKIDRNSLKNI 1641
Cdd:PRK06839 471 VFLKELPKNATGKIQKAQLVNQ 492
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
4662-4989 |
1.38e-37 |
|
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new carbon-carbon bond by a decarboxylating Claisen-like condensation reaction. Members are involved in the synthesis of fatty acids and polyketides, a diverse group of natural products. Both pathways are an iterative series of additions of small carbon units, usually acetate, to a nascent acyl group. There are 2 classes of decarboxylating condensing enzymes, which can be distinguished by sequence similarity, type of active site residues and type of primer units (acetyl CoA or acyl carrier protein (ACP) linked units).
Pssm-ID: 238421 [Multi-domain] Cd Length: 332 Bit Score: 146.63 E-value: 1.38e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4662 QALLVLEECLKLLYHAGYTPEEIKGKPVGVYIG-----GRSQHKpDEDSLDHAkNPIVTVGQNY--LAANLSQFFDVRGP 4734
Cdd:cd00825 11 VSILGFEAAERAIADAGLSREYQKNPIVGVVVGtgggsPRFQVF-GADAMRAV-GPYVVTKAMFpgASGQIATPLGIHGP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4735 SVVVDTACSSALVGMNMAIQALRGGDIQSAIVGGVSLLSsDASHRLFDRRGILSKHS-SFHVFDERADGVVLGEGVGMVM 4813
Cdd:cd00825 89 AYDVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEELA-APMDCEFDAMGALSTPEkASRTFDAAADGFVFGDGAGALV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4814 LKTVKQALEDGDTIYAVVKAASVNNDGRTAGPATPNLEAQKEVMKDALFKSGKKPEDISYLEANGSGSIVTDLLELKAIQ 4893
Cdd:cd00825 168 VEELEHALARGAHIYAEIVGTAATIDGAGMGAFAPSAEGLARAAKEALAVAGLTVWDIDYLVAHGTGTPIGDVKELKLLR 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4894 SVYRsghSSPLSLGSIKPNIGHPLCAEGIASFIKVVLMLKerrfVPFLSGEKEMAHFDQQKANITfsralEKWTDSQP-T 4972
Cdd:cd00825 248 SEFG---DKSPAVSATKAMTGNLSSAAVVLAVDEAVLMLE----HGFIPPSIHIEELDEAGLNIV-----TETTPRELrT 315
|
330
....*....|....*..
gi 1776025254 4973 AAINCFADGGTNVHVIV 4989
Cdd:cd00825 316 ALLNGFGLGGTNATLVL 332
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
30-564 |
3.01e-37 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 152.20 E-value: 3.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 30 TIPEVLYRTAAELGDTKGIIYLQ----PDGTEVYQSYRRLwddglrivkGLRQSGLKAKQSVILQLGDNSQLLP------ 99
Cdd:PRK12476 35 TLISLIERNIANVGDTVAYRYLDhshsAAGCAVELTWTQL---------GVRLRAVGARLQQVAGPGDRVAILApqgidy 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 100 --AFWGCVLTGVVPAPLAVP--PTYAESSSGTqkLKDAwtlldKPAVITDRGmhqemldwAKEQGLEGF----------R 165
Cdd:PRK12476 106 vaGFFAAIKAGTIAVPLFAPelPGHAERLDTA--LRDA-----EPTVVLTTT--------AAAEAVEGFlrnlprlrrpR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 166 AIIV--------EDLLSAEADTDwhqsspeDLALLLLTSGSTGTPKAVMLNHRNIMS-MVKGIIQMQGFTREDITFNWMP 236
Cdd:PRK12476 171 VIAIdaipdsagESFVPVELDTD-------DVSHLQYTSGSTRPPVGVEITHRAVGTnLVQMILSIDLLDRNTHGVSWLP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 237 FDHVGGIGMLHLRDVYLGcqeinvssETILMEPLKWLD----WID------HYRASVTWAPNFAF------GLVTDfAEE 300
Cdd:PRK12476 244 LYHDMGLSMIGFPAVYGG--------HSTLMSPTAFVRrpqrWIKalsegsRTGRVVTAAPNFAYewaaqrGLPAE-GDD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 301 IkdrkwDLSSMrYMLNGGEAMVAKVGRRILELLEPHGLPADAIRPAWGMSETS------------SGVIFSHEFTRAGTS 368
Cdd:PRK12476 315 I-----DLSNV-VLIIGSEPVSIDAVTTFNKAFAPYGLPRTAFKPSYGIAEATlfvatiapdaepSVVYLDREQLGAGRA 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 369 ---DDDH-----FVEIGSPIPGFSMRIVNDH--NELvEEGEIGRFQVSGLSVTSGYYQRPDLNESVF------------- 425
Cdd:PRK12476 389 vrvAADApnavaHVSCGQVARSQWAVIVDPDtgAEL-PDGEVGEIWLHGDNIGRGYWGRPEETERTFgaklqsrlaegsh 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 426 ---TEDG--WFETGDLGFLRNGRLTITGRTKDAIIINGINYYSHAIESAVEELSEI-ETSYTAACAVRLGQNstDQLAIF 499
Cdd:PRK12476 468 adgAADDgtWLRTGDLGVYLDGELYITGRIADLIVIDGRNHYPQDIEATVAEASPMvRRGYVTAFTVPAEDN--ERLVIV 545
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1776025254 500 FVTSAKLNDEQMSQLLRNIQSHVSQVIGVTPEYLLPVQKEEIPKTAIGKIQRTQLKTSFENGEFD 564
Cdd:PRK12476 546 AERAAGTSRADPAPAIDAIRAAVSRRHGLAVADVRLVPAGAIPRTTSGKLARRACRAQYLDGRLG 610
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
3351-3779 |
4.16e-37 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 147.24 E-value: 4.16e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3351 PGAMDIDEFWKNLEEGKDSItevpkdrwdwrehygNPDTDVNKTDI--KWGGFIDGvaeFDPLFFgISPREADYVDPQQR 3428
Cdd:PRK07314 14 PLGNDVESTWKNLLAGKSGI---------------GPITHFDTSDLavKIAGEVKD---FNPDDY-MSRKEARRMDRFIQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3429 LLMTYVWKALEDAGCPPQSLSGTGTGIFIGTGNTGYKdlfhranlPIEGHAATGH----------MIPSVGPNRMSYFLN 3498
Cdd:PRK07314 75 YGIAAAKQAVEDAGLEITEENADRIGVIIGSGIGGLE--------TIEEQHITLLekgprrvspfFVPMAIINMAAGHVS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3499 IH----GPSEPVETACSSSLVAIHRAVTAMQNGDCEMAIAGGVntilteEAHIS------YSKAGMLSKD-----GRCKT 3563
Cdd:PRK07314 147 IRygakGPNHSIVTACATGAHAIGDAARLIAYGDADVMVAGGA------EAAITplgiagFAAARALSTRnddpeRASRP 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3564 FSADANGYVRGEGVGMVMLKKLEDAERDGNHIYGVIRGTAENhgGRANTLTSPNPK----AQAdlLVRAYRQAGIDPSTV 3639
Cdd:PRK07314 221 FDKDRDGFVMGEGAGILVLEELEHAKARGAKIYAEVVGYGMT--GDAYHMTAPAPDgegaARA--MKLALKDAGINPEDI 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3640 TYIEAHGTGTELGDPIEINGLKAAFkelsnmrGESQPDVPdhrcgIGSVKSNIGHLELAAGISGLIKVLLQMKHKTLVKS 3719
Cdd:PRK07314 297 DYINAHGTSTPAGDKAETQAIKRVF-------GEHAYKVA-----VSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPT 364
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1776025254 3720 LHCETLNPylqltdspfyivqekqewksvtDCDGNELP---RRAGI-----SSFGIGGVNAHIVIEEY 3779
Cdd:PRK07314 365 INLDNPDE----------------------ECDLDYVPneaRERKIdyalsNSFGFGGTNASLVFKRY 410
|
|
| PTZ00050 |
PTZ00050 |
3-oxoacyl-acyl carrier protein synthase; Provisional |
3351-3772 |
7.62e-37 |
|
3-oxoacyl-acyl carrier protein synthase; Provisional
Pssm-ID: 240245 [Multi-domain] Cd Length: 421 Bit Score: 146.76 E-value: 7.62e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3351 PGAMDIDEFWKNLEEGK---DSITEVPKDRWDWREHYGNPDTDVNKTDIKWGGFIDGVaEFDPLFFGISPREADYVdpqq 3427
Cdd:PTZ00050 4 PLGVGAESTWEALIAGKsgiRKLTEFPKFLPDCIPEQKALENLVAAMPCQIAAEVDQS-EFDPSDFAPTKRESRAT---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3428 RLLMTYVWKALEDAGCPPQS-LSGTGTGIFIGTGNTGYKDLFH-RANLPIEGHAATGHM-IPSVGPNRMSYFL----NIH 3500
Cdd:PTZ00050 79 HFAMAAAREALADAKLDILSeKDQERIGVNIGSGIGSLADLTDeMKTLYEKGHSRVSPYfIPKILGNMAAGLVaikhKLK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3501 GPSEPVETACSSSLVAIHRAVTAMQNGDCEMAIAGGVNTILTEEAHISYSKAGMLSK------DGRCKTFSADANGYVRG 3574
Cdd:PTZ00050 159 GPSGSAVTACATGAHCIGEAFRWIKYGEADIMICGGTEASITPVSFAGFSRMRALCTkynddpQRASRPFDKDRAGFVMG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3575 EGVGMVMLKKLEDAERDGNHIYGVIRGTAENhgGRANTLTSPNPKAQAdlLVRAYRQA-----GIDPSTVTYIEAHGTGT 3649
Cdd:PTZ00050 239 EGAGILVLEELEHALRRGAKIYAEIRGYGSS--SDAHHITAPHPDGRG--ARRCMENAlkdgaNININDVDYVNAHATST 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3650 ELGDPIEINGLKAAFKelsnmrgesqpDVPDHRCGIGSVKSNIGHLELAAGISGLIKVLLQMKHKTLVKSLHCETLNPYL 3729
Cdd:PTZ00050 315 PIGDKIELKAIKKVFG-----------DSGAPKLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINLENPDAEC 383
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1776025254 3730 QLTdspfyIVQEKQEwKSVTDCDgnelprrAGIS-SFGIGGVNA 3772
Cdd:PTZ00050 384 DLN-----LVQGKTA-HPLQSID-------AVLStSFGFGGVNT 414
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
1178-1639 |
9.30e-37 |
|
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.
Pssm-ID: 341238 [Multi-domain] Cd Length: 411 Bit Score: 146.34 E-value: 9.30e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1178 TLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLEDSEVfitltt 1257
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDV------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1258 selvntlswngvttalldqDWDEIAQtasdrkvltrtvtpenlayVIYTSGSTGKPKGVMIPHKALTNFLVSMGETPGLT 1337
Cdd:cd05912 75 -------------------KLDDIAT-------------------IMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLT 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1338 AEDKMLAVTTYcFDIAALELFL-PLIKGAHCYIcqteHTK-DVEKLKRDIRTIKPTVMQATPA--TWKMLFYSGWENEEN 1413
Cdd:cd05912 117 EDDNWLCALPL-FHISGLSILMrSVIYGMTVYL----VDKfDAEQVLHLINSGKVTIISVVPTmlQRLLEILGEGYPNNL 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1414 VKILCGGEALPETLKRYFLDTGSEAWNMFGPTETTIWSAVQRINDECSR-ATIGRPIANTQIYITDsqlAPVPAGVPGEL 1492
Cdd:cd05912 192 RCILLGGGPAPKPLLEQCKEKGIPVYQSYGMTETCSQIVTLSPEDALNKiGSAGKPLFPVELKIED---DGQPPYEVGEI 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1493 CIAGDGVAKGYYKKEELTDSRFIDNPFEpgsklyrTGDmarwlpggrieyIGRIDNQ----VKIR--------GFRIELG 1560
Cdd:cd05912 269 LLKGPNVTKGYLNRPDATEESFENGWFK-------TGD------------IGYLDEEgflyVLDRrsdliisgGENIYPA 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1561 DIESRLSEHPGILECVVVADMDNL-----AAYYTakhANASLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDR 1635
Cdd:cd05912 330 EIEEVLLSHPAIKEAGVVGIPDDKwgqvpVAFVV---SERPISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLR 406
|
....
gi 1776025254 1636 NSLK 1639
Cdd:cd05912 407 HELK 410
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
61-478 |
1.08e-36 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 146.26 E-value: 1.08e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 61 SYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNS-QLLPAFWGCVLTGVVPAPLAvpPTYAESSsgTQK-LKDAwtllD 138
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGGVGPGDRVAVLLERSaELVVAILAVLKAGAAYVPLD--PAYPAER--LAFiLEDA----G 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 139 KPAVITDRGMHQEMLDWAKEQGLEgfrAIIVEDLLSAEADTDWHQ--SSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMV 216
Cdd:TIGR01733 73 ARLLLTDSALASRLAGLVLPVILL---DPLELAALDDAPAPPPPDapSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 217 KGIIQMQGFTREDITFNWMP--FDhvggigmLHLRDVYL----GCQEINVSSETILMEPLKWLDWIDHYRASVTWAPNFA 290
Cdd:TIGR01733 150 AWLARRYGLDPDDRVLQFASlsFD-------ASVEEIFGallaGATLVVPPEDEERDDAALLAALIAEHPVTVLNLTPSL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 291 FGLVTDFAEEikdrkwDLSSMRYMLNGGEAMVAKVGRRILELlephgLPADAIRPAWGMSETSsgvIFSHEFTRAGTSDD 370
Cdd:TIGR01733 223 LALLAAALPP------ALASLRLVILGGEALTPALVDRWRAR-----GPGARLINLYGPTETT---VWSTATLVDPDDAP 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 371 DHF-VEIGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGYYQRPDLNESVFTEDG--------WFETGDLGFLR- 440
Cdd:TIGR01733 289 RESpVPIGRPLANTRLYVLDDDLRPVPVGVVGELYIGGPGVARGYLNRPELTAERFVPDPfaggdgarLYRTGDLVRYLp 368
|
410 420 430
....*....|....*....|....*....|....*...
gi 1776025254 441 NGRLTITGRTKDAIIINGinyysHAIesaveELSEIET 478
Cdd:TIGR01733 369 DGNLEFLGRIDDQVKIRG-----YRI-----ELGEIEA 396
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
1161-1641 |
1.22e-36 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 147.80 E-value: 1.22e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1161 QQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAE 1240
Cdd:PRK03640 10 QRAFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSRE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1241 RLEYMLEDSEVFITLTTSELVNTLswngvtTALLDQDWDEIAQTASDRKVLTRTVTPENLAYVIYTSGSTGKPKGVMIPH 1320
Cdd:PRK03640 90 ELLWQLDDAEVKCLITDDDFEAKL------IPGISVKFAELMNGPKEEAEIQEEFDLDEVATIMYTSGTTGKPKGVIQTY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1321 KaltNFL---VSMGETPGLTAEDKMLAVTTYcFDIAALE-LFLPLIKGAHCYIcqteHTK-DVEKLKRDIRTIKPTVMQA 1395
Cdd:PRK03640 164 G---NHWwsaVGSALNLGLTEDDCWLAAVPI-FHISGLSiLMRSVIYGMRVVL----VEKfDAEKINKLLQTGGVTIISV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1396 TPATWKMLF--YSGWENEENVK--ILCGGEALPETLKRyfldtgSEAWNM-----FGPTETTiwSAVQRINDECSRATI- 1465
Cdd:PRK03640 236 VSTMLQRLLerLGEGTYPSSFRcmLLGGGPAPKPLLEQ------CKEKGIpvyqsYGMTETA--SQIVTLSPEDALTKLg 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1466 --GRPIANTQIYITDsQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPFepgsklyRTGDmarwlpggrieyI 1543
Cdd:PRK03640 308 saGKPLFPCELKIEK-DGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQDGWF-------KTGD------------I 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1544 GRIDNQ----VKIR--------GFRIELGDIESRLSEHPGILECVVVADMDNL-----AAYYTAkhaNASLTARELRHFV 1606
Cdd:PRK03640 368 GYLDEEgflyVLDRrsdliisgGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKwgqvpVAFVVK---SGEVTEEELRHFC 444
|
490 500 510
....*....|....*....|....*....|....*
gi 1776025254 1607 KNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLKNI 1641
Cdd:PRK03640 445 EEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQL 479
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
33-555 |
2.38e-36 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 148.34 E-value: 2.38e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 33 EVLYRTAAELGDTKGIIYLQPDGTEVYQSYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNSQLLPAFWGCVLTGVVPA 112
Cdd:COG0365 13 NCLDRHAEGRGDKVALIWEGEDGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 113 PLAV---PPTYAEsssgtqKLKDAwtlldKP-AVITDRG--------MHQEMLDWAKEQgLEGFRAIIV----EDLLSAE 176
Cdd:COG0365 93 PVFPgfgAEALAD------RIEDA-----EAkVLITADGglrggkviDLKEKVDEALEE-LPSLEHVIVvgrtGADVPME 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 177 ADTDWH-----QSSP--------EDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQM-QGFTREDITFN-----WMpF 237
Cdd:COG0365 161 GDLDWDellaaASAEfepeptdaDDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYvLDLKPGDVFWCtadigWA-T 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 238 DHVGGI--GMLHlrdvylGCqeinvsseTILM--------EPLKWLDWIDHYRASVTWAPNFAFGLVTDFAEEIKdRKWD 307
Cdd:COG0365 240 GHSYIVygPLLN------GA--------TVVLyegrpdfpDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPL-KKYD 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 308 LSSMRYMLNGGEAMVAKVGRRILELLephGLPadaIRPAWGMSETSSGVIFSHEFT--RAGtsdddhfvEIGSPIPGFSM 385
Cdd:COG0365 305 LSSLRLLGSAGEPLNPEVWEWWYEAV---GVP---IVDGWGQTETGGIFISNLPGLpvKPG--------SMGKPVPGYDV 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 386 RIVNDHNELVEEGEIGRFQVSG--LSVTSGYYQRPDLNESVF--TEDGWFETGDLGFL-RNGRLTITGRTKDAIIINGIN 460
Cdd:COG0365 371 AVVDEDGNPVPPGEEGELVIKGpwPGMFRGYWNDPERYRETYfgRFPGWYRTGDGARRdEDGYFWILGRSDDVINVSGHR 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 461 YYSHAIESAVEELSEIetsytAACAVrLGQNS--TDQLAIFFVT---SAKLNDEqmsqLLRNIQSHVSQVIGvtpEYLLP 535
Cdd:COG0365 451 IGTAEIESALVSHPAV-----AEAAV-VGVPDeiRGQVVKAFVVlkpGVEPSDE----LAKELQAHVREELG---PYAYP 517
|
570 580
....*....|....*....|...
gi 1776025254 536 ---VQKEEIPKTAIGKIQRTQLK 555
Cdd:COG0365 518 reiEFVDELPKTRSGKIMRRLLR 540
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
1161-1579 |
3.54e-36 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 147.77 E-value: 3.54e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1161 QQAKKTPDRAAVSY------EGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYvDRSLDMLVGLLAILKAGGAYVPL- 1233
Cdd:cd05931 1 RRAAARPDRPAYTFlddeggREETLTYAELDRRARAIAARLQAVGKPGDRVLLLA-PPGLDFVAAFLGCLYAGAIAVPLp 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1234 --DPSYPAERLEYMLEDSEVFITLTTSELVNTLSWNGVTTALLDQDW----DEIAQTASDRkVLTRTVTPENLAYVIYTS 1307
Cdd:cd05931 80 ppTPGRHAERLAAILADAGPRVVLTTAAALAAVRAFAASRPAAGTPRllvvDLLPDTSAAD-WPPPSPDPDDIAYLQYTS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1308 GSTGKPKGVMIPHKALTNFLVSMGETPGLTAEDKMlaVT---TYcFD---IAAleLFLPLIKGAHCYICQTEHTkdVEKL 1381
Cdd:cd05931 159 GSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVV--VSwlpLY-HDmglIGG--LLTPLYSGGPSVLMSPAAF--LRRP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1382 KRDIRTI---KPTVMQA------------TPATWKMLFYSGWENeenvkILCGGEAL-PETLKRyFLDTGSEA---WNMF 1442
Cdd:cd05931 232 LRWLRLIsryRATISAApnfaydlcvrrvRDEDLEGLDLSSWRV-----ALNGAEPVrPATLRR-FAEAFAPFgfrPEAF 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1443 GPT----ETTIWSAVQRINDE-------------------------CSRATIGRPIANTQIYITDSQ-LAPVPAGVPGEL 1492
Cdd:cd05931 306 RPSyglaEATLFVSGGPPGTGpvvlrvdrdalagravavaaddpaaRELVSCGRPLPDQEVRIVDPEtGRELPDGEVGEI 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1493 CIAGDGVAKGYYKKEELTDSRFIDNPFEPGSKLYRTGDMARwLPGGRIeYI-GRIDNQVKIRGFRIELGDIESRLSE-HP 1570
Cdd:cd05931 386 WVRGPSVASGYWGRPEATAETFGALAATDEGGWLRTGDLGF-LHDGEL-YItGRLKDLIIVRGRNHYPQDIEATAEEaHP 463
|
....*....
gi 1776025254 1571 GILECVVVA 1579
Cdd:cd05931 464 ALRPGCVAA 472
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
1154-1649 |
1.42e-35 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 146.07 E-value: 1.42e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1154 TFHELFEQQAKKTPDRAAVSY--EGQTLTYRELDERSTQLAIYLQAHGVGP-DRLaGIYVDRSLDMLVGLLAILKAGGAY 1230
Cdd:PRK12583 19 TIGDAFDATVARFPDREALVVrhQALRYTWRQLADAVDRLARGLLALGVQPgDRV-GIWAPNCAEWLLTQFATARIGAIL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1231 VPLDPSYPAERLEYMLEDSEVFITLT-----TSELVNTLS------WNGVTTALLDQD--------------------WD 1279
Cdd:PRK12583 98 VNINPAYRASELEYALGQSGVRWVICadafkTSDYHAMLQellpglAEGQPGALACERlpelrgvvslapapppgflaWH 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1280 EI---AQTASDRKVLTRT--VTPENLAYVIYTSGSTGKPKGVMIPHKALTNFLVSMGETPGLTAEDKMLA-VTTY-CFDI 1352
Cdd:PRK12583 178 ELqarGETVSREALAERQasLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVpVPLYhCFGM 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1353 AaLELFLPLIKGAhCYICQTEHTKDVEKLkRDIRTIKPTVMQATPAtwkmLFYSGWENEE---------NVKILCGGEAL 1423
Cdd:PRK12583 258 V-LANLGCMTVGA-CLVYPNEAFDPLATL-QAVEEERCTALYGVPT----MFIAELDHPQrgnfdlsslRTGIMAGAPCP 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1424 PETLKRYFLDTG-SEAWNMFGPTETTIWSAVQRINDECSR--ATIGRPIANTQIYITDSQLAPVPAGVPGELCIAGDGVA 1500
Cdd:PRK12583 331 IEVMRRVMDEMHmAEVQIAYGMTETSPVSLQTTAADDLERrvETVGRTQPHLEVKVVDPDGATVPRGEIGELCTRGYSVM 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1501 KGYYKKEELTdSRFIDnpfepGSKLYRTGDMARWLPGGRIEYIGRIDNQVkIRGFR-IELGDIESRLSEHPGILECVVVA 1579
Cdd:PRK12583 411 KGYWNNPEAT-AESID-----EDGWMHTGDLATMDEQGYVRIVGRSKDMI-IRGGEnIYPREIEEFLFTHPAVADVQVFG 483
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1776025254 1580 DMDNlaaYYTAK-------HANASLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLKniDLSGEQLK 1649
Cdd:PRK12583 484 VPDE---KYGEEivawvrlHPGHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMR--EISIEELA 555
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
172-556 |
1.43e-35 |
|
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.
Pssm-ID: 341238 [Multi-domain] Cd Length: 411 Bit Score: 142.87 E-value: 1.43e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 172 LLSAEADTDwhqsspeDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDitfNW---MPFDHVGGIGMLhL 248
Cdd:cd05912 69 LKDSDVKLD-------DIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLTEDD---NWlcaLPLFHISGLSIL-M 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 249 RDVYLGCQeinvsseTILME---PLKWLDWIDHYRASVtwapnfaFGLVTDFAEEIKDR--KWDLSSMRYMLNGGeamvA 323
Cdd:cd05912 138 RSVIYGMT-------VYLVDkfdAEQVLHLINSGKVTI-------ISVVPTMLQRLLEIlgEGYPNNLRCILLGG----G 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 324 KVGRRILELLEPHGLPadaIRPAWGMSETSSGVI-FSHEF--TRAGTSdddhfveiGSPIPGFSMRIVNDHNELVEEGEI 400
Cdd:cd05912 200 PAPKPLLEQCKEKGIP---VYQSYGMTETCSQIVtLSPEDalNKIGSA--------GKPLFPVELKIEDDGQPPYEVGEI 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 401 grfQVSGLSVTSGYYQRPDLNESVFtEDGWFETGDLGFLRN-GRLTITGRTKDAIIINGINYYSHAIESAVEELSEIets 479
Cdd:cd05912 269 ---LLKGPNVTKGYLNRPDATEESF-ENGWFKTGDIGYLDEeGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAI--- 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 480 ytAACAVrLGQnsTD----QLAI-FFVTSAKLNDEQMSQLLrniQSHVSQvigvtpeYLLPVQ---KEEIPKTAIGKIQR 551
Cdd:cd05912 342 --KEAGV-VGI--PDdkwgQVPVaFVVSERPISEEELIAYC---SEKLAK-------YKVPKKiyfVDELPRTASGKLLR 406
|
....*
gi 1776025254 552 TQLKT 556
Cdd:cd05912 407 HELKQ 411
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
184-551 |
1.57e-35 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341240 [Multi-domain] Cd Length: 463 Bit Score: 144.12 E-value: 1.57e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 184 SSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDHVGGIGMLHLRDVYLGCQEI---NV 260
Cdd:cd05914 86 SDEDDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVfldKI 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 261 SSETILME-----------PLKWLdwIDHYRASVTWAPNFAFGLVTDFAEEIKDRKwdLSSM-------------RYMLN 316
Cdd:cd05914 166 PSAKIIALafaqvtptlgvPVPLV--IEKIFKMDIIPKLTLKKFKFKLAKKINNRK--IRKLafkkvheafggniKEFVI 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 317 GGeamvAKVGRRILELLEPHGLPAdAIrpAWGMSETSSGVIFSH-EFTRAGTSdddhfveiGSPIPGFSMRIvNDHNELV 395
Cdd:cd05914 242 GG----AKINPDVEEFLRTIGFPY-TI--GYGMTETAPIISYSPpNRIRLGSA--------GKVIDGVEVRI-DSPDPAT 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 396 EEGEIgrfQVSGLSVTSGYYQRPDLNESVFTEDGWFETGDLG-FLRNGRLTITGRTKDAIII-NGINYYSHAIESAVEEL 473
Cdd:cd05914 306 GEGEI---IVRGPNVMKGYYKNPEATAEAFDKDGWFHTGDLGkIDAEGYLYIRGRKKEMIVLsSGKNIYPEEIEAKINNM 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 474 SEIETSYTAAcavrlgQNSTDQLAI-----FFVTSAKLNDEQMSQLLRNIQSHVSQvigVTPEYL----LPVQKEEIPKT 544
Cdd:cd05914 383 PFVLESLVVV------QEKKLVALAyidpdFLDVKALKQRNIIDAIKWEVRDKVNQ---KVPNYKkiskVKIVKEEFEKT 453
|
....*..
gi 1776025254 545 AIGKIQR 551
Cdd:cd05914 454 PKGKIKR 460
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
1164-1639 |
3.25e-35 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 144.36 E-value: 3.25e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1164 KKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGP-DRLAGIYVDRSlDMLVGLLAILKAGGAYVPLDPSYPAERL 1242
Cdd:PRK06188 23 KRYPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTgDAVALLSLNRP-EVLMAIGAAQLAGLRRTALHPLGSLDDH 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1243 EYMLEDSEVfitltTSELVNTLSWNGVTTALLDQ-----------------DWDEIAQTASDRKVLTRTVTPEnLAYVIY 1305
Cdd:PRK06188 102 AYVLEDAGI-----STLIVDPAPFVERALALLARvpslkhvltlgpvpdgvDLLAAAAKFGPAPLVAAALPPD-IAGLAY 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1306 TSGSTGKPKGVMIPHKALTNFLVSMGETPGLTAEDKMLAVTTYCFdiAALELFLP-LIKGAHCYICQTEHTKDVeklkrd 1384
Cdd:PRK06188 176 TGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSH--AGGAFFLPtLLRGGTVIVLAKFDPAEV------ 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1385 IRTIKPTVMQATPATWKMLF------------YSGWENeenvkILCGGEAL-PETLKryfldtgsEAWNMFGP------- 1444
Cdd:PRK06188 248 LRAIEEQRITATFLVPTMIYalldhpdlrtrdLSSLET-----VYYGASPMsPVRLA--------EAIERFGPifaqyyg 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1445 -TETTIWSAVQRINDECSR-----ATIGRPIANTQIYITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNp 1518
Cdd:PRK06188 315 qTEAPMVITYLRKRDHDPDdpkrlTSCGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAFRDG- 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1519 fepgskLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMDN-----LAAYYTAKhA 1593
Cdd:PRK06188 394 ------WLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEkwgeaVTAVVVLR-P 466
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1776025254 1594 NASLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLK 1639
Cdd:PRK06188 467 GAAVDAAELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALR 512
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
1154-1634 |
3.94e-35 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 144.26 E-value: 3.94e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1154 TFHELFEQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPL 1233
Cdd:PRK07798 4 NIADLFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1234 DPSYPAERLEYMLEDSEVfitlttSELVNTLSWNGVTTALLDQ-----------------------DWDEI-AQTASDRK 1289
Cdd:PRK07798 84 NYRYVEDELRYLLDDSDA------VALVYEREFAPRVAEVLPRlpklrtlvvvedgsgndllpgavDYEDAlAAGSPERD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1290 VLTRtvTPENLaYVIYTSGSTGKPKGVMIPHKALtnFLVSMGETPGLTAEDKM--LAVTTYCFDIAALELFL--PLIKGA 1365
Cdd:PRK07798 158 FGER--SPDDL-YLLYTGGTTGMPKGVMWRQEDI--FRVLLGGRDFATGEPIEdeEELAKRAAAGPGMRRFPapPLMHGA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1366 ------------HCYICQTEHTKDVEKLKRDIRTIKPTVMQ------ATPATWKMLFYSGWENEENVKILCGGEALPETL 1427
Cdd:PRK07798 233 gqwaafaalfsgQTVVLLPDVRFDADEVWRTIEREKVNVITivgdamARPLLDALEARGPYDLSSLFAIASGGALFSPSV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1428 KRYFLD-------TGSeawnmFGPTET----TIWSAVQRINDECSRATIGRPIAntqiyITDSQLAPVPAGVPGELCIAG 1496
Cdd:PRK07798 313 KEALLEllpnvvlTDS-----IGSSETgfggSGTVAKGAVHTGGPRFTIGPRTV-----VLDEDGNPVEPGSGEIGWIAR 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1497 DG-VAKGYYKKEELTDSRF--IDnpfepGSKLYRTGDMARWLPGGRIEYIGRiDNQV------KIrgFRIElgdIESRLS 1567
Cdd:PRK07798 383 RGhIPLGYYKDPEKTAETFptID-----GVRYAIPGDRARVEADGTITLLGR-GSVCintggeKV--FPEE---VEEALK 451
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1776025254 1568 EHPGILECVVVADMDN-----LAAyYTAKHANASLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKID 1634
Cdd:PRK07798 452 AHPDVADALVVGVPDErwgqeVVA-VVQLREGARPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGKAD 522
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
1154-1652 |
5.92e-35 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 144.04 E-value: 5.92e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1154 TFHELFEQQAKKTPDRAAV------SYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAG 1227
Cdd:PRK13295 25 TINDDLDACVASCPDKTAVtavrlgTGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1228 GAYVPLDPSYPAERLEYMLE--DSEVFITLTT------SELVNTL--SW--------------NGVTTALLDQDWDeiaQ 1283
Cdd:PRK13295 105 AVLNPLMPIFRERELSFMLKhaESKVLVVPKTfrgfdhAAMARRLrpELpalrhvvvvggdgaDSFEALLITPAWE---Q 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1284 TASDRKVLTRTVT-PENLAYVIYTSGSTGKPKGVMIPHKALTNFLVSMGETPGLTAEDKMLAVTTycfdIAALELF---- 1358
Cdd:PRK13295 182 EPDAPAILARLRPgPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASP----MAHQTGFmygl 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1359 -LPLIKGAHCYIcqtEHTKDVEKLKRDIRTIKPT-VMQATPatwkmlFYSGW-----ENEENV----KILCGGEALPETL 1427
Cdd:PRK13295 258 mMPVMLGATAVL---QDIWDPARAAELIRTEGVTfTMASTP------FLTDLtravkESGRPVsslrTFLCAGAPIPGAL 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1428 KRyfldtgsEAWNMFGPTETTIW-----SAVQRIN----DECSRATIGRPIANTQIYITDSQLAPVPAGVPGELCIAGDG 1498
Cdd:PRK13295 329 VE-------RARAALGAKIVSAWgmtenGAVTLTKlddpDERASTTDGCPLPGVEVRVVDADGAPLPAGQIGRLQVRGCS 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1499 VAKGYYKKEELTDSRFiDNPFEpgsklyrTGDMARWLPGGRIEYIGRiDNQVKIRGFR-IELGDIESRLSEHPGILECVV 1577
Cdd:PRK13295 402 NFGGYLKRPQLNGTDA-DGWFD-------TGDLARIDADGYIRISGR-SKDVIIRGGEnIPVVEIEALLYRHPAIAQVAI 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1578 VADMD-----NLAAYYTAKhANASLTARELRHFVKN---ALPAYmvPSYFIQLDHMPLTPNGKIDRNSLKnidlsgEQLK 1649
Cdd:PRK13295 473 VAYPDerlgeRACAFVVPR-PGQSLDFEEMVEFLKAqkvAKQYI--PERLVVRDALPRTPSGKIQKFRLR------EMLR 543
|
...
gi 1776025254 1650 QRQ 1652
Cdd:PRK13295 544 GED 546
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1305-1639 |
9.92e-35 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 138.56 E-value: 9.92e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1305 YTSGSTGKPKGVMIPHKALTNFLVSMGETPGLTAEDKM-LAVTTY-CFDIAaLELFLPLIKGAHCYIcqTEHTKDVEKLK 1382
Cdd:cd05917 9 FTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLcIPVPLFhCFGSV-LGVLACLTHGATMVF--PSPSFDPLAVL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1383 RDIRTIKPTVMQATPATWKMLFYSGWENEENVKILCGG-----EALPETLKRYFldtgsEAWNM------FGPTETTIWS 1451
Cdd:cd05917 86 EAIEKEKCTALHGVPTMFIAELEHPDFDKFDLSSLRTGimagaPCPPELMKRVI-----EVMNMkdvtiaYGMTETSPVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1452 AVQRINDECSR--ATIGRPIANTQIYITDSQLAPVPA-GVPGELCIAGDGVAKGYYKKEELTdSRFIDnpfepGSKLYRT 1528
Cdd:cd05917 161 TQTRTDDSIEKrvNTVGRIMPHTEAKIVDPEGGIVPPvGVPGELCIRGYSVMKGYWNDPEKT-AEAID-----GDGWLHT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1529 GDMARWLPGGRIEYIGRIDNQVkIRGFR-IELGDIESRLSEHPGILECVVVADMD-----NLAAYyTAKHANASLTAREL 1602
Cdd:cd05917 235 GDLAVMDEDGYCRIVGRIKDMI-IRGGEnIYPREIEEFLHTHPKVSDVQVVGVPDerygeEVCAW-IRLKEGAELTEEDI 312
|
330 340 350
....*....|....*....|....*....|....*..
gi 1776025254 1603 RHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLK 1639
Cdd:cd05917 313 KAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
53-555 |
1.07e-34 |
|
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.
Pssm-ID: 341249 [Multi-domain] Cd Length: 493 Bit Score: 142.07 E-value: 1.07e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 53 PDGTEVYqSYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNSQLLPAFWGCVLTGVVPAPLAvpPTYAEsssgtQKLKD 132
Cdd:cd05926 9 PGSTPAL-TYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLN--PAYKK-----AEFEF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 133 AWTLLDKPAVITDRGMHQEMLDWAK-------EQGLEGFRAIIV---EDLLSAEADTDWHQSS----PEDLALLLLTSGS 198
Cdd:cd05926 81 YLADLGSKLVLTPKGELGPASRAASklglailELALDVGVLIRApsaESLSNLLADKKNAKSEgvplPDDLALILHTSGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 199 TGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDHVGG-IGMLhLRDVYLGcqeinvSSETILM--EPLKWLDW 275
Cdd:cd05926 161 TGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLVVMPLFHVHGlVASL-LSTLAAG------GSVVLPPrfSASTFWPD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 276 IDHYRAsvTW---APNFAFGLVTDFAEEIKDRKwdlSSMRYMLNGGEAMVAKVGRRILE-----LLEphglpadairpAW 347
Cdd:cd05926 234 VRDYNA--TWytaVPTIHQILLNRPEPNPESPP---PKLRFIRSCSASLPPAVLEALEAtfgapVLE-----------AY 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 348 GMSETSSGViFSHEFtragtsdDDHFVEIGS-PIP-GFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGYYQRPDLNESVF 425
Cdd:cd05926 298 GMTEAAHQM-TSNPL-------PPGPRKPGSvGKPvGVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAA 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 426 TEDGWFETGDLGFL-RNGRLTITGRTKDAIIINGinyyshaiesavEELS--EIEtsytaacAVRLGQNSTDQLAIFFVT 502
Cdd:cd05926 370 FKDGWFRTGDLGYLdADGYLFLTGRIKELINRGG------------EKISplEVD-------GVLLSHPAVLEAVAFGVP 430
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1776025254 503 SAKLNDEQMSQLLRNIQSHVS--QVIGVTPEYLLP--VQKE-----EIPKTAIGKIQRTQLK 555
Cdd:cd05926 431 DEKYGEEVAAAVVLREGASVTeeELRAFCRKHLAAfkVPKKvyfvdELPKTATGKIQRRKVA 492
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
184-990 |
2.31e-34 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 147.24 E-value: 2.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 184 SSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTRED-------ITFN------WMPFdhVGGIGMLhLR- 249
Cdd:PRK05691 2330 SLPQHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDcelhfysINFDaaserlLVPL--LCGARVV-LRa 2406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 250 ----DVYLGCQEINVSSETILmeplkwldwidhyrasvTWAPNFAFGLVTDFAEEikdrkWDLSSMRYMLNGGEAMVAKV 325
Cdd:PRK05691 2407 qgqwGAEEICQLIREQQVSIL-----------------GFTPSYGSQLAQWLAGQ-----GEQLPVRMCITGGEALTGEH 2464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 326 GRRILELLEPhglpaDAIRPAWGMSETssgVIF-----SHEFTRAGTSDddhfVEIGSPIPGFSMRIVNDHNELVEEGEI 400
Cdd:PRK05691 2465 LQRIRQAFAP-----QLFFNAYGPTET---VVMplaclAPEQLEEGAAS----VPIGRVVGARVAYILDADLALVPQGAT 2532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 401 GRFQVSGLSVTSGYYQRPDLNESVFTEDGW-------FETGDLGFLR-NGRLTITGRTKDAIIINGINYyshaiesaveE 472
Cdd:PRK05691 2533 GELYVGGAGLAQGYHDRPGLTAERFVADPFaadggrlYRTGDLVRLRaDGLVEYVGRIDHQVKIRGFRI----------E 2602
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 473 LSEIETSYTAACAVR------LGQNSTDQLAIFFVTS-AKLNDEQMSQLLRNIQSHVSQVIgvtPEYLLPVQ---KEEIP 542
Cdd:PRK05691 2603 LGEIESRLLEHPAVReavvlaLDTPSGKQLAGYLVSAvAGQDDEAQAALREALKAHLKQQL---PDYMVPAHlilLDSLP 2679
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 543 KTAIGKIQRTQLKTSfengefdhllhkpnrmnDAVQDEEMQQADhvkrvREEIQEHLLTCLTEELHVSRdwVEPNANIQS 622
Cdd:PRK05691 2680 LTANGKLDRRALPAP-----------------DPELNRQAYQAP-----RSELEQQLAQIWREVLNVER--VGLGDNFFE 2735
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 623 LGVNSIKMMKLIrSIEKNYHIKLTAREIHQYPTIERLASYLSEHEDLSSSSADKKGTdtyktepersqatfQPLSEVQKg 702
Cdd:PRK05691 2736 LGGDSILSIQVV-SRARQLGIHFSPRDLFQHQTVQTLAAVATHSEAAQAEQGPLQGA--------------SGLTPIQH- 2799
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 703 lWTLQKMSPEKSAYHVPLCFKFSSGLHLETLQQAFGLVLNQHPILKHVIQEKDGVPILKNEPALSIEI-KTENISSMKES 781
Cdd:PRK05691 2800 -WFFDSPVPQPQHWNQALLLEPRQALDPALLEQALQALVEHHDALRLRFSQADGRWQAEYRAVTAQELlWQVTVADFAEC 2878
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 782 dipAFLRKKVKEPYVKENSPLVRVMSFSRSEQEHFLLVVIHHLIFDGVSSVTFIHSLFDTYQLLLKGQQPEIAVSPAIYH 861
Cdd:PRK05691 2879 ---AALFADAQRSLDLQQGPLLRALLVDGPQGQQRLLLAIHHLVVDGVSWRVLLEDLQALYRQLSAGAEPALPAKTSAFR 2955
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 862 DFAA-WEKnmLAGKDGVKHR-TYWQKQLSGtlPNLQLPKVSASSVSEFRE-DTYTRRLSSGFMNQVRMFA-KEHSVNVTT 937
Cdd:PRK05691 2956 DWAArLQA--YAGSESLREElGWWQAQLGG--PRAELPCDRPQGGNLNRHaQTVSVRLDAERTRQLLQQApAAYRTQVND 3031
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*...
gi 1776025254 938 VFLSCYMMLLGRYTGQKEQIVGMPAMVRpEERFDD-----AIGHFLNMLPIRseLNPA 990
Cdd:PRK05691 3032 LLLTALARVLCRWSGQPSVLVQLEGHGR-EALFDDidltrSVGWFTSAYPLR--LTPA 3086
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
188-558 |
3.72e-34 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 136.31 E-value: 3.72e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 188 DLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDHVGGIGMLHlRDVYLGcqeinvsSETILM 267
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLAILV-RSLLAG-------AELVLL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 268 EPlKWLDWIDHYRASVTWA----PNFAFGLVTDFAEEikdrkwDLSSMRYMLNGGEAMVAKVGRRILELlephGLPadaI 343
Cdd:cd17630 73 ER-NQALAEDLAPPGVTHVslvpTQLQRLLDSGQGPA------ALKSLRAVLLGGAPIPPELLERAADR----GIP---L 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 344 RPAWGMSETSSGVIfsheftrAGTSDDDHFVEIGSPIPGFSMRIVNDhnelveegeiGRFQVSGLSVTSGYYQRPDLNEs 423
Cdd:cd17630 139 YTTYGMTETASQVA-------TKRPDGFGRGGVGVLLPGRELRIVED----------GEIWVGGASLAMGYLRGQLVPE- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 424 vFTEDGWFETGDLGFLR-NGRLTITGRTKDAIIINGINYYSHAIESAVEELSEIEtsytAACAV-----RLGQnstdQLA 497
Cdd:cd17630 201 -FNEDGWFTTKDLGELHaDGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVR----DAFVVgvpdeELGQ----RPV 271
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1776025254 498 IFFVTSAKLNDEQMSQllrniqsHVSQVIGV--TPEYLLPVQkeEIPKTAIGKIQRTQLKTSF 558
Cdd:cd17630 272 AVIVGRGPADPAELRA-------WLKDKLARfkLPKRIYPVP--ELPRTGGGKVDRRALRAWL 325
|
|
| PKS_DH |
smart00826 |
Dehydratase domain in polyketide synthase (PKS) enzymes; |
2373-2539 |
4.16e-34 |
|
Dehydratase domain in polyketide synthase (PKS) enzymes;
Pssm-ID: 214837 Cd Length: 167 Bit Score: 130.81 E-value: 4.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2373 HPLLHQNTSDFSEQkfSSVFTG-----DEFFLRDHVVRGKPVLPGVAYLEMAYAAinqaaGSEIGQDVRIRLNHTVWVQP 2447
Cdd:smart00826 1 HPLLGARVELADGG--GVVLTGrlslrTHPWLADHRVGGTVVLPGAAYVELALAA-----ADEVGGGAPARLEELTLEAP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2448 VVVDRHSA-QVDISLF-PEEDGKITFDIYSTQEDGDDPVIHSQGSAELASAAETPVADLTEISRRCGKGKMSPDQFYEEG 2525
Cdd:smart00826 74 LVLPEDGAvRVQVVVGaPDEDGRRTFTVYSRPDGDGPWTRHATGTLRPAAAAPAAPAADLAAWPPAGAEPVDVDDLYERL 153
|
170
....*....|....
gi 1776025254 2526 RSRGMFHGPAFQGI 2539
Cdd:smart00826 154 AARGLEYGPAFQGL 167
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
1151-1652 |
4.22e-34 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 141.44 E-value: 4.22e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1151 PYITFHELFEQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAH-GVGP-DRLAgIYVDRSLDMLVGLLAILKAGG 1228
Cdd:PRK05677 22 EYPNIQAVLKQSCQRFADKPAFSNLGKTLTYGELYKLSGAFAAWLQQHtDLKPgDRIA-VQLPNVLQYPVAVFGAMRAGL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1229 AYVPLDPSYPAERLEYMLEDS--EVFITLTT--SELVNTLSWNGVTTALLDQDWD------------------------E 1280
Cdd:PRK05677 101 IVVNTNPLYTAREMEHQFNDSgaKALVCLANmaHLAEKVLPKTGVKHVIVTEVADmlpplkrllinavvkhvkkmvpayH 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1281 IAQTASDRKVLTR---------TVTPENLAYVIYTSGSTGKPKGVMIPHKaltNFLVSMGETPGLTAEDKMLAVTTYcfd 1351
Cdd:PRK05677 181 LPQAVKFNDALAKgagqpvteaNPQADDVAVLQYTGGTTGVAKGAMLTHR---NLVANMLQCRALMGSNLNEGCEIL--- 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1352 IAALELFLPLIKGAHCYICQT--EHT------KDVEKLKRDIRTIKPTVMQATpatwKMLFYSGWENEENVKI------- 1416
Cdd:PRK05677 255 IAPLPLYHIYAFTFHCMAMMLigNHNilisnpRDLPAMVKELGKWKFSGFVGL----NTLFVALCNNEAFRKLdfsalkl 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1417 -LCGGEALP-ETLKRYFLDTGSEAWNMFGPTETtiwSAVQRIN--DECSRATIGRPIANTQIYITDSQLAPVPAGVPGEL 1492
Cdd:PRK05677 331 tLSGGMALQlATAERWKEVTGCAICEGYGMTET---SPVVSVNpsQAIQVGTIGIPVPSTLCKVIDDDGNELPLGEVGEL 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1493 CIAGDGVAKGYYKKEELTDSRFIDNPFepgsklYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGI 1572
Cdd:PRK05677 408 CVKGPQVMKGYWQRPEATDEILDSDGW------LKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGV 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1573 LECVVVADMDNLAA----YYTAKHANASLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLKNidlsgEQL 1648
Cdd:PRK05677 482 LQCAAIGVPDEKSGeaikVFVVVKPGETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRRELRD-----EEL 556
|
....
gi 1776025254 1649 KQRQ 1652
Cdd:PRK05677 557 KKAG 560
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
1761-2181 |
5.70e-34 |
|
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, including beta-ketoacyl [ACP] synthase, type I and II and polyketide synthases.They are characterized by the utlization of acyl carrier protein (ACP) thioesters as primer substrates, as well as the nature of their active site residues.
Pssm-ID: 238424 [Multi-domain] Cd Length: 407 Bit Score: 137.96 E-value: 5.70e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1761 SVAIIGISCEFP---GAKNHDEFWENLRDGKESIAFFN--KEELQRFGiskeiaenADYVPaKASIEGKDrfdpsffqis 1835
Cdd:cd00828 2 RVVITGIGVVSPhgeGCDEVEEFWEALREGRSGIAPVArlKSRFDRGV--------AGQIP-TGDIPGWD---------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1836 PKDAEFMDPQLRMLLTHSWKAIEDAGYAAGQI---PQTSVFMSASNNSYRALLPSDTTESLETPDGYVSWVLAQSGTIP- 1911
Cdd:cd00828 63 AKRTGIVDRTTLLALVATEEALADAGITDPYEvhpSEVGVVVGSGMGGLRFLRRGGKLDARAVNPYVSPKWMLSPNTVAg 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1912 TMISHKLGLRGPSYFVHANCSSSLIGLHSAYKSLLSAESDYALVGGA-TLHTESNIGYVHQPGL---NFSSDGHIKAFDA 1987
Cdd:cd00828 143 WVNILLLSSHGPIKTPVGACATALEALDLAVEAIRSGKADIVVVGGVeDPLEEGLSGFANMGALstaEEEPEEMSRPFDE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1988 SADGMIGGEGVAVVLLKKAADAVKDGDHIYALLRGIGVNNDGADKvgFYAPSVKGQADVVQQVMNQTKIHPESICYVEAH 2067
Cdd:cd00828 223 TRDGFVEAEGAGVLVLERAELALARGAPIYGRVAGTASTTDGAGR--SVPAGGKGIARAIRTALAKAGLSLDDLDVISAH 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2068 GTGTKLGDPIELAALTnvyRQYTNKTQFCGIGSVKTNIGHLDTAAGLAGCIKVVMSLYHQELAPSINYKEPNPNTDLASS 2147
Cdd:cd00828 301 GTSTPANDVAESRAIA---EVAGALGAPLPVTAQKALFGHSKGAAGALQLIGALQSLEHGLIPPTANLDDVDPDVEHLSV 377
|
410 420 430
....*....|....*....|....*....|....*.
gi 1776025254 2148 PfyvvdqkkTLSREIQ-THRAALS-SFGLGGTNTHA 2181
Cdd:cd00828 378 V--------GLSRDLNlKVRAALVnAFGFGGSNAAL 405
|
|
| CT_NRPS-like |
cd19542 |
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ... |
695-1111 |
7.71e-34 |
|
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike bacterial NRPS, which typically have specialized terminal thioesterase (TE) domains to cyclize peptide products, many fungal NRPSs employ a terminal condensation-like (CT) domain to produce macrocyclic peptidyl products (e.g. cyclosporine and echinocandin). Domains in this subfamily (which includes both terminal and non-terminal domains) typically have a non-canonical conserved [SN]HxxxDx(14)Y motif at their active site compared to the standard Condensation (C) domain active site motif (HHxxxD). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380464 [Multi-domain] Cd Length: 401 Bit Score: 137.44 E-value: 7.71e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 695 PLSEVQKGLWTLQKMSPekSAYHVPLCFKFSSGLHLETLQQAFGLVLNQHPILKHVIQEKDGVP-----ILKNePALSIE 769
Cdd:cd19542 3 PCTPMQEGMLLSQLRSP--GLYFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFVESSAEGtflqvVLKS-LDPPIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 770 IKTENissmkESDIPAFLRKKVKEPyVKENSPLVRVMSFSRSEQEHFLLVVIHHLIFDGVSsvtfIHSLFDTYQLLLKGQ 849
Cdd:cd19542 80 EVETD-----EDSLDALTRDLLDDP-TLFGQPPHRLTLLETSSGEVYLVLRISHALYDGVS----LPIILRDLAAAYNGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 850 QPEIAVSpaiYHDFAAweknMLAGKDGVKHRTYWQKQLSGTLPNLQlPkvsassvSEFREDTYTRRLSSGFMNQ--VRMF 927
Cdd:cd19542 150 LLPPAPP---FSDYIS----YLQSQSQEESLQYWRKYLQGASPCAF-P-------SLSPKRPAERSLSSTRRSLakLEAF 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 928 AKEHSVNVTTVFLSCYMMLLGRYTGQKEQIVGMpaMVR----PEERFDDAIGHFLNMLPIRSELNPADTFSSFISKLQLT 1003
Cdd:cd19542 215 CASLGVTLASLFQAAWALVLARYTGSRDVVFGY--VVSgrdlPVPGIDDIVGPCINTLPVRVKLDPDWTVLDLLRQLQQQ 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1004 ILDGLDHAAYPFPKMVRDLNIPRSQagsPVFQTAFFYQNFLQSGSYQSLLSRYadfFSVDYVEYIHqegEYELVFELWET 1083
Cdd:cd19542 293 YLRSLPHQHLSLREIQRALGLWPSG---TLFNTLVSYQNFEASPESELSGSSV---FELSAAEDPT---EYPVAVEVEPS 363
|
410 420 430
....*....|....*....|....*....|.
gi 1776025254 1084 EEKMELNIKYNTGLFD---AASISAMFDHFV 1111
Cdd:cd19542 364 GDSLKVSLAYSTSVLSeeqAEELLEQFDDIL 394
|
|
| PTZ00050 |
PTZ00050 |
3-oxoacyl-acyl carrier protein synthase; Provisional |
1778-2186 |
1.31e-33 |
|
3-oxoacyl-acyl carrier protein synthase; Provisional
Pssm-ID: 240245 [Multi-domain] Cd Length: 421 Bit Score: 137.13 E-value: 1.31e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1778 DEFWENLRDGKESIAFFNKEELQRFGISKEIAENADYVPA-----KASIEGKDrFDPSFFQISPKDaefmDPQLRMLLTH 1852
Cdd:PTZ00050 10 ESTWEALIAGKSGIRKLTEFPKFLPDCIPEQKALENLVAAmpcqiAAEVDQSE-FDPSDFAPTKRE----SRATHFAMAA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1853 SWKAIEDAG--YAAGQIP-QTSVFMSASNNSYRALLpsDTTESLETpDGY--VSWVLaqsgtIPTMISH--------KLG 1919
Cdd:PTZ00050 85 AREALADAKldILSEKDQeRIGVNIGSGIGSLADLT--DEMKTLYE-KGHsrVSPYF-----IPKILGNmaaglvaiKHK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1920 LRGPSYFVHANC--SSSLIGlhSAYKSLLSAESDYALVGG--ATLHTESNIGYVHQPGL----NFSSDGHIKAFDASADG 1991
Cdd:PTZ00050 157 LKGPSGSAVTACatGAHCIG--EAFRWIKYGEADIMICGGteASITPVSFAGFSRMRALctkyNDDPQRASRPFDKDRAG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1992 MIGGEGVAVVLLKKAADAVKDGDHIYALLRGIGVNNDGADkVGFYAPSVKGQADVVQQVMNQT-KIHPESICYVEAHGTG 2070
Cdd:PTZ00050 235 FVMGEGAGILVLEELEHALRRGAKIYAEIRGYGSSSDAHH-ITAPHPDGRGARRCMENALKDGaNININDVDYVNAHATS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2071 TKLGDPIELAALTNVYRQYTNKTqfCGIGSVKTNIGHLDTAAGLAGCIKVVMSLYHQELAPSINYKEPNPNTDLasspfy 2150
Cdd:PTZ00050 314 TPIGDKIELKAIKKVFGDSGAPK--LYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINLENPDAECDL------ 385
|
410 420 430
....*....|....*....|....*....|....*..
gi 1776025254 2151 vVDQKKTLSREIQTHRAALS-SFGLGGTNTHAIFEQF 2186
Cdd:PTZ00050 386 -NLVQGKTAHPLQSIDAVLStSFGFGGVNTALLFTKY 421
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
75-555 |
1.46e-33 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 137.96 E-value: 1.46e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 75 GLRQSGLKAKQSVILQLGDNSQLLPAFWGCVLTGVVPAPLAVP--PTYAESSsgtqkLKDAWTLLDKPAVITDRGMHQEM 152
Cdd:cd05922 9 ALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRLGLVFVPlnPTLKESV-----LRYLVADAGGRIVLADAGAADRL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 153 LDWAKEQGLEGFrAIIVEDLLSAEADTDWHQSSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITF 232
Cdd:cd05922 84 RDALPASPDPGT-VLDADGIRAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDRAL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 233 NWMPFDHVGGIGMLHlrdVYLGCQEINVSSETILMEPLKWLDWIDHYRASVTWAPNFAfglvtdfaeEIKDR-KWD---L 308
Cdd:cd05922 163 TVLPLSYDYGLSVLN---THLLRGATLVLTNDGVLDDAFWEDLREHGATGLAGVPSTY---------AMLTRlGFDpakL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 309 SSMRYMLNGGEAMVAKVGRRILELlephgLPADAIRPAWGMSETSSGVIF--SHEFTRAGTSdddhfveIGSPIPGFSMR 386
Cdd:cd05922 231 PSLRYLTQAGGRLPQETIARLREL-----LPGAQVYVMYGQTEATRRMTYlpPERILEKPGS-------IGLAIPGGEFE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 387 IVNDHNELVEEGEIGRFQVSGLSVTSGYYQRPDLNESVFTEDGWFETGDLGFLR-NGRLTITGRTKDAIIINGINYYSHA 465
Cdd:cd05922 299 ILDDDGTPTPPGEPGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDeDGFLFIVGRRDRMIKLFGNRISPTE 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 466 IESAVEELSEIETsytaACAVRLGQNSTDQLAIFFVTSAKLNDEQMSQLLRNiqshvsqvigVTPEYLLPVQK---EEIP 542
Cdd:cd05922 379 IEAAARSIGLIIE----AAAVGLPDPLGEKLALFVTAPDKIDPKDVLRSLAE----------RLPPYKVPATVrvvDELP 444
|
490
....*....|...
gi 1776025254 543 KTAIGKIQRTQLK 555
Cdd:cd05922 445 LTASGKVDYAALR 457
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
27-554 |
2.09e-33 |
|
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.
Pssm-ID: 341244 [Multi-domain] Cd Length: 482 Bit Score: 137.84 E-value: 2.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 27 QPATIPEVLYRTAAELGDTKGIIylqpDGtEVYQSYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNSQLLPAFWGCVL 106
Cdd:cd05920 13 QDEPLGDLLARSAARHPDRIAVV----DG-DRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 107 TGVVPApLAVPPTYAESSSGTQKLKDAwtlldkPAVITDRgmhqemldwakEQGLEGFRAIIVEdLLSAEADTdwhqssp 186
Cdd:cd05920 88 LGAVPV-LALPSHRRSELSAFCAHAEA------VAYIVPD-----------RHAGFDHRALARE-LAESIPEV------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 187 edlALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDH------VGGIGMLHLRdvylGCQEINV 260
Cdd:cd05920 142 ---ALFLLSGGTTGTPKLIPRTHNDYAYNVRASAEVCGLDQDTVYLAVLPAAHnfplacPGVLGTLLAG----GRVVLAP 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 261 SSEtilmePLKWLDWIDHYRASVTWA-PnfafGLVTDFAEEIKDRKWDLSSMRYMLNGGEAMVAKVGRRILELLEPhglp 339
Cdd:cd05920 215 DPS-----PDAAFPLIEREGVTVTALvP----ALVSLWLDAAASRRADLSSLRLLQVGGARLSPALARRVPPVLGC---- 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 340 adAIRPAWGMSEtssGVIfshEFTRAGTSDDDHFVEIGSPI-PGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGYYQRP 418
Cdd:cd05920 282 --TLQQVFGMAE---GLL---NYTRLDDPDEVIIHTQGRPMsPDDEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAP 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 419 DLNESVFTEDGWFETGDLGFL-RNGRLTITGRTKDAIIINGINYYSHAIESAVEELSEIEtsYTAACAV---RLGQNSTd 494
Cdd:cd05920 354 EHNARAFTPDGFYRTGDLVRRtPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVH--DAAVVAMpdeLLGERSC- 430
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 495 qlAIFFVTSAKLNDEQMSQLLRNIQSHVSQVigvtPEYLLPVqkEEIPKTAIGKIQRTQL 554
Cdd:cd05920 431 --AFVVLRDPPPSAAQLRRFLRERGLAAYKL----PDRIEFV--DSLPLTAVGKIDKKAL 482
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
1172-1635 |
3.82e-33 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341240 [Multi-domain] Cd Length: 463 Bit Score: 136.80 E-value: 3.82e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1172 VSYEGQTLTYRELDERSTQLAIYLQAHGVGP-DRLAgIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLEDSE 1250
Cdd:cd05914 1 LYYGGEPLTYKDLADNIAKFALLLKINGVGTgDRVA-LMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1251 VFITLTTSElvntlswngvttalldqdwdeiaqtasdrkvltrtvtpENLAYVIYTSGSTGKPKGVMIPHKALTNFLVSM 1330
Cdd:cd05914 80 AKAIFVSDE--------------------------------------DDVALINYTSGTTGNSKGVMLTYRNIVSNVDGV 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1331 GETPGLTAEDKMLAVTTY------CFDiaaleLFLPLIKGAHCYICQTEHTKDVEKLKRDirTIKPTVMQATP------- 1397
Cdd:cd05914 122 KEVVLLGKGDKILSILPLhhiyplTFT-----LLLPLLNGAHVVFLDKIPSAKIIALAFA--QVTPTLGVPVPlviekif 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1398 ----------ATWKMLFYSGWENEE---------------NVKILC-GGEALPETLKRYFLDTGSEAWNMFGPTETTIWS 1451
Cdd:cd05914 195 kmdiipkltlKKFKFKLAKKINNRKirklafkkvheafggNIKEFViGGAKINPDVEEFLRTIGFPYTIGYGMTETAPII 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1452 AVQRINDECSrATIGRPIANTQIYITDsqlaPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPFepgsklYRTGDM 1531
Cdd:cd05914 275 SYSPPNRIRL-GSAGKVIDGVEVRIDS----PDPATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDGW------FHTGDL 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1532 ARWLPGGRIEYIGRIDNQ-VKIRGFRIELGDIESRLSEHPGILECVVVADMDNLAA----YYTAKHANASLTAR------ 1600
Cdd:cd05914 344 GKIDAEGYLYIRGRKKEMiVLSSGKNIYPEEIEAKINNMPFVLESLVVVQEKKLVAlayiDPDFLDVKALKQRNiidaik 423
|
490 500 510
....*....|....*....|....*....|....*..
gi 1776025254 1601 -ELRHFVKNALPAY-MVPSYFIQLDHMPLTPNGKIDR 1635
Cdd:cd05914 424 wEVRDKVNQKVPNYkKISKVKIVKEEFEKTPKGKIKR 460
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
1154-1639 |
4.70e-33 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 137.97 E-value: 4.70e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1154 TFHELFEQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDrlagiyvDR-------SLDMLVGLLAILKA 1226
Cdd:COG1021 26 TLGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPG-------DRvvvqlpnVAEFVIVFFALFRA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1227 GGayVPLDpSYPAER---LEYMLEDSE--VFITLTTS------ELVNTL--SWNGVTTALLD------QDWDEIAQTASD 1287
Cdd:COG1021 99 GA--IPVF-ALPAHRraeISHFAEQSEavAYIIPDRHrgfdyrALARELqaEVPSLRHVLVVgdagefTSLDALLAAPAD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1288 RKVltRTVTPENLAYVIYTSGSTGKPKgvMIP--HKA-LTNFLVSmGETPGLTAEDKMLAV----------------TTY 1348
Cdd:COG1021 176 LSE--PRPDPDDVAFFQLSGGTTGLPK--LIPrtHDDyLYSVRAS-AEICGLDADTVYLAAlpaahnfplsspgvlgVLY 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1349 -------CFDIAALELFlPLIkgahcyicqtehtkdvEKLKRDIRTIKPTV----MQATPATWKMLfySGWEneenvKIL 1417
Cdd:COG1021 251 aggtvvlAPDPSPDTAF-PLI----------------ERERVTVTALVPPLallwLDAAERSRYDL--SSLR-----VLQ 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1418 CGGEALPETLKRYFLDT-GSEAWNMFGPTE----TTiwsavqRIND--ECSRATIGRPI-ANTQIYITDSQLAPVPAGVP 1489
Cdd:COG1021 307 VGGAKLSPELARRVRPAlGCTLQQVFGMAEglvnYT------RLDDpeEVILTTQGRPIsPDDEVRIVDEDGNPVPPGEV 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1490 GELCIAGDGVAKGYYKKEELTDSRFIDNPFepgsklYRTGDMARWLPGGRIEYIGRIDNQVkIRGfrielG------DIE 1563
Cdd:COG1021 381 GELLTRGPYTIRGYYRAPEHNARAFTPDGF------YRTGDLVRRTPDGYLVVEGRAKDQI-NRG-----GekiaaeEVE 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1564 SRLSEHPGILECVVVADMDNL-----AAYYTAKhaNASLTARELRHFVKNA-LPAYMVPSYFIQLDHMPLTPNGKIDRNS 1637
Cdd:COG1021 449 NLLLAHPAVHDAAVVAMPDEYlgersCAFVVPR--GEPLTLAELRRFLRERgLAAFKLPDRLEFVDALPLTAVGKIDKKA 526
|
..
gi 1776025254 1638 LK 1639
Cdd:COG1021 527 LR 528
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
1142-1647 |
9.06e-33 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 137.82 E-value: 9.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1142 TWNATGKTYPYITFHELFEQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGP-DRLAgIYVDRSLDMLVGL 1220
Cdd:PRK05605 21 PWTPHDLDYGDTTLVDLYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPgDRVA-IVLPNCPQHIVAF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1221 LAILKAGGAYVPLDPSYPAERLEYMLED--SEVFITL-----TTSELVNTLSWNGV-----TTA--LLDQ---------- 1276
Cdd:PRK05605 100 YAVLRLGAVVVEHNPLYTAHELEHPFEDhgARVAIVWdkvapTVERLRRTTPLETIvsvnmIAAmpLLQRlalrlpipal 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1277 ---------------DWDEIAQTA---SDRKVLTRTVTPENLAYVIYTSGSTGKPKGVMIPHKAL-TNflVSMGET--PG 1335
Cdd:PRK05605 180 rkaraaltgpapgtvPWETLVDAAiggDGSDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLfAN--AAQGKAwvPG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1336 LTAED-KMLAVTTYcFDIAALEL---FLPLIKGAHCYIcqteHTKDVEKLKRDIRTIKPTVMQATPATWKMLFYSGweNE 1411
Cdd:PRK05605 258 LGDGPeRVLAALPM-FHAYGLTLcltLAVSIGGELVLL----PAPDIDLILDAMKKHPPTWLPGVPPLYEKIAEAA--EE 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1412 ENVKI------LCGGEALP-ETLKRYFLDTGSEAWNMFGPTETTIWSAVQRINDECSRATIGRPIANTQIYITDsqlaP- 1483
Cdd:PRK05605 331 RGVDLsgvrnaFSGAMALPvSTVELWEKLTGGLLVEGYGLTETSPIIVGNPMSDDRRPGYVGVPFPDTEVRIVD----Pe 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1484 -----VPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNpfepgskLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIE 1558
Cdd:PRK05605 407 dpdetMPDGEEGELLVRGPQVFKGYWNRPEETAKSFLDG-------WFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVY 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1559 LGDIESRLSEHPGILECVVV------ADMDNLAAYYTAKHanASLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGK 1632
Cdd:PRK05605 480 PAEVEEVLREHPGVEDAAVVglpredGSEEVVAAVVLEPG--AALDPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGK 557
|
570
....*....|....*
gi 1776025254 1633 IDRNSLKNIDLSGEQ 1647
Cdd:PRK05605 558 VRRREVREELLEKLG 572
|
|
| DCL_NRPS-like |
cd19536 |
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ... |
695-1110 |
1.82e-32 |
|
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal fungal CT domains and Dual Epimerization/Condensation (E/C) domains; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type [D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L))], which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380459 [Multi-domain] Cd Length: 419 Bit Score: 133.73 E-value: 1.82e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 695 PLSEVQKGLWTLQKMSPEKSAYHVPLCFKFSSGLHLETLQQAFGLVLNQHPILKHV-IQEKDGVPILKNEPALSIEIKTE 773
Cdd:cd19536 3 PLSSLQEGMLFHSLLNPGGSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSfIEDGLGQPVQVVHRQAQVPVTEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 774 NISSMKESDIPafLRKKVKEPYVKE----NSPLVRVMSFSRSEQEHFLLVV-IHHLIFDGVSsvtfIHSLFDTYQLLLKG 848
Cdd:cd19536 83 DLTPLEEQLDP--LRAYKEETKIRRfdlgRAPLVRAALVRKDERERFLLVIsDHHSILDGWS----LYLLVKEILAVYNQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 849 Q--QPEIAVSPAI-YHDFAAWEKnmlAGKDGVKHRTYWQKQLSG-TLPNlqLPKVSASSVSEFREDTYTrRLSSGFMNQV 924
Cdd:cd19536 157 LleYKPLSLPPAQpYRDFVAHER---ASIQQAASERYWREYLAGaTLAT--LPALSEAVGGGPEQDSEL-LVSVPLPVRS 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 925 RMFAKEHSVNVTTVFLSCYMMLLGRYTGQKEQIVGMPAMVRPEErFDDA---IGHFLNMLPIRSELnPADTFSSFISKLQ 1001
Cdd:cd19536 231 RSLAKRSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEE-TTGAerlLGLFLNTLPLRVTL-SEETVEDLLKRAQ 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1002 LTILDGLDHAAYPFPkmvrdlNIPRSQAGSPVFQTAFFYQNFLQsgsYQSLLSRYADFFSVDYVEYIHQEGEYELVFELW 1081
Cdd:cd19536 309 EQELESLSHEQVPLA------DIQRCSEGEPLFDSIVNFRHFDL---DFGLPEWGSDEGMRRGLLFSEFKSNYDVNLSVL 379
|
410 420
....*....|....*....|....*....
gi 1776025254 1082 ETEEKMELNIKYNTGLFDAASISAMFDHF 1110
Cdd:cd19536 380 PKQDRLELKLAYNSQVLDEEQAQRLAAYY 408
|
|
| PRK06333 |
PRK06333 |
beta-ketoacyl-ACP synthase; |
3351-3781 |
1.94e-32 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235781 [Multi-domain] Cd Length: 424 Bit Score: 133.97 E-value: 1.94e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3351 PGAMDIDEFWKNLEEGKDSITEVPKDrwdwrehygnpdtDVNKTDIKWGGFI-----DGVAEFDPLFFgISPREADYVDP 3425
Cdd:PRK06333 16 PLGCGVETFWQRLLAGQSGIRTLTDF-------------PVGDLATKIGGQVpdlaeDAEAGFDPDRY-LDPKDQRKMDR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3426 QQRLLMTYVWKALEDAGCPPQSLSGT-GTGIFIGTGNTGykdlfhranLPIEGHAATghMIPSVGPNRMS-----YFL-N 3498
Cdd:PRK06333 82 FILFAMAAAKEALAQAGWDPDTLEDReRTATIIGSGVGG---------FPAIAEAVR--TLDSRGPRRLSpftipSFLtN 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3499 I-----------HGPSEPVETACSSSLVAIHRAVTAMQNGDCEMAIAGGvntilTEEAHISYSKAGM-----LSKDGR-- 3560
Cdd:PRK06333 151 MaaghvsirygfKGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGG-----TEAAIDRVSLAGFaaaraLSTRFNda 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3561 ----CKTFSADANGYVRGEGVGMVMLKKLEDAERDGNHIYGVIRG---TAEnhggrANTLTSPNP--KAQADLLVRAYRQ 3631
Cdd:PRK06333 226 peqaSRPFDRDRDGFVMGEGAGILVIETLEHALARGAPPLAELVGygtSAD-----AYHMTAGPEdgEGARRAMLIALRQ 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3632 AGIDPSTVTYIEAHGTGTELGDPIEINGLKAAFKELSNMRgesqpdvpdhrcgIGSVKSNIGHLELAAGISGLIKVLLQM 3711
Cdd:PRK06333 301 AGIPPEEVQHLNAHATSTPVGDLGEVAAIKKVFGHVSGLA-------------VSSTKSATGHLLGAAGGVEAIFTILAL 367
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1776025254 3712 KHKTLVKSLHCETLNPYLQLTDspfYIVQEKQEWksvtdcdgnelPRRAGIS-SFGIGGVNAHIVIEEYMP 3781
Cdd:PRK06333 368 RDQIAPPTLNLENPDPAAEGLD---VVANKARPM-----------DMDYALSnGFGFGGVNASILFRRWEP 424
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
1175-1639 |
2.40e-32 |
|
C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.
Pssm-ID: 341235 [Multi-domain] Cd Length: 490 Bit Score: 135.15 E-value: 2.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1175 EGQTLTYRELDERSTQLAIYLQAhGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLEDSEVFIT 1254
Cdd:cd05909 4 LGTSLTYRKLLTGAIALARKLAK-MTKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1255 LTTSELVNTLSWNGVTTALLDQDW---DE------------------IAQTASDRKVLTRTVTPENLAYVIYTSGSTGKP 1313
Cdd:cd05909 83 LTSKQFIEKLKLHHLFDVEYDARIvylEDlrakiskadkckaflagkFPPKWLLRIFGVAPVQPDDPAVILFTSGSEGLP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1314 KGVMIPHKALTNFLVSMGETPGLTAEDKMLAVTT--YCFDIAAlELFLPLIKGAHcyICQTEHTKDVEKLKRDIRTIKPT 1391
Cdd:cd05909 163 KGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPffHSFGLTG-CLWLPLLSGIK--VVFHPNPLDYKKIPELIYDKKAT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1392 VMQATPaTWKMLFYSGWENEENVK---ILCGGEALPETLKRYFLDT-GSEAWNMFGPTETtiwSAVQRINDECSRA---T 1464
Cdd:cd05909 240 ILLGTP-TFLRGYARAAHPEDFSSlrlVVAGAEKLKDTLRQEFQEKfGIRILEGYGTTEC---SPVISVNTPQSPNkegT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1465 IGRPIANTQIYITDSQ-LAPVPAGVPGELCIAGDGVAKGYYKKEELTDsrfidnpFEPGSKLYRTGDMARWLPGGRIEYI 1543
Cdd:cd05909 316 VGRPLPGMEVKIVSVEtHEEVPIGEGGLLLVRGPNVMLGYLNEPELTS-------FAFGDGWYDTGDIGKIDGEGFLTIT 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1544 GRIDNQVKIRGFRIELGDIESRLSEH-PGILECVVVADMDN-----LAAYYTAKHANASltarELRHFVKNA-LPAYMVP 1616
Cdd:cd05909 389 GRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDGrkgekIVLLTTTTDTDPS----SLNDILKNAgISNLAKP 464
|
490 500
....*....|....*....|...
gi 1776025254 1617 SYFIQLDHMPLTPNGKIDRNSLK 1639
Cdd:cd05909 465 SYIHQVEEIPLLGTGKPDYVTLK 487
|
|
| KR_1_FAS_SDR_x |
cd08954 |
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 1, complex (x) SDRs; ... |
2851-3063 |
2.72e-32 |
|
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 1, complex (x) SDRs; NADP-dependent KR domain of the multidomain type I FAS, a complex SDR family. This subfamily also includes proteins identified as polyketide synthase (PKS), a protein with related modular protein architecture and similar function. It includes the KR domains of mammalian and chicken FAS, and Dictyostelium discoideum putative polyketide synthases (PKSs). These KR domains contain two subdomains, each of which is related to SDR Rossmann fold domains. However, while the C-terminal subdomain has an active site similar to the other SDRs and a NADP-binding capability, the N-terminal SDR-like subdomain is truncated and lacks these functions, serving a supportive structural role. In some instances, such as porcine FAS, an enoyl reductase (a Rossman fold NAD-binding domain of the medium-chain dehydrogenase/reductase, MDR family) module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consists of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthesis uses a dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-ketoacyl reductase (KR), forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-enoyl reductase (ER); this KR and ER are members of the SDR family. This KR subfamily has an active site tetrad with a similar 3D orientation compared to archetypical SDRs, but the active site Lys and Asn residue positions are swapped. The characteristic NADP-binding is typical of the multidomain complex SDRs, with a GGXGXXG NADP binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.
Pssm-ID: 187657 [Multi-domain] Cd Length: 452 Bit Score: 134.11 E-value: 2.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2851 YLITGGAGSLGLLFAKEIANRTGRSTIVLTGRSVLSEDKENELEALRSIGAEVVYREADVSDQHAVHHLFEEIKERY--G 2928
Cdd:cd08954 221 YLITGGSGGLGLEILKWLVKRGAVENIIILSRSGMKWELELLIREWKSQNIKFHFVSVDVSDVSSLEKAINLILNAPkiG 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2929 TLNGIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSGLLHVDECS--KDFPLDFFIFFSSVSGCLGNAGQADYAAANSFMDA 3006
Cdd:cd08954 301 PIGGIFHLAFVLIDKVLEIDTESLFISVNKAKVMGAINLHNQSikRCWKLDYFVLFSSVSSIRGSAGQCNYVCANSVLDS 380
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1776025254 3007 FAEYRRSLAAskkrfgSTISFNWPLWEEGGMQVGAEDEKRMLKTTGMVPMPTDSGLK 3063
Cdd:cd08954 381 LSRYRKSIGL------PSIAINWGAIGDVGFVSRNESVDTLLGGQGLLPQSINSCLG 431
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
195-555 |
3.31e-32 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 131.25 E-value: 3.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 195 TSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDHVGGIGMLHLRDVYLGCQEINVSSEtilMEPLKWLD 274
Cdd:cd05917 10 TSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPVPLFHCFGSVLGVLACLTHGATMVFPSPS---FDPLAVLE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 275 WIDHYRASvtwapnFAFGLVTDFAEEI---KDRKWDLSSMRYMLNGGEAMVAKVGRRILELLephGLPADAIrpAWGMSE 351
Cdd:cd05917 87 AIEKEKCT------ALHGVPTMFIAELehpDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVM---NMKDVTI--AYGMTE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 352 TSSgVIFShefTRAGTSDDDHFVEIGSPIPGFSMRIVN-DHNELVEEGEIGRFQVSGLSVTSGYYQRPDLNESVFTEDGW 430
Cdd:cd05917 156 TSP-VSTQ---TRTDDSIEKRVNTVGRIMPHTEAKIVDpEGGIVPPVGVPGELCIRGYSVMKGYWNDPEKTAEAIDGDGW 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 431 FETGDLGFL-RNGRLTITGRTKDAIIINGINYYSHAIES------AVEELSEI----ETSYTAACA-VRLGQNstdqlai 498
Cdd:cd05917 232 LHTGDLAVMdEDGYCRIVGRIKDMIIRGGENIYPREIEEflhthpKVSDVQVVgvpdERYGEEVCAwIRLKEG------- 304
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1776025254 499 ffvtsAKLNDEQMSQLLRNIQSHVSqvigvTPEYLLPVqkEEIPKTAIGKIQRTQLK 555
Cdd:cd05917 305 -----AELTEEDIKAYCKGKIAHYK-----VPRYVFFV--DEFPLTVSGKIQKFKLR 349
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
186-554 |
5.40e-32 |
|
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341298 [Multi-domain] Cd Length: 450 Bit Score: 133.20 E-value: 5.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 186 PEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDI--TFNWMPFD-HVGGI--GMLHlrdvylGCQEINV 260
Cdd:cd17643 92 PDDLAYVIYTSGSTGRPKGVVVSHANVLALFAATQRWFGFNEDDVwtLFHSYAFDfSVWEIwgALLH------GGRLVVV 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 261 SSETiLMEPLKWLDWIDHYRASVTWAPNFAFGlvtDFAEEIKDRKWDLSSMRYMLNGGEAMVAKVGRRileLLEPHGLPA 340
Cdd:cd17643 166 PYEV-ARSPEDFARLLRDEGVTVLNQTPSAFY---QLVEAADRDGRDPLALRYVIFGGEALEAAMLRP---WAGRFGLDR 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 341 DAIRPAWGMSETSSGVIFsHEFTRAGTSDDDHFVeIGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGYYQRPDL 420
Cdd:cd17643 239 PQLVNMYGITETTVHVTF-RPLDAADLPAAAASP-IGRPLPGLRVYVLDADGRPVPPGVVGELYVSGAGVARGYLGRPEL 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 421 NESVFTEDGW-------FETGDLG-FLRNGRLTITGRTKDAIIINGinyysHAIesaveELSEIETSYT-------AACA 485
Cdd:cd17643 317 TAERFVANPFggpgsrmYRTGDLArRLPDGELEYLGRADEQVKIRG-----FRI-----ELGEIEAALAthpsvrdAAVI 386
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1776025254 486 VRLGQNSTDQLAIFFVTsaklnDEQMSQLLRNIQSHVSQVIgvtPEYLLP---VQKEEIPKTAIGKIQRTQL 554
Cdd:cd17643 387 VREDEPGDTRLVAYVVA-----DDGAAADIAELRALLKELL---PDYMVParyVPLDALPLTVNGKLDRAAL 450
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
1152-1642 |
1.07e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 133.90 E-value: 1.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1152 YITFHELFEQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYV 1231
Cdd:PRK07788 48 YGPFAGLVAHAARRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARII 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1232 PLDPSYPAERLEYMLE---------DSEvFITLTT---SELVNTLSWNGVTTAL-----LDQDWDEIAQTASDRKVLTrt 1294
Cdd:PRK07788 128 LLNTGFSGPQLAEVAAregvkalvyDDE-FTDLLSalpPDLGRLRAWGGNPDDDepsgsTDETLDDLIAGSSTAPLPK-- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1295 vTPENLAYVIYTSGSTGKPKGVMIPH-KALTNF--LVS-----MGETPGLTAedKMLAVTTYcfdiAALELFLPLikGAH 1366
Cdd:PRK07788 205 -PPKPGGIVILTSGTTGTPKGAPRPEpSPLAPLagLLSrvpfrAGETTLLPA--PMFHATGW----AHLTLAMAL--GST 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1367 CYIcqteHTK-DVEKLKRDIRTIKPTVMQATPATWKMLFysgwENEENVK----------ILCGGEALPETLKRYFLDT- 1434
Cdd:PRK07788 276 VVL----RRRfDPEATLEDIAKHKATALVVVPVMLSRIL----DLGPEVLakydtsslkiIFVSGSALSPELATRALEAf 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1435 GSEAWNMFGPTETTiWSAVQRIND-ECSRATIGRPIANTQIYITDSQLAPVPAGVPGELCIAGDGVAKGYykkeelTDSR 1513
Cdd:PRK07788 348 GPVLYNLYGSTEVA-FATIATPEDlAEAPGTVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGY------TDGR 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1514 fiDNPFEPGskLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMDN-----LAAYy 1588
Cdd:PRK07788 421 --DKQIIDG--LLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEefgqrLRAF- 495
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1776025254 1589 TAKHANASLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLKNID 1642
Cdd:PRK07788 496 VVKAPGAALDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELREMD 549
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
1151-1640 |
1.24e-31 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 133.99 E-value: 1.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1151 PYITFHELFEQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGP-DRLAgIYVDRSLDMLVGLLAILKAGGA 1229
Cdd:PRK07059 21 QYPSLADLLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKgARVA-IMMPNVLQYPVAIAAVLRAGYV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1230 YVPLDPSYPAERLEYMLEDS--EVFITL----TTSELV--NTLSWNGVTTALLDQ--------------------DW--- 1278
Cdd:PRK07059 100 VVNVNPLYTPRELEHQLKDSgaEAIVVLenfaTTVQQVlaKTAVKHVVVASMGDLlgfkghivnfvvrrvkkmvpAWslp 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1279 ------DEIAQTAsdRKVLTR-TVTPENLAYVIYTSGSTGKPKGVMIPHKaltNFLVSMGET-----PGLTAEDKMLAVT 1346
Cdd:PRK07059 180 ghvrfnDALAEGA--RQTFKPvKLGPDDVAFLQYTGGTTGVSKGATLLHR---NIVANVLQMeawlqPAFEKKPRPDQLN 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1347 TYC----FDIAALEL--FLPLIKGAHCYIcqTEHTKDVEKLKRDIRTIKPTVMqatPATwKMLFYSGWENEENVKI---- 1416
Cdd:PRK07059 255 FVCalplYHIFALTVcgLLGMRTGGRNIL--IPNPRDIPGFIKELKKYQVHIF---PAV-NTLYNALLNNPDFDKLdfsk 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1417 ----LCGGEALPETL-KRYFLDTGSEAWNMFGPTETTIWSAVQRINDECSRATIGRPIANTQIYITDSQLAPVPAGVPGE 1491
Cdd:PRK07059 329 livaNGGGMAVQRPVaERWLEMTGCPITEGYGLSETSPVATCNPVDATEFSGTIGLPLPSTEVSIRDDDGNDLPLGEPGE 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1492 LCIAGDGVAKGYYKKEELTDSRFIDNPFepgsklYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPG 1571
Cdd:PRK07059 409 ICIRGPQVMAGYWNRPDETAKVMTADGF------FRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPG 482
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1776025254 1572 ILECVVVADMDN-----LAAYYTAKhaNASLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLKN 1640
Cdd:PRK07059 483 VLEVAAVGVPDEhsgeaVKLFVVKK--DPALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRRELRD 554
|
|
| PLN02836 |
PLN02836 |
3-oxoacyl-[acyl-carrier-protein] synthase |
3436-3775 |
1.86e-31 |
|
3-oxoacyl-[acyl-carrier-protein] synthase
Pssm-ID: 215449 [Multi-domain] Cd Length: 437 Bit Score: 131.07 E-value: 1.86e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3436 KALEDAGCPPQSLSGTG-TGIFIGTGNTGYKDLFHRANLPIEGHA--ATGHMIPSVGPNRMSYFLNI----HGPSEPVET 3508
Cdd:PLN02836 103 EALSDARWLPSEDEAKErTGVSIGGGIGSITDILEAAQLICEKRLrrLSPFFVPRILINMAAGHVSIrygfQGPNHAAVT 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3509 ACSSSLVAIHRAVTAMQNGDCEMAIAGGVNTILTEEAHISYSKAGMLS-KDGRCKT-----FSADANGYVRGEGVGMVML 3582
Cdd:PLN02836 183 ACATGAHSIGDAFRMIQFGDADVMVAGGTESSIDALSIAGFSRSRALStKFNSCPTeasrpFDCDRDGFVIGEGAGVLVL 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3583 KKLEDAERDGNHIYGVIRGTAENhgGRANTLTSPNPKAQADLLV--RAYRQAGIDPSTVTYIEAHGTGTELGDPIEINGL 3660
Cdd:PLN02836 263 EELEHAKRRGAKIYAEVRGYGMS--GDAHHITQPHEDGRGAVLAmtRALQQSGLHPNQVDYVNAHATSTPLGDAVEARAI 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3661 KAAFKElsnmrgesqpDVPDHRCGIGSVKSNIGHLELAAGISGLIKVLLQMKHKTLVKSLHCETLNP-----YLQLTDSP 3735
Cdd:PLN02836 341 KTVFSE----------HATSGGLAFSSTKGATGHLLGAAGAVEAIFSVLAIHHGIAPPTLNLERPDPifddgFVPLTASK 410
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1776025254 3736 fyivqekqewksvtdcdgnELPRRAGIS-SFGIGGVNAHIV 3775
Cdd:PLN02836 411 -------------------AMLIRAALSnSFGFGGTNASLL 432
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
1154-1638 |
1.96e-31 |
|
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.
Pssm-ID: 341247 [Multi-domain] Cd Length: 493 Bit Score: 132.25 E-value: 1.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1154 TFHELFEQQAKKTPDRAA-VSYEGQT-LTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYV 1231
Cdd:cd05923 2 TVFEMLRRAASRAPDACAiADPARGLrLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1232 PLDPSYPAERLEYMLEDSE---VFITLTTSELVNTLSWNGVTTALLDQDWDEIAQTASDrKVLTRTVTPENLAYVIYTSG 1308
Cdd:cd05923 82 LINPRLKAAELAELIERGEmtaAVIAVDAQVMDAIFQSGVRVLALSDLVGLGEPESAGP-LIEDPPREPEQPAFVFYTSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1309 STGKPKGVMIPHKALTNFLVSMGETPGLT--AEDKMLAVTTYCFDIAALELFLPLIKGAHCYiCQTEHTKDVEKLKRdIR 1386
Cdd:cd05923 161 TTGLPKGAVIPQRAAESRVLFMSTQAGLRhgRHNVVLGLMPLYHVIGFFAVLVAALALDGTY-VVVEEFDPADALKL-IE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1387 TIKPTVMQATPATWKMLFYSGWENEENVKIL----CGGEALPET-LKRYFLDTGSEAWNMFGPTETTiwsaVQRINDECS 1461
Cdd:cd05923 239 QERVTSLFATPTHLDALAAAAEFAGLKLSSLrhvtFAGATMPDAvLERVNQHLPGEKVNIYGTTEAM----NSLYMRDAR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1462 RATIGRPIANTQIYIT---DSQLAPVPAGVPGELCIA--GDGVAKGYYKKEELTDSRFIDNpfepgskLYRTGDMARWLP 1536
Cdd:cd05923 315 TGTEMRPGFFSEVRIVrigGSPDEALANGEEGELIVAaaADAAFTGYLNQPEATAKKLQDG-------WYRTGDVGYVDP 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1537 GGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMDN-----LAAYYTAKHANasLTARELRHFVK-NAL 1610
Cdd:cd05923 388 SGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADErwgqsVTACVVPREGT--LSADELDQFCRaSEL 465
|
490 500
....*....|....*....|....*...
gi 1776025254 1611 PAYMVPSYFIQLDHMPLTPNGKIDRNSL 1638
Cdd:cd05923 466 ADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
1158-1646 |
2.69e-31 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 132.57 E-value: 2.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1158 LFEQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGP-DRLAGIYVDRS--LDMLVGLLAIlkaGGAYVPLD 1234
Cdd:PRK06155 26 MLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRgDRVALMCGNRIefLDVFLGCAWL---GAIAVPIN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1235 PSYPAERLEYMLEDSEVFITLTTSELVNTLS------------W--NGVTTALLDQDWDEIAQTASDRKVLTRTVTPENL 1300
Cdd:PRK06155 103 TALRGPQLEHILRNSGARLLVVEAALLAALEaadpgdlplpavWllDAPASVSVPAGWSTAPLPPLDAPAPAAAVQPGDT 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1301 AYVIYTSGSTGKPKGVMIPHKALTNFLVSMGETPGLTAEDkMLAVTTYCFDIAALELFLP-LIKGAHCYICQ-------- 1371
Cdd:PRK06155 183 AAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADD-VLYTTLPLFHTNALNAFFQaLLAGATYVLEPrfsasgfw 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1372 ---TEHTKDVEKLKRDIRTIkptvMQATPATWKmlfysgwENEENVKILCGGEALPETLKRYFLDTGSEAWNMFGPTETT 1448
Cdd:PRK06155 262 pavRRHGATVTYLLGAMVSI----LLSQPARES-------DRAHRVRVALGPGVPAALHAAFRERFGVDLLDGYGSTETN 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1449 IWSAVQRinDECSRATIGRPIANTQIYITDSQLAPVPAGVPGELCIAGD---GVAKGYYKKEELTDSRFIDNPFEPGSKL 1525
Cdd:PRK06155 331 FVIAVTH--GSQRPGSMGRLAPGFEARVVDEHDQELPDGEPGELLLRADepfAFATGYFGMPEKTVEAWRNLWFHTGDRV 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1526 YRTGDmarwlpgGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVA-----DMDNLAAYYTAKHANAsLTAR 1600
Cdd:PRK06155 409 VRDAD-------GWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPvpselGEDEVMAAVVLRDGTA-LEPV 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1776025254 1601 ELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLKNIDLSGE 1646
Cdd:PRK06155 481 ALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLREQGVTAD 526
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
1154-1638 |
2.95e-31 |
|
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.
Pssm-ID: 341244 [Multi-domain] Cd Length: 482 Bit Score: 131.68 E-value: 2.95e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1154 TFHELFEQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPL 1233
Cdd:cd05920 16 PLGDLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVLA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1234 DPSYPAERLEYMLEDSEVfitlttselvntlswngvtTALLDQD-WDEIAQTASDRKVLTRTVTPenlAYVIYTSGSTGK 1312
Cdd:cd05920 96 LPSHRRSELSAFCAHAEA-------------------VAYIVPDrHAGFDHRALARELAESIPEV---ALFLLSGGTTGT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1313 PKgvMIP--HKALTNFLVSMGETPGLTAEDKMLAV--TTYCFDIAALELFLPLIKGAHCYICQTEHTKDVEKLkrdIRTI 1388
Cdd:cd05920 154 PK--LIPrtHNDYAYNVRASAEVCGLDQDTVYLAVlpAAHNFPLACPGVLGTLLAGGRVVLAPDPSPDAAFPL---IERE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1389 KPTVMQATPATWKM-LFYSGWENEE--NVKIL-CGGEALPETLKRYFLDT-GSEAWNMFGPTETTIwsAVQRIND--ECS 1461
Cdd:cd05920 229 GVTVTALVPALVSLwLDAAASRRADlsSLRLLqVGGARLSPALARRVPPVlGCTLQQVFGMAEGLL--NYTRLDDpdEVI 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1462 RATIGRPI-ANTQIYITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPFepgsklYRTGDMARWLPGGRI 1540
Cdd:cd05920 307 IHTQGRPMsPDDEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGF------YRTGDLVRRTPDGYL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1541 EYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMDNL-----AAYYTAKhaNASLTARELRHFVKNA-LPAYM 1614
Cdd:cd05920 381 VVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELlgersCAFVVLR--DPPPSAAQLRRFLRERgLAAYK 458
|
490 500
....*....|....*....|....
gi 1776025254 1615 VPSYFIQLDHMPLTPNGKIDRNSL 1638
Cdd:cd05920 459 LPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
162-1002 |
3.16e-31 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 136.83 E-value: 3.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 162 EGFRAIIVE---DLLSAEADTDWHQS-SPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPF 237
Cdd:PRK12467 1689 DGLRSLVLDqedDWLEGYSDSNPAVNlAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSF 1768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 238 ----DHVGGIGMLhlrdvyLGCQEINVSSETILMEPLKWLDWIDHYRASVTWAPNFAFGLVTDFAEEIKDrkwdLSSMRY 313
Cdd:PRK12467 1769 afdvSVWELFWPL------INGARLVIAPPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQMDEQVEH----PLSLRR 1838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 314 MLNGGEAMVAKVGRRILEllephGLPADAIRPAWGMSETSSGVifSHEFTRAGTSDDDHFVEIGSPIPGFSMRIVNDHNE 393
Cdd:PRK12467 1839 VVCGGEALEVEALRPWLE-----RLPDTGLFNLYGPTETAVDV--THWTCRRKDLEGRDSVPIGQPIANLSTYILDASLN 1911
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 394 LVEEGEIGRFQVSGLSVTSGYYQRPDLNESVFTEDGW-------FETGDLGFLR-NGRLTITGRTKDAIIINGINYYSHA 465
Cdd:PRK12467 1912 PVPIGVAGELYLGGVGLARGYLNRPALTAERFVADPFgtvgsrlYRTGDLARYRaDGVIEYLGRIDHQVKIRGFRIELGE 1991
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 466 IESAVEELSEIETSYTAACAVRLGQnstdQLAIFFVTSAKL---NDEQMSQLLRNIQSHVSQVIgvtPEYLLPVQ---KE 539
Cdd:PRK12467 1992 IEARLREQGGVREAVVIAQDGANGK----QLVAYVVPTDPGlvdDDEAQVALRAILKNHLKASL---PEYMVPAHlvfLA 2064
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 540 EIPKTAIGKIQRTQLKtsfengefdhllhKPnrmnDAVQdeeMQQAdhVKRVREEIQEHLLTCLTEELHVSRdwVEPNAN 619
Cdd:PRK12467 2065 RMPLTPNGKLDRKALP-------------AP----DASE---LQQA--YVAPQSELEQRLAAIWQDVLGLEQ--VGLHDN 2120
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 620 IQSLGVNSIKMMKLIrSIEKNYHIKLTAREIHQYPTIERLASYLSEHEDLSSSSADKKGTDTyktepersqatfqPLSEV 699
Cdd:PRK12467 2121 FFELGGDSIISIQVV-SRARQAGIRFTPKDLFQHQTVQSLAAVAQEGDGTVSIDQGPVTGDL-------------PLLPI 2186
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 700 QKGLWTLQkmSPEKSAYHVPLCFKFSSGLHLETLQQAFGLVLNQHPILKHVIQEKDG------VPILKNEPALSIEIKTE 773
Cdd:PRK12467 2187 QQMFFADD--IPERHHWNQSVLLEPREALDAELLEAALQALLVHHDALRLGFVQEDGgwsamhRAPEQERRPLLWQVVVA 2264
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 774 NISSMKEsdipafLRKKVKEPYVKENSPLVRVMSFSRSEQEHFLLVVIHHLIFDGVSSVTFIHSLFDTYQLLLKGQQpei 853
Cdd:PRK12467 2265 DKEELEA------LCEQAQRSLDLEEGPLLRAVLATLPDGSQRLLLVIHHLVVDGVSWRILLEDLQTAYRQLQGGQP--- 2335
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 854 AVSPAIYHDFAAWEKNM--LAGKDGVK-HRTYWQKQLSGT---LP------NLQLpKVSASSVSEFREDtYTRRLssgfm 921
Cdd:PRK12467 2336 VKLPAKTSAFKAWAERLqtYAASAALAdELGYWQAQLQGAsteLPcdhpqgGLQR-RHAASVTTHLDSE-WTRRL----- 2408
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 922 nqVRMFAKEHSVNVTTVFLSCYMMLLGRYTGQKEQIVGMPAMVRpEERFDD-----AIGHFLNMLPIRseLNPADTFSSF 996
Cdd:PRK12467 2409 --LQEAPAAYRTQVNDLLLTALARVIARWTGQASTLIQLEGHGR-EDLFDEidltrTVGWFTSLYPVK--LSPTASLATS 2483
|
....*...
gi 1776025254 997 IS--KLQL 1002
Cdd:PRK12467 2484 IKtiKEQL 2491
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
13-555 |
3.80e-31 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 132.59 E-value: 3.80e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 13 PSVSHGEPLHISEKQpaTIPEVLYRTAAELGDTKGIIYLQpdgTEVYQSYRRLWDDGLRIVKGLRQSGLKAKQSVILQLG 92
Cdd:PRK12583 4 PSYYQGGGDKPLLTQ--TIGDAFDATVARFPDREALVVRH---QALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 93 DN-----SQLLPAFWGCVLTGVVPAPLAVPPTYAESSSGTQKL--KDAWTLLDKPAVITD--RGMHQEMLDWAKEQGLEG 163
Cdd:PRK12583 79 NCaewllTQFATARIGAILVNINPAYRASELEYALGQSGVRWVicADAFKTSDYHAMLQEllPGLAEGQPGALACERLPE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 164 FRAIIVEDLLSAEADTDWHQ-------SSPEDLAL------------LLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQG 224
Cdd:PRK12583 159 LRGVVSLAPAPPPGFLAWHElqargetVSREALAErqasldrddpinIQYTSGTTGFPKGATLSHHNILNNGYFVAESLG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 225 FTREDITFNWMPFDHVGGIGMLHLrdvylGCqeinVSSETILMEPLKWLDWIDHYRASVTWAPNFAFGLVTDFAEEIK-- 302
Cdd:PRK12583 239 LTEHDRLCVPVPLYHCFGMVLANL-----GC----MTVGACLVYPNEAFDPLATLQAVEEERCTALYGVPTMFIAELDhp 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 303 DRK-WDLSSMRYMLNGGEAMVAKVGRRILEllEPHglpADAIRPAWGMSETSSgviFSHEFTRagTSDDDHFVE-IGSPI 380
Cdd:PRK12583 310 QRGnFDLSSLRTGIMAGAPCPIEVMRRVMD--EMH---MAEVQIAYGMTETSP---VSLQTTA--ADDLERRVEtVGRTQ 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 381 PGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGYYQRPDLNESVFTEDGWFETGDLGFL-RNGRLTITGRTKDAIIINGI 459
Cdd:PRK12583 380 PHLEVKVVDPDGATVPRGEIGELCTRGYSVMKGYWNNPEATAESIDEDGWMHTGDLATMdEQGYVRIVGRSKDMIIRGGE 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 460 NYYSHAIEsaveelsEIETSYTAACAVRL----GQNSTDQLAIFFV--TSAKLNDEQMSQLLRNIQSHVSqvigvTPEYL 533
Cdd:PRK12583 460 NIYPREIE-------EFLFTHPAVADVQVfgvpDEKYGEEIVAWVRlhPGHAASEEELREFCKARIAHFK-----VPRYF 527
|
570 580
....*....|....*....|..
gi 1776025254 534 LPVqkEEIPKTAIGKIQRTQLK 555
Cdd:PRK12583 528 RFV--DEFPMTVTGKVQKFRMR 547
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
1162-1645 |
3.90e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 131.47 E-value: 3.90e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1162 QAKKTPDR-AAVSY-EGQTLTYRELDERSTQLAIYLQAHGVGP-DRLAgIYVDRSLDMLVGLLAILKAGGAYVPLDPSYP 1238
Cdd:PRK09088 4 HARLQPQRlAAVDLaLGRRWTYAELDALVGRLAAVLRRRGCVDgERLA-VLARNSVWLVALHFACARVGAIYVPLNWRLS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1239 AERLEYMLEDSEVFITLTTSELVntlswnGVTTALLDQDwDEIAQTASDRKVLTRTVTPENLAYVIYTSGSTGKPKGVMI 1318
Cdd:PRK09088 83 ASELDALLQDAEPRLLLGDDAVA------AGRTDVEDLA-AFIASADALEPADTPSIPPERVSLILFTSGTSGQPKGVML 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1319 PHKALTNFLVSMGETPGLTAEDKMLaVTTYCFDIAAL--ELFLPLIKGAHCYICQT-EHTKDVEKLKRDIRTIK-----P 1390
Cdd:PRK09088 156 SERNLQQTAHNFGVLGRVDAHSSFL-CDAPMFHIIGLitSVRPVLAVGGSILVSNGfEPKRTLGRLGDPALGIThyfcvP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1391 TVMQA-------TPATWKMLfysgweneenVKILCGGEALPETLKRYFLDTG---------SEAWNMFG-PTETTIwsav 1453
Cdd:PRK09088 235 QMAQAfraqpgfDAAALRHL----------TALFTGGAPHAAEDILGWLDDGipmvdgfgmSEAGTVFGmSVDCDV---- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1454 qrINDECSRATIGRPIANTQIyiTDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFidnpfePGSKLYRTGDMAR 1533
Cdd:PRK09088 301 --IRAKAGAAGIPTPTVQTRV--VDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAF------TGDGWFRTGDIAR 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1534 WLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMD---NLAAYYTAKHANAS-LTARELRHFVKNA 1609
Cdd:PRK09088 371 RDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADaqwGEVGYLAIVPADGApLDLERIRSHLSTR 450
|
490 500 510
....*....|....*....|....*....|....*.
gi 1776025254 1610 LPAYMVPSYFIQLDHMPLTPNGKIDRNSLKNIDLSG 1645
Cdd:PRK09088 451 LAKYKVPKHLRLVDALPRTASGKLQKARLRDALAAG 486
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
1778-2187 |
5.69e-31 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 129.14 E-value: 5.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1778 DEFWENLRDGKESIAFfnkeeLQRFGISKEIAENADYVPAkasiegkdrFDPSFFqISPKDAEFMDPQLRMLLTHSWKAI 1857
Cdd:PRK07314 20 ESTWKNLLAGKSGIGP-----ITHFDTSDLAVKIAGEVKD---------FNPDDY-MSRKEARRMDRFIQYGIAAAKQAV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1858 EDAGYAAGQI--PQTSVFMSASNNSYRALlpSDTTESLET--PDgYVSwVLAQSGTIPTMISH----KLGLRGPSYFVHA 1929
Cdd:PRK07314 85 EDAGLEITEEnaDRIGVIIGSGIGGLETI--EEQHITLLEkgPR-RVS-PFFVPMAIINMAAGhvsiRYGAKGPNHSIVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1930 NCSSsliGLHS---AYKSLLSAESDYALVGGAtlhtESNI------GYVHQPGLNFSSDGHIKA---FDASADGMIGGEG 1997
Cdd:PRK07314 161 ACAT---GAHAigdAARLIAYGDADVMVAGGA----EAAItplgiaGFAAARALSTRNDDPERAsrpFDKDRDGFVMGEG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1998 VAVVLLKKAADAVKDGDHIYALLRGIGVNNDGadkvgfY---APSVKGQ--ADVVQQVMNQTKIHPESICYVEAHGTGTK 2072
Cdd:PRK07314 234 AGILVLEELEHAKARGAKIYAEVVGYGMTGDA------YhmtAPAPDGEgaARAMKLALKDAGINPEDIDYINAHGTSTP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2073 LGDPIELAALTNVYRQYTNKTQfcgIGSVKTNIGHLDTAAGLAGCIKVVMSLYHQELAPSINYKEPNPNTDLAsspfYVV 2152
Cdd:PRK07314 308 AGDKAETQAIKRVFGEHAYKVA---VSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTINLDNPDEECDLD----YVP 380
|
410 420 430
....*....|....*....|....*....|....*.
gi 1776025254 2153 DQKKtlSREIQthrAALS-SFGLGGTNTHAIFEQFK 2187
Cdd:PRK07314 381 NEAR--ERKID---YALSnSFGFGGTNASLVFKRYE 411
|
|
| KR_3_FAS_SDR_x |
cd08956 |
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 3, complex (x); ... |
4152-4411 |
5.71e-31 |
|
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 3, complex (x); Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. In some instances, such as porcine FAS, an enoyl reductase (ER) module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consists of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthesis uses a dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-KR, forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta- ER. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes KR domains found in many multidomain PKSs, including six of seven Sorangium cellulosum PKSs (encoded by spiDEFGHIJ) which participate in the synthesis of the polyketide scaffold of the cytotoxic spiroketal polyketide spirangien. These seven PKSs have either a single PKS module (SpiF), two PKR modules (SpiD,-E,-I,-J), or three PKS modules (SpiG,-H). This subfamily includes the second KR domains of SpiE,-G, I, and -J, both KR domains of SpiD, and the third KR domain of SpiH. The single KR domain of SpiF, the first and second KR domains of SpiH, the first KR domains of SpiE,-G,- I, and -J, and the third KR domain of SpiG, belong to a different KR_FAS_SDR subfamily. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.
Pssm-ID: 187659 [Multi-domain] Cd Length: 448 Bit Score: 130.08 E-value: 5.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4152 KAHPETGKATEQSAVFPKDHVLlITGGTRGIGLLCARHFAECYGVKKLVLTGR--EQLPPREEWarfktsntslaekiqa 4229
Cdd:cd08956 176 RVAPAATLPPVPRPLDPDGTVL-ITGGTGTLGALLARHLVTEHGVRHLLLVSRrgPDAPGAAEL---------------- 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4230 VRELEAKGVQVEMLSLTLSDDAQVEQTLQHIKRTlGPIGGVIHCAGLTDMDTLAfiRKTSDDIQRVMEPKVSGLTTLYRH 4309
Cdd:cd08956 239 VAELAALGAEVTVAACDVADRAALAALLAAVPAD-HPLTAVVHAAGVLDDGVLT--SLTPERLDAVLRPKVDAAWHLHEL 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4310 VCNEPLQFFVLFSSVSAIIPelSAGQADYAMANSYMDyfAEAHQKH---VPIISVQWPNWKETGM-----GEVTNQAYRE 4381
Cdd:cd08956 316 TRDLDLAAFVLFSSAAGVLG--SPGQANYAAANAFLD--ALAQHRRargLPATSLAWGLWAQASGmtahlSDADLARLAR 391
|
250 260 270
....*....|....*....|....*....|
gi 1776025254 4382 SGLFSITNSEGLRFLDQIVSkMFGPVVLPA 4411
Cdd:cd08956 392 GGLRPLSAEEGLALFDAALA-ADEPVLVPA 420
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
1300-1640 |
6.77e-31 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 126.68 E-value: 6.77e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1300 LAYVIYTSGSTGKPKGVMIPHKALTNFLVSMGETPGLTAEDKMLaVTTYCFDIAALE-LFLPLIKGAHCYIcqTEHTKDV 1378
Cdd:cd17630 2 LATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWL-LSLPLYHVGGLAiLVRSLLAGAELVL--LERNQAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1379 EKlkrDIRTIKPTVMQATPATWKMLFYSGWENE--ENVK-ILCGGEALPETLKRYFLDTGSEAWNMFGPTETTIWSAVQR 1455
Cdd:cd17630 79 AE---DLAPPGVTHVSLVPTQLQRLLDSGQGPAalKSLRaVLLGGAPIPPELLERAADRGIPLYTTYGMTETASQVATKR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1456 INDECsRATIGRPIANTQIYITDsqlapvpagvPGELCIAGDGVAKGYYKKEEltdsrfIDNPFEPGskLYRTGDMARWL 1535
Cdd:cd17630 156 PDGFG-RGGVGVLLPGRELRIVE----------DGEIWVGGASLAMGYLRGQL------VPEFNEDG--WFTTKDLGELH 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1536 PGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMDN-----LAAYYTakhANASLTARELRHFVKNAL 1610
Cdd:cd17630 217 ADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEelgqrPVAVIV---GRGPADPAELRAWLKDKL 293
|
330 340 350
....*....|....*....|....*....|
gi 1776025254 1611 PAYMVPSYFIQLDHMPLTPNGKIDRNSLKN 1640
Cdd:cd17630 294 ARFKLPKRIYPVPELPRTGGGKVDRRALRA 323
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
27-555 |
9.18e-31 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 131.04 E-value: 9.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 27 QPATIPEVLYRTAAELGDTKGIIylqpDGTEVYqSYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNSQLLPAFWGCVL 106
Cdd:COG1021 23 RGETLGDLLRRRAERHPDRIAVV----DGERRL-SYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 107 TGVVPApLAVPP-------TYAESSsgtqklkdawtlldKP-AVITDRGM----HQEMldwAKE--QGLEGFRAIIV--- 169
Cdd:COG1021 98 AGAIPV-FALPAhrraeisHFAEQS--------------EAvAYIIPDRHrgfdYRAL---ARElqAEVPSLRHVLVvgd 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 170 -------EDLLSAEADTDWHQSSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDH--- 239
Cdd:COG1021 160 ageftslDALLAAPADLSEPRPDPDDVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEICGLDADTVYLAALPAAHnfp 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 240 -----------VGGigmlhlrdvylgcqeinvsseTILM----EPLKWLDWIDHYRASVTwapnfafGLV----TDFAEE 300
Cdd:COG1021 240 lsspgvlgvlyAGG---------------------TVVLapdpSPDTAFPLIERERVTVT-------ALVpplaLLWLDA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 301 IKDRKWDLSSMRYMLNGGeamvAKVGRRIlellephglpADAIRPAW--------GMSEtssGVIfshEFTRAGTSDDDH 372
Cdd:COG1021 292 AERSRYDLSSLRVLQVGG----AKLSPEL----------ARRVRPALgctlqqvfGMAE---GLV---NYTRLDDPEEVI 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 373 FVEIGSPI-PGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGYYQRPDLNESVFTEDGWFETGDL-GFLRNGRLTITGRT 450
Cdd:COG1021 352 LTTQGRPIsPDDEVRIVDEDGNPVPPGEVGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLvRRTPDGYLVVEGRA 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 451 KDAIIINGINYYSHAIESAVEELSEIetsyTAACAV-----RLGQNSTdqlAifFVTsakLNDEQMSqlLRNIQSHVSQV 525
Cdd:COG1021 432 KDQINRGGEKIAAEEVENLLLAHPAV----HDAAVVampdeYLGERSC---A--FVV---PRGEPLT--LAELRRFLRER 497
|
570 580 590
....*....|....*....|....*....|...
gi 1776025254 526 iGVtPEYLLP---VQKEEIPKTAIGKIQRTQLK 555
Cdd:COG1021 498 -GL-AAFKLPdrlEFVDALPLTAVGKIDKKALR 528
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
1179-1592 |
1.29e-30 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.
Pssm-ID: 341250 [Multi-domain] Cd Length: 545 Bit Score: 130.80 E-value: 1.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1179 LTYRELDERSTQLAIYLQAHGV--GPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLEDSEVFITLT 1256
Cdd:cd05927 6 ISYKEVAERADNIGSALRSLGGkpAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVFC 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1257 TselvntlswNGVTTALldqdWDEIAQTASDRKVLTRTVTPENLAYVIYTSGSTGKPKGVMIPHKALTNFLVSM----GE 1332
Cdd:cd05927 86 D---------AGVKVYS----LEEFEKLGKKNKVPPPPPKPEDLATICYTSGTTGNPKGVMLTHGNIVSNVAGVfkilEI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1333 TPGLTAEDKMLAvttycfdiaalelFLPLikgAHCY----ICQTEH--------TKDVEKLKRDIRTIKPTV-------- 1392
Cdd:cd05927 153 LNKINPTDVYIS-------------YLPL---AHIFervvEALFLYhgakigfySGDIRLLLDDIKALKPTVfpgvprvl 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1393 ----------MQATPATWKMLFYSGWENEE----------------------------NVKILCGGEA--LPETLKryFL 1432
Cdd:cd05927 217 nriydkifnkVQAKGPLKRKLFNFALNYKLaelrsgvvraspfwdklvfnkikqalggNVRLMLTGSAplSPEVLE--FL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1433 DT--GSEAWNMFGPTETTIWSAVQRINDECSrATIGRPIANTQIYITD------SQLAPVPAgvpGELCIAGDGVAKGYY 1504
Cdd:cd05927 295 RValGCPVLEGYGQTECTAGATLTLPGDTSV-GHVGGPLPCAEVKLVDvpemnyDAKDPNPR---GEVCIRGPNVFSGYY 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1505 KKEELTDSRFIDNPFepgsklYRTGDMARWLPGGRIEYIGRIDNQVKI-RGFRIELGDIESRLSEHPGI----------- 1572
Cdd:cd05927 371 KDPEKTAEALDEDGW------LHTGDIGEWLPNGTLKIIDRKKNIFKLsQGEYVAPEKIENIYARSPFVaqifvygdslk 444
|
490 500
....*....|....*....|..
gi 1776025254 1573 --LECVVVADMDNLAAYYTAKH 1592
Cdd:cd05927 445 sfLVAIVVPDPDVLKEWAASKG 466
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
1151-1654 |
1.94e-30 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 130.56 E-value: 1.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1151 PYITFHELFEQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQaHGVG---PDRLAgIYVDRSLDMLVGLLAILKAG 1227
Cdd:PRK08974 21 RYQSLVDMFEQAVARYADQPAFINMGEVMTFRKLEERSRAFAAYLQ-NGLGlkkGDRVA-LMMPNLLQYPIALFGILRAG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1228 GAYVPLDPSYPAERLEYMLEDSEVFITLTTSELVNTLSW--------NGVTTALLDQ---------------------DW 1278
Cdd:PRK08974 99 MIVVNVNPLYTPRELEHQLNDSGAKAIVIVSNFAHTLEKvvfktpvkHVILTRMGDQlstakgtlvnfvvkyikrlvpKY 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1279 DeIAQTASDRKVLTR---------TVTPENLAYVIYTSGSTGKPKGVMIPHK-ALTNFLVSMGETPGLTAEDKMLAVTTY 1348
Cdd:PRK08974 179 H-LPDAISFRSALHKgrrmqyvkpELVPEDLAFLQYTGGTTGVAKGAMLTHRnMLANLEQAKAAYGPLLHPGKELVVTAL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1349 -CFDIAALE----LFLPLikGAHCYIcqTEHTKDVEKLKRDIRTIKPTVMQATpatwKMLFySGWENEENVKIL------ 1417
Cdd:PRK08974 258 pLYHIFALTvnclLFIEL--GGQNLL--ITNPRDIPGFVKELKKYPFTAITGV----NTLF-NALLNNEEFQELdfsslk 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1418 ---CGGEALPETL-KRYFLDTGSEAWNMFGPTETTIWSAVQRINDECSRATIGRPIANTQIYITDSQLAPVPAGVPGELC 1493
Cdd:PRK08974 329 lsvGGGMAVQQAVaERWVKLTGQYLLEGYGLTECSPLVSVNPYDLDYYSGSIGLPVPSTEIKLVDDDGNEVPPGEPGELW 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1494 IAGDGVAKGYYKKEELTDSRFIDNpfepgskLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGIL 1573
Cdd:PRK08974 409 VKGPQVMLGYWQRPEATDEVIKDG-------WLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVL 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1574 ECVVV-----ADMDNLAAYYTAKhaNASLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLKNidlsgEQL 1648
Cdd:PRK08974 482 EVAAVgvpseVSGEAVKIFVVKK--DPSLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRD-----EAR 554
|
....*.
gi 1776025254 1649 KQRQTS 1654
Cdd:PRK08974 555 AKVDNK 560
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
1163-1650 |
2.52e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 128.74 E-value: 2.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1163 AKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAgIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERL 1242
Cdd:PRK07638 11 ASLQPNKIAIKENDRVLTYKDWFESVCKVANWLNEKESKNKTIA-ILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1243 EYMLEDSEVFITLTTSELVNTLSwnGVTTALLDQD-WDEIAQTASDRkvLTRTVTPENLA-YVIYTSGSTGKPKGVMIPH 1320
Cdd:PRK07638 90 KERLAISNADMIVTERYKLNDLP--DEEGRVIEIDeWKRMIEKYLPT--YAPIENVQNAPfYMGFTSGSTGKPKAFLRAQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1321 KALTNFLVSMGETPGLTAEDKMLAVTTYC---FDIAALE-LFLplikGAHCYICQTEHTKDVeklKRDIRTIKPTVMQAT 1396
Cdd:PRK07638 166 QSWLHSFDCNVHDFHMKREDSVLIAGTLVhslFLYGAIStLYV----GQTVHLMRKFIPNQV---LDKLETENISVMYTV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1397 PAtwkML--FYSGWENEEN-VKILCGG--------EALPET---LKRYfldtgseawNMFGPTETTIWSAVQRINDECSR 1462
Cdd:PRK07638 239 PT---MLesLYKENRVIENkMKIISSGakweaeakEKIKNIfpyAKLY---------EFYGASELSFVTALVDEESERRP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1463 ATIGRPIANTQIYITDSqlapvpagvPGELCIAGDgVAKGYYKkeelTDSRFIDnpFEPGSKLYRTGDMARWLPGGRIEY 1542
Cdd:PRK07638 307 NSVGRPFHNVQVRICNE---------AGEEVQKGE-IGTVYVK----SPQFFMG--YIIGGVLARELNADGWMTVRDVGY 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1543 I---------GRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMDnlaAYYTAK-----HANAslTARELRHFVKN 1608
Cdd:PRK07638 371 EdeegfiyivGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPD---SYWGEKpvaiiKGSA--TKQQLKSFCLQ 445
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1776025254 1609 ALPAYMVPSYFIQLDHMPLTPNGKIDRNSLKNIDLSGEQLKQ 1650
Cdd:PRK07638 446 RLSSFKIPKEWHFVDEIPYTNSGKIARMEAKSWIENQEKIYE 487
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
61-554 |
3.18e-30 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 128.18 E-value: 3.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 61 SYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNSQLLPAFWGCVLTGVVPAPLAvpPTY-AESSSGTqkLKDAwtlldK 139
Cdd:cd12116 14 SYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLD--PDYpADRLRYI--LEDA-----E 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 140 PAVI-TDRGMhqemldwakeqgLEGFRAIIVEDLLSAEADTD-----WHQSSPEDLALLLLTSGSTGTPKAVMLNHRNIM 213
Cdd:cd12116 85 PALVlTDDAL------------PDRLPAGLPVLLLALAAAAAapaapRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 214 SMVKGIIQMQGFTRED-----ITFNwmpFDhvggIGMLHLRDVYLGCQEINVSSETILMEPLKWLDWIDHYRASV----- 283
Cdd:cd12116 153 NFLHSMRERLGLGPGDrllavTTYA---FD----ISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSITVmqatp 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 284 -TWAPNFAFGlvtdfaeeikdrkW-DLSSMRyMLNGGEAMVAKVGRRILellephglpaDAIRPAWGM---SETSsgvIF 358
Cdd:cd12116 226 aTWRMLLDAG-------------WqGRAGLT-ALCGGEALPPDLAARLL----------SRVGSLWNLygpTETT---IW 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 359 ShefTRAGTSDDDHFVEIGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGYYQRPDLNESVFTEDG-------WF 431
Cdd:cd12116 279 S---TAARVTAAAGPIPIGRPLANTQVYVLDAALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPfagpgsrLY 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 432 ETGDLGFLR-NGRLTITGRTKDAIIINGinyysHAIesaveELSEIETSYT-----AACAVRLGQNSTDQLAIFFVTSAK 505
Cdd:cd12116 356 RTGDLVRRRaDGRLEYLGRADGQVKIRG-----HRI-----ELGEIEAALAahpgvAQAAVVVREDGGDRRLVAYVVLKA 425
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1776025254 506 LNDEQMSQLLRNIQSHVsqvigvtPEYLLP---VQKEEIPKTAIGKIQRTQL 554
Cdd:cd12116 426 GAAPDAAALRAHLRATL-------PAYMVPsafVRLDALPLTANGKLDRKAL 470
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
1152-1640 |
3.26e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 128.85 E-value: 3.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1152 YITFHelfeqqAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYV 1231
Cdd:PRK06145 7 SIAFH------ARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1232 PLDPSYPAERLEYMLEDSEVFITLTTSEL---VNTLSWNGVTTALLDQDWDEIAQTASDRKVLTrTVTPENLAYVIYTSG 1308
Cdd:PRK06145 81 PINYRLAADEVAYILGDAGAKLLLVDEEFdaiVALETPKIVIDAAAQADSRRLAQGGLEIPPQA-AVAPTDLVRLMYTSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1309 STGKPKGVMIPHKALTNFLVSMGETPGLTAEDKMLAVTTYcFDIAALElfLPLIK-----GAHCYICQTEHTKDVEKLKR 1383
Cdd:PRK06145 160 TTDRPKGVMHSYGNLHWKSIDHVIALGLTASERLLVVGPL-YHVGAFD--LPGIAvlwvgGTLRIHREFDPEAVLAAIER 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1384 DIRT------IKPTVMQATPATWKMLFYS-GWeneenvkILCGGEALPETLKRYF--LDTGSEAWNMFGPTETTIWSAVQ 1454
Cdd:PRK06145 237 HRLTcawmapVMLSRVLTVPDRDRFDLDSlAW-------CIGGGEKTPESRIRDFtrVFTRARYIDAYGLTETCSGDTLM 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1455 RINDECSR-ATIGRPIANTQIYITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPFepgsklyRTGDMAR 1533
Cdd:PRK06145 310 EAGREIEKiGSTGRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWF-------RSGDVGY 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1534 WLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMD-NLAAYYTAK---HANASLTARELRHFVKNA 1609
Cdd:PRK06145 383 LDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDdRWGERITAVvvlNPGATLTLEALDRHCRQR 462
|
490 500 510
....*....|....*....|....*....|.
gi 1776025254 1610 LPAYMVPSYFIQLDHMPLTPNGKIDRNSLKN 1640
Cdd:PRK06145 463 LASFKVPRQLKVRDELPRNPSGKVLKRVLRD 493
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
1169-1639 |
4.23e-30 |
|
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.
Pssm-ID: 341268 [Multi-domain] Cd Length: 439 Bit Score: 127.21 E-value: 4.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1169 RAAVSYEGQTLTYRELDERSTQLAIYLQAHGVgpDRLAGIYVDRSLD--MLVG-LLAILKAGGAYVPLDPSYPAERLEYM 1245
Cdd:cd05958 1 RTCLRSPEREWTYRDLLALANRIANVLVGELG--IVPGNRVLLRGSNspELVAcWFGIQKAGAIAVATMPLLRPKELAYI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1246 LEDSEVfitlttselvntlswngvTTALLDQdwdeiAQTASDrkvltrtvtpeNLAYVIYTSGSTGKPKGVMIPHKALtn 1325
Cdd:cd05958 79 LDKARI------------------TVALCAH-----ALTASD-----------DICILAFTSGTTGAPKATMHFHRDP-- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1326 FLVSMGETP---GLTAEDKMLAVTTYCFDIA-ALELFLPLIKGAHCyICQTEHTKDveKLKRDIRTIKPTVMQATPATWK 1401
Cdd:cd05958 123 LASADRYAVnvlRLREDDRFVGSPPLAFTFGlGGVLLFPFGVGASG-VLLEEATPD--LLLSAIARYKPTVLFTAPTAYR 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1402 MLFYSGWENEEN----VKILCGGEALP-ETLKRYFLDTGSEAWNMFGPTET--TIWSAVQrinDECSRATIGRPIANTQI 1474
Cdd:cd05958 200 AMLAHPDAAGPDlsslRKCVSAGEALPaALHRAWKEATGIPIIDGIGSTEMfhIFISARP---GDARPGATGKPVPGYEA 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1475 YITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRfidnpfepGSKLYrTGDMARWLPGGRIEYIGRIDNQVKIRG 1554
Cdd:cd05958 277 KVVDDEGNPVPDGTIGRLAVRGPTGCRYLADKRQRTYVQ--------GGWNI-TGDTYSRDPDGYFRHQGRSDDMIVSGG 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1555 FRIELGDIESRLSEHPGILECVVVA--DMDNLA---AYYTAK--HANASLTARELRHFVKNALPAYMVPSYFIQLDHMPL 1627
Cdd:cd05958 348 YNIAPPEVEDVLLQHPAVAECAVVGhpDESRGVvvkAFVVLRpgVIPGPVLARELQDHAKAHIAPYKYPRAIEFVTELPR 427
|
490
....*....|..
gi 1776025254 1628 TPNGKIDRNSLK 1639
Cdd:cd05958 428 TATGKLQRFALR 439
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
30-454 |
4.46e-30 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 128.92 E-value: 4.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 30 TIPEV-----LYRTAAELGDTKGIIYLqpdGTEVyqSYRRLWDDGLRIVKGLRQS-GLKAKQSVILQLGDNSQLLPAFWG 103
Cdd:PRK08314 6 TLPETslfhnLEVSARRYPDKTAIVFY---GRAI--SYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 104 CVLTG--VVPA-PLAVPPTYAE--SSSGTQKLKDAWTLLDK--PAVITDR------GMHQEML---------DWAKE--- 158
Cdd:PRK08314 81 ILRANavVVPVnPMNREEELAHyvTDSGARVAIVGSELAPKvaPAVGNLRlrhvivAQYSDYLpaepeiavpAWLRAepp 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 159 -QGLEGFRAIIVEDLLSAEADTDWHQSSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPF 237
Cdd:PRK08314 161 lQALAPGGVVAWKEALAAGLAPPPHTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 238 DHVGG-IGMLHlRDVYLGcqeinvssETILMEPlKW-----LDWIDHYRASVTWAPNfafGLVTDFAEEIKDRKWDLSSM 311
Cdd:PRK08314 241 FHVTGmVHSMN-APIYAG--------ATVVLMP-RWdreaaARLIERYRVTHWTNIP---TMVVDFLASPGLAERDLSSL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 312 RYMLNGGEAMVAKVGRRILELLephGLPadaIRPAWGMSETSSgvifsheFTRAGTSDDDHFVEIGSPIPGFSMRIVN-D 390
Cdd:PRK08314 308 RYIGGGGAAMPEAVAERLKELT---GLD---YVEGYGLTETMA-------QTHSNPPDRPKLQCLGIPTFGVDARVIDpE 374
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1776025254 391 HNELVEEGEIGRFQVSGLSVTSGYYQRPDLNESVFTE-DG--WFETGDLGFL-RNGRLTITGRTKDAI 454
Cdd:PRK08314 375 TLEELPPGEVGEIVVHGPQVFKGYWNRPEATAEAFIEiDGkrFFRTGDLGRMdEEGYFFITDRLKRMI 442
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
185-549 |
7.94e-30 |
|
C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.
Pssm-ID: 341235 [Multi-domain] Cd Length: 490 Bit Score: 127.45 E-value: 7.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 185 SPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDH----VGGIGMLHLRDVYLGCQEINV 260
Cdd:cd05909 145 QPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFFHsfglTGCLWLPLLSGIKVVFHPNPL 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 261 SSETILmeplkwlDWIDHYRASVTWA-PNFaFGLVTDFAEeikdrKWDLSSMRYMLNGGEAMVAKVGRRILELLephGLP 339
Cdd:cd05909 225 DYKKIP-------ELIYDKKATILLGtPTF-LRGYARAAH-----PEDFSSLRLVVAGAEKLKDTLRQEFQEKF---GIR 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 340 adaIRPAWGMSETSSGVIFSHEFT--RAGTsdddhfveIGSPIPGFSMRIVN-DHNELVEEGEIGRFQVSGLSVTSGYYQ 416
Cdd:cd05909 289 ---ILEGYGTTECSPVISVNTPQSpnKEGT--------VGRPLPGMEVKIVSvETHEEVPIGEGGLLLVRGPNVMLGYLN 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 417 RPDLNESVFtEDGWFETGDLGFL-RNGRLTITGRTKDAIIINGiNYYSHaieSAVEE-LSEIETSYTAACAVRLGQNSTD 494
Cdd:cd05909 358 EPELTSFAF-GDGWYDTGDIGKIdGEGFLTITGRLSRFAKIAG-EMVSL---EAIEDiLSEILPEDNEVAVVSVPDGRKG 432
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1776025254 495 QLAIFFVTSAKLNDEQMSQLLRNIQshvsqvigvTPEYLLP---VQKEEIPKTAIGKI 549
Cdd:cd05909 433 EKIVLLTTTTDTDPSSLNDILKNAG---------ISNLAKPsyiHQVEEIPLLGTGKP 481
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
28-555 |
1.27e-29 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 128.53 E-value: 1.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 28 PATIPEVLYRTAAELGDTKGIIYlQPDGTE----VYQSYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNSQLLPAFWG 103
Cdd:PRK07529 24 PASTYELLSRAAARHPDAPALSF-LLDADPldrpETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 104 CVLTGVVPA--PLAVPPTYAE--SSSGT---------------QKLKDA---------WTLLD-KPAVITDRGMHQEMLD 154
Cdd:PRK07529 103 GEAAGIANPinPLLEPEQIAEllRAAGAkvlvtlgpfpgtdiwQKVAEVlaalpelrtVVEVDlARYLPGPKRLAVPLIR 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 155 WAKEQGLEGFRAIIveDLLSAEADTDWHQSSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNW 234
Cdd:PRK07529 183 RKAHARILDFDAEL--ARQPGDRLFSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDTVFCG 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 235 MPFDHVGG---IGMLHLrdvylgcqeinvSS--ETILMEPLKWLD-------W--IDHYRasvtwaPNFAFGLVTDFAE- 299
Cdd:PRK07529 261 LPLFHVNAllvTGLAPL------------ARgaHVVLATPQGYRGpgvianfWkiVERYR------INFLSGVPTVYAAl 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 300 -EIKDRKWDLSSMRYMLNGGEAMVAKVGRRILELLephGLPadaIRPAWGMSETSSGVIFS---HEfTRAGTsdddhfve 375
Cdd:PRK07529 323 lQVPVDGHDISSLRYALCGAAPLPVEVFRRFEAAT---GVR---IVEGYGLTEATCVSSVNppdGE-RRIGS-------- 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 376 IGSPIPGFSMRIV---NDHNELVE--EGEIGRFQVSGLSVTSGYYQrPDLNESVFTEDGWFETGDLGFL-RNGRLTITGR 449
Cdd:PRK07529 388 VGLRLPYQRVRVVildDAGRYLRDcaVDEVGVLCIAGPNVFSGYLE-AAHNKGLWLEDGWLNTGDLGRIdADGYFWLTGR 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 450 TKDAIIINGINYYSHAIESAVEELSEIetsyTAACAVrlGQNST--DQLAIFFVTSAKLNDEQMSQLLRNIQSHVSQVIG 527
Cdd:PRK07529 467 AKDLIIRGGHNIDPAAIEEALLRHPAV----ALAAAV--GRPDAhaGELPVAYVQLKPGASATEAELLAFARDHIAERAA 540
|
570 580
....*....|....*....|....*...
gi 1776025254 528 VtPEYLLPVqkEEIPKTAIGKIQRTQLK 555
Cdd:PRK07529 541 V-PKHVRIL--DALPKTAVGKIFKPALR 565
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
1154-1639 |
1.98e-29 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 127.01 E-value: 1.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1154 TFHELFEQQAKKTPDRAAVSY----EGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGA 1229
Cdd:cd05906 11 TLLELLLRAAERGPTKGITYIdadgSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1230 YVPLDP----SYPAERLEYMLEDSEVF---ITLTTSELVNTLSwnGVTTALLDQDWDEIAQT---ASDRKVLTRTVTPEN 1299
Cdd:cd05906 91 PAPLTVpptyDEPNARLRKLRHIWQLLgspVVLTDAELVAEFA--GLETLSGLPGIRVLSIEellDTAADHDLPQSRPDD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1300 LAYVIYTSGSTGKPKGVMIPHKALTNFLVSMGETPGLTAEDKMLAVTTycFD-IAAL-ELFL-PLIKGAHCYICQTEHT- 1375
Cdd:cd05906 169 LALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVP--LDhVGGLvELHLrAVYLGCQQVHVPTEEIl 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1376 KDVEKLKRDI------RTIKPTVMQA---------TPATW-----KMLFYSGwenEENVKILCggEALPETLKRYFL--D 1433
Cdd:cd05906 247 ADPLRWLDLIdryrvtITWAPNFAFAllndlleeiEDGTWdlsslRYLVNAG---EAVVAKTI--RRLLRLLEPYGLppD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1434 TGSEAWNMfgpTET---TIWSAV---QRINDECSRATIGRPIANTQIYITDSQLAPVPAGVPGELCIAGDGVAKGYYKKE 1507
Cdd:cd05906 322 AIRPAFGM---TETcsgVIYSRSfptYDHSQALEFVSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNP 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1508 ELTDSRFIDNPFepgsklYRTGDMArWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVA-------- 1579
Cdd:cd05906 399 EANAEAFTEDGW------FRTGDLG-FLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPSFTAAfavrdpga 471
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1776025254 1580 DMDNLAAYY--TAKHANA-SLTARELRHFVKNAL---PAYMVPsyfIQLDHMPLTPNGKIDRNSLK 1639
Cdd:cd05906 472 ETEELAIFFvpEYDLQDAlSETLRAIRSVVSREVgvsPAYLIP---LPKEEIPKTSLGKIQRSKLK 534
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
185-473 |
3.97e-29 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 125.37 E-value: 3.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 185 SPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDHVGGIgmlhlrdvylgcqeiNVSSET 264
Cdd:PRK07514 154 GADDLAAILYTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIHALPIFHTHGL---------------FVATNV 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 265 ILMEplkwldwidhyRASVTWAPNFAFGLVTDF------------------AEEIKDRKwDLSSMRYMLNGGEAMVA--- 323
Cdd:PRK07514 219 ALLA-----------GASMIFLPKFDPDAVLALmpratvmmgvptfytrllQEPRLTRE-AAAHMRLFISGSAPLLAeth 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 324 -----KVGRRILEllephglpadaiRpaWGMSETssGVIFSHEFT---RAGTsdddhfveIGSPIPGFSMRIVN-DHNEL 394
Cdd:PRK07514 287 refqeRTGHAILE------------R--YGMTET--NMNTSNPYDgerRAGT--------VGFPLPGVSLRVTDpETGAE 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 395 VEEGEIGRFQVSGLSVTSGYYQRPDLNESVFTEDGWFETGDLGFL-RNGRLTITGRTKDAIIINGINYYSHAIESAVEEL 473
Cdd:PRK07514 343 LPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGFFITGDLGKIdERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDEL 422
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
186-554 |
4.01e-29 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 124.50 E-value: 4.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 186 PEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKG---IIQMQGFTREDITFNWMPFDHVGGIgmlHLRDVYLGCQEINVSS 262
Cdd:cd17650 92 PEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAwrrEYELDSFPVRLLQMASFSFDVFAGD---FARSLLNGGTLVICPD 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 263 ETiLMEPLKWLDWIDHYRASVTWA-PNFAFGLVtdfaEEIKDRKWDLSSMRYMLNGGEAMVAKVGRRILELLEPHglpaD 341
Cdd:cd17650 169 EV-KLDPAALYDLILKSRITLMEStPALIRPVM----AYVYRNGLDLSAMRLLIVGSDGCKAQDFKTLAARFGQG----M 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 342 AIRPAWGMSETS--SGVifsHEFTRAGTSDDDhFVEIGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGYYQRPD 419
Cdd:cd17650 240 RIINSYGVTEATidSTY---YEEGRDPLGDSA-NVPIGRPLPNTAMYVLDERLQPQPVGVAGELYIGGAGVARGYLNRPE 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 420 LNESVFTEDGW------FETGDLG-FLRNGRLTITGRTKDAIIINGINYYSHAIESAVEELSEIEtsyTAACAVRLGQNS 492
Cdd:cd17650 316 LTAERFVENPFapgermYRTGDLArWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAID---EAVVAVREDKGG 392
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1776025254 493 TDQLAIFFVTSAKLNdeqmsqlLRNIQSHVSQVIgvtPEYLLP---VQKEEIPKTAIGKIQRTQL 554
Cdd:cd17650 393 EARLCAYVVAAATLN-------TAELRAFLAKEL---PSYMIPsyyVQLDALPLTPNGKVDRRAL 447
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
3426-3776 |
4.02e-29 |
|
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) Claisen-like condensation reaction. Members are share strong structural similarity, and are involved in the synthesis and degradation of fatty acids, and the production of polyketides, a diverse group of natural products.
Pssm-ID: 238201 [Multi-domain] Cd Length: 254 Bit Score: 119.47 E-value: 4.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3426 QQRLLMTYVWKALEDAGCPpqslSGTGTGIFIGTGNTGYkdlfhranlpiEGHAATGhmipsvgpnRMSYFLNI-HGPSE 3504
Cdd:cd00327 7 ASELGFEAAEQAIADAGLS----KGPIVGVIVGTTGGSG-----------EFSGAAG---------QLAYHLGIsGGPAY 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3505 PVETACSSSLVAIHRAVTAMQNGDCEMAIAGGVNTIlteeahisyskagmlskdgrcktfsadangyVRGEGVGMVMLKK 3584
Cdd:cd00327 63 SVNQACATGLTALALAVQQVQNGKADIVLAGGSEEF-------------------------------VFGDGAAAAVVES 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3585 LEDAERDGNHIYGVIRGTAENHGGrANTLTSPNPKAQADLLVRAYRQAGIDPSTVTYIEAHGTGTELGDPIEINGLKAAF 3664
Cdd:cd00327 112 EEHALRRGAHPQAEIVSTAATFDG-ASMVPAVSGEGLARAARKALEGAGLTPSDIDYVEAHGTGTPIGDAVELALGLDPD 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3665 KelsnmrgesqpdvpDHRCGIGSVKSNIGHLELAAGISGLIKVLLQMKHktlvkslhcetlnpylqltdspfyivqekqE 3744
Cdd:cd00327 191 G--------------VRSPAVSATLIMTGHPLGAAGLAILDELLLMLEH------------------------------E 226
|
330 340 350
....*....|....*....|....*....|..
gi 1776025254 3745 WKSVTDcdgnELPRRAGISSFGIGGVNAHIVI 3776
Cdd:cd00327 227 FIPPTP----REPRTVLLLGFGLGGTNAAVVL 254
|
|
| PRK08439 |
PRK08439 |
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed |
1816-2186 |
5.31e-29 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
Pssm-ID: 236265 [Multi-domain] Cd Length: 406 Bit Score: 123.30 E-value: 5.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1816 PAKASIEGKDrFDPSFFqISPKDAEFMDPQLRMLLTHSWKAIEDAGYAAGQIPQTSvfMSASNNSYRALLPSDTTESLet 1895
Cdd:PRK08439 45 PVQIAGEITD-FDPTEV-MDPKEVKKADRFIQLGLKAAREAMKDAGFLPEELDAER--FGVSSASGIGGLPNIEKNSI-- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1896 pdgyvswVLAQSGT-------IPT--------MISHKLGLRGPSYFVHANCSSSLIGLHSAYKSLLSAESDYALVGGAtl 1960
Cdd:PRK08439 119 -------ICFEKGPrkispffIPSalvnmlggFISIEHGLKGPNLSSVTACAAGTHAIIEAVKTIMLGGADKMLVVGA-- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1961 htESNI------GYVHQPGLNFSSDGHIKA---FDASADGMIGGEGVAVVLLKKAADAVKDGDHIYALLRGIGvnnDGAD 2031
Cdd:PRK08439 190 --ESAIcpvgigGFAAMKALSTRNDDPKKAsrpFDKDRDGFVMGEGAGALVLEEYESAKKRGAKIYAEIIGFG---ESGD 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2032 KVGFYAPSVKGQADVVQQVMNQTKihPESICYVEAHGTGTKLGDPIELAALTNVyrqYTNKTQFCGIGSVKTNIGHLDTA 2111
Cdd:PRK08439 265 ANHITSPAPEGPLRAMKAALEMAG--NPKIDYINAHGTSTPYNDKNETAALKEL---FGSKEKVPPVSSTKGQIGHCLGA 339
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1776025254 2112 AGLAGCIKVVMSLYHQELAPSINYKEPNPNTDLASSPfyvvdqkkTLSREIQTHRAALSSFGLGGTNTHAIFEQF 2186
Cdd:PRK08439 340 AGAIEAVISIMAMRDGILPPTINQETPDPECDLDYIP--------NVARKAELNVVMSNSFGFGGTNGVVIFKKV 406
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
1176-1638 |
5.89e-29 |
|
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.
Pssm-ID: 341230 [Multi-domain] Cd Length: 505 Bit Score: 125.04 E-value: 5.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1176 GQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLEDSEVFITL 1255
Cdd:cd05904 30 GRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1256 TTSELVNTLSWNGVTTALLDQD-------WDEIAQTASDRKVLTRtVTPENLAYVIYTSGSTGKPKGVMIPHK---ALTN 1325
Cdd:cd05904 110 TTAELAEKLASLALPVVLLDSAefdslsfSDLLFEADEAEPPVVV-IKQDDVAALLYSSGTTGRSKGVMLTHRnliAMVA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1326 FLVsMGETPGLTAEDKMLAVTTYcFDIAALELFL--PLIKGAHCYICQtehTKDVEKLKRDIRTIKPTVMQATPATWKML 1403
Cdd:cd05904 189 QFV-AGEGSNSDSEDVFLCVLPM-FHIYGLSSFAlgLLRLGATVVVMP---RFDLEELLAAIERYKVTHLPVVPPIVLAL 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1404 FYSGWENEENVK----ILCGGEALP----ETLKRYF----LDTGseawnmFGPTETTIWSAVQrINDECSRA---TIGRP 1468
Cdd:cd05904 264 VKSPIVDKYDLSslrqIMSGAAPLGkeliEAFRAKFpnvdLGQG------YGMTESTGVVAMC-FAPEKDRAkygSVGRL 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1469 IANTQIYITD-SQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSrfidnpfepgsklyrTGDMARWLPGGRIEYI---- 1543
Cdd:cd05904 337 VPNVEAKIVDpETGESLPPNQTGELWIRGPSIMKGYLNNPEATAA---------------TIDKEGWLHTGDLCYIdedg 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1544 -----GRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMDNLA----AYYTAKHANASLTARELRHFVknalpAYM 1614
Cdd:cd05904 402 ylfivDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAgevpMAFVVRKPGSSLTEDEIMDFV-----AKQ 476
|
490 500 510
....*....|....*....|....*....|.
gi 1776025254 1615 VPSY-------FIqlDHMPLTPNGKIDRNSL 1638
Cdd:cd05904 477 VAPYkkvrkvaFV--DAIPKSPSGKILRKEL 505
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
185-554 |
6.47e-29 |
|
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341306 [Multi-domain] Cd Length: 491 Bit Score: 124.76 E-value: 6.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 185 SPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMP--FDH---------VGGiGMLHLRdvyl 253
Cdd:cd17651 134 DADDLAYVIYTSGSTGRPKGVVMPHRSLANLVAWQARASSLGPGARTLQFAGlgFDVsvqeifstlCAG-ATLVLP---- 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 254 gcqeinvsSETILMEPLKWLDWIDHYRASVTWAPNFAFGLVtdfAEEIKDRKWDLSSMRYMLNGGEAMVakVGRRILELL 333
Cdd:cd17651 209 --------PEEVRTDPPALAAWLDEQRISRVFLPTVALRAL---AEHGRPLGVRLAALRYLLTGGEQLV--LTEDLREFC 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 334 EphGLPADAIRPAWGMSETSsgVIFSHEFTrAGTSDDDHFVEIGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSG 413
Cdd:cd17651 276 A--GLPGLRLHNHYGPTETH--VVTALSLP-GDPAAWPAPPPIGRPIDNTRVYVLDAALRPVPPGVPGELYIGGAGLARG 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 414 YYQRPDLNESVFTEDGW------FETGDLG-FLRNGRLTITGRTKDAIIINGinyysHAIesaveELSEIETS------- 479
Cdd:cd17651 351 YLNRPELTAERFVPDPFvpgarmYRTGDLArWLPDGELEFLGRADDQVKIRG-----FRI-----ELGEIEAAlarhpgv 420
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1776025254 480 YTAACAVRLGQNSTDQLAIFFVTsaklnDEQMSQLLRNIQSHVSQVIgvtPEYLLP---VQKEEIPKTAIGKIQRTQL 554
Cdd:cd17651 421 REAVVLAREDRPGEKRLVAYVVG-----DPEAPVDAAELRAALATHL---PEYMVPsafVLLDALPLTPNGKLDRRAL 490
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
34-554 |
8.74e-29 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.
Pssm-ID: 341284 [Multi-domain] Cd Length: 518 Bit Score: 124.67 E-value: 8.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 34 VLYRTAAELGDTKgIIYLQPDGTEVYQSYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNSQLLPAFWGCVLTGVV--P 111
Cdd:cd12119 1 LLEHAARLHGDRE-IVSRTHEGEVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVlhT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 112 APLAVPP---TY----AEsssgtqklkDAWTLLDK---P--AVITDRGMHQE----MLDWAKEQGLEGFRAIIVEDLLSA 175
Cdd:cd12119 80 INPRLFPeqiAYiinhAE---------DRVVFVDRdflPllEAIAPRLPTVEhvvvMTDDAAMPEPAGVGVLAYEELLAA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 176 EADT-DWHQSSPEDLALLLLTSGSTGTPKAVMLNHRNIM--SMVKGIIQMQGFTREDITFNWMPFDHVGGIGMLHLRdVY 252
Cdd:cd12119 151 ESPEyDWPDFDENTAAAICYTSGTTGNPKGVVYSHRSLVlhAMAALLTDGLGLSESDVVLPVVPMFHVNAWGLPYAA-AM 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 253 LGcqeinvsSETIL----MEPLKWLDWIDHYRasVTWA---PNFAFGLvtdfAEEIKDRKWDLSSMRYMLNGGEAMVAKV 325
Cdd:cd12119 230 VG-------AKLVLpgpyLDPASLAELIEREG--VTFAagvPTVWQGL----LDHLEANGRDLSSLRRVVIGGSAVPRSL 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 326 GRRILEllepHGLPadaIRPAWGMSETSSGVIFSHEFTRAGTSDDDHFVEI----GSPIPGFSMRIVNDH-NELVEEGE- 399
Cdd:cd12119 297 IEAFEE----RGVR---VIHAWGMTETSPLGTVARPPSEHSNLSEDEQLALrakqGRPVPGVELRIVDDDgRELPWDGKa 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 400 IGRFQVSGLSVTSGYYQRPDLNESvFTEDGWFETGDLGFL-RNGRLTITGRTKDAIIINGINYYSHAIESAveeLSEIET 478
Cdd:cd12119 370 VGELQVRGPWVTKSYYKNDEESEA-LTEDGWLRTGDVATIdEDGYLTITDRSKDVIKSGGEWISSVELENA---IMAHPA 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 479 SYTAAC--------------AVRLGQNSTdqlaiffVTSAKLNDeQMSQLLRNIQshvsqvigvTPEYLLPVqkEEIPKT 544
Cdd:cd12119 446 VAEAAVigvphpkwgerplaVVVLKEGAT-------VTAEELLE-FLADKVAKWW---------LPDDVVFV--DEIPKT 506
|
570
....*....|
gi 1776025254 545 AIGKIQRTQL 554
Cdd:cd12119 507 STGKIDKKAL 516
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
1154-1633 |
9.18e-29 |
|
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341289 [Multi-domain] Cd Length: 587 Bit Score: 125.38 E-value: 9.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1154 TFHELFEQQAKKTPDRAAVSYEG------QTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAG 1227
Cdd:cd17634 54 LAANALDRHLRENGDRTAIIYEGddtsqsRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIG 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1228 GAYVPLDPSYPAERLEYMLEDSEVFITLTTSE------LVN---------TLSWNGVTTALL--------------DQDW 1278
Cdd:cd17634 134 AVHSVIFGGFAPEAVAGRIIDSSSRLLITADGgvragrSVPlkknvddalNPNVTSVEHVIVlkrtgsdidwqegrDLWW 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1279 DEIAQTASDRKVLTRtVTPENLAYVIYTSGSTGKPKGVMIPHKAltnFLVSMGETpgltaedkmlavTTYCFDIAALELF 1358
Cdd:cd17634 214 RDLIAKASPEHQPEA-MNAEDPLFILYTSGTTGKPKGVLHTTGG---YLVYAATT------------MKYVFDYGPGDIY 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1359 L-----------------PLIKGAHCYI-------------CQTehtkdVEKLKRDIRTIKPTVMQA-TPATWKMLfysG 1407
Cdd:cd17634 278 WctadvgwvtghsyllygPLACGATTLLyegvpnwptparmWQV-----VDKHGVNILYTAPTAIRAlMAAGDDAI---E 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1408 WENEENVKILCG-GEAL-PETLKRYFLDTGSEAW---NMFGPTETTiWSAVQ--RINDECSRATIGRPIANTQIYITDSQ 1480
Cdd:cd17634 350 GTDRSSLRILGSvGEPInPEAYEWYWKKIGKEKCpvvDTWWQTETG-GFMITplPGAIELKAGSATRPVFGVQPAVVDNE 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1481 LAPVPAGVPGELCIAGD--GVAKGYYKKEEltdsRFIDNPFEPGSKLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIE 1558
Cdd:cd17634 429 GHPQPGGTEGNLVITDPwpGQTRTLFGDHE----RFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLG 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1559 LGDIESRLSEHPGILECVVVADMDNL-----AAYYTAKHA--NASLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNG 1631
Cdd:cd17634 505 TAEIESVLVAHPKVAEAAVVGIPHAIkgqapYAYVVLNHGvePSPELYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSG 584
|
..
gi 1776025254 1632 KI 1633
Cdd:cd17634 585 KI 586
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
140-551 |
1.49e-28 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 127.67 E-value: 1.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 140 PAVITDRGMHQEMLDWakeqgleGFRAIIVEDLLSAEADTDWHQS--SPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVK 217
Cdd:COG1020 575 RLVLTQSALAARLPEL-------GVPVLALDALALAAEPATNPPVpvTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLA 647
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 218 GIIQMQGFTRED-------ITFN------WMPFdhVGGiGMLHLRDvylgcqeinvssETILMEPLKWLDWIDHYRASVT 284
Cdd:COG1020 648 WMQRRYGLGPGDrvlqfasLSFDasvweiFGAL--LSG-ATLVLAP------------PEARRDPAALAELLARHRVTVL 712
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 285 WAPNFAFGLVTDFAEEikdrkwDLSSMRYMLNGGEAMVAKVGRRILELlephgLPADAIRPAWGMSETSsgvIFSHEFTR 364
Cdd:COG1020 713 NLTPSLLRALLDAAPE------ALPSLRLVLVGGEALPPELVRRWRAR-----LPGARLVNLYGPTETT---VDSTYYEV 778
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 365 AGTSDDDHFVEIGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGYYQRPDLNESVFTEDGWFE-------TGDLG 437
Cdd:COG1020 779 TPPDADGGSVPIGRPIANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFGFpgarlyrTGDLA 858
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 438 -FLRNGRLTITGRTKDAIIINGinyysHAIesaveELSEIET------SYTAACAVRLGQNSTDQLAIFFVTSAKLNDEQ 510
Cdd:COG1020 859 rWLPDGNLEFLGRADDQVKIRG-----FRI-----ELGEIEAallqhpGVREAVVVAREDAPGDKRLVAYVVPEAGAAAA 928
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1776025254 511 MSQLLRNIQSHVSQVigvtPEYLLPVQKEEIPKTAIGKIQR 551
Cdd:COG1020 929 AALLRLALALLLPPY----MVPAAVVLLLPLPLTGNGKLDR 965
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
1157-1633 |
1.58e-28 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 124.54 E-value: 1.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1157 ELFEQQAKKTPDRAAVSYEGQTL--TYRELDERSTQLAIYLQAHGVGP-DRLaGIYVDRSLDMLVGLLAILKAGGAYVPL 1233
Cdd:PRK08315 20 QLLDRTAARYPDREALVYRDQGLrwTYREFNEEVDALAKGLLALGIEKgDRV-GIWAPNVPEWVLTQFATAKIGAILVTI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1234 DPSYPAERLEYMLEDSEV-FITLTTS-------ELVNTL------SWNGV----------TTALLDQD-------WDEIA 1282
Cdd:PRK08315 99 NPAYRLSELEYALNQSGCkALIAADGfkdsdyvAMLYELapelatCEPGQlqsarlpelrRVIFLGDEkhpgmlnFDELL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1283 QTASDrkvltrtVTPENLAY---------VI---YTSGSTGKPKGVMIPHKALTN--FLVsmGETPGLTAEDKM-LAVTT 1347
Cdd:PRK08315 179 ALGRA-------VDDAELAArqatldpddPIniqYTSGTTGFPKGATLTHRNILNngYFI--GEAMKLTEEDRLcIPVPL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1348 Y-CFDI-----AAL----------ELFLPL-----IKGAHC---------YICQTEHtKDVEKLkrDIRTIKPTVMQATP 1397
Cdd:PRK08315 250 YhCFGMvlgnlACVthgatmvypgEGFDPLatlaaVEEERCtalygvptmFIAELDH-PDFARF--DLSSLRTGIMAGSP 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1398 atwkmlfysgweneenvkilCggealP-ETLKRYfldtgSEAWNM------FGPTETTIWSAVQRINDECSR--ATIGRP 1468
Cdd:PRK08315 327 --------------------C-----PiEVMKRV-----IDKMHMsevtiaYGMTETSPVSTQTRTDDPLEKrvTTVGRA 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1469 IANTQIYITDSQL-APVPAGVPGELCIAGDGVAKGYYKKEELTdSRFIDnpfePGSKLyRTGDMARWLPGGRIEYIGRID 1547
Cdd:PRK08315 377 LPHLEVKIVDPETgETVPRGEQGELCTRGYSVMKGYWNDPEKT-AEAID----ADGWM-HTGDLAVMDEEGYVNIVGRIK 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1548 NQVkIRGfrielG------DIESRLSEHPGILECVVVADMDN-----LAAYYTAKhANASLTARELRHFVKNALPAYMVP 1616
Cdd:PRK08315 451 DMI-IRG-----GeniyprEIEEFLYTHPKIQDVQVVGVPDEkygeeVCAWIILR-PGATLTEEDVRDFCRGKIAHYKIP 523
|
570
....*....|....*..
gi 1776025254 1617 SYFIQLDHMPLTPNGKI 1633
Cdd:PRK08315 524 RYIRFVDEFPMTVTGKI 540
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
1152-1640 |
1.67e-28 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 124.60 E-value: 1.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1152 YITFHELFEQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYL--QAHGVGPDRLAgIYVDRSLDMLVGLLAILKAGGA 1229
Cdd:PRK08751 24 FRTVAEVFATSVAKFADRPAYHSFGKTITYREADQLVEQFAAYLlgELQLKKGDRVA-LMMPNCLQYPIATFGVLRAGLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1230 YVPLDPSYPAERLEYMLEDSEV--------FITLTTSELVNTLSWNGVTTALLDQ------------------------- 1276
Cdd:PRK08751 103 VVNVNPLYTPRELKHQLIDSGAsvlvvidnFGTTVQQVIADTPVKQVITTGLGDMlgfpkaalvnfvvkyvkklvpeyri 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1277 ----DWDEIAQTASDRKVLTRTVTPENLAYVIYTSGSTGKPKGVMIPHKALTNFLVSMGE---TPGLTAEDKMLAVTT-- 1347
Cdd:PRK08751 183 ngaiRFREALALGRKHSMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQwlaGTGKLEEGCEVVITAlp 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1348 --YCFDIAALELFLPLIKGAHCYICQTEHTKD-VEKLKRDIRTIKPTV------MQATPATWKMLFYSgweneenVKILC 1418
Cdd:PRK08751 263 lyHIFALTANGLVFMKIGGCNHLISNPRDMPGfVKELKKTRFTAFTGVntlfngLLNTPGFDQIDFSS-------LKMTL 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1419 GG-----EALPETLKRYfldTGSEAWNMFGPTETTIWSAVQRINDECSRATIGRPIANTQIYITDSQLAPVPAGVPGELC 1493
Cdd:PRK08751 336 GGgmavqRSVAERWKQV---TGLTLVEAYGLTETSPAACINPLTLKEYNGSIGLPIPSTDACIKDDAGTVLAIGEIGELC 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1494 IAGDGVAKGYYKKEELTdSRFIDnpfepGSKLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGIL 1573
Cdd:PRK08751 413 IKGPQVMKGYWKRPEET-AKVMD-----ADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVL 486
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1776025254 1574 ECVVVADMDN-----LAAYYTAKHANasLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLKN 1640
Cdd:PRK08751 487 EVAAVGVPDEksgeiVKVVIVKKDPA--LTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRRELRD 556
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
61-554 |
1.68e-28 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.
Pssm-ID: 341279 [Multi-domain] Cd Length: 477 Bit Score: 123.15 E-value: 1.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 61 SYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNSQLLPAFWGCVLTGV--VPAPLAVPPT-----YAESSSGTqklkda 133
Cdd:cd12114 14 TYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAayVPVDIDQPAArreaiLADAGARL------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 134 wtlldkpaVITDrgmhqemLDWAKeQGLEGFRAIIVE-DLLSAEADTDWHQSSPEDLALLLLTSGSTGTPKAVMLNHRNI 212
Cdd:cd12114 88 --------VLTD-------GPDAQ-LDVAVFDVLILDlDALAAPAPPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 213 MSMVKGIIQMQGFTREDITFNWMPFDH------------VGGigmlhlrdvylgcqEINVSSETILMEPLKWLDWIDHYR 280
Cdd:cd12114 152 LNTILDINRRFAVGPDDRVLALSSLSFdlsvydifgalsAGA--------------TLVLPDEARRRDPAHWAELIERHG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 281 ASVtWapNFA---FGLVTDFAEEIKDRkwdLSSMRYMLNGGeamvakvgRRIlellePHGLPAdAIRPAW---------G 348
Cdd:cd12114 218 VTL-W--NSVpalLEMLLDVLEAAQAL---LPSLRLVLLSG--------DWI-----PLDLPA-RLRALApdarlislgG 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 349 MSETSsgvIFS--HEFTRAgtsdDDHFVEI--GSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGYYQRPDLNESV 424
Cdd:cd12114 278 ATEAS---IWSiyHPIDEV----PPDWRSIpyGRPLANQRYRVLDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAAR 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 425 FTEDG----WFETGDLGFLR-NGRLTITGRTKDAIIINGINYYSHAIESAVEELSEIetsyTAACAVRLGQNSTDQLAIF 499
Cdd:cd12114 351 FVTHPdgerLYRTGDLGRYRpDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGV----ARAVVVVLGDPGGKRLAAF 426
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1776025254 500 FVTSAKLN-------DEQMSQLLRN--IQSHVSQVigvtpeyllpvqkEEIPKTAIGKIQRTQL 554
Cdd:cd12114 427 VVPDNDGTpiapdalRAFLAQTLPAymIPSRVIAL-------------EALPLTANGKVDRAAL 477
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
187-555 |
1.90e-28 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 124.09 E-value: 1.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 187 EDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDHvgGIGMLH-LRDVYLgcqeinVSSETI 265
Cdd:PRK06087 187 DELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGH--ATGFLHgVTAPFL------IGARSV 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 266 LME---PLKWLDWIDhyRASVTWAPNfAFGLVTDFAEEIKDRKWDLSSMRYMLNGGEAMVAKVGRRILEllepHGLPADA 342
Cdd:PRK06087 259 LLDiftPDACLALLE--QQRCTCMLG-ATPFIYDLLNLLEKQPADLSALRFFLCGGTTIPKKVARECQQ----RGIKLLS 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 343 IrpaWGMSETSsgvifSHEFTRAGTSDDDHFVEIGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGYYQRPDLNE 422
Cdd:PRK06087 332 V---YGSTESS-----PHAVVNLDDPLSRFMHTDGYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTA 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 423 SVFTEDGWFETGDLGFL-RNGRLTITGRTKDAIIINGINYYSHAIESAVEELSEIETSYTAACA-VRLGQNStdqlaiff 500
Cdd:PRK06087 404 RALDEEGWYYSGDLCRMdEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPdERLGERS-------- 475
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1776025254 501 VTSAKLNDEQMSQLLRNIQSHVSQviGVTPEYLLP---VQKEEIPKTAIGKIQRTQLK 555
Cdd:PRK06087 476 CAYVVLKAPHHSLTLEEVVAFFSR--KRVAKYKYPehiVVIDKLPRTASGKIQKFLLR 531
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
185-555 |
1.94e-28 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 124.34 E-value: 1.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 185 SPEDLALLLLTSGSTGTPKAVMLNHRNIMS-MVKGIIQMQGFTREDITF-NWMPFDHVGGIGMLHLRDVYLGcqeinvsS 262
Cdd:PRK05605 217 TPDDVALILYTSGTTGKPKGAQLTHRNLFAnAAQGKAWVPGLGDGPERVlAALPMFHAYGLTLCLTLAVSIG-------G 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 263 ETIL---------MEPLKwldwidhyRASVTWAPnfafGLVTDF---AEEIKDRKWDLSSMRYMLNGgeAMVAKVgrRIL 330
Cdd:PRK05605 290 ELVLlpapdidliLDAMK--------KHPPTWLP----GVPPLYekiAEAAEERGVDLSGVRNAFSG--AMALPV--STV 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 331 ELLEPH--GLpadaIRPAWGMSETSSgVIFSHEFT---RAGTsdddhfveIGSPIPGFSMRIVNDHN--ELVEEGEIGRF 403
Cdd:PRK05605 354 ELWEKLtgGL----LVEGYGLTETSP-IIVGNPMSddrRPGY--------VGVPFPDTEVRIVDPEDpdETMPDGEEGEL 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 404 QVSGLSVTSGYYQRPDLNESVFtEDGWFETGDLGFL-RNGRLTITGRTKDAIIINGINYYSHAIESAVEELSEIETsyta 482
Cdd:PRK05605 421 LVRGPQVFKGYWNRPEETAKSF-LDGWFRTGDVVVMeEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVED---- 495
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1776025254 483 ACAVRLGQNSTDQ---LAIFFVTSAKLNDEQMSQLLRniqSHVSQvigvtpeYLLP---VQKEEIPKTAIGKIQRTQLK 555
Cdd:PRK05605 496 AAVVGLPREDGSEevvAAVVLEPGAALDPEGLRAYCR---EHLTR-------YKVPrrfYHVDELPRDQLGKVRRREVR 564
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
1152-1641 |
2.60e-28 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 123.78 E-value: 2.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1152 YITFHELFEQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHG--VGPDRLAgIYVDRSLDMLVGLLAILKAGGA 1229
Cdd:PRK12492 23 YKSVVEVFERSCKKFADRPAFSNLGVTLSYAELERHSAAFAAYLQQHTdlVPGDRIA-VQMPNVLQYPIAVFGALRAGLI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1230 YVPLDPSYPAERLEYMLEDS------------------------EVFITLTTSELVNTLSWNGVTTAL-----------L 1274
Cdd:PRK12492 102 VVNTNPLYTAREMRHQFKDSgaralvylnmfgklvqevlpdtgiEYLIEAKMGDLLPAAKGWLVNTVVdkvkkmvpayhL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1275 DQ--DWDEIAQTASDRKVLTRTVTPENLAYVIYTSGSTGKPKGVMIPHKAL-TNFLVSMGETPGLTAEDKMLAVTTYCFD 1351
Cdd:PRK12492 182 PQavPFKQALRQGRGLSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLvANMLQVRACLSQLGPDGQPLMKEGQEVM 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1352 IAALELFLPLIKGAHCYICQTEHTKDVekLKRDIRTIKPTVMQAtpATWKM--------LFYSGWENEE-------NVKI 1416
Cdd:PRK12492 262 IAPLPLYHIYAFTANCMCMMVSGNHNV--LITNPRDIPGFIKEL--GKWRFsallglntLFVALMDHPGfkdldfsALKL 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1417 L-CGGEALPE-TLKRYFLDTGSEAWNMFGPTETtiwSAVQRINDECSRA---TIGRPIANTQIYITDSQLAPVPAGVPGE 1491
Cdd:PRK12492 338 TnSGGTALVKaTAERWEQLTGCTIVEGYGLTET---SPVASTNPYGELArlgTVGIPVPGTALKVIDDDGNELPLGERGE 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1492 LCIAGDGVAKGYYKKEELTdSRFIDnpfepGSKLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPG 1571
Cdd:PRK12492 415 LCIKGPQVMKGYWQQPEAT-AEALD-----AEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPK 488
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1776025254 1572 ILECVVVADMDNLAA-----YYTAKhaNASLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLKNI 1641
Cdd:PRK12492 489 VANCAAIGVPDERSGeavklFVVAR--DPGLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELRDI 561
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
50-554 |
2.78e-28 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 122.66 E-value: 2.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 50 YLQPD-----GTEVYQSYRRLWDDGLRIVKGLRQS-GLKAKQSVILQLGDNSQLLPAFWGCVLTGVVPAPLAVPPTYAE- 122
Cdd:PRK06839 13 YLHPDriaiiTEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENEl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 123 ----SSSGTQKLKDAWTLLDKPAVITDRGMHQEMLDWAKEQGLEGFRAIIVEDllsaeadtdwhqSSPEDLALLLLTSGS 198
Cdd:PRK06839 93 ifqlKDSGTTVLFVEKTFQNMALSMQKVSYVQRVISITSLKEIEDRKIDNFVE------------KNESASFIICYTSGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 199 TGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDHVGGIGMLHLRDVYLGCQEInVSSEtilMEPLKWLDWIDH 278
Cdd:PRK06839 161 TGKPKGAVLTQENMFWNALNNTFAIDLTMHDRSIVLLPLFHIGGIGLFAFPTLFAGGVII-VPRK---FEPTKALSMIEK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 279 YRASVTwapnfaFGLVT---DFAEEIKDRKWDLSSMRYMLNGGEAMVAKVGRRILELLEPHGlpadairPAWGMSETSSG 355
Cdd:PRK06839 237 HKVTVV------MGVPTihqALINCSKFETTNLQSVRWFYNGGAPCPEELMREFIDRGFLFG-------QGFGMTETSPT 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 356 V--IFSHEFTRAGTSdddhfveIGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGYYQRPDLNESVFtEDGWFET 433
Cdd:PRK06839 304 VfmLSEEDARRKVGS-------IGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETI-QDGWLCT 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 434 GDLG-FLRNGRLTITGRTKDAIIINGINYYSHAIESAVEELSEI-ETSYTAACAVRLGQnsTDQLAIFFVTSAKLNDEQm 511
Cdd:PRK06839 376 GDLArVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVyEVAVVGRQHVKWGE--IPIAFIVKKSSSVLIEKD- 452
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1776025254 512 sqllrnIQSHVSQVIGvtpEYLLP---VQKEEIPKTAIGKIQRTQL 554
Cdd:PRK06839 453 ------VIEHCRLFLA---KYKIPkeiVFLKELPKNATGKIQKAQL 489
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
185-555 |
3.48e-28 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 123.33 E-value: 3.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 185 SPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTRED---ITFNWMPFDHVGGIGMLHLRDVYLGCQEINVS 261
Cdd:PRK05677 205 QADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCRALMGSNLNEgceILIAPLPLYHIYAFTFHCMAMMLIGNHNILIS 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 262 S----ETILMEPLKWldwidHYRASVtwapnfafGLVTDFAEEIKD---RKWDLSSMRYMLNGGEAMVAKVGRRILELLe 334
Cdd:PRK05677 285 NprdlPAMVKELGKW-----KFSGFV--------GLNTLFVALCNNeafRKLDFSALKLTLSGGMALQLATAERWKEVT- 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 335 phGLPadaIRPAWGMSETSSGVIFS-HEFTRAGTsdddhfveIGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSG 413
Cdd:PRK05677 351 --GCA---ICEGYGMTETSPVVSVNpSQAIQVGT--------IGIPVPSTLCKVIDDDGNELPLGEVGELCVKGPQVMKG 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 414 YYQRPDLNESVFTEDGWFETGDLGFLR-NGRLTITGRTKDAIIINGINYYSHAIESAVEELSEIETsyTAACAVRlGQNS 492
Cdd:PRK05677 418 YWQRPEATDEILDSDGWLKTGDIALIQeDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQ--CAAIGVP-DEKS 494
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1776025254 493 TDQLAIFFV--TSAKLNDEQMSQLLRniqshvSQVIGvtpeYLLPVQ---KEEIPKTAIGKIQRTQLK 555
Cdd:PRK05677 495 GEAIKVFVVvkPGETLTKEQVMEHMR------ANLTG----YKVPKAvefRDELPTTNVGKILRRELR 552
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
1158-1639 |
5.86e-28 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 121.91 E-value: 5.86e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1158 LFEQQAKKTPDRAAVSYE---GQTLTYRELDERSTQLAIYLQAHGVGP-DRLAgIYVDRSLDMLVGLLAILKAGGAYVPL 1233
Cdd:PRK07514 5 LFDALRAAFADRDAPFIEtpdGLRYTYGDLDAASARLANLLVALGVKPgDRVA-VQVEKSPEALALYLATLRAGAVFLPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1234 DPSYPAERLEYMLEDSE--VFIT-----LTTSELVNTLSWNGVTTalLDQDWD----EIAQTASDRKVlTRTVTPENLAY 1302
Cdd:PRK07514 84 NTAYTLAELDYFIGDAEpaLVVCdpanfAWLSKIAAAAGAPHVET--LDADGTgsllEAAAAAPDDFE-TVPRGADDLAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1303 VIYTSGSTGKPKGVMIPHKALTNFLVSMGETPGLTAEDKMlavttycfdIAALELF----------LPLIKGAHCYICQT 1372
Cdd:PRK07514 161 ILYTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVL---------IHALPIFhthglfvatnVALLAGASMIFLPK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1373 EHTKDV-EKLKRdirtikPTVMQATPATWKMLFYSGWENEE---NVKILCGGEA--LPETLKRYFLDTGSEAWNMFGPTE 1446
Cdd:PRK07514 232 FDPDAVlALMPR------ATVMMGVPTFYTRLLQEPRLTREaaaHMRLFISGSAplLAETHREFQERTGHAILERYGMTE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1447 TTIWSAvqriN--DECSRA-TIGRPIANTQIYITDSQL-APVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPFepg 1522
Cdd:PRK07514 306 TNMNTS----NpyDGERRAgTVGFPLPGVSLRVTDPETgAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGF--- 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1523 sklYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVV----ADMDNLAAYYTAKHANASLT 1598
Cdd:PRK07514 379 ---FITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIgvphPDFGEGVTAVVVPKPGAALD 455
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1776025254 1599 ARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLK 1639
Cdd:PRK07514 456 EAAILAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLLR 496
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
133-556 |
5.91e-28 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 121.61 E-value: 5.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 133 AWTLLDKPA--VITDRGMHQEmldwakeqgLEGFRAIIVEDLL-SAEADTDWHQSSPED-LALLLLTSGSTGTPKAVMLN 208
Cdd:PRK03640 92 LWQLDDAEVkcLITDDDFEAK---------LIPGISVKFAELMnGPKEEAEIQEEFDLDeVATIMYTSGTTGKPKGVIQT 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 209 HRN-IMSMVKGIIQMqGFTREDitfNW---MPFDHVGGIGMLhLRDVYLGCQeinvsseTILME---PLKWLDWIDHYR- 280
Cdd:PRK03640 163 YGNhWWSAVGSALNL-GLTEDD---CWlaaVPIFHISGLSIL-MRSVIYGMR-------VVLVEkfdAEKINKLLQTGGv 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 281 --ASVTWApnfafgLVTDFAEEIKDRKWDlSSMRYMLNGGeamvAKVGRRILELLEPHGLPadaIRPAWGMSETSSGVif 358
Cdd:PRK03640 231 tiISVVST------MLQRLLERLGEGTYP-SSFRCMLLGG----GPAPKPLLEQCKEKGIP---VYQSYGMTETASQI-- 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 359 sheftrAGTSDDDHFVEIGS---PIPGFSMRIVNDHNEL--VEEGEIgrfQVSGLSVTSGYYQRPDLNESVFtEDGWFET 433
Cdd:PRK03640 295 ------VTLSPEDALTKLGSagkPLFPCELKIEKDGVVVppFEEGEI---VVKGPNVTKGYLNREDATRETF-QDGWFKT 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 434 GDLGFL-RNGRLTITGRTKDAIIINGINYYSHAIESAVEELSEIETsytaacAVRLGqnSTDQL-----AIFFVTSAKLN 507
Cdd:PRK03640 365 GDIGYLdEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAE------AGVVG--VPDDKwgqvpVAFVVKSGEVT 436
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1776025254 508 DEQMSQLLRNIQSHvsqvigvtpeYLLPVQ---KEEIPKTAIGKIQRTQLKT 556
Cdd:PRK03640 437 EEELRHFCEEKLAK----------YKVPKRfyfVEELPRNASGKLLRHELKQ 478
|
|
| PLN02836 |
PLN02836 |
3-oxoacyl-[acyl-carrier-protein] synthase |
1914-2183 |
7.92e-28 |
|
3-oxoacyl-[acyl-carrier-protein] synthase
Pssm-ID: 215449 [Multi-domain] Cd Length: 437 Bit Score: 120.28 E-value: 7.92e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1914 ISHKLGLRGPSYFVHANCSSsliGLHS---AYKSLLSAESDYALVGGatlhTESNI------GYVHQPGL----NFSSDG 1980
Cdd:PLN02836 167 VSIRYGFQGPNHAAVTACAT---GAHSigdAFRMIQFGDADVMVAGG----TESSIdalsiaGFSRSRALstkfNSCPTE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1981 HIKAFDASADGMIGGEGVAVVLLKKAADAVKDGDHIYALLRGIGVNNDGADkvgFYAPSVKGQADV--VQQVMNQTKIHP 2058
Cdd:PLN02836 240 ASRPFDCDRDGFVIGEGAGVLVLEELEHAKRRGAKIYAEVRGYGMSGDAHH---ITQPHEDGRGAVlaMTRALQQSGLHP 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2059 ESICYVEAHGTGTKLGDPIELAALTNVYRQYTNkTQFCGIGSVKTNIGHLDTAAGLAGCIKVVMSLYHQELAPSINYKEP 2138
Cdd:PLN02836 317 NQVDYVNAHATSTPLGDAVEARAIKTVFSEHAT-SGGLAFSSTKGATGHLLGAAGAVEAIFSVLAIHHGIAPPTLNLERP 395
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1776025254 2139 NPNTDLASSPFyvvdqkkTLSREIQThRAALS-SFGLGGTNTHAIF 2183
Cdd:PLN02836 396 DPIFDDGFVPL-------TASKAMLI-RAALSnSFGFGGTNASLLF 433
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
186-1002 |
9.00e-28 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 125.45 E-value: 9.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 186 PEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDHVGGIGMLHLrdVYLGCQEINVSSETI 265
Cdd:PRK12316 654 PENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFW--PLMSGARLVVAAPGD 731
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 266 LMEPLKWLDWIDHYRASVTwapNFAFGLVTDFAEEIKDRkwDLSSMRYMLNGGEAMVAKVGRRILELLephglPADAIRP 345
Cdd:PRK12316 732 HRDPAKLVELINREGVDTL---HFVPSMLQAFLQDEDVA--SCTSLRRIVCSGEALPADAQEQVFAKL-----PQAGLYN 801
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 346 AWGMSETSSGVIFSHEFTRAGTSdddhfVEIGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGYYQRPDLNESVF 425
Cdd:PRK12316 802 LYGPTEAAIDVTHWTCVEEGGDS-----VPIGRPIANLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERF 876
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 426 TEDGW------FETGDLGFLR-NGRLTITGRTKDAIIINGINYyshaiesaveELSEIETSYTAACAVR----LGQnSTD 494
Cdd:PRK12316 877 VPSPFvagermYRTGDLARYRaDGVIEYAGRIDHQVKLRGLRI----------ELGEIEARLLEHPWVReaavLAV-DGK 945
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 495 QLAIFFVTSAKLNDeqmsqLLRNIQSHVSQVIgvtPEYLLPVQ---KEEIPKTAIGKIQRTQLKtsfengefdhllhKPn 571
Cdd:PRK12316 946 QLVGYVVLESEGGD-----WREALKAHLAASL---PEYMVPAQwlaLERLPLTPNGKLDRKALP-------------AP- 1003
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 572 rmndavqDEEMQQADHVKRvREEIQEHLLTCLTEELHVSRdwVEPNANIQSLGVNSIKMMKLIrSIEKNYHIKLTAREIH 651
Cdd:PRK12316 1004 -------EASVAQQGYVAP-RNALERTLAAIWQDVLGVER--VGLDDNFFELGGDSIVSIQVV-SRARQAGIQLSPRDLF 1072
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 652 QYPTIERLAsylsehedlssSSADKKGTDTYKTEPERSQAtfqPLSEVQKglWTLQKMSPEKSAYHVPLCFKFSSGLHLE 731
Cdd:PRK12316 1073 QHQTIRSLA-----------LVAKAGQATAADQGPASGEV---ALAPVQR--WFFEQAIPQRQHWNQSLLLQARQPLDPD 1136
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 732 TLQQAFGLVLNQHPILKHVIQEKDGvpilKNEPALSIEIKTENI---SSMKESDIPAfLRKKVKEPYVKENSPLVRVMSF 808
Cdd:PRK12316 1137 RLGRALERLVAHHDALRLRFREEDG----GWQQAYAAPQAGEVLwqrQAASEEELLA-LCEEAQRSLDLEQGPLLRALLV 1211
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 809 SRSEQEHFLLVVIHHLIFDGVSSVTFIHSLFDTYQLLLkgqqpeiAVSPAIYHDFAAWEKNM--LAGKDGvKHRTYWQKQ 886
Cdd:PRK12316 1212 DMADGSQRLLLVIHHLVVDGVSWRILLEDLQRAYADLD-------ADLPARTSSYQAWARRLheHAGARA-EELDYWQAQ 1283
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 887 LSGTlpNLQLPKVSASSVSEFR-EDTYTRRLSSGFMNQVRMFA-KEHSVNVTTVFLSCYMMLLGRYTGQKEQIVGMPAMV 964
Cdd:PRK12316 1284 LEDA--PHELPCENPDGALENRhERKLELRLDAERTRQLLQEApAAYRTQVNDLLLTALARVTCRWSGQASVLVQLEGHG 1361
|
810 820 830 840
....*....|....*....|....*....|....*....|....*
gi 1776025254 965 RpEERFDD-----AIGHFLNMLPIRseLNPADTFSSFIS--KLQL 1002
Cdd:PRK12316 1362 R-EDLFEDidlsrTVGWFTSLFPVR--LTPAADLGESIKaiKEQL 1403
|
|
| PRK07103 |
PRK07103 |
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated |
1914-2179 |
9.10e-28 |
|
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
Pssm-ID: 180839 [Multi-domain] Cd Length: 410 Bit Score: 119.75 E-value: 9.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1914 ISHKLGLRGPSYFVHANCSSSLIGLHSAYKSLLSAESDYALVGGATLHtesnIGYVHQPGL---------NFSSDGHI-- 1982
Cdd:PRK07103 150 CSEQFGIRGEGFTVGGASASGQLAVIQAARLVQSGSVDACIAVGALMD----LSYWECQALrslgamgsdRFADEPEAac 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1983 KAFDASADGMIGGEGVAVVLLKKAADAVKDGDHIYALLRGIGVNNDGADKVgfyAPSVKGQADVVQQVMNQTKIHPESIC 2062
Cdd:PRK07103 226 RPFDQDRDGFIYGEACGAVVLESAESARRRGARPYAKLLGWSMRLDANRGP---DPSLEGEMRVIRAALRRAGLGPEDID 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2063 YVEAHGTGTKLGDPIELAALTNVY--RQYTNKTqfcgigsvKTNIGHLDTAAGLAGCIKVVMSLYHQELAPSINYKEPNP 2140
Cdd:PRK07103 303 YVNPHGTGSPLGDETELAALFASGlaHAWINAT--------KSLTGHGLSAAGIVELIATLLQMRAGFLHPSRNLDEPID 374
|
250 260 270
....*....|....*....|....*....|....*....
gi 1776025254 2141 NTdlasspFYVVDQKktlSREIQTHRAALSSFGLGGTNT 2179
Cdd:PRK07103 375 ER------FRWVGST---AESARIRYALSLSFGFGGINT 404
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
184-560 |
9.91e-28 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 120.73 E-value: 9.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 184 SSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMP--FDhvggigmLHLRDVYL-----GCq 256
Cdd:cd05918 103 SSPSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGLTSESRVLQFASytFD-------VSILEIFTtlaagGC- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 257 eINVSSETILMEPLkwLDWIDHYRasVTWA---PNFAFGLvtdfaeeikDRKwDLSSMRYMLNGGEAMVAKVgrrilelL 333
Cdd:cd05918 175 -LCIPSEEDRLNDL--AGFINRLR--VTWAfltPSVARLL---------DPE-DVPSLRTLVLGGEALTQSD-------V 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 334 EPHGLPADAIRpAWGMSETSsgvIFShefTRAGTSDDDHFVEIGSPIPGfSMRIVN--DHNELVEEGEIGRFQVSGLSVT 411
Cdd:cd05918 233 DTWADRVRLIN-AYGPAECT---IAA---TVSPVVPSTDPRNIGRPLGA-TCWVVDpdNHDRLVPIGAVGELLIEGPILA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 412 SGYYQRPDLNESVFTED-GW------------FETGDLG-FLRNGRLTITGRTKDAIIINGINYYSHAIESAVEELSEIE 477
Cdd:cd05918 305 RGYLNDPEKTAAAFIEDpAWlkqegsgrgrrlYRTGDLVrYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGA 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 478 TSYTAACAVRLGQNSTDQLAIFFVTS------------AKLNDEQMSQLLRNIQSHVSQVIgvtPEY-----LLPVQkeE 540
Cdd:cd05918 385 KEVVVEVVKPKDGSSSPQLVAFVVLDgsssgsgdgdslFLEPSDEFRALVAELRSKLRQRL---PSYmvpsvFLPLS--H 459
|
410 420
....*....|....*....|
gi 1776025254 541 IPKTAIGKIQRTQLKTSFEN 560
Cdd:cd05918 460 LPLTASGKIDRRALRELAES 479
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
1855-2182 |
1.32e-27 |
|
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) Claisen-like condensation reaction. Members are share strong structural similarity, and are involved in the synthesis and degradation of fatty acids, and the production of polyketides, a diverse group of natural products.
Pssm-ID: 238201 [Multi-domain] Cd Length: 254 Bit Score: 115.23 E-value: 1.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1855 KAIEDAGYAAGQIPQTSVfmsasnnsyrallpsdttesletpdGYVSWVLAQSGTIPTMISHKLGLRGPSYFVHANCSSS 1934
Cdd:cd00327 17 QAIADAGLSKGPIVGVIV-------------------------GTTGGSGEFSGAAGQLAYHLGISGGPAYSVNQACATG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1935 LIGLHSAYKSLLSAESDYALVGGatlhtesnigyvhqpglnfssdghikaFDASadgmIGGEGVAVVLLKKAADAVKDGD 2014
Cdd:cd00327 72 LTALALAVQQVQNGKADIVLAGG---------------------------SEEF----VFGDGAAAAVVESEEHALRRGA 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2015 HIYALLRGIGVNNDGADKVgfYAPSVKGQADVVQQVMNQTKIHPESICYVEAHGTGTKLGDPIELAALTNVYRQytnktQ 2094
Cdd:cd00327 121 HPQAEIVSTAATFDGASMV--PAVSGEGLARAARKALEGAGLTPSDIDYVEAHGTGTPIGDAVELALGLDPDGV-----R 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2095 FCGIGSVKTNIGHLDTAAGLAGCIKVVMSLYHQElapsinykepnpntdlasspfyvvdqKKTLSREIQThrAALSSFGL 2174
Cdd:cd00327 194 SPAVSATLIMTGHPLGAAGLAILDELLLMLEHEF--------------------------IPPTPREPRT--VLLLGFGL 245
|
....*...
gi 1776025254 2175 GGTNTHAI 2182
Cdd:cd00327 246 GGTNAAVV 253
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
1118-1638 |
1.47e-27 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 120.87 E-value: 1.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1118 MLNPSQPLKEYSLLPEAEKqmilktwnatGKTYPYItfheLFEQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQA 1197
Cdd:PRK13383 14 LLNPPSPRAVLRLLREASR----------GGTNPYT----LLAVTAARWPGRTAIIDDDGALSYRELQRATESLARRLTR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1198 HGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLEDSEVFITLTTSELVNTLSWNGVTTALLDqd 1277
Cdd:PRK13383 80 DGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAALRAHHISTVVADNEFAERIAGADDAVAVID-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1278 wdeiAQTASDRKVLTRTVTPENLAYVIYTSGSTGKPKGVmiPHK----ALTNFLVSMGETPGLTAEDKMLAVTTYCFDIA 1353
Cdd:PRK13383 158 ----PATAGAEESGGRPAVAAPGRIVLLTSGTTGKPKGV--PRApqlrSAVGVWVTILDRTRLRTGSRISVAMPMFHGLG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1354 ALELFLPLIKG----------AHCYICQTE-HTKD----VEKLKRDIRTIKPTVMQATPATWKMLfysgweneenvkILC 1418
Cdd:PRK13383 232 LGMLMLTIALGgtvlthrhfdAEAALAQASlHRADaftaVPVVLARILELPPRVRARNPLPQLRV------------VMS 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1419 GGEALPETLKRYFLDT-GSEAWNMFGPTETTIWSAVQRINDECSRATIGRPIANTQIYITDSQLAPVPAGVPGELCIAGd 1497
Cdd:PRK13383 300 SGDRLDPTLGQRFMDTyGDILYNGYGSTEVGIGALATPADLRDAPETVGKPVAGCPVRILDRNNRPVGPRVTGRIFVGG- 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1498 gvakgyykkeELTDSRFIDNpfepGSK-----LYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGI 1572
Cdd:PRK13383 379 ----------ELAGTRYTDG----GGKavvdgMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAV 444
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1776025254 1573 LECVVVADMDN-----LAAYYTAkHANASLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSL 1638
Cdd:PRK13383 445 ADNAVIGVPDErfghrLAAFVVL-HPGSGVDAAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| PRK07103 |
PRK07103 |
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated |
3340-3777 |
2.45e-27 |
|
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
Pssm-ID: 180839 [Multi-domain] Cd Length: 410 Bit Score: 118.21 E-value: 2.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3340 PVAIVGISGRFPGAMDIDEFWKNLEEGKDSITEVpkdrwdwrEHYGNPD---TDVNKTDIKWGGFIDGVAEFDPLFFGIS 3416
Cdd:PRK07103 3 EVVVTGVGVVSAIGQGRPSFAAALLAGRHAFGVM--------RRPGRQVpddAGAGLASAFIGAELDSLALPERLDAKLL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3417 pREADYvdPQQRLLMTyVWKALEDAGCPPqsLSGTGTGIFIGTGNTGYKDLF--HRANlpiEGHAAtgHMIPSVGPNRM- 3493
Cdd:PRK07103 75 -RRASL--SAQAALAA-AREAWRDAALGP--VDPDRIGLVVGGSNLQQREQAlvHETY---RDRPA--FLRPSYGLSFMd 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3494 -------SYFLNIHGPSEPVETACSSSLVAIHRAVTAMQNGDCEMAIAGGVNTILTEEAHISYSKAGMLSKDGR------ 3560
Cdd:PRK07103 144 tdlvglcSEQFGIRGEGFTVGGASASGQLAVIQAARLVQSGSVDACIAVGALMDLSYWECQALRSLGAMGSDRFadepea 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3561 -CKTFSADANGYVRGEGVGMVMLKKLEDAERDGNHIYGVIRGTAENHGgrANTLTSPNPKAQADLLVRAYRQAGIDPSTV 3639
Cdd:PRK07103 224 aCRPFDQDRDGFIYGEACGAVVLESAESARRRGARPYAKLLGWSMRLD--ANRGPDPSLEGEMRVIRAALRRAGLGPEDI 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3640 TYIEAHGTGTELGDPIEINGLKAAfkelsnmrGESQPdvpdhrcGIGSVKSNIGHLELAAGISGLIKVLLQMKHktlvKS 3719
Cdd:PRK07103 302 DYVNPHGTGSPLGDETELAALFAS--------GLAHA-------WINATKSLTGHGLSAAGIVELIATLLQMRA----GF 362
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1776025254 3720 LHcetlnPYLQLT---DSPFYIVQEKQEWKSVtdcdgnelpRRAGISSFGIGGVNAHIVIE 3777
Cdd:PRK07103 363 LH-----PSRNLDepiDERFRWVGSTAESARI---------RYALSLSFGFGGINTALVLE 409
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
32-554 |
2.50e-27 |
|
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341301 [Multi-domain] Cd Length: 488 Bit Score: 119.69 E-value: 2.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 32 PEVLYRTAAELGDTKGIIYlqpDGTEVyqSYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNSQLLPAFWGCVLTGVVP 111
Cdd:cd17646 1 HALVAEQAARTPDAPAVVD---EGRTL--TYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 112 APLavPPTYAEsssgtQKLkdAWTLLDKPA--VITDRGMhqemLDWAkeqGLEGFRAIIVEDLLSAEADTD-WHQSSPED 188
Cdd:cd17646 76 LPL--DPGYPA-----DRL--AYMLADAGPavVLTTADL----AARL---PAGGDVALLGDEALAAPPATPpLVPPRPDN 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 189 LALLLLTSGSTGTPKAVMLNHRNImsmVKGIIQMQ---GFTRED-------ITFN------WMPFDHVGGIGM----LHl 248
Cdd:cd17646 140 LAYVIYTSGSTGRPKGVMVTHAGI---VNRLLWMQdeyPLGPGDrvlqktpLSFDvsvwelFWPLVAGARLVVarpgGH- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 249 RDV-YLgcqeinvssetilmeplkwLDWIDHYRASVTwapNFAFGLVTDFAEEIKDRKWDlsSMRYMLNGGEAMVAKVGR 327
Cdd:cd17646 216 RDPaYL-------------------AALIREHGVTTC---HFVPSMLRVFLAEPAAGSCA--SLRRVFCSGEALPPELAA 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 328 RILELL--EPHGLpadairpaWGMSETSSGVifSHEFTRAGTsdDDHFVEIGSPIPGFSMRIVNDHNELVEEGEIGRFQV 405
Cdd:cd17646 272 RFLALPgaELHNL--------YGPTEAAIDV--THWPVRGPA--ETPSVPIGRPVPNTRLYVLDDALRPVPVGVPGELYL 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 406 SGLSVTSGYYQRPDLNESVFTEDgWFE-------TGDLG-FLRNGRLTITGRTKDAIIINGinyysHAIesaveELSEIE 477
Cdd:cd17646 340 GGVQLARGYLGRPALTAERFVPD-PFGpgsrmyrTGDLArWRPDGALEFLGRSDDQVKIRG-----FRV-----EPGEIE 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 478 TSYTA------ACAVRLGQNSTDQLAIFFVTSAKLNDEQMSQLLRniqSHVSQVIgvtPEYLLP---VQKEEIPKTAIGK 548
Cdd:cd17646 409 AALAAhpavthAVVVARAAPAGAARLVGYVVPAAGAAGPDTAALR---AHLAERL---PEYMVPaafVVLDALPLTANGK 482
|
....*.
gi 1776025254 549 IQRTQL 554
Cdd:cd17646 483 LDRAAL 488
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
156-449 |
2.82e-27 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 123.11 E-value: 2.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 156 AKEQGLEGFRAIIVEDLLSAEADTDW--HQSSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFN 233
Cdd:PRK08633 749 AKISKVDKLTALLAARLLPARLLKRLygPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILS 828
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 234 WMPFDHVGGIGMLHLRDVYLGCQEINVSSETilmEPLKWLDWIDHYRASVTWA-PNFaFGLvtdFAEEIKDRKWDLSSMR 312
Cdd:PRK08633 829 SLPFFHSFGLTVTLWLPLLEGIKVVYHPDPT---DALGIAKLVAKHRATILLGtPTF-LRL---YLRNKKLHPLMFASLR 901
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 313 YMLNGGE--------AMVAKVGRRILEllephglpadairpAWGMSETS-----------SGVIFSHEFTRAGTsdddhf 373
Cdd:PRK08633 902 LVVAGAEklkpevadAFEEKFGIRILE--------------GYGATETSpvasvnlpdvlAADFKRQTGSKEGS------ 961
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 374 veIGSPIPGFSMRIVN-DHNELVEEGEIGRFQVSGLSVTSGYYQRPDLNESVFTE---DGWFETGDLGFL-RNGRLTITG 448
Cdd:PRK08633 962 --VGMPLPGVAVRIVDpETFEELPPGEDGLILIGGPQVMKGYLGDPEKTAEVIKDidgIGWYVTGDKGHLdEDGFLTITD 1039
|
.
gi 1776025254 449 R 449
Cdd:PRK08633 1040 R 1040
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
1291-1641 |
3.75e-27 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 122.73 E-value: 3.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1291 LTRTVTPENLAYVIYTSGSTGKPKGVMIPHKALTNFLVSMGETPGLTAEDKMLAVTT--YCFDIAAlELFLPLIKGAHCy 1368
Cdd:PRK08633 775 YGPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLPffHSFGLTV-TLWLPLLEGIKV- 852
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1369 ICQTEHTkDVEKLKRDIRTIKPTVMQATPaTWKMLFysgwenEENVKI-----------LCGGEALPETLKRYFLDT-GS 1436
Cdd:PRK08633 853 VYHPDPT-DALGIAKLVAKHRATILLGTP-TFLRLY------LRNKKLhplmfaslrlvVAGAEKLKPEVADAFEEKfGI 924
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1437 EAWNMFGPTETTIWSAVQ----RINDE-----CSRATIGRPIANTQIYITD-SQLAPVPAGVPGELCIAGDGVAKGYYKK 1506
Cdd:PRK08633 925 RILEGYGATETSPVASVNlpdvLAADFkrqtgSKEGSVGMPLPGVAVRIVDpETFEELPPGEDGLILIGGPQVMKGYLGD 1004
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1507 EELTDS--RFIDnpfepGSKLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSE--HPGILECVVVADMD 1582
Cdd:PRK08633 1005 PEKTAEviKDID-----GIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKalGGEEVVFAVTAVPD 1079
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1776025254 1583 nlaayytAK--------HANASLTARELRHFVKNA-LPAYMVPSYFIQLDHMPLTPNGKIDRNSLKNI 1641
Cdd:PRK08633 1080 -------EKkgeklvvlHTCGAEDVEELKRAIKESgLPNLWKPSRYFKVEALPLLGSGKLDLKGLKEL 1140
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
50-555 |
4.01e-27 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 118.33 E-value: 4.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 50 YLQPDGTevyQSYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNSQLLPAFWGCVLTGVVPA---PLAVPPTYAESSSG 126
Cdd:cd05919 4 FYAADRS---VTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVvinPLLHPDDYAYIARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 127 TQKlkdawtlldkpavitdrgmhqemldwakeqglegfRAIIVEDllsaeadtdwhqsspEDLALLLLTSGSTGTPKAVM 206
Cdd:cd05919 81 CEA-----------------------------------RLVVTSA---------------DDIAYLLYSSGTTGPPKGVM 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 207 LNHRNIMSMVKGI-IQMQGFTREDITFNW--MPFdhvgGIGMLHlrDVYLGCQeinVSSETILMEplkwlDWIDHYRASV 283
Cdd:cd05919 111 HAHRDPLLFADAMaREALGLTPGDRVFSSakMFF----GYGLGN--SLWFPLA---VGASAVLNP-----GWPTAERVLA 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 284 TWA---PNFAFGLVTDFAEEIKDRKW---DLSSMRYMLNGGEAMVAKVGRRileLLEPHGLP-ADAIrpawGMSETssGV 356
Cdd:cd05919 177 TLArfrPTVLYGVPTFYANLLDSCAGspdALRSLRLCVSAGEALPRGLGER---WMEHFGGPiLDGI----GATEV--GH 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 357 IF---SHEFTRAGTSdddhfveiGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGYYQRPDLNESVFtEDGWFET 433
Cdd:cd05919 248 IFlsnRPGAWRLGST--------GRPVPGYEIRLVDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATF-NGGWYRT 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 434 GDL-GFLRNGRLTITGRTKDAIIINGINYYSHAIESAVeelseIETSYTAACAVRLGQNSTD--QLAIFFVtsakLNDEQ 510
Cdd:cd05919 319 GDKfCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLI-----IQHPAVAEAAVVAVPESTGlsRLTAFVV----LKSPA 389
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1776025254 511 MSQ--LLRNIQSHVSQVIgvtPEYLLPVQ---KEEIPKTAIGKIQRTQLK 555
Cdd:cd05919 390 APQesLARDIHRHLLERL---SAHKVPRRiafVDELPRTATGKLQRFKLR 436
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
1163-1642 |
4.59e-27 |
|
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.
Pssm-ID: 341274 [Multi-domain] Cd Length: 537 Bit Score: 119.52 E-value: 4.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1163 AKKTPDRAAVSY-----EGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSY 1237
Cdd:cd05970 27 AKEYPDKLALVWcddagEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1238 PAERLEYMLEDSEVFITLTTSE---------------LVNTLSWNG--VTTALLDQDwDEIAQTASDRKVLTRTVTP--E 1298
Cdd:cd05970 107 TAKDIVYRIESADIKMIVAIAEdnipeeiekaapecpSKPKLVWVGdpVPEGWIDFR-KLIKNASPDFERPTANSYPcgE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1299 NLAYVIYTSGSTGKPKgvMIPHkaltNFLVSMGETpgLTAE--------DKMLAVTTYCFDIAAL-ELFLPLIKGAHCYI 1369
Cdd:cd05970 186 DILLVYFSSGTTGMPK--MVEH----DFTYPLGHI--VTAKywqnvregGLHLTVADTGWGKAVWgKIYGQWIAGAAVFV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1370 cqTEHTK-DVEKLKRDIRTIKPTVMQATPATWKMLFYSGWENEENVKI---LCGGEAL-PETLKRYFLDTGSEAWNMFGP 1444
Cdd:cd05970 258 --YDYDKfDPKALLEKLSKYGVTTFCAPPTIYRFLIREDLSRYDLSSLrycTTAGEALnPEVFNTFKEKTGIKLMEGFGQ 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1445 TETTIWSAVQRINdECSRATIGRPIANTQIYITDSQLAPVPAGVPGELCIAGD-----GVAKGYYKKEELTDSRFIDNpf 1519
Cdd:cd05970 336 TETTLTIATFPWM-EPKPGSMGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTSkgkpvGLFGGYYKDAEKTAEVWHDG-- 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1520 epgskLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMDN-----------LAAYY 1588
Cdd:cd05970 413 -----YYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPirgqvvkativLAKGY 487
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1776025254 1589 TAKHAnasLTaRELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLKNID 1642
Cdd:cd05970 488 EPSEE---LK-KELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEIRERD 537
|
|
| PRK06333 |
PRK06333 |
beta-ketoacyl-ACP synthase; |
1778-2187 |
5.60e-27 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235781 [Multi-domain] Cd Length: 424 Bit Score: 117.41 E-value: 5.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1778 DEFWENLRDGKESIAFfnkeelqrfgISKEIAEN-----ADYVPAKASiEGKDRFDPSFFqISPKDAEFMDPQLRMLLTH 1852
Cdd:PRK06333 22 ETFWQRLLAGQSGIRT----------LTDFPVGDlatkiGGQVPDLAE-DAEAGFDPDRY-LDPKDQRKMDRFILFAMAA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1853 SWKAIEDAGYAAGQIPQ---TSVFMSASNNSYRALlpsdtTESLETPDgyvswvlaQSG-------TIPTM--------I 1914
Cdd:PRK06333 90 AKEALAQAGWDPDTLEDrerTATIIGSGVGGFPAI-----AEAVRTLD--------SRGprrlspfTIPSFltnmaaghV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1915 SHKLGLRGPSYFVHANCSSSLIGLHSAYKSLLSAESDYALVGGatlhTESNIGYVHQPGLN----FSS---DGHIKA--- 1984
Cdd:PRK06333 157 SIRYGFKGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGG----TEAAIDRVSLAGFAaaraLSTrfnDAPEQAsrp 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1985 FDASADGMIGGEGVAVVLLKKAADAVKDGDHIYALLRGIGVNNDgADKVGFYAPSVKGQADVVQQVMNQTKIHPESICYV 2064
Cdd:PRK06333 233 FDRDRDGFVMGEGAGILVIETLEHALARGAPPLAELVGYGTSAD-AYHMTAGPEDGEGARRAMLIALRQAGIPPEEVQHL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2065 EAHGTGTKLGDPIELAALTNVYRQYTNktqfCGIGSVKTNIGHLDTAAGLAGCIKVVMSLYHQELAPSINYKEPNPNTDl 2144
Cdd:PRK06333 312 NAHATSTPVGDLGEVAAIKKVFGHVSG----LAVSSTKSATGHLLGAAGGVEAIFTILALRDQIAPPTLNLENPDPAAE- 386
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1776025254 2145 assPFYVVDQKktlSREIQTHRAALSSFGLGGTNTHAIFEQFK 2187
Cdd:PRK06333 387 ---GLDVVANK---ARPMDMDYALSNGFGFGGVNASILFRRWE 423
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
1157-1639 |
7.47e-27 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 118.84 E-value: 7.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1157 ELFEQQAKKTPDRAA--VSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLD 1234
Cdd:PRK05852 20 DLVEVAATRLPEAPAlvVTADRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1235 PSYPAERLEYMLEDSEVFITLTTSELVN-----TLSWNGVTTALLDQDWDEIAQTASDRKVLT----RTVTPENL----A 1301
Cdd:PRK05852 100 PALPIAEQRVRSQAAGARVVLIDADGPHdraepTTRWWPLTVNVGGDSGPSGGTLSVHLDAATeptpATSTPEGLrpddA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1302 YVIYTSGSTGKPKGVMIPHKALTNFLVSMGETPGLTAEDKMLAVTTYCFD---IAAL--------ELFLPlikgAHCYIc 1370
Cdd:PRK05852 180 MIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGhglIAALlatlasggAVLLP----ARGRF- 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1371 qTEHTkdvekLKRDIRTIKPTVMQATPATWKMLFYSGWENEENVKIL-------CGGEALPET---LKRYFLDTGSEAwn 1440
Cdd:PRK05852 255 -SAHT-----FWDDIKAVGATWYTAVPTIHQILLERAATEPSGRKPAalrfirsCSAPLTAETaqaLQTEFAAPVVCA-- 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1441 mFGPTETTIWSAVQRIN----DECSRATIGRPIANT--QIYITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRF 1514
Cdd:PRK05852 327 -FGMTEATHQVTTTQIEgigqTENPVVSTGLVGRSTgaQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANF 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1515 IDNPFepgsklyRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMDNL----AAYYTA 1590
Cdd:PRK05852 406 TDGWL-------RTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLygeaVAAVIV 478
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1776025254 1591 KHANASLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLK 1639
Cdd:PRK05852 479 PRESAPPTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAVA 527
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
1177-1583 |
7.65e-27 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.
Pssm-ID: 341294 [Multi-domain] Cd Length: 507 Bit Score: 118.47 E-value: 7.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1177 QTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGgayvpldpsypaerleymledsevfITLT 1256
Cdd:cd17639 4 KYMSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQN-------------------------IPIV 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1257 TseLVNTLSWNGVTTALldqdwdeiAQTASdRKVLTrTVTPENLAYVIYTSGSTGKPKGVMIPHKALTNFLVSMGE--TP 1334
Cdd:cd17639 59 T--VYATLGEDALIHSL--------NETEC-SAIFT-DGKPDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDrvPE 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1335 GLTAEDKMLAvttycfdiaalelFLPLikgAH--------------CYIC----QTEHTKDVEKLKRDIRTIKPTVMQAT 1396
Cdd:cd17639 127 LLGPDDRYLA-------------YLPL---AHifelaaenvclyrgGTIGygspRTLTDKSKRGCKGDLTEFKPTLMVGV 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1397 PATW------------------KMLFYSGWENEEN------------------VK---------ILCGGEALPETLKRYF 1431
Cdd:cd17639 191 PAIWdtirkgvlaklnpmgglkRTLFWTAYQSKLKalkegpgtplldelvfkkVRaalggrlryMLSGGAPLSADTQEFL 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1432 LDTGSEAWNMFGPTETTIWSAVQRINDeCSRATIGRPIANTQI---------YITDsqlAPVPAGvpgELCIAGDGVAKG 1502
Cdd:cd17639 271 NIVLCPVIQGYGLTETCAGGTVQDPGD-LETGRVGPPLPCCEIklvdweeggYSTD---KPPPRG---EILIRGPNVFKG 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1503 YYKKEELTDSRFIDNPFepgsklYRTGDMARWLPGGRIEYIGRIDNQVKIR-GFRIELGDIESRLSEHPGILECVVVADM 1581
Cdd:cd17639 344 YYKNPEKTKEAFDGDGW------FHTGDIGEFHPDGTLKIIDRKKDLVKLQnGEYIALEKLESIYRSNPLVNNICVYADP 417
|
..
gi 1776025254 1582 DN 1583
Cdd:cd17639 418 DK 419
|
|
| X-Domain_NRPS |
cd19546 |
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ... |
695-1121 |
7.99e-27 |
|
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to the non-ribosomal peptide synthetase (NRPS); The X-domain is a catalytically inactive member of the Condensation (C) domain family of non-ribosomal peptide synthetase (NRPS). It has been shown to recruit oxygenases to the NRPS to perform side-chain crosslinking in the production of glycopeptide antibiotics. C-domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as this X-domain, the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, and dual E/C (epimerization and condensation) domains. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity; members of this X-domain subfamily lack the second H of this motif.
Pssm-ID: 380468 [Multi-domain] Cd Length: 440 Bit Score: 117.58 E-value: 7.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 695 PLSEVQKGLWTLQKMSPEKSAYHVPLCFKFSSGLHLETLQQAFGLVLNQHPILK------------HVIQEKDGVPILKN 762
Cdd:cd19546 6 PATAGQLRTWLLARLDEETRGRHLSVALRLRGRLDRDALEAALGDVAARHEILRttfpgdggdvhqRILDADAARPELPV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 763 EPAlsieiktenissmKESDIPAFLRKKVKEPYvkensPLVRVMS-----FSRSEQEHFLLVVIHHLIFDGVSSVTFIHS 837
Cdd:cd19546 86 VPA-------------TEEELPALLADRAAHLF-----DLTRETPwrctlFALSDTEHVLLLVVHRIAADDESLDVLVRD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 838 LFDTYQLLLKGQQPEIAVSPAIYHDFAAWEKNMLAGKDGVK-----HRTYWQKQLSGTLPNLQLPKVSASSV-SEFREDT 911
Cdd:cd19546 148 LAAAYGARREGRAPERAPLPLQFADYALWERELLAGEDDRDsligdQIAYWRDALAGAPDELELPTDRPRPVlPSRRAGA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 912 YTRRLSSGFMNQVRMFAKEHSVNVTTVFLSCYMMLLGRYTGQKEQIVGMpAMVRPEER--FDDAIGHFLNMLPIRSELNP 989
Cdd:cd19546 228 VPLRLDAEVHARLMEAAESAGATMFTVVQAALAMLLTRLGAGTDVTVGT-VLPRDDEEgdLEGMVGPFARPLALRTDLSG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 990 ADTFSSFISKLQLTILDGLDHAAYPFPKMVRDLNIPRSQAGSPVFQTAFfyqnFLQSGSYQSLLSRYADFFSVDYVEYIH 1069
Cdd:cd19546 307 DPTFRELLGRVREAVREARRHQDVPFERLAELLALPPSADRHPVFQVAL----DVRDDDNDPWDAPELPGLRTSPVPLGT 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1776025254 1070 QEGEYELVFELWETE------EKMELNIKYNTGLFDAASISAMFDHFVYVTEQAMLNP 1121
Cdd:cd19546 383 EAMELDLSLALTERRnddgdpDGLDGSLRYAADLFDRATAAALARRLVRVLEQVAADP 440
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
60-477 |
8.05e-27 |
|
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341295 [Multi-domain] Cd Length: 468 Bit Score: 117.85 E-value: 8.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 60 QSYRRLWDDGLRIVKGLRQSGLKAKQSVILqLGDNS-QLLPAFWGCVLTGVVPAPLAvpptyaeSSSGTQKLkdawtlld 138
Cdd:cd17640 6 ITYKDLYQEILDFAAGLRSLGVKAGEKVAL-FADNSpRWLIADQGIMALGAVDVVRG-------SDSSVEEL-------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 139 kpavitdrgmhqemldwakeqglegfrAIIVEDllsAEADTDWHQSSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKG 218
Cdd:cd17640 70 ---------------------------LYILNH---SESVALVVENDSDDLATIIYTSGTTGNPKGVMLTHANLLHQIRS 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 219 IIQMQGFTREDITFNWMPFDHVggigMLHLRDVYL---GCQEINVSSETILmEPLKwlDWIDHYRASVtwaPNFAFGLVT 295
Cdd:cd17640 120 LSDIVPPQPGDRFLSILPIWHS----YERSAEYFIfacGCSQAYTSIRTLK-DDLK--RVKPHYIVSV---PRLWESLYS 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 296 DFAEEIKDRkwdlSSMRYML--------------NGGEAMVAKVGRrileLLEPHGLPadaIRPAWGMSETSsGVIFSHE 361
Cdd:cd17640 190 GIQKQVSKS----SPIKQFLflfflsggifkfgiSGGGALPPHVDT----FFEAIGIE---VLNGYGLTETS-PVVSARR 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 362 FTR--AGTsdddhfveIGSPIPGFSMRIVNDH-NELVEEGEIGRFQVSGLSVTSGYYQRPDLNESVFTEDGWFETGDLGF 438
Cdd:cd17640 258 LKCnvRGS--------VGRPLPGTEIKIVDPEgNVVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGWFNTGDLGW 329
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1776025254 439 L-RNGRLTITGRTKDAIII-NGINYYSHAIESAVEELSEIE 477
Cdd:cd17640 330 LtCGGELVLTGRAKDTIVLsNGENVEPQPIEEALMRSPFIE 370
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
61-555 |
9.29e-27 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 117.01 E-value: 9.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 61 SYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNSQLLPAFWGCVLTGVVPAPLAvpPTYAESSSgtqklkdawtlldkP 140
Cdd:cd05934 5 TYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPIN--TALRGDEL--------------A 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 141 AVITDRGMHqemldwakeqglegfrAIIVedllsaeadtdwhqsspeDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGII 220
Cdd:cd05934 69 YIIDHSGAQ----------------LVVV------------------DPASILYTSGTTGPPKGVVITHANLTFAGYYSA 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 221 QMQGFTREDITFNWMPFDHVGGIGMLHLRDVYLGCqeinvsseTILMEPL----KWLDWIDHYRASVTWAPNFAFGLVTD 296
Cdd:cd05934 115 RRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGA--------TLVLLPRfsasRFWSDVRRYGATVTNYLGAMLSYLLA 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 297 FAEEIKDRKWDLSsmrymlnggEAMVAKVGRRIL-ELLEPHGLPadaIRPAWGMSETSSGVIFSHEFTRAGTSdddhfve 375
Cdd:cd05934 187 QPPSPDDRAHRLR---------AAYGAPNPPELHeEFEERFGVR---LLEGYGMTETIVGVIGPRDEPRRPGS------- 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 376 IGSPIPGFSMRIVNDHNELVEEGEIGRFQV---SGLSVTSGYYQRPDLNESVFtEDGWFETGDLGFLR-NGRLTITGRTK 451
Cdd:cd05934 248 IGRPAPGYEVRIVDDDGQELPAGEPGELVIrglRGWGFFKGYYNMPEATAEAM-RNGWFHTGDLGYRDaDGFFYFVDRKK 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 452 DAIIINGINYYSHAIESAVEELSEIETSytAACAVRlGQNSTDQLAIFFVT--SAKLNDEQMSQLLRniqshvsqviGVT 529
Cdd:cd05934 327 DMIRRRGENISSAEVERAILRHPAVREA--AVVAVP-DEVGEDEVKAVVVLrpGETLDPEELFAFCE----------GQL 393
|
490 500
....*....|....*....|....*....
gi 1776025254 530 PEYLLP--VQ-KEEIPKTAIGKIQRTQLK 555
Cdd:cd05934 394 AYFKVPryIRfVDDLPKTPTEKVAKAQLR 422
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
187-551 |
9.57e-27 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 115.05 E-value: 9.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 187 EDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQ-GFTREDITFNWMPFDHVGgiGMLHLRDVYLGCQEINVSSETI 265
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGlNWVVGDVTYLPLPATHIG--GLWWILTCLIHGGLCVTGGENT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 266 LMEPLkwLDWIDHYRASVT-WAPNFAFGLVTDFAEEIKDRKwdlsSMRYMLNGGEAMVAKVGRRILellephGLPADAIR 344
Cdd:cd17635 79 TYKSL--FKILTTNAVTTTcLVPTLLSKLVSELKSANATVP----SLRLIGYGGSRAIAADVRFIE------ATGLTNTA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 345 PAWGMSETSSGVIFSHEftragtSDDDHFVEIGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGYYQRPDLNESV 424
Cdd:cd17635 147 QVYGLSETGTALCLPTD------DDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 425 FTeDGWFETGDLGFLR-NGRLTITGRTKDAIIINGINYYSHAIESAVEELSEIEtsyTAACAvRLGQNSTDQLAIFFVTS 503
Cdd:cd17635 221 LI-DGWVNTGDLGERReDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQ---ECACY-EISDEEFGELVGLAVVA 295
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1776025254 504 AKLNDEQMsqllrnIQSHVSQVIGVTPEYLLP---VQKEEIPKTAIGKIQR 551
Cdd:cd17635 296 SAELDENA------IRALKHTIRRELEPYARPstiVIVTDIPRTQSGKVKR 340
|
|
| PRK06501 |
PRK06501 |
beta-ketoacyl-ACP synthase; |
3508-3776 |
1.25e-26 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235817 [Multi-domain] Cd Length: 425 Bit Score: 116.65 E-value: 1.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3508 TACSSSLVAIHRAVTAMQNGDCEMAIAGGVNTILTEEAHISYSKAGMLSK-----DGRCKTFSADANGYVRGEGVGMVML 3582
Cdd:PRK06501 173 TACASGATAIQLGVEAIRRGETDRALCIATDGSVSAEALIRFSLLSALSTqndppEKASKPFSKDRDGFVMAEGAGALVL 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3583 KKLEDAERDGNHIYGVIRGTAENHGGRANTLTSPNPKAQADLLVRAYRQAGIDPSTVTYIEAHGTGTELGDPIEINGLKA 3662
Cdd:PRK06501 253 ESLESAVARGAKILGIVAGCGEKADSFHRTRSSPDGSPAIGAIRAALADAGLTPEQIDYINAHGTSTPENDKMEYLGLSA 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3663 AFkelsnmrGESQPDVPdhrcgIGSVKSNIGHLELAAGISGLIKVLLQMKHKTLVKSLHCETLNPYLqltdsPFYIVQEK 3742
Cdd:PRK06501 333 VF-------GERLASIP-----VSSNKSMIGHTLTAAGAVEAVFSLLTIQTGRLPPTINYDNPDPAI-----PLDVVPNV 395
|
250 260 270
....*....|....*....|....*....|....
gi 1776025254 3743 QEWKSVTDCDGNelprragisSFGIGGVNAHIVI 3776
Cdd:PRK06501 396 ARDARVTAVLSN---------SFGFGGQNASLVL 420
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
1299-1635 |
2.90e-26 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 112.88 E-value: 2.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1299 NLAYVIYTSGSTGKPKGVMIPHKAltnFLVSMGETPGL---TAEDKMLAVTTYCFDIAALELFLPLIKGAHCYICQTEHT 1375
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERS---WIESFVCNEDLfniSGEDAILAPGPLSHSLFLYGAISALYLGGTFIGQRKFNP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1376 KdveKLKRDIRTIKPTVMQATPATWKMLfYSGWENEENVK-ILCGGEALPET----LKRYFLDtgSEAWNMFGPTETTI- 1449
Cdd:cd17633 78 K---SWIRKINQYNATVIYLVPTMLQAL-ARTLEPESKIKsIFSSGQKLFEStkkkLKNIFPK--ANLIEFYGTSELSFi 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1450 -WSAVQrinDECSRATIGRPIANTQIYITDSQlapvpAGVPGELCIAGDGVAKGYYKKEELtdsrfidNPFEPgsklYRT 1528
Cdd:cd17633 152 tYNFNQ---ESRPPNSVGRPFPNVEIEIRNAD-----GGEIGKIFVKSEMVFSGYVRGGFS-------NPDGW----MSV 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1529 GDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMDN-----LAAYYTAKhanaSLTARELR 1603
Cdd:cd17633 213 GDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDArfgeiAVALYSGD----KLTYKQLK 288
|
330 340 350
....*....|....*....|....*....|..
gi 1776025254 1604 HFVKNALPAYMVPSYFIQLDHMPLTPNGKIDR 1635
Cdd:cd17633 289 RFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
1160-1640 |
3.55e-26 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.
Pssm-ID: 341283 [Multi-domain] Cd Length: 486 Bit Score: 116.24 E-value: 3.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1160 EQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPA 1239
Cdd:cd12118 11 ERAAAVYPDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1240 ERLEYMLEDSEVFITLTTSELVntlswngvTTALLDQ--DWDEIAQTASDRKVLTrtvtpenlayVIYTSGSTGKPKGVM 1317
Cdd:cd12118 91 EEIAFILRHSEAKVLFVDREFE--------YEDLLAEgdPDFEWIPPADEWDPIA----------LNYTSGTTGRPKGVV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1318 IPHK-----ALTNFLVS-MGETPGLTAEDKMLAVTTYCF--DIAAlelflplIKGAHcyICQteHTKDVEKLKRDIRTIK 1389
Cdd:cd12118 153 YHHRgaylnALANILEWeMKQHPVYLWTLPMFHCNGWCFpwTVAA-------VGGTN--VCL--RKVDAKAIYDLIEKHK 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1390 PTVMQATPATWKMLFYSGWENEEN----VKILCGGEALPETLKRYFLDTGSEAWNMFGPTETT------IWSAVQrinDE 1459
Cdd:cd12118 222 VTHFCGAPTVLNMLANAPPSDARPlphrVHVMTAGAPPPAAVLAKMEELGFDVTHVYGLTETYgpatvcAWKPEW---DE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1460 CSRATIGRPIANTQI-YITDSQLA--------PVPA-GVP-GELCIAGDGVAKGYYKKEELTDSRFIDNPFepgsklyRT 1528
Cdd:cd12118 299 LPTEERARLKARQGVrYVGLEEVDvldpetmkPVPRdGKTiGEIVFRGNIVMKGYLKNPEATAEAFRGGWF-------HS 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1529 GDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMDN-----LAAYYTAKHAnASLTARELR 1603
Cdd:cd12118 372 GDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEkwgevPCAFVELKEG-AKVTEEEII 450
|
490 500 510
....*....|....*....|....*....|....*..
gi 1776025254 1604 HFVKNALPAYMVPSYFIqLDHMPLTPNGKIDRNSLKN 1640
Cdd:cd12118 451 AFCREHLAGFMVPKTVV-FGELPKTSTGKIQKFVLRD 486
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
61-445 |
3.87e-26 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 117.15 E-value: 3.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 61 SYRRLWDDGLRIVKGLRQSGLKAKQSVILqLGDNS--QLLPAFwGCVLTGVVPAPlaVPPTYAESSSGTQKLKDAWTLLd 138
Cdd:cd05921 27 TYAEALRQVRAIAQGLLDLGLSAERPLLI-LSGNSieHALMAL-AAMYAGVPAAP--VSPAYSLMSQDLAKLKHLFELL- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 139 KPAVI--TDRGMHQEMLDWAKEQGL---------EGFRAIIVEDLLS----AEADTDWHQSSPEDLALLLLTSGSTGTPK 203
Cdd:cd05921 102 KPGLVfaQDAAPFARALAAIFPLGTplvvsrnavAGRGAISFAELAAtpptAAVDAAFAAVGPDTVAKFLFTSGSTGLPK 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 204 AVMLNHRNIMSMVKGIIQMQGFTREDI--TFNWMPFDHV-GGIGMLHLRDVYLGCQEINVSSETILM--EPLKWLdwidh 278
Cdd:cd05921 182 AVINTQRMLCANQAMLEQTYPFFGEEPpvLVDWLPWNHTfGGNHNFNLVLYNGGTLYIDDGKPMPGGfeETLRNL----- 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 279 YRASVTWAPNFAFGLvTDFAEEIKD----RKWDLSSMRYMLNGGEAMVAKVGRRILELLEPHGLPADAIRPAWGMSETSS 354
Cdd:cd05921 257 REISPTVYFNVPAGW-EMLVAALEKdealRRRFFKRLKLMFYAGAGLSQDVWDRLQALAVATVGERIPMMAGLGATETAP 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 355 GVIFSHEFT-RAGTsdddhfveIGSPIPGFSMRivndhneLVEEGeiGRFQ--VSGLSVTSGYYQRPDLNESVFTEDGWF 431
Cdd:cd05921 336 TATFTHWPTeRSGL--------IGLPAPGTELK-------LVPSG--GKYEvrVKGPNVTPGYWRQPELTAQAFDEEGFY 398
|
410 420
....*....|....*....|....*
gi 1776025254 432 ETGDL-----------GFLRNGRLT 445
Cdd:cd05921 399 CLGDAakladpddpakGLVFDGRVA 423
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
61-554 |
6.29e-26 |
|
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.
Pssm-ID: 341230 [Multi-domain] Cd Length: 505 Bit Score: 115.80 E-value: 6.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 61 SYRRLWDDGLRIVKGLRQSGLKaKQSVILQLGDNSQLLP-AFWGCVLTGVV--PA-PLAVPPTYAE------------SS 124
Cdd:cd05904 34 TYAELERRVRRLAAGLAKRGGR-KGDVVLLLSPNSIEFPvAFLAVLSLGAVvtTAnPLSTPAEIAKqvkdsgaklaftTA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 125 SGTQKLKDawtlLDKPAVITDRgmhqemldwAKEQGLEGFRAIIVEDllsaEADTDWHQSSPEDLALLLLTSGSTGTPKA 204
Cdd:cd05904 113 ELAEKLAS----LALPVVLLDS---------AEFDSLSFSDLLFEAD----EAEPPVVVIKQDDVAALLYSSGTTGRSKG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 205 VMLNHRNIMSMVKGIIQMQG--FTREDITFNWMPFDHVGGIGMLHLRDVYLGcqeinvsSETILM---EPLKWLDWIDHY 279
Cdd:cd05904 176 VMLTHRNLIAMVAQFVAGEGsnSDSEDVFLCVLPMFHIYGLSSFALGLLRLG-------ATVVVMprfDLEELLAAIERY 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 280 RasVTWAPnFAFGLVTDFAEEIKDRKWDLSSMRYMLNGGeamvAKVGRRILELLEPHgLPADAIRPAWGMSEtSSGVIFS 359
Cdd:cd05904 249 K--VTHLP-VVPPIVLALVKSPIVDKYDLSSLRQIMSGA----APLGKELIEAFRAK-FPNVDLGQGYGMTE-STGVVAM 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 360 HeFTRAGtsDDDHFVEIGSPIPGFSMRIVN-DHNELVEEGEIGRFQVSGLSVTSGYYQRPDLNESVFTEDGWFETGDLGF 438
Cdd:cd05904 320 C-FAPEK--DRAKYGSVGRLVPNVEAKIVDpETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKEGWLHTGDLCY 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 439 LRN-GRLTITGRTKDAIIINGinyY------------SH-AIESAV------EELSEIetsyTAACAVR-LGQNSTDQLA 497
Cdd:cd05904 397 IDEdGYLFIVDRLKELIKYKG---FqvapaelealllSHpEILDAAvipypdEEAGEV----PMAFVVRkPGSSLTEDEI 469
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1776025254 498 IFFVtsAKlndeqmsqllrniqshvsQVIgvtpeyllPVQK-------EEIPKTAIGKIQRTQL 554
Cdd:cd05904 470 MDFV--AK------------------QVA--------PYKKvrkvafvDAIPKSPSGKILRKEL 505
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
168-555 |
6.70e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 115.29 E-value: 6.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 168 IVEDL--LSAEAD----TDWHQSSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDHVg 241
Cdd:PRK09088 110 DVEDLaaFIASADalepADTPSIPPERVSLILFTSGTSGQPKGVMLSERNLQQTAHNFGVLGRVDAHSSFLCDAPMFHI- 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 242 gIGML-HLRDVYLGCQEINVSSEtilMEPLKWLDW-------IDHYrasvtwapnfaFGlVTDFAEEIKDRK-WDLSSMR 312
Cdd:PRK09088 189 -IGLItSVRPVLAVGGSILVSNG---FEPKRTLGRlgdpalgITHY-----------FC-VPQMAQAFRAQPgFDAAALR 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 313 YM---LNGGEamvakvgrrilellePHglPADAIRpAW-----------GMSEtsSGVIFSHEF------TRAGTSdddh 372
Cdd:PRK09088 253 HLtalFTGGA---------------PH--AAEDIL-GWlddgipmvdgfGMSE--AGTVFGMSVdcdvirAKAGAA---- 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 373 fveiGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGYYQRPDLNESVFTEDGWFETGDLGfLRN--GRLTITGRT 450
Cdd:PRK09088 309 ----GIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDGWFRTGDIA-RRDadGFFWVVDRK 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 451 KDAIIINGINYYSHAIESAVEELSEIetsytAACAV------RLGqnstdQLAIFFVTSAklndEQMSQLLRNIQSHVSQ 524
Cdd:PRK09088 384 KDMFISGGENVYPAEIEAVLADHPGI-----RECAVvgmadaQWG-----EVGYLAIVPA----DGAPLDLERIRSHLST 449
|
410 420 430
....*....|....*....|....*....|...
gi 1776025254 525 VIG--VTPEYLLPVqkEEIPKTAIGKIQRTQLK 555
Cdd:PRK09088 450 RLAkyKVPKHLRLV--DALPRTASGKLQKARLR 480
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
1158-1640 |
7.04e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 115.09 E-value: 7.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1158 LFEQQAKKTPDRA-AVSYEGQTLTYRELDERSTQLAiylqahgvgpDRLAGiyVDR-------SLDMLVGLLAILKAGGA 1229
Cdd:PRK07787 4 LNPAAVAAAADIAdAVRIGGRVLSRSDLAGAATAVA----------ERVAG--ARRvavlatpTLATVLAVVGALIAGVP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1230 YVPLDP-SYPAERlEYMLEDSevfitlttselvntlswnGVTTALLDQDWDEIAQTASDRKVLTRT------VTPENLAY 1302
Cdd:PRK07787 72 VVPVPPdSGVAER-RHILADS------------------GAQAWLGPAPDDPAGLPHVPVRLHARSwhrypePDPDAPAL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1303 VIYTSGSTGKPKGVMIPHKALTNFLVSMGETPGLTAEDKMlavttycfdIAALELFL----------PLIKGAhcyicqt 1372
Cdd:PRK07787 133 IVYTSGTTGPPKGVVLSRRAIAADLDALAEAWQWTADDVL---------VHGLPLFHvhglvlgvlgPLRIGN------- 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1373 ehtkdveklkRDIRTIKPT---VMQATPATWKMLFysG----W----ENEENVKIL-------CGGEALP----ETLKRY 1430
Cdd:PRK07787 197 ----------RFVHTGRPTpeaYAQALSEGGTLYF--GvptvWsriaADPEAARALrgarllvSGSAALPvpvfDRLAAL 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1431 fldTGSEAWNMFGPTETTIWSAVqRINDECSRATIGRPIANTQIYITDSQLAPVPAGVP--GELCIAGDGVAKGYYKKEE 1508
Cdd:PRK07787 265 ---TGHRPVERYGMTETLITLST-RADGERRPGWVGLPLAGVETRLVDEDGGPVPHDGEtvGELQVRGPTLFDGYLNRPD 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1509 LTDSRFIDNPFepgsklYRTGDMARWLPGGRIEYIGR--IDnQVKIRGFRIELGDIESRLSEHPGILECVVV--ADMD-- 1582
Cdd:PRK07787 341 ATAAAFTADGW------FRTGDVAVVDPDGMHRIVGResTD-LIKSGGYRIGAGEIETALLGHPGVREAAVVgvPDDDlg 413
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1776025254 1583 -NLAAYYTakhANASLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLKN 1640
Cdd:PRK07787 414 qRIVAYVV---GADDVAADELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLLS 469
|
|
| PRK07103 |
PRK07103 |
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated |
4590-4939 |
7.96e-26 |
|
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
Pssm-ID: 180839 [Multi-domain] Cd Length: 410 Bit Score: 113.97 E-value: 7.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4590 IAVVGLSCRFPGAETLESYWSLLSEGRSSIG-------PIPAERWGCKT-PYYAGVIDGVSYFDP-DFFLLHEE--DVRA 4658
Cdd:PRK07103 4 VVVTGVGVVSAIGQGRPSFAAALLAGRHAFGvmrrpgrQVPDDAGAGLAsAFIGAELDSLALPERlDAKLLRRAslSAQA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4659 mdpqALLVLEECLKllyHAGYTPEEikGKPVGVYIGG-----RSQHKPDEDSLDHAK--NP--IVTVGQNYLAANLSQFF 4729
Cdd:PRK07103 84 ----ALAAAREAWR---DAALGPVD--PDRIGLVVGGsnlqqREQALVHETYRDRPAflRPsyGLSFMDTDLVGLCSEQF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4730 DVRGPSVVVDTACSSALVGMNMAIQALRGGDIQSAI-VGGVSLLSSDASHRLFDRRGILSKHSSFHV------FDERADG 4802
Cdd:PRK07103 155 GIRGEGFTVGGASASGQLAVIQAARLVQSGSVDACIaVGALMDLSYWECQALRSLGAMGSDRFADEPeaacrpFDQDRDG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4803 VVLGEGVGMVMLKTVKQALEDGDTIYAVVKAASVNNDGrTAGPAtPNLEAQKEVMKDALFKSGKKPEDISYLEANGSGSI 4882
Cdd:PRK07103 235 FIYGEACGAVVLESAESARRRGARPYAKLLGWSMRLDA-NRGPD-PSLEGEMRVIRAALRRAGLGPEDIDYVNPHGTGSP 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1776025254 4883 VTDLLELKAIqsvYRSGHSSPLsLGSIKPNIGHPLCAEGIASFIKVVLMLKERRFVP 4939
Cdd:PRK07103 313 LGDETELAAL---FASGLAHAW-INATKSLTGHGLSAAGIVELIATLLQMRAGFLHP 365
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
1156-1648 |
9.99e-26 |
|
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.
Pssm-ID: 341272 [Multi-domain] Cd Length: 610 Bit Score: 116.44 E-value: 9.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1156 HELFEQQAKKTPDRAAVSYEGQ-----TLTYRELDERSTQLAIYLQAHGVGP-DRLaGIYVDRSLDMLVGLLAILKAGGA 1229
Cdd:cd05968 64 EQLLDKWLADTRTRPALRWEGEdgtsrTLTYGELLYEVKRLANGLRALGVGKgDRV-GIYLPMIPEIVPAFLAVARIGGI 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1230 YVPLDPSYPAERLEYMLEDSEVFITLTTselvNTLSWNGVTTALLDQDWDEIAQTASDRKVLT-----RTVTPENLAY-- 1302
Cdd:cd05968 143 VVPIFSGFGKEAAATRLQDAEAKALITA----DGFTRRGREVNLKEEADKACAQCPTVEKVVVvrhlgNDFTPAKGRDls 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1303 ----------------------VIYTSGSTGKPKGVM-----IPHKALTNFLVSMGETPGltaeDKMLAVTTYCFDIAAL 1355
Cdd:cd05968 219 ydeeketagdgaertesedplmIIYTSGTTGKPKGTVhvhagFPLKAAQDMYFQFDLKPG----DLLTWFTDLGWMMGPW 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1356 ELFLPLIKGAHC--YICQTEHTKD------VEKLKRDIRTIKPTVMQATpatwkMLFYSGWENEENVKILcggealpetl 1427
Cdd:cd05968 295 LIFGGLILGATMvlYDGAPDHPKAdrlwrmVEDHEITHLGLSPTLIRAL-----KPRGDAPVNAHDLSSL---------- 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1428 kRYFLDTGS----EAWNMFgpTETTIWSAVQRIN----DECSRATIG----RPIA---------NTQIYITDSQLAPVPA 1486
Cdd:cd05968 360 -RVLGSTGEpwnpEPWNWL--FETVGKGRNPIINysggTEISGGILGnvliKPIKpssfngpvpGMKADVLDESGKPARP 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1487 GVpGELCIAGD--GVAKGYYKKEEltdsRFIDNPFEPGSKLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIES 1564
Cdd:cd05968 437 EV-GELVLLAPwpGMTRGFWRDED----RYLETYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIES 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1565 RLSEHPGILECVVVADMDNLAAyyTAKHANASL---------TARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDR 1635
Cdd:cd05968 512 VLNAHPAVLESAAIGVPHPVKG--EAIVCFVVLkpgvtpteaLAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMR 589
|
570
....*....|...
gi 1776025254 1636 NSLKNIDLsGEQL 1648
Cdd:cd05968 590 RVIRAAYL-GKEL 601
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
188-490 |
1.13e-25 |
|
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.
Pssm-ID: 341293 [Multi-domain] Cd Length: 330 Bit Score: 111.44 E-value: 1.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 188 DLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDHVGGIGMlhlrdvylGCQEINVSSETIL- 266
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFFHTFGYKA--------GIVACLLTGATVVp 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 267 ---MEPLKWLDWIDHYRASVTWAPNFAFGLVTDfaeEIKDRKWDLSSMRYMLNGGEAMVAKVGRRILEllephGLPADAI 343
Cdd:cd17638 73 vavFDVDAILEAIERERITVLPGPPTLFQSLLD---HPGRKKFDLSSLRAAVTGAATVPVELVRRMRS-----ELGFETV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 344 RPAWGMSETSSGVIfshefTRAGTSDDDHFVEIGSPIPGFSMRIVNDhnelveeGEIgrfQVSGLSVTSGYYQRPDLNES 423
Cdd:cd17638 145 LTAYGLTEAGVATM-----CRPGDDAETVATTCGRACPGFEVRIADD-------GEV---LVRGYNVMQGYLDDPEATAE 209
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1776025254 424 VFTEDGWFETGDLGFL-RNGRLTITGRTKDAIIINGINYYSHAIESAVEELSEIetsytAACAV------RLGQ 490
Cdd:cd17638 210 AIDADGWLHTGDVGELdERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGV-----AQVAVigvpdeRMGE 278
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
30-564 |
1.55e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 114.64 E-value: 1.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 30 TIPEVLYRTAAELGDTKGIIYlqpdGTEVYqSYRRLWDDGLRIVKGLRQSGLKAKQSVILqLGDNS-QLLPAFWGCVLTG 108
Cdd:PRK08316 12 TIGDILRRSARRYPDKTALVF----GDRSW-TYAELDAAVNRVAAALLDLGLKKGDRVAA-LGHNSdAYALLWLACARAG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 109 VVpaplAVPPTYAESSsgtqklKDAWTLLDKP---AVITDRGMHQEMLDWAKEQGLEGFRAIIVEDLLSAEAD----TDW 181
Cdd:PRK08316 86 AV----HVPVNFMLTG------EELAYILDHSgarAFLVDPALAPTAEAALALLPVDTLILSLVLGGREAPGGwldfADW 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 182 HQSSP----------EDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDHVGGigmlhlRDV 251
Cdd:PRK08316 156 AEAGSvaepdveladDDLAQILYTSGTESLPKGAMLTHRALIAEYVSCIVAGDMSADDIPLHALPLYHCAQ------LDV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 252 YLGCQeINVSSETILME---PLKWLDWIDHYRASVTWA-PNFAFGLVT--DFAeeikdrKWDLSSMRYMLNGGEAMVAKV 325
Cdd:PRK08316 230 FLGPY-LYVGATNVILDapdPELILRTIEAERITSFFApPTVWISLLRhpDFD------TRDLSSLRKGYYGASIMPVEV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 326 GRRILEllephGLPADAIRPAWGMSETSS-GVIFSHEftragtsddDHFVEIGSP-IPGFSM--RIVNDHNELVEEGEIG 401
Cdd:PRK08316 303 LKELRE-----RLPGLRFYNCYGQTEIAPlATVLGPE---------EHLRRPGSAgRPVLNVetRVVDDDGNDVAPGEVG 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 402 RFQVSGLSVTSGYYQRPDLNESVFtEDGWFETGDLGFL-RNGRLTITGRTKDAIIINGINYYSHAIE------SAVEELS 474
Cdd:PRK08316 369 EIVHRSPQLMLGYWDDPEKTAEAF-RGGWFHSGDLGVMdEEGYITVVDRKKDMIKTGGENVASREVEealythPAVAEVA 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 475 EIETSY-------TAACAVRLGqnstdqlaiffvtsAKLNDEQmsqllrnIQSHVSQVIGV--TPEYLLPVqkEEIPKTA 545
Cdd:PRK08316 448 VIGLPDpkwieavTAVVVPKAG--------------ATVTEDE-------LIAHCRARLAGfkVPKRVIFV--DELPRNP 504
|
570
....*....|....*....
gi 1776025254 546 IGKIQRTQLKTSFENGEFD 564
Cdd:PRK08316 505 SGKILKRELRERYAGAFTD 523
|
|
| PRK06333 |
PRK06333 |
beta-ketoacyl-ACP synthase; |
4590-4993 |
2.26e-25 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235781 [Multi-domain] Cd Length: 424 Bit Score: 112.78 E-value: 2.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4590 IAVVGLSCRFPGAETLESYWSLLSEGRSSIGPIP---AERWGCKtpyYAGVI-----DGVSYFDPDFFLlHEEDVRAMDP 4661
Cdd:PRK06333 6 IVVTGMGAVSPLGCGVETFWQRLLAGQSGIRTLTdfpVGDLATK---IGGQVpdlaeDAEAGFDPDRYL-DPKDQRKMDR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4662 QALLVLEECLKLLYHAGYTPEEIK-----GKPVGVYIGGRSqhkpdedSLDHAKNPIVTVGQ-------------NYLAA 4723
Cdd:PRK06333 82 FILFAMAAAKEALAQAGWDPDTLEdrertATIIGSGVGGFP-------AIAEAVRTLDSRGPrrlspftipsfltNMAAG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4724 NLSQFFDVRGPSVVVDTACSSALVGMNMAIQALRGGDIQSAIVGG-------VSLLSSDASHRLFDRRGILSKHSSfHVF 4796
Cdd:PRK06333 155 HVSIRYGFKGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGteaaidrVSLAGFAAARALSTRFNDAPEQAS-RPF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4797 DERADGVVLGEGVGMVMLKTVKQALEDGDTIYAVVKAASVNNDGR--TAGPatPNLEAQKEVMKDALFKSGKKPEDISYL 4874
Cdd:PRK06333 234 DRDRDGFVMGEGAGILVIETLEHALARGAPPLAELVGYGTSADAYhmTAGP--EDGEGARRAMLIALRQAGIPPEEVQHL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4875 EANGSGSIVTDLLELKAIQSVYrsGHSSPLSLGSIKPNIGHPLCAEGIASFIKVVLMLKERRFVPFLSGEkemaHFDQQK 4954
Cdd:PRK06333 312 NAHATSTPVGDLGEVAAIKKVF--GHVSGLAVSSTKSATGHLLGAAGGVEAIFTILALRDQIAPPTLNLE----NPDPAA 385
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1776025254 4955 ANITFSRalekwTDSQPTA---AI-NCFADGGTNVHVIVEAWE 4993
Cdd:PRK06333 386 EGLDVVA-----NKARPMDmdyALsNGFGFGGVNASILFRRWE 423
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
1160-1639 |
3.45e-25 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 114.10 E-value: 3.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1160 EQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVG-PDRLAGIYVDRSlDMLVGLLAILKAGGAYVPLDPSYP 1238
Cdd:PRK07786 24 ARHALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGfGDRVLILMLNRT-EFVESVLAANMLGAIAVPVNFRLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1239 AERLEYMLEDSEVFITLTTSELVN----------TLSWNGVTTALLDQDW----DEIAQTASDRKVLTrtvTPENL-AYV 1303
Cdd:PRK07786 103 PPEIAFLVSDCGAHVVVTEAALAPvatavrdivpLLSTVVVAGGSSDDSVlgyeDLLAEAGPAHAPVD---IPNDSpALI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1304 IYTSGSTGKPKGVMIPHKALTNFLVSMGETPGLTAEDKMLAVTTYCFDIAALELFLP-LIKGAHCYICQT---EHTKDVE 1379
Cdd:PRK07786 180 MYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGADINSDVGFVGVPLFHIAGIGSMLPgLLLGAPTVIYPLgafDPGQLLD 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1380 KLKRDirtiKPTVMQATPATWKMLFYSGWENEENVK---ILCGGEALPETLKRYFLDTGSEAWNM--FGPTETTIWSAVQ 1454
Cdd:PRK07786 260 VLEAE----KVTGIFLVPAQWQAVCAEQQARPRDLAlrvLSWGAAPASDTLLRQMAATFPEAQILaaFGQTEMSPVTCML 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1455 RINDEC-SRATIGRPIANTQIYITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPFEpgsklyrTGDMAR 1533
Cdd:PRK07786 336 LGEDAIrKLGSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAGGWFH-------SGDLVR 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1534 WLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMDNL-----AAYYTAKHANASLTARELRHFVKN 1608
Cdd:PRK07786 409 QDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKwgevpVAVAAVRNDDAALTLEDLAEFLTD 488
|
490 500 510
....*....|....*....|....*....|.
gi 1776025254 1609 ALPAYMVPSYFIQLDHMPLTPNGKIDRNSLK 1639
Cdd:PRK07786 489 RLARYKHPKALEIVDALPRNPAGKVLKTELR 519
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
28-445 |
3.77e-25 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 114.59 E-value: 3.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 28 PATIPEVLYRTAAELGDTkgiIYL---QPDGTEVYQSYRRLWDDGLRIVKGLRQSGLKAKQSVILqLGDNS--QLLPAFw 102
Cdd:PRK08180 38 PRRLTDRLVHWAQEAPDR---VFLaerGADGGWRRLTYAEALERVRAIAQALLDRGLSAERPLMI-LSGNSieHALLAL- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 103 GCVLTGVVPAPlaVPPTYAESSSGTQKLKDAWTLLdKPAVI--TDRGMHQEMLDWAKEQGLE---------GFRAIIVED 171
Cdd:PRK08180 113 AAMYAGVPYAP--VSPAYSLVSQDFGKLRHVLELL-TPGLVfaDDGAAFARALAAVVPADVEvvavrgavpGRAATPFAA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 172 LL----SAEADTDWHQSSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTRED--ITFNWMPFDHVGG--- 242
Cdd:PRK08180 190 LLatppTAAVDAAHAAVGPDTIAKFLFTSGSTGLPKAVINTHRMLCANQQMLAQTFPFLAEEppVLVDWLPWNHTFGgnh 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 243 -IGM-LH-----------------------LRDVylgcqeinvsSETI-LMEPLKWLDWIDHYRASVTWAPNFafglvtd 296
Cdd:PRK08180 270 nLGIvLYnggtlyiddgkptpggfdetlrnLREI----------SPTVyFNVPKGWEMLVPALERDAALRRRF------- 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 297 faeeikdrkwdLSSMRYMLNGGEAM------------VAKVGRRILellephglpadaIRPAWGMSETSSGVIFSHEFT- 363
Cdd:PRK08180 333 -----------FSRLKLLFYAGAALsqdvwdrldrvaEATCGERIR------------MMTGLGMTETAPSATFTTGPLs 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 364 RAGtsdddhfvEIGSPIPGFSMRivndhneLVEEGeiGRFQ--VSGLSVTSGYYQRPDLNESVFTEDGWFETGD------ 435
Cdd:PRK08180 390 RAG--------NIGLPAPGCEVK-------LVPVG--GKLEvrVKGPNVTPGYWRAPELTAEAFDEEGYYRSGDavrfvd 452
|
490
....*....|....*
gi 1776025254 436 -----LGFLRNGRLT 445
Cdd:PRK08180 453 padpeRGLMFDGRIA 467
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
1168-1639 |
5.01e-25 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 113.84 E-value: 5.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1168 DRAAVSYEG----QTLTYRELDERSTQLAIYLQAHGVGP-DRLAgIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERL 1242
Cdd:PRK04319 59 DKVALRYLDasrkEKYTYKELKELSNKFANVLKELGVEKgDRVF-IFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAV 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1243 EYMLEDSEVFITLTTSEL-----VNTLSwnGVTTALL----------DQDWDEIAQTASDRkVLTRTVTPENLAYVIYTS 1307
Cdd:PRK04319 138 RDRLEDSEAKVLITTPALlerkpADDLP--SLKHVLLvgedveegpgTLDFNALMEQASDE-FDIEWTDREDGAILHYTS 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1308 GSTGKPKGVMIPHKALTNFLVSmGET-----PG----LTAEDKMLAVTTYcfdiaalELFLPLIKGAHCYICQTEHtkDV 1378
Cdd:PRK04319 215 GSTGKPKGVLHVHNAMLQHYQT-GKYvldlhEDdvywCTADPGWVTGTSY-------GIFAPWLNGATNVIDGGRF--SP 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1379 EKLKRDIRTIKPTVMQATPATWKMLFYSGwenEENVK---------ILCGGEAL-PE-------TLKRYFLDTgseaWNM 1441
Cdd:PRK04319 285 ERWYRILEDYKVTVWYTAPTAIRMLMGAG---DDLVKkydlsslrhILSVGEPLnPEvvrwgmkVFGLPIHDN----WWM 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1442 fgpTETtiwsAVQRIndeCSRAT-------IGRPIANTQIYITDSQLAPVPAGVPGELCI-AG-DGVAKGYYKKEELTDS 1512
Cdd:PRK04319 358 ---TET----GGIMI---ANYPAmdikpgsMGKPLPGIEAAIVDDQGNELPPNRMGNLAIkKGwPSMMRGIWNNPEKYES 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1513 RFIDNpfepgskLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMDNLA-----AY 1587
Cdd:PRK04319 428 YFAGD-------WYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRgeiikAF 500
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1776025254 1588 YTAK--HANASLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLK 1639
Cdd:PRK04319 501 VALRpgYEPSEELKEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVLK 554
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
184-554 |
6.20e-25 |
|
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.
Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 111.42 E-value: 6.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 184 SSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDHVGGIGMLHLRDVYLGcqeinvsSE 263
Cdd:cd05935 81 SELDDLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVG-------GT 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 264 TILMEplKW-----LDWIDHYRASVTWApnfAFGLVTDFAEEIKDRKWDLSSMRYMLNGGEAMVAKVGRRILELLephgl 338
Cdd:cd05935 154 YVLMA--RWdretaLELIEKYKVTFWTN---IPTMLVDLLATPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLT----- 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 339 padAIR--PAWGMSETSSGVifsheftragTSDDDHFVE---IGSPIPGFSMRIVN-DHNELVEEGEIGRFQVSGLSVTS 412
Cdd:cd05935 224 ---GLRfvEGYGLTETMSQT----------HTNPPLRPKlqcLGIP*FGVDARVIDiETGRELPPNEVGEIVVRGPQIFK 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 413 GYYQRPDLNESVFTEDG---WFETGDLGFL-RNGRLTITGRTKDAIIINGINYYSHAIESAVEELSEIETsytaACAVRL 488
Cdd:cd05935 291 GYWNRPEETEESFIEIKgrrFFRTGDLGYMdEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*E----VCVISV 366
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1776025254 489 GQNSTDQLAIFFVT-----SAKLNDEQMSQLLRNIQSHVSQVIGVtpEYLlpvqkEEIPKTAIGKIQRTQL 554
Cdd:cd05935 367 PDERVGEEVKAFIVlrpeyRGKVTEEDIIEWAREQMAAYKYPREV--EFV-----DELPRSASGKILWRLL 430
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
1303-1635 |
6.70e-25 |
|
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341292 [Multi-domain] Cd Length: 333 Bit Score: 109.28 E-value: 6.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1303 VIYTSGSTGKPKGVMIPHKALTNFLVSMGETPGLTAEDKMLAVTTYcFDIAALELFLPLIKGAHCYICQTEHtkDVEKLK 1382
Cdd:cd17637 5 IIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPL-FHIAGLNLALATFHAGGANVVMEKF--DPAEAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1383 RDIRTIKPTVMQATPATWKMLFYSGWENEENVKIL--CGGEALPETLKRYFLDTGSEAWNMFGPTETTIWSAVQRINDEC 1460
Cdd:cd17637 82 ELIEEEKVTLMGSFPPILSNLLDAAEKSGVDLSSLrhVLGLDAPETIQRFEETTGATFWSLYGQTETSGLVTLSPYRERP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1461 SRAtiGRPIANTQIYITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNpfepgskLYRTGDMARWLPGGRI 1540
Cdd:cd17637 162 GSA--GRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTFRNG-------WHHTGDLGRFDEDGYL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1541 EYIGRIDNQ--VKIRGFRIELGDIESRLSEHPGILECVV--VADmdnlaayytAK-----------HANASLTARELRHF 1605
Cdd:cd17637 233 WYAGRKPEKelIKPGGENVYPAEVEKVILEHPAIAEVCVigVPD---------PKwgegikavcvlKPGATLTADELIEF 303
|
330 340 350
....*....|....*....|....*....|
gi 1776025254 1606 VKNALPAYMVPSYFIQLDHMPLTPNGKIDR 1635
Cdd:cd17637 304 VGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
168-554 |
6.84e-25 |
|
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341310 [Multi-domain] Cd Length: 490 Bit Score: 112.42 E-value: 6.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 168 IVEDLLSAEADTDWHQ-SSPEDLALLLLTSGSTGTPKAVMLNHRN----IMSMVKGIIQMQGFTRedITFNWMPFD-HVG 241
Cdd:cd17655 117 LDEDTIYHEESENLEPvSKSDDLAYVIYTSGSTGKPKGVMIEHRGvvnlVEWANKVIYQGEHLRV--ALFASISFDaSVT 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 242 GIGMLHLrdvyLGCQEINVSSETILMEPlKWLDWIDHYRASVTWAPNfafgLVTDFAEEIKDRKWdlSSMRYMLNGGEAM 321
Cdd:cd17655 195 EIFASLL----SGNTLYIVRKETVLDGQ-ALTQYIRQNRITIIDLTP----AHLKLLDAADDSEG--LSLKHLIVGGEAL 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 322 VAKVGRRILELLEPhglpADAIRPAWGMSETSSG-VIFSHEftraGTSDDDHFVEIGSPIPGFSMRIVNDHNELVEEGEI 400
Cdd:cd17655 264 STELAKKIIELFGT----NPTITNAYGPTETTVDaSIYQYE----PETDQQVSVPIGKPLGNTRIYILDQYGRPQPVGVA 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 401 GRFQVSGLSVTSGYYQRPDLNESVFTEDGW------FETGDLG-FLRNGRLTITGRTKDAIIINGinyysHAIesaveEL 473
Cdd:cd17655 336 GELYIGGEGVARGYLNRPELTAEKFVDDPFvpgermYRTGDLArWLPDGNIEFLGRIDHQVKIRG-----YRI-----EL 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 474 SEIETSYT-------AACAVRLGQNSTDQLAIFFVTSAKLNDEQMSQLLRNiqshvsqvigVTPEYLLP---VQKEEIPK 543
Cdd:cd17655 406 GEIEARLLqhpdikeAVVIARKDEQGQNYLCAYIVSEKELPVAQLREFLAR----------ELPDYMIPsyfIKLDEIPL 475
|
410
....*....|.
gi 1776025254 544 TAIGKIQRTQL 554
Cdd:cd17655 476 TPNGKVDRKAL 486
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
1154-1639 |
1.25e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 112.14 E-value: 1.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1154 TFHELFEQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGP-DRLAGIYVDRSlDMLVGLLAILKAGGAYVP 1232
Cdd:PRK06164 11 TLASLLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRgDRVAVWLPNCI-EWVVLFLACARLGATVIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1233 LDPSYPAERLEYMLEDSEV--------FITLTTSELVNTLSWNGVTT----ALLDQDWDEI-AQTASDRKVL-----TRT 1294
Cdd:PRK06164 90 VNTRYRSHEVAHILGRGRArwlvvwpgFKGIDFAAILAAVPPDALPPlraiAVVDDAADATpAPAPGARVQLfalpdPAP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1295 VT-------PENLAYVIYT-SGSTGKPKGVMIPHKALTNFLVSMGETPGLTAEDKMLAVTTYC--FDIAALELFL----P 1360
Cdd:PRK06164 170 PAaageraaDPDAGALLFTtSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCgvFGFSTLLGALaggaP 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1361 LIkgahcyicqTEHTKDVEKLKRDIRTIKPTVMQATPATWKMLFYSGWENEENVKI-LCG--------GEALPETLKRYF 1431
Cdd:PRK06164 250 LV---------CEPVFDAARTARALRRHRVTHTFGNDEMLRRILDTAGERADFPSArLFGfasfapalGELAALARARGV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1432 LDTGseawnMFGPTETTIWSAVQRINDECS--RATIGRPI-ANTQIYITDSQLAPV-PAGVPGELCIAGDGVAKGYYKKE 1507
Cdd:PRK06164 321 PLTG-----LYGSSEVQALVALQPATDPVSvrIEGGGRPAsPEARVRARDPQDGALlPDGESGEIEIRAPSLMRGYLDNP 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1508 ELTDSRFIDNPFepgsklYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVA---DMDNL 1584
Cdd:PRK06164 396 DATARALTDDGY------FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGatrDGKTV 469
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1776025254 1585 AAYYTAKHANASLTARELRHFVKNALPAYMVPSYFIQLDHMPLT--PNG-KIDRNSLK 1639
Cdd:PRK06164 470 PVAFVIPTDGASPDEAGLMAACREALAGFKVPARVQVVEAFPVTesANGaKIQKHRLR 527
|
|
| PRK08722 |
PRK08722 |
beta-ketoacyl-ACP synthase II; |
1827-2186 |
1.30e-24 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 181539 [Multi-domain] Cd Length: 414 Bit Score: 110.09 E-value: 1.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1827 FDPSFFqISPKDAEFMDPQLRMLLTHSWKAIEDAGYAAGQIPQTSVFMS-ASNNSYRALLPSDTTESLETPDGYVSWVLA 1905
Cdd:PRK08722 57 FNCEEY-MSKKDARKMDLFIQYGIAAGIQALDDSGLEVTEENAHRIGVAiGSGIGGLGLIEAGHQALVEKGPRKVSPFFV 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1906 QSgTIPTMISHKL----GLRGPSYFVHANCSSSLIGLHSAYKSLLSAESDYALVGGA-TLHTESNI-GYVHQPGLNFSSD 1979
Cdd:PRK08722 136 PS-TIVNMIAGNLsimrGLRGPNIAISTACTTGLHNIGHAARMIAYGDADAMVAGGAeKASTPLGMaGFGAAKALSTRND 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1980 GHIKA---FDASADGMIGGEGVAVVLLKKAADAVKDGDHIYALLRGIGVNNDgADKVGFYAPSVKGQADVVQQVMNQTKI 2056
Cdd:PRK08722 215 EPQKAsrpWDKDRDGFVLGDGAGMMVLEEYEHAKARGAKIYAELVGFGMSGD-AYHMTSPSEDGSGGALAMEAAMRDAGV 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2057 HPESICYVEAHGTGTKLGDPIELAALTNVYRQYTNKTQFcgIGSVKTNIGHLDTAAGLAGCIKVVMSLYHQELAPSINYK 2136
Cdd:PRK08722 294 TGEQIGYVNAHGTSTPAGDVAEIKGIKRALGEAGSKQVL--VSSTKSMTGHLLGAAGSVEAIITVMSLVDQIVPPTINLD 371
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1776025254 2137 EPNPNTDlasspfyvVDQKKTLSREIQTHRAAL-SSFGLGGTNTHAIFEQF 2186
Cdd:PRK08722 372 DPEEGLD--------IDLVPHTARKVESMEYAIcNSFGFGGTNGSLIFKKM 414
|
|
| KR_1_SDR_x |
cd08952 |
ketoreductase (KR), subgroup 1, complex (x) SDRs; Ketoreductase, a module of the multidomain ... |
4174-4384 |
1.65e-24 |
|
ketoreductase (KR), subgroup 1, complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes KR domains found in many multidomain PKSs, including six of seven Sorangium cellulosum PKSs (encoded by spiDEFGHIJ) which participate in the synthesis of the polyketide scaffold of the cytotoxic spiroketal polyketide spirangien. These seven PKSs have either a single PKS module (SpiF), two PKR modules (SpiD,-E,-I,-J), or three PKS modules (SpiG,-H). This subfamily includes the single KR domain of SpiF, the first KR domains of SpiE,-G,H,-I,and #J, the third KR domain of SpiG, and the second KR domain of SpiH. The second KR domains of SpiE,-G, I, and #J, and the KR domains of SpiD, belong to a different KR_FAS_SDR subfamily. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.
Pssm-ID: 187655 [Multi-domain] Cd Length: 480 Bit Score: 111.11 E-value: 1.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4174 LITGGTRGIGLLCARHFAECyGVKKLVLTGR--EQLPPREEwarfktsntslaekiqAVRELEAKGVQVEMLSLTLSDDA 4251
Cdd:cd08952 234 LVTGGTGALGAHVARWLARR-GAEHLVLTSRrgPDAPGAAE----------------LVAELTALGARVTVAACDVADRD 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4252 QVEQTLQHIkRTLGPIGGVIHCAGLTDMDTLAfiRKTSDDIQRVMEPKVSGLTTLYRHVCNEPLQFFVLFSSVSAIIPel 4331
Cdd:cd08952 297 ALAALLAAL-PAGHPLTAVVHAAGVLDDGPLD--DLTPERLAEVLRAKVAGARHLDELTRDRDLDAFVLFSSIAGVWG-- 371
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1776025254 4332 SAGQADYAMANSYMDYFAEAHQKH-VPIISVQWPNWKETGMGEVTNQAY-RESGL 4384
Cdd:cd08952 372 SGGQGAYAAANAYLDALAERRRARgLPATSVAWGPWAGGGMAAGAAAERlRRRGL 426
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
1149-1638 |
1.69e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 112.05 E-value: 1.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1149 TYPYITFHELFEQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGG 1228
Cdd:PRK06710 20 SYDIQPLHKYVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1229 AYVPLDPSYPAERLEYMLEDSEV-------------------------------------------FITLTTSELVNTLS 1265
Cdd:PRK06710 100 IVVQTNPLYTERELEYQLHDSGAkvilcldlvfprvtnvqsatkiehvivtriadflpfpknllypFVQKKQSNLVVKVS 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1266 -------WNGVttallDQDWDEIAQTASDrkvltrtvtPEN-LAYVIYTSGSTGKPKGVMIPHKAL-TNFLVSMGETPG- 1335
Cdd:PRK06710 180 esetihlWNSV-----EKEVNTGVEVPCD---------PENdLALLQYTGGTTGFPKGVMLTHKNLvSNTLMGVQWLYNc 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1336 LTAEDKMLAVTTYcFDIAALE--LFLPLIKGahcYICQTEHTKDVEKLKRDIRTIKPTVMQATPATWKMLFYSGWENEEN 1413
Cdd:PRK06710 246 KEGEEVVLGVLPF-FHVYGMTavMNLSIMQG---YKMVLIPKFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1414 VK----ILCGGEALP-ETLKRYFLDTGSEAWNMFGPTETTIWSAVQRINDECSRATIGRPIANTQIYITDSQLAPV-PAG 1487
Cdd:PRK06710 322 ISsiraCISGSAPLPvEVQEKFETVTGGKLVEGYGLTESSPVTHSNFLWEKRVPGSIGVPWPDTEAMIMSLETGEAlPPG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1488 VPGELCIAGDGVAKGYYKKEELTDSRFIDNpfepgskLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLS 1567
Cdd:PRK06710 402 EIGEIVVKGPQIMKGYWNKPEETAAVLQDG-------WLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLY 474
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1776025254 1568 EHPGILECVVVADMD-----NLAAYYTAKHaNASLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSL 1638
Cdd:PRK06710 475 EHEKVQEVVTIGVPDpyrgeTVKAFVVLKE-GTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
1153-1639 |
1.81e-24 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 111.77 E-value: 1.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1153 ITFHELFEQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVP 1232
Cdd:PRK13382 43 MGPTSGFAIAAQRCPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1233 LDPSYPAERLEYMLEDSEVFITLTTSELVNTL--SWNGVTTALLDQDW-DEIAQTASDrkVLTRT-------VTPENLAY 1302
Cdd:PRK13382 123 LNTSFAGPALAEVVTREGVDTVIYDEEFSATVdrALADCPQATRIVAWtDEDHDLTVE--VLIAAhagqrpePTGRKGRV 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1303 VIYTSGSTGKPKGVMIPHKALTNFLVS-MGETPgLTAEDKMLAVT----TYCFDIAALELFLplikgaHCYICqTEHTKD 1377
Cdd:PRK13382 201 ILLTSGTTGTPKGARRSGPGGIGTLKAiLDRTP-WRAEEPTVIVApmfhAWGFSQLVLAASL------ACTIV-TRRRFD 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1378 VEKLKRDIRTIKPTVMQATPATWKMLF---------YSGweneENVKILCG-GEALPETLKRYFLDT-GSEAWNMFGPTE 1446
Cdd:PRK13382 273 PEATLDLIDRHRATGLAVVPVMFDRIMdlpaevrnrYSG----RSLRFAAAsGSRMRPDVVIAFMDQfGDVIYNNYNATE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1447 TTiWSAVQRINDecSRA---TIGRPIANTQIYITDSQLAPVPAGVPGELCIAGDGVAKGYYKKeelTDSRFIDNpfepgs 1523
Cdd:PRK13382 349 AG-MIATATPAD--LRAapdTAGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGYTSG---STKDFHDG------ 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1524 kLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMDN-----LAAYYTAKhANASLT 1598
Cdd:PRK13382 417 -FMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEqygqrLAAFVVLK-PGASAT 494
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1776025254 1599 ARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLK 1639
Cdd:PRK13382 495 PETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQ 535
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
186-451 |
1.97e-24 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.
Pssm-ID: 341250 [Multi-domain] Cd Length: 545 Bit Score: 111.54 E-value: 1.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 186 PEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQM----QGFTREDITFNWMPFDHV-------------GGIGMLH- 247
Cdd:cd05927 113 PEDLATICYTSGTTGNPKGVMLTHGNIVSNVAGVFKIleilNKINPTDVYISYLPLAHIfervvealflyhgAKIGFYSg 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 248 ----LRD-------------------VYLGCQEiNVSSETILmepLKWL-DWIDHYRASvtwapNFAFGLVTdfaeeiKD 303
Cdd:cd05927 193 dirlLLDdikalkptvfpgvprvlnrIYDKIFN-KVQAKGPL---KRKLfNFALNYKLA-----ELRSGVVR------AS 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 304 RKWD-----------LSSMRYMLNGGEAMVAKVGRRILELLephGLPadaIRPAWGMSETSSGVIFSHEF-TRAGTsddd 371
Cdd:cd05927 258 PFWDklvfnkikqalGGNVRLMLTGSAPLSPEVLEFLRVAL---GCP---VLEGYGQTECTAGATLTLPGdTSVGH---- 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 372 hfveIGSPIPGFSMRIVN------DHNELVEEGEIgrfQVSGLSVTSGYYQRPDLNESVFTEDGWFETGDLG-FLRNGRL 444
Cdd:cd05927 328 ----VGGPLPCAEVKLVDvpemnyDAKDPNPRGEV---CIRGPNVFSGYYKDPEKTAEALDEDGWLHTGDIGeWLPNGTL 400
|
....*..
gi 1776025254 445 TITGRTK 451
Cdd:cd05927 401 KIIDRKK 407
|
|
| PRK07967 |
PRK07967 |
beta-ketoacyl-ACP synthase I; |
3437-3779 |
4.27e-24 |
|
beta-ketoacyl-ACP synthase I;
Pssm-ID: 181184 [Multi-domain] Cd Length: 406 Bit Score: 108.60 E-value: 4.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3437 ALEDAGCPPQSLSGTGTGIFIGTGNTGYKDLFHRANLPIE--GHAATGhmiPSVGPNRMS--------YFLNIHGPSEPV 3506
Cdd:PRK07967 82 AIADAGLSEEQVSNPRTGLIAGSGGGSTRNQVEAADAMRGprGPKRVG---PYAVTKAMAstvsaclaTPFKIKGVNYSI 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3507 ETACSSSLVAIHRAVTAMQNGDCEMAIAGGvntilTEEAHISYS-----KAGMLSK-----DGRCKTFSADANGYVRGEG 3576
Cdd:PRK07967 159 SSACATSAHCIGNAVEQIQLGKQDIVFAGG-----GEELDWEMSclfdaMGALSTKyndtpEKASRAYDANRDGFVIAGG 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3577 VGMVMLKKLEDAERDGNHIYGVIRGTAENHGGrantltspnpkaqADLL-------VRAYRQA--GIDpSTVTYIEAHGT 3647
Cdd:PRK07967 234 GGVVVVEELEHALARGAKIYAEIVGYGATSDG-------------YDMVapsgegaVRCMQMAlaTVD-TPIDYINTHGT 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3648 GTELGDPIEINGLKAAFkelsnmrGESQPdvpdhrcGIGSVKSNIGHLELAAGISGLIKVLLQMKHKTLVKSLHCETLNP 3727
Cdd:PRK07967 300 STPVGDVKELGAIREVF-------GDKSP-------AISATKSLTGHSLGAAGVQEAIYSLLMMEHGFIAPSANIEELDP 365
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1776025254 3728 ylQLTDSPfyIVQEKQEWKSVTDCDGNelprragisSFGIGGVNAHIVIEEY 3779
Cdd:PRK07967 366 --QAAGMP--IVTETTDNAELTTVMSN---------SFGFGGTNATLVFRRY 404
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
185-555 |
4.30e-24 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 110.53 E-value: 4.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 185 SPEDLALLLLTSGSTGTPKAVMLNHRNIMSMV---KGIIQMQGFTREDITFNWMPFDHVGGIGMLHLRDVYLGCQEINVS 261
Cdd:PRK08974 204 VPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLeqaKAAYGPLLHPGKELVVTALPLYHIFALTVNCLLFIELGGQNLLIT 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 262 SETILMEPLKWLDwidHYRASVTWAPNFAF-GLVTDfaEEIKdrKWDLSSMRYMLNGGEAM---VAK-----VGRRILEl 332
Cdd:PRK08974 284 NPRDIPGFVKELK---KYPFTAITGVNTLFnALLNN--EEFQ--ELDFSSLKLSVGGGMAVqqaVAErwvklTGQYLLE- 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 333 lephglpadairpAWGMSETSSGVifsheftrAGTSDD--DHFVEIGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSV 410
Cdd:PRK08974 356 -------------GYGLTECSPLV--------SVNPYDldYYSGSIGLPVPSTEIKLVDDDGNEVPPGEPGELWVKGPQV 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 411 TSGYYQRPDLNESVFtEDGWFETGDLGFL-RNGRLTITGRTKDAIIINGINYYSHAIESAVE---ELSEIetsytAACAV 486
Cdd:PRK08974 415 MLGYWQRPEATDEVI-KDGWLATGDIAVMdEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMlhpKVLEV-----AAVGV 488
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1776025254 487 RlGQNSTDQLAIFFVTsaklNDEQMS--QLLRNIQSHVSQvigvtpeYLLPVQ---KEEIPKTAIGKIQRTQLK 555
Cdd:PRK08974 489 P-SEVSGEAVKIFVVK----KDPSLTeeELITHCRRHLTG-------YKVPKLvefRDELPKSNVGKILRRELR 550
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
1154-1639 |
4.35e-24 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 111.20 E-value: 4.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1154 TFHELFEQQAKKTPDRAAVSY--------EGQTLTYRELDERSTQLAIYLQAHGVGPD--------------------RL 1205
Cdd:PRK07529 26 STYELLSRAAARHPDAPALSFlldadpldRPETWTYAELLADVTRTANLLHSLGVGPGdvvafllpnlpethfalwggEA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1206 AGIyVDRSLDMLVG--LLAILKAGGA--YVPLDPsYP----AERLEYMLEDSEVFITLTTSELVNTLSWNGVTTALLDQ- 1276
Cdd:PRK07529 106 AGI-ANPINPLLEPeqIAELLRAAGAkvLVTLGP-FPgtdiWQKVAEVLAALPELRTVVEVDLARYLPGPKRLAVPLIRr 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1277 -------DWD-EIAQTASDRKVLTRTVTPENLAYVIYTSGSTGKPKGVMIPHKALTNFLVSMGETPGLTAEDKMLAvtty 1348
Cdd:PRK07529 184 kaharilDFDaELARQPGDRLFSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDTVFC---- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1349 cfdiaALELF----------LPLIKGAHCYICQTEHTKD----------VEKLKRDIRTIKPTVMQATpatwkMLFYSGW 1408
Cdd:PRK07529 260 -----GLPLFhvnallvtglAPLARGAHVVLATPQGYRGpgvianfwkiVERYRINFLSGVPTVYAAL-----LQVPVDG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1409 ENEENVKI-LCGGEALPETLKRYFLD-TGSEAWNMFGPTETTIWSAVQRINDECSRATIGRPIANTQIYI-----TDSQL 1481
Cdd:PRK07529 330 HDISSLRYaLCGAAPLPVEVFRRFEAaTGVRIVEGYGLTEATCVSSVNPPDGERRIGSVGLRLPYQRVRVvilddAGRYL 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1482 APVPAGVPGELCIAGDGVAKGYykkeeLTDSRFIDNPFEPGskLYRTGDMAR-------WLPGGRIEYIgridnqvkIR- 1553
Cdd:PRK07529 410 RDCAVDEVGVLCIAGPNVFSGY-----LEAAHNKGLWLEDG--WLNTGDLGRidadgyfWLTGRAKDLI--------IRg 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1554 GFRIELGDIESRLSEHPGILECVVVADMDNLA-----AYYTAKhANASLTARELRHFVKNALP---AymVPSYFIQLDHM 1625
Cdd:PRK07529 475 GHNIDPAAIEEALLRHPAVALAAAVGRPDAHAgelpvAYVQLK-PGASATEAELLAFARDHIAeraA--VPKHVRILDAL 551
|
570
....*....|....
gi 1776025254 1626 PLTPNGKIDRNSLK 1639
Cdd:PRK07529 552 PKTAVGKIFKPALR 565
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
1161-1651 |
4.94e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 110.13 E-value: 4.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1161 QQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGP-DRLAgIYVDRSLDMLVGLLAILKAGGAYVPLD-PSYP 1238
Cdd:PRK07470 15 QAARRFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKgDRIL-VHSRNCNQMFESMFAAFRLGAVWVPTNfRQTP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1239 AErLEYMLEDSE--VFI------------TLTTSELVNTLSWNGVTTALldqDWDEIAQTASDRKVLTRTVTPENLAYVI 1304
Cdd:PRK07470 94 DE-VAYLAEASGarAMIchadfpehaaavRAASPDLTHVVAIGGARAGL---DYEALVARHLGARVANAAVDHDDPCWFF 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1305 YTSGSTGKPKGVMIPHKAL----TNFLVSMgeTPGLTAEDKMLAVTtycfdiaalelflPLIKGA--HcYICQTEHTK-- 1376
Cdd:PRK07470 170 FTSGTTGRPKAAVLTHGQMafviTNHLADL--MPGTTEQDASLVVA-------------PLSHGAgiH-QLCQVARGAat 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1377 --------DVEKLKRDIRTIKPTVMQATPATWKMLFysgwENEENVK---------ILCGGEALPETLKRYFLDTGSEAW 1439
Cdd:PRK07470 234 vllpserfDPAEVWALVERHRVTNLFTVPTILKMLV----EHPAVDRydhsslryvIYAGAPMYRADQKRALAKLGKVLV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1440 NMFGPTETT-----IWSAVQRIND--ECSRATIGRPIANTQIYITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDS 1512
Cdd:PRK07470 310 QYFGLGEVTgnitvLPPALHDAEDgpDARIGTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAK 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1513 RFIDNPFepgsklyRTGDMARwLPGGRIEYI-GRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMDNL-----AA 1586
Cdd:PRK07470 390 AFRDGWF-------RTGDLGH-LDARGFLYItGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVwgevgVA 461
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1776025254 1587 YYTAKhANASLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLKnidlsgEQLKQR 1651
Cdd:PRK07470 462 VCVAR-DGAPVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVR------EELEER 519
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
1298-1635 |
5.32e-24 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 106.96 E-value: 5.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1298 ENLAYVIYTSGSTGKPKGVMIPHKALtnFLVS---MGETPGLTAEDKMLAVTTYCFDIAALELFLPLIKGAHCYI-CQTE 1373
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTF--FAVPdilQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTgGENT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1374 HTKDVEKLkrdIRTIKPTVMQATPATW-KMLFYSGWENEENVKILC---GGEALPETLKRYFLDTG-SEAWNMFGPTETT 1448
Cdd:cd17635 79 TYKSLFKI---LTTNAVTTTCLVPTLLsKLVSELKSANATVPSLRLigyGGSRAIAADVRFIEATGlTNTAQVYGLSETG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1449 IWSAVQRINDECSRATIGRPIANTQIYITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPFepgsklyRT 1528
Cdd:cd17635 156 TALCLPTDDDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLIDGWV-------NT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1529 GDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMDN-----LAAYYTAKHANASLTARELR 1603
Cdd:cd17635 229 GDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEefgelVGLAVVASAELDENAIRALK 308
|
330 340 350
....*....|....*....|....*....|..
gi 1776025254 1604 HFVKNALPAYMVPSYFIQLDHMPLTPNGKIDR 1635
Cdd:cd17635 309 HTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
4592-4934 |
8.66e-24 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 107.57 E-value: 8.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4592 VVGLSCRFPGAETLESYWSLLSEGRSSIGPIP---AERWGCKtpyYAGVIDGvsyFDPDFFLlHEEDVRAMDPQALLVLE 4668
Cdd:PRK07314 6 VTGLGAVSPLGNDVESTWKNLLAGKSGIGPIThfdTSDLAVK---IAGEVKD---FNPDDYM-SRKEARRMDRFIQYGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4669 ECLKLLYHAGYTPEEIKGKPVGVYIG---GRSQHKPDEDSLDHAKNP-----------IVtvgqNYLAANLSQFFDVRGP 4734
Cdd:PRK07314 79 AAKQAVEDAGLEITEENADRIGVIIGsgiGGLETIEEQHITLLEKGPrrvspffvpmaII----NMAAGHVSIRYGAKGP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4735 SVVVDTACSSALVGMNMAIQALRGGDIQSAIVGGVSllssDASHRLfdrrGI--------LS------KHSSfHVFDERA 4800
Cdd:PRK07314 155 NHSIVTACATGAHAIGDAARLIAYGDADVMVAGGAE----AAITPL----GIagfaaaraLStrnddpERAS-RPFDKDR 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4801 DGVVLGEGVGMVMLKTVKQALEDGDTIYAVVKAASVNNDGR--TAgPATPNLEAQKeVMKDALFKSGKKPEDISYLEANG 4878
Cdd:PRK07314 226 DGFVMGEGAGILVLEELEHAKARGAKIYAEVVGYGMTGDAYhmTA-PAPDGEGAAR-AMKLALKDAGINPEDIDYINAHG 303
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1776025254 4879 SGSIVTDLLELKAIQSVYrSGHSSPLSLGSIKPNIGHPLCAEGIASFIKVVLMLKE 4934
Cdd:PRK07314 304 TSTPAGDKAETQAIKRVF-GEHAYKVAVSSTKSMTGHLLGAAGAVEAIFSVLAIRD 358
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
186-555 |
1.56e-23 |
|
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341304 [Multi-domain] Cd Length: 450 Bit Score: 107.45 E-value: 1.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 186 PEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDHVGGI-----GMLHLRDVYLGCQEINV 260
Cdd:cd17649 93 PRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAERYGLTPGDRELQFASFNFDGAHeqllpPLICGACVVLRPDELWA 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 261 SSETILMEplkwldwIDHYRASV-TWAPNFAFGLVTDFAEEIKDRKwdlSSMRYMLNGGEAMVAKVGRRILE----LLEP 335
Cdd:cd17649 173 SADELAEM-------VRELGVTVlDLPPAYLQQLAEEADRTGDGRP---PSLRLYIFGGEALSPELLRRWLKapvrLFNA 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 336 HGlPADAIRpawgmseTSSGVIFSHEFTRAGTSdddhfVEIGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGYY 415
Cdd:cd17649 243 YG-PTEATV-------TPLVWKCEAGAARAGAS-----MPIGRPLGGRSAYILDADLNPVPVGVTGELYIGGEGLARGYL 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 416 QRPDLNESVFTEDG-------WFETGDLGFLR-NGRLTITGRTKDAIIINGINYYSHAIESAVEELSEIEtsytAACAVR 487
Cdd:cd17649 310 GRPELTAERFVPDPfgapgsrLYRTGDLARWRdDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVR----EAAVVA 385
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1776025254 488 LGQNSTDQLAIFFVTSAklnDEQMSQLLRNIQSHVSQVIgvtPEYLLP---VQKEEIPKTAIGKIQRTQLK 555
Cdd:cd17649 386 LDGAGGKQLVAYVVLRA---AAAQPELRAQLRTALRASL---PDYMVPahlVFLARLPLTPNGKLDRKALP 450
|
|
| PLN02787 |
PLN02787 |
3-oxoacyl-[acyl-carrier-protein] synthase II |
1762-2187 |
1.60e-23 |
|
3-oxoacyl-[acyl-carrier-protein] synthase II
Pssm-ID: 215421 [Multi-domain] Cd Length: 540 Bit Score: 108.91 E-value: 1.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1762 VAIIGISCEFPGAKNHDEFWENLRDGKESIAffnkeELQRFGISKeiaenadyVPAKASIEGKdrfdpSFFQ---ISPKD 1838
Cdd:PLN02787 131 VVVTGMGVVSPLGHDPDVFYNNLLEGVSGIS-----EIERFDCSQ--------FPTRIAGEIK-----SFSTdgwVAPKL 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1839 AEFMDPQLRMLLTHSWKAIEDAGYaagqipqTSVFMSASNNSYRALLP----------SDTTESLEtpdgyVSWVLAQSG 1908
Cdd:PLN02787 193 SKRMDKFMLYLLTAGKKALADGGI-------TEDVMKELDKTKCGVLIgsamggmkvfNDAIEALR-----ISYRKMNPF 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1909 TIP--------TMISHKLGLRGPSYFVHANCSSSLIGLHSAYKSLLSAESDYALVGG--ATLHTESNIGYVHQPGLNFSS 1978
Cdd:PLN02787 261 CVPfattnmgsAMLAMDLGWMGPNYSISTACATSNFCILNAANHIIRGEADVMLCGGsdAAIIPIGLGGFVACRALSQRN 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1979 DGHIKA---FDASADGMIGGEGVAVVLLKKAADAVKDGDHIYALLRGIGVNNDgADKVGFYAPSVKGQADVVQQVMNQTK 2055
Cdd:PLN02787 341 DDPTKAsrpWDMNRDGFVMGEGAGVLLLEELEHAKKRGANIYAEFLGGSFTCD-AYHMTEPHPEGAGVILCIEKALAQSG 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2056 IHPESICYVEAHGTGTKLGDPIELAALTNVYRQYTNktqfCGIGSVKTNIGHLDTAAGLAGCIKVVMSLYHQELAPSINY 2135
Cdd:PLN02787 420 VSKEDVNYINAHATSTKAGDLKEYQALMRCFGQNPE----LRVNSTKSMIGHLLGAAGAVEAIATVQAIRTGWVHPNINL 495
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1776025254 2136 KEPNPNTDLAsspFYVVDQKKTLsrEIqthRAALS-SFGLGGTNTHAIFEQFK 2187
Cdd:PLN02787 496 ENPESGVDTK---VLVGPKKERL--DI---KVALSnSFGFGGHNSSILFAPYK 540
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
1159-1640 |
1.72e-23 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 109.19 E-value: 1.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1159 FEQQAKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYP 1238
Cdd:PRK08279 43 FEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQR 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1239 AERLEYML------------EDSEVFIT----LTTSELVNTLSWNGVTTALLDQDWDEIAQTASDR-KVLTRTVTPENLA 1301
Cdd:PRK08279 123 GAVLAHSLnlvdakhlivgeELVEAFEEaradLARPPRLWVAGGDTLDDPEGYEDLAAAAAGAPTTnPASRSGVTAKDTA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1302 YVIYTSGSTGKPKGVMIPHKALTNFLVSMGETPGLTAEDKMlavttYCfdiaalelFLPL-------------IKGAHCY 1368
Cdd:PRK08279 203 FYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDVL-----YC--------CLPLyhntggtvawssvLAAGATL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1369 IcqtehtkdvekLKR---------DIRTIKPTVMQ----------ATPATWKmlfysgwENEENVKILCG----GEALPE 1425
Cdd:PRK08279 270 A-----------LRRkfsasrfwdDVRRYRATAFQyigelcryllNQPPKPT-------DRDHRLRLMIGnglrPDIWDE 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1426 TLKRYFLDTGSEAWnmfGPTETTIwsavQRINDECSRATIGR-------PIA------NTQIYITDSQ--LAPVPAGVPG 1490
Cdd:PRK08279 332 FQQRFGIPRILEFY---AASEGNV----GFINVFNFDGTVGRvplwlahPYAivkydvDTGEPVRDADgrCIKVKPGEVG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1491 ELC--IAGDGVAKGYYKKEElTDSRFIDNPFEPGSKLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSE 1568
Cdd:PRK08279 405 LLIgrITDRGPFDGYTDPEA-SEKKILRDVFKKGDAWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENALSG 483
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1776025254 1569 HPGILECVV----VADMDNLA--AYYTAkHANASLTARELRHFVKNALPAYMVPsYFIQL-DHMPLTPNGKIDRNSLKN 1640
Cdd:PRK08279 484 FPGVEEAVVygveVPGTDGRAgmAAIVL-ADGAEFDLAALAAHLYERLPAYAVP-LFVRLvPELETTGTFKYRKVDLRK 560
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
194-551 |
2.13e-23 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 104.41 E-value: 2.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 194 LTSGSTGTPKAVMLNHRN-IMSMVKGIIQMQgFTREDITFNWMPFDHVGGIGMLhLRDVYLGcQEINVSSETIlmePLKW 272
Cdd:cd17633 7 FTSGTTGLPKAYYRSERSwIESFVCNEDLFN-ISGEDAILAPGPLSHSLFLYGA-ISALYLG-GTFIGQRKFN---PKSW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 273 LDWIDHYRASVTW-APNFAFGLV-TDFAEeikdrkwdlSSMRYMLNGGEAMVAKVGRRIlellePHGLPADAIRPAWGMS 350
Cdd:cd17633 81 IRKINQYNATVIYlVPTMLQALArTLEPE---------SKIKSIFSSGQKLFESTKKKL-----KNIFPKANLIEFYGTS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 351 ETS-SGVIFSHEFTRAGTsdddhfveIGSPIPGFSMRIVNDhnelvEEGEIGRFQVSGLSVTSGYyqrpdLNESVFTEDG 429
Cdd:cd17633 147 ELSfITYNFNQESRPPNS--------VGRPFPNVEIEIRNA-----DGGEIGKIFVKSEMVFSGY-----VRGGFSNPDG 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 430 WFETGDLGFL-RNGRLTITGRTKDAIIINGINYYSHAIESAVEELSEIETsytaacAVRLGQNST--DQLAIFFVTSAKL 506
Cdd:cd17633 209 WMSVGDIGYVdEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEE------AIVVGIPDArfGEIAVALYSGDKL 282
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1776025254 507 NDEQMSQLLRniQSHVSQVIgvtPEYLLPVqkEEIPKTAIGKIQR 551
Cdd:cd17633 283 TYKQLKRFLK--QKLSRYEI---PKKIIFV--DSLPYTSSGKIAR 320
|
|
| PRK08439 |
PRK08439 |
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed |
3405-3779 |
2.41e-23 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
Pssm-ID: 236265 [Multi-domain] Cd Length: 406 Bit Score: 106.36 E-value: 2.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3405 VAEFDPLFFgISPREADYVDPQQRLLMTYVWKALEDAGCPPQSLSGTGTGIFIGTGNTGykdlfhranLP-IEGHAATgh 3483
Cdd:PRK08439 52 ITDFDPTEV-MDPKEVKKADRFIQLGLKAAREAMKDAGFLPEELDAERFGVSSASGIGG---------LPnIEKNSII-- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3484 mIPSVGPNRMSYFL-----------------NIHGPSEPVETACSSSLVAIHRAV-TAMQNGDCEMAIAGGVNTILTeeA 3545
Cdd:PRK08439 120 -CFEKGPRKISPFFipsalvnmlggfisiehGLKGPNLSSVTACAAGTHAIIEAVkTIMLGGADKMLVVGAESAICP--V 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3546 HISySKAGMLSKDGR-------CKTFSADANGYVRGEGVGMVMLKKLEDAERDGNHIYGVIRGTAENhgGRANTLTSPNP 3618
Cdd:PRK08439 197 GIG-GFAAMKALSTRnddpkkaSRPFDKDRDGFVMGEGAGALVLEEYESAKKRGAKIYAEIIGFGES--GDANHITSPAP 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3619 KAQADLLVRAYRQAGIDPstVTYIEAHGTGTELGDPIEINGLKAAFKelsnmrgeSQPDVPDhrcgIGSVKSNIGHLELA 3698
Cdd:PRK08439 274 EGPLRAMKAALEMAGNPK--IDYINAHGTSTPYNDKNETAALKELFG--------SKEKVPP----VSSTKGQIGHCLGA 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3699 AGISGLIKVLLQMKHKTLVKSLHCETLNPylqltdspfyivqekqewksvtDCDGNELP---RRAGI-----SSFGIGGV 3770
Cdd:PRK08439 340 AGAIEAVISIMAMRDGILPPTINQETPDP----------------------ECDLDYIPnvaRKAELnvvmsNSFGFGGT 397
|
....*....
gi 1776025254 3771 NAHIVIEEY 3779
Cdd:PRK08439 398 NGVVIFKKV 406
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
186-555 |
2.62e-23 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 105.26 E-value: 2.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 186 PEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDHVGGIGMLHLRDVYLGcqeinvsSETI 265
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASG-------AHVV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 266 LMEPLKWLD-------W--IDHYRasvtwaPNFAFGLVTDFAEEIK---DRkwDLSSMRYMLNGGEAMVAKVGRRIlell 333
Cdd:cd05944 74 LAGPAGYRNpglfdnfWklVERYR------ITSLSTVPTVYAALLQvpvNA--DISSLRFAMSGAAPLPVELRARF---- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 334 EPH-GLPadaIRPAWGMSETSSGVifshefTRAGTSDDDHFVEIGSPIPGFSMRIV---NDHNELVEEG--EIGRFQVSG 407
Cdd:cd05944 142 EDAtGLP---VVEGYGLTEATCLV------AVNPPDGPKRPGSVGLRLPYARVRIKvldGVGRLLRDCApdEVGEICVAG 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 408 LSVTSGYYQRpDLNESVFTEDGWFETGDLGFL-RNGRLTITGRTKDAIIINGinyysHAIESA-VEELSEIETSYTAACA 485
Cdd:cd05944 213 PGVFGGYLYT-EGNKNAFVADGWLNTGDLGRLdADGYLFITGRAKDLIIRGG-----HNIDPAlIEEALLRHPAVAFAGA 286
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 486 VRLGQNSTDQLAIFFVTSAKLNDEQMSQLLRNIQSHVSQVIGVtPEYLLPVqkEEIPKTAIGKIQRTQLK 555
Cdd:cd05944 287 VGQPDAHAGELPVAYVQLKPGAVVEEEELLAWARDHVPERAAV-PKHIEVL--EELPVTAVGKVFKPALR 353
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
1161-1731 |
3.15e-23 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 110.64 E-value: 3.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1161 QQAKKTPDRAAVSY------EGQTLTYRELDERSTQLAIYLQAHGVGPDRlAGIYVDRSLDMLVGLLAILKAGGAYVPld 1234
Cdd:PRK05691 17 RRAAQTPDRLALRFladdpgEGVVLSYRDLDLRARTIAAALQARASFGDR-AVLLFPSGPDYVAAFFGCLYAGVIAVP-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1235 pSYPAE--------RLEYMLEDSEVFITLTTSELVNTL------------SWNGVTT--ALLDQDWDEIAqtasdrkvlt 1292
Cdd:PRK05691 94 -AYPPEsarrhhqeRLLSIIADAEPRLLLTVADLRDSLlqmeelaaanapELLCVDTldPALAEAWQEPA---------- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1293 rtVTPENLAYVIYTSGSTGKPKGVMIPHKAL--TNFLVSMGETPGLTAEDKMLAVTTYCFDIAAL-ELFLPLIKGAHCYI 1369
Cdd:PRK05691 163 --LQPDDIAFLQYTSGSTALPKGVQVSHGNLvaNEQLIRHGFGIDLNPDDVIVSWLPLYHDMGLIgGLLQPIFSGVPCVL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1370 CQTEHTkdvekLKRDIR----------TI--------KPTVMQATPATWKMLFYSGWEneenvKILCGGEALPE-TLKRY 1430
Cdd:PRK05691 241 MSPAYF-----LERPLRwleaiseyggTIsggpdfayRLCSERVSESALERLDLSRWR-----VAYSGSEPIRQdSLERF 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1431 ---FLDTGSEAWNMF---GPTETTIWSA---------VQRINDEC---SRA---------TIGRPIANTQIYITDSQ-LA 1482
Cdd:PRK05691 311 aekFAACGFDPDSFFasyGLAEATLFVSggrrgqgipALELDAEAlarNRAepgtgsvlmSCGRSQPGHAVLIVDPQsLE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1483 PVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPfepGSKLYRTGDMArWLPGGRIEYIGRIDNQVKIRGFRIELGDI 1562
Cdd:PRK05691 391 VLGDNRVGEIWASGPSIAHGYWRNPEASAKTFVEHD---GRTWLRTGDLG-FLRDGELFVTGRLKDMLIVRGHNLYPQDI 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1563 ESRLSEhpgileCVVVADMDNLAAYYTAKHANASL-TARELRHFVKNALPA---------------YMVPSYFIQLD--H 1624
Cdd:PRK05691 467 EKTVER------EVEVVRKGRVAAFAVNHQGEEGIgIAAEISRSVQKILPPqaliksirqavaeacQEAPSVVLLLNpgA 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1625 MPLTPNGKIDRNSLKN------ID-------LSGEQLKQRQTSPKNIQDTVFTIWQEVLKTSDIEWDDGFFDVGGDSLLA 1691
Cdd:PRK05691 541 LPKTSSGKLQRSACRLrladgsLDsyalfpaLQAVEAAQTAASGDELQARIAAIWCEQLKVEQVAADDHFFLLGGNSIAA 620
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1776025254 1692 VTVADRIKHELSCEFSVTDLFEYSTIKNISQYITEQRMGN 1731
Cdd:PRK05691 621 TQVVARLRDELGIDLNLRQLFEAPTLAAFSAAVARQLAGG 660
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
28-437 |
3.67e-23 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 108.21 E-value: 3.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 28 PATIPEVLYRTAAELGDTkgiIYL----QPDGTEVYQSYRrlwdDGLRIVKGLRQS----GLKAKQSVILqLGDNS--QL 97
Cdd:PRK12582 48 PRSIPHLLAKWAAEAPDR---PWLaqrePGHGQWRKVTYG----EAKRAVDALAQAlldlGLDPGRPVMI-LSGNSieHA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 98 LPAFwGCVLTGVVPAPlaVPPTYAESSSGTQKLKDAWTLLdKPAVI--TDRGMHQEMLDWAKEQGL---------EGFRA 166
Cdd:PRK12582 120 LMTL-AAMQAGVPAAP--VSPAYSLMSHDHAKLKHLFDLV-KPRVVfaQSGAPFARALAALDLLDVtvvhvtgpgEGIAS 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 167 IIVEDLLS----AEADTDWHQSSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTRED---ITFNWMPFDH 239
Cdd:PRK12582 196 IAFADLAAtpptAAVAAAIAAITPDTVAKYLFTSGSTGMPKAVINTQRMMCANIAMQEQLRPREPDPpppVSLDWMPWNH 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 240 ------------VGGiGMLHLRDVYLGCQEInvsSETI--LMEPLKWldwidhYRASVtwaPnFAFGLVTDFAEEIKD-R 304
Cdd:PRK12582 276 tmggnanfngllWGG-GTLYIDDGKPLPGMF---EETIrnLREISPT------VYGNV---P-AGYAMLAEAMEKDDAlR 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 305 KWDLSSMRYMLNGGEAM------------VAKVGRRILellephglpadaIRPAWGMSETSSGVIFSHEFT-RAGtsddd 371
Cdd:PRK12582 342 RSFFKNLRLMAYGGATLsddlyermqalaVRTTGHRIP------------FYTGYGATETAPTTTGTHWDTeRVG----- 404
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1776025254 372 hfvEIGSPIPGFSMRivndhneLVEEGEIGRFQVSGLSVTSGYYQRPDLNESVFTEDGWFETGDLG 437
Cdd:PRK12582 405 ---LIGLPLPGVELK-------LAPVGDKYEVRVKGPNVTPGYHKDPELTAAAFDEEGFYRLGDAA 460
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
4733-4989 |
4.42e-23 |
|
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) Claisen-like condensation reaction. Members are share strong structural similarity, and are involved in the synthesis and degradation of fatty acids, and the production of polyketides, a diverse group of natural products.
Pssm-ID: 238201 [Multi-domain] Cd Length: 254 Bit Score: 101.75 E-value: 4.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4733 GPSVVVDTACSSALVGMNMAIQALRGGDIQSAIVGGVsllssdashrlfdrrgilskhssfhvfderaDGVVLGEGVGMV 4812
Cdd:cd00327 59 GPAYSVNQACATGLTALALAVQQVQNGKADIVLAGGS-------------------------------EEFVFGDGAAAA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4813 MLKTVKQALEDGDTIYAVVKAASVNNDGRTAGPAtPNLEAQKEVMKDALFKSGKKPEDISYLEANGSGSIVTDLLELKAI 4892
Cdd:cd00327 108 VVESEEHALRRGAHPQAEIVSTAATFDGASMVPA-VSGEGLARAARKALEGAGLTPSDIDYVEAHGTGTPIGDAVELALG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4893 QSVYRSGHSSPlslGSIKPNIGHPLCAEGIASFIKVVLMLKerrfvpflsgekemahfdqqkanitfsRALEKWTDSQPT 4972
Cdd:cd00327 187 LDPDGVRSPAV---SATLIMTGHPLGAAGLAILDELLLMLE---------------------------HEFIPPTPREPR 236
|
250
....*....|....*...
gi 1776025254 4973 AA-INCFADGGTNVHVIV 4989
Cdd:cd00327 237 TVlLLGFGLGGTNAAVVL 254
|
|
| PRK08722 |
PRK08722 |
beta-ketoacyl-ACP synthase II; |
3341-3778 |
4.45e-23 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 181539 [Multi-domain] Cd Length: 414 Bit Score: 105.47 E-value: 4.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3341 VAIVGISGRFPGAMDIDEFWKNLEEGKDSITEVpkdrwdwrEHYgnpdtDVNKTDIKWGGFIDGvaeFDPLFFgISPREA 3420
Cdd:PRK08722 6 VVVTGMGMLSPVGNTVESSWKALLAGQSGIVNI--------EHF-----DTTNFSTRFAGLVKD---FNCEEY-MSKKDA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3421 DYVDPQQRLLMTYVWKALEDAGCPPQSLSGTGTGIFIGTG-------NTGYKDLFHRANLPIEGHAATGHMIPSVGPNrM 3493
Cdd:PRK08722 69 RKMDLFIQYGIAAGIQALDDSGLEVTEENAHRIGVAIGSGigglgliEAGHQALVEKGPRKVSPFFVPSTIVNMIAGN-L 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3494 SYFLNIHGPSEPVETACSSSLVAIHRAVTAMQNGDCEMAIAGGVNTILTEEAHISYSKAGMLSKDGR-----CKTFSADA 3568
Cdd:PRK08722 148 SIMRGLRGPNIAISTACTTGLHNIGHAARMIAYGDADAMVAGGAEKASTPLGMAGFGAAKALSTRNDepqkaSRPWDKDR 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3569 NGYVRGEGVGMVMLKKLEDAERDGNHIYGVIRGTAENhgGRANTLTSPNPKAQADLLVR--AYRQAGIDPSTVTYIEAHG 3646
Cdd:PRK08722 228 DGFVLGDGAGMMVLEEYEHAKARGAKIYAELVGFGMS--GDAYHMTSPSEDGSGGALAMeaAMRDAGVTGEQIGYVNAHG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3647 TGTELGDPIEINGLKAAFKElsnmrgESQPDVPdhrcgIGSVKSNIGHLELAAG-ISGLIKVLlqmkhkTLVKSLHCETL 3725
Cdd:PRK08722 306 TSTPAGDVAEIKGIKRALGE------AGSKQVL-----VSSTKSMTGHLLGAAGsVEAIITVM------SLVDQIVPPTI 368
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1776025254 3726 NpylqlTDSPF------YIVQEKQEWKSVtdcdgnelpRRAGISSFGIGGVNAHIVIEE 3778
Cdd:PRK08722 369 N-----LDDPEegldidLVPHTARKVESM---------EYAICNSFGFGGTNGSLIFKK 413
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
48-566 |
4.95e-23 |
|
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.
Pssm-ID: 341231 [Multi-domain] Cd Length: 571 Bit Score: 107.43 E-value: 4.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 48 IIYLQPDGTEVYQ-SYRRLWDDGLRIVKGLR-QSGLKAKQSVILQLGDNSQLLPAFWGCVLTGVVPAPLAVPPTYAESSS 125
Cdd:cd05905 2 YTLLDSKGKEATTlTWGKLLSRAEKIAAVLQkKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 126 --GTQKLKDAWTlldkpAVITDRGmHQEMLDWAKEQGL----EGFRAIIVEDLLS---AEADTDWHQSSP---EDLALLL 193
Cdd:cd05905 82 llGTCKVRVALT-----VEACLKG-LPKKLLKSKTAAEiakkKGWPKILDFVKIPkskRSKLKKWGPHPPtrdGDTAYIE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 194 LTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWmpFDHVGGIGMLH--LRDVYLGCQEINVSSETILMEPLK 271
Cdd:cd05905 156 YSFSSDGSLSGVAVSHSSLLAHCRALKEACELYESRPLVTV--LDFKSGLGLWHgcLLSVYSGHHTILIPPELMKTNPLL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 272 WLDWIDHYRASVTWAP----NFAFGLVTDFAEEIKDRKWDLSSMRyMLnggeaMVAKVGR-------RILELLEPHGLPA 340
Cdd:cd05905 234 WLQTLSQYKVRDAYVKlrtlHWCLKDLSSTLASLKNRDVNLSSLR-MC-----MVPCENRprisscdSFLKLFQTLGLSP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 341 DAI----------RPAW-GMSETSSG-VIFS-----HEFTRAGTSDDDHFV---EIGSPIPGFSMRIVN-DHNELVEEGE 399
Cdd:cd05905 308 RAVstefgtrvnpFICWqGTSGPEPSrVYLDmralrHGVVRLDERDKPNSLplqDSGKVLPGAQVAIVNpETKGLCKDGE 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 400 IGRFQVSGLSVTSGYYQRPDLNESVF------------TEDGWFETGDLGFLRNGRLT-----------ITGRTKDAIII 456
Cdd:cd05905 388 IGEIWVNSPANASGYFLLDGETNDTFkvfpstrlstgiTNNSYARTGLLGFLRPTKCTdlnveehdllfVVGSIDETLEV 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 457 NGINYYSHAIESAVEELSeietSYTAACAVRlgqnSTDQLAIFFVTSAKLNDEQMSQLLRNIQSHVSQVIGVTPEYLLPV 536
Cdd:cd05905 468 RGLRHHPSDIEATVMRVH----PYRGRCAVF----SITGLVVVVAEQPPGSEEEALDLVPLVLNAILEEHQVIVDCVALV 539
|
570 580 590
....*....|....*....|....*....|
gi 1776025254 537 QKEEIPKTAIGKIQRTQLKTSFENGEFDHL 566
Cdd:cd05905 540 PPGSLPKNPLGEKQRMEIRQAFLAGKLHPI 569
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
58-452 |
6.48e-23 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.
Pssm-ID: 341294 [Multi-domain] Cd Length: 507 Bit Score: 106.53 E-value: 6.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 58 VYQSYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNSQLLPAFWGCVLTGVVPAPLavpptYAEsssgtqklkdawtlL 137
Cdd:cd17639 4 KYMSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTV-----YAT--------------L 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 138 DKPAVITdrGMHQEmldwakeqgleGFRAIIvedllsaeadTDwhqSSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVK 217
Cdd:cd17639 65 GEDALIH--SLNET-----------ECSAIF----------TD---GKPDDLACIMYTSGSTGNPKGVMLTHGNLVAGIA 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 218 GIIQM--QGFTREDITFNWMPFDHV------------GG-IGMLHLR----DVYLGCQ-EINVSSETILME-PLKWldwi 276
Cdd:cd17639 119 GLGDRvpELLGPDDRYLAYLPLAHIfelaaenvclyrGGtIGYGSPRtltdKSKRGCKgDLTEFKPTLMVGvPAIW---- 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 277 DHYR----ASVTWAPNFAFGLVtDFAEEIKDR--KWDLSSM------------------RYMLNGGEAMVAKVGRRILEL 332
Cdd:cd17639 195 DTIRkgvlAKLNPMGGLKRTLF-WTAYQSKLKalKEGPGTPlldelvfkkvraalggrlRYMLSGGAPLSADTQEFLNIV 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 333 LEPhglpadaIRPAWGMSETSSGvifsheftrAGTSDDDHFV--EIGSPIPGFSMRIVNdhnelVEE-----------GE 399
Cdd:cd17639 274 LCP-------VIQGYGLTETCAG---------GTVQDPGDLEtgRVGPPLPCCEIKLVD-----WEEggystdkppprGE 332
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1776025254 400 IgrfQVSGLSVTSGYYQRPDLNESVFTEDGWFETGDLG-FLRNGRLTITGRTKD 452
Cdd:cd17639 333 I---LIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGeFHPDGTLKIIDRKKD 383
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
184-555 |
7.84e-23 |
|
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341308 [Multi-domain] Cd Length: 433 Bit Score: 105.08 E-value: 7.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 184 SSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKgiiqmqgftreditfnWMPFD-HVG-GIGMLHLRDVYLGCQeINVS 261
Cdd:cd17653 102 DSPDDLAYIIFTSGSTGIPKGVMVPHRGVLNYVS----------------QPPARlDVGpGSRVAQVLSIAFDAC-IGEI 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 262 SETI-------LMEPLKwlDWIDHYRaSVTwapnfAFGLVTDFAEEIKDRkwDLSSMRYMLNGGEAMVAKV------GRR 328
Cdd:cd17653 165 FSTLcnggtlvLADPSD--PFAHVAR-TVD-----ALMSTPSILSTLSPQ--DFPNLKTIFLGGEAVPPSLldrwspGRR 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 329 ILEllephglpadairpAWGMSETSsgVIFSHEFTRAGTsdddhFVEIGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGL 408
Cdd:cd17653 235 LYN--------------AYGPTECT--ISSTMTELLPGQ-----PVTIGKPIPNSTCYILDADLQPVPEGVVGEICISGV 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 409 SVTSGYYQRPDLNESVFTEDGW------FETGDLGFL-RNGRLTITGRTKDAIIING--INYYshAIESAVEELSEIETS 479
Cdd:cd17653 294 QVARGYLGNPALTASKFVPDPFwpgsrmYRTGDYGRWtEDGGLEFLGREDNQVKVRGfrINLE--EIEEVVLQSQPEVTQ 371
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1776025254 480 YTAacavrlgQNSTDQLaIFFVTSAKLNDEQMSQLLRNI--QSHVSQVIgvtpeyllpVQKEEIPKTAIGKIQRTQLK 555
Cdd:cd17653 372 AAA-------IVVNGRL-VAFVTPETVDVDGLRSELAKHlpSYAVPDRI---------IALDSFPLTANGKVDRKALR 432
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1177-1578 |
8.60e-23 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 105.62 E-value: 8.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1177 QTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLEDSE--VFIt 1254
Cdd:cd05910 1 SRLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAEpdAFI- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1255 lttselvntlswnGVTTALLDqdwdeiaqtasdrkvltrtvtpenlAYVIYTSGSTGKPKGVMIPHKALTNFLVSMGETP 1334
Cdd:cd05910 80 -------------GIPKADEP-------------------------AAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLY 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1335 GLTAEDKMLAvttyCFDIAAleLFLPLIkGAHCYICQTEHTK----DVEKLKRDIRTIKPTVMQATPATWKMLFYSGWEN 1410
Cdd:cd05910 122 GIRPGEVDLA----TFPLFA--LFGPAL-GLTSVIPDMDPTRparaDPQKLVGAIRQYGVSIVFGSPALLERVARYCAQH 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1411 EENV----KILCGGEALP----ETLKRyFLDTGSEAWNMFGPTETTIWSAVQRINDECSRAT---------IGRPIANTQ 1473
Cdd:cd05910 195 GITLpslrRVLSAGAPVPialaARLRK-MLSDEAEILTPYGATEALPVSSIGSRELLATTTAatsggagtcVGRPIPGVR 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1474 ---IYITDSQLAP------VPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPFEpgSKLYRTGDMARWLPGGRIEYIG 1544
Cdd:cd05910 274 vriIEIDDEPIAEwddtleLPRGEIGEITVTGPTVTPTYVNRPVATALAKIDDNSE--GFWHRMGDLGYLDDEGRLWFCG 351
|
410 420 430
....*....|....*....|....*....|....
gi 1776025254 1545 RIDNQVKIRGFRIELGDIESRLSEHPGILECVVV 1578
Cdd:cd05910 352 RKAHRVITTGGTLYTEPVERVFNTHPGVRRSALV 385
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
176-559 |
1.12e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 105.74 E-value: 1.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 176 EADTDWHQSSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDHVGGIGMLHLRDVYLG- 254
Cdd:PRK06145 138 LEIPPQAAVAPTDLVRLMYTSGTTDRPKGVMHSYGNLHWKSIDHVIALGLTASERLLVVGPLYHVGAFDLPGIAVLWVGg 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 255 --CQEINVSSETILMEplkwldwIDHYRASVTW-APNFAFGLVTdfaeeIKDR-KWDLSSMRYMLNGGEAMVAKVGRRIL 330
Cdd:PRK06145 218 tlRIHREFDPEAVLAA-------IERHRLTCAWmAPVMLSRVLT-----VPDRdRFDLDSLAWCIGGGEKTPESRIRDFT 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 331 ELLEpHGLPADairpAWGMSETSSGVIF---SHEFTRAGTSdddhfveiGSPIPGFSMRIVNDHNELVEEGEIGRFQVSG 407
Cdd:PRK06145 286 RVFT-RARYID----AYGLTETCSGDTLmeaGREIEKIGST--------GRALAHVEIRIADGAGRWLPPNMKGEICMRG 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 408 LSVTSGYYQRPDLNESVFTeDGWFETGDLGFL-RNGRLTITGRTKDAIIINGINYYSHAIESAVEELSEI-ETSYTAACA 485
Cdd:PRK06145 353 PKVTKGYWKDPEKTAEAFY-GDWFRSGDVGYLdEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVaEAAVIGVHD 431
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1776025254 486 VRLGQNstdqlaiffVTSAKLNDEQMSQLLRNIQSHVSQVIGV--TPEYLlpVQKEEIPKTAIGKIQRTQLKTSFE 559
Cdd:PRK06145 432 DRWGER---------ITAVVVLNPGATLTLEALDRHCRQRLASfkVPRQL--KVRDELPRNPSGKVLKRVLRDELN 496
|
|
| PRK08722 |
PRK08722 |
beta-ketoacyl-ACP synthase II; |
4590-4984 |
1.34e-22 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 181539 [Multi-domain] Cd Length: 414 Bit Score: 104.31 E-value: 1.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4590 IAVVGLSCRFPGAETLESYWSLLSEGRSSIGPIPAERWGCKTPYYAGVIDGvsyFDPDFFLlHEEDVRAMDPQALLVLEE 4669
Cdd:PRK08722 6 VVVTGMGMLSPVGNTVESSWKALLAGQSGIVNIEHFDTTNFSTRFAGLVKD---FNCEEYM-SKKDARKMDLFIQYGIAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4670 CLKLLYHAGYTPEEIKGKPVGVYIGG--------RSQHK------PDEDSLDHAKNPIVtvgqNYLAANLSQFFDVRGPS 4735
Cdd:PRK08722 82 GIQALDDSGLEVTEENAHRIGVAIGSgigglgliEAGHQalvekgPRKVSPFFVPSTIV----NMIAGNLSIMRGLRGPN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4736 VVVDTACSSALVGMNMAIQALRGGDIQSAIVGGVSLLSSDASHRLFDRRGILSK-----HSSFHVFDERADGVVLGEGVG 4810
Cdd:PRK08722 158 IAISTACTTGLHNIGHAARMIAYGDADAMVAGGAEKASTPLGMAGFGAAKALSTrndepQKASRPWDKDRDGFVLGDGAG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4811 MVMLKTVKQALEDGDTIYAVVKAASVNNDGRTAGPATPNLEAQKEVMKDALFKSGKKPEDISYLEANGSGSIVTDLLELK 4890
Cdd:PRK08722 238 MMVLEEYEHAKARGAKIYAELVGFGMSGDAYHMTSPSEDGSGGALAMEAAMRDAGVTGEQIGYVNAHGTSTPAGDVAEIK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4891 AIQSVYRSGHSSPLSLGSIKPNIGHPLCAEGIASFIKVVLMLKERRFVPFLSGEKEmahfdQQKANITFSRALEKWTDSQ 4970
Cdd:PRK08722 318 GIKRALGEAGSKQVLVSSTKSMTGHLLGAAGSVEAIITVMSLVDQIVPPTINLDDP-----EEGLDIDLVPHTARKVESM 392
|
410
....*....|....
gi 1776025254 4971 PTAAINCFADGGTN 4984
Cdd:PRK08722 393 EYAICNSFGFGGTN 406
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
183-557 |
1.41e-22 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 106.11 E-value: 1.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 183 QSSPEDLALLLLTSGSTGTPKAVMLNHRNI---MSMVKGIIQMQGFTRE--DITFNWMPFDHVGGI---GMLHLRdvYLG 254
Cdd:PRK08751 204 QIEPDDIAFLQYTGGTTGVAKGAMLTHRNLvanMQQAHQWLAGTGKLEEgcEVVITALPLYHIFALtanGLVFMK--IGG 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 255 CQEI--NVSSETILMEPLKwldwidHYRASVTWAPNFAFG--LVTDFAEEIkdrkwDLSSMRYMLNGGEAMVAKVGRRIL 330
Cdd:PRK08751 282 CNHLisNPRDMPGFVKELK------KTRFTAFTGVNTLFNglLNTPGFDQI-----DFSSLKMTLGGGMAVQRSVAERWK 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 331 ELLephGLPadaIRPAWGMSETSSGVIFSheftraGTSDDDHFVEIGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSV 410
Cdd:PRK08751 351 QVT---GLT---LVEAYGLTETSPAACIN------PLTLKEYNGSIGLPIPSTDACIKDDAGTVLAIGEIGELCIKGPQV 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 411 TSGYYQRPDLNESVFTEDGWFETGDLGFL-RNGRLTITGRTKDAIIINGINYYSHAIESAVEELSEIETsyTAACAVRLG 489
Cdd:PRK08751 419 MKGYWKRPEETAKVMDADGWLHTGDIARMdEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLE--VAAVGVPDE 496
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1776025254 490 QNSTDQLAIFFVTSAKLNDEQMSQLLRniqshvSQVIGVTPEYLLPVQKeEIPKTAIGKIQRTQLKTS 557
Cdd:PRK08751 497 KSGEIVKVVIVKKDPALTAEDVKAHAR------ANLTGYKQPRIIEFRK-ELPKTNVGKILRRELRDA 557
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
1154-1639 |
1.75e-22 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 105.15 E-value: 1.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1154 TFHELFEQQAKKTPDRAAVSYEG-----QTLTYRELDERSTQLAIYLQAHGVGP-DRLAgIYVDRSLDMLVGLLAILKAG 1227
Cdd:PRK08008 8 HLRQMWDDLADVYGHKTALIFESsggvvRRYSYLELNEEINRTANLFYSLGIRKgDKVA-LHLDNCPEFIFCWFGLAKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1228 GAYVPLDPSYPAERLEYMLEDSEVFITLTTSELV-----------NTLSWNGVTTALLDQ-----DWDEIAQTASDRKVL 1291
Cdd:PRK08008 87 AIMVPINARLLREESAWILQNSQASLLVTSAQFYpmyrqiqqedaTPLRHICLTRVALPAddgvsSFTQLKAQQPATLCY 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1292 TRTVTPENLAYVIYTSGSTGKPKGVMIPHkalTNFLVSMGETP---GLTAEDKMLAVTTYC---FDIAALelfLPLIKGA 1365
Cdd:PRK08008 167 APPLSTDDTAEILFTSGTTSRPKGVVITH---YNLRFAGYYSAwqcALRDDDVYLTVMPAFhidCQCTAA---MAAFSAG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1366 HCYICqtehtkdVEKLK-----RDIRTIKPTVMQATPATWKMLFY---SGWENEENVKILCGGEALPETLKRYFLDT-GS 1436
Cdd:PRK08008 241 ATFVL-------LEKYSarafwGQVCKYRATITECIPMMIRTLMVqppSANDRQHCLREVMFYLNLSDQEKDAFEERfGV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1437 EAWNMFGPTETTIWSAVQRINDECSRATIGRPIANTQIYITDSQLAPVPAGVPGELCI---AGDGVAKGYYKKEELTDSr 1513
Cdd:PRK08008 314 RLLTSYGMTETIVGIIGDRPGDKRRWPSIGRPGFCYEAEIRDDHNRPLPAGEIGEICIkgvPGKTIFKEYYLDPKATAK- 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1514 fidnPFEPGSKLYrTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVV--VADM--DNLAAYYT 1589
Cdd:PRK08008 393 ----VLEADGWLH-TGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVvgIKDSirDEAIKAFV 467
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1590 AKHANASLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLK 1639
Cdd:PRK08008 468 VLNEGETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
18-555 |
2.17e-22 |
|
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341297 [Multi-domain] Cd Length: 532 Bit Score: 105.30 E-value: 2.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 18 GEPLHisEKQPATIPEVLYRTAAELGDTKGIIYLQPDGTEVYQSYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNSQL 97
Cdd:cd17642 5 PGPFY--PLEDGTAGEQLHKAMKRYASVPGTIAFTDAHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 98 LPAFWGCVLTGVVPAPLAVppTYAE-----------------SSSGTQKL---KDAWTLLDKPAV---ITDRGMHQEMLD 154
Cdd:cd17642 83 FLPVIAGLFIGVGVAPTND--IYNEreldhslniskptivfcSKKGLQKVlnvQKKLKIIKTIIIldsKEDYKGYQCLYT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 155 WAKEQGLEGFRaiiVEDLLSAEADTDwhqsspEDLALLLLTSGSTGTPKAVMLNHRNI---MSMVKGIIQMQGFTREDIT 231
Cdd:cd17642 161 FITQNLPPGFN---EYDFKPPSFDRD------EQVALIMNSSGSTGLPKGVQLTHKNIvarFSHARDPIFGNQIIPDTAI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 232 FNWMPFDHvgGIGMLHLRDvYLGCqeinvSSETILM---EPLKWLDWIDHYRASVTW--APNFAFglvtdFAEEIKDRKW 306
Cdd:cd17642 232 LTVIPFHH--GFGMFTTLG-YLIC-----GFRVVLMykfEEELFLRSLQDYKVQSALlvPTLFAF-----FAKSTLVDKY 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 307 DLSSMRYMLNGGEAMVAKVGRRILELLephGLPadAIRPAWGMSETSSGVIFSHE-FTRAGTSdddhfveiGSPIPGFSM 385
Cdd:cd17642 299 DLSNLHEIASGGAPLSKEVGEAVAKRF---KLP--GIRQGYGLTETTSAILITPEgDDKPGAV--------GKVVPFFYA 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 386 RIVN-DHNELVEEGEIGRFQVSGLSVTSGYYQRPDLNESVFTEDGWFETGDLGFLRN-GRLTITGRTKDAIIINGINYYS 463
Cdd:cd17642 366 KVVDlDTGKTLGPNERGELCVKGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYDEdGHFFIVDRLKSLIKYKGYQVPP 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 464 HAIES-----------AVEELSEIETSYTAACAVRL--GQNSTDQLAIFFVTSAKLNdeqmSQLLRniqshvSQVIGVtp 530
Cdd:cd17642 446 AELESillqhpkifdaGVAGIPDEDAGELPAAVVVLeaGKTMTEKEVMDYVASQVST----AKRLR------GGVKFV-- 513
|
570 580
....*....|....*....|....*
gi 1776025254 531 eyllpvqkEEIPKTAIGKIQRTQLK 555
Cdd:cd17642 514 --------DEVPKGLTGKIDRRKIR 530
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
171-559 |
2.64e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 105.12 E-value: 2.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 171 DLLSAEAD----TDWHQSSPEDLALLLLTSGSTGTPKAVMLNHRN-IMSMVKGIIQMQGFTREDITFNWMPFDHVGG--I 243
Cdd:PRK06178 189 DLLPALRActapVPLPPPALDALAALNYTGGTTGMPKGCEHTQRDmVYTAAAAYAVAVVGGEDSVFLSFLPEFWIAGenF 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 244 GMLHlrDVYLGCQeinvsseTILM---EPLKWLDWIDHYRASVTwapnfafGLVTDFAEEIKD----RKWDLSSMRymln 316
Cdd:PRK06178 269 GLLF--PLFSGAT-------LVLLarwDAVAFMAAVERYRVTRT-------VMLVDNAVELMDhprfAEYDLSSLR---- 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 317 ggEAMVAKVGRRilelLEP------HGLPADAIRPA-WGMSETSSgvifSHEFTrAGTSDDDH-------FVeiGSPIPG 382
Cdd:PRK06178 329 --QVRVVSFVKK----LNPdyrqrwRALTGSVLAEAaWGMTETHT----CDTFT-AGFQDDDFdllsqpvFV--GLPVPG 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 383 FSMRIVN-DHNELVEEGEIGRFQVSGLSVTSGYYQRPDLNESVFtEDGWFETGDLG-FLRNGRLTITGRTKDAIIINGIN 460
Cdd:PRK06178 396 TEFKICDfETGELLPLGAEGEIVVRTPSLLKGYWNKPEATAEAL-RDGWLHTGDIGkIDEQGFLHYLGRRKEMLKVNGMS 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 461 YYSHAIESAVEELSEIEtsytaACAVrLGQNSTD--QLAIFFVT---SAKLNDEQMSQLLRNiQSHVSQVigvtPE-YLL 534
Cdd:PRK06178 475 VFPSEVEALLGQHPAVL-----GSAV-VGRPDPDkgQVPVAFVQlkpGADLTAAALQAWCRE-NMAVYKV----PEiRIV 543
|
410 420
....*....|....*....|....*
gi 1776025254 535 pvqkEEIPKTAIGKIQRTQLKTSFE 559
Cdd:PRK06178 544 ----DALPMTATGKVRKQDLQALAE 564
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
185-555 |
3.95e-22 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 104.72 E-value: 3.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 185 SPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVkgiIQMQ-----GFTRED-----ITFNWMPFDHV-------------G 241
Cdd:PRK07059 202 GPDDVAFLQYTGGTTGVSKGATLLHRNIVANV---LQMEawlqpAFEKKPrpdqlNFVCALPLYHIfaltvcgllgmrtG 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 242 GIGML--HLRDVylgcqeinvsseTILMEPLKwldwidHYRASVTWAPNFAF-GLVT--DFaeeikdRKWDLSSMRYMLN 316
Cdd:PRK07059 279 GRNILipNPRDI------------PGFIKELK------KYQVHIFPAVNTLYnALLNnpDF------DKLDFSKLIVANG 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 317 GGEAMVAKVGRRILELLephGLPadaIRPAWGMSETSSGVIfsheftrAGTSDDDHFV-EIGSPIPGFSMRIVNDHNELV 395
Cdd:PRK07059 335 GGMAVQRPVAERWLEMT---GCP---ITEGYGLSETSPVAT-------CNPVDATEFSgTIGLPLPSTEVSIRDDDGNDL 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 396 EEGEIGRFQVSGLSVTSGYYQRPDLNESVFTEDGWFETGDLGFL-RNGRLTITGRTKDAIIINGINYYSHAIESAVEELS 474
Cdd:PRK07059 402 PLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMdERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHP 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 475 EI-EtsyTAACAVRlGQNSTDQLAIFFVTS-AKLNDEQmsqllrnIQSHV-SQVIGvtpeYLLPVQKE---EIPKTAIGK 548
Cdd:PRK07059 482 GVlE---VAAVGVP-DEHSGEAVKLFVVKKdPALTEED-------VKAFCkERLTN----YKRPKFVEfrtELPKTNVGK 546
|
....*..
gi 1776025254 549 IQRTQLK 555
Cdd:PRK07059 547 ILRRELR 553
|
|
| YqjQ |
COG0300 |
Short-chain dehydrogenase [General function prediction only]; |
2843-3078 |
4.45e-22 |
|
Short-chain dehydrogenase [General function prediction only];
Pssm-ID: 440069 [Multi-domain] Cd Length: 252 Bit Score: 98.79 E-value: 4.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2843 MPWRDeGVYLITGGAGSLGLLFAKEIANRtGRsTIVLTGRSvlsEDKENEL-EALRSIGAEVVYREADVSDQHAVHHLFE 2921
Cdd:COG0300 1 MSLTG-KTVLITGASSGIGRALARALAAR-GA-RVVLVARD---AERLEALaAELRAAGARVEVVALDVTDPDAVAALAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2922 EIKERYGTLNGIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSGLLHvdeCSKDF-PL------DFFIFFSSVSGCLGNAGQ 2994
Cdd:COG0300 75 AVLARFGPIDVLVNNAGVGGGGPFEELDLEDLRRVFEVNVFGPVR---LTRALlPLmrargrGRIVNVSSVAGLRGLPGM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2995 ADYAAANSFMDAFAEyrrSLAASKKRFG---STISFNW---PLWEEGGMQVGAEdekrmlkttgmvPMPTDSGLKAFYQG 3068
Cdd:COG0300 152 AAYAASKAALEGFSE---SLRAELAPTGvrvTAVCPGPvdtPFTARAGAPAGRP------------LLSPEEVARAILRA 216
|
250
....*....|
gi 1776025254 3069 IASDKPQVFV 3078
Cdd:COG0300 217 LERGRAEVYV 226
|
|
| YqjQ |
COG0300 |
Short-chain dehydrogenase [General function prediction only]; |
4174-4373 |
5.64e-22 |
|
Short-chain dehydrogenase [General function prediction only];
Pssm-ID: 440069 [Multi-domain] Cd Length: 252 Bit Score: 98.40 E-value: 5.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4174 LITGGTRGIGLLCARHFAECyGVKkLVLTGREqlppreewarfktsntslAEKIQAVR-ELEAKGVQVEMLSLTLSDDAQ 4252
Cdd:COG0300 9 LITGASSGIGRALARALAAR-GAR-VVLVARD------------------AERLEALAaELRAAGARVEVVALDVTDPDA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4253 VEQTLQHIKRTLGPIGGVIHCAGLtdMDTLAFIRKTSDDIQRVMEPKVSGLTTLYRHVcnepLQFF--------VLFSSV 4324
Cdd:COG0300 69 VAALAEAVLARFGPIDVLVNNAGV--GGGGPFEELDLEDLRRVFEVNVFGPVRLTRAL----LPLMrargrgriVNVSSV 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1776025254 4325 SAIIPelSAGQADYAMANSYMDYFAEA-----HQKHVPIISVQwPNWKETGMGE 4373
Cdd:COG0300 143 AGLRG--LPGMAAYAASKAALEGFSESlraelAPTGVRVTAVC-PGPVDTPFTA 193
|
|
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
3509-3776 |
6.65e-22 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 101.28 E-value: 6.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3509 ACSSSLVAIHRAVTAMQNGDCEMAIAGGVNTILTEEAHISYSKAGMLSKDGrCKTFSADANGYVRGEGVGMVMLKKLEDA 3588
Cdd:PRK05952 145 ACATGLWAIAQGVELIQTGQCQRVIAGAVEAPITPLTLAGFQQMGALAKTG-AYPFDRQREGLVLGEGGAILVLESAELA 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3589 ERDGNHIYGVIRG---TAENHGGRAntlTSPNPKAQADLLVRAYRQAGIDPSTVTYIEAHGTGTELGDPIEINGLKAAFK 3665
Cdd:PRK05952 224 QKRGAKIYGQILGfglTCDAYHMSA---PEPDGKSAIAAIQQCLARSGLTPEDIDYIHAHGTATRLNDQREANLIQALFP 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3666 elsnmrgesqpdvpdHRCGIGSVKSNIGHLELAAGISGLIKVLLQMKHKTLVKSLHCETlnPYLQLTdspfyIVQEkqew 3745
Cdd:PRK05952 301 ---------------HRVAVSSTKGATGHTLGASGALGVAFSLLALRHQQLPPCVGLQE--PEFDLN-----FVRQ---- 354
|
250 260 270
....*....|....*....|....*....|....*.
gi 1776025254 3746 ksvtdcdgnelPRRAGIS-----SFGIGGVNAHIVI 3776
Cdd:PRK05952 355 -----------AQQSPLQnvlclSFGFGGQNAAIAL 379
|
|
| PLN02787 |
PLN02787 |
3-oxoacyl-[acyl-carrier-protein] synthase II |
3322-3779 |
8.33e-22 |
|
3-oxoacyl-[acyl-carrier-protein] synthase II
Pssm-ID: 215421 [Multi-domain] Cd Length: 540 Bit Score: 103.52 E-value: 8.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3322 QPIiAKAERNKKQAADFEPVAIVGISGRFPGAMDIDEFWKNLEEGKDSITEVpkDRWDWREHYGNPDTDVNK--TDiKWg 3399
Cdd:PLN02787 113 QPE-KEVETKKKPLTKQRRVVVTGMGVVSPLGHDPDVFYNNLLEGVSGISEI--ERFDCSQFPTRIAGEIKSfsTD-GW- 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3400 gfidgvaefdplffgISPREADYVDPQQRLLMTYVWKALEDAGCPPQ---SLSGTGTGIFIGTGNTGYKdLFHRA--NLP 3474
Cdd:PLN02787 188 ---------------VAPKLSKRMDKFMLYLLTAGKKALADGGITEDvmkELDKTKCGVLIGSAMGGMK-VFNDAieALR 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3475 IEGHAATGHMIPSVGPNRMSYFLNIH----GPSEPVETACSSSLVAIHRAVTAMQNGDCEMAIAGGvntilTEEAHISYS 3550
Cdd:PLN02787 252 ISYRKMNPFCVPFATTNMGSAMLAMDlgwmGPNYSISTACATSNFCILNAANHIIRGEADVMLCGG-----SDAAIIPIG 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3551 KAGMLSkdgrCKTFS--------------ADANGYVRGEGVGMVMLKKLEDAERDGNHIYgvirgtAENHGGR----ANT 3612
Cdd:PLN02787 327 LGGFVA----CRALSqrnddptkasrpwdMNRDGFVMGEGAGVLLLEELEHAKKRGANIY------AEFLGGSftcdAYH 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3613 LTSPNPKAQADLLV--RAYRQAGIDPSTVTYIEAHGTGTELGDPIEINGLKAAFKELSNMRgesqpdvpdhrcgIGSVKS 3690
Cdd:PLN02787 397 MTEPHPEGAGVILCieKALAQSGVSKEDVNYINAHATSTKAGDLKEYQALMRCFGQNPELR-------------VNSTKS 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3691 NIGHLELAAGISGLIKVLLQMKHKTLVKSLHCEtlNPYlQLTDSPFYIVQEKQewksvtdcdgnELPRRAGIS-SFGIGG 3769
Cdd:PLN02787 464 MIGHLLGAAGAVEAIATVQAIRTGWVHPNINLE--NPE-SGVDTKVLVGPKKE-----------RLDIKVALSnSFGFGG 529
|
490
....*....|
gi 1776025254 3770 VNAHIVIEEY 3779
Cdd:PLN02787 530 HNSSILFAPY 539
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
187-558 |
9.26e-22 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 100.50 E-value: 9.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 187 EDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTReditfNW---MPFDHVGGIGMLhLRDVYLGCQ--EINVS 261
Cdd:PRK07824 35 DDVALVVATSGTTGTPKGAMLTAAALTASADATHDRLGGPG-----QWllaLPAHHIAGLQVL-VRSVIAGSEpvELDVS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 262 SEtilMEPLKWLDWIDHYRASVTWApnfafGLV-TDFAEEIKDRKW--DLSSMRYMLNGGEAMVAKVGRRILELlephGL 338
Cdd:PRK07824 109 AG---FDPTALPRAVAELGGGRRYT-----SLVpMQLAKALDDPAAtaALAELDAVLVGGGPAPAPVLDAAAAA----GI 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 339 PadaIRPAWGMSETSSGVIFSheftragtsdddhfveiGSPIPGFSMRIVNdhnelveegeiGRFQVSGLSVTSGYYQRP 418
Cdd:PRK07824 177 N---VVRTYGMSETSGGCVYD-----------------GVPLDGVRVRVED-----------GRIALGGPTLAKGYRNPV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 419 DlnESVFTEDGWFETGDLGFLRNGRLTITGRTKDAIIINGINYYSHAIESAVEELSEIetsytAACAV------RLGQNs 492
Cdd:PRK07824 226 D--PDPFAEPGWFRTDDLGALDDGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAV-----ADCAVfglpddRLGQR- 297
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1776025254 493 tdqlaiffVTSAKLNDEQMSQLLRNIQSHVSQVIGVT--PEYLLPVqkEEIPKTAIGKIQRTQLKTSF 558
Cdd:PRK07824 298 --------VVAAVVGDGGPAPTLEALRAHVARTLDRTaaPRELHVV--DELPRRGIGKVDRRALVRRF 355
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
173-676 |
9.49e-22 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 105.42 E-value: 9.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 173 LSAEADTDWHQSS---------PEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDHVG-G 242
Cdd:PRK12316 4671 LALDRDEDWEGFPahdpavrlhPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGsH 4750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 243 IGMLHLrdvyLGCQEINVSSETILMEPLKWLDWIDHYRASVTWAPNFAFGLVTDFAEeikdRKWDLSSMRYMLNGGEAMV 322
Cdd:PRK12316 4751 EGLYHP----LINGASVVIRDDSLWDPERLYAEIHEHRVTVLVFPPVYLQQLAEHAE----RDGEPPSLRVYCFGGEAVA 4822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 323 AKVGRRILELLEPhglpaDAIRPAWGMSETSsgVIFSHEFTRAGTSDDDHFVEIGSPIPGFSMRIVNDHNELVEEGEIGR 402
Cdd:PRK12316 4823 QASYDLAWRALKP-----VYLFNGYGPTETT--VTVLLWKARDGDACGAAYMPIGTPLGNRSGYVLDGQLNPLPVGVAGE 4895
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 403 FQVSGLSVTSGYYQRPDLNESVFTEDGW-------FETGDLGFLR-NGRLTITGRTKDAIIINGINYyshaiesaveELS 474
Cdd:PRK12316 4896 LYLGGEGVARGYLERPALTAERFVPDPFgapggrlYRTGDLARYRaDGVIDYLGRVDHQVKIRGFRI----------ELG 4965
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 475 EIETSYTAACAVR----LGQNST--DQLAIFFV--TSAKLNDEQMSQLLRN-IQSHVSQVIgvtPEYLLPVQ---KEEIP 542
Cdd:PRK12316 4966 EIEARLREHPAVReavvIAQEGAvgKQLVGYVVpqDPALADADEAQAELRDeLKAALRERL---PEYMVPAHlvfLARMP 5042
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 543 KTAIGKIQRTQLKtsfengefdhllhKPnrmnDAVQdeeMQQADHVKrvREEIQEHLLTCLTEELHVSRdwVEPNANIQS 622
Cdd:PRK12316 5043 LTPNGKLDRKALP-------------QP----DASL---LQQAYVAP--RSELEQQVAAIWAEVLQLER--VGLDDNFFE 5098
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1776025254 623 LGVNSIKMMKLIRSIEKNYHIKLTAREIHQYPTierLASYLSEHEDLSSSSADK 676
Cdd:PRK12316 5099 LGGHSLLAIQVTSRIQLELGLELPLRELFQTPT---LAAFVELAAAAGSGDDEK 5149
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
61-555 |
1.03e-21 |
|
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.
Pssm-ID: 341276 [Multi-domain] Cd Length: 428 Bit Score: 101.64 E-value: 1.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 61 SYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNSQLLPAFWGCVLTGVVPAPLAvpptyaesssgtqklkdawTLLdKP 140
Cdd:cd05972 2 SFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLT-------------------TLL-GP 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 141 AVITDRGMHQemldwakeqgleGFRAIIVEDllsaeadtdwhqsspEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGII 220
Cdd:cd05972 62 KDIEYRLEAA------------GAKAIVTDA---------------EDPALIYFTSGTTGLPKGVLHTHSYPLGHIPTAA 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 221 QMQGFTREDITFN-----WMPFDHVGGIGMLhlrdvYLGCQeiNVSSETILMEPLKWLDWIDHYRASVTWAPNFAFGLVT 295
Cdd:cd05972 115 YWLGLRPDDIHWNiadpgWAKGAWSSFFGPW-----LLGAT--VFVYEGPRFDAERILELLERYGVTSFCGPPTAYRMLI 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 296 dfAEEIKDRkwDLSSMRYMLNGGEAM---VAKVGRRILellephGLPadaIRPAWGMSETSSgVIFSHEFT--RAGTsdd 370
Cdd:cd05972 188 --KQDLSSY--KFSHLRLVVSAGEPLnpeVIEWWRAAT------GLP---IRDGYGQTETGL-TVGNFPDMpvKPGS--- 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 371 dhfveIGSPIPGFSMRIVNDHNELVEEGEIGRFQV--SGLSVTSGYYQRPDLNESVFTEDgWFETGDLG-FLRNGRLTIT 447
Cdd:cd05972 251 -----MGRPTPGYDVAIIDDDGRELPPGEEGDIAIklPPPGLFLGYVGDPEKTEASIRGD-YYLTGDRAyRDEDGYFWFV 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 448 GRTKDAIIINGINYYSHAIESAVeelseIETSYTAACAVrlgQNSTD----QLAIFFVTSAKlnDEQMS-QLLRNIQSHV 522
Cdd:cd05972 325 GRADDIIKSSGYRIGPFEVESAL-----LEHPAVAEAAV---VGSPDpvrgEVVKAFVVLTS--GYEPSeELAEELQGHV 394
|
490 500 510
....*....|....*....|....*....|....*.
gi 1776025254 523 SQVIGvtpEYLLPVQKE---EIPKTAIGKIQRTQLK 555
Cdd:cd05972 395 KKVLA---PYKYPREIEfveELPKTISGKIRRVELR 427
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
184-555 |
1.04e-21 |
|
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.
Pssm-ID: 341268 [Multi-domain] Cd Length: 439 Bit Score: 101.79 E-value: 1.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 184 SSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGI-IQMQGFTREDITFNWMPFDHVGGIGMLHLRDVYLGcqeinvsS 262
Cdd:cd05958 94 TASDDICILAFTSGTTGAPKATMHFHRDPLASADRYaVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVG-------A 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 263 ETILME---PLKWLDWIDHYRASVTW-APNFAFGLVT--DFAEEikdrkwDLSSMRYMLNGGEAMVAKVGRRILELLeph 336
Cdd:cd05958 167 SGVLLEeatPDLLLSAIARYKPTVLFtAPTAYRAMLAhpDAAGP------DLSSLRKCVSAGEALPAALHRAWKEAT--- 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 337 GLP-ADAIrpawGMSETssgvifSHEFTRAgTSDDDHFVEIGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGlsvTSGYY 415
Cdd:cd05958 238 GIPiIDGI----GSTEM------FHIFISA-RPGDARPGATGKPVPGYEAKVVDDEGNPVPDGTIGRLAVRG---PTGCR 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 416 QRPDLNESVFTEDGWFETGDLgFLR--NGRLTITGRTKDAIIINGINYYSHAIESAVeelseIETSYTAACAVrLGQNST 493
Cdd:cd05958 304 YLADKRQRTYVQGGWNITGDT-YSRdpDGYFRHQGRSDDMIVSGGYNIAPPEVEDVL-----LQHPAVAECAV-VGHPDE 376
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1776025254 494 DQLAI---FFVTSAKLNDEQmsQLLRNIQSHVSQVIGvtpEYLLPVQKE---EIPKTAIGKIQRTQLK 555
Cdd:cd05958 377 SRGVVvkaFVVLRPGVIPGP--VLARELQDHAKAHIA---PYKYPRAIEfvtELPRTATGKLQRFALR 439
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
173-561 |
1.22e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 102.76 E-value: 1.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 173 LSAEADTDWHQ-----SSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVkgIIQMQGFT-REDITF-NWMPFDHVGGI-- 243
Cdd:PRK06188 149 LLAAAAKFGPAplvaaALPPDIAGLAYTGGTTGKPKGVMGTHRSIATMA--QIQLAEWEwPADPRFlMCTPLSHAGGAff 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 244 -------GMLHLRDVYlgcqeinvssetilmEPLKWLDWIDHYRASVTW-APNFAFGLVtdfaEEIKDRKWDLSSMRYML 315
Cdd:PRK06188 227 lptllrgGTVIVLAKF---------------DPAEVLRAIEEQRITATFlVPTMIYALL----DHPDLRTRDLSSLETVY 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 316 NGGEAMVAKvgrRILELLEPHGlPADAirPAWGMSETSSGVIF----SHEftragTSDDDHFVEIGSPIPGFSMRIVNDH 391
Cdd:PRK06188 288 YGASPMSPV---RLAEAIERFG-PIFA--QYYGQTEAPMVITYlrkrDHD-----PDDPKRLTSCGRPTPGLRVALLDED 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 392 NELVEEGEIGRFQVSGLSVTSGYYQRPDLNESVFtEDGWFETGDL------GFlrngrLTITGRTKDAIIINGINYYSHA 465
Cdd:PRK06188 357 GREVAQGEVGEICVRGPLVMDGYWNRPEETAEAF-RDGWLHTGDVarededGF-----YYIVDRKKDMIVTGGFNVFPRE 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 466 IESAVEELSEIetsytAACAV------RLGQNSTdqlAIFFVTSAKLNDEQmsqllrNIQSHVSQVIGV--TPEYLLPVq 537
Cdd:PRK06188 431 VEDVLAEHPAV-----AQVAVigvpdeKWGEAVT---AVVVLRPGAAVDAA------ELQAHVKERKGSvhAPKQVDFV- 495
|
410 420
....*....|....*....|....
gi 1776025254 538 kEEIPKTAIGKIQRTQLKTSFENG 561
Cdd:PRK06188 496 -DSLPLTALGKPDKKALRARYWEG 518
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
1160-1648 |
1.41e-21 |
|
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.
Pssm-ID: 341270 [Multi-domain] Cd Length: 608 Bit Score: 103.02 E-value: 1.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1160 EQQAKKTPDRAAVSYEG------QTLTYRELDERSTQLAIYLQAHGVGP-DRLAgIYVDRSLDMLVGLLAILKAGGAYVP 1232
Cdd:cd05966 60 DRHLKERGDKVAIIWEGdepdqsRTITYRELLREVCRFANVLKSLGVKKgDRVA-IYMPMIPELVIAMLACARIGAVHSV 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1233 LDPSYPAERLEYMLEDSEVFITLTTSElvntlSWNG---------VTTAL------------------------LDQDWD 1279
Cdd:cd05966 139 VFAGFSAESLADRINDAQCKLVITADG-----GYRGgkviplkeiVDEALekcpsvekvlvvkrtggevpmtegRDLWWH 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1280 EIAQTASDRkVLTRTVTPENLAYVIYTSGSTGKPKGVMipHKaltnflvsmgeTPGLtaedkML--AVTT-YCFDIAALE 1356
Cdd:cd05966 214 DLMAKQSPE-CEPEWMDSEDPLFILYTSGSTGKPKGVV--HT-----------TGGY-----LLyaATTFkYVFDYHPDD 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1357 LFL-----------------PLIKGAHCYIcqTEHTKD----------VEKLKRDIRTIKPTVMQATpatwkMLFYSGWE 1409
Cdd:cd05966 275 IYWctadigwitghsyivygPLANGATTVM--FEGTPTypdpgrywdiVEKHKVTIFYTAPTAIRAL-----MKFGDEWV 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1410 NE---ENVKILcG--GEAL-PETLKRYF----------LDTgseaWNMfgpTET-----TIWSAVQRINDecsrATIGRP 1468
Cdd:cd05966 348 KKhdlSSLRVL-GsvGEPInPEAWMWYYevigkercpiVDT----WWQ---TETggimiTPLPGATPLKP----GSATRP 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1469 IANTQIYITDSQLAPVPAGVPGELCIAGD--GVAKGYYKKEEltdsRFIDNPFEPGSKLYRTGDMARWLPGGRIEYIGRI 1546
Cdd:cd05966 416 FFGIEPAILDEEGNEVEGEVEGYLVIKRPwpGMARTIYGDHE----RYEDTYFSKFPGYYFTGDGARRDEDGYYWITGRV 491
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1547 DNQVKIRGFRIELGDIESRLSEHPGILECVVVADMDNL-----AAYYTAK--HANASLTARELRHFVKNALPAYMVPSYF 1619
Cdd:cd05966 492 DDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIkgeaiYAFVTLKdgEEPSDELRKELRKHVRKEIGPIATPDKI 571
|
570 580
....*....|....*....|....*....
gi 1776025254 1620 IQLDHMPLTPNGKIDRNSLKNIDLSGEQL 1648
Cdd:cd05966 572 QFVPGLPKTRSGKIMRRILRKIAAGEEEL 600
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
1153-1649 |
1.66e-21 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 102.52 E-value: 1.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1153 ITFHELFEQQAKKTPDRAAV--SYEGQTL--TYRELDERSTQLAIYLQAHGVGP-DRLAGIY--VDRSLDMLVGLLAIlk 1225
Cdd:PRK06018 10 LLCHRIIDHAARIHGNREVVtrSVEGPIVrtTYAQIHDRALKVSQALDRDGIKLgDRVATIAwnTWRHLEAWYGIMGI-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1226 aGGAYVPLDPSYPAERLEYML---EDSEVFITLTTSELVNTLS--WNGVTTALLDQDWDEIAQT-------------ASD 1287
Cdd:PRK06018 88 -GAICHTVNPRLFPEQIAWIInhaEDRVVITDLTFVPILEKIAdkLPSVERYVVLTDAAHMPQTtlknavayeewiaEAD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1288 RKVLTRTVTPENLAYVIYTSGSTGKPKGVMIPHKA--LTNFLVSMGETPGLTAEDKMLAV----------TTYCFDIAAL 1355
Cdd:PRK06018 167 GDFAWKTFDENTAAGMCYTSGTTGDPKGVLYSHRSnvLHALMANNGDALGTSAADTMLPVvplfhanswgIAFSAPSMGT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1356 ELFLPLIK--GAHCYicqteHTKDVEKLkrdirtikpTVMQATPATWKMLFYSGWENEENV----KILCGGEALPETLKR 1429
Cdd:PRK06018 247 KLVMPGAKldGASVY-----ELLDTEKV---------TFTAGVPTVWLMLLQYMEKEGLKLphlkMVVCGGSAMPRSMIK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1430 YFLDTGSEAWNMFGPTETTIWSAVQRINDECS----------RATIGRPIANTQIYITDSQLAPVP--AGVPGELCIAGD 1497
Cdd:PRK06018 313 AFEDMGVEVRHAWGMTEMSPLGTLAALKPPFSklpgdarldvLQKQGYPPFGVEMKITDDAGKELPwdGKTFGRLKVRGP 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1498 GVAKGYYK--KEELTDSRFIDnpfepgsklyrTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILEC 1575
Cdd:PRK06018 393 AVAAAYYRvdGEILDDDGFFD-----------TGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEA 461
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1776025254 1576 VVVA----DMDNLAAYYTAKHANASLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLKnidlsgEQLK 1649
Cdd:PRK06018 462 AVIGvyhpKWDERPLLIVQLKPGETATREEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALR------EQFK 533
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
1180-1640 |
1.67e-21 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 102.16 E-value: 1.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1180 TYRELDERSTQLA-IYLQAHGVGP-DRLAGIyVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLEDSEVFITLTT 1257
Cdd:cd05928 43 SFRELGSLSRKAAnVLSGACGLQRgDRVAVI-LPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTS 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1258 SEL---VNTLSWN--GVTTALL--DQDWD------EIAQTASDRKVLTRTVTPENLAyVIYTSGSTGKPKgvMIPHK--- 1321
Cdd:cd05928 122 DELapeVDSVASEcpSLKTKLLvsEKSRDgwlnfkELLNEASTEHHCVETGSQEPMA-IYFTSGTTGSPK--MAEHShss 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1322 ALTNFLVSMGETPGLTAEDKMLAVTTYCFDIAAL-ELFLPLIKGAhCYICQTEHTKDVEKLKRDIRTIKPTVMQATPATW 1400
Cdd:cd05928 199 LGLGLKVNGRYWLDLTASDIMWNTSDTGWIKSAWsSLFEPWIQGA-CVFVHHLPRFDPLVILKTLSSYPITTFCGAPTVY 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1401 KMLF---YSGWENEENVKILCGGEAL-PETLKRYFLDTGSEAWNMFGPTETTIWSAVQRiNDECSRATIGRPIANTQIYI 1476
Cdd:cd05928 278 RMLVqqdLSSYKFPSLQHCVTGGEPLnPEVLEKWKAQTGLDIYEGYGQTETGLICANFK-GMKIKPGSMGKASPPYDVQI 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1477 TDSQLAPVPAGVPGELCIAGDGVAKGYYKkeeltdSRFIDNPFEPGSKL----YRTGDMARWLPGGRIEYIGRIDNQVKI 1552
Cdd:cd05928 357 IDDNGNVLPPGTEGDIGIRVKPIRPFGLF------SGYVDNPEKTAATIrgdfYLTGDRGIMDEDGYFWFMGRADDVINS 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1553 RGFRIELGDIESRLSEHPGILECVVVADMDN-----------LAAYYTAkHANASLTaRELRHFVKNALPAYMVPSYFIQ 1621
Cdd:cd05928 431 SGYRIGPFEVESALIEHPAVVESAVVSSPDPirgevvkafvvLAPQFLS-HDPEQLT-KELQQHVKSVTAPYKYPRKVEF 508
|
490
....*....|....*....
gi 1776025254 1622 LDHMPLTPNGKIDRNSLKN 1640
Cdd:cd05928 509 VQELPKTVTGKIQRNELRD 527
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
1155-1641 |
1.82e-21 |
|
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341297 [Multi-domain] Cd Length: 532 Bit Score: 102.22 E-value: 1.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1155 FHELFEQQA-----------KKTPDRAAV--SYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLL 1221
Cdd:cd17642 8 FYPLEDGTAgeqlhkamkryASVPGTIAFtdAHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1222 AILKAGGAYVPLDPSYPAERLEYMLEDSE---VFIT-LTTSELVNTLSWNGV--TTALLDQDWDeIAQTASDRKVLTRTV 1295
Cdd:cd17642 88 AGLFIGVGVAPTNDIYNERELDHSLNISKptiVFCSkKGLQKVLNVQKKLKIikTIIILDSKED-YKGYQCLYTFITQNL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1296 TP---------------ENLAYVIYTSGSTGKPKGVMIPHK-ALTNFLVSMGETPG--LTAEDKMLAVTTYCFDIAALEL 1357
Cdd:cd17642 167 PPgfneydfkppsfdrdEQVALIMNSSGSTGLPKGVQLTHKnIVARFSHARDPIFGnqIIPDTAILTVIPFHHGFGMFTT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1358 FLPLIKGAHCYICQT--EHT--KDVEKLKRDIRTIKPTVMQATPatwKMLFYSGWENEENVKILCGG--------EALPE 1425
Cdd:cd17642 247 LGYLICGFRVVLMYKfeEELflRSLQDYKVQSALLVPTLFAFFA---KSTLVDKYDLSNLHEIASGGaplskevgEAVAK 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1426 TLKRYFLDTGseawnmFGPTETTiwSAVQRINDE-CSRATIGRPIANTQIYITDSQLAP-VPAGVPGELCIAGDGVAKGY 1503
Cdd:cd17642 324 RFKLPGIRQG------YGLTETT--SAILITPEGdDKPGAVGKVVPFFYAKVVDLDTGKtLGPNERGELCVKGPMIMKGY 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1504 YKKEELTDSRFIDNPFepgsklYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMD- 1582
Cdd:cd17642 396 VNNPEATKALIDKDGW------LHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDe 469
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1776025254 1583 ---NLAAYYTAKHANASLTARELRHFVK-NALPAYMVPSYFIQLDHMPLTPNGKIDRNSLKNI 1641
Cdd:cd17642 470 dagELPAAVVVLEAGKTMTEKEVMDYVAsQVSTAKRLRGGVKFVDEVPKGLTGKIDRRKIREI 532
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
60-555 |
2.22e-21 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 102.18 E-value: 2.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 60 QSYRRLWDDGLRIVKGLRQSGLKaKQSVILQLGDNSQL-LPAFWGCVLTGVVPAPLAVPPTYAESSSGTQKLKDAWTLLD 138
Cdd:PLN02860 33 RTGHEFVDGVLSLAAGLLRLGLR-NGDVVAIAALNSDLyLEWLLAVACAGGIVAPLNYRWSFEEAKSAMLLVRPVMLVTD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 139 K------PAVITDR----GMHQEMLDWAKEQGLEGFRAIIVEDLL-----SAEADTDWhqsSPEDLALLLLTSGSTGTPK 203
Cdd:PLN02860 112 EtcsswyEELQNDRlpslMWQVFLESPSSSVFIFLNSFLTTEMLKqralgTTELDYAW---APDDAVLICFTSGTTGRPK 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 204 AVMLNHRN--IMSMVKgiIQMQGFTREDITFNWMPFDHVGGI----GML------------HLRDVYLGCQEINVSSETI 265
Cdd:PLN02860 189 GVTISHSAliVQSLAK--IAIVGYGEDDVYLHTAPLCHIGGLssalAMLmvgachvllpkfDAKAALQAIKQHNVTSMIT 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 266 LmePLKWLDWIDHYRASVTWAPNfafglvtdfaeeikdrkwdlSSMRYMLNGGEAMVAKVGRRILELLephglPADAIRP 345
Cdd:PLN02860 267 V--PAMMADLISLTRKSMTWKVF--------------------PSVRKILNGGGSLSSRLLPDAKKLF-----PNAKLFS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 346 AWGMSETSSGVIFS--HEFTRA---------GTSDDDHF-----VEIGSPIPGFSMRIVNDhnelvEEGEIGRFQVSGLS 409
Cdd:PLN02860 320 AYGMTEACSSLTFMtlHDPTLEspkqtlqtvNQTKSSSVhqpqgVCVGKPAPHVELKIGLD-----ESSRVGRILTRGPH 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 410 VTSGYYQRPDLNESVFTEDGWFETGDLGFL-RNGRLTITGRTKDAIIINGINYYSHAIE----------SAV------EE 472
Cdd:PLN02860 395 VMLGYWGQNSETASVLSNDGWLDTGDIGWIdKAGNLWLIGRSNDRIKTGGENVYPEEVEavlsqhpgvaSVVvvgvpdSR 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 473 LSEIetsyTAACaVRLGQNSTdqlaifFVTSAKLNDEQMSQLLRNIQSHVSQVIGVTpEYLLP----VQKEEIPKTAIGK 548
Cdd:PLN02860 475 LTEM----VVAC-VRLRDGWI------WSDNEKENAKKNLTLSSETLRHHCREKNLS-RFKIPklfvQWRKPFPLTTTGK 542
|
....*..
gi 1776025254 549 IQRTQLK 555
Cdd:PLN02860 543 IRRDEVR 549
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
1177-1578 |
2.68e-21 |
|
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341255 [Multi-domain] Cd Length: 508 Bit Score: 101.39 E-value: 2.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1177 QTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLEDSEVFITLT 1256
Cdd:cd05932 5 VEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1257 ------------TSELVNTLSWNGVTTALLDQDWDEI-AQTASDRKVLTRTvtPENLAYVIYTSGSTGKPKGVMIPHKAL 1323
Cdd:cd05932 85 gklddwkamapgVPEGLISISLPPPSAANCQYQWDDLiAQHPPLEERPTRF--PEQLATLIYTSGTTGQPKGVMLTFGSF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1324 TNFLVSMGETPGLTAEDKMLAVTTYCFDIAALELFL-PLIKGAHCYICQTEHTKdVEKLKRDirtiKPTVMQATPATWkM 1402
Cdd:cd05932 163 AWAAQAGIEHIGTEENDRMLSYLPLAHVTERVFVEGgSLYGGVLVAFAESLDTF-VEDVQRA----RPTLFFSVPRLW-T 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1403 LFYSGWENE-----------------------------ENVKILCGGEA-LPETLKRYFLDTG---SEAWNMfgpTETTI 1449
Cdd:cd05932 237 KFQQGVQDKipqqklnlllkipvvnslvkrkvlkglglDQCRLAGCGSApVPPALLEWYRSLGlniLEAYGM---TENFA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1450 WSAVQRINDEcSRATIGRPIANTQIYITDSqlapvpagvpGELCIAGDGVAKGYYKKEELTDSRFIDNPFepgsklYRTG 1529
Cdd:cd05932 314 YSHLNYPGRD-KIGTVGNAGPGVEVRISED----------GEILVRSPALMMGYYKDPEATAEAFTADGF------LRTG 376
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1530 DMARWLPGGRIEYIGRIDNQVKI-RGFRIELGDIESRLSEHPGILECVVV 1578
Cdd:cd05932 377 DKGELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKLAEHDRVEMVCVI 426
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
186-554 |
2.88e-21 |
|
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341299 [Multi-domain] Cd Length: 465 Bit Score: 100.97 E-value: 2.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 186 PEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTRED--ITFNWMPFDhvggigmlhlrdvylgcqeinVSSE 263
Cdd:cd17644 105 PENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGITSSDrvLQFASIAFD---------------------VAAE 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 264 TILMEPLKwldwidhyRASVTWAPNFAFGLVTDFAEEIKDRK---WDL--------------------SSMRYMLNGGEA 320
Cdd:cd17644 164 EIYVTLLS--------GATLVLRPEEMRSSLEDFVQYIQQWQltvLSLppaywhllvlelllstidlpSSLRLVIVGGEA 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 321 -------MVAKVGRRILELLEphglpadairpAWGMSETSSGVIFSHefTRAGTSDDDHFVEIGSPIPGFSMRIVNDHNE 393
Cdd:cd17644 236 vqpelvrQWQKNVGNFIQLIN-----------VYGPTEATIAATVCR--LTQLTERNITSVPIGRPIANTQVYILDENLQ 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 394 LVEEGEIGRFQVSGLSVTSGYYQRPDLNESVFTEDGW--------FETGDLG-FLRNGRLTITGRTKDAIIINGINYYSH 464
Cdd:cd17644 303 PVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFnsseserlYKTGDLArYLPDGNIEYLGRIDNQVKIRGFRIELG 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 465 AIESAVEELSEIEtsyTAACAVRLGQNSTDQLAIFFVtsAKLNDEQMSQLLRniqSHVSQVIgvtPEYLLP---VQKEEI 541
Cdd:cd17644 383 EIEAVLSQHNDVK---TAVVIVREDQPGNKRLVAYIV--PHYEESPSTVELR---QFLKAKL---PDYMIPsafVVLEEL 451
|
410
....*....|...
gi 1776025254 542 PKTAIGKIQRTQL 554
Cdd:cd17644 452 PLTPNGKIDRRAL 464
|
|
| SDR_c |
cd05233 |
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ... |
2852-3016 |
3.16e-21 |
|
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.
Pssm-ID: 212491 [Multi-domain] Cd Length: 234 Bit Score: 95.81 E-value: 3.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2852 LITGGAGSLGLLFAKEIANRtGrSTIVLTGRSvlsEDKENELEALRSIGAEVVYREADVSDQHAVHHLFEEIKERYGTLN 2931
Cdd:cd05233 2 LVTGASSGIGRAIARRLARE-G-AKVVLADRN---EEALAELAAIEALGGNAVAVQADVSDEEDVEALVEEALEEFGRLD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2932 GIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSGLLHV-DECSKDFPLDFF---IFFSSVSGCLGNAGQADYAAANSFMDAF 3007
Cdd:cd05233 77 ILVNNAGIARPGPLEELTDEDWDRVLDVNLTGVFLLtRAALPHMKKQGGgriVNISSVAGLRPLPGQAAYAASKAALEGL 156
|
....*....
gi 1776025254 3008 AeyrRSLAA 3016
Cdd:cd05233 157 T---RSLAL 162
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
186-554 |
3.68e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 101.65 E-value: 3.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 186 PE-DLALLLLTSGSTGTPKAVMLNHRNIMS-MVKGIIQMQGFTR-EDITFNWMPFDHVGGIGMLHLRDVYLGCQEINVSS 262
Cdd:PRK06710 204 PEnDLALLQYTGGTTGFPKGVMLTHKNLVSnTLMGVQWLYNCKEgEEVVLGVLPFFHVYGMTAVMNLSIMQGYKMVLIPK 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 263 ETILM--EPLKwldwiDHYRASVTWAPNFAFGLVTdfAEEIKDrkWDLSSMRYMLNGGEAMVAKVGRRIlellepHGLPA 340
Cdd:PRK06710 284 FDMKMvfEAIK-----KHKVTLFPGAPTIYIALLN--SPLLKE--YDISSIRACISGSAPLPVEVQEKF------ETVTG 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 341 DAIRPAWGMSETS--SGVIFSHEFTRAGTsdddhfveIGSPIPGFSMRIVN-DHNELVEEGEIGRFQVSGLSVTSGYYQR 417
Cdd:PRK06710 349 GKLVEGYGLTESSpvTHSNFLWEKRVPGS--------IGVPWPDTEAMIMSlETGEALPPGEIGEIVVKGPQIMKGYWNK 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 418 PDLNESVFtEDGWFETGDLGFL-RNGRLTITGRTKDAIIINGINYYSHAIESAVEELSEIETsytaacAVRLG-----QN 491
Cdd:PRK06710 421 PEETAAVL-QDGWLHTGDVGYMdEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQE------VVTIGvpdpyRG 493
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1776025254 492 STDQLAIFFVTSAKLNDEQMSQLLRNIQShvsqvigvtpEYLLPVQKE---EIPKTAIGKIQRTQL 554
Cdd:PRK06710 494 ETVKAFVVLKEGTECSEEELNQFARKYLA----------AYKVPKVYEfrdELPKTTVGKILRRVL 549
|
|
| PRK09116 |
PRK09116 |
beta-ketoacyl-ACP synthase; |
3436-3700 |
4.08e-21 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 181657 [Multi-domain] Cd Length: 405 Bit Score: 99.68 E-value: 4.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3436 KALEDAG-CPPQSLSGTGTGIFIG--TGNTGYKDLFhrANLPIEGHA----ATGH--MIPSVGPNRMSYFLNIHGPSEPV 3506
Cdd:PRK09116 83 LALEDAGlLGDPILTDGRMGIAYGssTGSTDPIGAF--GTMLLEGSMsgitATTYvrMMPHTTAVNVGLFFGLKGRVIPT 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3507 ETACSSSLVAIHRAVTAMQNGDCEMAIAGGVNTILTEEAHISYSKAGMLSKDGRCKT----FSADANGYVRGEGVGMVML 3582
Cdd:PRK09116 161 SSACTSGSQGIGYAYEAIKYGYQTVMLAGGAEELCPTEAAVFDTLFATSTRNDAPELtprpFDANRDGLVIGEGAGTLVL 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3583 KKLEDAERDGNHIYGVIRGTAENHGGRAntLTSPNPKAQADLLVRAYRQAGIDPSTVTYIEAHGTGTELGDPIEINGLKA 3662
Cdd:PRK09116 241 EELEHAKARGATIYAEIVGFGTNSDGAH--VTQPQAETMQIAMELALKDAGLAPEDIGYVNAHGTATDRGDIAESQATAA 318
|
250 260 270
....*....|....*....|....*....|....*...
gi 1776025254 3663 AFkelsnmrGESQPdvpdhrcgIGSVKSNIGHLELAAG 3700
Cdd:PRK09116 319 VF-------GARMP--------ISSLKSYFGHTLGACG 341
|
|
| FabG |
COG1028 |
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ... |
2850-3016 |
6.32e-21 |
|
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and metabolism]; NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440651 [Multi-domain] Cd Length: 249 Bit Score: 95.62 E-value: 6.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGLLFAKEIANRtGrSTIVLTGRSvlsEDKENEL-EALRSIGAEVVYREADVSDQHAVHHLFEEIKERYG 2928
Cdd:COG1028 8 VALVTGGSSGIGRAIARALAAE-G-ARVVITDRD---AEALEAAaAELRAAGGRALAVAADVTDEAAVEALVAAAVAAFG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2929 TLNGIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSGLLHvdeCSKDFpLDFF--------IFFSSVSGCLGNAGQADYAAA 3000
Cdd:COG1028 83 RLDILVNNAGITPPGPLEELTEEDWDRVLDVNLKGPFL---LTRAA-LPHMrergggriVNISSIAGLRGSPGQAAYAAS 158
|
170
....*....|....*.
gi 1776025254 3001 NSFMDAFAeyrRSLAA 3016
Cdd:COG1028 159 KAAVVGLT---RSLAL 171
|
|
| PRK07967 |
PRK07967 |
beta-ketoacyl-ACP synthase I; |
1776-2187 |
6.69e-21 |
|
beta-ketoacyl-ACP synthase I;
Pssm-ID: 181184 [Multi-domain] Cd Length: 406 Bit Score: 98.97 E-value: 6.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1776 NHDEFWENLRDGKESIAFfnkeelqrfgiSKEIAENAdyvpAKASIEGKDRFDPsffqispkdAEFMDPQLRMLLTH--S 1853
Cdd:PRK07967 18 NQQEVLASLREGRSGITF-----------SPEFAEMG----MRSQVWGNVKLDP---------TGLIDRKVMRFMGDasA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1854 W------KAIEDAGYAAGQI--PQTSVFMSASNNSYRALL-PSDTTESLETPDGYVSWVL--AQSGTIPTMISHKLGLRG 1922
Cdd:PRK07967 74 YaylameQAIADAGLSEEQVsnPRTGLIAGSGGGSTRNQVeAADAMRGPRGPKRVGPYAVtkAMASTVSACLATPFKIKG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1923 PSYFVHANCSSSLIGLHSAYKSLLSAESDYALVGGA-----TLHTESNIGYVHQPGLNFSSDGHIKAFDASADGMIGGEG 1997
Cdd:PRK07967 154 VNYSISSACATSAHCIGNAVEQIQLGKQDIVFAGGGeeldwEMSCLFDAMGALSTKYNDTPEKASRAYDANRDGFVIAGG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1998 VAVVLLKKAADAVKDGDHIYALLRGIGVNNDGADKVgfyAPSVKGQADVVQQVMNQTKihpESICYVEAHGTGTKLGDPI 2077
Cdd:PRK07967 234 GGVVVVEELEHALARGAKIYAEIVGYGATSDGYDMV---APSGEGAVRCMQMALATVD---TPIDYINTHGTSTPVGDVK 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2078 ELAALTNVyrqYTNKTQFcgIGSVKTNIGHLDTAAGLAGCIKVVMSLYHQELAPSINYKEPNPntDLASSPfyvVDQKKT 2157
Cdd:PRK07967 308 ELGAIREV---FGDKSPA--ISATKSLTGHSLGAAGVQEAIYSLLMMEHGFIAPSANIEELDP--QAAGMP---IVTETT 377
|
410 420 430
....*....|....*....|....*....|.
gi 1776025254 2158 LSREIQThraALS-SFGLGGTNTHAIFEQFK 2187
Cdd:PRK07967 378 DNAELTT---VMSnSFGFGGTNATLVFRRYK 405
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
182-555 |
7.44e-21 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 100.67 E-value: 7.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 182 HQSSPEDLALLLLTSGSTGTPKAVMLNHRNI---MSMVKGIIQMQG-----FTRE--DITFNWMPFDHVggigmlHLRDV 251
Cdd:PRK12492 202 VPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLvanMLQVRACLSQLGpdgqpLMKEgqEVMIAPLPLYHI------YAFTA 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 252 YLGCQEINVSSETILMEPLKWLDWIDHYRasvTWAPNFAFGLVTDFAEEIKD---RKWDLSSMRYMLNGGEAMVAKVGRR 328
Cdd:PRK12492 276 NCMCMMVSGNHNVLITNPRDIPGFIKELG---KWRFSALLGLNTLFVALMDHpgfKDLDFSALKLTNSGGTALVKATAER 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 329 IlellepHGLPADAIRPAWGMSETSSgVIFSH---EFTRAGTsdddhfveIGSPIPGFSMRIVNDHNELVEEGEIGRFQV 405
Cdd:PRK12492 353 W------EQLTGCTIVEGYGLTETSP-VASTNpygELARLGT--------VGIPVPGTALKVIDDDGNELPLGERGELCI 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 406 SGLSVTSGYYQRPDLNESVFTEDGWFETGDLGFL-RNGRLTITGRTKDAIIINGINYYSHAIESAVEELSEIetsytAAC 484
Cdd:PRK12492 418 KGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIdPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKV-----ANC 492
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1776025254 485 AVrLG---QNSTDQLAIFFVTS-AKLNDEQMSQLLR-NIQShvsqvigvtpeYLLP---VQKEEIPKTAIGKIQRTQLK 555
Cdd:PRK12492 493 AA-IGvpdERSGEAVKLFVVARdPGLSVEELKAYCKeNFTG-----------YKVPkhiVLRDSLPMTPVGKILRRELR 559
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
185-452 |
1.08e-20 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 100.19 E-value: 1.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 185 SPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDHVGGiGMLHLRDVYLGCQEIN-VSSE 263
Cdd:cd17641 156 KGEDVAVLCTTSGTTGKPKLAMLSHGNFLGHCAAYLAADPLGPGDEYVSVLPLPWIGE-QMYSVGQALVCGFIVNfPEEP 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 264 TILMEPLK-------------WLDWIDHYRASVTWAPNF---------------------------AFGLVTDFAEEI-- 301
Cdd:cd17641 235 ETMMEDLReigptfvllpprvWEGIAADVRARMMDATPFkrfmfelgmklglraldrgkrgrpvslWLRLASWLADALlf 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 302 ---KDRkWDLSSMRYMLNGGEAMvakvGRRILELLEPHGLPadaIRPAWGMSETSsGVIFSHeftRAGTSDDDhfvEIGS 378
Cdd:cd17641 315 rplRDR-LGFSRLRSAATGGAAL----GPDTFRFFHAIGVP---LKQLYGQTELA-GAYTVH---RDGDVDPD---TVGV 379
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1776025254 379 PIPGFSMRIVNdhnelveEGEIgrfQVSGLSVTSGYYQRPDLNESVFTEDGWFETGDLGFLR-NGRLTITGRTKD 452
Cdd:cd17641 380 PFPGTEVRIDE-------VGEI---LVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKeNGHLVVIDRAKD 444
|
|
| PRK09116 |
PRK09116 |
beta-ketoacyl-ACP synthase; |
4722-4988 |
1.93e-20 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 181657 [Multi-domain] Cd Length: 405 Bit Score: 97.37 E-value: 1.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4722 AANLSQFFDVRGPSVVVDTACSSALVGMNMAIQALRGGDIQSAIVGGVSLLSSDASHrLFDRRGILSK-----HSSFHVF 4796
Cdd:PRK09116 144 AVNVGLFFGLKGRVIPTSSACTSGSQGIGYAYEAIKYGYQTVMLAGGAEELCPTEAA-VFDTLFATSTrndapELTPRPF 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4797 DERADGVVLGEGVGMVMLKTVKQALEDGDTIYAVVKAASVNNDGrtAGPATPNLEAQKEVMKDALFKSGKKPEDISYLEA 4876
Cdd:PRK09116 223 DANRDGLVIGEGAGTLVLEELEHAKARGATIYAEIVGFGTNSDG--AHVTQPQAETMQIAMELALKDAGLAPEDIGYVNA 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4877 NGSGSIVTDLLELKAIQSVYrsGHSSPLSlgSIKPNIGHPLCAEGIASFIKVVLMLKERRFVPFLSgekeMAHFDQQKAN 4956
Cdd:PRK09116 301 HGTATDRGDIAESQATAAVF--GARMPIS--SLKSYFGHTLGACGALEAWMSIEMMNEGWFAPTLN----LTQVDPACGA 372
|
250 260 270
....*....|....*....|....*....|..
gi 1776025254 4957 ITFSRALEKWTDSQPTAAiNCFADGGTNVHVI 4988
Cdd:PRK09116 373 LDYIMGEAREIDTEYVMS-NNFAFGGINTSLI 403
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
1167-1639 |
2.48e-20 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 98.52 E-value: 2.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1167 PDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGgaYVPLDPSYPAERLE--- 1243
Cdd:PRK10946 37 SDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLG--VAPVNALFSHQRSElna 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1244 YMLE----------DSEVFitlTTSELVNTL--SWNGVTTALLDQDWDE------IAQTASDrkvLTRTVTP-ENLAYVI 1304
Cdd:PRK10946 115 YASQiepalliadrQHALF---SDDDFLNTLvaEHSSLRVVLLLNDDGEhslddaINHPAED---FTATPSPaDEVAFFQ 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1305 YTSGSTGKPKgvMIP--HK----------------ALTNFLVS-------MGETPG----LTAEDKMLAVT----TYCFd 1351
Cdd:PRK10946 189 LSGGSTGTPK--LIPrtHNdyyysvrrsveicgftPQTRYLCAlpaahnyPMSSPGalgvFLAGGTVVLAPdpsaTLCF- 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1352 iaalelflPLIKgahcyicqtEHTKDVEKLkrdirtIKPTV---MQATPAtwkmlfySGWENE-ENVKIL-CGGEALPET 1426
Cdd:PRK10946 266 --------PLIE---------KHQVNVTAL------VPPAVslwLQAIAE-------GGSRAQlASLKLLqVGGARLSET 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1427 LKRYFLDT-GSEAWNMFGPTETTIwsAVQRINDECSR--ATIGRPIA-NTQIYITDSQLAPVPAGVPGELCIAGDGVAKG 1502
Cdd:PRK10946 316 LARRIPAElGCQLQQVFGMAEGLV--NYTRLDDSDERifTTQGRPMSpDDEVWVADADGNPLPQGEVGRLMTRGPYTFRG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1503 YYKKEELTDSRFIDNPFepgsklYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMD 1582
Cdd:PRK10946 394 YYKSPQHNASAFDANGF------YCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMED 467
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1776025254 1583 NL-----AAYYTAKHAnasLTARELRHFVKNALPA-YMVPSYFIQLDHMPLTPNGKIDRNSLK 1639
Cdd:PRK10946 468 ELmgeksCAFLVVKEP---LKAVQLRRFLREQGIAeFKLPDRVECVDSLPLTAVGKVDKKQLR 527
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
184-554 |
2.82e-20 |
|
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).
Pssm-ID: 341307 [Multi-domain] Cd Length: 436 Bit Score: 97.32 E-value: 2.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 184 SSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTRED--ITFNWMPFDhvGGI----------GMLHLRDv 251
Cdd:cd17652 90 TTPDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAAFDVGPGSrvLQFASPSFD--ASVwellmallagATLVLAP- 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 252 ylgcqeinvSSETILMEPLkwLDWIDHYRASVTWAPNFAFGLVTDFaeeikdrkwDLSSMRYMLNGGEA----MVAK--V 325
Cdd:cd17652 167 ---------AEELLPGEPL--ADLLREHRITHVTLPPAALAALPPD---------DLPDLRTLVVAGEAcpaeLVDRwaP 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 326 GRRILEllephglpadairpAWGMSETSSGVifshefTRAGTSDDDHFVEIGSPIPGFSMRIVNDHNELVEEGEIGRFQV 405
Cdd:cd17652 227 GRRMIN--------------AYGPTETTVCA------TMAGPLPGGGVPPIGRPVPGTRVYVLDARLRPVPPGVPGELYI 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 406 SGLSVTSGYYQRPDLNESVFTEDGW-------FETGDLGFLRN-GRLTITGRTKDAIIINGinyysHAIesaveELSEIE 477
Cdd:cd17652 287 AGAGLARGYLNRPGLTAERFVADPFgapgsrmYRTGDLARWRAdGQLEFLGRADDQVKIRG-----FRI-----ELGEVE 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 478 TSYT-------AACAVRLGQNSTDQLAIFFVTSAKLNDEQmSQLLRNIQSHVsqvigvtPEYLLP---VQKEEIPKTAIG 547
Cdd:cd17652 357 AALTehpgvaeAVVVVRDDRPGDKRLVAYVVPAPGAAPTA-AELRAHLAERL-------PGYMVPaafVVLDALPLTPNG 428
|
....*..
gi 1776025254 548 KIQRTQL 554
Cdd:cd17652 429 KLDRRAL 435
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
1158-1568 |
4.04e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 98.48 E-value: 4.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1158 LFEQQAKKTPDRAA---VSYEG------QTLTYRELDERSTQLAIYLQAHGVGPDRlAGIYVDRSLDMLVGLLAILKAGG 1228
Cdd:PRK05850 6 LLRERASLQPDDAAftfIDYEQdpagvaETLTWSQLYRRTLNVAEELRRHGSTGDR-AVILAPQGLEYIVAFLGALQAGL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1229 AYVPLDPSYPA---ERLEYMLEDSEVFITLTTSELVN------TLSWNGVTTA-----LLDQDwdeiaqtaSDRKVLTRT 1294
Cdd:PRK05850 85 IAVPLSVPQGGahdERVSAVLRDTSPSVVLTTSAVVDdvteyvAPQPGQSAPPvievdLLDLD--------SPRGSDARP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1295 VTPENLAYVIYTSGSTGKPKGVMIPHKALT-NFLVSM----GETPGLTAEDKMLaVTTYCF--DIA-ALELFLPLIKGah 1366
Cdd:PRK05850 157 RDLPSTAYLQYTSGSTRTPAGVMVSHRNVIaNFEQLMsdyfGDTGGVPPPDTTV-VSWLPFyhDMGlVLGVCAPILGG-- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1367 cyiCQTEHTKDVEKLKRDIRTIK-----PTVMQATP------ATWK-----MlfySGWENEENVKILCGGEAL-PETLKR 1429
Cdd:PRK05850 234 ---CPAVLTSPVAFLQRPARWMQllasnPHAFSAAPnfafelAVRKtsdddM---AGLDLGGVLGIISGSERVhPATLKR 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1430 yFLDTGSeAWNM--------FGPTETTIWSA----------------------VQRINDECSRATIGRPIANTQIY-ITD 1478
Cdd:PRK05850 308 -FADRFA-PFNLretairpsYGLAEATVYVAtrepgqppesvrfdyeklsaghAKRCETGGGTPLVSYGSPRSPTVrIVD 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1479 SQ-LAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRF---IDNPFE--PGSKLYRTGDMArWLPGGRIEYIGRIDNQVKI 1552
Cdd:PRK05850 386 PDtCIECPAGTVGEIWVHGDNVAAGYWQKPEETERTFgatLVDPSPgtPEGPWLRTGDLG-FISEGELFIVGRIKDLLIV 464
|
490
....*....|....*.
gi 1776025254 1553 RGFRIELGDIESRLSE 1568
Cdd:PRK05850 465 DGRNHYPDDIEATIQE 480
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
100-556 |
7.73e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 96.60 E-value: 7.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 100 AFWGCVLTGV--VPaplaVPPtyaesSSGTQKLKDawtlldkpaVITDRGMhQEMLDWAKEqGLEGFRAIIVEdlLSAEA 177
Cdd:PRK07787 61 AVVGALIAGVpvVP----VPP-----DSGVAERRH---------ILADSGA-QAWLGPAPD-DPAGLPHVPVR--LHARS 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 178 DTDWHQSSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDHVGGI--GML-HLRdvyLG 254
Cdd:PRK07787 119 WHRYPEPDPDAPALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAWQWTADDVLVHGLPLFHVHGLvlGVLgPLR---IG 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 255 CQEINVSSETilmePlkwldwiDHYRASVTWAPNFAFGLVTDFAEEIKDRKWD--LSSMRYMLNGGEAMVAKVGRRILEL 332
Cdd:PRK07787 196 NRFVHTGRPT----P-------EAYAQALSEGGTLYFGVPTVWSRIAADPEAAraLRGARLLVSGSAALPVPVFDRLAAL 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 333 LephGLpadaiRPA--WGMSET--SSGVIFSHEfTRAGTsdddhfveIGSPIPGFSMRIVNDH-NELVEEGE-IGRFQVS 406
Cdd:PRK07787 265 T---GH-----RPVerYGMTETliTLSTRADGE-RRPGW--------VGLPLAGVETRLVDEDgGPVPHDGEtVGELQVR 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 407 GLSVTSGYYQRPDLNESVFTEDGWFETGDL------GFLRngrltITGRTKDAIIINGiNYYSHAiesaveelSEIETSY 480
Cdd:PRK07787 328 GPTLFDGYLNRPDATAAAFTADGWFRTGDVavvdpdGMHR-----IVGRESTDLIKSG-GYRIGA--------GEIETAL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 481 TAACAVR-----------LGQnstdQLAIFFVTSAKLNDEQMSQllrniqsHVSQvigvtpeyLLPVQK--------EEI 541
Cdd:PRK07787 394 LGHPGVReaavvgvpdddLGQ----RIVAYVVGADDVAADELID-------FVAQ--------QLSVHKrprevrfvDAL 454
|
490
....*....|....*
gi 1776025254 542 PKTAIGKIQRTQLKT 556
Cdd:PRK07787 455 PRNAMGKVLKKQLLS 469
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
61-554 |
9.37e-20 |
|
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341311 [Multi-domain] Cd Length: 479 Bit Score: 96.39 E-value: 9.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 61 SYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNSQLLPAFWGCVLTGvvPAPLAVPPTYAESssgtqklKDAWTLLDKP 140
Cdd:cd17656 15 TYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAG--GAFVPIDPEYPEE-------RRIYIMLDSG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 141 A-VITDRGMHQEMLDWAKEQGLegfraiIVEDLLSAEADTDWHQS-SPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKG 218
Cdd:cd17656 86 VrVVLTQRHLKSKLSFNKSTIL------LEDPSISQEDTSNIDYInNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLLHF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 219 IIQMQGFTRED--ITFNWMPFDhvggIGMLHLRDVYLGCQEINVSSETILMEPLKWLDWIDHYRASVTWAPNfAF----- 291
Cdd:cd17656 160 EREKTNINFSDkvLQFATCSFD----VCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNIEVVFLPV-AFlkfif 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 292 ---GLVTDFAEEIKdrkwdlssmrYMLNGGEAMVakVGRRILELLEPHGLpadAIRPAWGMSETssgvifsHEFTRAGTS 368
Cdd:cd17656 235 serEFINRFPTCVK----------HIITAGEQLV--ITNEFKEMLHEHNV---HLHNHYGPSET-------HVVTTYTIN 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 369 DDDHFVE---IGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGYYQRPDLNESVFTEDGW------FETGDLG-F 438
Cdd:cd17656 293 PEAEIPElppIGKPISNTWIYILDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFdpnermYRTGDLArY 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 439 LRNGRLTITGRTKDAIIINGINYYSHAIESAveeLSEIETSYTAACAVRLGQNSTDQLAIFFVTSAKLNDEQMSQLLRni 518
Cdd:cd17656 373 LPDGNIEFLGRADHQVKIRGYRIELGEIEAQ---LLNHPGVSEAVVLDKADDKGEKYLCAYFVMEQELNISQLREYLA-- 447
|
490 500 510
....*....|....*....|....*....|....*....
gi 1776025254 519 qshvSQVigvtPEYLLP---VQKEEIPKTAIGKIQRTQL 554
Cdd:cd17656 448 ----KQL----PEYMIPsffVPLDQLPLTPNGKVDRKAL 478
|
|
| PTZ00050 |
PTZ00050 |
3-oxoacyl-acyl carrier protein synthase; Provisional |
4604-4939 |
9.58e-20 |
|
3-oxoacyl-acyl carrier protein synthase; Provisional
Pssm-ID: 240245 [Multi-domain] Cd Length: 421 Bit Score: 95.53 E-value: 9.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4604 TLESYWSLLSEGRSSIGPI---PAERWGCKTPYY-------------AGVIDGVSYFDPDFFLLHEED------VRAMDp 4661
Cdd:PTZ00050 8 GAESTWEALIAGKSGIRKLtefPKFLPDCIPEQKalenlvaampcqiAAEVDQSEFDPSDFAPTKRESrathfaMAAAR- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4662 QALlvleECLKLLYHAGYTPEEIkGKPVGVYIGGRSQHKpDEDSLDHAKNP-------IVTVGQNYLAANLSQFFDVRGP 4734
Cdd:PTZ00050 87 EAL----ADAKLDILSEKDQERI-GVNIGSGIGSLADLT-DEMKTLYEKGHsrvspyfIPKILGNMAAGLVAIKHKLKGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4735 SVVVDTACSSALVGMNMAIQALRGGDIQSAIVGG----VSLLSSDASHRLfdrRGILSKH-----SSFHVFDERADGVVL 4805
Cdd:PTZ00050 161 SGSAVTACATGAHCIGEAFRWIKYGEADIMICGGteasITPVSFAGFSRM---RALCTKYnddpqRASRPFDKDRAGFVM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4806 GEGVGMVMLKTVKQALEDGDTIYAVVKAASVNNDGRTAGPATPNLEAQKEVMKDALFKSGKKP-EDISYLEANGSGSIVT 4884
Cdd:PTZ00050 238 GEGAGILVLEELEHALRRGAKIYAEIRGYGSSSDAHHITAPHPDGRGARRCMENALKDGANINiNDVDYVNAHATSTPIG 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1776025254 4885 DLLELKAIQSVYRSGHSSPLSLGSIKPNIGHPLCAEGIASFIKVVLMLKERRFVP 4939
Cdd:PTZ00050 318 DKIELKAIKKVFGDSGAPKLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPP 372
|
|
| PLN02836 |
PLN02836 |
3-oxoacyl-[acyl-carrier-protein] synthase |
4719-4984 |
1.07e-19 |
|
3-oxoacyl-[acyl-carrier-protein] synthase
Pssm-ID: 215449 [Multi-domain] Cd Length: 437 Bit Score: 95.63 E-value: 1.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4719 NYLAANLSQFFDVRGPSVVVDTACSSALVGMNMAIQALRGGDIQSAIVGGvSLLSSDA-SHRLFDR-RGILSKHSSFHV- 4795
Cdd:PLN02836 161 NMAAGHVSIRYGFQGPNHAAVTACATGAHSIGDAFRMIQFGDADVMVAGG-TESSIDAlSIAGFSRsRALSTKFNSCPTe 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4796 ----FDERADGVVLGEGVGMVMLKTVKQALEDGDTIYAVVKAASVNNDGRTAGPATPNLEAQKEVMKDALFKSGKKPEDI 4871
Cdd:PLN02836 240 asrpFDCDRDGFVIGEGAGVLVLEELEHAKRRGAKIYAEVRGYGMSGDAHHITQPHEDGRGAVLAMTRALQQSGLHPNQV 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4872 SYLEANGSGSIVTDLLELKAIQSVYRS-GHSSPLSLGSIKPNIGHPLCAEGIASFIKVVLMLKERRFVPFLSGEKEMAHF 4950
Cdd:PLN02836 320 DYVNAHATSTPLGDAVEARAIKTVFSEhATSGGLAFSSTKGATGHLLGAAGAVEAIFSVLAIHHGIAPPTLNLERPDPIF 399
|
250 260 270
....*....|....*....|....*....|....
gi 1776025254 4951 DQQKANITFSRAlekwtDSQPTAAINCFADGGTN 4984
Cdd:PLN02836 400 DDGFVPLTASKA-----MLIRAALSNSFGFGGTN 428
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
1161-1572 |
1.11e-19 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 96.89 E-value: 1.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1161 QQAKKTPDRAAV----------SYEGQTLTYRELDERSTQLAIYLQAHGVGP-DRLAgIYVDRSLDMLVGLLAILKAGGA 1229
Cdd:PRK09274 14 RAAQERPDQLAVavpggrgadgKLAYDELSFAELDARSDAIAHGLNAAGIGRgMRAV-LMVTPSLEFFALTFALFKAGAV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1230 YVPLDPSYPAERLEYMLEDS--EVFITLTTSELV------------------NTLSWNGVTTALLDQDWD----EIAQTA 1285
Cdd:PRK09274 93 PVLVDPGMGIKNLKQCLAEAqpDAFIGIPKAHLArrlfgwgkpsvrrlvtvgGRLLWGGTTLATLLRDGAaapfPMADLA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1286 SDrkvltrtvtpeNLAYVIYTSGSTGKPKGVMIPHKALTNFLVSMGETPGLTAEDKMLAvttyCFDIAAleLFLPLIkGA 1365
Cdd:PRK09274 173 PD-----------DMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDLP----TFPLFA--LFGPAL-GM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1366 HCYICQTEHTK----DVEKLKRDIRTIKPTVMQATPATWKMLFYSGWENE---ENVK-ILCGGE-ALPETLKRY--FLDT 1434
Cdd:PRK09274 235 TSVIPDMDPTRpatvDPAKLFAAIERYGVTNLFGSPALLERLGRYGEANGiklPSLRrVISAGApVPIAVIERFraMLPP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1435 GSEAWNMFGPTE----TTIWSavQRINDECSRAT-------IGRPIANTQ---IYITD------SQLAPVPAGVPGELCI 1494
Cdd:PRK09274 315 DAEILTPYGATEalpiSSIES--REILFATRAATdngagicVGRPVDGVEvriIAISDapipewDDALRLATGEIGEIVV 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1776025254 1495 AGDGVAKGYYKKEELTDSRFIDNPfePGSKLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGI 1572
Cdd:PRK09274 393 AGPMVTRSYYNRPEATRLAKIPDG--QGDVWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGV 468
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
166-554 |
2.45e-19 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.
Pssm-ID: 341280 [Multi-domain] Cd Length: 447 Bit Score: 94.69 E-value: 2.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 166 AIIVEDLLSAEADTDwhqssPEDLALLLLTSGSTGTPKAVMLNHRNIMSMvkgiIQ--MQGFTRED---------ITFNW 234
Cdd:cd12115 89 RFILEDAQARLVLTD-----PDDLAYVIYTSGSTGRPKGVAIEHRNAAAF----LQwaAAAFSAEElagvlastsICFDL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 235 MPFDHVGgigmlhlrdvylgcqEINVSSETILMEPLkwLDWIDHYRASVTWAPNfafgLVTDFAEEIKDRKWDLSSMRyM 314
Cdd:cd12115 160 SVFELFG---------------PLATGGKVVLADNV--LALPDLPAAAEVTLIN----TVPSAAAELLRHDALPASVR-V 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 315 LN-GGEAMVAKVGRRILELLephglPADAIRPAWGMSETSSgviFS--HEFTRAGTSDddhfVEIGSPIPGFSMRIVNDH 391
Cdd:cd12115 218 VNlAGEPLPRDLVQRLYARL-----QVERVVNLYGPSEDTT---YStvAPVPPGASGE----VSIGRPLANTQAYVLDRA 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 392 NELVEEGEIGRFQVSGLSVTSGYYQRPDLNESVFTEDGW------FETGDLGFLR-NGRLTITGRTKDAIIINGINYYSH 464
Cdd:cd12115 286 LQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFgpgarlYRTGDLVRWRpDGLLEFLGRADNQVKVRGFRIELG 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 465 AIESAVEELSEIEtsytAACAVRLGQNSTD-QLAIFFVTSAKLndeqmSQLLRNIQSHVSQVIgvtPEYLLP---VQKEE 540
Cdd:cd12115 366 EIEAALRSIPGVR----EAVVVAIGDAAGErRLVAYIVAEPGA-----AGLVEDLRRHLGTRL---PAYMVPsrfVRLDA 433
|
410
....*....|....
gi 1776025254 541 IPKTAIGKIQRTQL 554
Cdd:cd12115 434 LPLTPNGKIDRSAL 447
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
1218-1641 |
2.56e-19 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 95.68 E-value: 2.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1218 VGLLAILKAGGAYVPLDPSYPAERLEYMLEDSEVFITLTTSELVNTLSWNGVTTALLDQ--DWDEIAQT--------ASD 1287
Cdd:PLN02574 107 VIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFTSPENVEKLSPLGVPVIGVPEnyDFDSKRIEfpkfyeliKED 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1288 RKVLTR-TVTPENLAYVIYTSGSTGKPKGVMIPHKAL-------TNFLVSMGETPGltAEDKMLAVTTYcFDIAALELFL 1359
Cdd:PLN02574 187 FDFVPKpVIKQDDVAAIMYSSGTTGASKGVVLTHRNLiamvelfVRFEASQYEYPG--SDNVYLAALPM-FHIYGLSLFV 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1360 P--LIKGAHCYICQ----TEHTKDVEKLKRDIRTIKPTVMQATPATWKMLfySGWENEENVKILCGGEALPETLKRYFLD 1433
Cdd:PLN02574 264 VglLSLGSTIVVMRrfdaSDMVKVIDRFKVTHFPVVPPILMALTKKAKGV--CGEVLKSLKQVSCGAAPLSGKFIQDFVQ 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1434 TGSEA--WNMFGPTETTiwsAV--QRINDECSR--ATIGRPIANTQIYITD-SQLAPVPAGVPGELCIAGDGVAKGYYKK 1506
Cdd:PLN02574 342 TLPHVdfIQGYGMTEST---AVgtRGFNTEKLSkySSVGLLAPNMQAKVVDwSTGCLLPPGNCGELWIQGPGVMKGYLNN 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1507 EELTDSRFIDNPFepgsklYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMDNLAA 1586
Cdd:PLN02574 419 PKATQSTIDKDGW------LRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECG 492
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1776025254 1587 ----YYTAKHANASLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLKNI 1641
Cdd:PLN02574 493 eipvAFVVRRQGSTLSQEAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELKRS 551
|
|
| PRK14691 |
PRK14691 |
3-oxoacyl-(acyl carrier protein) synthase II; Provisional |
3475-3780 |
2.96e-19 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
Pssm-ID: 173154 [Multi-domain] Cd Length: 342 Bit Score: 92.87 E-value: 2.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3475 IEGHAATGHMI---PSVGPNRMSYFL-----------------NIHGPSEPVETACSSSLVAIHRAVTAMQNGDCEMAIA 3534
Cdd:PRK14691 36 IGGFPAIAHAVrtsDSRGPKRLSPFTvpsflvnlaaghvsikhHFKGPIGAPVTACAAGVQAIGDAVRMIRNNEADVALC 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3535 GGVNTILTEEAHISYSKAGMLSK------DGRCKTFSADANGYVRGEGVGMVMLKKLEDAERDGNHIYGVIRGTAENHGG 3608
Cdd:PRK14691 116 GGAEAVIDTVSLAGFAAARALSThfnstpEKASRPFDTARDGFVMGEGAGLLIIEELEHALARGAKPLAEIVGYGTSADA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3609 RANTLTSPNPKAQADLLVRAYRQAGIDPSTVTYIEAHGTGTELGDPIEINGLKAAFkelsnmrGESQPdvpdhrCGIGSV 3688
Cdd:PRK14691 196 YHMTSGAEDGDGAYRAMKIALRQAGITPEQVQHLNAHATSTPVGDLGEINAIKHLF-------GESNA------LAITST 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3689 KSNIGHLELAAGISGLIKVLLQMKHKTLVKSLHCETLNPYLqltdspfyivqekqewKSVTDCDGNELPRR---AGISSF 3765
Cdd:PRK14691 263 KSATGHLLGAAGGLETIFTVLALRDQIVPATLNLENPDPAA----------------KGLNIIAGNAQPHDmtyALSNGF 326
|
330
....*....|....*
gi 1776025254 3766 GIGGVNAHIVIEEYM 3780
Cdd:PRK14691 327 GFAGVNASILLKRWV 341
|
|
| FabG |
COG1028 |
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ... |
4169-4351 |
3.51e-19 |
|
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and metabolism]; NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440651 [Multi-domain] Cd Length: 249 Bit Score: 90.23 E-value: 3.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4169 KDHVLLITGGTRGIGLLCARHFAECyGVKkLVLTGReqlppREEWARfktsntslaekiQAVRELEAKGVQVEMLSLTLS 4248
Cdd:COG1028 5 KGKVALVTGGSSGIGRAIARALAAE-GAR-VVITDR-----DAEALE------------AAAAELRAAGGRALAVAADVT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4249 DDAQVEQTLQHIKRTLGPIGGVIHCAGLTDMDTLAfiRKTSDDIQRVMEPKVSGLTTLYRHVcnepLQFF--------VL 4320
Cdd:COG1028 66 DEAAVEALVAAAVAAFGRLDILVNNAGITPPGPLE--ELTEEDWDRVLDVNLKGPFLLTRAA----LPHMrergggriVN 139
|
170 180 190
....*....|....*....|....*....|.
gi 1776025254 4321 FSSVSAIIPelSAGQADYAMANSYMDYFAEA 4351
Cdd:COG1028 140 ISSIAGLRG--SPGQAAYAASKAAVVGLTRS 168
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
186-452 |
3.71e-19 |
|
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341255 [Multi-domain] Cd Length: 508 Bit Score: 94.84 E-value: 3.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 186 PEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDHVGGIGMLHLRDVYLGCQEINVSSETI 265
Cdd:cd05932 136 PEQLATLIYTSGTTGQPKGVMLTFGSFAWAAQAGIEHIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAESLDT 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 266 LMEPLKwldwidhyRASvtwaPNFAFG---LVTDFAEEIKDR----KWD---------------------LSSMRYMLNG 317
Cdd:cd05932 216 FVEDVQ--------RAR----PTLFFSvprLWTKFQQGVQDKipqqKLNlllkipvvnslvkrkvlkglgLDQCRLAGCG 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 318 GeamvAKVGRRILELLEPHGLPadaIRPAWGMSETSSGVIFSHEF-TRAGTsdddhfveIGSPIPGFSMRIVndhnelvE 396
Cdd:cd05932 284 S----APVPPALLEWYRSLGLN---ILEAYGMTENFAYSHLNYPGrDKIGT--------VGNAGPGVEVRIS-------E 341
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1776025254 397 EGEIgrfQVSGLSVTSGYYQRPDLNESVFTEDGWFETGDLGFL-RNGRLTITGRTKD 452
Cdd:cd05932 342 DGEI---LVRSPALMMGYYKDPEATAEAFTADGFLRTGDKGELdADGNLTITGRVKD 395
|
|
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
1985-2179 |
4.17e-19 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 93.19 E-value: 4.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1985 FDASADGMIGGEGVAVVLLKKAADAVKDGDHIYALLRGIGVNNDgADKVGFYAPSVKGQADVVQQVMNQTKIHPESICYV 2064
Cdd:PRK05952 199 FDRQREGLVLGEGGAILVLESAELAQKRGAKIYGQILGFGLTCD-AYHMSAPEPDGKSAIAAIQQCLARSGLTPEDIDYI 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2065 EAHGTGTKLGDPIELAALTNVYRQYTnktqfcGIGSVKTNIGHLDTAAGLAGCIKVVMSLYHQELAPSINYKEPNPNTDL 2144
Cdd:PRK05952 278 HAHGTATRLNDQREANLIQALFPHRV------AVSSTKGATGHTLGASGALGVAFSLLALRHQQLPPCVGLQEPEFDLNF 351
|
170 180 190
....*....|....*....|....*....|....*
gi 1776025254 2145 ASSPfyvvdqkktlsREIQTHRAALSSFGLGGTNT 2179
Cdd:PRK05952 352 VRQA-----------QQSPLQNVLCLSFGFGGQNA 375
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
27-555 |
6.14e-19 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 94.29 E-value: 6.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 27 QPATipEVLYRTAAelGDTKGIIylqpDGTEVYqSYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNSQLLPAFWGCVL 106
Cdd:PRK10946 25 LPLT--DILTRHAA--SDAIAVI----CGERQF-SYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 107 TGVVPaplaVPPTYAEsssgtQKLK-DAWTLLDKPA-VITDRGmHQEMLDwakEQGLEGFRAII---------------- 168
Cdd:PRK10946 96 LGVAP----VNALFSH-----QRSElNAYASQIEPAlLIADRQ-HALFSD---DDFLNTLVAEHsslrvvlllnddgehs 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 169 VEDLLSAEADTDWHQSSPED-LALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDH------VG 241
Cdd:PRK10946 163 LDDAINHPAEDFTATPSPADeVAFFQLSGGSTGTPKLIPRTHNDYYYSVRRSVEICGFTPQTRYLCALPAAHnypmssPG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 242 GIGMLHLRdvylGCQEINVSSETILMEPLkwldwIDHYRASVTWAPNFAFGLVTDFAEEIKDRKwDLSSMRYMLNGGEAM 321
Cdd:PRK10946 243 ALGVFLAG----GTVVLAPDPSATLCFPL-----IEKHQVNVTALVPPAVSLWLQAIAEGGSRA-QLASLKLLQVGGARL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 322 VAKVGRRILELLephglpADAIRPAWGMSEtssGVIfshEFTRAGTSDDDHFVEIGSPI-PGFSMRIVNDHNELVEEGEI 400
Cdd:PRK10946 313 SETLARRIPAEL------GCQLQQVFGMAE---GLV---NYTRLDDSDERIFTTQGRPMsPDDEVWVADADGNPLPQGEV 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 401 GRFQVSGLSVTSGYYQRPDLNESVFTEDGWFETGDLGFLR-NGRLTITGRTKDAIIINGINYYSHAIESAVeeLSEIETS 479
Cdd:PRK10946 381 GRLMTRGPYTFRGYYKSPQHNASAFDANGFYCSGDLVSIDpDGYITVVGREKDQINRGGEKIAAEEIENLL--LRHPAVI 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 480 YTAACAV---RLGQNStdqlAIFFVTSAKLNDEQMSQLLRNiqshvsqvIGVTpEYLLPVQKEEI---PKTAIGKIQRTQ 553
Cdd:PRK10946 459 HAALVSMedeLMGEKS----CAFLVVKEPLKAVQLRRFLRE--------QGIA-EFKLPDRVECVdslPLTAVGKVDKKQ 525
|
..
gi 1776025254 554 LK 555
Cdd:PRK10946 526 LR 527
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
162-564 |
6.64e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 93.95 E-value: 6.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 162 EGFRAIIVEDLLSAEADTDWHQSSPedlALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQ--MQGFTREDITFNWMPFDH 239
Cdd:PRK07470 141 LDYEALVARHLGARVANAAVDHDDP---CWFFFTSGTTGRPKAAVLTHGQMAFVITNHLAdlMPGTTEQDASLVVAPLSH 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 240 vgGIGMLHLRDVYLGCQEINVSSETilMEPLKWLDWIDHYRASVTWA-PNFAFGLVTDFAEEikdrKWDLSSMRYMLNGG 318
Cdd:PRK07470 218 --GAGIHQLCQVARGAATVLLPSER--FDPAEVWALVERHRVTNLFTvPTILKMLVEHPAVD----RYDHSSLRYVIYAG 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 319 EAMVAKVGRRILELLEPhglpadAIRPAWGMSETSSGVIF----SHEftragtSDDDHFVEIGS---PIPGFSMRIVNDH 391
Cdd:PRK07470 290 APMYRADQKRALAKLGK------VLVQYFGLGEVTGNITVlppaLHD------AEDGPDARIGTcgfERTGMEVQIQDDE 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 392 NELVEEGEIGRFQVSGLSVTSGYYQRPDLNESVFtEDGWFETGDLGFL-RNGRLTITGRTKDAIIINGINYYSHAIES-- 468
Cdd:PRK07470 358 GRELPPGETGEICVIGPAVFAGYYNNPEANAKAF-RDGWFRTGDLGHLdARGFLYITGRASDMYISGGSNVYPREIEEkl 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 469 ----AVEELS----------EIEtsyTAACAVRLGqnstdqlaiffvtsAKLNDEQMSQLLRniqshvsqviGVTPEYLL 534
Cdd:PRK07470 437 lthpAVSEVAvlgvpdpvwgEVG---VAVCVARDG--------------APVDEAELLAWLD----------GKVARYKL 489
|
410 420 430
....*....|....*....|....*....|....
gi 1776025254 535 P---VQKEEIPKTAIGKIQRTQLKTSFEN-GEFD 564
Cdd:PRK07470 490 PkrfFFWDALPKSGYGKITKKMVREELEErGLLD 523
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
195-552 |
7.43e-19 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 92.90 E-value: 7.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 195 TSGSTGTPKAVMLNHR---NIMSMVKGIIQMQGFTREDITFNWMPFD-HVGGIGMlhlrdvYLGCQEINVSseTILMEPL 270
Cdd:COG1541 91 SSGTTGKPTVVGYTRKdldRWAELFARSLRAAGVRPGDRVQNAFGYGlFTGGLGL------HYGAERLGAT--VIPAGGG 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 271 ---KWLDWIDHYRASVTWA-PNFAFGLvtdfAEEIKDRKWDL--SSMRYMLNGGEAMVAKVGRRILELLephGLPA-DAi 343
Cdd:COG1541 163 nteRQLRLMQDFGPTVLVGtPSYLLYL----AEVAEEEGIDPrdLSLKKGIFGGEPWSEEMRKEIEERW---GIKAyDI- 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 344 rpaWGMSETSSGVIFSHEfTRAGTS-DDDHF-VEIGSPIPGfsmrivndhnELVEEGEIGRfqvsgLSVTSgyyqrpdln 421
Cdd:COG1541 235 ---YGLTEVGPGVAYECE-AQDGLHiWEDHFlVEIIDPETG----------EPVPEGEEGE-----LVVTT--------- 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 422 esvFTEDGW----FETGDLGFLRNG---------RLT-ITGRTKDAIIINGINYYSHAIESAVEELSEIETSYTaacAVR 487
Cdd:COG1541 287 ---LTKEAMplirYRTGDLTRLLPEpcpcgrthpRIGrILGRADDMLIIRGVNVFPSQIEEVLLRIPEVGPEYQ---IVV 360
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1776025254 488 LGQNSTDQLAIFFVTSAKLNDEqmsQLLRNIQSHVSQVIGVTPEYLLpVQKEEIPKTAiGKIQRT 552
Cdd:COG1541 361 DREGGLDELTVRVELAPGASLE---ALAEAIAAALKAVLGLRAEVEL-VEPGSLPRSE-GKAKRV 420
|
|
| PRK09185 |
PRK09185 |
beta-ketoacyl-ACP synthase; |
1908-2183 |
8.17e-19 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236398 [Multi-domain] Cd Length: 392 Bit Score: 92.21 E-value: 8.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1908 GTIPTMISHKLGLRGPSYFVHANCSSSLIGLHSAyKSLLSAE-SDYALVGGA------TLHtesniGYvhqPGLNFSSDG 1980
Cdd:PRK09185 137 GSLADFLRAYLGLSGPAYTISTACSSSAKVFASA-RRLLEAGlCDAAIVGGVdslcrlTLN-----GF---NSLESLSPQ 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1981 HIKAFDASADGMIGGEGVAVVLLKKAADAVkdgdhiyALLRGIGVNNDgadkvgfyA-------PSVKGQADVVQQVMNQ 2053
Cdd:PRK09185 208 PCRPFSANRDGINIGEAAAFFLLEREDDAA-------VALLGVGESSD--------AhhmsaphPEGLGAILAMQQALAD 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2054 TKIHPESICYVEAHGTGTKLGDPIELAALTNVYRQYTNktqfCgiGSVKTNIGHldtAAGLAGCIKVV---MSLYHQELA 2130
Cdd:PRK09185 273 AGLAPADIGYINLHGTATPLNDAMESRAVAAVFGDGVP----C--SSTKGLTGH---TLGAAGAVEAAicwLALRHGLPP 343
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1776025254 2131 PSINYKEPNPntDLAssPFYVVDQKKTLSReiqthRAALS-SFGLGGTNTHAIF 2183
Cdd:PRK09185 344 HGWNTGQPDP--ALP--PLYLVENAQALAI-----RYVLSnSFAFGGNNCSLIF 388
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
186-663 |
1.45e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 94.84 E-value: 1.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 186 PEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDHVGGI----------GMLHLRDvylgc 255
Cdd:PRK12467 3236 GENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSFSFDGAQerflwtlicgGCLVVRD----- 3310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 256 qeinvsseTILMEPLKWLDWIDHYRASVTwapNFAFGLVTDFAEEIKDRkwDLSSMRYMLNGGEAMVAKVGRRILELLEP 335
Cdd:PRK12467 3311 --------NDLWDPEELWQAIHAHRISIA---CFPPAYLQQFAEDAGGA--DCASLDIYVFGGEAVPPAAFEQVKRKLKP 3377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 336 HGLpadaiRPAWGMSETSSGVIfsHEFTRAGTSDDDHFVEIGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGYY 415
Cdd:PRK12467 3378 RGL-----TNGYGPTEAVVTVT--LWKCGGDAVCEAPYAPIGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGVGLARGYH 3450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 416 QRPDLNESVFTEDGW-------FETGDLGFLR-NGRLTITGRTKDAIIINGINYyshaiesaveELSEIETSYTAACAVR 487
Cdd:PRK12467 3451 QRPSLTAERFVADPFsgsggrlYRTGDLARYRaDGVIEYLGRIDHQVKIRGFRI----------ELGEIEARLLQHPSVR 3520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 488 ----LGQNSTD--QLAIFFVtSAKLNDEQMSQLLRNIQSHVsqvigvtPEYLLPVQ---KEEIPKTAIGKIQRtqlktsf 558
Cdd:PRK12467 3521 eavvLARDGAGgkQLVAYVV-PADPQGDWRETLRDHLAASL-------PDYMVPAQllvLAAMPLGPNGKVDR------- 3585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 559 engefdhllhkpnrmnDAVQDEEMQQADHVKRVREEIQEHLLTCLTEELHVSRdwVEPNANIQSLGVNSIKMMKLIRSIE 638
Cdd:PRK12467 3586 ----------------KALPDPDAKGSREYVAPRSEVEQQLAAIWADVLGVEQ--VGVTDNFFELGGDSLLALQVLSRIR 3647
|
490 500
....*....|....*....|....*
gi 1776025254 639 KNYHIKLTAREIHQYPTIERLASYL 663
Cdd:PRK12467 3648 QSLGLKLSLRDLMSAPTIAELAGYS 3672
|
|
| adh_short |
pfam00106 |
short chain dehydrogenase; This family contains a wide variety of dehydrogenases. |
2852-3015 |
1.61e-18 |
|
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
Pssm-ID: 395056 [Multi-domain] Cd Length: 195 Bit Score: 86.90 E-value: 1.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2852 LITGGAGSLGLLFAKEIAnRTGrSTIVLTGRSVlsEDKENELEALRSIGAEVVYREADVSDQHAVHHLFEEIKERYGTLN 2931
Cdd:pfam00106 4 LVTGASSGIGRAIAKRLA-KEG-AKVVLVDRSE--EKLEAVAKELGALGGKALFIQGDVTDRAQVKALVEQAVERLGRLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2932 GIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSGLLHvdeCSKDFpLDFF--------IFFSSVSGCLGNAGQADYAAANSF 3003
Cdd:pfam00106 80 ILVNNAGITGLGPFSELSDEDWERVIDVNLTGVFN---LTRAV-LPAMikgsggriVNISSVAGLVPYPGGSAYSASKAA 155
|
170
....*....|..
gi 1776025254 3004 MDAFAeyrRSLA 3015
Cdd:pfam00106 156 VIGFT---RSLA 164
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
1170-1633 |
1.85e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 92.66 E-value: 1.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1170 AAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLEDS 1249
Cdd:PRK08276 3 VIMAPSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1250 E--VFITL-----TTSELVNTLSwNGVTTALLD-------QDWDEIAQTASDRKVLTRTVTpenlAYVIYTSGSTGKPKG 1315
Cdd:PRK08276 83 GakVLIVSaaladTAAELAAELP-AGVPLLLVVagpvpgfRSYEEALAAQPDTPIADETAG----ADMLYSSGTTGRPKG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1316 VMI------PHKALTNFLVSMGETPGLTAEDKML--------AVTTYCFDIAAL------------ELFLPLI---KGAH 1366
Cdd:PRK08276 158 IKRplpgldPDEAPGMMLALLGFGMYGGPDSVYLspaplyhtAPLRFGMSALALggtvvvmekfdaEEALALIeryRVTH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1367 CYICQT---------EHTK---DVEKLKRDIRTIKPTvmqATPATWKMLFYsgWeneenvkilcgGEALPETlkrYfldT 1434
Cdd:PRK08276 238 SQLVPTmfvrmlklpEEVRaryDVSSLRVAIHAAAPC---PVEVKRAMIDW--W-----------GPIIHEY---Y---A 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1435 GSEAwNMFgptetTIWSAVQRINdecSRATIGRPIAnTQIYITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSrf 1514
Cdd:PRK08276 296 SSEG-GGV-----TVITSEDWLA---HPGSVGKAVL-GEVRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAA-- 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1515 IDNPfepgSKLYRTGDMArWLPGGRIEYI-GRIDNQVKIRGFRIELGDIESRLSEHPGILECVVV----ADMDN--LAAY 1587
Cdd:PRK08276 364 ARNP----HGWVTVGDVG-YLDEDGYLYLtDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFgvpdEEMGErvKAVV 438
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1776025254 1588 YTAKHANAS-LTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKI 1633
Cdd:PRK08276 439 QPADGADAGdALAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKL 485
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
1154-1580 |
1.88e-18 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 93.64 E-value: 1.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1154 TFHELFEQQAKKTPD------RAAVSYEGQT-----------------LTYRELDERSTQLAIYLQAHGVGPDRLAGIYV 1210
Cdd:PLN02387 59 TLAALFEQSCKKYSDkrllgtRKLISREFETssdgrkfeklhlgeyewITYGQVFERVCNFASGLVALGHNKEERVAIFA 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1211 DRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLEDSEVFI----------------TLTTSELVNTLSWNGVTTALL 1274
Cdd:PLN02387 139 DTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTvicdskqlkklidissQLETVKRVIYMDDEGVDSDSS 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1275 DQD---W-----DEIAQTASDRKVLTRTVTPENLAYVIYTSGSTGKPKGVMIPHKALTNFLVS-MGETPGLTAEDKMLAV 1345
Cdd:PLN02387 219 LSGssnWtvssfSEVEKLGKENPVDPDLPSPNDIAVIMYTSGSTGLPKGVMMTHGNIVATVAGvMTVVPKLGKNDVYLAY 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1346 --TTYCFDIAAlELFLPLIKGAHCYICQTEHTKDVEKLKR----DIRTIKPTVMQATPATW------------------K 1401
Cdd:PLN02387 299 lpLAHILELAA-ESVMAAVGAAIGYGSPLTLTDTSNKIKKgtkgDASALKPTLMTAVPAILdrvrdgvrkkvdakgglaK 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1402 MLF---------------YSGWENE---------ENVK---------ILCGGEALPETLKRyFLDT--GSEAWNMFGPTE 1446
Cdd:PLN02387 378 KLFdiaykrrlaaiegswFGAWGLEkllwdalvfKKIRavlggrirfMLSGGAPLSGDTQR-FINIclGAPIGQGYGLTE 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1447 TTIWSAVQRINDEcSRATIGRPIANTQI---------Y-ITDSqlaPVPAgvpGELCIAGDGVAKGYYKKEELTDSRFID 1516
Cdd:PLN02387 457 TCAGATFSEWDDT-SVGRVGPPLPCCYVklvsweeggYlISDK---PMPR---GEIVIGGPSVTLGYFKNQEKTDEVYKV 529
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1776025254 1517 NpfEPGSKLYRTGDMARWLPGGRIEYIGRIDNQVKIR-GFRIELGDIESRLSEHPGILECVVVAD 1580
Cdd:PLN02387 530 D--ERGMRWFYTGDIGQFHPDGCLEIIDRKKDIVKLQhGEYVSLGKVEAALSVSPYVDNIMVHAD 592
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
1168-1639 |
2.56e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 92.44 E-value: 2.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1168 DRAAVSYEGQTLTYRELDERSTQLAIYLQAHgVGPDRLA--GIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYM 1245
Cdd:PRK07867 18 DDRGLYFEDSFTSWREHIRGSAARAAALRAR-LDPTRPPhvGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1246 LEDSEVFITLTTSELVNTLSWNGVTTALLDQD---WDEIAQTASDRKVLTRTVTPENLAYVIYTSGSTGKPKGVMIPHKA 1322
Cdd:PRK07867 97 IAHADCQLVLTESAHAELLDGLDPGVRVINVDspaWADELAAHRDAEPPFRVADPDDLFMLIFTSGTSGDPKAVRCTHRK 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1323 LTNFLVSMGETPGLTAEDkmlavTTYC----FDIAA-LELFLP-LIKGAHCYICQtehtkdveklKRDIRTIKPTVMQ-- 1394
Cdd:PRK07867 177 VASAGVMLAQRFGLGPDD-----VCYVsmplFHSNAvMAGWAVaLAAGASIALRR----------KFSASGFLPDVRRyg 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1395 ATPATW--KMLFY------SGWENEENVKILCGGEALPETLKRYFLDTGSEAWNMFGPTETTIwsAVQRINDECSRAtIG 1466
Cdd:PRK07867 242 ATYANYvgKPLSYvlatpeRPDDADNPLRIVYGNEGAPGDIARFARRFGCVVVDGFGSTEGGV--AITRTPDTPPGA-LG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1467 RPIANTQIYITDSqLAPVPAGVP------------GELC-IAGDGVAKGYYKKEELTDSRFIDNpfepgskLYRTGDMAR 1533
Cdd:PRK07867 319 PLPPGVAIVDPDT-GTECPPAEDadgrllnadeaiGELVnTAGPGGFEGYYNDPEADAERMRGG-------VYWSGDLAY 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1534 WLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMDNLaayyTAKHANASLTARELRHFVKNALPAY 1613
Cdd:PRK07867 391 RDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPV----VGDQVMAALVLAPGAKFDPDAFAEF 466
|
490 500 510
....*....|....*....|....*....|....*.
gi 1776025254 1614 ----------MVPSYFIQLDHMPLTPNGKIDRNSLK 1639
Cdd:PRK07867 467 laaqpdlgpkQWPSYVRVCAELPRTATFKVLKRQLS 502
|
|
| PRK09116 |
PRK09116 |
beta-ketoacyl-ACP synthase; |
1985-2183 |
2.76e-18 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 181657 [Multi-domain] Cd Length: 405 Bit Score: 90.82 E-value: 2.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1985 FDASADGMIGGEGVAVVLLKKAADAVKDGDHIYALLRGIGVNNDGADkvgFYAPSVKGQADVVQQVMNQTKIHPESICYV 2064
Cdd:PRK09116 222 FDANRDGLVIGEGAGTLVLEELEHAKARGATIYAEIVGFGTNSDGAH---VTQPQAETMQIAMELALKDAGLAPEDIGYV 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2065 EAHGTGTKLGDPIELAALTNVYRQYTNktqfcgIGSVKTNIGHldtAAGLAGCIKVVMSLYHQE---LAPSINYKEPNPN 2141
Cdd:PRK09116 299 NAHGTATDRGDIAESQATAAVFGARMP------ISSLKSYFGH---TLGACGALEAWMSIEMMNegwFAPTLNLTQVDPA 369
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1776025254 2142 T-DLAsspfYVVDQkktlSREIQTHRAALSSFGLGGTNTHAIF 2183
Cdd:PRK09116 370 CgALD----YIMGE----AREIDTEYVMSNNFAFGGINTSLIF 404
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
61-454 |
3.10e-18 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 92.26 E-value: 3.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 61 SYR---RLWDDglrIVKGLRQSGLKAKQSVILQLGDNSQLLPAFWGCVLTGVVPAPLAVPPTYAESSSGTQKLKDAWTLL 137
Cdd:PRK05852 45 SYRdlaRLVDD---LAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLI 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 138 DKPAVI-TDRGMHQEMLDWAKEQGLEGFRAIIVEDLLSAEADTDWHQSSPEDL----ALLLLTSGSTGTPKAVMLNHRNI 212
Cdd:PRK05852 122 DADGPHdRAEPTTRWWPLTVNVGGDSGPSGGTLSVHLDAATEPTPATSTPEGLrpddAMIMFTGGTTGLPKMVPWTHANI 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 213 MSMVKGIIQMQGFTREDITFNWMPFDH-------------VGGIGMLHLRDVYlgcqeinvSSETIlmeplkwldWIDHY 279
Cdd:PRK05852 202 ASSVRAIITGYRLSPRDATVAVMPLYHghgliaallatlaSGGAVLLPARGRF--------SAHTF---------WDDIK 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 280 RASVTW---APNFAFGLVTDFAEEIKDRKwdLSSMRYMLNGGEAMVAKVGrriLELLEPHGLPadaIRPAWGMSETSSGV 356
Cdd:PRK05852 265 AVGATWytaVPTIHQILLERAATEPSGRK--PAALRFIRSCSAPLTAETA---QALQTEFAAP---VVCAFGMTEATHQV 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 357 ifshEFTRAGTSDDDHFVEIGSPIPGFS----MRIVNDHNELVEEGEIGRFQVSGLSVTSGYYQRPDLNESVFTeDGWFE 432
Cdd:PRK05852 337 ----TTTQIEGIGQTENPVVSTGLVGRStgaqIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANFT-DGWLR 411
|
410 420
....*....|....*....|...
gi 1776025254 433 TGDLGFLR-NGRLTITGRTKDAI 454
Cdd:PRK05852 412 TGDLGSLSaAGDLSIRGRIKELI 434
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
61-555 |
3.15e-18 |
|
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.
Pssm-ID: 341273 [Multi-domain] Cd Length: 442 Bit Score: 91.02 E-value: 3.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 61 SYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNSQLLPAFWGCVLTGVVPAPLAvpptyaeSSSGTQKLKDAWTLLDKP 140
Cdd:cd05969 2 TFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLF-------SAFGPEAIRDRLENSEAK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 141 AVITdrgmHQEMLDwakeqglegfraiivedllsaeadtdwhQSSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGII 220
Cdd:cd05969 75 VLIT----TEELYE----------------------------RTDPEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGK 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 221 QMQGFTREDITF-----NWMPFDHVGGIG-MLHlrdvylGCQEINVSSEtilMEPLKWLDWIDHYRASVTWAPNFAFGLV 294
Cdd:cd05969 123 YVLDLHPDDIYWctadpGWVTGTVYGIWApWLN------GVTNVVYEGR---FDAESWYGIIERVKVTVWYTAPTAIRML 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 295 TDFAEEIKdRKWDLSSMRYMLNGGEAMVAKVGRRILELLephGLPadaIRPAWGMSETSSGVIFSH--EFTRAGTsdddh 372
Cdd:cd05969 194 MKEGDELA-RKYDLSSLRFIHSVGEPLNPEAIRWGMEVF---GVP---IHDTWWQTETGSIMIANYpcMPIKPGS----- 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 373 fveIGSPIPGFSMRIVNDHNELVEEGEIGRFQV-SGL-SVTSGYYQRPDLNESVFTeDGWFETGDLGFL-RNGRLTITGR 449
Cdd:cd05969 262 ---MGKPLPGVKAAVVDENGNELPPGTKGILALkPGWpSMFRGIWNDEERYKNSFI-DGWYLTGDLAYRdEDGYFWFVGR 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 450 TKDAIIINGINYYSHAIESAVeelseIETSYTAACAVrLGQnsTDQLAIFFVT---SAKLNDEQMSQLLRNIQSHVSQVI 526
Cdd:cd05969 338 ADDIIKTSGHRVGPFEVESAL-----MEHPAVAEAGV-IGK--PDPLRGEIIKafiSLKEGFEPSDELKEEIINFVRQKL 409
|
490 500 510
....*....|....*....|....*....|..
gi 1776025254 527 GVTpeyLLPVQ---KEEIPKTAIGKIQRTQLK 555
Cdd:cd05969 410 GAH---VAPREiefVDNLPKTRSGKIMRRVLK 438
|
|
| PRK07910 |
PRK07910 |
beta-ketoacyl-ACP synthase; |
3338-3779 |
3.16e-18 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236129 [Multi-domain] Cd Length: 418 Bit Score: 90.94 E-value: 3.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3338 FEPVAIVGISGRFPGAMDIDEFWKNLEEGKDSITEVPKDrwdWREHYGNPdtdvnktdIKWGGFIdgVAEFDPLFFGISP 3417
Cdd:PRK07910 11 FPNVVVTGIAMTTALATDAETTWKLLLDGQSGIRTLDDP---FVEEFDLP--------VRIGGHL--LEEFDHQLTRVEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3418 READYVDPQQRLLMTYVWkalEDAGCP---PQSLsgtgtGIFIGTGNTGYKDL-FHRANLPIEGHAATGHM-IPSVGPNR 3492
Cdd:PRK07910 78 RRMSYLQRMSTVLGRRVW---ENAGSPevdTNRL-----MVSIGTGLGSAEELvFAYDDMRARGLRAVSPLaVQMYMPNG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3493 MSYF--LNIH---GPSEPVeTACSSSLVAIHRAVTAMQNGDCEMAIAGGVNTILTEEAHISYSKAGM-LSKD-----GRC 3561
Cdd:PRK07910 150 PAAAvgLERHakaGVITPV-SACASGSEAIAQAWRQIVLGEADIAICGGVETRIEAVPIAGFAQMRIvMSTNnddpaGAC 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3562 KTFSADANGYVRGEGVGMVMLKKLEDAERDGNHIYGVIRGTAENHGGRANTLTSPNPKAQADLLVRAYRQAGIDPSTVTY 3641
Cdd:PRK07910 229 RPFDKDRDGFVFGEGGALMVIETEEHAKARGANILARIMGASITSDGFHMVAPDPNGERAGHAMTRAIELAGLTPGDIDH 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3642 IEAHGTGTELGDPIEINGLKAAfkelsnmrgesqpdVPDHRCGIGSVKSNIGHLELAAGISGLIKVLLQMKHKTLVKSLH 3721
Cdd:PRK07910 309 VNAHATGTSVGDVAEGKAINNA--------------LGGHRPAVYAPKSALGHSVGAVGAVESILTVLALRDGVIPPTLN 374
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1776025254 3722 CETLNPYLQLTdspfyIVQEKqewksvtdcdgnelPRRAGI-----SSFGIGGVNAHIVIEEY 3779
Cdd:PRK07910 375 LENLDPEIDLD-----VVAGE--------------PRPGNYryainNSFGFGGHNVALAFGRY 418
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
1160-1641 |
3.31e-18 |
|
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called acetyl-CoA synthetase and acetyl-activating enzyme. It catalyzes the reaction ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA and belongs to the family of AMP-binding enzymes described by pfam00501.
Pssm-ID: 274022 [Multi-domain] Cd Length: 626 Bit Score: 92.31 E-value: 3.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1160 EQQAKKTPDRAAVSYEG------QTLTYRELDERSTQLAIYLQAHGVGP-DRLAgIYVDRSLDMLVGLLAILKAGGAYVP 1232
Cdd:TIGR02188 64 DRHLEARPDKVAIIWEGdepgevRKITYRELHREVCRFANVLKSLGVKKgDRVA-IYMPMIPEAAIAMLACARIGAIHSV 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1233 LDPSYPAERLEYMLEDSEVFITLTTSElvntlSWNG---------VTTALL--------------------------DQD 1277
Cdd:TIGR02188 143 VFGGFSAEALADRINDAGAKLVITADE-----GLRGgkviplkaiVDEALEkcpvsvehvlvvrrtgnpvvpwvegrDVW 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1278 WDEIAQTASDrKVLTRTVTPENLAYVIYTSGSTGKPKGVMipHKaltnflvsmgetpglTAEDKMLAVTT--YCFDIAAL 1355
Cdd:TIGR02188 218 WHDLMAKASA-YCEPEPMDSEDPLFILYTSGSTGKPKGVL--HT---------------TGGYLLYAAMTmkYVFDIKDG 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1356 ELFL-----------------PLIKGAHCYIcqTEHTKD----------VEKLKRDIRTIKPTVMqatpatwKMLFYSGw 1408
Cdd:TIGR02188 280 DIFWctadvgwitghsyivygPLANGATTVM--FEGVPTypdpgrfweiIEKHKVTIFYTAPTAI-------RALMRLG- 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1409 enEENVKI-------LCG--GEAL-PETLKRYFLDTGSEA-------W------NMFGP----TETTIWSAvqrindecs 1461
Cdd:TIGR02188 350 --DEWVKKhdlsslrLLGsvGEPInPEAWMWYYKVVGKERcpivdtwWqtetggIMITPlpgaTPTKPGSA--------- 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1462 ratiGRPIANTQIYITDSQLAPVP-AGVPGELCIAGD--GVAKGYYKKEEltdsRFIDNPFEPGSKLYRTGDMARWLPGG 1538
Cdd:TIGR02188 419 ----TLPFFGIEPAVVDEEGNPVEgPGEGGYLVIKQPwpGMLRTIYGDHE----RFVDTYFSPFPGYYFTGDGARRDKDG 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1539 RIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMDNL-----AAYYTAKHANA--SLTARELRHFVKNALP 1611
Cdd:TIGR02188 491 YIWITGRVDDVINVSGHRLGTAEIESALVSHPAVAEAAVVGIPDDIkgqaiYAFVTLKDGYEpdDELRKELRKHVRKEIG 570
|
570 580 590
....*....|....*....|....*....|
gi 1776025254 1612 AYMVPSYFIQLDHMPLTPNGKIDRNSLKNI 1641
Cdd:TIGR02188 571 PIAKPDKIRFVPGLPKTRSGKIMRRLLRKI 600
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
1180-1568 |
3.66e-18 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 92.39 E-value: 3.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1180 TYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLEDSEVFITLT--- 1256
Cdd:PLN02614 81 TYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVeek 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1257 -TSELVNT-----------LSWNGV---------TTALLDQDWDEIAQTASDRKVLTRTVTPENLAYVIYTSGSTGKPKG 1315
Cdd:PLN02614 161 kISELFKTcpnsteymktvVSFGGVsreqkeeaeTFGLVIYAWDEFLKLGEGKQYDLPIKKKSDICTIMYTSGTTGDPKG 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1316 VMIPHKALT-------NFLVSMGETpgLTAEDKMLAV--TTYCFDIAALELFLPLikGAHCYICQtehtKDVEKLKRDIR 1386
Cdd:PLN02614 241 VMISNESIVtliagviRLLKSANAA--LTVKDVYLSYlpLAHIFDRVIEECFIQH--GAAIGFWR----GDVKLLIEDLG 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1387 TIKPTVMQATPATWKMLfYSGWENE-------------------------------------------------ENVKIL 1417
Cdd:PLN02614 313 ELKPTIFCAVPRVLDRV-YSGLQKKlsdggflkkfvfdsafsykfgnmkkgqshveasplcdklvfnkvkqglgGNVRII 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1418 CGGEALPETLKRYFLDTGS--EAWNMFGPTETTIWSAVQRINDECSRATIGRPIANTQIyitdsQLAPVP-------AGV 1488
Cdd:PLN02614 392 LSGAAPLASHVESFLRVVAccHVLQGYGLTESCAGTFVSLPDELDMLGTVGPPVPNVDI-----RLESVPemeydalAST 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1489 P-GELCIAGDGVAKGYYKKEELTDSRFIDNpfepgskLYRTGDMARWLPGGRIEYIGRIDNQVKI-RGFRIELGDIESRL 1566
Cdd:PLN02614 467 PrGEICIRGKTLFSGYYKREDLTKEVLIDG-------WLHTGDVGEWQPNGSMKIIDRKKNIFKLsQGEYVAVENIENIY 539
|
..
gi 1776025254 1567 SE 1568
Cdd:PLN02614 540 GE 541
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
185-549 |
4.74e-18 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 92.72 E-value: 4.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 185 SPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDH----VGG--IGMLHLRDVYLgcqei 258
Cdd:PRK06814 791 DPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPEDKVFNALPVFHsfglTGGlvLPLLSGVKVFL----- 865
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 259 nvssetiLMEPLkwldwidHYRA--SVTWAPN--FAFGlvTDF--------AEeikdrKWDLSSMRYMLNGGEAMVA--- 323
Cdd:PRK06814 866 -------YPSPL-------HYRIipELIYDTNatILFG--TDTflngyaryAH-----PYDFRSLRYVFAGAEKVKEetr 924
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 324 -----KVGRRILELlephglpadairpaWGMSETSSGVIFSHE-FTRAGTsdddhfveIGSPIPGFSMRIvnDHNELVEE 397
Cdd:PRK06814 925 qtwmeKFGIRILEG--------------YGVTETAPVIALNTPmHNKAGT--------VGRLLPGIEYRL--EPVPGIDE 980
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 398 GeiGRFQVSGLSVTSGYYqRPDlNESVF--TEDGWFETGDL------GFlrngrLTITGRTKDAIIINGinyyshaiE-- 467
Cdd:PRK06814 981 G--GRLFVRGPNVMLGYL-RAE-NPGVLepPADGWYDTGDIvtideeGF-----ITIKGRAKRFAKIAG--------Emi 1043
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 468 --SAVEEL-SEIETSYTAACAVRLGQNSTDQLaIFFVTSAKLNDEqmsqllrNIQSHVSQvIGVtPEYLLP---VQKEEI 541
Cdd:PRK06814 1044 slAAVEELaAELWPDALHAAVSIPDARKGERI-ILLTTASDATRA-------AFLAHAKA-AGA-SELMVPaeiITIDEI 1113
|
....*...
gi 1776025254 542 PKTAIGKI 549
Cdd:PRK06814 1114 PLLGTGKI 1121
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
172-671 |
4.80e-18 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 92.80 E-value: 4.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 172 LLSAEADTDWHQSSPEDLALLLLTSGSTGTPKAVMLNHRNImsmVKGIIQMQ---GFTREDI-------TFN------WM 235
Cdd:PRK10252 583 PLAPQGAAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAI---VNRLLWMQnhyPLTADDVvlqktpcSFDvsvwefFW 659
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 236 PFdhvggigmlhlrdvylgcqeinVSSETILM-------EPLKWLDWIDHYRASVT-WAPNFAFGLVTDFAEEIKDRKwd 307
Cdd:PRK10252 660 PF----------------------IAGAKLVMaepeahrDPLAMQQFFAEYGVTTThFVPSMLAAFVASLTPEGARQS-- 715
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 308 LSSMRYMLNGGEAMVAKVGRRILELL--EPHGL--PADAI-----RPAWGmsetssgvifshEFTRAGTSDDdhfVEIGS 378
Cdd:PRK10252 716 CASLRQVFCSGEALPADLCREWQQLTgaPLHNLygPTEAAvdvswYPAFG------------EELAAVRGSS---VPIGY 780
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 379 PIPGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGYYQRPDLNESVFTEDGW------FETGDLG-FLRNGRLTITGRTK 451
Cdd:PRK10252 781 PVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFapgermYRTGDVArWLDDGAVEYLGRSD 860
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 452 DAIIINGINYYSHAIESAVEELSEIETSYTAACAVRLGQNSTD---QLaIFFVTSAKLNDEQMSQLlrniQSHVSQVIgv 528
Cdd:PRK10252 861 DQLKIRGQRIELGEIDRAMQALPDVEQAVTHACVINQAAATGGdarQL-VGYLVSQSGLPLDTSAL----QAQLRERL-- 933
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 529 tPEYLLP---VQKEEIPKTAIGKIQRTQLKtsfengefdhllhKPNrmndavqdeemQQADHVKRVREEIQEHLLTCLTE 605
Cdd:PRK10252 934 -PPHMVPvvlLQLDQLPLSANGKLDRKALP-------------LPE-----------LKAQVPGRAPKTGTETIIAAAFS 988
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1776025254 606 ELhVSRDWVEPNANIQSLGVNSIKMMKLIRSIEKNYHIKLTAREIHQYPTIERLASYLSEHEDLSS 671
Cdd:PRK10252 989 SL-LGCDVVDADADFFALGGHSLLAMKLAAQLSRQFARQVTPGQVMVASTVAKLATLLDAEEDESR 1053
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
34-608 |
5.28e-18 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 92.02 E-value: 5.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 34 VLYRTAAELGDTKGIIYLQPDGTevyqSYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNSQLLPAFWGCVLTGVVpAP 113
Cdd:PRK06060 9 LLAEQASEAGWYDRPAFYAADVV----THGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVM-AF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 114 LAVPPTYAESSSgTQKLKDAWTLLDKPAVITDRGMHQEMLDWAkeqglegfraiiveDLLSAEA---DTDWHQSSPEDLA 190
Cdd:PRK06060 84 LANPELHRDDHA-LAARNTEPALVVTSDALRDRFQPSRVAEAA--------------ELMSEAArvaPGGYEPMGGDALA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 191 LLLLTSGSTGTPKAVMLNHRNIMSMVKGII-QMQGFTREDITFN--------------WMPFdHVGGIGMLHlrdvylgc 255
Cdd:PRK06060 149 YATYTSGTTGPPKAAIHRHADPLTFVDAMCrKALRLTPEDTGLCsarmyfayglgnsvWFPL-ATGGSAVIN-------- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 256 qEINVSSETILMeplkwldwidhyrASVTWAPNFAFGLVTDFAEEIKDRKWD-LSSMRYMLNGGEAMVAKVGRRILELLe 334
Cdd:PRK06060 220 -SAPVTPEAAAI-------------LSARFGPSVLYGVPNFFARVIDSCSPDsFRSLRCVVSAGEALELGLAERLMEFF- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 335 pHGLPadaIRPAWGMSETSSGVIfsheftrAGTSDDDHFVEIGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGY 414
Cdd:PRK06060 285 -GGIP---ILDGIGSTEVGQTFV-------SNRVDEWRLGTLGRVLPPYEIRVVAPDGTTAGPGVEGDLWVRGPAIAKGY 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 415 YQRPDlneSVFTEDGWFETGD-LGFLRNGRLTITGRTKDAIIINGINYYSHAIESAVEElsEIETSYTAACAVRLGQNST 493
Cdd:PRK06060 354 WNRPD---SPVANEGWLDTRDrVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIE--DEAVAEAAVVAVRESTGAS 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 494 DQLAIFFVTSAKLNDEQ-MSQLLRNIQSHVSQVigVTPEYLLPVqkEEIPKTAIGKIQRTQL------KTSFENGEFDHL 566
Cdd:PRK06060 429 TLQAFLVATSGATIDGSvMRDLHRGLLNRLSAF--KVPHRFAVV--DRLPRTPNGKLVRGALrkqsptKPIWELSLTEPG 504
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 1776025254 567 LHKPNRMNDAVQDEEMQQADHvkrVREEIQEHLLTCLTEELH 608
Cdd:PRK06060 505 SGVRAQRDDLSASNMTIAGGN---DGGATLRERLVALRQERQ 543
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
1299-1633 |
7.16e-18 |
|
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.
Pssm-ID: 341293 [Multi-domain] Cd Length: 330 Bit Score: 88.33 E-value: 7.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1299 NLAYVIYTSGSTGKPKGVMIPHKALTNFLVSMGETPGLTAEDKMLAVTTY--CFDIAAlELFLPLIKGAHCYicqTEHTK 1376
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFfhTFGYKA-GIVACLLTGATVV---PVAVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1377 DVEKLKRDIRTIKPTVMQATPATWKMLFYSGWENEENVKIL----CGGEALPETL-KRYFLDTGSEA-WNMFGPTETTIW 1450
Cdd:cd17638 77 DVDAILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLraavTGAATVPVELvRRMRSELGFETvLTAYGLTEAGVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1451 SAVQRINDECSRA-TIGRPIANTQIYITDsqlapvpagvPGELCIAGDGVAKGYYKKEELTdSRFIDnpfepGSKLYRTG 1529
Cdd:cd17638 157 TMCRPGDDAETVAtTCGRACPGFEVRIAD----------DGEVLVRGYNVMQGYLDDPEAT-AEAID-----ADGWLHTG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1530 DMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVV--VAD--MDNLAAYYTAKHANASLTARELRHF 1605
Cdd:cd17638 221 DVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVigVPDerMGEVGKAFVVARPGVTLTEEDVIAW 300
|
330 340
....*....|....*....|....*...
gi 1776025254 1606 VKNALPAYMVPSYFIQLDHMPLTPNGKI 1633
Cdd:cd17638 301 CRERLANYKVPRFVRFLDELPRNASGKV 328
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
1154-1638 |
8.82e-18 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 90.86 E-value: 8.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1154 TFHELFEQQAkkTPDRAAVSYEGQTLTYRE-LDERSTQ--LAIYLQAHGvGPDRLaGIYVDRSLDMLVGLLAILKAGGAY 1230
Cdd:PRK13388 4 TIAQLLRDRA--GDDTIAVRYGDRTWTWREvLAEAAARaaALIALADPD-RPLHV-GVLLGNTPEMLFWLAAAALGGYVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1231 VPLDPSYPAERLEYMLEDSEVFITLTTSE---LVNTLSWNGVTtaLLDQDWDEIAQTASDRKVLT--RTVTPENLAYVIY 1305
Cdd:PRK13388 80 VGLNTTRRGAALAADIRRADCQLLVTDAEhrpLLDGLDLPGVR--VLDVDTPAYAELVAAAGALTphREVDAMDPFMLIF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1306 TSGSTGKPKGVMIPHKALTNFLVSMGETPGLTAEDkmlavTTYCfdiaALELF----------LPLIKGAHcyICQTEHT 1375
Cdd:PRK13388 158 TSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDD-----VCYV----SMPLFhsnavmagwaPAVASGAA--VALPAKF 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1376 KDVEKLKrDIRTIKPTVMQ----------ATPATwkmlfysgWENEEN-VKILCGGEALPETLKRYFLDTGSEAWNMFGP 1444
Cdd:PRK13388 227 SASGFLD-DVRRYGATYFNyvgkplayilATPER--------PDDADNpLRVAFGNEASPRDIAEFSRRFGCQVEDGYGS 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1445 TETTIwsAVQRiNDECSRATIGRPIANTQIYITDS-QLAPV-----------PAGVPGELC-IAGDGVAKGYYKKEELTD 1511
Cdd:PRK13388 298 SEGAV--IVVR-EPGTPPGSIGRGAPGVAIYNPETlTECAVarfdahgallnADEAIGELVnTAGAGFFEGYYNNPEATA 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1512 SRFIDNpfepgskLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMDNlaayYTAK 1591
Cdd:PRK13388 375 ERMRHG-------MYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDE----RVGD 443
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1776025254 1592 HANASLTARELRHFVKNALPAYMV----------PSYFIQLDHMPLTPNGKIDRNSL 1638
Cdd:PRK13388 444 QVMAALVLRDGATFDPDAFAAFLAaqpdlgtkawPRYVRIAADLPSTATNKVLKREL 500
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
1179-1639 |
1.50e-17 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 89.16 E-value: 1.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1179 LTYRELDERSTQLAIYLQAHGVGPDrlagiyvDRSLDML-------VGLLAILKAGGAYVPldpsypAERLeymledsev 1251
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRG-------DRILLMLgnvvelwEAMLAAMKLGAVVIP------ATTL--------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1252 fitLTTSELVNTLSWNGVTTALLDQDwdeiaqTASDRKVLtrtvtpenlayVIYTSGSTGKPKGVMIPHKALTNFLVSMG 1331
Cdd:cd05974 59 ---LTPDDLRDRVDRGGAVYAAVDEN------THADDPML-----------LYFTSGTTSKPKLVEHTHRSYPVGHLSTM 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1332 ETPGLTAEDKMLAVTTYCFDIAALE-LFLPLIKGAhCYICQTEHTKDVEKLKRDIRTIKPTVMQATPATWKMLFYsgwEN 1410
Cdd:cd05974 119 YWIGLKPGDVHWNISSPGWAKHAWScFFAPWNAGA-TVFLFNYARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQ---QD 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1411 EENVKI----LCG-GEAL-PETLKRYfldtgSEAWNM-----FGPTETTIW---SAVQRIndecSRATIGRPIANTQIYI 1476
Cdd:cd05974 195 LASFDVklreVVGaGEPLnPEVIEQV-----RRAWGLtirdgYGQTETTALvgnSPGQPV----KAGSMGRPLPGYRVAL 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1477 TDSQLAPVPAGvpgELCIA-GD----GVAKGYYKKEELTDSRFidnpfepGSKLYRTGDMARWLPGGRIEYIGRIDNQVK 1551
Cdd:cd05974 266 LDPDGAPATEG---EVALDlGDtrpvGLMKGYAGDPDKTAHAM-------RGGYYRTGDIAMRDEDGYLTYVGRADDVFK 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1552 IRGFRIELGDIESRLSEHPGILECVVVADMDNL-----AAY--YTAKHANASLTARELRHFVKNALPAYMVPSYfIQLDH 1624
Cdd:cd05974 336 SSDYRISPFELESVLIEHPAVAEAAVVPSPDPVrlsvpKAFivLRAGYEPSPETALEIFRFSRERLAPYKRIRR-LEFAE 414
|
490
....*....|....*
gi 1776025254 1625 MPLTPNGKIDRNSLK 1639
Cdd:cd05974 415 LPKTISGKIRRVELR 429
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
1174-1639 |
2.19e-17 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 89.03 E-value: 2.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1174 YEGQTLTYRELDERSTQLAIYLQ-AHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAyvpldpsyPAerleymledsevf 1252
Cdd:cd05937 1 FEGKTWTYSETYDLVLRYAHWLHdDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAA--------PA------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1253 itlttseLVNtlsWNGVTTALLdqdwdEIAQTASDRKVLtrtVTPENLAYVIYTSGSTGKPKGVMIPHKALTNFLVSMGE 1332
Cdd:cd05937 60 -------FIN---YNLSGDPLI-----HCLKLSGSRFVI---VDPDDPAILIYTSGTTGLPKAAAISWRRTLVTSNLLSH 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1333 TPGLTAEDKMLavttYCfdiaalelfLPLIKGAHCYICQTE-----------HTKDVEKLKRDIRTIKPTVMQ------- 1394
Cdd:cd05937 122 DLNLKNGDRTY----TC---------MPLYHGTAAFLGACNclmsggtlalsRKFSASQFWKDVRDSGATIIQyvgelcr 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1395 ---ATPAtwkmlfySGWENEENVKILCGGEALPETLKRYFLDTG-SEAWNMFGPTE-----TTIWSAVQRINDECSRATI 1465
Cdd:cd05937 189 yllSTPP-------SPYDRDHKVRVAWGNGLRPDIWERFRERFNvPEIGEFYAATEgvfalTNHNVGDFGAGAIGHHGLI 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1466 GRPIANTQIYI------TDSQL--------APVPAGVPGELCIA----GDGVAKGYYKKEELTDSRFIDNPFEPGSKLYR 1527
Cdd:cd05937 262 RRWKFENQVVLvkmdpeTDDPIrdpktgfcVRAPVGEPGEMLGRvpfkNREAFQGYLHNEDATESKLVRDVFRKGDIYFR 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1528 TGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVV----VADMDNLAAYYTAKHANASL-----T 1598
Cdd:cd05937 342 TGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVygvkVPGHDGRAGCAAITLEESSAvptefT 421
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1776025254 1599 ARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLK 1639
Cdd:cd05937 422 KSLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLR 462
|
|
| fabG |
PRK05557 |
3-ketoacyl-(acyl-carrier-protein) reductase; Validated |
2850-3015 |
2.26e-17 |
|
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
Pssm-ID: 235500 [Multi-domain] Cd Length: 248 Bit Score: 84.86 E-value: 2.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGLLFAKEIAnRTGrSTIVLTGRSvlSEDKENEL-EALRSIGAEVVYREADVSDQHAVHHLFEEIKERYG 2928
Cdd:PRK05557 7 VALVTGASRGIGRAIAERLA-AQG-ANVVINYAS--SEAGAEALvAEIGALGGKALAVQGDVSDAESVERAVDEAKAEFG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2929 TLNGIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSGLLHvdeCSKDFPLDF-------FIFFSSVSGCLGNAGQADYAAAN 3001
Cdd:PRK05557 83 GVDILVNNAGITRDNLLMRMKEEDWDRVIDTNLTGVFN---LTKAVARPMmkqrsgrIINISSVVGLMGNPGQANYAASK 159
|
170
....*....|....
gi 1776025254 3002 SFMDAFAeyrRSLA 3015
Cdd:PRK05557 160 AGVIGFT---KSLA 170
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
186-452 |
3.49e-17 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 89.39 E-value: 3.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 186 PEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDH----VGGIGMLHLrDVYLGCQEINVs 261
Cdd:PLN02736 220 PEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKFYPSDVHISYLPLAHiyerVNQIVMLHY-GVAVGFYQGDN- 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 262 setilmepLKWLDWIDHYR----ASVTWAPNFAFGLVTDFAEE---IKDR---------------------KWDL----- 308
Cdd:PLN02736 298 --------LKLMDDLAALRptifCSVPRLYNRIYDGITNAVKEsggLKERlfnaaynakkqalengknpspMWDRlvfnk 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 309 ------SSMRYMLNGGEAMVAKV--------GRRILEllephglpadairpAWGMSETSSgVIfsheftrAGTSDDDHFV 374
Cdd:PLN02736 370 ikaklgGRVRFMSSGASPLSPDVmeflricfGGRVLE--------------GYGMTETSC-VI-------SGMDEGDNLS 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 375 -EIGSPIPGFSMRIVN--DHNELVEE-----GEIGrfqVSGLSVTSGYYQRPDLNESVFTEDGWFETGDLG-FLRNGRLT 445
Cdd:PLN02736 428 gHVGSPNPACEVKLVDvpEMNYTSEDqpyprGEIC---VRGPIIFKGYYKDEVQTREVIDEDGWLHTGDIGlWLPGGRLK 504
|
....*..
gi 1776025254 446 ITGRTKD 452
Cdd:PLN02736 505 IIDRKKN 511
|
|
| C_NRPS-like |
cd19537 |
Condensation family domain with an atypical active site motif; Condensation (C) domains of ... |
695-1106 |
3.51e-17 |
|
Condensation family domain with an atypical active site motif; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily typically have a non-canonical conserved SHXXXDX(14)Y motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380460 [Multi-domain] Cd Length: 395 Bit Score: 87.24 E-value: 3.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 695 PLSEVQKGLWTLQKMSPEKSAYHVPLCFKFSSGLHLETLQQAFGLVLNQHPILKHVIQEKDGVP--ILKNEPALSIEIKT 772
Cdd:cd19537 3 ALSPIEREWWHKYQLSTGTSSFNVSFACRLSGDVDRDRLASAWNTVLARHRILRSRYVPRDGGLrrSYSSSPPRVQRVDT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 773 ENISsmKESDIPAFLrkkvkepyvkENSPLVRVMSfSRSEqehfLLVVIHHLIFDGVSSVTFIHSLFDTYQ-LLLKGQQP 851
Cdd:cd19537 83 LDVW--KEINRPFDL----------EREDPIRVFI-SPDT----LLVVMSHIICDLTTLQLLLREVSAAYNgKLLPPVRR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 852 EiavspaiYHDFAAWEKNMLAGkdgvkHRTYWQKQLSGtLPNLQLPKVSA-------SSVSEFREDTYTRrlssgfMNQv 924
Cdd:cd19537 146 E-------YLDSTAWSRPASPE-----DLDFWSEYLSG-LPLLNLPRRTSsksyrgtSRVFQLPGSLYRS------LLQ- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 925 rmFAKEHSVN-----VTTVFLScymmlLGRYTGQKEQIVGMPAMVRPEERFDDAIGHFLNMLPIR--SELNPADTFSSFI 997
Cdd:cd19537 206 --FSTSSGITlhqlaLAAVALA-----LQDLSDRTDIVLGAPYLNRTSEEDMETVGLFLEPLPIRirFPSSSDASAADFL 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 998 SKLQLTILDGLDHAAyPFPKMVRDLNIPRSQAGSPVFQ---TafFYQNFLQSGSyqsllsryadfFSVDYVE--YIHQEG 1072
Cdd:cd19537 279 RAVRRSSQAALAHAI-PWHQLLEHLGLPPDSPNHPLFDvmvT--FHDDRGVSLA-----------LPIPGVEplYTWAEG 344
|
410 420 430
....*....|....*....|....*....|....*.
gi 1776025254 1073 -EYELVFELWET-EEKMELNIKYNTGLFDAASISAM 1106
Cdd:cd19537 345 aKFPLMFEFTALsDDSLLLRLEYDTDCFSEEEIDRI 380
|
|
| PRK06501 |
PRK06501 |
beta-ketoacyl-ACP synthase; |
1904-2183 |
4.30e-17 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235817 [Multi-domain] Cd Length: 425 Bit Score: 87.38 E-value: 4.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1904 LAQSGTIPTMISHKLGLRGPSYFVHANCSSSLIGLHSAYKSLLSAESDYALVGGA--TLHTESNIGYVHQPGLNFSSDGH 1981
Cdd:PRK06501 148 RFQFGSIADRLADRFGTRGLPISLSTACASGATAIQLGVEAIRRGETDRALCIATdgSVSAEALIRFSLLSALSTQNDPP 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1982 IKA---FDASADGMIGGEGVAVVLLKKAADAVKDGDHIYALLRGIGvnnDGADkvGFY----APSVKGQADVVQQVMNQT 2054
Cdd:PRK06501 228 EKAskpFSKDRDGFVMAEGAGALVLESLESAVARGAKILGIVAGCG---EKAD--SFHrtrsSPDGSPAIGAIRAALADA 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2055 KIHPESICYVEAHGTGTKLGDPIELAALTNVYRQYTNKTQfcgIGSVKTNIGHLDTAAGlagCIKVVMSLY---HQELAP 2131
Cdd:PRK06501 303 GLTPEQIDYINAHGTSTPENDKMEYLGLSAVFGERLASIP---VSSNKSMIGHTLTAAG---AVEAVFSLLtiqTGRLPP 376
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1776025254 2132 SINYKEPNPntdlaSSPFYVVDQKKtlsREIQThRAALS-SFGLGGTNTHAIF 2183
Cdd:PRK06501 377 TINYDNPDP-----AIPLDVVPNVA---RDARV-TAVLSnSFGFGGQNASLVL 420
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
153-555 |
4.36e-17 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 88.28 E-value: 4.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 153 LDWAKEQGlegfrAIIVEDLLSAEADtDWHQSSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITF 232
Cdd:PRK13382 168 VAWTDEDH-----DLTVEVLIAAHAG-QRPEPTGRKGRVILLTSGTTGTPKGARRSGPGGIGTLKAILDRTPWRAEEPTV 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 233 NWMPFDHVGGIGMLHLRdVYLGCqeinvsseTILM----EPLKWLDWIDHYRASVTWAPNFAFGLVTDFAEEIKDRkWDL 308
Cdd:PRK13382 242 IVAPMFHAWGFSQLVLA-ASLAC--------TIVTrrrfDPEATLDLIDRHRATGLAVVPVMFDRIMDLPAEVRNR-YSG 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 309 SSMRYMLNGGEAMVAKVgrrILELLEPHGlpaDAIRPAWGMSETSSGVIFSHEFTRAgtsdddHFVEIGSPIPGFSMRIV 388
Cdd:PRK13382 312 RSLRFAAASGSRMRPDV---VIAFMDQFG---DVIYNNYNATEAGMIATATPADLRA------APDTAGRPAEGTEIRIL 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 389 N-DHNELvEEGEIGRFQVSGLSVTSGYYQRPDLNesvfTEDGWFETGDLGFL-RNGRLTITGRTKDAIIINGINYYSHAI 466
Cdd:PRK13382 380 DqDFREV-PTGEVGTIFVRNDTQFDGYTSGSTKD----FHDGFMASGDVGYLdENGRLFVVGRDDEMIVSGGENVYPIEV 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 467 ESAVEELSEIetsytAACAVR------LGQnstdQLAIFFVTSAKLndeqmSQLLRNIQSHVSQVIGvtpEYLLP---VQ 537
Cdd:PRK13382 455 EKTLATHPDV-----AEAAVIgvddeqYGQ----RLAAFVVLKPGA-----SATPETLKQHVRDNLA---NYKVPrdiVV 517
|
410
....*....|....*...
gi 1776025254 538 KEEIPKTAIGKIQRTQLK 555
Cdd:PRK13382 518 LDELPRGATGKILRRELQ 535
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
166-560 |
4.68e-17 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 88.27 E-value: 4.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 166 AIIVEDLLS-AEADTDWHQSSPEDLALLLLTSGSTGTPKAVMLNHR-NIM-SMVKGIIQMQGFTREDITFNWMPFDHVG- 241
Cdd:PRK06018 155 AVAYEEWIAeADGDFAWKTFDENTAAGMCYTSGTTGDPKGVLYSHRsNVLhALMANNGDALGTSAADTMLPVVPLFHANs 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 242 -GIGM----LHLRDVYLGCQ-------EInVSSETILME---PLKWLDWIDHYRASvtwapnfafglvtdfaeeikdrKW 306
Cdd:PRK06018 235 wGIAFsapsMGTKLVMPGAKldgasvyEL-LDTEKVTFTagvPTVWLMLLQYMEKE----------------------GL 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 307 DLSSMRYMLNGGEAMvakvGRRILELLEPHGLpadAIRPAWGMSETSS-GVIFSHEFTRAGTSDD---DHFVEIGSPIPG 382
Cdd:PRK06018 292 KLPHLKMVVCGGSAM----PRSMIKAFEDMGV---EVRHAWGMTEMSPlGTLAALKPPFSKLPGDarlDVLQKQGYPPFG 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 383 FSMRIVNDH-NELVEEGE-IGRFQVSGLSVTSGYYQrpdLNESVFTEDGWFETGDLGFL-RNGRLTITGRTKDaiiingi 459
Cdd:PRK06018 365 VEMKITDDAgKELPWDGKtFGRLKVRGPAVAAAYYR---VDGEILDDDGFFDTGDVATIdAYGYMRITDRSKD------- 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 460 nyyshAIESAVEELSEIETSYTA--------ACAVRLGQNSTDQLAIFFVTSAKLNDEQMSQLLRNIQSHVSQviGVTPE 531
Cdd:PRK06018 435 -----VIKSGGEWISSIDLENLAvghpkvaeAAVIGVYHPKWDERPLLIVQLKPGETATREEILKYMDGKIAK--WWMPD 507
|
410 420
....*....|....*....|....*....
gi 1776025254 532 YLLPVqkEEIPKTAIGKIQRTQLKTSFEN 560
Cdd:PRK06018 508 DVAFV--DAIPHTATGKILKTALREQFKD 534
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
51-469 |
6.72e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 87.65 E-value: 6.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 51 LQPDGTEVyqSYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNSQLLPAFWGCVLTGVVPAPLAVPPTYAESssgtqkl 130
Cdd:PRK08276 5 MAPSGEVV--TYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEI------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 131 kdAWTLLDKPA--VITDRGMHQEMLDWAKE------------QGLEGFRAIivEDLLSAEADTDwhqssPEDL---ALLL 193
Cdd:PRK08276 76 --AYIVDDSGAkvLIVSAALADTAAELAAElpagvplllvvaGPVPGFRSY--EEALAAQPDTP-----IADEtagADML 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 194 LTSGSTGTPKAVM--LNHRNI-----MSMVKGIIQMQGFTrEDITFNWMPFDH--VGGIGMLHLRdvyLGcqeinvsSET 264
Cdd:PRK08276 147 YSSGTTGRPKGIKrpLPGLDPdeapgMMLALLGFGMYGGP-DSVYLSPAPLYHtaPLRFGMSALA---LG-------GTV 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 265 ILME---PLKWLDWIDHYRASVT-WAPnfafglvTDF------AEEIKDRkWDLSSMRYMLNGGEAMVAKVGRRILELle 334
Cdd:PRK08276 216 VVMEkfdAEEALALIERYRVTHSqLVP-------TMFvrmlklPEEVRAR-YDVSSLRVAIHAAAPCPVEVKRAMIDW-- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 335 phglpadairpaWG--MSETSSG-------VIFSHEF-TRAGTsdddhfveIGSPIPGfSMRIVNDHNELVEEGEIGR-- 402
Cdd:PRK08276 286 ------------WGpiIHEYYASsegggvtVITSEDWlAHPGS--------VGKAVLG-EVRILDEDGNELPPGEIGTvy 344
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1776025254 403 FQVSGLSVTsgYYQRPDLNESVFTEDGWFETGDLGFL-RNGRLTITGRTKDAIIINGINYYSHAIESA 469
Cdd:PRK08276 345 FEMDGYPFE--YHNDPEKTAAARNPHGWVTVGDVGYLdEDGYLYLTDRKSDMIISGGVNIYPQEIENL 410
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
188-477 |
7.42e-17 |
|
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341292 [Multi-domain] Cd Length: 333 Bit Score: 85.40 E-value: 7.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 188 DLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDHVGGIGMLhlrdvyLGCQEinVSSETILM 267
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAGLNLA------LATFH--AGGANVVM 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 268 E---PLKWLDWIDHYRASV--TWAPnfafgLVTDFAEEIKDRKWDLSSMRYMLnggeamvakvgrrilellephGLPA-D 341
Cdd:cd17637 73 EkfdPAEALELIEEEKVTLmgSFPP-----ILSNLLDAAEKSGVDLSSLRHVL---------------------GLDApE 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 342 AIRP-----------AWGMSETSSGVIFSHEFTRAGTSdddhfveiGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSV 410
Cdd:cd17637 127 TIQRfeettgatfwsLYGQTETSGLVTLSPYRERPGSA--------GRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLV 198
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 411 TSGYYQRPDLNESVFtEDGWFETGDLG-FLRNGRLTITGRT--KDAIIINGINYYSHAIESAVEELSEIE 477
Cdd:cd17637 199 FQGYWNLPELTAYTF-RNGWHHTGDLGrFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIA 267
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
183-473 |
8.44e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 87.49 E-value: 8.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 183 QSSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDHVGGIGMLhlrdvyLGCQEINVss 262
Cdd:PRK06164 177 AADPDAGALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGFSTL------LGALAGGA-- 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 263 eTILMEPL----KWLDWIDHYRASVTWAPNFAFGLVTDFAeeikDRKWDLSSMRYMlngGEAMVAKVGRRILELLEPHGL 338
Cdd:PRK06164 249 -PLVCEPVfdaaRTARALRRHRVTHTFGNDEMLRRILDTA----GERADFPSARLF---GFASFAPALGELAALARARGV 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 339 PadaIRPAWGMSETSSgvIFSheftrAGTSDDDHFVEI---GSPI-PGFSMRIVN-DHNELVEEGEIGRFQVSGLSVTSG 413
Cdd:PRK06164 321 P---LTGLYGSSEVQA--LVA-----LQPATDPVSVRIeggGRPAsPEARVRARDpQDGALLPDGESGEIEIRAPSLMRG 390
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1776025254 414 YYQRPDLNESVFTEDGWFETGDLGFLR-NGRLTITGRTKDAIIINGINYYSHAIESAVEEL 473
Cdd:PRK06164 391 YLDNPDATARALTDDGYFRTGDLGYTRgDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEAL 451
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
1157-1546 |
9.51e-17 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 87.79 E-value: 9.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1157 ELFEQQAKKTPDRAAVSYEGQT------LTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAY 1230
Cdd:PRK12582 53 HLLAKWAAEAPDRPWLAQREPGhgqwrkVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPA 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1231 VPLDPSYPA-----ERLEY----------MLEDSEVFitlttSELVNTLSWNGVTTALLDQDWDEIAQTASDRKVLT--- 1292
Cdd:PRK12582 133 APVSPAYSLmshdhAKLKHlfdlvkprvvFAQSGAPF-----ARALAALDLLDVTVVHVTGPGEGIASIAFADLAATppt 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1293 -------RTVTPENLAYVIYTSGSTGKPKGVMIPHKALTNFLVsMGEtpGLTAEDKMLAVTTYcfdiaaLElFLP----- 1360
Cdd:PRK12582 208 aavaaaiAAITPDTVAKYLFTSGSTGMPKAVINTQRMMCANIA-MQE--QLRPREPDPPPPVS------LD-WMPwnhtm 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1361 ---------LIKGAHCYIcqtEHTKDV----EKLKRDIRTIKPTVMQATPATWKMLFysgwENEENVKILC--------- 1418
Cdd:PRK12582 278 ggnanfnglLWGGGTLYI---DDGKPLpgmfEETIRNLREISPTVYGNVPAGYAMLA----EAMEKDDALRrsffknlrl 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1419 ---GGEALPETL--KRYFL---DTGSEA--WNMFGPTET------TIWsAVQRIndecsrATIGRPIANTQIyitdsQLA 1482
Cdd:PRK12582 351 mayGGATLSDDLyeRMQALavrTTGHRIpfYTGYGATETaptttgTHW-DTERV------GLIGLPLPGVEL-----KLA 418
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1776025254 1483 PVpaGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPFepgsklYRTGDMARWL----PGGRIEYIGRI 1546
Cdd:PRK12582 419 PV--GDKYEVRVKGPNVTPGYHKDPELTAAAFDEEGF------YRLGDAARFVdpddPEKGLIFDGRV 478
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
195-467 |
1.02e-16 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 87.56 E-value: 1.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 195 TSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTRED---ITfnwMPFDHVGGIGMLHLrdvylGCqeINVSSETILM---- 267
Cdd:PRK08315 207 TSGTTGFPKGATLTHRNILNNGYFIGEAMKLTEEDrlcIP---VPLYHCFGMVLGNL-----AC--VTHGATMVYPgegf 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 268 EPLKWLDWIDHYRASVtwapnfAFGLVTDFAEEIKDR---KWDLSSMRYMLNGG-----EAMvakvgRRILELLephGLP 339
Cdd:PRK08315 277 DPLATLAAVEEERCTA------LYGVPTMFIAELDHPdfaRFDLSSLRTGIMAGspcpiEVM-----KRVIDKM---HMS 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 340 ADAIrpAWGMSETSSGvifsheFTRAGTSDD-DHFVE-IGSPIPGFSMRIVN-DHNELVEEGEIGRFQVSGLSVTSGYYQ 416
Cdd:PRK08315 343 EVTI--AYGMTETSPV------STQTRTDDPlEKRVTtVGRALPHLEVKIVDpETGETVPRGEQGELCTRGYSVMKGYWN 414
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1776025254 417 RPDLNESVFTEDGWFETGDLGFLR-NGRLTITGRTKDAIIINGINYYSHAIE 467
Cdd:PRK08315 415 DPEKTAEAIDADGWMHTGDLAVMDeEGYVNIVGRIKDMIIRGGENIYPREIE 466
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1296-1634 |
1.06e-16 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 85.51 E-value: 1.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1296 TPENLaYVIYTSGSTGKPKGVMIPHKALtnFLVSMGETPGLTAEDKMLAVTTYCFDIAALELFL---PLIKGAHCY---- 1368
Cdd:cd05924 2 SADDL-YILYTGGTTGMPKGVMWRQEDI--FRMLMGGADFGTGEFTPSEDAHKAAAAAAGTVMFpapPLMHGTGSWtafg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1369 -------ICQTEHTKDVEKLKRDIRTIKPTVMQ------ATPATWKMLFYSGWENEENVKILCGGEALPETLKRYFLDTG 1435
Cdd:cd05924 79 gllggqtVVLPDDRFDPEEVWRTIEKHKVTSMTivgdamARPLIDALRDAGPYDLSSLFAISSGGALLSPEVKQGLLELV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1436 SEA--WNMFGPTETTIWSAVqrINDECSRATIGRPIANTQIYITDSQLAPVPAGVPGELCIAGDG-VAKGYYKKEELTDS 1512
Cdd:cd05924 159 PNItlVDAFGSSETGFTGSG--HSAGSGPETGPFTRANPDTVVLDDDGRVVPPGSGGVGWIARRGhIPLGYYGDEAKTAE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1513 RF--IDnpfepGSKLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMD-----NLA 1585
Cdd:cd05924 237 TFpeVD-----GVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDerwgqEVV 311
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1776025254 1586 AYYTAKhANASLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKID 1634
Cdd:cd05924 312 AVVQLR-EGAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGKAD 359
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
1162-1639 |
1.18e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 86.99 E-value: 1.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1162 QAKKTPDRAAV--SYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPA 1239
Cdd:PRK13390 6 HAQIAPDRPAVivAETGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1240 ERLEYMLEDSEVFITLTTSELVNTLSWNGVTTALLDQDWDEIAQTASDRKVLTRTVTPENL----AYVIYTSGSTGKPKG 1315
Cdd:PRK13390 86 PEADYIVGDSGARVLVASAALDGLAAKVGADLPLRLSFGGEIDGFGSFEAALAGAGPRLTEqpcgAVMLYSSGTTGFPKG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1316 VM--IPHKALtnflvsmgETPGltaeDKMLAVTTYCFDIAALELFL---PLIKGAHCYICQTEHTK----------DVEK 1380
Cdd:PRK13390 166 IQpdLPGRDV--------DAPG----DPIVAIARAFYDISESDIYYssaPIYHAAPLRWCSMVHALggtvvlakrfDAQA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1381 LKRDIRTIKPTVMQATPATW-KML-----FYSGWENEENVKILCGGEALPETLKRYFLD-TGSEAWNMFGPTETTIWSAV 1453
Cdd:PRK13390 234 TLGHVERYRITVTQMVPTMFvRLLkldadVRTRYDVSSLRAVIHAAAPCPVDVKHAMIDwLGPIVYEYYSSTEAHGMTFI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1454 QRINDECSRATIGRPIANTqIYITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSrfIDNPFEPgskLYRT-GDMA 1532
Cdd:PRK13390 314 DSPDWLAHPGSVGRSVLGD-LHICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAA--AQHPAHP---FWTTvGDLG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1533 RWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMD-------NLAAYYTAKHANASLTARELRHF 1605
Cdd:PRK13390 388 SVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDpemgeqvKAVIQLVEGIRGSDELARELIDY 467
|
490 500 510
....*....|....*....|....*....|....
gi 1776025254 1606 VKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLK 1639
Cdd:PRK13390 468 TRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
1166-1660 |
1.42e-16 |
|
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.
Pssm-ID: 341271 [Multi-domain] Cd Length: 617 Bit Score: 87.37 E-value: 1.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1166 TPDRAAVSYEG------QTLTYRELDERSTQLAIYLQAHGVGP-DRLAgIYVDRSLDMLVGLLAILKAG-------GAYV 1231
Cdd:cd05967 64 RGDQIALIYDSpvtgteRTYTYAELLDEVSRLAGVLRKLGVVKgDRVI-IYMPMIPEAAIAMLACARIGaihsvvfGGFA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1232 P---------------LDPSY---PAERLEY--MLEDSevfITLTTSELVNTLSWN------GVTTALLDQDWDEIAQTA 1285
Cdd:cd05967 143 AkelasriddakpkliVTASCgiePGKVVPYkpLLDKA---LELSGHKPHHVLVLNrpqvpaDLTKPGRDLDWSELLAKA 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1286 SDRKVLTrtVTPENLAYVIYTSGSTGKPKGVMIP---HKALTNFlvSMGETPGLTAEDKMLAVTtycfDIA-----ALEL 1357
Cdd:cd05967 220 EPVDCVP--VAATDPLYILYTSGTTGKPKGVVRDnggHAVALNW--SMRNIYGIKPGDVWWAAS----DVGwvvghSYIV 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1358 FLPLIKGAHC--YICQTEHTKD-------VEKLK--------RDIRTIKptvmQATPATWKMLFY--SGWENeenvkILC 1418
Cdd:cd05967 292 YGPLLHGATTvlYEGKPVGTPDpgafwrvIEKYQvnalftapTAIRAIR----KEDPDGKYIKKYdlSSLRT-----LFL 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1419 GGEAL-PET-------LKRYFLDtgsEAWNmfgpTET--TIWSAVQRINDECSRA-TIGRPIANTQIYITDSQLAPVPAG 1487
Cdd:cd05967 363 AGERLdPPTlewaentLGVPVID---HWWQ----TETgwPITANPVGLEPLPIKAgSPGKPVPGYQVQVLDEDGEPVGPN 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1488 VPGELCIAGD---GVAKGYYKKEEltdsRFIDNPFEPGSKLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIES 1564
Cdd:cd05967 436 ELGNIVIKLPlppGCLLTLWKNDE----RFKKLYLSKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEE 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1565 RLSEHPGILECVVVADMDNLA-----AYYTAKhANASLTA----RELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDR 1635
Cdd:cd05967 512 SVLSHPAVAECAVVGVRDELKgqvplGLVVLK-EGVKITAeeleKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILR 590
|
570 580
....*....|....*....|....*
gi 1776025254 1636 NSLKNIdLSGEQLkqrqTSPKNIQD 1660
Cdd:cd05967 591 RTLRKI-ADGEDY----TIPSTIED 610
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
1179-1572 |
2.08e-16 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 86.82 E-value: 2.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1179 LTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLEDSEVFITLT-- 1256
Cdd:PLN02861 78 LTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSIAFVqe 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1257 -------------TSELVNTLSWNGVTTALLDQ---------DWDEIAQTASDRKVLTRTvTPENLAYVIYTSGSTGKPK 1314
Cdd:PLN02861 158 skissilsclpkcSSNLKTIVSFGDVSSEQKEEaeelgvscfSWEEFSLMGSLDCELPPK-QKTDICTIMYTSGTTGEPK 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1315 GVMIPHKALtnflvsmgeTPGLTAEDKMLAVTtycfDIAALE-----LFLPLikgAHCY------ICQTEHTK------D 1377
Cdd:PLN02861 237 GVILTNRAI---------IAEVLSTDHLLKVT----DRVATEedsyfSYLPL---AHVYdqvietYCISKGASigfwqgD 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1378 VEKLKRDIRTIKPTVMQATPATW------------------KMLF---YS--------GWENEE---------------- 1412
Cdd:PLN02861 301 IRYLMEDVQALKPTIFCGVPRVYdriytgimqkissggmlrKKLFdfaYNyklgnlrkGLKQEEasprldrlvfdkikeg 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1413 ---NVKILCGGEA-LPETLKRYFLDTG-SEAWNMFGPTETTIWSAVQRINDECSRATIGRPIANTQiyitdSQLAPVP-- 1485
Cdd:PLN02861 381 lggRVRLLLSGAApLPRHVEEFLRVTScSVLSQGYGLTESCGGCFTSIANVFSMVGTVGVPMTTIE-----ARLESVPem 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1486 -----AGVP-GELCIAGDGVAKGYYKKEELTDSRFIDNPFEpgsklyrTGDMARWLPGGRIEYIGRIDNQVKI-RGFRIE 1558
Cdd:PLN02861 456 gydalSDVPrGEICLRGNTLFSGYHKRQDLTEEVLIDGWFH-------TGDIGEWQPNGAMKIIDRKKNIFKLsQGEYVA 528
|
490
....*....|....
gi 1776025254 1559 LGDIESRLSEHPGI 1572
Cdd:PLN02861 529 VENLENTYSRCPLI 542
|
|
| PRK09185 |
PRK09185 |
beta-ketoacyl-ACP synthase; |
3497-3776 |
2.23e-16 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236398 [Multi-domain] Cd Length: 392 Bit Score: 84.89 E-value: 2.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3497 LNIHGPSEPVETACSSSLVAIHRAVTAMQNGDCEMAIAGGVNTI--LTE------EAhisyskagmLSkDGRCKTFSADA 3568
Cdd:PRK09185 147 LGLSGPAYTISTACSSSAKVFASARRLLEAGLCDAAIVGGVDSLcrLTLngfnslES---------LS-PQPCRPFSANR 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3569 NGYVRGEGVGMVMLKKLEDAE---------RDGNHIygvirgtaenhggrantlTSPNPK----AQAdlLVRAYRQAGID 3635
Cdd:PRK09185 217 DGINIGEAAAFFLLEREDDAAvallgvgesSDAHHM------------------SAPHPEglgaILA--MQQALADAGLA 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3636 PSTVTYIEAHGTGTELGDPIEINGLKAAFkelsnmrGESQPdvpdhrCgiGSVKSNIGHLELAAGISGLIKVLLQMKHKT 3715
Cdd:PRK09185 277 PADIGYINLHGTATPLNDAMESRAVAAVF-------GDGVP------C--SSTKGLTGHTLGAAGAVEAAICWLALRHGL 341
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1776025254 3716 LVKSLHCETLNPylqlTDSPFYIVQEKQewksvtdcdgnELPRRAGIS-SFGIGGVNAHIVI 3776
Cdd:PRK09185 342 PPHGWNTGQPDP----ALPPLYLVENAQ-----------ALAIRYVLSnSFAFGGNNCSLIF 388
|
|
| PRK07910 |
PRK07910 |
beta-ketoacyl-ACP synthase; |
1931-2183 |
2.37e-16 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236129 [Multi-domain] Cd Length: 418 Bit Score: 85.17 E-value: 2.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1931 CSSSLIGLHSAYKSLLSAESDYALVGGATLHTES-NIGYVHQPGLNFSSD-----GHIKAFDASADGMIGGEGVAVVLLK 2004
Cdd:PRK07910 171 CASGSEAIAQAWRQIVLGEADIAICGGVETRIEAvPIAGFAQMRIVMSTNnddpaGACRPFDKDRDGFVFGEGGALMVIE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2005 KAADAVKDGDHIYALLRGIGVNNDGADKVgfyAPSVKGQ--ADVVQQVMNQTKIHPESICYVEAHGTGTKLGDPIELAAL 2082
Cdd:PRK07910 251 TEEHAKARGANILARIMGASITSDGFHMV---APDPNGEraGHAMTRAIELAGLTPGDIDHVNAHATGTSVGDVAEGKAI 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2083 TNVYrqytnKTQFCGIGSVKTNIGHLDTAAGLAGCIKVVMSLYHQELAPSINYKEPNPNTDL---ASSPFYvvdqkktls 2159
Cdd:PRK07910 328 NNAL-----GGHRPAVYAPKSALGHSVGAVGAVESILTVLALRDGVIPPTLNLENLDPEIDLdvvAGEPRP--------- 393
|
250 260
....*....|....*....|....*
gi 1776025254 2160 reiQTHRAALS-SFGLGGTNTHAIF 2183
Cdd:PRK07910 394 ---GNYRYAINnSFGFGGHNVALAF 415
|
|
| BKR_SDR_c |
cd05333 |
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ... |
2850-3015 |
2.63e-16 |
|
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; This subgroup includes the Escherichai coli K12 BKR, FabG. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet) NAD(P)(H) binding region and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H) binding pattern: TGxxxGxG in classical SDRs. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P) binding motif and an altered active site motif (YXXXN). Fungal type type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P) binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr-151 and Lys-155, and well as Asn-111 (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.
Pssm-ID: 187594 [Multi-domain] Cd Length: 240 Bit Score: 81.83 E-value: 2.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGllfaKEIANRTGR--STIVLTGRSvlSEDKENELEALRSIGAEVVYREADVSDQHAVHHLFEEIKERY 2927
Cdd:cd05333 2 VALVTGASRGIG----RAIALRLAAegAKVAVTDRS--EEAAAETVEEIKALGGNAAALEADVSDREAVEALVEKVEAEF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2928 GTLNGIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSGLLHvdeCSKDFPLDF-------FIFFSSVSGCLGNAGQADYAAA 3000
Cdd:cd05333 76 GPVDILVNNAGITRDNLLMRMSEEDWDAVINVNLTGVFN---VTQAVIRAMikrrsgrIINISSVVGLIGNPGQANYAAS 152
|
170
....*....|....*
gi 1776025254 3001 NSFMDAFAeyrRSLA 3015
Cdd:cd05333 153 KAGVIGFT---KSLA 164
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
29-555 |
3.34e-16 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 85.80 E-value: 3.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 29 ATIPEVLYRTAAELGDTKGIIYLQPDGTEVYQSYRRlwdDGLRIVKGLRQSGLKAKQSVILQLGDNSQllpafWGCVLTG 108
Cdd:PLN02330 28 LTLPDFVLQDAELYADKVAFVEAVTGKAVTYGEVVR---DTRRFAKALRSLGLRKGQVVVVVLPNVAE-----YGIVALG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 109 VVPAP---LAVPPTYAESssgtqKLKDAWTLLDKPAVITDRgmhqemLDWAKEQGLeGFRAIIV-----------EDLLS 174
Cdd:PLN02330 100 IMAAGgvfSGANPTALES-----EIKKQAEAAGAKLIVTND------TNYGKVKGL-GLPVIVLgeekiegavnwKELLE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 175 AE---ADTDWHQSSPE-DLALLLLTSGSTGTPKAVMLNHRNIMSMVKGII-----QMQGftrEDITFNWMPFDHVGGIgm 245
Cdd:PLN02330 168 AAdraGDTSDNEEILQtDLCALPFSSGTTGISKGVMLTHRNLVANLCSSLfsvgpEMIG---QVVTLGLIPFFHIYGI-- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 246 lhlrdVYLGCQEINVSSETILMEPLKWLDWIDHYRA-SVTWAPNFAFGLVTDFAEEIKDrKWDLSSMRymLNGGEAMVAK 324
Cdd:PLN02330 243 -----TGICCATLRNKGKVVVMSRFELRTFLNALITqEVSFAPIVPPIILNLVKNPIVE-EFDLSKLK--LQAIMTAAAP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 325 VGRRILELLEPHgLPADAIRPAWGMSETSSgVIFSHeftraGTSDDDHFV----EIGSPIPGFSMRIVN-DHNELVEEGE 399
Cdd:PLN02330 315 LAPELLTAFEAK-FPGVQVQEAYGLTEHSC-ITLTH-----GDPEKGHGIakknSVGFILPNLEVKFIDpDTGRSLPKNT 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 400 IGRFQVSGLSVTSGYYQRPDLNESVFTEDGWFETGDLGFLRN-GRLTITGRTKDAIIINGINYYSHAIESAVEELSEIET 478
Cdd:PLN02330 388 PGELCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIGYIDDdGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVED 467
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1776025254 479 sytaACAVRLGQNSTDQLAIFFVTSAKLNDEQMSQLLRNIQSHVSQVIGVTPEYLLpvqkEEIPKTAIGKIQRTQLK 555
Cdd:PLN02330 468 ----AAVVPLPDEEAGEIPAACVVINPKAKESEEDILNFVAANVAHYKKVRVVQFV----DSIPKSLSGKIMRRLLK 536
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
1163-1578 |
3.84e-16 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 84.92 E-value: 3.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1163 AKKTPDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGPDrlAGI-YVDR-SLDMLVGLLAILKAGGAYVPLDPSYPAE 1240
Cdd:PRK09029 13 AQVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEG--SGVaLRGKnSPETLLAYLALLQCGARVLPLNPQLPQP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1241 RLEYMLEDSEVFITLTTSELVNtlsWNGVTTALLDQDWDEIAQTASdrkvltrtvtPENLAYVIYTSGSTGKPKGVMIPH 1320
Cdd:PRK09029 91 LLEELLPSLTLDFALVLEGENT---FSALTSLHLQLVEGAHAVAWQ----------PQRLATMTLTSGSTGLPKAAVHTA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1321 KA----------LTNFlvsmgetpglTAEDKMLavttycfdiaaleLFLP-------------LIKGAhcyicqTEHTKD 1377
Cdd:PRK09029 158 QAhlasaegvlsLMPF----------TAQDSWL-------------LSLPlfhvsgqgivwrwLYAGA------TLVVRD 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1378 VEKLKRDIRtikptvmQATPAT------WKMLFYsgWENEENVK-ILCGGEALPETLKRYFLDTGSEAWNMFGPTE--TT 1448
Cdd:PRK09029 209 KQPLEQALA-------GCTHASlvptqlWRLLDN--RSEPLSLKaVLLGGAAIPVELTEQAEQQGIRCWCGYGLTEmaST 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1449 IwSAVQriNDecSRATIGRPIANTQIYITDsqlapvpagvpGELCIAGDGVAKGYYKKEELTdsrfidnPFEPGSKLYRT 1528
Cdd:PRK09029 280 V-CAKR--AD--GLAGVGSPLPGREVKLVD-----------GEIWLRGASLALGYWRQGQLV-------PLVNDEGWFAT 336
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1529 GDMARWLpGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVV 1578
Cdd:PRK09029 337 RDRGEWQ-NGELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVV 385
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
184-554 |
3.89e-16 |
|
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.
Pssm-ID: 341300 [Multi-domain] Cd Length: 440 Bit Score: 84.53 E-value: 3.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 184 SSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDHVGGIgmLHLRDVYLGCQEINVSSE 263
Cdd:cd17645 101 TNPDDLAYVIYTSGSTGLPKGVMIEHHNLVNLCEWHRPYFGVTPADKSLVYASFSFDASA--WEIFPHLTAGAALHVVPS 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 264 TILMEPLKWLDWIDHYRASVTWAPnfafglvTDFAEEIKdrKWDLSSMRYMLNGGEAMvAKVGRRILELLEPHGLPADAI 343
Cdd:cd17645 179 ERRLDLDALNDYFNQEGITISFLP-------TGAAEQFM--QLDNQSLRVLLTGGDKL-KKIERKGYKLVNNYGPTENTV 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 344 rpawgmsetssgVIFSHEFTRAGTSdddhfVEIGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGYYQRPDLNES 423
Cdd:cd17645 249 ------------VATSFEIDKPYAN-----IPIGKPIDNTRVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAE 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 424 VFTEDGW------FETGDLG-FLRNGRLTITGRTKDAIIINGINYYSHAIESAVEELSEIETsyTAACAVRLGQNSTdQL 496
Cdd:cd17645 312 KFIVHPFvpgermYRTGDLAkFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIEL--AAVLAKEDADGRK-YL 388
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1776025254 497 AIFFVTSAKLNDEQMSQLLRNiqshvsqvigVTPEYLLP---VQKEEIPKTAIGKIQRTQL 554
Cdd:cd17645 389 VAYVTAPEEIPHEELREWLKN----------DLPDYMIPtyfVHLKALPLTANGKVDRKAL 439
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
184-680 |
4.31e-16 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 86.76 E-value: 4.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 184 SSPEDLALLLLTSGSTGTPKAVMLNHRnimsmvkGIIQMQgftreditFNWMPFdhvggigmLHL--RDVY--LGCQEIN 259
Cdd:PRK05691 3866 SGPDNLAYVIYTSGSTGLPKGVMVEQR-------GMLNNQ--------LSKVPY--------LALseADVIaqTASQSFD 3922
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 260 VSSETILMEPLkwldwidhYRASVTWAPN-FAF---GLVTDFAEE---------------IKDRKWDLSSMRYMLNGGEA 320
Cdd:PRK05691 3923 ISVWQFLAAPL--------FGARVEIVPNaIAHdpqGLLAHVQAQgitvlesvpsliqgmLAEDRQALDGLRWMLPTGEA 3994
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 321 MVAKVGRRILELLephglPADAIRPAWGMSETSSGVIF---SHEFTRAGtsdddhFVEIGSPIPGFSMRIVNDHNELVEE 397
Cdd:PRK05691 3995 MPPELARQWLQRY-----PQIGLVNAYGPAECSDDVAFfrvDLASTRGS------YLPIGSPTDNNRLYLLDEALELVPL 4063
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 398 GEIGRFQVSGLSVTSGYYQRPDLNESVFTEDGW-------FETGDLGFLR-NGRLTITGRTKDAIIINGINYYSHAIESA 469
Cdd:PRK05691 4064 GAVGELCVAGTGVGRGYVGDPLRTALAFVPHPFgapgerlYRTGDLARRRsDGVLEYVGRIDHQVKIRGYRIELGEIEAR 4143
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 470 VEELSEIEtsyTAACAVRLGQNSTDQLAIFFVTSAKLNDeqmSQLLRNIQSHVSQVIgvtPEYLLPVQ---KEEIPKTAI 546
Cdd:PRK05691 4144 LHEQAEVR---EAAVAVQEGVNGKHLVGYLVPHQTVLAQ---GALLERIKQRLRAEL---PDYMVPLHwlwLDRLPLNAN 4214
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 547 GKIQRTQLKtsfengefdhllhkpnrmndAVQDEEMQQADHVKRvREEIQEHLLTCLTEELHVSRdwVEPNANIQSLGVN 626
Cdd:PRK05691 4215 GKLDRKALP--------------------ALDIGQLQSQAYLAP-RNELEQTLATIWADVLKVER--VGVHDNFFELGGH 4271
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1776025254 627 SIKMMKLIRSIEKNYHIKLTAREIHQYPTIERLASYLsehEDLSSSSADKKGTD 680
Cdd:PRK05691 4272 SLLATQIASRVQKALQRNVPLRAMFECSTVEELAEYI---EGLAGSAIDEQKVD 4322
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
1157-1534 |
4.53e-16 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 85.70 E-value: 4.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1157 ELFEQQAKKTPDRAAVSYEG-----QTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYV 1231
Cdd:PRK08180 43 DRLVHWAQEAPDRVFLAERGadggwRRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMYAGVPYA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1232 PLDPSYPA-----ERLEYMLE----------DSEVF---ITLTTSELVNTLSWNGVTTALLDQDWDEIAQTASDRKV--L 1291
Cdd:PRK08180 123 PVSPAYSLvsqdfGKLRHVLElltpglvfadDGAAFaraLAAVVPADVEVVAVRGAVPGRAATPFAALLATPPTAAVdaA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1292 TRTVTPENLAYVIYTSGSTGKPKGVMIPHKaltnflvsMgetpgLTAEDKMLAVTTYCFDIAALEL--FLP--------- 1360
Cdd:PRK08180 203 HAAVGPDTIAKFLFTSGSTGLPKAVINTHR--------M-----LCANQQMLAQTFPFLAEEPPVLvdWLPwnhtfggnh 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1361 -----LIKGAHCYICQTEHT-KDVEKLKRDIRTIKPTVMQATPATWKML-------------FYSgweneeNVKILC-GG 1420
Cdd:PRK08180 270 nlgivLYNGGTLYIDDGKPTpGGFDETLRNLREISPTVYFNVPKGWEMLvpalerdaalrrrFFS------RLKLLFyAG 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1421 EALPETL-------------KRYFLDTGseaWNMfgpTET------TIWSAvqrindecSRA-TIGRPIANTQIYItdsq 1480
Cdd:PRK08180 344 AALSQDVwdrldrvaeatcgERIRMMTG---LGM---TETapsatfTTGPL--------SRAgNIGLPAPGCEVKL---- 405
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1776025254 1481 lapVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPFepgsklYRTGDMARW 1534
Cdd:PRK08180 406 ---VPVGGKLEVRVKGPNVTPGYWRAPELTAEAFDEEGY------YRSGDAVRF 450
|
|
| KR_1_FAS_SDR_x |
cd08954 |
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 1, complex (x) SDRs; ... |
4173-4408 |
4.89e-16 |
|
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 1, complex (x) SDRs; NADP-dependent KR domain of the multidomain type I FAS, a complex SDR family. This subfamily also includes proteins identified as polyketide synthase (PKS), a protein with related modular protein architecture and similar function. It includes the KR domains of mammalian and chicken FAS, and Dictyostelium discoideum putative polyketide synthases (PKSs). These KR domains contain two subdomains, each of which is related to SDR Rossmann fold domains. However, while the C-terminal subdomain has an active site similar to the other SDRs and a NADP-binding capability, the N-terminal SDR-like subdomain is truncated and lacks these functions, serving a supportive structural role. In some instances, such as porcine FAS, an enoyl reductase (a Rossman fold NAD-binding domain of the medium-chain dehydrogenase/reductase, MDR family) module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consists of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthesis uses a dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-ketoacyl reductase (KR), forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-enoyl reductase (ER); this KR and ER are members of the SDR family. This KR subfamily has an active site tetrad with a similar 3D orientation compared to archetypical SDRs, but the active site Lys and Asn residue positions are swapped. The characteristic NADP-binding is typical of the multidomain complex SDRs, with a GGXGXXG NADP binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.
Pssm-ID: 187657 [Multi-domain] Cd Length: 452 Bit Score: 84.42 E-value: 4.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4173 LLITGGTRGIGLLCARHFAECYGVKKLVLTGREqlPPREEWARfktsntslaekiqAVRELEAKGVQVEMLSLTLSDDAQ 4252
Cdd:cd08954 221 YLITGGSGGLGLEILKWLVKRGAVENIIILSRS--GMKWELEL-------------LIREWKSQNIKFHFVSVDVSDVSS 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4253 VEQTLQHI--KRTLGPIGGVIHcagltdmdtLAFIRKT--------SDDIQrVMEPKVSGLTTLYRHV--CNEPLQFFVL 4320
Cdd:cd08954 286 LEKAINLIlnAPKIGPIGGIFH---------LAFVLIDkvleidteSLFIS-VNKAKVMGAINLHNQSikRCWKLDYFVL 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4321 FSSVSAIIPelSAGQADYAMANSYMDYFAEaHQKHV--PIISVQWPNWKETGM---GEVTNQAYRESGLFSITNSEGLRF 4395
Cdd:cd08954 356 FSSVSSIRG--SAGQCNYVCANSVLDSLSR-YRKSIglPSIAINWGAIGDVGFvsrNESVDTLLGGQGLLPQSINSCLGT 432
|
250
....*....|....
gi 1776025254 4396 LD-QIVSKMFGPVV 4408
Cdd:cd08954 433 LDlFLQNPSPNLVL 446
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
186-555 |
5.11e-16 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 84.41 E-value: 5.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 186 PEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFD--HVGGIGMLHLRDVYLGCQEINVSSE 263
Cdd:cd05971 87 SDDPALIIYTSGTTGPPKGALHAHRVLLGHLPGVQFPFNLFPRDGDLYWTPADwaWIGGLLDVLLPSLYFGVPVLAHRMT 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 264 TilMEPLKWLDWIDHYRASVTWAPNFAFGLVTDFAEEIKDrkWDLsSMRYMLNGGEAMVAKV---GRRILellephglpA 340
Cdd:cd05971 167 K--FDPKAALDLMSRYGVTTAFLPPTALKMMRQQGEQLKH--AQV-KLRAIATGGESLGEELlgwAREQF---------G 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 341 DAIRPAWGMSE-----TSSGVIFShefTRAGTsdddhfveIGSPIPGFSMRIVNDHNELVEEGEIGRFQVS-GLSVTS-G 413
Cdd:cd05971 233 VEVNEFYGQTEcnlviGNCSALFP---IKPGS--------MGKPIPGHRVAIVDDNGTPLPPGEVGEIAVElPDPVAFlG 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 414 YYQRPDLNESVFTEDgWFETGDLGFL-RNGRLTITGRTKDAIIINGINYYSHAIESAVEELSEIetsYTAACAVRLGQNS 492
Cdd:cd05971 302 YWNNPSATEKKMAGD-WLLTGDLGRKdSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAV---LMAAVVGIPDPIR 377
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1776025254 493 TDQLAIFFVTSAKLNDEQmsQLLRNIQSHVSQVIGvtpEYLLPVQKE---EIPKTAIGKIQRTQLK 555
Cdd:cd05971 378 GEIVKAFVVLNPGETPSD--ALAREIQELVKTRLA---AHEYPREIEfvnELPRTATGKIRRRELR 438
|
|
| PRK14691 |
PRK14691 |
3-oxoacyl-(acyl carrier protein) synthase II; Provisional |
4719-4935 |
5.29e-16 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
Pssm-ID: 173154 [Multi-domain] Cd Length: 342 Bit Score: 82.85 E-value: 5.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4719 NYLAANLSQFFDVRGPSVVVDTACSSALVGMNMAIQALRGGDIQSAIVGGVSLLSSDASHRLFDRRGILSKH------SS 4792
Cdd:PRK14691 68 NLAAGHVSIKHHFKGPIGAPVTACAAGVQAIGDAVRMIRNNEADVALCGGAEAVIDTVSLAGFAAARALSTHfnstpeKA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4793 FHVFDERADGVVLGEGVGMVMLKTVKQALEDGDTIYAVVKAASVNNDGRTAGPATPNLEAQKEVMKDALFKSGKKPEDIS 4872
Cdd:PRK14691 148 SRPFDTARDGFVMGEGAGLLIIEELEHALARGAKPLAEIVGYGTSADAYHMTSGAEDGDGAYRAMKIALRQAGITPEQVQ 227
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1776025254 4873 YLEANGSGSIVTDLLELKAIQSVYrsGHSSPLSLGSIKPNIGHPLCAEGIASFIKVVLMLKER 4935
Cdd:PRK14691 228 HLNAHATSTPVGDLGEINAIKHLF--GESNALAITSTKSATGHLLGAAGGLETIFTVLALRDQ 288
|
|
| FUM14_C_NRPS-like |
cd19545 |
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ... |
695-1121 |
5.30e-16 |
|
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond forming Fusarium verticillioides FUM14 protein; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) typically catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. However, some C-domains have ester-bond forming activity. This subfamily includes Fusarium verticillioides FUM14 (also known as NRPS8), a bi-domain protein with an ester-bond forming NRPS C-domain, which catalyzes linkages between an aminoacyl/peptidyl-PCP donor and a hydroxyl-containing acceptor. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. FUM14 has an altered active site motif DHTHCD instead of the typical HHxxxD motif seen in other subfamily members. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380467 [Multi-domain] Cd Length: 395 Bit Score: 83.89 E-value: 5.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 695 PLSEVQKGLWTLQKMSPEksAYHVPLCFKFSSGLHLETLQQAFGLVLNQHPILKHVIQEKDGVPilknepALSIEIKTEN 774
Cdd:cd19545 3 PCTPLQEGLMALTARQPG--AYVGQRVFELPPDIDLARLQAAWEQVVQANPILRTRIVQSDSGG------LLQVVVKESP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 775 ISSMKESDIPAFLRKKVKEPyVKENSPLVRVMSFSRSEQEHFLLVVIHHLIFDGvSSVTFIhslFDTYQLLLKGQQPEIA 854
Cdd:cd19545 75 ISWTESTSLDEYLEEDRAAP-MGLGGPLVRLALVEDPDTERYFVWTIHHALYDG-WSLPLI---LRQVLAAYQGEPVPQP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 855 VSPAiyhDFaaweKNMLAGKDGVKHRTYWQKQLSGTLPNL--QLPKVSASSVSEfREDTYTRRLSSGFmnqvrmfakEHS 932
Cdd:cd19545 150 PPFS---RF----VKYLRQLDDEAAAEFWRSYLAGLDPAVfpPLPSSRYQPRPD-ATLEHSISLPSSA---------SSG 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 933 VNVTTVFLSCYMMLLGRYTGQKEqiVGMPAMV--R--PEERFDDAIGHFLNMLPIRSELNPADTFSSFISKLQLTILDGL 1008
Cdd:cd19545 213 VTLATVLRAAWALVLSRYTGSDD--VVFGVTLsgRnaPVPGIEQIVGPTIATVPLRVRIDPEQSVEDFLQTVQKDLLDMI 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1009 DHAAYPFPKMvRDLNIPRSQAGSpvFQTAFFYQ-NFLQSGS------YQSLLSRYADFFSvdyveyihqegeYELVFELW 1081
Cdd:cd19545 291 PFEHTGLQNI-RRLGPDARAACN--FQTLLVVQpALPSSTSeslelgIEEESEDLEDFSS------------YGLTLECQ 355
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1776025254 1082 ETEEKMELNIKYNTGLFDAASISAMFDHFVYVTEQAMLNP 1121
Cdd:cd19545 356 LSGSGLRVRARYDSSVISEEQVERLLDQFEHVLQQLASAP 395
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
30-554 |
5.48e-16 |
|
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.
Pssm-ID: 341247 [Multi-domain] Cd Length: 493 Bit Score: 84.87 E-value: 5.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 30 TIPEVLYRTAAELGDTKGIiyLQPD-GTEVyqSYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNSQLLPAFWGCVLTG 108
Cdd:cd05923 2 TVFEMLRRAASRAPDACAI--ADPArGLRL--TYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 109 VVPAPLAvpptyaesssgtqklkdaWTLldKPAVITDRGMHQEMLDWAKEQGLEGFRAIIV-----------EDLLSAEA 177
Cdd:cd05923 78 AVPALIN------------------PRL--KAAELAELIERGEMTAAVIAVDAQVMDAIFQsgvrvlalsdlVGLGEPES 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 178 DTD---WHQSSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQG--FTREDITFNWMPFDHVGGIGMLHLRDVY 252
Cdd:cd05923 138 AGPlieDPPREPEQPAFVFYTSGTTGLPKGAVIPQRAAESRVLFMSTQAGlrHGRHNVVLGLMPLYHVIGFFAVLVAALA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 253 LGCQEINVSSetilMEPLKWLDWIDHYRASVTWA-PNFAFGLVTdfAEEIKDRKwdLSSMRYMLNGGEAMVAKVgrriLE 331
Cdd:cd05923 218 LDGTYVVVEE----FDPADALKLIEQERVTSLFAtPTHLDALAA--AAEFAGLK--LSSLRHVTFAGATMPDAV----LE 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 332 LLEPHgLPADAIRpAWGMSETSSGVIFSHEFT----RAGTSDDDHFVEIGspipGFSMRIVNDhnelVEEGEIgRFQVSG 407
Cdd:cd05923 286 RVNQH-LPGEKVN-IYGTTEAMNSLYMRDARTgtemRPGFFSEVRIVRIG----GSPDEALAN----GEEGEL-IVAAAA 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 408 LSVTSGYYQRPDLNESVFtEDGWFETGDLGFLR-NGRLTITGRTKDAIIINGINYYSHAIES------AVEELSEIETSY 480
Cdd:cd05923 355 DAAFTGYLNQPEATAKKL-QDGWYRTGDVGYVDpSGDVRILGRVDDMIISGGENIHPSEIERvlsrhpGVTEVVVIGVAD 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 481 T------AACAVR-LGQNSTDQLAIFFVTSAklndeqmsqlLRNIQSHVSQVIgvtpeyllpvqKEEIPKTAIGKIQRTQ 553
Cdd:cd05923 434 ErwgqsvTACVVPrEGTLSADELDQFCRASE----------LADFKRPRRYFF-----------LDELPKNAMNKVLRRQ 492
|
.
gi 1776025254 554 L 554
Cdd:cd05923 493 L 493
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
1180-1552 |
5.96e-16 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 85.25 E-value: 5.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1180 TYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLEDSE---VFITLT 1256
Cdd:PLN02430 78 TYKEVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVAMEACAAHSLICVPLYDTLGPGAVDYIVDHAEidfVFVQDK 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1257 -TSELVN-----------TLSWNGVTTALLDQ---------DWDEIAQTASDRKVLTRTVTPENLAYVIYTSGSTGKPKG 1315
Cdd:PLN02430 158 kIKELLEpdcksakrlkaIVSFTSVTEEESDKasqigvktySWIDFLHMGKENPSETNPPKPLDICTIMYTSGTSGDPKG 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1316 VMIPHKALTNFLVSMgETPGLTAEDKMLAVTTYCFdiaalelFLPLikgAHCYICQTE------------HTKDVEKLKR 1383
Cdd:PLN02430 238 VVLTHEAVATFVRGV-DLFMEQFEDKMTHDDVYLS-------FLPL---AHILDRMIEeyffrkgasvgyYHGDLNALRD 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1384 DIRTIKPTVMQATPATW------------------KMLFYS------GWENE----------------ENVK-------- 1415
Cdd:PLN02430 307 DLMELKPTLLAGVPRVFerihegiqkalqelnprrRLIFNAlykyklAWMNRgyshkkaspmadflafRKVKaklggrlr 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1416 -ILCGGEALPETLKRyFLDTGSEAWNM--FGPTETTIWSAVQRINDECSRATIGRPIANTQIYITD-SQLAPVPAGVP-- 1489
Cdd:PLN02430 387 lLISGGAPLSTEIEE-FLRVTSCAFVVqgYGLTETLGPTTLGFPDEMCMLGTVGAPAVYNELRLEEvPEMGYDPLGEPpr 465
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1776025254 1490 GELCIAGDGVAKGYYKKEELTDSRFIDNPFEpgsklyrTGDMARWLPGGRIEYIGRIDNQVKI 1552
Cdd:PLN02430 466 GEICVRGKCLFSGYYKNPELTEEVMKDGWFH-------TGDIGEILPNGVLKIIDRKKNLIKL 521
|
|
| beta-lac_NRPS |
cd19547 |
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ... |
801-1121 |
9.44e-16 |
|
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis NocB which exhibits an unusual cyclization to form beta-lactam rings in pro-nocardicin G synthesis; Nocardia uniformis NRPS NocB acts centrally in the biosynthesis of the nocardicin monocyclic beta-lactam antibiotics. Along with another NRPS NocA, it mediates an unusual cyclization to form beta-lactam rings in the synthesis of the beta-lactam-containing pentapeptide pro-nocardicin G. This small subfamily is related to DCL-type Condensation (C) domains, which catalyze condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; domains belonging to this subfamily have an HHHxxxD motif at the active site.
Pssm-ID: 380469 [Multi-domain] Cd Length: 422 Bit Score: 83.51 E-value: 9.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 801 PLVRVMSFSRSEQEHFLLVVIHHLIFDGVSSVTFIHSLFDTYQLLLKGQQPEIA-VSPaiYHDFAAWEKNMLAGKDgvKH 879
Cdd:cd19547 114 PLYRLTLVRLGGGRHYLLWSHHHILLDGWCLSLIWGDVFRVYEELAHGREPQLSpCRP--YRDYVRWIRARTAQSE--ES 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 880 RTYWQKQLSGTLPNlqlPKVSASSVSEFREDTYTRRLSSGFMNQVRMFAKEHSVNVTTVFLSCYMMLLGRYTGQKEQIVG 959
Cdd:cd19547 190 ERFWREYLRDLTPS---PFSTAPADREGEFDTVVHEFPEQLTRLVNEAARGYGVTTNAISQAAWSMLLALQTGARDVVHG 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 960 MPAMVRPEER--FDDAIGHFLNMLPIRSELNPADTFSSFISKLQLTILDGLDHAAYPFPKmVRDLNIPRSQAGSPVFQTA 1037
Cdd:cd19547 267 LTIAGRPPELegSEHMVGIFINTIPLRIRLDPDQTVTGLLETIHRDLATTAAHGHVPLAQ-IKSWASGERLSGGRVFDNL 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1038 FFYQNFLQSgsyqsllSRYADFFSVDYVEYIHQEG-EYE---LVFELweteEKMELNIKYNTGLFDAASISAMFDHFVYV 1113
Cdd:cd19547 346 VAFENYPED-------NLPGDDLSIQIIDLHAQEKtEYPiglIVLPL----QKLAFHFNYDTTHFTRAQVDRFIEVFRLL 414
|
....*...
gi 1776025254 1114 TEQAMLNP 1121
Cdd:cd19547 415 TEQLCRRP 422
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
1298-1638 |
1.52e-15 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 82.02 E-value: 1.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1298 ENLAYVIYTSGSTGKPKGVMIPHKALtnflVSMGET-------PGltaeDKMLAVTTYcfDIAALELFL-PLIKGAHCYI 1369
Cdd:PRK07824 35 DDVALVVATSGTTGTPKGAMLTAAAL----TASADAthdrlggPG----QWLLALPAH--HIAGLQVLVrSVIAGSEPVE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1370 CQTEHTKDVEKLKRDIRTIKP-------TVMQ-----ATPATWKMLfysgwenEENVKILCGGEALPETLKRYFLDTGSE 1437
Cdd:PRK07824 105 LDVSAGFDPTALPRAVAELGGgrrytslVPMQlakalDDPAATAAL-------AELDAVLVGGGPAPAPVLDAAAAAGIN 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1438 AWNMFGPTETtiwsAVQRINDecsratiGRPIANTQIYITDSQLApvpagvpgelcIAGDGVAKGYYKKEEltdsrfiDN 1517
Cdd:PRK07824 178 VVRTYGMSET----SGGCVYD-------GVPLDGVRVRVEDGRIA-----------LGGPTLAKGYRNPVD-------PD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1518 PF-EPGskLYRTGDMARwLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMDN------LAAYYTA 1590
Cdd:PRK07824 229 PFaEPG--WFRTDDLGA-LDDGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDrlgqrvVAAVVGD 305
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1776025254 1591 KHAnaSLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSL 1638
Cdd:PRK07824 306 GGP--APTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRAL 351
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
1295-1640 |
2.76e-15 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 82.91 E-value: 2.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1295 VTPENLAYVI-YTSGSTGKPKGVMIPHKALtnFLVSMGetpgLTAEDKmLAVT---------------TYCFDIAALELF 1358
Cdd:PRK05620 177 ELDETTAAAIcYSTGTTGAPKGVVYSHRSL--YLQSLS----LRTTDS-LAVThgesflccvpiyhvlSWGVPLAAFMSG 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1359 LPLIkgahcyicQTEHTKDVEKLKRDIRTIKPTVMQATPATWKMLFYSGWENEEN----VKILCGGEALPETL-----KR 1429
Cdd:PRK05620 250 TPLV--------FPGPDLSAPTLAKIIATAMPRVAHGVPTLWIQLMVHYLKNPPErmslQEIYVGGSAVPPILikaweER 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1430 YFLDTgSEAWNMfgpTETTIWSAVQRINDECS-------RATIGR-PIANTQIYITDSQLAPVPAGVPGELCIAGDGVAK 1501
Cdd:PRK05620 322 YGVDV-VHVWGM---TETSPVGTVARPPSGVSgearwayRVSQGRfPASLEYRIVNDGQVMESTDRNEGEIQVRGNWVTA 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1502 GYYK----KEELTDSRFIDNPFEPGSKLY------RTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPG 1571
Cdd:PRK05620 398 SYYHspteEGGGAASTFRGEDVEDANDRFtadgwlRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPE 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1572 ILECVVVADMDN-----------LAAYYTAKHAnaslTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLKN 1640
Cdd:PRK05620 478 VVECAVIGYPDDkwgerplavtvLAPGIEPTRE----TAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLRQ 553
|
|
| AcpA |
COG3433 |
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ... |
1468-1732 |
2.82e-15 |
|
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442659 [Multi-domain] Cd Length: 295 Bit Score: 80.18 E-value: 2.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1468 PIANTQIYITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPFEPGSKLYRTGDMARWLPGGRIEYIGRID 1547
Cdd:COG3433 21 PPAIVQARALLLIVDLQGYFGGFGGEGGLLGAGLLLRIRLLAAAARAPFIPVPYPAQPGRQADDLRLLLRRGLGPGGGLE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1548 NQVKIRGFRIELGDIESRLSEHPGILECVVVADM------DNLAAYYTAKHANASLTARELRHFVKNALPAYMVPSYFIQ 1621
Cdd:COG3433 101 RLVQQVVIRAERGEEEELLLVLRAAAVVRVAVLAalrgagVGLLLIVGAVAALDGLAAAAALAALDKVPPDVVAASAVVA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1622 LDHMPLTPNGKIDRNSLKnidLSGEQLKQRQTSPKNIQDTVFT------IWQEVLKTS--DIEWDDGFFDVGGDSLLAVT 1693
Cdd:COG3433 181 LDALLLLALKVVARAAPA---LAAAEALLAAASPAPALETALTeeelraDVAELLGVDpeEIDPDDNLFDLGLDSIRLMQ 257
|
250 260 270
....*....|....*....|....*....|....*....
gi 1776025254 1694 VADRIKhELSCEFSVTDLFEYSTIKNISQYITEQRMGNA 1732
Cdd:COG3433 258 LVERWR-KAGLDVSFADLAEHPTLAAWWALLAAAQAAAA 295
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
1176-1640 |
2.92e-15 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 82.72 E-value: 2.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1176 GQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLEDSEVFITL 1255
Cdd:PLN02246 48 GRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLII 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1256 TTSELVNTLS----WNGVTTALLDQDWD------EIAQtASDRKVLTRTVTPENLAYVIYTSGSTGKPKGVMIPHKALTN 1325
Cdd:PLN02246 128 TQSCYVDKLKglaeDDGVTVVTIDDPPEgclhfsELTQ-ADENELPEVEISPDDVVALPYSSGTTGLPKGVMLTHKGLVT 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1326 FLVSM--GETPGL--TAEDKMLAVTTYcFDIAALE--LFLPLIKGAHCYICQT-EHTKDVEKLKRDIRTIKPTV------ 1392
Cdd:PLN02246 207 SVAQQvdGENPNLyfHSDDVILCVLPM-FHIYSLNsvLLCGLRVGAAILIMPKfEIGALLELIQRHKVTIAPFVppivla 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1393 MQATPATWKMLFYSgweneenVKILCGGEA-----LPETLKRYF----LDTG---SEA---WNM---FGPTETTIWSAvq 1454
Cdd:PLN02246 286 IAKSPVVEKYDLSS-------IRMVLSGAAplgkeLEDAFRAKLpnavLGQGygmTEAgpvLAMclaFAKEPFPVKSG-- 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1455 rindecSRATIGRpiaNTQIYITDSQL-APVPAGVPGELCIAGDGVAKGYYKKEELTDsrfidnpfepgsklyRTGDMAR 1533
Cdd:PLN02246 357 ------SCGTVVR---NAELKIVDPETgASLPRNQPGEICIRGPQIMKGYLNDPEATA---------------NTIDKDG 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1534 WLPGGRIEYI---------GRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMDNLA----AYYTAKHANASLTAR 1600
Cdd:PLN02246 413 WLHTGDIGYIddddelfivDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAgevpVAFVVRSNGSEITED 492
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1776025254 1601 ELRHFVKNALPAY----MVpsYFIqlDHMPLTPNGKIDRNSLKN 1640
Cdd:PLN02246 493 EIKQFVAKQVVFYkrihKV--FFV--DSIPKAPSGKILRKDLRA 532
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
1177-1600 |
3.14e-15 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 82.86 E-value: 3.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1177 QTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLEDSE-VFITL 1255
Cdd:cd17641 10 QEFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGaRVVIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1256 TTSELVNTLSWNGVTTALLDQ--DWDE---------------------IAQTASDRKVLTRTVT---PENLAYVIYTSGS 1309
Cdd:cd17641 90 EDEEQVDKLLEIADRIPSVRYviYCDPrgmrkyddprlisfedvvalgRALDRRDPGLYEREVAagkGEDVAVLCTTSGT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1310 TGKPKGVMIPHKALTNFLVSMGETPGLTAEDKMLAVttycfdiaaleLFLPLI--------KGAHCYICqTEHTKDVEKL 1381
Cdd:cd17641 170 TGKPKLAMLSHGNFLGHCAAYLAADPLGPGDEYVSV-----------LPLPWIgeqmysvgQALVCGFI-VNFPEEPETM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1382 KRDIRTIKPTVMQATPATW-----------------KMLFY--------------------SGWENEE------------ 1412
Cdd:cd17641 238 MEDLREIGPTFVLLPPRVWegiaadvrarmmdatpfKRFMFelgmklglraldrgkrgrpvSLWLRLAswladallfrpl 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1413 -------NVKI-LCGGEAL-PETLkRYFLDTGSEAWNMFGPTETTIWSAVQRINDECSRaTIGRPIANTQIYITDSqlap 1483
Cdd:cd17641 318 rdrlgfsRLRSaATGGAALgPDTF-RFFHAIGVPLKQLYGQTELAGAYTVHRDGDVDPD-TVGVPFPGTEVRIDEV---- 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1484 vpagvpGELCIAGDGVAKGYYKKEELTDSRFIDNPFepgsklYRTGDMARWLPGGRIEYIGRI-DNQVKIRGFRIELGDI 1562
Cdd:cd17641 392 ------GEILVRSPGVFVGYYKNPEATAEDFDEDGW------LHTGDAGYFKENGHLVVIDRAkDVGTTSDGTRFSPQFI 459
|
490 500 510
....*....|....*....|....*....|....*....
gi 1776025254 1563 ESRLSEHPGILECVVV-ADMDNLAAYYTAKHANASLTAR 1600
Cdd:cd17641 460 ENKLKFSPYIAEAVVLgAGRPYLTAFICIDYAIVGKWAE 498
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
184-549 |
3.73e-15 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 81.68 E-value: 3.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 184 SSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTRED----ITFNWMPFDHvggigmlHLR---DVYLGCQ 256
Cdd:cd17648 91 TNSTDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSLSERYFGRDNGdeavLFFSNYVFDF-------FVEqmtLALLNGQ 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 257 EINVSSETILMEPLKWLDWIDHYRASVTWAPNFAFGLVtDFAEeikdrkwdLSSMRYMLNGGEAMVAKVGRRILELLeph 336
Cdd:cd17648 164 KLVVPPDEMRFDPDRFYAYINREKVTYLSGTPSVLQQY-DLAR--------LPHLKRVDAAGEEFTAPVFEKLRSRF--- 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 337 glpADAIRPAWGMSETSsgvIFSHEFTRAGTSDDDHfvEIGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGYYQ 416
Cdd:cd17648 232 ---AGLIINAYGPTETT---VTNHKRFFPGDQRFDK--SLGRPVRNTKCYVLNDAMKRVPVGAVGELYLGGDGVARGYLN 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 417 RPDLNESVFTEDGW--------------FETGDLG-FLRNGRLTITGRTKDAIIINGINYyshaiesaveELSEIE---T 478
Cdd:cd17648 304 RPELTAERFLPNPFqteqerargrnarlYKTGDLVrWLPSGELEYLGRNDFQVKIRGQRI----------EPGEVEaalA 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 479 SYTA--ACAV-------RLGQNSTDQLAIFFVTSAKLNDEQmsQLLRNIQSHVsqvigvtPEYLLP---VQKEEIPKTAI 546
Cdd:cd17648 374 SYPGvrECAVvakedasQAQSRIQKYLVGYYLPEPGHVPES--DLLSFLRAKL-------PRYMVParlVRLEGIPVTIN 444
|
...
gi 1776025254 547 GKI 549
Cdd:cd17648 445 GKL 447
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
347-564 |
4.00e-15 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 82.52 E-value: 4.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 347 WGMSETS---------SGVifsheftrAGTSDDDHFVEIGSPIPGFSMRIVNDHNELV----EEGEIgrfQVSGLSVTSG 413
Cdd:PRK05620 330 WGMTETSpvgtvarppSGV--------SGEARWAYRVSQGRFPASLEYRIVNDGQVMEstdrNEGEI---QVRGNWVTAS 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 414 YYQRP----------------DLNESVFTEDGWFETGDLGFL-RNGRLTITGRTKDAIIINGINYYSHAIESAVeelseI 476
Cdd:PRK05620 399 YYHSPteegggaastfrgedvEDANDRFTADGWLRTGDVGSVtRDGFLTIHDRARDVIRSGGEWIYSAQLENYI-----M 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 477 ETSYTAACAV------RLGQNStdqLAIFFVTSAKLNDEQMSQLLRNiqshvsQVIGVTPEYLLP---VQKEEIPKTAIG 547
Cdd:PRK05620 474 AAPEVVECAVigypddKWGERP---LAVTVLAPGIEPTRETAERLRD------QLRDRLPNWMLPeywTFVDEIDKTSVG 544
|
250
....*....|....*..
gi 1776025254 548 KIQRTQLKTSFENGEFD 564
Cdd:PRK05620 545 KFDKKDLRQHLADGDFE 561
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
187-469 |
4.15e-15 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 81.74 E-value: 4.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 187 EDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPfdhvggigMLHLRDVYLGCQ----EINvSS 262
Cdd:cd05910 85 DEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEVDLATFP--------LFALFGPALGLTsvipDMD-PT 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 263 ETILMEPLKWLDWIDHYRASVTWAPNFAFGLVTDFAEEIkDRKwdLSSMRYMLNGGEAMVAKVGRRILELLEPHglpADA 342
Cdd:cd05910 156 RPARADPQKLVGAIRQYGVSIVFGSPALLERVARYCAQH-GIT--LPSLRRVLSAGAPVPIALAARLRKMLSDE---AEI 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 343 IRPaWGMSET-SSGVIFSHEF--TRAGTSDDDHFVEIGSPIPGFSMRIVN---------DHNELVEEGEIGRFQVSGLSV 410
Cdd:cd05910 230 LTP-YGATEAlPVSSIGSRELlaTTTAATSGGAGTCVGRPIPGVRVRIIEiddepiaewDDTLELPRGEIGEITVTGPTV 308
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1776025254 411 TSGYYQRPDLNESVFTEDG----WFETGDLGFLRN-GRLTITGRTKDAIIINGINYYSHAIESA 469
Cdd:cd05910 309 TPTYVNRPVATALAKIDDNsegfWHRMGDLGYLDDeGRLWFCGRKAHRVITTGGTLYTEPVERV 372
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
1176-1640 |
4.77e-15 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 81.25 E-value: 4.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1176 GQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGayvpldpsyPAERLEYmledsevfiTL 1255
Cdd:cd05940 1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGA---------VAALINY---------NL 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1256 TTSELVNTLswngvttalldqdwdeiaQTASDRKVLTrtvtpeNLAYVIYTSGSTGKPKGVMIPHKALTNFLVSMGETPG 1335
Cdd:cd05940 63 RGESLAHCL------------------NVSSAKHLVV------DAALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGG 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1336 LTAEDKmLAVTTYCFDIAALELFLP--LIKGAHCYICQTEHTKDvekLKRDIRTIKPTVMQATPATWKMLFYSGWENEE- 1412
Cdd:cd05940 119 ALPSDV-LYTCLPLYHSTALIVGWSacLASGATLVIRKKFSASN---FWDDIRKYQATIFQYIGELCRYLLNQPPKPTEr 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1413 --NVKILCG----GEALPETLKRYFLDTGSEawnMFGPTETTIWSavqrINDECSRATIGR---------PIANTQiYIT 1477
Cdd:cd05940 195 khKVRMIFGnglrPDIWEEFKERFGVPRIAE---FYAATEGNSGF----INFFGKPGAIGRnpsllrkvaPLALVK-YDL 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1478 DSQ---------LAPVPAGVPGELC--IAGDGVAKGYYKKEElTDSRFIDNPFEPGSKLYRTGDMARWLPGGRIEYIGRI 1546
Cdd:cd05940 267 ESGepirdaegrCIKVPRGEPGLLIsrINPLEPFDGYTDPAA-TEKKILRDVFKKGDAWFNTGDLMRLDGEGFWYFVDRL 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1547 DNQVKIRGFRIELGDIESRLSEHPGILECVV----VADMD---NLAAYYTAKHANASLTAreLRHFVKNALPAYMVPsYF 1619
Cdd:cd05940 346 GDTFRWKGENVSTTEVAAVLGAFPGVEEANVygvqVPGTDgraGMAAIVLQPNEEFDLSA--LAAHLEKNLPGYARP-LF 422
|
490 500
....*....|....*....|..
gi 1776025254 1620 IQL-DHMPLTPNGKIDRNSLKN 1640
Cdd:cd05940 423 LRLqPEMEITGTFKQQKVDLRN 444
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
170-476 |
5.62e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 81.75 E-value: 5.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 170 EDLLSAEADTDWHQSSPEDL-ALLLLTSGSTGTPKAVMLNHRNIMSM-VKGIIQMQGFTREDITFNWMPFDHVGGIGMLh 247
Cdd:PRK07786 156 EDLLAEAGPAHAPVDIPNDSpALIMYTSGTTGRPKGAVLTHANLTGQaMTCLRTNGADINSDVGFVGVPLFHIAGIGSM- 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 248 LRDVYLGcqeinvssETILMEPLK------WLDWIDHYRAS------VTWAPNFAfglvtdfaeEIKDRKWDLSsMRYML 315
Cdd:PRK07786 235 LPGLLLG--------APTVIYPLGafdpgqLLDVLEAEKVTgiflvpAQWQAVCA---------EQQARPRDLA-LRVLS 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 316 NGGEAMVAKVGRRILELLephglPADAIRPAWGMSETS--SGVIFSHEFTRAGTSdddhfveIGSPIPGFSMRIVNDHNE 393
Cdd:PRK07786 297 WGAAPASDTLLRQMAATF-----PEAQILAAFGQTEMSpvTCMLLGEDAIRKLGS-------VGKVIPTVAARVVDENMN 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 394 LVEEGEIGRFQVSGLSVTSGYYQRPDLNESVFtEDGWFETGDLgfLR---NGRLTITGRTKDAIIINGINYYSHAIESAV 470
Cdd:PRK07786 365 DVPVGEVGEIVYRAPTLMSGYWNNPEATAEAF-AGGWFHSGDL--VRqdeEGYVWVVDRKKDMIISGGENIYCAEVENVL 441
|
....*.
gi 1776025254 471 EELSEI 476
Cdd:PRK07786 442 ASHPDI 447
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
52-554 |
5.66e-15 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 81.48 E-value: 5.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 52 QPDgTEVYQ------SYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNSQLLPAFWGCVLTG--VVPAPLAVPptyAES 123
Cdd:PRK04813 15 QPD-FPAYDylgeklTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGhaYIPVDVSSP---AER 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 124 ssgTQKLKDAwtlLDKPAVITDRGMHQEMLDwakeqgLEGFRAIIVEDLLSAEADTDW-HQSSPEDLALLLLTSGSTGTP 202
Cdd:PRK04813 91 ---IEMIIEV---AKPSLIIATEELPLEILG------IPVITLDELKDIFATGNPYDFdHAVKGDDNYYIIFTSGTTGKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 203 KAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMP--FDhvggigmLHLRDVY----LGCQEINVSSETI-----LMEPLK 271
Cdd:PRK04813 159 KGVQISHDNLVSFTNWMLEDFALPEGPQFLNQAPysFD-------LSVMDLYptlaSGGTLVALPKDMTanfkqLFETLP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 272 WLDwIDhyrasvTW--APNFA---FgLVTDFAEEikdrkwDLSSMRYMLNGGEAMVAKVGRRILEllephGLPADAIRPA 346
Cdd:PRK04813 232 QLP-IN------VWvsTPSFAdmcL-LDPSFNEE------HLPNLTHFLFCGEELPHKTAKKLLE-----RFPSATIYNT 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 347 WGMSETS---SGVIFSHEFTRAGTSdddhfVEIGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGYYQRPDLNES 423
Cdd:PRK04813 293 YGPTEATvavTSIEITDEMLDQYKR-----LPIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAE 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 424 VF-TEDGW--FETGDLGFLRNGRLTITGRTKDAIIING--InyyshaiesaveELSEIET-----SYT-AACAVRLGQNS 492
Cdd:PRK04813 368 AFfTFDGQpaYHTGDAGYLEDGLLFYQGRIDFQIKLNGyrI------------ELEEIEQnlrqsSYVeSAVVVPYNKDH 435
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1776025254 493 TDQLAIFFVTSAKLNDEQMSQLLRNIQSHVSQVIgvtPEYLLP---VQKEEIPKTAIGKIQRTQL 554
Cdd:PRK04813 436 KVQYLIAYVVPKEEDFEREFELTKAIKKELKERL---MEYMIPrkfIYRDSLPLTPNGKIDRKAL 497
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
191-557 |
9.82e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 81.13 E-value: 9.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 191 LLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDHVGGIGMLHLrDVYLGCQeinvsseTILME-- 268
Cdd:PRK07788 211 IVILTSGTTGTPKGAPRPEPSPLAPLAGLLSRVPFRAGETTLLPAPMFHATGWAHLTL-AMALGST-------VVLRRrf 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 269 -PLKWLDWIDHYRASvtwapnfafGLVT---------DFAEEIkDRKWDLSSMRYMLNGGEAMVAKVGRRILELLEP--H 336
Cdd:PRK07788 283 dPEATLEDIAKHKAT---------ALVVvpvmlsrilDLGPEV-LAKYDTSSLKIIFVSGSALSPELATRALEAFGPvlY 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 337 GLpadairpaWGMSETSSGVIFS-HEFTRA-GTsdddhfveIGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGY 414
Cdd:PRK07788 353 NL--------YGSTEVAFATIATpEDLAEApGT--------VGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGY 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 415 YQRPDLNesvfTEDGWFETGDLGFL-RNGRLTITGRTKDAIIINGINYYSHAIESAVEELSEIETSytAACAVR---LGQ 490
Cdd:PRK07788 417 TDGRDKQ----IIDGLLSSGDVGYFdEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEA--AVIGVDdeeFGQ 490
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1776025254 491 nstdQLAIFFVTS--AKLNDEQMSQLLRNiqsHVSqvigvtpEYLLP---VQKEEIPKTAIGKIQRTQLKTS 557
Cdd:PRK07788 491 ----RLRAFVVKApgAALDEDAIKDYVRD---NLA-------RYKVPrdvVFLDELPRNPTGKVLKRELREM 548
|
|
| fabG |
PRK12825 |
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional |
2852-3015 |
9.82e-15 |
|
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
Pssm-ID: 237218 [Multi-domain] Cd Length: 249 Bit Score: 77.22 E-value: 9.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2852 LITGGAGSLGllfaKEIANRTGRS--TIVLTGRSvlSEDKENEL-EALRSIGAEVVYREADVSDQHAVHHLFEEIKERYG 2928
Cdd:PRK12825 10 LVTGAARGLG----RAIALRLARAgaDVVVHYRS--DEEAAEELvEAVEALGRRAQAVQADVTDKAALEAAVAAAVERFG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2929 TLNGIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSGLLHVDE------CSKDFplDFFIFFSSVSGCLGNAGQADYAAANS 3002
Cdd:PRK12825 84 RIDILVNNAGIFEDKPLADMSDDEWDEVIDVNLSGVFHLLRavvppmRKQRG--GRIVNISSVAGLPGWPGRSNYAAAKA 161
|
170
....*....|...
gi 1776025254 3003 FMDAFAeyrRSLA 3015
Cdd:PRK12825 162 GLVGLT---KALA 171
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
71-449 |
9.91e-15 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 80.30 E-value: 9.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 71 RIVKGLRQSGLKAKQSVILqLGDNS-QLLPAFWGCVLTGVVPAPLAVPPTYAEsssgTQKLKDAWTLldkpavitdrgmh 149
Cdd:PRK09029 40 QLAAGFAQQGVVEGSGVAL-RGKNSpETLLAYLALLQCGARVLPLNPQLPQPL----LEELLPSLTL------------- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 150 QEMLDwakeqgLEGFRAIIVEDLLS--AEADTDWHQSSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTR 227
Cdd:PRK09029 102 DFALV------LEGENTFSALTSLHlqLVEGAHAVAWQPQRLATMTLTSGSTGLPKAAVHTAQAHLASAEGVLSLMPFTA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 228 EDitfNWM---PFDHVGGIG----------MLHLRDvylgcqeinvssetilMEPLkwldwiDHYRASVTWA---PNFAF 291
Cdd:PRK09029 176 QD---SWLlslPLFHVSGQGivwrwlyagaTLVVRD----------------KQPL------EQALAGCTHAslvPTQLW 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 292 GLVTDFAEEIkdrkwdlsSMRYMLNGGeAMVAkvgrriLEL---LEPHGlpadaIRpAW---GMSETSSGVifshefT-- 363
Cdd:PRK09029 231 RLLDNRSEPL--------SLKAVLLGG-AAIP------VELteqAEQQG-----IR-CWcgyGLTEMASTV------Cak 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 364 RAGTSDDdhfveIGSPIPGFSMRIVNDhnelveegEIgrfQVSGLSVTSGYYQ----RPDLNEsvfteDGWFETGDLGFL 439
Cdd:PRK09029 284 RADGLAG-----VGSPLPGREVKLVDG--------EI---WLRGASLALGYWRqgqlVPLVND-----EGWFATRDRGEW 342
|
410
....*....|
gi 1776025254 440 RNGRLTITGR 449
Cdd:PRK09029 343 QNGELTILGR 352
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
178-562 |
1.23e-14 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 80.82 E-value: 1.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 178 DTDWHQSSP----EDLALLLLTSGSTGTPKAVMLNHRNIMSmVKGIIQMQGFTRED-----ITFNWMPFDHVGGI----- 243
Cdd:PRK05857 156 DAASLAGNAdqgsEDPLAMIFTSGTTGEPKAVLLANRTFFA-VPDILQKEGLNWVTwvvgeTTYSPLPATHIGGLwwilt 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 244 GMLHLRDVYLGCQeiNVSSetiLMEPLkwldwIDHYRASVTWAPNfafgLVTDFAEEIKDRKWDLSSMRYMLNGGEAMVA 323
Cdd:PRK05857 235 CLMHGGLCVTGGE--NTTS---LLEIL-----TTNAVATTCLVPT----LLSKLVSELKSANATVPSLRLVGYGGSRAIA 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 324 KVGRRIlellephglPADAIRPA--WGMSETSSGVIfsheftrAGTSDDDHFVEI-----GSPIPGFSMRIVNDHN---- 392
Cdd:PRK05857 301 ADVRFI---------EATGVRTAqvYGLSETGCTAL-------CLPTDDGSIVKIeagavGRPYPGVDVYLAATDGigpt 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 393 --ELVEEGEIGRFQVSGLSVTSGYYQRPDLNESVFTeDGWFETGDLGFLR-NGRLTITGRTKDAIIINGINYYSHAIESA 469
Cdd:PRK05857 365 apGAGPSASFGTLWIKSPANMLGYWNNPERTAEVLI-DGWVNTGDLLERReDGFFYIKGRSSEMIICGGVNIAPDEVDRI 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 470 VEELSEIEtsyTAACAVRLGQNSTDQLAIFFVTSAKLNDEQMSQLLRNIQSHV---SQVIGvTPEYLLPVqkEEIPKTAI 546
Cdd:PRK05857 444 AEGVSGVR---EAACYEIPDEEFGALVGLAVVASAELDESAARALKHTIAARFrreSEPMA-RPSTIVIV--TDIPRTQS 517
|
410
....*....|....*.
gi 1776025254 547 GKIQRTQLKTSFeNGE 562
Cdd:PRK05857 518 GKVMRASLAAAA-TAD 532
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
191-486 |
1.31e-14 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 78.50 E-value: 1.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 191 LLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDHVG----GIGMLHL--RDVYLGCqeinVSSET 264
Cdd:cd17636 4 LAIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLNSGPLFHIGtlmfTLATFHAggTNVFVRR----VDAEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 265 ILmeplkwlDWIDHYRasVTWApnFAFGLVTD-FAEEIKDRKWDLSSMRymlnggeAMVAKVGRRILellephgLPADAi 343
Cdd:cd17636 80 VL-------ELIEAER--CTHA--FLLPPTIDqIVELNADGLYDLSSLR-------SSPAAPEWNDM-------ATVDT- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 344 rPAW-------GMSETSSGVIFSHeftRAGTSDDDHfveiGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGYYQ 416
Cdd:cd17636 134 -SPWgrkpggyGQTEVMGLATFAA---LGGGAIGGA----GRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWN 205
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1776025254 417 RPDLNeSVFTEDGWFETGDLGfLRN--GRLTITGrTKDAIIINGI-NYYSHAIESAVEELSEIetsytAACAV 486
Cdd:cd17636 206 RPEVN-ARRTRGGWHHTNDLG-RREpdGSLSFVG-PKTRMIKSGAeNIYPAEVERCLRQHPAV-----ADAAV 270
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
19-555 |
1.59e-14 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 80.19 E-value: 1.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 19 EPLHISEKqpaTIPEVLYRTAAELGDTkgiIYLQPDGTevyqsyRRLWDDGLRIVKG----LRQSGLKAKQSVILQLGDN 94
Cdd:PRK06155 14 DPLPPSER---TLPAMLARQAERYPDR---PLLVFGGT------RWTYAEAARAAAAaahaLAAAGVKRGDRVALMCGNR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 95 SQLLPAFWGCVLTGVVPAP---------------------LAVPPTYAES----SSGTQKLKDAWTLLDKPAVITDRGmh 149
Cdd:PRK06155 82 IEFLDVFLGCAWLGAIAVPintalrgpqlehilrnsgarlLVVEAALLAAleaaDPGDLPLPAVWLLDAPASVSVPAG-- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 150 qemldWAkeqglegfraiiVEDLLSAEADTDWHQSSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTRED 229
Cdd:PRK06155 160 -----WS------------TAPLPPLDAPAPAAAVQPGDTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADD 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 230 ITFNWMPFDHVGGIGMLHlrdvylgcqEINVSSETILMEPlkwldwidHYRASVTWAPNFAFGLVTDFAeeikdrkwdLS 309
Cdd:PRK06155 223 VLYTTLPLFHTNALNAFF---------QALLAGATYVLEP--------RFSASGFWPAVRRHGATVTYL---------LG 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 310 SMRYMLNGGEAMVAKVGRRILELLEPhGLPADAIRP-----------AWGMSETSSGVIFSHEFTRAGTsdddhfveIGS 378
Cdd:PRK06155 277 AMVSILLSQPARESDRAHRVRVALGP-GVPAALHAAfrerfgvdlldGYGSTETNFVIAVTHGSQRPGS--------MGR 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 379 PIPGFSMRIVNDHNELVEEGEIGRFQVSG---LSVTSGYYQRPdlNESVFT-EDGWFETGDLGFLR-NGRLTITGRTKDA 453
Cdd:PRK06155 348 LAPGFEARVVDEHDQELPDGEPGELLLRAdepFAFATGYFGMP--EKTVEAwRNLWFHTGDRVVRDaDGWFRFVDRIKDA 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 454 IIINGINYYSHAIESAVEELSEIetsytAACAVrlgqnstdqlaiFFVTSAKLNDEQMS-------------QLLRNIQS 520
Cdd:PRK06155 426 IRRRGENISSFEVEQVLLSHPAV-----AAAAV------------FPVPSELGEDEVMAavvlrdgtalepvALVRHCEP 488
|
570 580 590
....*....|....*....|....*....|....*
gi 1776025254 521 HVSQVigVTPEYLLPVQkeEIPKTAIGKIQRTQLK 555
Cdd:PRK06155 489 RLAYF--AVPRYVEFVA--ALPKTENGKVQKFVLR 519
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
184-554 |
1.60e-14 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 79.82 E-value: 1.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 184 SSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITF--NWMPFDH--VGGIGMLHLrdvylGCQEIN 259
Cdd:cd17654 115 RTDECLAYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFNITSEDILFltSPLTFDPsvVEIFLSLSS-----GATLLI 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 260 VSSETILMePLKWLDWID-HYRASVTWAPN---FAFGlvtdfAEEIKDRKWD-LSSMRYMLNGGEAMVAKVgrrILELLE 334
Cdd:cd17654 190 VPTSVKVL-PSKLADILFkRHRITVLQATPtlfRRFG-----SQSIKSTVLSaTSSLRVLALGGEPFPSLV---ILSSWR 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 335 PHGLPADAIRpAWGMSETSSGVIFSHeftragTSDDDHFVEIGSPIPGFSMRIVnDHNELVEEGEIGRFQVSGLSVTSGY 414
Cdd:cd17654 261 GKGNRTRIFN-IYGITEVSCWALAYK------VPEEDSPVQLGSPLLGTVIEVR-DQNGSEGTGQVFLGGLNRVCILDDE 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 415 YQRPdlnesvftEDGWFETGDLGFLRNGRLTITGRTKDAIIINGINYYSHAIESAVEELSEIEtsytaACAVRLGQNstD 494
Cdd:cd17654 333 VTVP--------KGTMRATGDFVTVKDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVE-----SCAVTLSDQ--Q 397
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 495 QLAIFFVTSAKLNDEQMSQLLRNIQSHvsqvigVTPEYLlpVQKEEIPKTAIGKIQRTQL 554
Cdd:cd17654 398 RLIAFIVGESSSSRIHKELQLTLLSSH------AIPDTF--VQIDKLPLTSHGKVDKSEL 449
|
|
| PRK14691 |
PRK14691 |
3-oxoacyl-(acyl carrier protein) synthase II; Provisional |
1914-2140 |
1.63e-14 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
Pssm-ID: 173154 [Multi-domain] Cd Length: 342 Bit Score: 78.62 E-value: 1.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1914 ISHKLGLRGPSYFVHANCSSSLIGLHSAYKSLLSAESDYALVGGA--TLHTESNIGYVHQPGL----NFSSDGHIKAFDA 1987
Cdd:PRK14691 74 VSIKHHFKGPIGAPVTACAAGVQAIGDAVRMIRNNEADVALCGGAeaVIDTVSLAGFAAARALsthfNSTPEKASRPFDT 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1988 SADGMIGGEGVAVVLLKKAADAVKDGDHIYALLRGIGVNNDgADKVGFYAPSVKGQADVVQQVMNQTKIHPESICYVEAH 2067
Cdd:PRK14691 154 ARDGFVMGEGAGLLIIEELEHALARGAKPLAEIVGYGTSAD-AYHMTSGAEDGDGAYRAMKIALRQAGITPEQVQHLNAH 232
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1776025254 2068 GTGTKLGDPIELAALTNVYrqytNKTQFCGIGSVKTNIGHLDTAAGLAGCIKVVMSLYHQELAPSINYKEPNP 2140
Cdd:PRK14691 233 ATSTPVGDLGEINAIKHLF----GESNALAITSTKSATGHLLGAAGGLETIFTVLALRDQIVPATLNLENPDP 301
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
1180-1649 |
1.77e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 80.14 E-value: 1.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1180 TYRELDERSTQLAIYLQAHGVGP-DRLAGI----YvdRSLDMLVGLlailkAGGAYV--PLDPSYPAERLEYML---EDS 1249
Cdd:PRK07008 41 TYRDCERRAKQLAQALAALGVEPgDRVGTLawngY--RHLEAYYGV-----SGSGAVchTINPRLFPEQIAYIVnhaEDR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1250 EVFITLTTSELVNTLS--------WNGVTTA----------LLDQDWDEIAQTASDRKVLTrtvtpENLA-YVIYTSGST 1310
Cdd:PRK07008 114 YVLFDLTFLPLVDALApqcpnvkgWVAMTDAahlpagstplLCYETLVGAQDGDYDWPRFD-----ENQAsSLCYTSGTT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1311 GKPKGVMIPHKA--LTNFLVSMGETPGLTAEDKMLAVT----------TYCFDIAALELFLPlikGAHCyicqtehtkDV 1378
Cdd:PRK07008 189 GNPKGALYSHRStvLHAYGAALPDAMGLSARDAVLPVVpmfhvnawglPYSAPLTGAKLVLP---GPDL---------DG 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1379 EKLKRDIRTIKPTVMQATPATWKMLFysGWENEENVKI------LCGGEALPETLKRYFLDT-GSE---AWNM-----FG 1443
Cdd:PRK07008 257 KSLYELIEAERVTFSAGVPTVWLGLL--NHMREAGLRFstlrrtVIGGSACPPAMIRTFEDEyGVEvihAWGMtemspLG 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1444 PTETTIWSAVQRINDE--CSRATIGRPIANTQIYITDSQLAPVP-AGVP-GELCIAGDGVAKGYYKKEeltDSRFIDNPF 1519
Cdd:PRK07008 335 TLCKLKWKHSQLPLDEqrKLLEKQGRVIYGVDMKIVGDDGRELPwDGKAfGDLQVRGPWVIDRYFRGD---ASPLVDGWF 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1520 EpgsklyrTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILE--CVVVA--DMDNLAAYYTAKHANA 1595
Cdd:PRK07008 412 P-------TGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEaaCIACAhpKWDERPLLVVVKRPGA 484
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1776025254 1596 SLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLKnidlsgEQLK 1649
Cdd:PRK07008 485 EVTREELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLR------EQFR 532
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
1180-1579 |
1.81e-14 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 79.84 E-value: 1.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1180 TYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGgaYVPLdPSYPAERLEYMLEDSEVFITLTTSE 1259
Cdd:cd05908 17 SYRHLREEALGYLGALQELGIKPGQEVVFQITHNNKFLYLFWACLLGG--MIAV-PVSIGSNEEHKLKLNKVWNTLKNPY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1260 LVNTlswngvttallDQDWDEIaqtasdrkvltrtvtPENLAYVIYTSGSTGKPKGVMIPHKALTNFLVSMGETPGLTAE 1339
Cdd:cd05908 94 LITE-----------EEVLCEL---------------ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1340 DKMLAVTTYCFDIAALELFL-PLIKGAHCYICQTEH--------TKDVEKLKRDI------------RTIKPTVMqatpa 1398
Cdd:cd05908 148 DRILSWMPLTHDMGLIAFHLaPLIAGMNQYLMPTRLfirrpilwLKKASEHKATIvsspnfgykyflKTLKPEKA----- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1399 twkmlfySGWENEENVKILCGGEALPETLKRYFLDTGSE-------AWNMFGPTETTIWS-------------------- 1451
Cdd:cd05908 223 -------NDWDLSSIRMILNGAEPIDYELCHEFLDHMSKyglkrnaILPVYGLAEASVGAslpkaqspfktitlgrrhvt 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1452 ------AVQRINDECSR-ATIGRPIANTQIYITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNPFepgsk 1524
Cdd:cd05908 296 hgepepEVDKKDSECLTfVEVGKPIDETDIRICDEDNKILPDGYIGHIQIRGKNVTPGYYNNPEATAKVFTDDGW----- 370
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1776025254 1525 lYRTGDMArWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVA 1579
Cdd:cd05908 371 -LKTGDLG-FIRNGRLVITGREKDIIFVNGQNVYPHDIERIAEELEGVELGRVVA 423
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
51-562 |
2.51e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 79.44 E-value: 2.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 51 LQPDGTEVYQSYRRL----WDDGLRIV-KGLRQSGLKAKQSVILqLGDNSQLLPAFWGCVLTGVVPAPLAVPPTYAEsss 125
Cdd:PRK07638 13 LQPNKIAIKENDRVLtykdWFESVCKVaNWLNEKESKNKTIAIL-LENRIEFLQLFAGAAMAGWTCVPLDIKWKQDE--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 126 gtqkLKDAWTLLDKPAVITDRGMHQEMLDwakEQGlegfrAIIVED----LLSAEADTDWHQSSPEDLALLL-LTSGSTG 200
Cdd:PRK07638 89 ----LKERLAISNADMIVTERYKLNDLPD---EEG-----RVIEIDewkrMIEKYLPTYAPIENVQNAPFYMgFTSGSTG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 201 TPKAVMLNHRNimsmvkgiiQMQGFTREDITFNWMPFDHVGGIGML-HLRDVYLGCQEINVSSETILME---PLKWLDWI 276
Cdd:PRK07638 157 KPKAFLRAQQS---------WLHSFDCNVHDFHMKREDSVLIAGTLvHSLFLYGAISTLYVGQTVHLMRkfiPNQVLDKL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 277 DHYRASVTWA-PNFAFGLVTdfAEEIKDrkwdlSSMRYMLNGGEAMVAKVGRriLELLEPHGLPADAirpaWGMSETSSg 355
Cdd:PRK07638 228 ETENISVMYTvPTMLESLYK--ENRVIE-----NKMKIISSGAKWEAEAKEK--IKNIFPYAKLYEF----YGASELSF- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 356 VIFSH--EFTRAGTSdddhfveIGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGYyqrpdLNESVF----TEDG 429
Cdd:PRK07638 294 VTALVdeESERRPNS-------VGRPFHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGY-----IIGGVLarelNADG 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 430 WFETGDLGFL-RNGRLTITGRTKDAIIINGINYYSHAIESAVEELSEIET--------SY--TAACAVRLGQNSTDQLAi 498
Cdd:PRK07638 362 WMTVRDVGYEdEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEivvigvpdSYwgEKPVAIIKGSATKQQLK- 440
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1776025254 499 ffvtsaklndeqmSQLLRNIQShvsqvIGVTPEYLLpvqKEEIPKTAIGKIQRTQLKTSFENGE 562
Cdd:PRK07638 441 -------------SFCLQRLSS-----FKIPKEWHF---VDEIPYTNSGKIARMEAKSWIENQE 483
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
1297-1587 |
5.33e-14 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 78.99 E-value: 5.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1297 PENLAYVIYTSGSTGKPKGVMIPHKaltNFLVSmgetpgltAEDKMLAVTTYCFDIAALelFLPLikgAHCY----ICQT 1372
Cdd:PLN02736 220 PEDVATICYTSGTTGTPKGVVLTHG---NLIAN--------VAGSSLSTKFYPSDVHIS--YLPL---AHIYervnQIVM 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1373 EH--------TKDVEKLKRDIRTIKPTVMQATPATW------------------KMLFYSGW-------ENEEN------ 1413
Cdd:PLN02736 284 LHygvavgfyQGDNLKLMDDLAALRPTIFCSVPRLYnriydgitnavkesgglkERLFNAAYnakkqalENGKNpspmwd 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1414 ------VKILCGGE-------ALP------ETLKRYFLDTGSEAWNMfgpTETTIWSAVQRINDECSrATIGRPIANTQI 1474
Cdd:PLN02736 364 rlvfnkIKAKLGGRvrfmssgASPlspdvmEFLRICFGGRVLEGYGM---TETSCVISGMDEGDNLS-GHVGSPNPACEV 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1475 YITD-------SQLAPVPAGvpgELCIAGDGVAKGYYKKEELTDSrFIDnpfEPGskLYRTGDMARWLPGGRIEYIGRID 1547
Cdd:PLN02736 440 KLVDvpemnytSEDQPYPRG---EICVRGPIIFKGYYKDEVQTRE-VID---EDG--WLHTGDIGLWLPGGRLKIIDRKK 510
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1776025254 1548 NQVKI-RGFRIELGDIESRLSEHPGILEC-------------VVVADMDNLAAY 1587
Cdd:PLN02736 511 NIFKLaQGEYIAPEKIENVYAKCKFVAQCfvygdslnsslvaVVVVDPEVLKAW 564
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
1167-1643 |
9.21e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 77.68 E-value: 9.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1167 PDRAAVSYEGQTLTYRELDERSTQLAIYLQAHGVGP-DRLAGIYVDRSlDMLVGLLAILKAGGAYVPLDPSYPAERLEYM 1245
Cdd:PRK08162 32 PDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRgDTVAVLLPNIP-AMVEAHFGVPMAGAVLNTLNTRLDAASIAFM 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1246 LEDSEVFITLTTSELVNT----LSWNGVTTALL---------------DQDWDEIAQTASDRKVLTRtvtPENLAYVI-- 1304
Cdd:PRK08162 111 LRHGEAKVLIVDTEFAEVareaLALLPGPKPLVidvddpeypggrfigALDYEAFLASGDPDFAWTL---PADEWDAIal 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1305 -YTSGSTGKPKGVMIPHK-----ALTNFLV-SMGETPGLTAEDKMLAVTTYCF--DIAALelflpliKGAHcyICQteHT 1375
Cdd:PRK08162 188 nYTSGTTGNPKGVVYHHRgaylnALSNILAwGMPKHPVYLWTLPMFHCNGWCFpwTVAAR-------AGTN--VCL--RK 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1376 KDVEKLKRDIRTIK-------PTVMQA---TPATWKMLFysgwenEENVKILCGGEALPETLKRYFLDTGSEAWNMFGPT 1445
Cdd:PRK08162 257 VDPKLIFDLIREHGvthycgaPIVLSAlinAPAEWRAGI------DHPVHAMVAGAAPPAAVIAKMEEIGFDLTHVYGLT 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1446 ETTIWSAVQRINDECS------RATIG-----RPIANTQIYITDSQ-LAPVPAG--VPGELCIAGDGVAKGYYKKEELTD 1511
Cdd:PRK08162 331 ETYGPATVCAWQPEWDalpldeRAQLKarqgvRYPLQEGVTVLDPDtMQPVPADgeTIGEIMFRGNIVMKGYLKNPKATE 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1512 SRFIDNPFEpgsklyrTGDMARWLPGGrieYIgridnQVKIR--------GFRIELGDIESRLSEHPGILECVVVADMDN 1583
Cdd:PRK08162 411 EAFAGGWFH-------TGDLAVLHPDG---YI-----KIKDRskdiiisgGENISSIEVEDVLYRHPAVLVAAVVAKPDP 475
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1776025254 1584 L-----AAYYTAKhANASLTARELRHFVKNALPAYMVPSYFIqLDHMPLTPNGKIDR-------NSLKNIDL 1643
Cdd:PRK08162 476 KwgevpCAFVELK-DGASATEEEIIAHCREHLAGFKVPKAVV-FGELPKTSTGKIQKfvlreqaKSLKAIDL 545
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
1159-1554 |
9.51e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 78.23 E-value: 9.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1159 FEQQAKKTPDRAAVSY---------EGQTLTYRELDERSTQLAIYLQAHGVGPDRLAgIYVDRSLDMLVGLLAILKAGGA 1229
Cdd:PRK07769 27 VERWAKVRGDKLAYRFldfsterdgVARDLTWSQFGARNRAVGARLQQVTKPGDRVA-ILAPQNLDYLIAFFGALYAGRI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1230 YVPL-DPSYP--AERLEYMLEDSEVFITLTTSElvntlSWNGVTTALLDQDWDE----IAQTASDRKVLTRTVTPE---- 1298
Cdd:PRK07769 106 AVPLfDPAEPghVGRLHAVLDDCTPSAILTTTD-----SAEGVRKFFRARPAKErprvIAVDAVPDEVGATWVPPEaned 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1299 NLAYVIYTSGSTGKPKGVMIPHKALTNFLVSMGETPGLTAEDKMLAVTTYCFDIAALELFLPLIKGAHCYIcqtehTKDV 1378
Cdd:PRK07769 181 TIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEGQEGDRGVSWLPFFHDMGLITVLLPALLGHYITF-----MSPA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1379 EKLKRDIRTIK---------PTVMQATP------ATWKMLFYSGwENE---ENVK-ILCGGEAL-PETLKRYFldtgsEA 1438
Cdd:PRK07769 256 AFVRRPGRWIRelarkpggtGGTFSAAPnfafehAAARGLPKDG-EPPldlSNVKgLLNGSEPVsPASMRKFN-----EA 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1439 WNMFG--PT---------ETTIWSAVQRINDECSRATIGR---------------PIANTQI---YITDSQLA------- 1482
Cdd:PRK07769 330 FAPYGlpPTaikpsygmaEATLFVSTTPMDEEPTVIYVDRdelnagrfvevpadaPNAVAQVsagKVGVSEWAvivdpet 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1483 --PVPAGVPGELCIAGDGVAKGYYKKEELTDSRF---IDNPF--------EPGSKLYRTGDMARWLPGGRieYI-GRIDN 1548
Cdd:PRK07769 410 asELPDGQIGEIWLHGNNIGTGYWGKPEETAATFqniLKSRLseshaegaPDDALWVRTGDYGVYFDGEL--YItGRVKD 487
|
....*.
gi 1776025254 1549 QVKIRG 1554
Cdd:PRK07769 488 LVIIDG 493
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
145-436 |
1.05e-13 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 77.88 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 145 DRGMHQEMLDWAKEQGLEGFRAIIVEDLLSAE------ADTDWHQSSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKG 218
Cdd:cd17632 175 EVDAHRAALESARERLAAVGIPVTTLTLIAVRgrdlppAPLFRPEPDDDPLALLIYTSGSTGTPKGAMYTERLVATFWLK 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 219 IIQMQGFT-REDITFNWMPFDHVGGIGMLH--------------------LRDVYLgcqeinVSSETILMEPLKWLDWID 277
Cdd:cd17632 255 VSSIQDIRpPASITLNFMPMSHIAGRISLYgtlarggtayfaaasdmstlFDDLAL------VRPTELFLVPRVCDMLFQ 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 278 HYRASVTWAPNFAFGLVTDfAEEIKdrkwdlSSMRYMLNGGEAMVAKVGRRIL---------ELLEPHglpadaIRPAWG 348
Cdd:cd17632 329 RYQAELDRRSVAGADAETL-AERVK------AELRERVLGGRLLAAVCGSAPLsaemkafmeSLLDLD------LHDGYG 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 349 MSETsSGVIFSHEFTRagtsdddhfveigSPipgfsmriVNDHnELVEEGEIGRFQ-----------VSGLSVTSGYYQR 417
Cdd:cd17632 396 STEA-GAVILDGVIVR-------------PP--------VLDY-KLVDVPELGYFRtdrphprgellVKTDTLFPGYYKR 452
|
330
....*....|....*....
gi 1776025254 418 PDLNESVFTEDGWFETGDL 436
Cdd:cd17632 453 PEVTAEVFDEDGFYRTGDV 471
|
|
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
4741-4939 |
1.23e-13 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 76.24 E-value: 1.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4741 ACSSALVGMNMAIQALRGGDIQSAIVGGVSLLSSDASHRLFDRRGILSKHSSFHvFDERADGVVLGEGVGMVMLKTVKQA 4820
Cdd:PRK05952 145 ACATGLWAIAQGVELIQTGQCQRVIAGAVEAPITPLTLAGFQQMGALAKTGAYP-FDRQREGLVLGEGGAILVLESAELA 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4821 LEDGDTIYAVVKAASVNNDG-RTAGPATPNLEAQKEVmKDALFKSGKKPEDISYLEANGSGSIVTDLLELKAIQSVYrsG 4899
Cdd:PRK05952 224 QKRGAKIYGQILGFGLTCDAyHMSAPEPDGKSAIAAI-QQCLARSGLTPEDIDYIHAHGTATRLNDQREANLIQALF--P 300
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1776025254 4900 HSSPLSlgSIKPNIGHPLCAEGIASFIKVVLMLKERRFVP 4939
Cdd:PRK05952 301 HRVAVS--STKGATGHTLGASGALGVAFSLLALRHQQLPP 338
|
|
| CLF |
cd00832 |
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ... |
3340-3664 |
1.37e-13 |
|
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic antibiotic-producing polyketide synthases (PKSs) of filamentous bacteria. CLFs have been shown to have decarboxylase activity towards malonyl-acyl carrier protein (ACP). CLFs are similar to other elongation ketosynthase domains, but their active site cysteine is replaced by a conserved glutamine.
Pssm-ID: 238428 [Multi-domain] Cd Length: 399 Bit Score: 76.25 E-value: 1.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3340 PVAIVGISGRFPGAMDIDEFWKNLEEGKDSITEVpkDRWDwREHYGNPdtdvnktdikWGGFIDGvaeFDPLFfGISPRE 3419
Cdd:cd00832 2 RAVVTGIGVVAPNGLGVEEYWKAVLDGRSGLGPI--TRFD-PSGYPAR----------LAGEVPD---FDAAE-HLPGRL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3420 ADYVDPQQRLLMTYVWKALEDAGCPPQSLSGTGTGIFIGTGNTGYkDLFHRanlpiEGHAATGHmipsvGPNRMSYFLNI 3499
Cdd:cd00832 65 LPQTDRMTRLALAAADWALADAGVDPAALPPYDMGVVTASAAGGF-EFGQR-----ELQKLWSK-----GPRHVSAYQSF 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3500 -----------------HGPSEPVETACSSSLVAIHRAVTAMQNGDCEMaIAGGVNTILTEEAHISYSKAGMLSKDGRCK 3562
Cdd:cd00832 134 awfyavntgqisirhgmRGPSGVVVAEQAGGLDALAQARRLVRRGTPLV-VSGGVDSALCPWGWVAQLSSGRLSTSDDPA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3563 T----FSADANGYVRGEGVGMVMLKKLEDAERDGNHIYGVIrgtaenhGGRANTLTSPNPKAQADLLVRAYR----QAGI 3634
Cdd:cd00832 213 RaylpFDAAAAGYVPGEGGAILVLEDAAAARERGARVYGEI-------AGYAATFDPPPGSGRPPGLARAIRlalaDAGL 285
|
330 340 350
....*....|....*....|....*....|
gi 1776025254 3635 DPSTVTYIEAHGTGTELGDPIEINGLKAAF 3664
Cdd:cd00832 286 TPEDVDVVFADAAGVPELDRAEAAALAAVF 315
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
1178-1631 |
1.47e-13 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 77.50 E-value: 1.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1178 TLTYRELDERSTQLAIYLQA-HGVGP-DRLAGIYVDrSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLEDSE----- 1250
Cdd:cd17632 67 TITYAELWERVGAVAAAHDPeQPVRPgDFVAVLGFT-SPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEprlla 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1251 -----------------------VF-----ITLTTSELVNT---LSWNGVTTALLDQDWDeIAQTASDRKVLTRTVTPEN 1299
Cdd:cd17632 146 vsaehldlaveavleggtpprlvVFdhrpeVDAHRAALESArerLAAVGIPVTTLTLIAV-RGRDLPPAPLFRPEPDDDP 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1300 LAYVIYTSGSTGKPKGVMIPHKALTNF--LVSMGEtpgltaEDKMLAVTTYCF----DIAA-LELFLPLIKGAHCYICQT 1372
Cdd:cd17632 225 LALLIYTSGSTGTPKGAMYTERLVATFwlKVSSIQ------DIRPPASITLNFmpmsHIAGrISLYGTLARGGTAYFAAA 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1373 EhtkDVEKLKRDIRTIKPTVMQATPATWKMLF--YSGWEN------------EENVKI--------------LCGGEALP 1424
Cdd:cd17632 299 S---DMSTLFDDLALVRPTELFLVPRVCDMLFqrYQAELDrrsvagadaetlAERVKAelrervlggrllaaVCGSAPLS 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1425 ETLKRyFLDT--GSEAWNMFGPTETtiwSAVQRINdecsraTIGRPiantqiYITDSQLAPVP------AGVP---GELC 1493
Cdd:cd17632 376 AEMKA-FMESllDLDLHDGYGSTEA---GAVILDG------VIVRP------PVLDYKLVDVPelgyfrTDRPhprGELL 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1494 IAGDGVAKGYYKKEELTDSRFIDNPFepgsklYRTGD-MARWLPgGRIEYIGRIDNQVKI-RGFRIELGDIESRLSEHPG 1571
Cdd:cd17632 440 VKTDTLFPGYYKRPEVTAEVFDEDGF------YRTGDvMAELGP-DRLVYVDRRNNVLKLsQGEFVTVARLEAVFAASPL 512
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1776025254 1572 I-------------LECVVVADMDNLAAYYTAK-----HANASLTARElrhfvkNALPAYMVPSYFIqLDHMPLTP-NG 1631
Cdd:cd17632 513 VrqifvygnserayLLAVVVPTQDALAGEDTARlraalAESLQRIARE------AGLQSYEIPRDFL-IETEPFTIaNG 584
|
|
| SDR_c |
cd05233 |
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ... |
4174-4341 |
1.49e-13 |
|
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.
Pssm-ID: 212491 [Multi-domain] Cd Length: 234 Bit Score: 73.47 E-value: 1.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4174 LITGGTRGIGLLCARHFAEcYGVkKLVLTGREqlppreewarfktsntslAEKIQAVRELEAKGVQVEMLSLTLSDDAQV 4253
Cdd:cd05233 2 LVTGASSGIGRAIARRLAR-EGA-KVVLADRN------------------EEALAELAAIEALGGNAVAVQADVSDEEDV 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4254 EQTLQHIKRTLGPIGGVIHCAGLTDMDTLAFIrkTSDDIQRVMEPKVSGLTtlyrHVCNEPLQFF--------VLFSSVS 4325
Cdd:cd05233 62 EALVEEALEEFGRLDILVNNAGIARPGPLEEL--TDEDWDRVLDVNLTGVF----LLTRAALPHMkkqgggriVNISSVA 135
|
170
....*....|....*.
gi 1776025254 4326 AIIPelSAGQADYAMA 4341
Cdd:cd05233 136 GLRP--LPGQAAYAAS 149
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1297-1639 |
1.61e-13 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 75.59 E-value: 1.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1297 PENLAYVIYTSGSTGKPKgvMIPHKALTnfLVSMGETPGLTA---EDKMLAVTTYCFDIAAL--ELFLPLIKGAHCYICQ 1371
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPK--LAQHTHSN--EVYNAWMLALNSlfdPDDVLLCGLPLFHVNGSvvTLLTPLASGAHVVLAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1372 TEHTKD---VEKLKRDIRTIKPTVMQATPATWKMLFysgwENEENVKI------LCGGEALPETLKRYFLD-TGSEAWNM 1441
Cdd:cd05944 77 PAGYRNpglFDNFWKLVERYRITSLSTVPTVYAALL----QVPVNADIsslrfaMSGAAPLPVELRARFEDaTGLPVVEG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1442 FGPTETTIWSAVQRINDECSRATIGRPIANTQIYItdSQLAPV-----PAGVP--GELCIAGDGVAKGYYKKEELTDSrF 1514
Cdd:cd05944 153 YGLTEATCLVAVNPPDGPKRPGSVGLRLPYARVRI--KVLDGVgrllrDCAPDevGEICVAGPGVFGGYLYTEGNKNA-F 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1515 IDNPFepgsklYRTGDMARWLPGGRIEYIGRIDNQVkIRG-FRIELGDIESRLSEHPGILECVVVADMDNLA-----AYY 1588
Cdd:cd05944 230 VADGW------LNTGDLGRLDADGYLFITGRAKDLI-IRGgHNIDPALIEEALLRHPAVAFAGAVGQPDAHAgelpvAYV 302
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1776025254 1589 TAKhANASLTARELRHFVKNALPAYM-VPSYFIQLDHMPLTPNGKIDRNSLK 1639
Cdd:cd05944 303 QLK-PGAVVEEEELLAWARDHVPERAaVPKHIEVLEELPVTAVGKVFKPALR 353
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
185-438 |
1.63e-13 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 77.03 E-value: 1.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 185 SPEDLALLLLTSGSTGTPKAVMLNHRNIM-SMVKGIIQMQgFTREDITFNWMPFDHVGgigmlhlrdvylgCQ------E 257
Cdd:PRK08008 171 STDDTAEILFTSGTTSRPKGVVITHYNLRfAGYYSAWQCA-LRDDDVYLTVMPAFHID-------------CQctaamaA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 258 INVSSETILMEPL---KWLDWIDHYRASVTWA-PNFAFGLVTDFAEEiKDRKWDLSSMRYMLN----GGEAMVAKVGRRI 329
Cdd:PRK08008 237 FSAGATFVLLEKYsarAFWGQVCKYRATITECiPMMIRTLMVQPPSA-NDRQHCLREVMFYLNlsdqEKDAFEERFGVRL 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 330 LEllephglpadairpAWGMSETSSGVIFSheftRAGtsDDDHFVEIGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGL- 408
Cdd:PRK08008 316 LT--------------SYGMTETIVGIIGD----RPG--DKRRWPSIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKGVp 375
|
250 260 270
....*....|....*....|....*....|..
gi 1776025254 409 --SVTSGYYQRPDLNESVFTEDGWFETGDLGF 438
Cdd:PRK08008 376 gkTIFKEYYLDPKATAKVLEADGWLHTGDTGY 407
|
|
| PKS_PP |
smart00823 |
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ... |
3111-3185 |
2.32e-13 |
|
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.
Pssm-ID: 214834 [Multi-domain] Cd Length: 86 Bit Score: 68.43 E-value: 2.32e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1776025254 3111 QTRKLEAALIQMVGAILKVNTDD-IDVNTELSEYGFDSVTFTVFTNKINEKFQLELTPTIFFEYGSVQSLAEYVVA 3185
Cdd:smart00823 9 RRRLLLDLVREQVAAVLGHAAAEaIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHLAA 84
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
33-549 |
2.51e-13 |
|
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341289 [Multi-domain] Cd Length: 587 Bit Score: 76.46 E-value: 2.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 33 EVLYRTAAELGDTKGIIYLQPDGTEVYQ-SYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNSQLLPAFWGCVLTGVVP 111
Cdd:cd17634 57 NALDRHLRENGDRTAIIYEGDDTSQSRTiSYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVH 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 112 APLAVPPTYAESSSgtqKLKDAWTLLdkpaVITDRGMHQ--------EMLDWAKEQGLEGFRAIIVEDLLSAE------A 177
Cdd:cd17634 137 SVIFGGFAPEAVAG---RIIDSSSRL----LITADGGVRagrsvplkKNVDDALNPNVTSVEHVIVLKRTGSDidwqegR 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 178 DTDWHQS-------------SPEDLALLLLTSGSTGTPKAVMlnHRNIMSMVKGIIQMQ---GFTREDItfnWMPFDHVG 241
Cdd:cd17634 210 DLWWRDLiakaspehqpeamNAEDPLFILYTSGTTGKPKGVL--HTTGGYLVYAATTMKyvfDYGPGDI---YWCTADVG 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 242 GIgMLHLRDVYLGcqeINVSSETILME-------PLKWLDWIDHYRASVTW-APNFAFGLVTDFAEEIKdrKWDLSSMRY 313
Cdd:cd17634 285 WV-TGHSYLLYGP---LACGATTLLYEgvpnwptPARMWQVVDKHGVNILYtAPTAIRALMAAGDDAIE--GTDRSSLRI 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 314 MLNGGEAMVAKVGRRILELLEPHGLPadaIRPAWGMSETSSGVIFS---HEFTRAGTSDddhfveigSPIPGFSMRIVND 390
Cdd:cd17634 359 LGSVGEPINPEAYEWYWKKIGKEKCP---VVDTWWQTETGGFMITPlpgAIELKAGSAT--------RPVFGVQPAVVDN 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 391 HNELVEEGEIGRFqVSGLS---VTSGYYQRPDLNESVF--TEDGWFETGDLGFL-RNGRLTITGRTKDAIIINGINYYSH 464
Cdd:cd17634 428 EGHPQPGGTEGNL-VITDPwpgQTRTLFGDHERFEQTYfsTFKGMYFSGDGARRdEDGYYWITGRSDDVINVAGHRLGTA 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 465 AIESAVEELSEIetsytAACAVRLGQNSTDQLAIFFVTSAKLNDEQMSQLLRNIQSHVSQVIG--VTPEYLLPVQkeEIP 542
Cdd:cd17634 507 EIESVLVAHPKV-----AEAAVVGIPHAIKGQAPYAYVVLNHGVEPSPELYAELRNWVRKEIGplATPDVVHWVD--SLP 579
|
....*..
gi 1776025254 543 KTAIGKI 549
Cdd:cd17634 580 KTRSGKI 586
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
43-562 |
2.54e-13 |
|
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.
Pssm-ID: 341271 [Multi-domain] Cd Length: 617 Bit Score: 76.59 E-value: 2.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 43 GDTKGIIYLQP-DGTEVYQSYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNSQLLPAFWGCVLTG----VVPAPLAVP 117
Cdd:cd05967 65 GDQIALIYDSPvTGTERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGaihsVVFGGFAAK 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 118 ptyaESSSgtqKLKDAwtlldKPAVI--TDRGM-------HQEMLDWAKEQGLEGFRAIIVEDLLSAEADT-------DW 181
Cdd:cd05967 145 ----ELAS---RIDDA-----KPKLIvtASCGIepgkvvpYKPLLDKALELSGHKPHHVLVLNRPQVPADLtkpgrdlDW 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 182 H----QSSPEDLALL--------LLTSGSTGTPK---------AVMLNH--RNIMSMVKGIIQmqgFTREDItfNWMpfd 238
Cdd:cd05967 213 SellaKAEPVDCVPVaatdplyiLYTSGTTGKPKgvvrdngghAVALNWsmRNIYGIKPGDVW---WAASDV--GWV--- 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 239 hVGgigmlHLRDVY----LGCQeinvsseTILME--PLKWLD----W--IDHYR-ASVTWAPNfAFGLVTDFAEEIKD-R 304
Cdd:cd05967 285 -VG-----HSYIVYgpllHGAT-------TVLYEgkPVGTPDpgafWrvIEKYQvNALFTAPT-AIRAIRKEDPDGKYiK 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 305 KWDLSSMRYMLNGGEamvaKVGRRILELLEPH-GLPadaIRPAWGMSETSSGVI-----FSHEFTRAGTSdddhfveiGS 378
Cdd:cd05967 351 KYDLSSLRTLFLAGE----RLDPPTLEWAENTlGVP---VIDHWWQTETGWPITanpvgLEPLPIKAGSP--------GK 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 379 PIPGFSMRIVNDHNELVEEGEIGRFQVSGL---SVTSGYYQRPDL-NESVFTED-GWFETGDLGFL-RNGRLTITGRTKD 452
Cdd:cd05967 416 PVPGYQVQVLDEDGEPVGPNELGNIVIKLPlppGCLLTLWKNDERfKKLYLSKFpGYYDTGDAGYKdEDGYLFIMGRTDD 495
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 453 AIIINGINYYSHAIESAVEELSEIetsytAACAVRLGQNSTD-QLAIFFV---TSAKLNDEQmsqLLRNIQSHVSQVIG- 527
Cdd:cd05967 496 VINVAGHRLSTGEMEESVLSHPAV-----AECAVVGVRDELKgQVPLGLVvlkEGVKITAEE---LEKELVALVREQIGp 567
|
570 580 590
....*....|....*....|....*....|....*.
gi 1776025254 528 -VTPEYLLPVQKeeIPKTAIGKIQRTQLKtSFENGE 562
Cdd:cd05967 568 vAAFRLVIFVKR--LPKTRSGKILRRTLR-KIADGE 600
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
1660-1719 |
2.65e-13 |
|
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.
Pssm-ID: 425746 [Multi-domain] Cd Length: 62 Bit Score: 67.59 E-value: 2.65e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1776025254 1660 DTVFTIWQEVLK--TSDIEWDDGFFDVGGDSLLAVTVADRIKHELSCEFSVTDLFEYSTIKN 1719
Cdd:pfam00550 1 ERLRELLAEVLGvpAEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLAE 62
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
186-548 |
2.66e-13 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 76.39 E-value: 2.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 186 PEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDHVGGIGMLHLRDVYLGcqeINVSSETI 265
Cdd:PRK06334 182 PEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLPPFHAYGFNSCTLFPLLSG---VPVVFAYN 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 266 LMEPLKWLDWIDHYRASVTWAPNFAFGLVTDFAeeiKDRKWDLSSMRYMLNGGEAMVAKVGRRILELlephgLPADAIRP 345
Cdd:PRK06334 259 PLYPKKIVEMIDEAKVTFLGSTPVFFDYILKTA---KKQESCLPSLRFVVIGGDAFKDSLYQEALKT-----FPHIQLRQ 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 346 AWGMSETSSGVIFSHEftragtSDDDHFVEIGSPIPGFSMRIVNDHNEL-VEEGEIGRFQVSGLSVTSGYYQRpDLNESV 424
Cdd:PRK06334 331 GYGTTECSPVITINTV------NSPKHESCVGMPIRGMDVLIVSEETKVpVSSGETGLVLTRGTSLFSGYLGE-DFGQGF 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 425 FTEDG--WFETGDLGFL-RNGRLTITGRTKDAIIINGINYYSHAIESA-VEELSEIETSYTAACAVRLGQNSTDQLAIFF 500
Cdd:PRK06334 404 VELGGetWYVTGDLGYVdRHGELFLKGRLSRFVKIGAEMVSLEALESIlMEGFGQNAADHAGPLVVCGLPGEKVRLCLFT 483
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1776025254 501 VTSAKLNdeQMSQLLRNIQShvSQVIGVTPEYllpvQKEEIPKTAIGK 548
Cdd:PRK06334 484 TFPTSIS--EVNDILKNSKT--SSILKISYHH----QVESIPMLGTGK 523
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
1151-1330 |
3.02e-13 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 76.32 E-value: 3.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1151 PYITFHELFEQQAKKTPDRAAVSY-------EGQT--LTYRELDERSTQLAIYLQAHGVGPDRLAgIYVDRSLDMLVGLL 1221
Cdd:PRK12476 32 PGTTLISLIERNIANVGDTVAYRYldhshsaAGCAveLTWTQLGVRLRAVGARLQQVAGPGDRVA-ILAPQGIDYVAGFF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1222 AILKAGGAYVPL-DPSYP--AERLEYMLEDSEVFITLTTS-------ELVNTLSWNGVTTALLdqdWDEIAQTASDRKVL 1291
Cdd:PRK12476 111 AAIKAGTIAVPLfAPELPghAERLDTALRDAEPTVVLTTTaaaeaveGFLRNLPRLRRPRVIA---IDAIPDSAGESFVP 187
|
170 180 190
....*....|....*....|....*....|....*....
gi 1776025254 1292 TRTVTpENLAYVIYTSGSTGKPKGVMIPHKALTNFLVSM 1330
Cdd:PRK12476 188 VELDT-DDVSHLQYTSGSTRPPVGVEITHRAVGTNLVQM 225
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
1305-1639 |
3.11e-13 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 76.42 E-value: 3.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1305 YTSGSTGKPKGVMIPHK-----ALTNFLV-SMGETPGLTAEDKMLAVTTYCFDIAAlelflplikGAHC--YICQTEHTk 1376
Cdd:PLN02479 202 YTSGTTASPKGVVLHHRgaylmALSNALIwGMNEGAVYLWTLPMFHCNGWCFTWTL---------AALCgtNICLRQVT- 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1377 dVEKLKRDIRTIKPTVMQATPATWKMLFYSGWENE-----ENVKILCGGEALPETLKRYFLDTGSEAWNMFGPTET---- 1447
Cdd:PLN02479 272 -AKAIYSAIANYGVTHFCAAPVVLNTIVNAPKSETilplpRVVHVMTAGAAPPPSVLFAMSEKGFRVTHTYGLSETygps 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1448 TI------WSAVQRINDECSRATIG-RPIANTQIYITDSQ-LAPVPA--GVPGELCIAGDGVAKGYYKKEELTDSRFidn 1517
Cdd:PLN02479 351 TVcawkpeWDSLPPEEQARLNARQGvRYIGLEGLDVVDTKtMKPVPAdgKTMGEIVMRGNMVMKGYLKNPKANEEAF--- 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1518 pfepGSKLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMDNL-----AAYYTAK- 1591
Cdd:PLN02479 428 ----ANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERwgespCAFVTLKp 503
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1776025254 1592 ---HANASLTARELRHFVKNALPAYMVPSYFIqLDHMPLTPNGKIDRNSLK 1639
Cdd:PLN02479 504 gvdKSDEAALAEDIMKFCRERLPAYWVPKSVV-FGPLPKTATGKIQKHVLR 553
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
1303-1634 |
3.12e-13 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 74.26 E-value: 3.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1303 VIYTSGSTGKPKGVMIPHKALTNFLVSMGETPGLTAEDKMLAVTTYcFDIAALELFLP--LIKGAHCYICQTehtkDVEK 1380
Cdd:cd17636 5 AIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLNSGPL-FHIGTLMFTLAtfHAGGTNVFVRRV----DAEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1381 LKRDIrtikptvmQATPATWKMLFYSGWEneenvKILCGGEALPETLKRYFLDTGSEAWNMFGPTETTIWS--------- 1451
Cdd:cd17636 80 VLELI--------EAERCTHAFLLPPTID-----QIVELNADGLYDLSSLRSSPAAPEWNDMATVDTSPWGrkpggygqt 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1452 -----AVQRINDECSRATIGRPIANTQIYITDSQLAPVPAGVPGELCIAGDGVAKGYYKKEELTDSRFIDNpfepgskLY 1526
Cdd:cd17636 147 evmglATFAALGGGAIGGAGRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTRGG-------WH 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1527 RTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVV--VAD---MDNLAAYYTAKhANASLTARE 1601
Cdd:cd17636 220 HTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVigVPDprwAQSVKAIVVLK-PGASVTEAE 298
|
330 340 350
....*....|....*....|....*....|...
gi 1776025254 1602 LRHFVKNALPAYMVPSYFIQLDHMPLTPNGKID 1634
Cdd:cd17636 299 LIEHCRARIASYKKPKSVEFADALPRTAGGADD 331
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
1561-1632 |
3.17e-13 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 67.57 E-value: 3.17e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1776025254 1561 DIESRLSEHPGILECVVVADMDN-----LAAYYTAKhANASLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGK 1632
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDElkgeaPVAFVVLK-PGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
3117-3178 |
3.22e-13 |
|
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.
Pssm-ID: 425746 [Multi-domain] Cd Length: 62 Bit Score: 67.20 E-value: 3.22e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1776025254 3117 AALIQMVGAILKVNTDDIDVNTELSEYGFDSVTFTVFTNKINEKFQLELTPTIFFEYGSVQS 3178
Cdd:pfam00550 1 ERLRELLAEVLGVPAEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLAE 62
|
|
| adh_short |
pfam00106 |
short chain dehydrogenase; This family contains a wide variety of dehydrogenases. |
4172-4297 |
3.60e-13 |
|
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
Pssm-ID: 395056 [Multi-domain] Cd Length: 195 Bit Score: 71.49 E-value: 3.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4172 VLLITGGTRGIGLLCARHFAEcYGvKKLVLTGReqlppreewarfktsntSLAEKIQAVRELEAKGVQVEMLSLTLSDDA 4251
Cdd:pfam00106 2 VALVTGASSGIGRAIAKRLAK-EG-AKVVLVDR-----------------SEEKLEAVAKELGALGGKALFIQGDVTDRA 62
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1776025254 4252 QVEQTLQHIKRTLGPIGGVIHCAGLTDMDTLAFIrkTSDDIQRVME 4297
Cdd:pfam00106 63 QVKALVEQAVERLGRLDILVNNAGITGLGPFSEL--SDEDWERVID 106
|
|
| fabG |
PRK05653 |
3-oxoacyl-ACP reductase FabG; |
4172-4341 |
4.87e-13 |
|
3-oxoacyl-ACP reductase FabG;
Pssm-ID: 235546 [Multi-domain] Cd Length: 246 Bit Score: 72.11 E-value: 4.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4172 VLLITGGTRGIGLLCARHFAEcYGVKkLVLTGReqlppreewarfktsNTSLAEKIQAvrELEAKGVQVEMLSLTLSDDA 4251
Cdd:PRK05653 7 TALVTGASRGIGRAIALRLAA-DGAK-VVIYDS---------------NEEAAEALAA--ELRAAGGEARVLVFDVSDEA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4252 QVEQTLQHIKRTLGPIGGVIHCAGLTDMDtlAFIRKTSDDIQRVMEpkVSgLTTLYrHVCNEPLQFF--------VLFSS 4323
Cdd:PRK05653 68 AVRALIEAAVEAFGALDILVNNAGITRDA--LLPRMSEEDWDRVID--VN-LTGTF-NVVRAALPPMikarygriVNISS 141
|
170
....*....|....*...
gi 1776025254 4324 VSAIIPelSAGQADYAMA 4341
Cdd:PRK05653 142 VSGVTG--NPGQTNYSAA 157
|
|
| PaaK |
cd05913 |
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ... |
195-551 |
5.71e-13 |
|
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic degradation pathway, by converting phenylacetic acid (PA) into phenylacetyl-CoA (PA-CoA). Phenylacetate-CoA ligase has been found in proteobacteria as well as gram positive prokaryotes. The enzyme is specifically induced after aerobic growth in a chemically defined medium containing PA or phenylalanine (Phe) as the sole carbon source. PaaKs are members of the adenylate-forming enzyme (AFE) family. However, sequence comparison reveals divergent features of PaaK with respect to the superfamily, including a novel N-terminal sequence.
Pssm-ID: 341239 [Multi-domain] Cd Length: 425 Bit Score: 74.58 E-value: 5.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 195 TSGSTGTPKAVMLNHRNIMS---MVKGIIQMQGFTREDI---TFNWMPFdhVGGIGmLHLRDVYLGCQEINVS---SEti 265
Cdd:cd05913 86 SSGTTGKPTVVGYTKNDLDVwaeLVARCLDAAGVTPGDRvqnAYGYGLF--TGGLG-FHYGAERLGALVIPAGggnTE-- 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 266 lmeplKWLDWIDHYRASVTWA-PNFAFGLvtdfAEEIKDRKWDL--SSMRYMLNGGEAMVAKVGRRILELL-----EPHG 337
Cdd:cd05913 161 -----RQLQLIKDFGPTVLCCtPSYALYL----AEEAEEEGIDPreLSLKVGIFGAEPWTEEMRKRIERRLgikayDIYG 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 338 LPADaIRPAWGMSETSSGVIFSHEftragtsddDHFVEIgspipgfsmrIVNDH-NELVEEGEIGRFQVSGLSVTSGYYQ 416
Cdd:cd05913 232 LTEI-IGPGVAFECEEKDGLHIWE---------DHFIPE----------IIDPEtGEPVPPGEVGELVFTTLTKEAMPLI 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 417 RpdlnesvftedgwFETGDLGFL-----RNGRLT-----ITGRTKDAIIINGINYYSHAIESAVEELSEIETSYtaacav 486
Cdd:cd05913 292 R-------------YRTRDITRLlpgpcPCGRTHrridrITGRSDDMLIIRGVNVFPSQIEDVLLKIPGLGPHY------ 352
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1776025254 487 RL---GQNSTDQLAIFF-VTSAKLNDEQMSQLLRNIQSHVSQVIGVTPEYLLpVQKEEIPKTaIGKIQR 551
Cdd:cd05913 353 QLiltRQEHLDELTIKVeVRPEADDDEKLEALKQRLERHIKSVLGVTVEVEL-VEPGSLPRS-EGKAKR 419
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
191-554 |
6.17e-13 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 75.03 E-value: 6.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 191 LLLLTSGSTGTPKAVMLNHRnIMSMVKGIIQMQGFTR----EDITFNwMPFDHVGGIGMLHLrDVYLGCQEI---NVSSE 263
Cdd:PRK13383 178 IVLLTSGTTGKPKGVPRAPQ-LRSAVGVWVTILDRTRlrtgSRISVA-MPMFHGLGLGMLML-TIALGGTVLthrHFDAE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 264 TILMEPlkwldwiDHYRASVTWAPNFAFGLVTDFAEEIKDRKwDLSSMRYMLNGGEAMVAKVGRRILELLephglpADAI 343
Cdd:PRK13383 255 AALAQA-------SLHRADAFTAVPVVLARILELPPRVRARN-PLPQLRVVMSSGDRLDPTLGQRFMDTY------GDIL 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 344 RPAWGMSETSSGVIFSHEFTRagtsddDHFVEIGSPIPGFSMRIVNDHNELVEEGEIGRFQVSGLSVTSGYYQRPdlNES 423
Cdd:PRK13383 321 YNGYGSTEVGIGALATPADLR------DAPETVGKPVAGCPVRILDRNNRPVGPRVTGRIFVGGELAGTRYTDGG--GKA 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 424 VFteDGWFETGDLGFLRN-GRLTITGRTKDAIIINGINYYSHAIESAVEELSEI-ETSYTAACAVRLGQnstdQLAIFFV 501
Cdd:PRK13383 393 VV--DGMTSTGDMGYLDNaGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVaDNAVIGVPDERFGH----RLAAFVV 466
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1776025254 502 T--SAKLNDEQMSQLLRNIQSHVSQvigvtPEYLLPVQkeEIPKTAIGKIQRTQL 554
Cdd:PRK13383 467 LhpGSGVDAAQLRDYLKDRVSRFEQ-----PRDINIVS--SIPRNPTGKVLRKEL 514
|
|
| PLN02787 |
PLN02787 |
3-oxoacyl-[acyl-carrier-protein] synthase II |
4504-4929 |
8.10e-13 |
|
3-oxoacyl-[acyl-carrier-protein] synthase II
Pssm-ID: 215421 [Multi-domain] Cd Length: 540 Bit Score: 75.02 E-value: 8.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4504 RINRKLEAALDPSILYEYPTIQRFTDWLIGSYSERLSALFGGRISDASAPLENKIEVEAPVPAKDRALTPQIQAPAILSP 4583
Cdd:PLN02787 45 KRRKCSSASGSASILVTSCLAFGPCTHYNSSGGNALSSLFGSNSVSLNRNQRRRNRAARSGKAMAVAVQPEKEVETKKKP 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4584 DSHAEGIAVVGLSCRFPGAETLESYWSLLSEGRSSIGPIpaERWGCKT--PYYAGVIDGVS---YFDPDFfllheedVRA 4658
Cdd:PLN02787 125 LTKQRRVVVTGMGVVSPLGHDPDVFYNNLLEGVSGISEI--ERFDCSQfpTRIAGEIKSFStdgWVAPKL-------SKR 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4659 MDPQALLVLEECLKLLYHAGYTPE---EIKGKPVGVYIG-GRSQHKPDEDSLDHAK------NPI------VTVGQNYLA 4722
Cdd:PLN02787 196 MDKFMLYLLTAGKKALADGGITEDvmkELDKTKCGVLIGsAMGGMKVFNDAIEALRisyrkmNPFcvpfatTNMGSAMLA 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4723 ANLSQFfdvrGPSVVVDTAC-SSALVGMNMAIQALRG-------GDIQSAIVGgVSLLSSDASHRLFDRRGILSKHSsfH 4794
Cdd:PLN02787 276 MDLGWM----GPNYSISTACaTSNFCILNAANHIIRGeadvmlcGGSDAAIIP-IGLGGFVACRALSQRNDDPTKAS--R 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4795 VFDERADGVVLGEGVGMVMLKTVKQALEDGDTIYAVVKAASVNNDGRTAGPATPNLEAQKEVMKDALFKSGKKPEDISYL 4874
Cdd:PLN02787 349 PWDMNRDGFVMGEGAGVLLLEELEHAKKRGANIYAEFLGGSFTCDAYHMTEPHPEGAGVILCIEKALAQSGVSKEDVNYI 428
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1776025254 4875 EANGSGSIVTDLLELKAIQSVYrsGHSSPLSLGSIKPNIGHPLCAEGIASFIKVV 4929
Cdd:PLN02787 429 NAHATSTKAGDLKEYQALMRCF--GQNPELRVNSTKSMIGHLLGAAGAVEAIATV 481
|
|
| fabG |
PRK05557 |
3-ketoacyl-(acyl-carrier-protein) reductase; Validated |
4172-4341 |
1.14e-12 |
|
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
Pssm-ID: 235500 [Multi-domain] Cd Length: 248 Bit Score: 71.38 E-value: 1.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4172 VLLITGGTRGIGLLCARHFAECyGVKkLVLTGReqlppreewarfktSNTSLAEKIqaVRELEAKGVQVEMLSLTLSDDA 4251
Cdd:PRK05557 7 VALVTGASRGIGRAIAERLAAQ-GAN-VVINYA--------------SSEAGAEAL--VAEIGALGGKALAVQGDVSDAE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4252 QVEQTLQHIKRTLGPIGGVIHCAGLTDmDTLaFIRKTSDDIQRVMEPKVSGLTTLYRHVC------------Neplqffv 4319
Cdd:PRK05557 69 SVERAVDEAKAEFGGVDILVNNAGITR-DNL-LMRMKEEDWDRVIDTNLTGVFNLTKAVArpmmkqrsgriiN------- 139
|
170 180
....*....|....*....|..
gi 1776025254 4320 lFSSVSAIIPelSAGQADYAMA 4341
Cdd:PRK05557 140 -ISSVVGLMG--NPGQANYAAS 158
|
|
| fabG |
PRK05653 |
3-oxoacyl-ACP reductase FabG; |
2852-3028 |
1.16e-12 |
|
3-oxoacyl-ACP reductase FabG;
Pssm-ID: 235546 [Multi-domain] Cd Length: 246 Bit Score: 70.96 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2852 LITGGAGSLGLLFAKEIAnRTGrSTIVLTGRSVlsEDKENELEALRSIGAEVVYREADVSDQHAVHHLFEEIKERYGTLN 2931
Cdd:PRK05653 9 LVTGASRGIGRAIALRLA-ADG-AKVVIYDSNE--EAAEALAAELRAAGGEARVLVFDVSDEAAVRALIEAAVEAFGALD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2932 GIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSGllhvdecskdfpldFF------------------IFFSSVSGCLGNAG 2993
Cdd:PRK05653 85 ILVNNAGITRDALLPRMSEEDWDRVIDVNLTG--------------TFnvvraalppmikarygriVNISSVSGVTGNPG 150
|
170 180 190
....*....|....*....|....*....|....*
gi 1776025254 2994 QADYAAANSFMDAFAeyrRSLAASKKRFGstISFN 3028
Cdd:PRK05653 151 QTNYSAAKAGVIGFT---KALALELASRG--ITVN 180
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
1160-1633 |
1.18e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 74.34 E-value: 1.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1160 EQQAKKTPDRAAV--SYEGQTLTYRELDERSTQLAIYLQAHGVGP-DRLAgIYVDRSLDMLVGLLAILKAGGAYVPLDPS 1236
Cdd:PRK13391 4 GIHAQTTPDKPAVimASTGEVVTYRELDERSNRLAHLFRSLGLKRgDHVA-IFMENNLRYLEVCWAAERSGLYYTCVNSH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1237 YPAERLEYMLEDSEVFItlttseLVNTLSWNGVTTALLDQ------DWDEIAQTASDRKVLTRTVTPENLAYVI------ 1304
Cdd:PRK13391 83 LTPAEAAYIVDDSGARA------LITSAAKLDVARALLKQcpgvrhRLVLDGDGELEGFVGYAEAVAGLPATPIadeslg 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1305 ----YTSGSTGKPKGVM--IPHKALtnflvsmGETPGLTAEDKMLavttycFDIAALELFL---PLIKGAHCYICQT--- 1372
Cdd:PRK13391 157 tdmlYSSGTTGRPKGIKrpLPEQPP-------DTPLPLTAFLQRL------WGFRSDMVYLspaPLYHSAPQRAVMLvir 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1373 --------EHTkDVEKLKRDIRTIKPTVMQATPATW-KMLfysgweneenvkilcggeALP-ETLKRYFLDT-------- 1434
Cdd:PRK13391 224 lggtvivmEHF-DAEQYLALIEEYGVTHTQLVPTMFsRML------------------KLPeEVRDKYDLSSlevaihaa 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1435 ---------------GSEAWNMFGPTETTIWSAVQRINDECSRATIGRPIANTqIYITDSQLAPVPAGVPGELCIAGdGV 1499
Cdd:PRK13391 285 apcppqvkeqmidwwGPIIHEYYAATEGLGFTACDSEEWLAHPGTVGRAMFGD-LHILDDDGAELPPGEPGTIWFEG-GR 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1500 AKGYYKKEELT-DSRfidnpfEPGSKLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGIL----- 1573
Cdd:PRK13391 363 PFEYLNDPAKTaEAR------HPDGTWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVAdaavf 436
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1574 --------ECV--VVADMDNLAayytakhANASLtARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKI 1633
Cdd:PRK13391 437 gvpnedlgEEVkaVVQPVDGVD-------PGPAL-AAELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKL 498
|
|
| fabG |
PRK08217 |
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional |
2850-3000 |
1.27e-12 |
|
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
Pssm-ID: 181297 [Multi-domain] Cd Length: 253 Bit Score: 71.14 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGLLFAKEIANRTGRSTIVltgrSVLSEDKENELEALRSIGAEVVYREADVSDQHAVHHLFEEIKERYGT 2929
Cdd:PRK08217 7 VIVITGGAQGLGRAMAEYLAQKGAKLALI----DLNQEKLEEAVAECGALGTEVRGYAANVTDEEDVEATFAQIAEDFGQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2930 LNGIIHGAG--------SIKDHFIIHKTN-EEFQEVLQPKVSGL--------LHVDECSKDfplDFFIFFSSVSGClGNA 2992
Cdd:PRK08217 83 LNGLINNAGilrdgllvKAKDGKVTSKMSlEQFQSVIDVNLTGVflcgreaaAKMIESGSK---GVIINISSIARA-GNM 158
|
....*...
gi 1776025254 2993 GQADYAAA 3000
Cdd:PRK08217 159 GQTNYSAS 166
|
|
| PKS_PP |
smart00823 |
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ... |
3221-3281 |
1.28e-12 |
|
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.
Pssm-ID: 214834 [Multi-domain] Cd Length: 86 Bit Score: 66.50 E-value: 1.28e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1776025254 3221 VSAILKVNSED-IDVNTELSEYGFDSVTFTVFTNKINEEFQLELTPTIFFEYGSIHSLAEYL 3281
Cdd:smart00823 21 VAAVLGHAAAEaIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHL 82
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
1160-1533 |
1.65e-12 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 74.01 E-value: 1.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1160 EQQAKKTPDRAAVSYEG-----QTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLD 1234
Cdd:cd05921 2 AHWARQAPDRTWLAEREgnggwRRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1235 PSYPA-----ERLEYMLE----------DSEVF-------ITLTTSELVNTLSWNGVTTALLDQDWDEIAQTASDRkvLT 1292
Cdd:cd05921 82 PAYSLmsqdlAKLKHLFEllkpglvfaqDAAPFaralaaiFPLGTPLVVSRNAVAGRGAISFAELAATPPTAAVDA--AF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1293 RTVTPENLAYVIYTSGSTGKPKGVMIPHKALTNFLVSMGETPGLTAED--KMLAVTTYCFDIAALELF-LPLIKGAHCYI 1369
Cdd:cd05921 160 AAVGPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEppVLVDWLPWNHTFGGNHNFnLVLYNGGTLYI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1370 CQTEHT-KDVEKLKRDIRTIKPTVMQATPATWKMLFySGWENEE--------NVKILC-GGEALP----ETLKRYFLDTG 1435
Cdd:cd05921 240 DDGKPMpGGFEETLRNLREISPTVYFNVPAGWEMLV-AALEKDEalrrrffkRLKLMFyAGAGLSqdvwDRLQALAVATV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1436 SEAWNM---FGPTET------TIWSAvqrindecSRA-TIGRPIANTQIYItdsqlapVPAGVPGELCIAGDGVAKGYYK 1505
Cdd:cd05921 319 GERIPMmagLGATETaptatfTHWPT--------ERSgLIGLPAPGTELKL-------VPSGGKYEVRVKGPNVTPGYWR 383
|
410 420
....*....|....*....|....*...
gi 1776025254 1506 KEELTDSRFIDNPFepgsklYRTGDMAR 1533
Cdd:cd05921 384 QPELTAQAFDEEGF------YCLGDAAK 405
|
|
| AcpP |
COG0236 |
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ... |
1654-1728 |
1.98e-12 |
|
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440006 [Multi-domain] Cd Length: 80 Bit Score: 65.65 E-value: 1.98e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1776025254 1654 SPKNIQDTVFTIWQEVLK--TSDIEWDDGFF-DVGGDSLLAVTVADRIKHELSCEFSVTDLFEYSTIKNISQYITEQR 1728
Cdd:COG0236 2 PREELEERLAEIIAEVLGvdPEEITPDDSFFeDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEEKL 79
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
1174-1740 |
2.33e-12 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 73.91 E-value: 2.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1174 YEGQTLTYRELDERSTQLAIYLQAHGVGP-DRLAGIYVDrSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLEDSEVF 1252
Cdd:PRK06060 26 YAADVVTHGQIHDGAARLGEVLRNRGLSSgDRVLLCLPD-SPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1253 ITLTTSELVNTLSWNGVTTALldqdwDEIAQTASDRKVLTRTVTPENLAYVIYTSGSTGKPKGVMIPHKALTNFLVSM-G 1331
Cdd:PRK06060 105 LVVTSDALRDRFQPSRVAEAA-----ELMSEAARVAPGGYEPMGGDALAYATYTSGTTGPPKAAIHRHADPLTFVDAMcR 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1332 ETPGLTAEDKMLAVTTYCFDIA-ALELFLPLIKGAHCYICQTEHTKDVEKLKRdiRTIKPTVMQATPATW-KMLFYSGWE 1409
Cdd:PRK06060 180 KALRLTPEDTGLCSARMYFAYGlGNSVWFPLATGGSAVINSAPVTPEAAAILS--ARFGPSVLYGVPNFFaRVIDSCSPD 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1410 NEENVK-ILCGGEAL----PETLKRYFldTGSEAWNMFGPTETTiWSAVQRINDECSRATIGRPIANTQIYITDSQLAPV 1484
Cdd:PRK06060 258 SFRSLRcVVSAGEALelglAERLMEFF--GGIPILDGIGSTEVG-QTFVSNRVDEWRLGTLGRVLPPYEIRVVAPDGTTA 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1485 PAGVPGELCIAGDGVAKGYYKKEE--LTDSRFIDnpfepgsklyrTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDI 1562
Cdd:PRK06060 335 GPGVEGDLWVRGPAIAKGYWNRPDspVANEGWLD-----------TRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREV 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1563 ESRLSEHPGILECVVVA-----DMDNLAAYYTAKHAnASLTARELRHFVK---NALPAYMVPSYFIQLDHMPLTPNGKID 1634
Cdd:PRK06060 404 ERLIIEDEAVAEAAVVAvrestGASTLQAFLVATSG-ATIDGSVMRDLHRgllNRLSAFKVPHRFAVVDRLPRTPNGKLV 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1635 RNSLK----------------------NID-------------LSGEQLKQR-----QTSPKNIQDTVFTIWQEVLKTSD 1674
Cdd:PRK06060 483 RGALRkqsptkpiwelsltepgsgvraQRDdlsasnmtiaggnDGGATLRERlvalrQERQRLVVDAVCAEAAKMLGEPD 562
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1776025254 1675 ---IEWDDGFFDVGGDSLLAVTVADRIKHELSCEFSVTDLFEYSTIKNISQYITEQRMGnaSDHMPTDP 1740
Cdd:PRK06060 563 pwsVDQDLAFSELGFDSQMTVTLCKRLAAVTGLRLPETVGWDYGSISGLAQYLEAELAG--GHGRLKSA 629
|
|
| PRK08439 |
PRK08439 |
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed |
4638-4931 |
2.62e-12 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
Pssm-ID: 236265 [Multi-domain] Cd Length: 406 Bit Score: 72.46 E-value: 2.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4638 IDGVSYFDPDFF---------------LLHEEDVRAMDPQALLVLEECLKLLYHAGYTPEEIKGKPVGVY----IGGRSQ 4698
Cdd:PRK08439 33 IKKITLFDASDFpvqiageitdfdpteVMDPKEVKKADRFIQLGLKAAREAMKDAGFLPEELDAERFGVSsasgIGGLPN 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4699 HKpdedsldhaKNPIV--TVGQ-------------NYLAANLSQFFDVRGPSVVVDTACSSALVGMNMAIQ--ALRGGD- 4760
Cdd:PRK08439 113 IE---------KNSIIcfEKGPrkispffipsalvNMLGGFISIEHGLKGPNLSSVTACAAGTHAIIEAVKtiMLGGADk 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4761 -----IQSAI----VGGVsllssdASHRLFDRRGILSKHSSfHVFDERADGVVLGEGVGMVMLKTVKQALEDGDTIYAVV 4831
Cdd:PRK08439 184 mlvvgAESAIcpvgIGGF------AAMKALSTRNDDPKKAS-RPFDKDRDGFVMGEGAGALVLEEYESAKKRGAKIYAEI 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4832 kaASVNNDGRTAGPATPNLEAQKEVMKDALfKSGKKPEdISYLEANGSGSIVTDLLELKAIQSVYRSGHSSPLsLGSIKP 4911
Cdd:PRK08439 257 --IGFGESGDANHITSPAPEGPLRAMKAAL-EMAGNPK-IDYINAHGTSTPYNDKNETAALKELFGSKEKVPP-VSSTKG 331
|
330 340
....*....|....*....|.
gi 1776025254 4912 NIGHPLCAEG-IASFIKVVLM 4931
Cdd:PRK08439 332 QIGHCLGAAGaIEAVISIMAM 352
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
1153-1640 |
2.89e-12 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 73.09 E-value: 2.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1153 ITFHELFEQQAKKTPDRAAV--SYEGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAY 1230
Cdd:PLN02330 28 LTLPDFVLQDAELYADKVAFveAVTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVF 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1231 VPLDPSYPAERLEYMLEDSEVFITLTTSELVNTLSWNGVTTALLDQ-------DWDEIAQtASDR---KVLTRTVTPENL 1300
Cdd:PLN02330 108 SGANPTALESEIKKQAEAAGAKLIVTNDTNYGKVKGLGLPVIVLGEekiegavNWKELLE-AADRagdTSDNEEILQTDL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1301 AYVIYTSGSTGKPKGVMIPHKALTNFLVS---------MGE--TPGLTAEDKMLAVTTYCFD----------IAALEL-- 1357
Cdd:PLN02330 187 CALPFSSGTTGISKGVMLTHRNLVANLCSslfsvgpemIGQvvTLGLIPFFHIYGITGICCAtlrnkgkvvvMSRFELrt 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1358 -----------FLPLIKGAHCYICQTEHTK--DVEKLKrdirtIKPTVMQATPATWKMLfySGWENEenvkilcggeaLP 1424
Cdd:PLN02330 267 flnalitqevsFAPIVPPIILNLVKNPIVEefDLSKLK-----LQAIMTAAAPLAPELL--TAFEAK-----------FP 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1425 etlkryfldtGSEAWNMFGPTETTIWSAVQRINDE----CSRATIGRPIANTQIYITDSQLA-PVPAGVPGELCIAGDGV 1499
Cdd:PLN02330 329 ----------GVQVQEAYGLTEHSCITLTHGDPEKghgiAKKNSVGFILPNLEVKFIDPDTGrSLPKNTPGELCVRSQCV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1500 AKGYYKKEELTDsrfidnpfepgsklyRTGDMARWLPGGRIEYIG---------RIDNQVKIRGFRIELGDIESRLSEHP 1570
Cdd:PLN02330 399 MQGYYNNKEETD---------------RTIDEDGWLHTGDIGYIDddgdifivdRIKELIKYKGFQVAPAELEAILLTHP 463
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1776025254 1571 GILECVVVADMDNLAAYYTAKHANASLTARE----LRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLKN 1640
Cdd:PLN02330 464 SVEDAAVVPLPDEEAGEIPAACVVINPKAKEseedILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKE 537
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
3219-3274 |
4.50e-12 |
|
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.
Pssm-ID: 425746 [Multi-domain] Cd Length: 62 Bit Score: 63.74 E-value: 4.50e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1776025254 3219 NMVSAILKVNSEDIDVNTELSEYGFDSVTFTVFTNKINEEFQLELTPTIFFEYGSI 3274
Cdd:pfam00550 5 ELLAEVLGVPAEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTL 60
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
159-555 |
5.00e-12 |
|
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.
Pssm-ID: 341274 [Multi-domain] Cd Length: 537 Bit Score: 72.14 E-value: 5.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 159 QGLEGFRAIIVEDLLSAEADTDWHQSSPEDLALLLLTSGSTGTPKavMLNHRNIMSMvkGIIQMQGFtreditfnWMPFD 238
Cdd:cd05970 157 EGWIDFRKLIKNASPDFERPTANSYPCGEDILLVYFSSGTTGMPK--MVEHDFTYPL--GHIVTAKY--------WQNVR 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 239 HVGgigmLHLR------------DVY----LGCQEINVSSEtiLMEPLKWLDWIDHYRASVTWAPN--FAFGLVTDFAee 300
Cdd:cd05970 225 EGG----LHLTvadtgwgkavwgKIYgqwiAGAAVFVYDYD--KFDPKALLEKLSKYGVTTFCAPPtiYRFLIREDLS-- 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 301 ikdrKWDLSSMRYMLNGGEAMVAKVGRRILELLephGLpadAIRPAWGMSETSSGV-IFSHEFTRAGTsdddhfveIGSP 379
Cdd:cd05970 297 ----RYDLSSLRYCTTAGEALNPEVFNTFKEKT---GI---KLMEGFGQTETTLTIaTFPWMEPKPGS--------MGKP 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 380 IPGFSMRIVnDHN----ELVEEGEIGRFQVSGLSVT--SGYYQRPDLNESVFtEDGWFETGDLGFL-RNGRLTITGRTKD 452
Cdd:cd05970 359 APGYEIDLI-DREgrscEAGEEGEIVIRTSKGKPVGlfGGYYKDAEKTAEVW-HDGYYHTGDAAWMdEDGYLWFVGRTDD 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 453 AIIINGINYYSHAIESA-VEELSEIETSYTAACAVRLGQnstdQLAIFFVTSAklnDEQMSQLLRN-IQSHVSQvigVTP 530
Cdd:cd05970 437 LIKSSGYRIGPFEVESAlIQHPAVLECAVTGVPDPIRGQ----VVKATIVLAK---GYEPSEELKKeLQDHVKK---VTA 506
|
410 420
....*....|....*....|....*...
gi 1776025254 531 EYLLPVQKE---EIPKTAIGKIQRTQLK 555
Cdd:cd05970 507 PYKYPRIVEfvdELPKTISGKIRRVEIR 534
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
1168-1641 |
5.03e-12 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 72.62 E-value: 5.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1168 DRAAVSYEGQ------TLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAER 1241
Cdd:PLN02654 104 DKIAIYWEGNepgfdaSLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAES 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1242 LEYMLEDSEVFITLTTSEL---VNTLSWNGVTTALLDQDWDE-----IAQTASDRKVLTRTVTP---------------- 1297
Cdd:PLN02654 184 LAQRIVDCKPKVVITCNAVkrgPKTINLKDIVDAALDESAKNgvsvgICLTYENQLAMKREDTKwqegrdvwwqdvvpny 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1298 -----------ENLAYVIYTSGSTGKPKGVMipHK-------ALTNFLVSMGETPG----LTAEDKMLAVTTYCfdiaal 1355
Cdd:PLN02654 264 ptkcevewvdaEDPLFLLYTSGSTGKPKGVL--HTtggymvyTATTFKYAFDYKPTdvywCTADCGWITGHSYV------ 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1356 eLFLPLIKGAHCYICQ-TEHTKDVEKLKRDIRTIKPTVMQATPATWKMLFYSGWE-----NEENVKILCG-GEALPETLK 1428
Cdd:PLN02654 336 -TYGPMLNGATVLVFEgAPNYPDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDEyvtrhSRKSLRVLGSvGEPINPSAW 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1429 RYFLDTG-------SEAWnmfGPTET---TIWSAVQRINDECSRATIgrPIANTQIYITDSQLAPVPAGVPGELCIAGD- 1497
Cdd:PLN02654 415 RWFFNVVgdsrcpiSDTW---WQTETggfMITPLPGAWPQKPGSATF--PFFGVQPVIVDEKGKEIEGECSGYLCVKKSw 489
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1498 -GVAKGYYKKEEltdsRFIDNPFEPGSKLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECV 1576
Cdd:PLN02654 490 pGAFRTLYGDHE----RYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAA 565
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1776025254 1577 VVA---DMDNLAAYYTAKHANASLTARELRH----FVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLKNI 1641
Cdd:PLN02654 566 VVGiehEVKGQGIYAFVTLVEGVPYSEELRKslilTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKI 637
|
|
| AcpP |
COG0236 |
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ... |
592-666 |
5.73e-12 |
|
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440006 [Multi-domain] Cd Length: 80 Bit Score: 64.10 E-value: 5.73e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1776025254 592 REEIQEHLLTCLTEELHVSRDWVEPNAN-IQSLGVNSIKMMKLIRSIEKNYHIKLTAREIHQYPTIERLASYLSEH 666
Cdd:COG0236 3 REELEERLAEIIAEVLGVDPEEITPDDSfFEDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEEK 78
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
49-516 |
5.73e-12 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 72.44 E-value: 5.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 49 IYLQPDgtevyqSYRRLWDDGL---RIVKGLRQSGlkakQSVILQLGDNSQLLPAFWGCVLTGVVPAPLavppTYaesSS 125
Cdd:PRK08043 227 VNFTPD------SYRKLLKKTLfvgRILEKYSVEG----ERIGLMLPNATISAAVIFGASLRRRIPAMM----NY---TA 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 126 GTQKLKDAWTLLDKPAVITDRGMHQEMLDWAKEQGLEGFRAIIVEDLLSAEADTD-----WH---------QSSPEDLAL 191
Cdd:PRK08043 290 GVKGLTSAITAAEIKTIFTSRQFLDKGKLWHLPEQLTQVRWVYLEDLKDDVTTADklwifAHllmprlaqvKQQPEDAAL 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 192 LLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDHVGGIGMLHLRDVYLGcqeinvsSETILM-EPL 270
Cdd:PRK08043 370 ILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRFMSALPLFHSFGLTVGLFTPLLTG-------AEVFLYpSPL 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 271 kwldwidHYR----------ASVTWAPNFAFGLVTDFAEeikdrKWDLSSMRYMLNGGEAMVA--------KVGRRILEl 332
Cdd:PRK08043 443 -------HYRivpelvydrnCTVLFGTSTFLGNYARFAN-----PYDFARLRYVVAGAEKLQEstkqlwqdKFGLRILE- 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 333 lephglpadairpAWGMSETSSGV-IFSHEFTRAGTsdddhfveIGSPIPGFSMRIVNDHNelVEEGeiGRFQVSGLSVT 411
Cdd:PRK08043 510 -------------GYGVTECAPVVsINVPMAAKPGT--------VGRILPGMDARLLSVPG--IEQG--GRLQLKGPNIM 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 412 SGYY--QRPDL-------NESVFTEDGWFETGDLGFL-RNGRLTITGRTKDAIIINGINYyshAIESaVEELS-EIETSY 480
Cdd:PRK08043 565 NGYLrvEKPGVlevptaeNARGEMERGWYDTGDIVRFdEQGFVQIQGRAKRFAKIAGEMV---SLEM-VEQLAlGVSPDK 640
|
490 500 510
....*....|....*....|....*....|....*.
gi 1776025254 481 TAACAVRLGQNSTDQLaIFFVTSAKLNDEQMSQLLR 516
Cdd:PRK08043 641 QHATAIKSDASKGEAL-VLFTTDSELTREKLQQYAR 675
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
173-452 |
6.26e-12 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 72.46 E-value: 6.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 173 LSAEADTDWHQSSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQ-MQGFTREDITFNWMPFDHV----------- 240
Cdd:PLN02387 236 LGKENPVDPDLPSPNDIAVIMYTSGSTGLPKGVMMTHGNIVATVAGVMTvVPKLGKNDVYLAYLPLAHIlelaaesvmaa 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 241 --GGIGM---LHLRD----VYLGCQ-EINVSSETILMEPLKWLDWI-DHYRASVTWAPNFAFGLVtDFAeeIKDR----- 304
Cdd:PLN02387 316 vgAAIGYgspLTLTDtsnkIKKGTKgDASALKPTLMTAVPAILDRVrDGVRKKVDAKGGLAKKLF-DIA--YKRRlaaie 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 305 -----KWDLSSM------------------RYMLNGGEAMVAKVGRRILELLephGLPadaIRPAWGMSETSSGVIFShE 361
Cdd:PLN02387 393 gswfgAWGLEKLlwdalvfkkiravlggriRFMLSGGAPLSGDTQRFINICL---GAP---IGQGYGLTETCAGATFS-E 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 362 FtragtsDDDHFVEIGSPIPGFSMRIVN--DHNELVEE-----GEIgrfQVSGLSVTSGYYQRPDLNESVFTEDG----W 430
Cdd:PLN02387 466 W------DDTSVGRVGPPLPCCYVKLVSweEGGYLISDkpmprGEI---VIGGPSVTLGYFKNQEKTDEVYKVDErgmrW 536
|
330 340
....*....|....*....|...
gi 1776025254 431 FETGDLG-FLRNGRLTITGRTKD 452
Cdd:PLN02387 537 FYTGDIGqFHPDGCLEIIDRKKD 559
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
170-556 |
7.74e-12 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.
Pssm-ID: 341283 [Multi-domain] Cd Length: 486 Bit Score: 71.56 E-value: 7.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 170 EDLL-SAEADTDWHQSSPEDLALLL-LTSGSTGTPKAVMLNHRNIMSMVKGII---QMQG----------FTREDITFNW 234
Cdd:cd12118 114 EDLLaEGDPDFEWIPPADEWDPIALnYTSGTTGRPKGVVYHHRGAYLNALANIlewEMKQhpvylwtlpmFHCNGWCFPW 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 235 MpfdhVGGIGMLH--LRdvylgcqeiNVSSETILmeplkwlDWIDHYRasVTW---APNfAFGLVTDFAEEIKDRkwdLS 309
Cdd:cd12118 194 T----VAAVGGTNvcLR---------KVDAKAIY-------DLIEKHK--VTHfcgAPT-VLNMLANAPPSDARP---LP 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 310 SMRYMLNGGEAMVAKVgrriLELLEPHGLpadAIRPAWGMSETSsGVIFSHEFTRA--GTSDDDHFVEI---GSPIPGFS 384
Cdd:cd12118 248 HRVHVMTAGAPPPAAV----LAKMEELGF---DVTHVYGLTETY-GPATVCAWKPEwdELPTEERARLKarqGVRYVGLE 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 385 MRIVNDHNELVE---EGE-IGRFQVSGLSVTSGYYQRPDLNESVFtEDGWFETGDLGFLR-NGRLTITGRTKDAIIINGI 459
Cdd:cd12118 320 EVDVLDPETMKPvprDGKtIGEIVFRGNIVMKGYLKNPEATAEAF-RGGWFHSGDLAVIHpDGYIEIKDRSKDIIISGGE 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 460 NYYSHAIESAVEELSEI-ETSYTAACAVRLGQNSTDqlaifFVT---SAKLNDEQMSQLLRNIQSHvsqvigvtpeYLLP 535
Cdd:cd12118 399 NISSVEVEGVLYKHPAVlEAAVVARPDEKWGEVPCA-----FVElkeGAKVTEEEIIAFCREHLAG----------FMVP 463
|
410 420
....*....|....*....|...
gi 1776025254 536 --VQKEEIPKTAIGKIQRTQLKT 556
Cdd:cd12118 464 ktVVFGELPKTSTGKIQKFVLRD 486
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
170-567 |
1.20e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 70.89 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 170 EDLLSAE-ADTDWHQSSPEDLALLLLTSGSTGTPKAVMLNHRNIM--SMVKGIIQMQGFTREDITFNWMPFDHVGGIGML 246
Cdd:PRK07008 158 ETLVGAQdGDYDWPRFDENQASSLCYTSGTTGNPKGALYSHRSTVlhAYGAALPDAMGLSARDAVLPVVPMFHVNAWGLP 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 247 HlrDVYL-GCQeinvssetiLMEPLKWLDWIDHYR----ASVTWA---PNFAFGLVTdfaeEIKDRKWDLSSMRYMLNGG 318
Cdd:PRK07008 238 Y--SAPLtGAK---------LVLPGPDLDGKSLYElieaERVTFSagvPTVWLGLLN----HMREAGLRFSTLRRTVIGG 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 319 ----EAMVakvgrRILEllEPHGLpadAIRPAWGMSETSS-GVIFSHEFTRAGTSDDD--HFVEI-GSPIPGFSMRIVN- 389
Cdd:PRK07008 303 sacpPAMI-----RTFE--DEYGV---EVIHAWGMTEMSPlGTLCKLKWKHSQLPLDEqrKLLEKqGRVIYGVDMKIVGd 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 390 DHNELVEEGE-IGRFQVSGLSVTSGYYQrpdlNESVFTEDGWFETGDLGFL-RNGRLTITGRTKDaiiinginyyshAIE 467
Cdd:PRK07008 373 DGRELPWDGKaFGDLQVRGPWVIDRYFR----GDASPLVDGWFPTGDVATIdADGFMQITDRSKD------------VIK 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 468 SAVEELSEIETS---------YTAACaVRLGQNSTDQLAIFFVT---SAKLNDEQMSQLLRniqshvsqviGVTPEYLLP 535
Cdd:PRK07008 437 SGGEWISSIDIEnvavahpavAEAAC-IACAHPKWDERPLLVVVkrpGAEVTREELLAFYE----------GKVAKWWIP 505
|
410 420 430
....*....|....*....|....*....|....*
gi 1776025254 536 ---VQKEEIPKTAIGKIQRTQLKTSFEngefDHLL 567
Cdd:PRK07008 506 ddvVFVDAIPHTATGKLQKLKLREQFR----DYVL 536
|
|
| PRK06501 |
PRK06501 |
beta-ketoacyl-ACP synthase; |
4722-4921 |
1.27e-11 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235817 [Multi-domain] Cd Length: 425 Bit Score: 70.43 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4722 AANLSQFFDVRGPSVVVDTACSSALVGMNMAIQALRGGDIQSAIV----GGV--------SLLSSDASHRlfDRRGILSK 4789
Cdd:PRK06501 155 ADRLADRFGTRGLPISLSTACASGATAIQLGVEAIRRGETDRALCiatdGSVsaealirfSLLSALSTQN--DPPEKASK 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4790 HssfhvFDERADGVVLGEGVGMVMLKTVKQALEDGDTIYAVVKAASVNNDG--RT-----AGPATpnleaqkEVMKDALF 4862
Cdd:PRK06501 233 P-----FSKDRDGFVMAEGAGALVLESLESAVARGAKILGIVAGCGEKADSfhRTrsspdGSPAI-------GAIRAALA 300
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1776025254 4863 KSGKKPEDISYLEANGSGSIVTDLLELKAIQSVY--RSGHsSPLSlgSIKPNIGHPLCAEG 4921
Cdd:PRK06501 301 DAGLTPEQIDYINAHGTSTPENDKMEYLGLSAVFgeRLAS-IPVS--SNKSMIGHTLTAAG 358
|
|
| PRK09185 |
PRK09185 |
beta-ketoacyl-ACP synthase; |
4721-4988 |
1.61e-11 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236398 [Multi-domain] Cd Length: 392 Bit Score: 69.87 E-value: 1.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4721 LAANLSQFFDVRGPSVVVDTAC-SSALVGMNmAIQALRGGDIQSAIVGGVSLLSsdashRL----FDRRGILSKHssfHV 4795
Cdd:PRK09185 139 LADFLRAYLGLSGPAYTISTACsSSAKVFAS-ARRLLEAGLCDAAIVGGVDSLC-----RLtlngFNSLESLSPQ---PC 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4796 --FDERADGVVLGEGVG-MVMLKTVKQAL------EDGDtiyavvkA---ASVNNDGRTAgpatpnleaqKEVMKDALFK 4863
Cdd:PRK09185 210 rpFSANRDGINIGEAAAfFLLEREDDAAVallgvgESSD-------AhhmSAPHPEGLGA----------ILAMQQALAD 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4864 SGKKPEDISYLEANGSGSIVTDLLELKAIQSVYrsGHSSPLSlgSIKPNIGHPLCAEGI--ASFIKVVLmlkERRFVPfl 4941
Cdd:PRK09185 273 AGLAPADIGYINLHGTATPLNDAMESRAVAAVF--GDGVPCS--STKGLTGHTLGAAGAveAAICWLAL---RHGLPP-- 343
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1776025254 4942 sgekemAHFDQQKANITFsrALEKWTDSQPTAAI-----NCFADGGTNVHVI 4988
Cdd:PRK09185 344 ------HGWNTGQPDPAL--PPLYLVENAQALAIryvlsNSFAFGGNNCSLI 387
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
187-555 |
1.69e-11 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 70.24 E-value: 1.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 187 EDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITfnWMPFDHVGGIGMLhlrdvYLGCQEINVSSETIL 266
Cdd:cd05973 88 SDPFVMMFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPEDSF--WNAADPGWAYGLY-----YAITGPLALGHPTIL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 267 ME-----PLKWLDWIDHYRASVTWAPNFAFGLVTDFAEEIKDRKwdlSSMRYMLNGGEAMVAKVGRRILELLephGLPad 341
Cdd:cd05973 161 LEggfsvESTWRVIERLGVTNLAGSPTAYRLLMAAGAEVPARPK---GRLRRVSSAGEPLTPEVIRWFDAAL---GVP-- 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 342 aIRPAWGMSETSSGVIFSHEftragtsdDDHFVEIGS---PIPGFSMRIVNDHNELVEEGEIGRFQV----SGLSVTSGY 414
Cdd:cd05973 233 -IHDHYGQTELGMVLANHHA--------LEHPVHAGSagrAMPGWRVAVLDDDGDELGPGEPGRLAIdianSPLMWFRGY 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 415 YQRPDLNESvfteDGWFETGDLG-FLRNGRLTITGRTKDAIIINGINYYSHAIESAVeelseIETSYTAACAV--RLGQN 491
Cdd:cd05973 304 QLPDTPAID----GGYYLTGDTVeFDPDGSFSFIGRADDVITMSGYRIGPFDVESAL-----IEHPAVAEAAVigVPDPE 374
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1776025254 492 STDQLAIFFVTSAklNDEQMSQLLRNIQSHVSQVIGV-----TPEYLlpvqkEEIPKTAIGKIQRTQLK 555
Cdd:cd05973 375 RTEVVKAFVVLRG--GHEGTPALADELQLHVKKRLSAhayprTIHFV-----DELPKTPSGKIQRFLLR 436
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
4465-4525 |
2.21e-11 |
|
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.
Pssm-ID: 425746 [Multi-domain] Cd Length: 62 Bit Score: 61.81 E-value: 2.21e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1776025254 4465 SWLIDLFTEELRIDREDFEIDGLFQDYGVDSIILAQVLQRINRKLEAALDPSILYEYPTIQ 4525
Cdd:pfam00550 1 ERLRELLAEVLGVPAEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLA 61
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
71-561 |
2.27e-11 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 70.01 E-value: 2.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 71 RIVKGLRQSGLKaKQSVILQLGDNS-QLLPAFWGCVLTGVVPA---PLAVPPTYAE--SSSG-----TQ-----KLKDAW 134
Cdd:PLN02246 62 RVAAGLHKLGIR-QGDVVMLLLPNCpEFVLAFLGASRRGAVTTtanPFYTPAEIAKqaKASGakliiTQscyvdKLKGLA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 135 TLLDKPAVITDRGmhqemldwakEQGLEGFRaiivEDLLSAEADTDWHQSSPEDLALLLLTSGSTGTPKAVMLNHRNIMS 214
Cdd:PLN02246 141 EDDGVTVVTIDDP----------PEGCLHFS----ELTQADENELPEVEISPDDVVALPYSSGTTGLPKGVMLTHKGLVT 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 215 MVKGiiQMQG------FTREDITFNWMPFDHV---GGIGMLHLRdvylgcqeinVSSETILM---EPLKWLDWIDHYRas 282
Cdd:PLN02246 207 SVAQ--QVDGenpnlyFHSDDVILCVLPMFHIyslNSVLLCGLR----------VGAAILIMpkfEIGALLELIQRHK-- 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 283 VTWAPnFAFGLVTDFAEEIKDRKWDLSSMRYMLNGGeamvAKVGRRILELLEPHgLPADAIRPAWGMSETSSGVIFSHEF 362
Cdd:PLN02246 273 VTIAP-FVPPIVLAIAKSPVVEKYDLSSIRMVLSGA----APLGKELEDAFRAK-LPNAVLGQGYGMTEAGPVLAMCLAF 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 363 TR---------AGTSDDDHFVEIGSPIPGFSMRivndHNelvEEGEIGrfqVSGLSVTSGYYQRPDLNESVFTEDGWFET 433
Cdd:PLN02246 347 AKepfpvksgsCGTVVRNAELKIVDPETGASLP----RN---QPGEIC---IRGPQIMKGYLNDPEATANTIDKDGWLHT 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 434 GDLGFL-RNGRLTITGRTKDAIIINGinyyshaIESAVEELSEIETSYTA---ACAVRLGQNSTDQLAIFFVtsAKLNDE 509
Cdd:PLN02246 417 GDIGYIdDDDELFIVDRLKELIKYKG-------FQVAPAELEALLISHPSiadAAVVPMKDEVAGEVPVAFV--VRSNGS 487
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1776025254 510 QMSQllRNIQSHVS-QVIgvtpeYLLPVQK----EEIPKTAIGKIQRTQLKTSFENG 561
Cdd:PLN02246 488 EITE--DEIKQFVAkQVV-----FYKRIHKvffvDSIPKAPSGKILRKDLRAKLAAG 537
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
1297-1634 |
2.71e-11 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 70.76 E-value: 2.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1297 PENLAYVIYTSGSTGKPKGVMIPHKA-LTNFLVSMGETPgLTAEDKMLAVTT--YCFDIAAlELFLPLIKGAHCYICQTE 1373
Cdd:PRK06814 792 PDDPAVILFTSGSEGTPKGVVLSHRNlLANRAQVAARID-FSPEDKVFNALPvfHSFGLTG-GLVLPLLSGVKVFLYPSP 869
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1374 -HTKDVEKLkrdIRTIKPTVMQATPAtwkmlFYSGWENEENV-------KILCGGEALPETLKRYFLDT-GSEAWNMFGP 1444
Cdd:PRK06814 870 lHYRIIPEL---IYDTNATILFGTDT-----FLNGYARYAHPydfrslrYVFAGAEKVKEETRQTWMEKfGIRILEGYGV 941
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1445 TETtiwSAVQRINDEC-SRA-TIGRPIANTqiyitDSQLAPVPaGVP--GELCIAGDGVAKGYYKKEeltdsrfidNPF- 1519
Cdd:PRK06814 942 TET---APVIALNTPMhNKAgTVGRLLPGI-----EYRLEPVP-GIDegGRLFVRGPNVMLGYLRAE---------NPGv 1003
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1520 --EPGSKLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSE-HPGILECVV-VADM---DNLAAYYTAKH 1592
Cdd:PRK06814 1004 lePPADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAElWPDALHAAVsIPDArkgERIILLTTASD 1083
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1776025254 1593 ANAsltARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKID 1634
Cdd:PRK06814 1084 ATR---AAFLAHAKAAGASELMVPAEIITIDEIPLLGTGKID 1122
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
186-498 |
2.74e-11 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 70.05 E-value: 2.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 186 PEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQG-----FTREDITFNWMPFDHV-------------GGIGMLH 247
Cdd:PLN02614 222 KSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLKsanaaLTVKDVYLSYLPLAHIfdrvieecfiqhgAAIGFWR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 248 lRDVYLGCQEINVSSETILMEPLKWLDWI-----------DHYRASV-TWAPNFAFGLV---------TDFAEEI---KD 303
Cdd:PLN02614 302 -GDVKLLIEDLGELKPTIFCAVPRVLDRVysglqkklsdgGFLKKFVfDSAFSYKFGNMkkgqshveaSPLCDKLvfnKV 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 304 RKWDLSSMRYMLNGGEAMVAKVGRRILELLEPHGLPAdairpaWGMSETSSG--VIFSHEFTRAGTsdddhfveIGSPIP 381
Cdd:PLN02614 381 KQGLGGNVRIILSGAAPLASHVESFLRVVACCHVLQG------YGLTESCAGtfVSLPDELDMLGT--------VGPPVP 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 382 GFSMRIvndhnELVEEGEI--------GRFQVSGLSVTSGYYQRPDLNESVFTeDGWFETGDLG-FLRNGRLTITGRTKD 452
Cdd:PLN02614 447 NVDIRL-----ESVPEMEYdalastprGEICIRGKTLFSGYYKREDLTKEVLI-DGWLHTGDVGeWQPNGSMKIIDRKKN 520
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1776025254 453 AIIINGINYYshaiesAVEELSEIETSYTAACAVRLGQNSTDQLAI 498
Cdd:PLN02614 521 IFKLSQGEYV------AVENIENIYGEVQAVDSVWVYGNSFESFLV 560
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
188-452 |
3.08e-11 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 69.87 E-value: 3.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 188 DLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQM-----QGFTREDITFNWMPFDHV-------------GGIGMLH-- 247
Cdd:PLN02861 221 DICTIMYTSGTTGEPKGVILTNRAIIAEVLSTDHLlkvtdRVATEEDSYFSYLPLAHVydqvietyciskgASIGFWQgd 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 248 ----LRDV------------------YLGCQEiNVSSETILMEPLkwLDWIDHYRASvtwapNFAFGLVTDFAEEIKDR- 304
Cdd:PLN02861 301 irylMEDVqalkptifcgvprvydriYTGIMQ-KISSGGMLRKKL--FDFAYNYKLG-----NLRKGLKQEEASPRLDRl 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 305 -----KWDLSS-MRYMLNGGeamvAKVGRRILELLEPhgLPADAIRPAWGMSETSSGVIFS--HEFTRAGTsdddhfveI 376
Cdd:PLN02861 373 vfdkiKEGLGGrVRLLLSGA----APLPRHVEEFLRV--TSCSVLSQGYGLTESCGGCFTSiaNVFSMVGT--------V 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 377 GSPIPGFSMRIVN------DHNELVEEGEIGrfqVSGLSVTSGYYQRPDLNESVFTeDGWFETGDLGFLR-NGRLTITGR 449
Cdd:PLN02861 439 GVPMTTIEARLESvpemgyDALSDVPRGEIC---LRGNTLFSGYHKRQDLTEEVLI-DGWFHTGDIGEWQpNGAMKIIDR 514
|
...
gi 1776025254 450 TKD 452
Cdd:PLN02861 515 KKN 517
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
185-472 |
3.23e-11 |
|
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341256 [Multi-domain] Cd Length: 596 Bit Score: 69.69 E-value: 3.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 185 SPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFT----REDITFNWMPFDHVGgIGMLhlrDVYLGcqeINV 260
Cdd:cd05933 148 KPNQCCTLIYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLRpatvGQESVVSYLPLSHIA-AQIL---DIWLP---IKV 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 261 SSETILMEP--LKW--------------------------------LDWIDHYRASVTWAPNFafGLVTDFAEEIKDRKw 306
Cdd:cd05933 221 GGQVYFAQPdaLKGtlvktlrevrptafmgvprvwekiqekmkavgAKSGTLKRKIASWAKGV--GLETNLKLMGGESP- 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 307 dlSSMRYMLngGEAMVAKVGRRILELLEPH-------GLPAD----------AIRPAWGMSETSSgvifSHEFTRagtSD 369
Cdd:cd05933 298 --SPLFYRL--AKKLVFKKVRKALGLDRCQkfftgaaPISREtlefflslniPIMELYGMSETSG----PHTISN---PQ 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 370 DDHFVEIGSPIPGFSMRIVNDHNElveegEIGRFQVSGLSVTSGYYQRPDLNESVFTEDGWFETGDLGFL-RNGRLTITG 448
Cdd:cd05933 367 AYRLLSCGKALPGCKTKIHNPDAD-----GIGEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLdEDGFLYITG 441
|
330 340
....*....|....*....|....*
gi 1776025254 449 RTKDAIII-NGINYYSHAIESAVEE 472
Cdd:cd05933 442 RIKELIITaGGENVPPVPIEDAVKK 466
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
1251-1658 |
3.37e-11 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 69.83 E-value: 3.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1251 VFITLTTSELVNTLSwNGVTTalldqdwDEIAQTASDRKVLTRTVTPENLAYVIYTSGSTGKPKGVMIPHKALTNFLVSM 1330
Cdd:PLN02860 133 VFLESPSSSVFIFLN-SFLTT-------EMLKQRALGTTELDYAWAPDDAVLICFTSGTTGRPKGVTISHSALIVQSLAK 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1331 GETPGLTAEDKMLAVTTYCfDIAALE--LFLPLIKGAHCYICQTEHTKDVEKLKRDIRT---IKPTVMQ------ATPAT 1399
Cdd:PLN02860 205 IAIVGYGEDDVYLHTAPLC-HIGGLSsaLAMLMVGACHVLLPKFDAKAALQAIKQHNVTsmiTVPAMMAdlisltRKSMT 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1400 WKmlfysgwENEENVKILCGGEALPETL----KRYFldTGSEAWNMFGPTETTIWSAVQRINDecsrATIGRPIANTQIY 1475
Cdd:PLN02860 284 WK-------VFPSVRKILNGGGSLSSRLlpdaKKLF--PNAKLFSAYGMTEACSSLTFMTLHD----PTLESPKQTLQTV 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1476 I-TDSQLAPVPAGV----PG---ELCIAGDG-------VAKGYYkkeelTDSRFIDNPFEPGSKLYR-----TGDMARWL 1535
Cdd:PLN02860 351 NqTKSSSVHQPQGVcvgkPAphvELKIGLDEssrvgriLTRGPH-----VMLGYWGQNSETASVLSNdgwldTGDIGWID 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1536 PGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMD-------------------NLAAYYTAKHaNAS 1596
Cdd:PLN02860 426 KAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDsrltemvvacvrlrdgwiwSDNEKENAKK-NLT 504
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1776025254 1597 LTARELRHFV-KNALPAYMVPSYFIQL-DHMPLTPNGKIDRNSLKnidlsGEQLKQRQTSPKNI 1658
Cdd:PLN02860 505 LSSETLRHHCrEKNLSRFKIPKLFVQWrKPFPLTTTGKIRRDEVR-----REVLSHLQSLPSNL 563
|
|
| 17beta-HSDXI-like_SDR_c |
cd05339 |
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ... |
2852-3020 |
3.39e-11 |
|
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid dehydrogenases (17betaHSD) are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. 17betaHSD type XI, a classical SDR, preferentially converts 3alpha-Adiol to androsterone but not numerous other tested steroids. This subgroup of classical SDRs also includes members identified as retinol dehydrogenases, which convert retinol to retinal, a property that overlaps with 17betaHSD activity. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.
Pssm-ID: 187598 [Multi-domain] Cd Length: 243 Bit Score: 66.88 E-value: 3.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2852 LITGGAGSLGLLFAKEIANRtgRSTIVLTGRSVLSEDKENELeaLRSIGAEVVYREADVSDQHAVHHLFEEIKERYGTLN 2931
Cdd:cd05339 3 LITGGGSGIGRLLALEFAKR--GAKVVILDINEKGAEETANN--VRKAGGKVHYYKCDVSKREEVYEAAKKIKKEVGDVT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2932 GIIHGAGSIKDHFIIHKTNEEFQEVLqpKVSGLLHVDECSKDFPL------DFFIFFSSVSGCLGNAGQADYAAANSFMD 3005
Cdd:cd05339 79 ILINNAGVVSGKKLLELPDEEIEKTF--EVNTLAHFWTTKAFLPDmlernhGHIVTIASVAGLISPAGLADYCASKAAAV 156
|
170
....*....|....*.
gi 1776025254 3006 AFAE-YRRSLAASKKR 3020
Cdd:cd05339 157 GFHEsLRLELKAYGKP 172
|
|
| PRK07967 |
PRK07967 |
beta-ketoacyl-ACP synthase I; |
4722-4994 |
4.66e-11 |
|
beta-ketoacyl-ACP synthase I;
Pssm-ID: 181184 [Multi-domain] Cd Length: 406 Bit Score: 68.54 E-value: 4.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4722 AANLSQFFDVRGPSVVVDTACSSALVGMNMAIQALRGG--DIQSAivGGVSLLSSDASHrLFDRRGILSK------HSSF 4793
Cdd:PRK07967 142 SACLATPFKIKGVNYSISSACATSAHCIGNAVEQIQLGkqDIVFA--GGGEELDWEMSC-LFDAMGALSTkyndtpEKAS 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4794 HVFDERADGVVLGEGVGMVMLKTVKQALEDGDTIYAVVKAASVNNDGrtAGPATPNLEAQKEVMKDALfkSGKKpEDISY 4873
Cdd:PRK07967 219 RAYDANRDGFVIAGGGGVVVVEELEHALARGAKIYAEIVGYGATSDG--YDMVAPSGEGAVRCMQMAL--ATVD-TPIDY 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4874 LEANGSGSIVTDLLELKAIQSVYrsGHSSPlSLGSIKPNIGHPLCAEGIASFIKVVLMLKERrfvpFLSGEKEMAHFDQQ 4953
Cdd:PRK07967 294 INTHGTSTPVGDVKELGAIREVF--GDKSP-AISATKSLTGHSLGAAGVQEAIYSLLMMEHG----FIAPSANIEELDPQ 366
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1776025254 4954 KANITFSRaleKWTDSQP--TAAINCFADGGTNVHVIVEAWEK 4994
Cdd:PRK07967 367 AAGMPIVT---ETTDNAEltTVMSNSFGFGGTNATLVFRRYKG 406
|
|
| PRK07910 |
PRK07910 |
beta-ketoacyl-ACP synthase; |
4740-4934 |
4.89e-11 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236129 [Multi-domain] Cd Length: 418 Bit Score: 68.60 E-value: 4.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4740 TACSSALVGMNMAIQALRGGDIQSAIVGGVSLLSSDASHRLFDR-RGILSKHS-----SFHVFDERADGVVLGEGVGMVM 4813
Cdd:PRK07910 169 SACASGSEAIAQAWRQIVLGEADIAICGGVETRIEAVPIAGFAQmRIVMSTNNddpagACRPFDKDRDGFVFGEGGALMV 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4814 LKTVKQALEDGDTIYAVVKAASVNNDGRTAGPATPNLEAQKEVMKDALFKSGKKPEDISYLEANGSGSIVTDLLELKAIQ 4893
Cdd:PRK07910 249 IETEEHAKARGANILARIMGASITSDGFHMVAPDPNGERAGHAMTRAIELAGLTPGDIDHVNAHATGTSVGDVAEGKAIN 328
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1776025254 4894 SVYRSGHSsplSLGSIKPNIGHPLCAEGIASFIKVVLMLKE 4934
Cdd:PRK07910 329 NALGGHRP---AVYAPKSALGHSVGAVGAVESILTVLALRD 366
|
|
| PRK12827 |
PRK12827 |
short chain dehydrogenase; Provisional |
2850-3056 |
6.06e-11 |
|
short chain dehydrogenase; Provisional
Pssm-ID: 237219 [Multi-domain] Cd Length: 249 Bit Score: 66.28 E-value: 6.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGLLFAKEIANRtGRSTIVLTGRSVLSEDKENELEAL-RSIGAEVVYREADVSDQHAVHHLFEEIKERYG 2928
Cdd:PRK12827 8 RVLITGGSGGLGRAIAVRLAAD-GADVIVLDIHPMRGRAEADAVAAGiEAAGGKALGLAFDVRDFAATRAALDAGVEEFG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2929 TLNGIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSGLLHVDECSKdFPL------DFFIFFSSVSGCLGNAGQADYAAANS 3002
Cdd:PRK12827 87 RLDILVNNAGIATDAAFAELSIEEWDDVIDVNLDGFFNVTQAAL-PPMirarrgGRIVNIASVAGVRGNRGQVNYAASKA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1776025254 3003 fmdAFAEYRRSLAASKKRFGSTISFNWPLWEEGGMQVGAEDEKRMLKTtgmVPM 3056
Cdd:PRK12827 166 ---GLIGLTKTLANELAPRGITVNAVAPGAINTPMADNAAPTEHLLNP---VPV 213
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
168-486 |
7.57e-11 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 68.19 E-value: 7.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 168 IVEDLLSAEA-DTDWH----QSSPEDL------ALLLLTSGSTGTPKAVmlnHRN------IMSMVKGIIQMQGFTREDI 230
Cdd:PRK12406 122 ISPALLTPPAgAIDWEgwlaQQEPYDGppvpqpQSMIYTSGTTGHPKGV---RRAaptpeqAAAAEQMRALIYGLKPGIR 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 231 TFNWMPfdhvggigMLHLRDVYLGCQEINVSSETILM---EPLKWLDWIDHYRASVTWAPNFAFGLVTDFAEEIKdRKWD 307
Cdd:PRK12406 199 ALLTGP--------LYHSAPNAYGLRAGRLGGVLVLQprfDPEELLQLIERHRITHMHMVPTMFIRLLKLPEEVR-AKYD 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 308 LSSMRYMLNGGEAMVAKVGRRILELLEPhglpadAIRPAWGMSETSSgVIFSheftragTSDD--DHFVEIGSPIPGFSM 385
Cdd:PRK12406 270 VSSLRHVIHAAAPCPADVKRAMIEWWGP------VIYEYYGSTESGA-VTFA-------TSEDalSHPGTVGKAAPGAEL 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 386 RIVNDHNELVEEGEIGRFQVSGLSVTS-GYYQRPDLNESVfTEDGWFETGDLGFL-RNGRLTITGRTKDAIIINGINYYS 463
Cdd:PRK12406 336 RFVDEDGRPLPQGEIGEIYSRIAGNPDfTYHNKPEKRAEI-DRGGFITSGDVGYLdADGYLFLCDRKRDMVISGGVNIYP 414
|
330 340
....*....|....*....|...
gi 1776025254 464 HAIESAVEELSEIetsytAACAV 486
Cdd:PRK12406 415 AEIEAVLHAVPGV-----HDCAV 432
|
|
| CLF |
cd00832 |
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ... |
1761-2144 |
1.24e-10 |
|
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic antibiotic-producing polyketide synthases (PKSs) of filamentous bacteria. CLFs have been shown to have decarboxylase activity towards malonyl-acyl carrier protein (ACP). CLFs are similar to other elongation ketosynthase domains, but their active site cysteine is replaced by a conserved glutamine.
Pssm-ID: 238428 [Multi-domain] Cd Length: 399 Bit Score: 67.00 E-value: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1761 SVAIIGISCEFPGAKNHDEFWENLRDGKESIAffnkeELQRFGISKEIAENADYVP---AKASIEGkdRFDPSffqispk 1837
Cdd:cd00832 2 RAVVTGIGVVAPNGLGVEEYWKAVLDGRSGLG-----PITRFDPSGYPARLAGEVPdfdAAEHLPG--RLLPQ------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1838 daefMDPQLRMLLTHSWKAIEDAGYAAGQIPQTSV-FMSASNN-----SYRAL--LPSDTTESLETPDGYVSWVLAQSGT 1909
Cdd:cd00832 68 ----TDRMTRLALAAADWALADAGVDPAALPPYDMgVVTASAAggfefGQRELqkLWSKGPRHVSAYQSFAWFYAVNTGQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1910 IPtmISHklGLRGPSYFVHANCSSSLIGLHSAyKSLLSAESDYALVGG--ATLHTESNIGYVHQPGLNFSSDGHI--KAF 1985
Cdd:cd00832 144 IS--IRH--GMRGPSGVVVAEQAGGLDALAQA-RRLVRRGTPLVVSGGvdSALCPWGWVAQLSSGRLSTSDDPARayLPF 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1986 DASADGMIGGEGVAVVLLKKAADAVKDGDHIYALLRGIGVNNDGADKvgfyAPSVKGQADVVQQVMNQTKIHPESICYVE 2065
Cdd:cd00832 219 DAAAAGYVPGEGGAILVLEDAAAARERGARVYGEIAGYAATFDPPPG----SGRPPGLARAIRLALADAGLTPEDVDVVF 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2066 AHGTGTKLGDPIELAALTNVYrqytnktqfcGIGSV-----KTNIGHLDTAAGLAGCIKVVMSLYHQELAPSINYKEPNP 2140
Cdd:cd00832 295 ADAAGVPELDRAEAAALAAVF----------GPRGVpvtapKTMTGRLYAGGAPLDVATALLALRDGVIPPTVNVTDVPP 364
|
....
gi 1776025254 2141 NTDL 2144
Cdd:cd00832 365 AYGL 368
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
1297-1644 |
1.44e-10 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 67.53 E-value: 1.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1297 PENLAYVIYTSGSTGKPKGVMIPHKALTNFLVSMGETPGLTAEDKMLAVT----TYCFDIAALelfLPLIKGAHcyICQT 1372
Cdd:PRK06334 182 PEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLppfhAYGFNSCTL---FPLLSGVP--VVFA 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1373 EHTKDVEKLKRDIRTIKPTVMQATPATWKMLFYSGWENEENVKIL----CGGEALPETL----KRYF----LDTGseawn 1440
Cdd:PRK06334 257 YNPLYPKKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQESCLPSLrfvvIGGDAFKDSLyqeaLKTFphiqLRQG----- 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1441 mFGPTETtiwSAVQRINDECS---RATIGRPIANTQIYITDSQL-APVPAGVPGELCIAGDGVAKGYYKKEEltDSRFID 1516
Cdd:PRK06334 332 -YGTTEC---SPVITINTVNSpkhESCVGMPIRGMDVLIVSEETkVPVSSGETGLVLTRGTSLFSGYLGEDF--GQGFVE 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1517 npfEPGSKLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILE---------CVVVADMDNLAAY 1587
Cdd:PRK06334 406 ---LGGETWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEGFGQNAadhagplvvCGLPGEKVRLCLF 482
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1776025254 1588 YTakhanASLTARELRHFVKNALPAYMVP-SYFIQLDHMPLTPNGKIDRNSLKNIDLS 1644
Cdd:PRK06334 483 TT-----FPTSISEVNDILKNSKTSSILKiSYHHQVESIPMLGTGKPDYCSLNALAKS 535
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
182-463 |
1.93e-10 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 67.23 E-value: 1.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 182 HQSSPEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIiqmqgftREDitFNWMPfdhvGGIGM-----LHLRDVYLGCQ 256
Cdd:PRK09274 169 ADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEAL-------RED--YGIEP----GEIDLptfplFALFGPALGMT 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 257 ----EINvSSETILMEPLKWLDWIDHYRasVTwapNFaFG------LVTDFAEEikdRKWDLSSMRYMLNGGEAMVAKVG 326
Cdd:PRK09274 236 svipDMD-PTRPATVDPAKLFAAIERYG--VT---NL-FGspalleRLGRYGEA---NGIKLPSLRRVISAGAPVPIAVI 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 327 RRILELLePHGLPadaIRPAWGMSE-------TSSGVIFShefTRAGTsdDDHF-VEIGSPIPGFSMRIVN--------- 389
Cdd:PRK09274 306 ERFRAML-PPDAE---ILTPYGATEalpissiESREILFA---TRAAT--DNGAgICVGRPVDGVEVRIIAisdapipew 376
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1776025254 390 DHNELVEEGEIGRFQVSGLSVTSGYYQRPDLNESVFTEDG----WFETGDLGFLRN-GRLTITGRTKDAIIINGINYYS 463
Cdd:PRK09274 377 DDALRLATGEIGEIVVAGPMVTRSYYNRPEATRLAKIPDGqgdvWHRMGDLGYLDAqGRLWFCGRKAHRVETAGGTLYT 455
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
187-566 |
1.99e-10 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 67.17 E-value: 1.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 187 EDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGII-----QMQGFTREDITFNWMPFDHVGGIGMLHLRDVYLGcqeinvs 261
Cdd:PLN02574 198 DDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVrfeasQYEYPGSDNVYLAALPMFHIYGLSLFVVGLLSLG------- 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 262 SETILMEPLKWLDW---IDHYRasVTWAPNFAFGLVTDFAEEIKDRKWDLSSMRYMLNGGEAMVAKVGRRILELLePHgl 338
Cdd:PLN02574 271 STIVVMRRFDASDMvkvIDRFK--VTHFPVVPPILMALTKKAKGVCGEVLKSLKQVSCGAAPLSGKFIQDFVQTL-PH-- 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 339 pADAIRpAWGMSE-TSSGvifshefTRA-GTSDDDHFVEIGSPIPGFSMRIVN-DHNELVEEGEIGRFQVSGLSVTSGYY 415
Cdd:PLN02574 346 -VDFIQ-GYGMTEsTAVG-------TRGfNTEKLSKYSSVGLLAPNMQAKVVDwSTGCLLPPGNCGELWIQGPGVMKGYL 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 416 QRPDLNESVFTEDGWFETGDLG-FLRNGRLTITGRTKDAIIINGINYYSHAIESAVEELSEIetsyTAACAVRLGQNSTD 494
Cdd:PLN02574 417 NNPKATQSTIDKDGWLRTGDIAyFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEI----IDAAVTAVPDKECG 492
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1776025254 495 QLAIFFVTsaKLNDEQMSQllrniqshvSQVIGVTPEYLLPVQK-------EEIPKTAIGKIQRTQLKTSFENGEFDHL 566
Cdd:PLN02574 493 EIPVAFVV--RRQGSTLSQ---------EAVINYVAKQVAPYKKvrkvvfvQSIPKSPAGKILRRELKRSLTNSVSSRL 560
|
|
| AcpP |
COG0236 |
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ... |
3115-3186 |
2.04e-10 |
|
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440006 [Multi-domain] Cd Length: 80 Bit Score: 59.87 E-value: 2.04e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1776025254 3115 LEAALIQMVGAILKVNTDDIDVNTEL-SEYGFDSVTFTVFTNKINEKFQLELTPTIFFEYGSVQSLAEYVVAA 3186
Cdd:COG0236 6 LEERLAEIIAEVLGVDPEEITPDDSFfEDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEEK 78
|
|
| Cyc_NRPS |
cd19535 |
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
727-1033 |
2.06e-10 |
|
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Cyc (heterocyclization) domains catalyze two separate reactions in the creation of heterocyclized peptide products in nonribosomal peptide synthesis: amide bond formation followed by intramolecular cyclodehydration between a Cys, Ser, or Thr side chain and a carbonyl carbon on the peptide backbone to form a thiazoline, oxazoline, or methyloxazoline ring. Cyc-domains are homologous to standard NRPS Condensation (C) domains. C-domains typically have a conserved HHxxxD motif at the active site; Cyc-domains have an alternative, conserved DxxxxD active site motif, mutation of the aspartate residues in this motif can abolish or diminish condensation activity. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and Cyc-domains. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380458 [Multi-domain] Cd Length: 423 Bit Score: 66.74 E-value: 2.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 727 GLHLETLQQAFGLVLNQHPILKHVIQEkDGVPILKNEPAlSIEIKTENISSMKESDIPAFLRK----------KVkepyv 796
Cdd:cd19535 36 DLDPDRLERAWNKLIARHPMLRAVFLD-DGTQQILPEVP-WYGITVHDLRGLSEEEAEAALEElrerlshrvlDV----- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 797 kENSPLVRVMSFSRSEQEHFLLVVIHHLIFDGVSSVTFIHSLFDTYQlllkgqQPEIAVSPAIYH--DFAAWEKNMLAG- 873
Cdd:cd19535 109 -ERGPLFDIRLSLLPEGRTRLHLSIDLLVADALSLQILLRELAALYE------DPGEPLPPLELSfrDYLLAEQALRETa 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 874 --KDgvkhRTYWQKQLSgTLPN-LQLP-KVSASSVSEFREDTYTRRLSSGFMNQVRMFAKEHSVNVTTVFLSCYMMLLGR 949
Cdd:cd19535 182 yeRA----RAYWQERLP-TLPPaPQLPlAKDPEEIKEPRFTRREHRLSAEQWQRLKERARQHGVTPSMVLLTAYAEVLAR 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 950 YTGQKEQIVGMPAMVRPE--ERFDDAIGHFLNMLPIRSELNPADTFSSFISKLQLTILDGLDHAAYPFPKMVRDLN--IP 1025
Cdd:cd19535 257 WSGQPRFLLNLTLFNRLPlhPDVNDVVGDFTSLLLLEVDGSEGQSFLERARRLQQQLWEDLDHSSYSGVVVVRRLLrrRG 336
|
....*...
gi 1776025254 1026 RSQAGSPV 1033
Cdd:cd19535 337 GQPVLAPV 344
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
1302-1661 |
2.78e-10 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 67.07 E-value: 2.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1302 YVIYTSGSTGKPKGV-------MIPHKALTNFLVSMGETPGLTAEDKMLAVTTYCFDIAALEL--FLPLIKGAhcyICQT 1372
Cdd:PTZ00237 258 YILYTSGTTGNSKAVvrsngphLVGLKYYWRSIIEKDIPTVVFSHSSIGWVSFHGFLYGSLSLgnTFVMFEGG---IIKN 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1373 EHTKD-----VEKLKRDIRTIKPTVM----QATPATWKMlfYSGWENEENVKILCGGEALPETLKRYFLDT-GSEAWNMF 1442
Cdd:PTZ00237 335 KHIEDdlwntIEKHKVTHTLTLPKTIryliKTDPEATII--RSKYDLSNLKEIWCGGEVIEESIPEYIENKlKIKSSRGY 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1443 GPTETTIWSAVQRINDECSRATIGRPiantQIYITDSQLAP----VPAGVPGELCIA---GDGVAKGYYKKEELTDSRFi 1515
Cdd:PTZ00237 413 GQTEIGITYLYCYGHINIPYNATGVP----SIFIKPSILSEdgkeLNVNEIGEVAFKlpmPPSFATTFYKNDEKFKQLF- 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1516 dNPFePGskLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVA----DMDN-----LAA 1586
Cdd:PTZ00237 488 -SKF-PG--YYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGiydpDCYNvpiglLVL 563
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1776025254 1587 YYTAKHANASLT--ARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLKN-IDLSGEQLkqrqtsPKNIQDT 1661
Cdd:PTZ00237 564 KQDQSNQSIDLNklKNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPRQIISKfLNDSNYQL------PDNVNDS 635
|
|
| KDSR-like_SDR_c |
cd08939 |
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ... |
2852-3030 |
2.81e-10 |
|
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These proteins include members identified as KDSR, ribitol type dehydrogenase, and others. The group shows strong conservation of the active site tetrad and glycine rich NAD-binding motif of the classical SDRs. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.
Pssm-ID: 187643 [Multi-domain] Cd Length: 239 Bit Score: 63.81 E-value: 2.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2852 LITGGAGSLGLLFAKEIANRtGRStIVLTGRSV--LSEDKEN-ELEALRSiGAEVVYREADVSDQHAVHHLFEEIKERYG 2928
Cdd:cd08939 5 LITGGSSGIGKALAKELVKE-GAN-VIIVARSEskLEEAVEEiEAEANAS-GQKVSYISADLSDYEEVEQAFAQAVEKGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2929 TLNGIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSGLLHVdeCSKDFPL------DFFIFFSSVSGCLGNAGQADYAAANS 3002
Cdd:cd08939 82 PPDLVVNCAGISIPGLFEDLTAEEFERGMDVNYFGSLNV--AHAVLPLmkeqrpGHIVFVSSQAALVGIYGYSAYCPSKF 159
|
170 180
....*....|....*....|....*...
gi 1776025254 3003 FMDAFAEyrrSLAASKKRFGSTISFNWP 3030
Cdd:cd08939 160 ALRGLAE---SLRQELKPYNIRVSVVYP 184
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
331-560 |
2.93e-10 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 66.17 E-value: 2.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 331 ELLEP---HGLPadaIRPAWGMSETSSGV--IFSHEFTRAGTSdddhfveIGSPIPGFSMRIVNdhnelveeGEIGRFQV 405
Cdd:PRK07445 245 SLLEQarqLQLR---LAPTYGMTETASQIatLKPDDFLAGNNS-------SGQVLPHAQITIPA--------NQTGNITI 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 406 SGLSVTSGYYqrPDLNESvfteDGWFETGDLGFL-RNGRLTITGRTKDAIIINGINYYSHAIESAVEELSEIETsytaAC 484
Cdd:PRK07445 307 QAQSLALGYY--PQILDS----QGIFETDDLGYLdAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQD----VC 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 485 AVRL-----GQnstdQLAIFFVtsakLNDEQMSqlLRNIQSHVSQVIGV--TPEYLLPVQkeEIPKTAIGKIQRTQLKTS 557
Cdd:PRK07445 377 VLGLpdphwGE----VVTAIYV----PKDPSIS--LEELKTAIKDQLSPfkQPKHWIPVP--QLPRNPQGKINRQQLQQI 444
|
...
gi 1776025254 558 FEN 560
Cdd:PRK07445 445 AVQ 447
|
|
| YdfG |
COG4221 |
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ... |
4169-4341 |
3.10e-10 |
|
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; NADP-dependent 3-hydroxy acid dehydrogenase YdfG is part of the Pathway/BioSystem: Pyrimidine degradation
Pssm-ID: 443365 [Multi-domain] Cd Length: 240 Bit Score: 63.66 E-value: 3.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4169 KDHVLLITGGTRGIGLLCARHFAEcYGVkKLVLTGReqlppREEwarfktsntslaekiqAVRELEAK-GVQVEMLSLTL 4247
Cdd:COG4221 4 KGKVALITGASSGIGAATARALAA-AGA-RVVLAAR-----RAE----------------RLEALAAElGGRALAVPLDV 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4248 SDDAQVEQTLQHIKRTLGPIGGVIHCAGLTDMDTLAFIrkTSDDIQRVMEPKVSGLTTLYRHVcnepLQ--------FFV 4319
Cdd:COG4221 61 TDEAAVEAAVAAAVAEFGRLDVLVNNAGVALLGPLEEL--DPEDWDRMIDVNVKGVLYVTRAA----LPamrargsgHIV 134
|
170 180
....*....|....*....|..
gi 1776025254 4320 LFSSVSAIIPelSAGQADYAMA 4341
Cdd:COG4221 135 NISSIAGLRP--YPGGAVYAAT 154
|
|
| GlcDH_SDR_c |
cd05358 |
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ... |
2850-3015 |
3.16e-10 |
|
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR family, it catalyzes the NAD(P)-dependent oxidation of beta-D-glucose to D-glucono-delta-lactone. GlcDH has a typical NAD-binding site glycine-rich pattern as well as the canonical active site tetrad (YXXXK motif plus upstream Ser and Asn). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.
Pssm-ID: 187616 [Multi-domain] Cd Length: 253 Bit Score: 63.94 E-value: 3.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGLLFAKEIAnRTGrSTIVLTGRSvlSEDKENEL-EALRSIGAEVVYREADVSDQHAVHHLFEEIKERYG 2928
Cdd:cd05358 5 VALVTGASSGIGKAIAIRLA-TAG-ANVVVNYRS--KEDAAEEVvEEIKAVGGKAIAVQADVSKEEDVVALFQSAIKEFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2929 TLNGIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSG-LLHVDECSKDF----PLDFFIFFSSVSGCLGNAGQADYAAANSF 3003
Cdd:cd05358 81 TLDILVNNAGLQGDASSHEMTLEDWNKVIDVNLTGqFLCAREAIKRFrkskIKGKIINMSSVHEKIPWPGHVNYAASKGG 160
|
170
....*....|..
gi 1776025254 3004 MDAFAEyrrSLA 3015
Cdd:cd05358 161 VKMMTK---TLA 169
|
|
| PRK12824 |
PRK12824 |
3-oxoacyl-ACP reductase; |
2852-3025 |
3.43e-10 |
|
3-oxoacyl-ACP reductase;
Pssm-ID: 183773 [Multi-domain] Cd Length: 245 Bit Score: 63.63 E-value: 3.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2852 LITGGAGSLGLLFAKEIANRtGRsTIVLTGRS--VLSEDKENELEALRsigAEVVYREADVSDQHAVHHLFEEIKERYGT 2929
Cdd:PRK12824 6 LVTGAKRGIGSAIARELLND-GY-RVIATYFSgnDCAKDWFEEYGFTE---DQVRLKELDVTDTEECAEALAEIEEEEGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2930 LNGIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSGLLHVDE------CSKDFPLdfFIFFSSVSGCLGNAGQADYAAANSF 3003
Cdd:PRK12824 81 VDILVNNAGITRDSVFKRMSHQEWNDVINTNLNSVFNVTQplfaamCEQGYGR--IINISSVNGLKGQFGQTNYSAAKAG 158
|
170 180
....*....|....*....|..
gi 1776025254 3004 MDAFAeyrRSLAASKKRFGSTI 3025
Cdd:PRK12824 159 MIGFT---KALASEGARYGITV 177
|
|
| AcpP |
COG0236 |
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ... |
4461-4531 |
3.63e-10 |
|
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440006 [Multi-domain] Cd Length: 80 Bit Score: 59.10 E-value: 3.63e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1776025254 4461 SETQSWLIDLFTEELRIDREDFEID-GLFQDYGVDSIILAQVLQRINRKLEAALDPSILYEYPTIQRFTDWL 4531
Cdd:COG0236 4 EELEERLAEIIAEVLGVDPEEITPDdSFFEDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYL 75
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
55-454 |
4.43e-10 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 66.38 E-value: 4.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 55 GTEVYQSYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNSQLLPAFWGCVLTGVVPAPL-------AVP--PTYAESSS 125
Cdd:PLN02430 72 GPYMWKTYKEVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVAMEACAAHSLICVPLydtlgpgAVDyiVDHAEIDF 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 126 GTQKLKDAWTLLDK--------PAVITDRGMHQEMLDWAKEQGLEGFRAiivEDLL--SAEADTDWHQSSPEDLALLLLT 195
Cdd:PLN02430 152 VFVQDKKIKELLEPdcksakrlKAIVSFTSVTEEESDKASQIGVKTYSW---IDFLhmGKENPSETNPPKPLDICTIMYT 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 196 SGSTGTPKAVMLNHRNIMSMVKGI-IQMQGF----TREDITFNWMPFDHV-------------GGIGMLH-----LRD-- 250
Cdd:PLN02430 229 SGTSGDPKGVVLTHEAVATFVRGVdLFMEQFedkmTHDDVYLSFLPLAHIldrmieeyffrkgASVGYYHgdlnaLRDdl 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 251 -----------------VYLG----CQEINVSSETILMEPLKW-LDWID----HYRASvTWAPNFAFglvtdfaEEIKDR 304
Cdd:PLN02430 309 melkptllagvprvferIHEGiqkaLQELNPRRRLIFNALYKYkLAWMNrgysHKKAS-PMADFLAF-------RKVKAK 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 305 KWdlSSMRYMLNGGeamvAKVGRRILELLEPHGLpADAIRpAWGMSETSSGVI--FSHEFTRAGTsdddhfveIGSPIPG 382
Cdd:PLN02430 381 LG--GRLRLLISGG----APLSTEIEEFLRVTSC-AFVVQ-GYGLTETLGPTTlgFPDEMCMLGT--------VGAPAVY 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 383 FSMRIvndhNELVEEG-------EIGRFQVSGLSVTSGYYQRPDLNESVFtEDGWFETGDLG-FLRNGRLTITGRTKDAI 454
Cdd:PLN02430 445 NELRL----EEVPEMGydplgepPRGEICVRGKCLFSGYYKNPELTEEVM-KDGWFHTGDIGeILPNGVLKIIDRKKNLI 519
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
1131-1578 |
5.17e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 66.15 E-value: 5.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1131 LPEAEKQMILKTWnatgktYPYITFHELFEQQAKKTPDRAAVSY---------------------------EGQTLTYRE 1183
Cdd:PTZ00216 53 VTDEEHERLRNEW------YYGPNFLQRLERICKERGDRRALAYrpvervekevvkdadgkertmevthfnETRYITYAE 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1184 LDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAI----LKAGGAYVPLDpsypAERLEYMLEDSE--------- 1250
Cdd:PTZ00216 127 LWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIwsqsMVAATVYANLG----EDALAYALRETEckaivcngk 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1251 ---VFITLTTS-ELVNT-LSWNGVTTALLDQD------WDEIAQTASDRKVLTRTVTPEN---LAYVIYTSGSTGKPKGV 1316
Cdd:PTZ00216 203 nvpNLLRLMKSgGMPNTtIIYLDSLPASVDTEgcrlvaWTDVVAKGHSAGSHHPLNIPENnddLALIMYTSGTTGDPKGV 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1317 MIPHKALTNFLVSMG----ETPGLTAEDKmlavtTYC--------FDIAALELFLplIKGAH-CYICQTEHTKDVEKLKR 1383
Cdd:PTZ00216 283 MHTHGSLTAGILALEdrlnDLIGPPEEDE-----TYCsylplahiMEFGVTNIFL--ARGALiGFGSPRTLTDTFARPHG 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1384 DIRTIKPTVMQATPATWKMLfysgwenEENVkilcggEA-LPE--TLKRYFLDTGSEA-------------WN------- 1440
Cdd:PTZ00216 356 DLTEFRPVFLIGVPRIFDTI-------KKAV------EAkLPPvgSLKRRVFDHAYQSrlralkegkdtpyWNekvfsap 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1441 ----------------------------MFGP-------TETTIWSAVQRIND-ECSraTIGRPIANTQIYITDSQL--- 1481
Cdd:PTZ00216 423 ravlggrvramlsgggplsaatqefvnvVFGMviqgwglTETVCCGGIQRTGDlEPN--AVGQLLKGVEMKLLDTEEykh 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1482 --APVPAGvpgELCIAGDGVAKGYYKKEELTDSRFIDNPFepgsklYRTGDMARWLPGGRIEYIGRIDNQVK-IRGFRIE 1558
Cdd:PTZ00216 501 tdTPEPRG---EILLRGPFLFKGYYKQEELTREVLDEDGW------FHTGDVGSIAANGTLRIIGRVKALAKnCLGEYIA 571
|
570 580
....*....|....*....|....*
gi 1776025254 1559 LGDIESRLSEHP-----GIleCVVV 1578
Cdd:PTZ00216 572 LEALEALYGQNElvvpnGV--CVLV 594
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
186-451 |
6.19e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 65.90 E-value: 6.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 186 PEDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDIT--FNWMPFDHVGGIGMLHLrDVYLGCQeINVSSE 263
Cdd:PTZ00342 303 PDFITSIVYTSGTSGKPKGVMLSNKNLYNTVVPLCKHSIFKKYNPKthLSYLPISHIYERVIAYL-SFMLGGT-INIWSK 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 264 -----------------------------TILME-----PLK-WL-DWIDHYRASVT--WAPNFAFGLvTDFAEEIKDRK 305
Cdd:PTZ00342 381 dinyfskdiynskgnilagvpkvfnriytNIMTEinnlpPLKrFLvKKILSLRKSNNngGFSKFLEGI-THISSKIKDKV 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 306 wdLSSMRYMLNGGEAMVAKVGRRILELLEPHglpadaIRPAWGMSETSSGVIFSHEftragtsDDDHFVEIGSPI-PGFS 384
Cdd:PTZ00342 460 --NPNLEVILNGGGKLSPKIAEELSVLLNVN------YYQGYGLTETTGPIFVQHA-------DDNNTESIGGPIsPNTK 524
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1776025254 385 MRIVN----DHNELVEEGEIgrfQVSGLSVTSGYYQRPDLNESVFTEDGWFETGDLGFL-RNGRLTITGRTK 451
Cdd:PTZ00342 525 YKVRTwetyKATDTLPKGEL---LIKSDSIFSGYFLEKEQTKNAFTEDGYFKTGDIVQInKNGSLTFLDRSK 593
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
38-555 |
6.46e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 65.42 E-value: 6.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 38 TAAELGDTKGIIYLQPDGTEVyqSYRRLWDDGLRIVKGLRQSGLKAKQSVILqLGDNS-QLLPAFWGCVLTGVVPAPLAV 116
Cdd:PRK13390 5 THAQIAPDRPAVIVAETGEQV--SYRQLDDDSAALARVLYDAGLRTGDVVAL-LSDNSpEALVVLWAALRSGLYITAINH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 117 PPTYAES-----SSGTQKLKdAWTLLDkpAVITDRGMHQEM-LDWAKEqgLEGFRAIivEDLLSAEADTDWHQSSPedlA 190
Cdd:PRK13390 82 HLTAPEAdyivgDSGARVLV-ASAALD--GLAAKVGADLPLrLSFGGE--IDGFGSF--EAALAGAGPRLTEQPCG---A 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 191 LLLLTSGSTGTPKAVM--LNHRNIMSMVKGIIQMQ----GFTREDITFNWMPFDHVGGI---GMLHLrdvyLGCQEINVS 261
Cdd:PRK13390 152 VMLYSSGTTGFPKGIQpdLPGRDVDAPGDPIVAIArafyDISESDIYYSSAPIYHAAPLrwcSMVHA----LGGTVVLAK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 262 SetilMEPLKWLDWIDHYRASVTWAPNFAFGLVTDFAEEIKDRkWDLSSMRYMLNGGEAMVAKVGRRILELLEPHGLPAD 341
Cdd:PRK13390 228 R----FDAQATLGHVERYRITVTQMVPTMFVRLLKLDADVRTR-YDVSSLRAVIHAAAPCPVDVKHAMIDWLGPIVYEYY 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 342 AIRPAWGMSETSSGVIFSHEFTragtsdddhfveIGSPIPGfSMRIVNDHNELVEEGEIGRFQVSGLSVTSGYYQRPDLN 421
Cdd:PRK13390 303 SSTEAHGMTFIDSPDWLAHPGS------------VGRSVLG-DLHICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKT 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 422 ESVF--TEDGWFETGDLGFL-RNGRLTITGRTKDAIIINGINYYSHAIESAVEELSEI-ETSYTAACAVRLGQNStdQLA 497
Cdd:PRK13390 370 AAAQhpAHPFWTTVGDLGSVdEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVhDVAVIGVPDPEMGEQV--KAV 447
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1776025254 498 IFFVTSAKLNDEQMSQLLRNIQSHVSQvigvtpeYLLPVQKE---EIPKTAIGKIQRTQLK 555
Cdd:PRK13390 448 IQLVEGIRGSDELARELIDYTRSRIAH-------YKAPRSVEfvdELPRTPTGKLVKGLLR 501
|
|
| CLF |
cd00832 |
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ... |
4591-4896 |
7.93e-10 |
|
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic antibiotic-producing polyketide synthases (PKSs) of filamentous bacteria. CLFs have been shown to have decarboxylase activity towards malonyl-acyl carrier protein (ACP). CLFs are similar to other elongation ketosynthase domains, but their active site cysteine is replaced by a conserved glutamine.
Pssm-ID: 238428 [Multi-domain] Cd Length: 399 Bit Score: 64.69 E-value: 7.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4591 AVVGLSCRFPGAETLESYWSLLSEGRSSIGPIpaERWGCkTPYYAGVIDGVSYFDPDFF----LLHEEDVraMDPQALLV 4666
Cdd:cd00832 4 VVTGIGVVAPNGLGVEEYWKAVLDGRSGLGPI--TRFDP-SGYPARLAGEVPDFDAAEHlpgrLLPQTDR--MTRLALAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4667 LEECLKllyHAGYTPEEIKGKPVGVY---------IGGRSQHKPDEDSLDHaknpiVTVGQNY---LAANLSQF---FDV 4731
Cdd:cd00832 79 ADWALA---DAGVDPAALPPYDMGVVtasaaggfeFGQRELQKLWSKGPRH-----VSAYQSFawfYAVNTGQIsirHGM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4732 RGPSVVVDTACSSALVGMNMAIQALRGGDiQSAIVGGV-------SLLSSDASHRLFD----RRGILSkhssfhvFDERA 4800
Cdd:cd00832 151 RGPSGVVVAEQAGGLDALAQARRLVRRGT-PLVVSGGVdsalcpwGWVAQLSSGRLSTsddpARAYLP-------FDAAA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4801 DGVVLGEGVGMVMLKTVKQALEDGDTIYAVVKAASVNNDGRTAGPATPNLEAqkeVMKDALFKSGKKPEDISYLEANGSG 4880
Cdd:cd00832 223 AGYVPGEGGAILVLEDAAAARERGARVYGEIAGYAATFDPPPGSGRPPGLAR---AIRLALADAGLTPEDVDVVFADAAG 299
|
330
....*....|....*.
gi 1776025254 4881 SIVTDLLELKAIQSVY 4896
Cdd:cd00832 300 VPELDRAEAAALAAVF 315
|
|
| MDH-like_SDR_c |
cd05352 |
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ... |
2850-3000 |
9.83e-10 |
|
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes the conversion of fructose to mannitol, an acyclic 6-carbon sugar. MDH is a tetrameric member of the SDR family. This subgroup also includes various other tetrameric SDRs, including Pichia stipitis D-arabinitol dehydrogenase (aka polyol dehydrogenase), Candida albicans Sou1p, a sorbose reductase, and Candida parapsilosis (S)-specific carbonyl reductase (SCR, aka S-specific alcohol dehydrogenase) which catalyzes the enantioselective reduction of 2-hydroxyacetophenone into (S)-1-phenyl-1,2-ethanediol. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser).
Pssm-ID: 187610 [Multi-domain] Cd Length: 252 Bit Score: 62.73 E-value: 9.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGLLFAKEIAnRTGRSTIVLTGRSVLSEDKENELEalRSIGAEVVYREADVSDQHAVHHLFEEIKERYGT 2929
Cdd:cd05352 10 VAIVTGGSRGIGLAIARALA-EAGADVAIIYNSAPRAEEKAEELA--KKYGVKTKAYKCDVSSQESVEKTFKQIQKDFGK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2930 LNGIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSGLLHvdeCSKDFPLDF-------FIFFSSVSGCLGNAGQ--ADYAAA 3000
Cdd:cd05352 87 IDILIANAGITVHKPALDYTYEQWNKVIDVNLNGVFN---CAQAAAKIFkkqgkgsLIITASMSGTIVNRPQpqAAYNAS 163
|
|
| SPR-like_SDR_c |
cd05367 |
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ... |
2850-3009 |
1.35e-09 |
|
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, catalyzes the NADP-dependent reduction of sepiaptern to 7,8-dihydrobiopterin (BH2). In addition to SPRs, this subgroup also contains Bacillus cereus yueD, a benzil reductase, which catalyzes the stereospecific reduction of benzil to (S)-benzoin. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.
Pssm-ID: 187625 [Multi-domain] Cd Length: 241 Bit Score: 61.92 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGLLFAKEIANRTGRSTIVLTGRSvlsEDKENELEALRSIGAEVVYREADVSDQHAVHHLFEEIKERYGT 2929
Cdd:cd05367 1 VIILTGASRGIGRALAEELLKRGSPSVVVLLARS---EEPLQELKEELRPGLRVTTVKADLSDAAGVEQLLEAIRKLDGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2930 LNGIIHGAGSIKDHFIIHKTN-EEFQEVLQPKV-SGLLHVDECSKDFPLDFF----IFFSSVSGCLGNAGQADY----AA 2999
Cdd:cd05367 78 RDLLINNAGSLGPVSKIEFIDlDELQKYFDLNLtSPVCLTSTLLRAFKKRGLkktvVNVSSGAAVNPFKGWGLYcsskAA 157
|
170
....*....|
gi 1776025254 3000 ANSFMDAFAE 3009
Cdd:cd05367 158 RDMFFRVLAA 167
|
|
| fabG |
PRK12825 |
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional |
4172-4341 |
1.37e-09 |
|
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
Pssm-ID: 237218 [Multi-domain] Cd Length: 249 Bit Score: 62.19 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4172 VLLITGGTRGIGLLCARHFAecygvkklvltgreqlppREEWARFKTSNTSLAEKIQAVRELEAKGVQVEMLSLTLSDDA 4251
Cdd:PRK12825 8 VALVTGAARGLGRAIALRLA------------------RAGADVVVHYRSDEEAAEELVEAVEALGRRAQAVQADVTDKA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4252 QVEQTLQHIKRTLGPIGGVIHCAGLTDMDTLAfiRKTSDDIQRVMEPKVSGLTTLYRHVCneP----LQF--FVLFSSVS 4325
Cdd:PRK12825 70 ALEAAVAAAVERFGRIDILVNNAGIFEDKPLA--DMSDDEWDEVIDVNLSGVFHLLRAVV--PpmrkQRGgrIVNISSVA 145
|
170
....*....|....*.
gi 1776025254 4326 AIIpeLSAGQADYAMA 4341
Cdd:PRK12825 146 GLP--GWPGRSNYAAA 159
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
1522-1639 |
1.91e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 63.52 E-value: 1.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1522 GSKLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMDNLA-----AYYTAKHanaS 1596
Cdd:PRK08308 289 GDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAgervkAKVISHE---E 365
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1776025254 1597 LTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLK 1639
Cdd:PRK08308 366 IDPVQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLLE 408
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
599-657 |
3.02e-09 |
|
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.
Pssm-ID: 425746 [Multi-domain] Cd Length: 62 Bit Score: 56.03 E-value: 3.02e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1776025254 599 LLTCLTEELHVSRDWVEPNANIQSLGVNSIKMMKLIRSIEKNYHIKLTAREIHQYPTIE 657
Cdd:pfam00550 3 LRELLAEVLGVPAEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLA 61
|
|
| 17beta-HSD-like_SDR_c |
cd05374 |
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ... |
2850-3022 |
3.65e-09 |
|
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.
Pssm-ID: 187632 [Multi-domain] Cd Length: 248 Bit Score: 60.71 E-value: 3.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGLLFAKEIANR------TGRSTIVLtgrsvlsedkeNELEALRSIGAEVVyrEADVSDQHAVHHLFEEI 2923
Cdd:cd05374 2 VVLITGCSSGIGLALALALAAQgyrviaTARNPDKL-----------ESLGELLNDNLEVL--ELDVTDEESIKAAVKEV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2924 KERYGTLNGIIHGAGsikdhfIIHK------TNEEFQEVLQPKVSGLLHVdecSKDFpLDFF--------IFFSSVSGCL 2989
Cdd:cd05374 69 IERFGRIDVLVNNAG------YGLFgpleetSIEEVRELFEVNVFGPLRV---TRAF-LPLMrkqgsgriVNVSSVAGLV 138
|
170 180 190
....*....|....*....|....*....|...
gi 1776025254 2990 GNAGQADYAAANSFMDAFAEyrrSLAASKKRFG 3022
Cdd:cd05374 139 PTPFLGPYCASKAALEALSE---SLRLELAPFG 168
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
268-555 |
4.00e-09 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 62.87 E-value: 4.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 268 EPLKWLDWIDHYRASVTWAPNFAFGLVT--DFAeeikdrKWDLSSMRYMLNGGEAMVAKVgrrILELLEPHGLpadAIRP 345
Cdd:cd05928 254 DPLVILKTLSSYPITTFCGAPTVYRMLVqqDLS------SYKFPSLQHCVTGGEPLNPEV---LEKWKAQTGL---DIYE 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 346 AWGMSETssGVI---FSHEFTRAGTsdddhfveIGSPIPGFSMRIVNDHNELV---EEGEIG-RFQ-VSGLSVTSGYYQR 417
Cdd:cd05928 322 GYGQTET--GLIcanFKGMKIKPGS--------MGKASPPYDVQIIDDNGNVLppgTEGDIGiRVKpIRPFGLFSGYVDN 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 418 PDLNESVFTEDGWFeTGDLGFL-RNGRLTITGRTKDAIIINGINYYSHAIESAVeelseIETSYTAACAVrlgQNSTDQL 496
Cdd:cd05928 392 PEKTAATIRGDFYL-TGDRGIMdEDGYFWFMGRADDVINSSGYRIGPFEVESAL-----IEHPAVVESAV---VSSPDPI 462
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1776025254 497 -----AIFFVTSAKLNDEQMSQLLRNIQSHVSQVigvTPEYLLPVQKE---EIPKTAIGKIQRTQLK 555
Cdd:cd05928 463 rgevvKAFVVLAPQFLSHDPEQLTKELQQHVKSV---TAPYKYPRKVEfvqELPKTVTGKIQRNELR 526
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
1179-1639 |
4.15e-09 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 62.79 E-value: 4.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1179 LTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLEDS--------- 1249
Cdd:PRK12406 12 RSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSgarvliaha 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1250 --------------EVFITLTTSELvntLSWNGVTTALL-----DQDWDE--IAQTASDRkvlTRTVTPENLayvIYTSG 1308
Cdd:PRK12406 92 dllhglasalpagvTVLSVPTPPEI---AAAYRISPALLtppagAIDWEGwlAQQEPYDG---PPVPQPQSM---IYTSG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1309 STGKPKGVM----IPHKALTNFLV---SMGETPGLTA--EDKMLAVTTYCFDIAALELflplikgAHCYICQTEHtkDVE 1379
Cdd:PRK12406 163 TTGHPKGVRraapTPEQAAAAEQMralIYGLKPGIRAllTGPLYHSAPNAYGLRAGRL-------GGVLVLQPRF--DPE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1380 KLKRDIRTIKPTVMQATPAtwkmLFYSGWENEENVK----------ILCGGEALPETLKRYFLDT-GSEAWNMFGPTETt 1448
Cdd:PRK12406 234 ELLQLIERHRITHMHMVPT----MFIRLLKLPEEVRakydvsslrhVIHAAAPCPADVKRAMIEWwGPVIYEYYGSTES- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1449 iwSAVQRINDECSRA---TIGRPIANTQIYITDSQLAPVPAGVPGELCIAGDGVAKGYY-----KKEELTDSRFIDnpfe 1520
Cdd:PRK12406 309 --GAVTFATSEDALShpgTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDFTYhnkpeKRAEIDRGGFIT---- 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1521 pgsklyrTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVV--VADMD---NLAAyYTAKHANA 1595
Cdd:PRK12406 383 -------SGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVfgIPDAEfgeALMA-VVEPQPGA 454
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1776025254 1596 SLTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLK 1639
Cdd:PRK12406 455 TLDEADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLR 498
|
|
| PRK12935 |
PRK12935 |
acetoacetyl-CoA reductase; Provisional |
2850-3046 |
4.71e-09 |
|
acetoacetyl-CoA reductase; Provisional
Pssm-ID: 183832 [Multi-domain] Cd Length: 247 Bit Score: 60.40 E-value: 4.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGLLFAKEIANRTGRstiVLTGRSVLSEDKENELEALRSIGAEVVYREADVSDQHAVHHLFEEIKERYGT 2929
Cdd:PRK12935 8 VAIVTGGAKGIGKAITVALAQEGAK---VVINYNSSKEAAENLVNELGKEGHDVYAVQADVSKVEDANRLVEEAVNHFGK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2930 LNGIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSGLLHVDECSKDFPLDF----FIFFSSVSGCLGNAGQADYAAANSFMD 3005
Cdd:PRK12935 85 VDILVNNAGITRDRTFKKLNREDWERVIDVNLSSVFNTTSAVLPYITEAeegrIISISSIIGQAGGFGQTNYSAAKAGML 164
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1776025254 3006 AFAeyrRSLAASKKRFGSTISFNWPLWEEGGMQVGAEDEKR 3046
Cdd:PRK12935 165 GFT---KSLALELAKTNVTVNAICPGFIDTEMVAEVPEEVR 202
|
|
| E-C_NRPS |
cd19544 |
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ... |
801-988 |
6.98e-09 |
|
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); Dual function Epimerization/Condensation (E/C) domains have both an epimerization and a DCL condensation activity. Dual E/C domains first epimerize the substrate amino acid to produce a D-configuration, then catalyze the condensation between the D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. They are D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. These Dual E/C domains contain an extended His-motif (HHx(N)GD) near the N-terminus of the domain in addition to the standard Condensation (C) domain active site motif (HHxxxD). C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains, these include the DCL-type, LCL-type, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C domains, and the X-domain.
Pssm-ID: 380466 [Multi-domain] Cd Length: 413 Bit Score: 61.68 E-value: 6.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 801 PLVRV-MSFSRSEQEHFLLVVIHHLIFDGVSsvtfIHSLFDTYQLLLKGQQPEIAVsPAIYHDFAAwekNMLAGKDGVKH 879
Cdd:cd19544 111 PLLRAhVAEDPANGRWLLLLLFHHLISDHTS----LELLLEEIQAILAGRAAALPP-PVPYRNFVA---QARLGASQAEH 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 880 RTYWQKQLSG----TLP-NLQLPKVSASSVSEFRedtytRRLSSGFMNQVRMFAKEHSVNVTTVFLSCYMMLLGRYTGQK 954
Cdd:cd19544 183 EAFFREMLGDvdepTAPfGLLDVQGDGSDITEAR-----LALDAELAQRLRAQARRLGVSPASLFHLAWALVLARCSGRD 257
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1776025254 955 EQIVG------MPAMvrpeERFDDAIGHFLNMLPIRSELN 988
Cdd:cd19544 258 DVVFGtvlsgrMQGG----AGADRALGMFINTLPLRVRLG 293
|
|
| PRK06198 |
PRK06198 |
short chain dehydrogenase; Provisional |
4170-4282 |
7.90e-09 |
|
short chain dehydrogenase; Provisional
Pssm-ID: 180462 [Multi-domain] Cd Length: 260 Bit Score: 60.02 E-value: 7.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4170 DHVLLITGGTRGIGLLCARHFAEcYGVKKLVLTGREQLPPReewarfktsntslaekiQAVRELEAKGVQVEMLSLTLSD 4249
Cdd:PRK06198 6 GKVALVTGGTQGLGAAIARAFAE-RGAAGLVICGRNAEKGE-----------------AQAAELEALGAKAVFVQADLSD 67
|
90 100 110
....*....|....*....|....*....|...
gi 1776025254 4250 DAQVEQTLQHIKRTLGPIGGVIHCAGLTDMDTL 4282
Cdd:PRK06198 68 VEDCRRVVAAADEAFGRLDALVNAAGLTDRGTI 100
|
|
| AcpP |
COG0236 |
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ... |
3219-3281 |
8.26e-09 |
|
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440006 [Multi-domain] Cd Length: 80 Bit Score: 55.24 E-value: 8.26e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1776025254 3219 NMVSAILKVNSEDIDVNTEL-SEYGFDSVTFTVFTNKINEEFQLELTPTIFFEYGSIHSLAEYL 3281
Cdd:COG0236 12 EIIAEVLGVDPEEITPDDSFfEDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYL 75
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
185-470 |
8.91e-09 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 60.86 E-value: 8.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 185 SPEDLaLLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQgfTREDITFNWM----------------PFDHvgGIGMLHL 248
Cdd:cd05924 2 SADDL-YILYTGGTTGMPKGVMWRQEDIFRMLMGGADFG--TGEFTPSEDAhkaaaaaagtvmfpapPLMH--GTGSWTA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 249 RDVYLGCQEINVSSETILMEPLkwldWIDHYRASVTWAPnfafgLVTD-FA----EEIKDRK-WDLSSMRYMLNGGEAMV 322
Cdd:cd05924 77 FGGLLGGQTVVLPDDRFDPEEV----WRTIEKHKVTSMT-----IVGDaMArpliDALRDAGpYDLSSLFAISSGGALLS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 323 AKVGRRILELLePHGLPADAIrpawGMSETSSGVIFS-----HE---FTRAG-----TSDDDHFVEIGSPIPGFsmrivn 389
Cdd:cd05924 148 PEVKQGLLELV-PNITLVDAF----GSSETGFTGSGHsagsgPEtgpFTRANpdtvvLDDDGRVVPPGSGGVGW------ 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 390 dhnelveegeIGRfqvSGLsVTSGYYQRPDLNESVFTE-DG--WFETGDLG-FLRNGRLTITGRtkDAIIIN--GINYYS 463
Cdd:cd05924 217 ----------IAR---RGH-IPLGYYGDEAKTAETFPEvDGvrYAVPGDRAtVEADGTVTLLGR--GSVCINtgGEKVFP 280
|
....*..
gi 1776025254 464 HAIESAV 470
Cdd:cd05924 281 EEVEEAL 287
|
|
| HSD10-like_SDR_c |
cd05371 |
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ... |
2850-2999 |
9.94e-09 |
|
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as amyloid-peptide-binding alcohol dehydrogenase (ABAD), was previously identified as a L-3-hydroxyacyl-CoA dehydrogenase, HADH2. In fatty acid metabolism, HADH2 catalyzes the third step of beta-oxidation, the conversion of a hydroxyl to a keto group in the NAD-dependent oxidation of L-3-hydroxyacyl CoA. In addition to alcohol dehydrogenase and HADH2 activites, HSD10 has steroid dehydrogenase activity. Although the mechanism is unclear, HSD10 is implicated in the formation of amyloid beta-petide in the brain (which is linked to the development of Alzheimer's disease). Although HSD10 is normally concentrated in the mitochondria, in the presence of amyloid beta-peptide it translocates into the plasma membrane, where it's action may generate cytotoxic aldehydes and may lower estrogen levels through its use of 17-beta-estradiol as a substrate. HSD10 is a member of the SRD family, but differs from other SDRs by the presence of two insertions of unknown function. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.
Pssm-ID: 187629 [Multi-domain] Cd Length: 252 Bit Score: 59.61 E-value: 9.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGLLFAKEIANRtGRSTIVLTgrsvLSEDKENELEALrsiGAEVVYREADVSDQHAVHHLFEEIKERYGT 2929
Cdd:cd05371 4 VAVVTGGASGLGLATVERLLAQ-GAKVVILD----LPNSPGETVAKL---GDNCRFVPVDVTSEKDVKAALALAKAKFGR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2930 LNGIIHGAGSIKDHFIIHKTN------EEFQEVLQPKVSGLLHVDECSKDF-----PLDF-----FIFFSSVSGCLGNAG 2993
Cdd:cd05371 76 LDIVVNCAGIAVAAKTYNKKGqqphslELFQRVINVNLIGTFNVIRLAAGAmgknePDQGgergvIINTASVAAFEGQIG 155
|
....*.
gi 1776025254 2994 QADYAA 2999
Cdd:cd05371 156 QAAYSA 161
|
|
| KAsynt_C_assoc |
pfam16197 |
Ketoacyl-synthetase C-terminal extension; KAsynt_C_assoc represents the very C-terminus of a ... |
2138-2249 |
1.20e-08 |
|
Ketoacyl-synthetase C-terminal extension; KAsynt_C_assoc represents the very C-terminus of a subset of proteins from the keto-acyl-synthetase 2 family. It is found in proteins ranging from bacteria to human.
Pssm-ID: 465059 [Multi-domain] Cd Length: 111 Bit Score: 56.01 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2138 PNPNTD-LASSPFYVVDQKKTLSREIqthrAALSSFGLGGTNTHAIFEQFKR--DSDKGKIDGTCIVPISAKNKERLQEY 2214
Cdd:pfam16197 1 PNPDIPaLLDGRLKVVTEPTPWPGGI----VGVNSFGFGGANAHVILKSNPKpkIPPESPDNLPRLVLLSGRTEEAVKAL 76
|
90 100 110
....*....|....*....|....*....|....*
gi 1776025254 2215 AEDILAYLerrgLENSQLPDFAYTLQVGREAMEHR 2249
Cdd:pfam16197 77 LEKLENHL----DDAEFLSLLNDIHSLPISGHPYR 107
|
|
| Ga5DH-like_SDR_c |
cd05347 |
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ... |
2850-2957 |
1.55e-08 |
|
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent conversion of carbon source D-gluconate and 5-keto-D-gluconate. This SDR subgroup has a classical Gly-rich NAD(P)-binding motif and a conserved active site tetrad pattern. However, it has been proposed that Arg104 (Streptococcus suis Ga5DH numbering), as well as an active site Ca2+, play a critical role in catalysis. In addition to Ga5DHs this subgroup contains Erwinia chrysanthemi KduD which is involved in pectin degradation, and is a putative 2,5-diketo-3-deoxygluconate dehydrogenase. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107,15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.
Pssm-ID: 187605 [Multi-domain] Cd Length: 248 Bit Score: 58.91 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGLLFAKEIANRTgrSTIVLTGRSvlSEDKENELEALRSIGAEVVYREADVSDQHAVHHLFEEIKERYGT 2929
Cdd:cd05347 7 VALVTGASRGIGFGIASGLAEAG--ANIVINSRN--EEKAEEAQQLIEKEGVEATAFTCDVSDEEAIKAAVEAIEEDFGK 82
|
90 100
....*....|....*....|....*...
gi 1776025254 2930 LNGIIHGAGSIKDHFIIHKTNEEFQEVL 2957
Cdd:cd05347 83 IDILVNNAGIIRRHPAEEFPEAEWRDVI 110
|
|
| PRK12829 |
PRK12829 |
short chain dehydrogenase; Provisional |
2852-3056 |
1.56e-08 |
|
short chain dehydrogenase; Provisional
Pssm-ID: 183778 [Multi-domain] Cd Length: 264 Bit Score: 59.30 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2852 LITGGAGSLGLLFAKEIANRTGRstIVLTGRSvlsedkENELEALRSI--GAEVVYREADVSDQHAVHHLFEEIKERYGT 2929
Cdd:PRK12829 15 LVTGGASGIGRAIAEAFAEAGAR--VHVCDVS------EAALAATAARlpGAKVTATVADVADPAQVERVFDTAVERFGG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2930 LNGIIHGAGSIKDHFIIHK-TNEEFQEVLQPKVSGLLHVdeCSKDFPL-------DFFIFFSSVSGCLGNAGQADYAAAN 3001
Cdd:PRK12829 87 LDVLVNNAGIAGPTGGIDEiTPEQWEQTLAVNLNGQFYF--ARAAVPLlkasghgGVIIALSSVAGRLGYPGRTPYAASK 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1776025254 3002 SfmdAFAEYRRSLAASKKRFGSTISFNWPLWEEGGMQVGAEDEKRMLKTTGMVPM 3056
Cdd:PRK12829 165 W---AVVGLVKSLAIELGPLGIRVNAILPGIVRGPRMRRVIEARAQQLGIGLDEM 216
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
1294-1584 |
1.90e-08 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 60.16 E-value: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1294 TVTPENLAYVIYTSGSTGKPKGVmiphkaltnflvsmgetpGLTAEDkmLAVTTYCF------------DIA----ALEL 1357
Cdd:COG1541 79 AVPLEEIVRIHASSGTTGKPTVV------------------GYTRKD--LDRWAELFarslraagvrpgDRVqnafGYGL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1358 F---LPLIKGAH---CYIC-----QTEHTKDVeklkrdIRTIKPTVMQATPatWKMLFYSGWENEENV--------KILC 1418
Cdd:COG1541 139 FtggLGLHYGAErlgATVIpagggNTERQLRL------MQDFGPTVLVGTP--SYLLYLAEVAEEEGIdprdlslkKGIF 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1419 GGEALPETLKRYFLDT-GSEAWNMFGPTETTIWSAVQ-------RINDECSRATIGRPiaNTqiyitdsqLAPVPAGVPG 1490
Cdd:COG1541 211 GGEPWSEEMRKEIEERwGIKAYDIYGLTEVGPGVAYEceaqdglHIWEDHFLVEIIDP--ET--------GEPVPEGEEG 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1491 ELCIAGdgvakgyykkeeLTDSrfidnpfepGSKL--YRTGDMARWLPG----G----RIEYI-GRIDNQVKIRGFRIEL 1559
Cdd:COG1541 281 ELVVTT------------LTKE---------AMPLirYRTGDLTRLLPEpcpcGrthpRIGRIlGRADDMLIIRGVNVFP 339
|
330 340 350
....*....|....*....|....*....|
gi 1776025254 1560 GDIESRLSEHPGIL-ECVVVAD----MDNL 1584
Cdd:COG1541 340 SQIEEVLLRIPEVGpEYQIVVDreggLDEL 369
|
|
| PKS_PP |
smart00823 |
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ... |
1658-1727 |
1.90e-08 |
|
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.
Pssm-ID: 214834 [Multi-domain] Cd Length: 86 Bit Score: 54.56 E-value: 1.90e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1776025254 1658 IQDTVFTIWQEVLKTSD---IEWDDGFFDVGGDSLLAVTVADRIKHELSCEFSVTDLFEYSTIKNISQYITEQ 1727
Cdd:smart00823 13 LLDLVREQVAAVLGHAAaeaIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHLAAE 85
|
|
| 3beta-17beta-HSD_like_SDR_c |
cd05341 |
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ... |
2850-3000 |
1.91e-08 |
|
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes members identified as 3beta17beta hydroxysteroid dehydrogenase, 20beta hydroxysteroid dehydrogenase, and R-alcohol dehydrogenase. These proteins exhibit the canonical active site tetrad and glycine rich NAD(P)-binding motif of the classical SDRs. 17beta-dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens, and include members of the SDR family. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.
Pssm-ID: 187600 [Multi-domain] Cd Length: 247 Bit Score: 58.55 E-value: 1.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGLLFAKEIAnRTGrSTIVLTgrSVLSEDKEnelEALRSIGAEVVYREADVSDQHAVHHLFEEIKERYGT 2929
Cdd:cd05341 7 VAIVTGGARGLGLAHARLLV-AEG-AKVVLS--DILDEEGQ---AAAAELGDAARFFHLDVTDEDGWTAVVDTAREAFGR 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1776025254 2930 LNGIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSGLL----HVDECSKDFPLDFFIFFSSVSGCLGNAGQADYAAA 3000
Cdd:cd05341 80 LDVLVNNAGILTGGTVETTTLEEWRRLLDINLTGVFlgtrAVIPPMKEAGGGSIINMSSIEGLVGDPALAAYNAS 154
|
|
| BKR_SDR_c |
cd05333 |
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ... |
4172-4341 |
2.01e-08 |
|
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; This subgroup includes the Escherichai coli K12 BKR, FabG. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet) NAD(P)(H) binding region and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H) binding pattern: TGxxxGxG in classical SDRs. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P) binding motif and an altered active site motif (YXXXN). Fungal type type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P) binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr-151 and Lys-155, and well as Asn-111 (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.
Pssm-ID: 187594 [Multi-domain] Cd Length: 240 Bit Score: 58.33 E-value: 2.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4172 VLLITGGTRGIGLLCARHFAEcYGVKkLVLTGReqlppreewarfktSNTSLAEKIQAVRELeakGVQVEMLSLTLSDDA 4251
Cdd:cd05333 2 VALVTGASRGIGRAIALRLAA-EGAK-VAVTDR--------------SEEAAAETVEEIKAL---GGNAAALEADVSDRE 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4252 QVEQTLQHIKRTLGPIGGVIHCAGLTdMDTLaFIRKTSDDIQRVMEpkvSGLTTLYRhvCNEPL------QFF---VLFS 4322
Cdd:cd05333 63 AVEALVEKVEAEFGPVDILVNNAGIT-RDNL-LMRMSEEDWDAVIN---VNLTGVFN--VTQAViramikRRSgriINIS 135
|
170
....*....|....*....
gi 1776025254 4323 SVSAIIPelSAGQADYAMA 4341
Cdd:cd05333 136 SVVGLIG--NPGQANYAAS 152
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
186-470 |
2.03e-08 |
|
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.
Pssm-ID: 341252 [Multi-domain] Cd Length: 473 Bit Score: 60.47 E-value: 2.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 186 PEDLA---LLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQ---MQGFTREDITFNWMPFDHVGGIG--MLHLRdvyLGCQe 257
Cdd:cd05929 121 IEDEAagwKMLYSGGTTGRPKGIKRGLPGGPPDNDTLMAaalGFGPGADSVYLSPAPLYHAAPFRwsMTALF---MGGT- 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 258 invsseTILME---PLKWLDWIDHYRasVTWApNFA---FGLVTDFAEEIKDrKWDLSSMRYMLNGGEAMVAKVGRRILE 331
Cdd:cd05929 197 ------LVLMEkfdPEEFLRLIERYR--VTFA-QFVptmFVRLLKLPEAVRN-AYDLSSLKRVIHAAAPCPPWVKEQWID 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 332 LLEPhglpadAIRPAWGMSETS-SGVIFSHEF-TRAGTsdddhfveIGSPIPGfSMRIVNDHNELVEEGEIGRFQVSGlS 409
Cdd:cd05929 267 WGGP------IIWEYYGGTEGQgLTIINGEEWlTHPGS--------VGRAVLG-KVHILDEDGNEVPPGEIGEVYFAN-G 330
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1776025254 410 VTSGYYQRPDLNESVFTEDGWFETGDLGFL-RNGRLTITGRTKDAIIINGINYYSHAIESAV 470
Cdd:cd05929 331 PGFEYTNDPEKTAAARNEGGWSTLGDVGYLdEDGYLYLTDRRSDMIISGGVNIYPQEIENAL 392
|
|
| KAsynt_C_assoc |
pfam16197 |
Ketoacyl-synthetase C-terminal extension; KAsynt_C_assoc represents the very C-terminus of a ... |
3726-3844 |
2.04e-08 |
|
Ketoacyl-synthetase C-terminal extension; KAsynt_C_assoc represents the very C-terminus of a subset of proteins from the keto-acyl-synthetase 2 family. It is found in proteins ranging from bacteria to human.
Pssm-ID: 465059 [Multi-domain] Cd Length: 111 Bit Score: 55.24 E-value: 2.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3726 NPYLQ-LTDSPFYIVQEKQEWKsvtdcdgnelPRRAGISSFGIGGVNAHIVIEEYMPKANSEHTATEQPNVIVLSAKNKS 3804
Cdd:pfam16197 2 NPDIPaLLDGRLKVVTEPTPWP----------GGIVGVNSFGFGGANAHVILKSNPKPKIPPESPDNLPRLVLLSGRTEE 71
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1776025254 3805 RLidraSQLLEAIRNKKYTDQGLHRIAYTLQVGREEMDER 3844
Cdd:pfam16197 72 AV----KALLEKLENHLDDAEFLSLLNDIHSLPISGHPYR 107
|
|
| PRK12826 |
PRK12826 |
SDR family oxidoreductase; |
2850-3008 |
2.36e-08 |
|
SDR family oxidoreductase;
Pssm-ID: 183775 [Multi-domain] Cd Length: 251 Bit Score: 58.39 E-value: 2.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGLLFAKEIAnRTGrSTIVLTGRSvlSEDKENELEALRSIGAEVVYREADVSDQHAVHHLFEEIKERYGT 2929
Cdd:PRK12826 8 VALVTGAARGIGRAIAVRLA-ADG-AEVIVVDIC--GDDAAATAELVEAAGGKARARQVDVRDRAALKAAVAAGVEDFGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2930 LNGIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSGLLHVDECS----KDFPLDFFIFFSSVSG-CLGNAGQADYAAA---- 3000
Cdd:PRK12826 84 LDILVANAGIFPLTPFAEMDDEQWERVIDVNLTGTFLLTQAAlpalIRAGGGRIVLTSSVAGpRVGYPGLAHYAASkagl 163
|
....*...
gi 1776025254 3001 NSFMDAFA 3008
Cdd:PRK12826 164 VGFTRALA 171
|
|
| SDR_c5 |
cd05346 |
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ... |
4173-4310 |
2.58e-08 |
|
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.
Pssm-ID: 187604 [Multi-domain] Cd Length: 249 Bit Score: 58.45 E-value: 2.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4173 LLITGGTRGIGLLCARHFAEcyGVKKLVLTGREqlppreewarfktsntslAEKIQAVR-ELEAK-GVQVEMLSLTLSDD 4250
Cdd:cd05346 3 VLITGASSGIGEATARRFAK--AGAKLILTGRR------------------AERLQELAdELGAKfPVKVLPLQLDVSDR 62
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1776025254 4251 AQVEQTLQHIKRTLGPIGGVIHCAGLT-DMDTLAFIRKtsDDIQRVMEPKVSGLTTLYRHV 4310
Cdd:cd05346 63 ESIEAALENLPEEFRDIDILVNNAGLAlGLDPAQEADL--EDWETMIDTNVKGLLNVTRLI 121
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
1177-1403 |
3.70e-08 |
|
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341256 [Multi-domain] Cd Length: 596 Bit Score: 60.06 E-value: 3.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1177 QTLTYRELDERSTQLAIYL------QAHGVGpdrlagIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLEDSE 1250
Cdd:cd05933 7 HTLTYKEYYEACRQAAKAFlklgleRFHGVG------ILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1251 VFITLTTSE---------------LVNTLSWNGVTTALLDQ--DWDEIAQTA---SDRKVLTR--TVTPENLAYVIYTSG 1308
Cdd:cd05933 81 ANILVVENQkqlqkilqiqdklphLKAIIQYKEPLKEKEPNlySWDEFMELGrsiPDEQLDAIisSQKPNQCCTLIYTSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1309 STGKPKGVMIPHKALTNFLVSMGETPGL-TAEDKMLAVTTY---CFdIAA--LELFLPLIKGAHCYICQtehtKDVEK-- 1380
Cdd:cd05933 161 TTGMPKGVMLSHDNITWTAKAASQHMDLrPATVGQESVVSYlplSH-IAAqiLDIWLPIKVGGQVYFAQ----PDALKgt 235
|
250 260
....*....|....*....|....
gi 1776025254 1381 LKRDIRTIKPTVMQATPATW-KML 1403
Cdd:cd05933 236 LVKTLREVRPTAFMGVPRVWeKIQ 259
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
400-556 |
3.87e-08 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 59.86 E-value: 3.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 400 IGRFQVSGLSVTSGYYQRPDLNESVFtEDGWFETGDLGFLR-NGRLTITGRTKDAIIINGINYYSHAIESAVEELSEI-E 477
Cdd:PLN02479 402 MGEIVMRGNMVMKGYLKNPKANEEAF-ANGWFHSGDLGVKHpDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVlE 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 478 TSYTAACAVRLGQNSTDqlaifFVT---SAKLNDEQmsQLLRNIQSHVSQVIgvtPEYLLP--VQKEEIPKTAIGKIQRT 552
Cdd:PLN02479 481 ASVVARPDERWGESPCA-----FVTlkpGVDKSDEA--ALAEDIMKFCRERL---PAYWVPksVVFGPLPKTATGKIQKH 550
|
....
gi 1776025254 553 QLKT 556
Cdd:PLN02479 551 VLRA 554
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
1179-1323 |
4.25e-08 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 59.63 E-value: 4.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1179 LTYRELDERSTQLAIYLQAHGVGP-DRLAGIyVDRSLDMLVGLLAILKAGGAYVPLdP---------SYpAERLEYMLED 1248
Cdd:PRK09192 50 LPYQTLRARAEAGARRLLALGLKPgDRVALI-AETDGDFVEAFFACQYAGLVPVPL-PlpmgfggreSY-IAQLRGMLAS 126
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1776025254 1249 SEVFITLTTSELVNTLswNGVTTAL---LDQDWDEIAQTASDRKVLTRtVTPENLAYVIYTSGSTGKPKGVMIPHKAL 1323
Cdd:PRK09192 127 AQPAAIITPDELLPWV--NEATHGNpllHVLSHAWFKALPEADVALPR-PTPDDIAYLQYSSGSTRFPRGVIITHRAL 201
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
347-451 |
4.46e-08 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 59.60 E-value: 4.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 347 WGMSET-SSGVIfshefTRAGtsdDDHFVEIGSPIPGFSMRIVNdhnelVEE----------GEI---GRFqvsglsVTS 412
Cdd:PTZ00216 459 WGLTETvCCGGI-----QRTG---DLEPNAVGQLLKGVEMKLLD-----TEEykhtdtpeprGEIllrGPF------LFK 519
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1776025254 413 GYYQRPDLNESVFTEDGWFETGDLG-FLRNGRLTITGRTK 451
Cdd:PTZ00216 520 GYYKQEELTREVLDEDGWFHTGDVGsIAANGTLRIIGRVK 559
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
1297-1582 |
5.31e-08 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 59.73 E-value: 5.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1297 PENLAYVIYTSGSTGKPKGVMIPHKALTNFLV-----SMGETPGLTAEDKMLAVT-TYCFDIAalelFLPLIKGAHCYIC 1370
Cdd:PTZ00342 303 PDFITSIVYTSGTSGKPKGVMLSNKNLYNTVVplckhSIFKKYNPKTHLSYLPIShIYERVIA----YLSFMLGGTINIW 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1371 qtehTKDVEKLKRDIRTIKPTVMQATPATWKMLF----------------------------YSGW-----ENEENVK-- 1415
Cdd:PTZ00342 379 ----SKDINYFSKDIYNSKGNILAGVPKVFNRIYtnimteinnlpplkrflvkkilslrksnNNGGfskflEGITHISsk 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1416 -----------ILCGGEAL-PETLKRYFLDTGSEAWNMFGPTETTIWSAVQRINDeCSRATIGRPIA-NTQIYITDSQLA 1482
Cdd:PTZ00342 455 ikdkvnpnlevILNGGGKLsPKIAEELSVLLNVNYYQGYGLTETTGPIFVQHADD-NNTESIGGPISpNTKYKVRTWETY 533
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1483 PVPAGVP-GELCIAGDGVAKGYYKKEELTDSRFIDNPFepgsklYRTGDMARWLPGGRIEYIGRIDNQVKI-RGFRIELG 1560
Cdd:PTZ00342 534 KATDTLPkGELLIKSDSIFSGYFLEKEQTKNAFTEDGY------FKTGDIVQINKNGSLTFLDRSKGLVKLsQGEYIETD 607
|
330 340
....*....|....*....|....
gi 1776025254 1561 DIESRLSEHPGILECVVVAD--MD 1582
Cdd:PTZ00342 608 MLNNLYSQISFINFCVVYGDdsMD 631
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
170-457 |
5.68e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 59.13 E-value: 5.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 170 EDLLSA-EADTDWHQSSPEDLaLLLLTSGSTGTPKAVMLNHRNI-MSMVKGIIQMQGFTRED--------------ITFN 233
Cdd:PRK07798 146 EDALAAgSPERDFGERSPDDL-YLLYTGGTTGMPKGVMWRQEDIfRVLLGGRDFATGEPIEDeeelakraaagpgmRRFP 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 234 WMPFDHVGG-----IGMLhlrdvylgcqeinvSSETILMEPLKWLD----W--IDHYRASVtwapnfaFGLVTD-FA--- 298
Cdd:PRK07798 225 APPLMHGAGqwaafAALF--------------SGQTVVLLPDVRFDadevWrtIEREKVNV-------ITIVGDaMArpl 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 299 -EEIKDRK-WDLSSMRYMLNGGEAMVAKVGRRILELLePHGLPADAIrpawGMSETssGVIFSHEFTRAGTSDDDHFVEI 376
Cdd:PRK07798 284 lDALEARGpYDLSSLFAIASGGALFSPSVKEALLELL-PNVVLTDSI----GSSET--GFGGSGTVAKGAVHTGGPRFTI 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 377 GSpipgfSMRIVNDHNELVE--EGEIGRFQVSGlSVTSGYYQRPDLNESVFTE-DG--WFETGDLGFLRN-GRLTITGRt 450
Cdd:PRK07798 357 GP-----RTVVLDEDGNPVEpgSGEIGWIARRG-HIPLGYYKDPEKTAETFPTiDGvrYAIPGDRARVEAdGTITLLGR- 429
|
....*..
gi 1776025254 451 kDAIIIN 457
Cdd:PRK07798 430 -GSVCIN 435
|
|
| SPR-like_SDR_c |
cd05367 |
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ... |
4172-4349 |
5.74e-08 |
|
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, catalyzes the NADP-dependent reduction of sepiaptern to 7,8-dihydrobiopterin (BH2). In addition to SPRs, this subgroup also contains Bacillus cereus yueD, a benzil reductase, which catalyzes the stereospecific reduction of benzil to (S)-benzoin. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.
Pssm-ID: 187625 [Multi-domain] Cd Length: 241 Bit Score: 56.91 E-value: 5.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4172 VLLITGGTRGIGLLCARHFAECYGVKKLVLTGREQLPPREewarfktsntsLAEKIQAvreleakGVQVEMLSLTLSDDA 4251
Cdd:cd05367 1 VIILTGASRGIGRALAEELLKRGSPSVVVLLARSEEPLQE-----------LKEELRP-------GLRVTTVKADLSDAA 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4252 QVEQTLQHIKRTLGPIGGVIHCAG-LTDMDTLAFIrkTSDDIQRVMEPKVSG---LT-TLYRHVCNEPLQFFVLF-SSVS 4325
Cdd:cd05367 63 GVEQLLEAIRKLDGERDLLINNAGsLGPVSKIEFI--DLDELQKYFDLNLTSpvcLTsTLLRAFKKRGLKKTVVNvSSGA 140
|
170 180
....*....|....*....|....
gi 1776025254 4326 AIIPELSAGQadYAMANSYMDYFA 4349
Cdd:cd05367 141 AVNPFKGWGL--YCSSKAARDMFF 162
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
174-436 |
6.49e-08 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 59.14 E-value: 6.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 174 SAEADTDWhqSSPEDLALLLLTSGSTGTPKAVMLNHrNIMsmvkgIIQMQ-GFTREDitfnwmpfdhvggigmLHLRDVY 252
Cdd:PRK04319 194 SDEFDIEW--TDREDGAILHYTSGSTGKPKGVLHVH-NAM-----LQHYQtGKYVLD----------------LHEDDVY 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 253 ---------------------LGCQEINVSSEtilMEPLKWLDWIDHYRASVtW--APNfAFGLVTDFAEEIKdRKWDLS 309
Cdd:PRK04319 250 wctadpgwvtgtsygifapwlNGATNVIDGGR---FSPERWYRILEDYKVTV-WytAPT-AIRMLMGAGDDLV-KKYDLS 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 310 SMRYMLNGGEAM---VAKVGRRILellephGLPadaIRPAWGMSETSSGVIfsheftrAGTSDDDhfVEIGS---PIPGF 383
Cdd:PRK04319 324 SLRHILSVGEPLnpeVVRWGMKVF------GLP---IHDNWWMTETGGIMI-------ANYPAMD--IKPGSmgkPLPGI 385
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1776025254 384 SMRIVNDHNELVEEGEIGRFQV-SGL-SVTSGYYQRPDLNESVFtEDGWFETGDL 436
Cdd:PRK04319 386 EAAIVDDQGNELPPNRMGNLAIkKGWpSMMRGIWNNPEKYESYF-AGDWYVSGDS 439
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
192-551 |
8.25e-08 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 58.98 E-value: 8.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 192 LLLTSGSTGTPKAVM---------LNHRNIMSMVKGIIQMQgFTREDItfNWMPFdHVGGIGMLHLRDVYlgcqeinVSS 262
Cdd:PTZ00237 259 ILYTSGTTGNSKAVVrsngphlvgLKYYWRSIIEKDIPTVV-FSHSSI--GWVSF-HGFLYGSLSLGNTF-------VMF 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 263 ETILMEPLKWLD--W--IDHYRASV--TWAPNFAFGLVTDFAEEIKDRKWDLSSMRYMLNGGEAMVAKVGRRILELLEph 336
Cdd:PTZ00237 328 EGGIIKNKHIEDdlWntIEKHKVTHtlTLPKTIRYLIKTDPEATIIRSKYDLSNLKEIWCGGEVIEESIPEYIENKLK-- 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 337 glpadaIRPAWGMSETSSGVIFSHEFTragtSDDDHFVEIGSPIPGFSMRIVNDHNELVEEGEIGRFQVS---GLSVTSG 413
Cdd:PTZ00237 406 ------IKSSRGYGQTEIGITYLYCYG----HINIPYNATGVPSIFIKPSILSEDGKELNVNEIGEVAFKlpmPPSFATT 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 414 YYQRPDLNESVFTE-DGWFETGDLGFL-RNGRLTITGRTKDAIIINGINYyshaiesaveELSEIETSYTAACAV----R 487
Cdd:PTZ00237 476 FYKNDEKFKQLFSKfPGYYNSGDLGFKdENGYYTIVSRSDDQIKISGNKV----------QLNTIETSILKHPLVleccS 545
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1776025254 488 LGQNSTDQLAIFFVTSAKLNDEQMSQL-LRNIQSHVSQVIGVTPEYLLPVQK----EEIPKTAIGKIQR 551
Cdd:PTZ00237 546 IGIYDPDCYNVPIGLLVLKQDQSNQSIdLNKLKNEINNIITQDIESLAVLRKiiivNQLPKTKTGKIPR 614
|
|
| PRK12938 |
PRK12938 |
3-ketoacyl-ACP reductase; |
2853-3026 |
8.41e-08 |
|
3-ketoacyl-ACP reductase;
Pssm-ID: 171822 [Multi-domain] Cd Length: 246 Bit Score: 56.56 E-value: 8.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2853 ITGGAGSLGLLFAKEIANRTGRstiVLTGRSVLSEDKENELEALRSIGAEVVYREADVSDQHAVHHLFEEIKERYGTLNG 2932
Cdd:PRK12938 8 VTGGMGGIGTSICQRLHKDGFK---VVAGCGPNSPRRVKWLEDQKALGFDFIASEGNVGDWDSTKAAFDKVKAEVGEIDV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2933 IIHGAGSIKDHFIIHKTNEEFQEVLQPKVSGLLHVDECSKDFPLDF----FIFFSSVSGCLGNAGQADYAAANSFMDAFA 3008
Cdd:PRK12938 85 LVNNAGITRDVVFRKMTREDWTAVIDTNLTSLFNVTKQVIDGMVERgwgrIINISSVNGQKGQFGQTNYSTAKAGIHGFT 164
|
170
....*....|....*...
gi 1776025254 3009 EYRRSLAASKKRFGSTIS 3026
Cdd:PRK12938 165 MSLAQEVATKGVTVNTVS 182
|
|
| SDR_c2 |
cd05370 |
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ... |
2852-2943 |
9.80e-08 |
|
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka Tyrosine-dependent oxidoreductases) are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.
Pssm-ID: 187628 [Multi-domain] Cd Length: 228 Bit Score: 56.16 E-value: 9.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2852 LITGGAGSLGLLFAKEIANRTgrSTIVLTGRSvlsedkENELEALRSIGAEVVYREADVSDQHAVHHLFEEIKERYGTLN 2931
Cdd:cd05370 9 LITGGTSGIGLALARKFLEAG--NTVIITGRR------EERLAEAKKELPNIHTIVLDVGDAESVEALAEALLSEYPNLD 80
|
90
....*....|..
gi 1776025254 2932 GIIHGAGSIKDH 2943
Cdd:cd05370 81 ILINNAGIQRPI 92
|
|
| fabG |
PRK08217 |
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional |
4169-4277 |
1.01e-07 |
|
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
Pssm-ID: 181297 [Multi-domain] Cd Length: 253 Bit Score: 56.51 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4169 KDHVLLITGGTRGIGLLCARHFAECyGVKkLVLTGREQlppreewarfktsntslaEKIQ-AVRELEAKGVQVEMLSLTL 4247
Cdd:PRK08217 4 KDKVIVITGGAQGLGRAMAEYLAQK-GAK-LALIDLNQ------------------EKLEeAVAECGALGTEVRGYAANV 63
|
90 100 110
....*....|....*....|....*....|
gi 1776025254 4248 SDDAQVEQTLQHIKRTLGPIGGVIHCAGLT 4277
Cdd:PRK08217 64 TDEEDVEATFAQIAEDFGQLNGLINNAGIL 93
|
|
| PKS_PP |
smart00823 |
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ... |
592-665 |
1.02e-07 |
|
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.
Pssm-ID: 214834 [Multi-domain] Cd Length: 86 Bit Score: 52.25 E-value: 1.02e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1776025254 592 REEIQEHLLTCLTEEL-HVSRDWVEPNANIQSLGVNSIKMMKLIRSIEKNYHIKLTAREIHQYPTIERLASYLSE 665
Cdd:smart00823 10 RRLLLDLVREQVAAVLgHAAAEAIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHLAA 84
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
138-239 |
1.18e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 58.15 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 138 DKPAVITDRGmHQEMLDwakeqGLE-GFRAIIVE-----DLLSAEADTDWHQS--SPEDLALLLLTSGSTGTPKAVMLNH 209
Cdd:PRK07867 101 DCQLVLTESA-HAELLD-----GLDpGVRVINVDspawaDELAAHRDAEPPFRvaDPDDLFMLIFTSGTSGDPKAVRCTH 174
|
90 100 110
....*....|....*....|....*....|
gi 1776025254 210 RNIMSMVKGIIQMQGFTREDITFNWMPFDH 239
Cdd:PRK07867 175 RKVASAGVMLAQRFGLGPDDVCYVSMPLFH 204
|
|
| PRK12939 |
PRK12939 |
short chain dehydrogenase; Provisional |
2850-2963 |
1.34e-07 |
|
short chain dehydrogenase; Provisional
Pssm-ID: 183833 [Multi-domain] Cd Length: 250 Bit Score: 56.13 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGLLFAKEIAnRTGrSTIVLTgrSVLSEDKENELEALRSIGAEVVYREADVSDQHAVHHLFEEIKERYGT 2929
Cdd:PRK12939 9 RALVTGAARGLGAAFAEALA-EAG-ATVAFN--DGLAAEARELAAALEAAGGRAHAIAADLADPASVQRFFDAAAAALGG 84
|
90 100 110
....*....|....*....|....*....|....
gi 1776025254 2930 LNGIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSG 2963
Cdd:PRK12939 85 LDGLVNNAGITNSKSATELDIDTWDAVMNVNVRG 118
|
|
| PRK06484 |
PRK06484 |
short chain dehydrogenase; Validated |
2842-3016 |
1.75e-07 |
|
short chain dehydrogenase; Validated
Pssm-ID: 168574 [Multi-domain] Cd Length: 520 Bit Score: 57.55 E-value: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2842 HMPWRDEGVYLITGGAGSLGLLFAKEIANrtgrstivLTGRSVLSEDKENELEALRSI-GAEVVYREADVSDQHAVHHLF 2920
Cdd:PRK06484 263 SPLAESPRVVAITGGARGIGRAVADRFAA--------AGDRLLIIDRDAEGAKKLAEAlGDEHLSVQADITDEAAVESAF 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2921 EEIKERYGTLNGIIHGAGsIKDHFI--IHKTNEEFQEVLQPKVSGLLH-VDECSKDFPLDFFIF-FSSVSGCLGNAGQAD 2996
Cdd:PRK06484 335 AQIQARWGRLDVLVNNAG-IAEVFKpsLEQSAEDFTRVYDVNLSGAFAcARAAARLMSQGGVIVnLGSIASLLALPPRNA 413
|
170 180
....*....|....*....|
gi 1776025254 2997 YAAANSFMDAFAeyrRSLAA 3016
Cdd:PRK06484 414 YCASKAAVTMLS---RSLAC 430
|
|
| fabG |
PRK05565 |
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional |
2850-2963 |
1.79e-07 |
|
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
Pssm-ID: 235506 [Multi-domain] Cd Length: 247 Bit Score: 55.62 E-value: 1.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLG----LLFAKEianrtGRSTIVLTGRSvlsEDKENELEA-LRSIGAEVVYREADVSDQHAVHHLFEEIK 2924
Cdd:PRK05565 7 VAIVTGASGGIGraiaELLAKE-----GAKVVIAYDIN---EEAAQELLEeIKEEGGDAIAVKADVSSEEDVENLVEQIV 78
|
90 100 110
....*....|....*....|....*....|....*....
gi 1776025254 2925 ERYGTLNGIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSG 2963
Cdd:PRK05565 79 EKFGKIDILVNNAGISNFGLVTDMTDEEWDRVIDVNLTG 117
|
|
| PKS_PP |
smart00823 |
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ... |
4461-4533 |
1.96e-07 |
|
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.
Pssm-ID: 214834 [Multi-domain] Cd Length: 86 Bit Score: 51.48 E-value: 1.96e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1776025254 4461 SETQSWLIDLFTEEL-----RIDREDFEIDGLFQDYGVDSIILAQVLQRINRKLEAALDPSILYEYPTIQRFTDWLIG 4533
Cdd:smart00823 7 AERRRLLLDLVREQVaavlgHAAAEAIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHLAA 84
|
|
| E_NRPS |
cd19534 |
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
695-894 |
2.46e-07 |
|
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Epimerization (E) domains of nonribosomal peptide synthetases (NRPS) flip the chirality of the end amino acid of a peptide being manufactured by the NRPS. E-domains are homologous to the Condensation (C) domains. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Specialized tailoring NRPS domains such as E-domains greatly increase the range of possible peptide products created by the NRPS machinery. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the E-domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380457 [Multi-domain] Cd Length: 428 Bit Score: 56.88 E-value: 2.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 695 PLSEVQKglWTLQKMSPEKSAYHVPLCFKFSSGLHLETLQQAFGLVLNQHPILKHVIQEKDGVPILKNEPALSIEIKTEn 774
Cdd:cd19534 3 PLTPIQR--WFFEQNLAGRHHFNQSVLLRVPQGLDPDALRQALRALVEHHDALRMRFRREDGGWQQRIRGDVEELFRLE- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 775 ISSMKESDIPAFLRKKVkEPYVK----ENSPLVRVMSFSRSEQEHFLLVVIHHLIFDGVSSVTFIHSLFDTYQLLLKGQQ 850
Cdd:cd19534 80 VVDLSSLAQAAAIEALA-AEAQSsldlEEGPLLAAALFDGTDGGDRLLLVIHHLVVDGVSWRILLEDLEAAYEQALAGEP 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1776025254 851 PEIAVSPAiYHDFAAWEKNMLAGKDGVKHRTYWQKQLSGTLPNL 894
Cdd:cd19534 159 IPLPSKTS-FQTWAELLAEYAQSPALLEELAYWRELPAADYWGL 201
|
|
| PRK06147 |
PRK06147 |
3-oxoacyl-(acyl carrier protein) synthase; Validated |
3500-3706 |
2.59e-07 |
|
3-oxoacyl-(acyl carrier protein) synthase; Validated
Pssm-ID: 235715 [Multi-domain] Cd Length: 348 Bit Score: 56.18 E-value: 2.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3500 HGPSEPVETACSSSLVAIHRAVTAMQNGDCEMAIAGGVNTILTEEAHISYskagmlSKDGRCKTfSADANGYVRGEGVGM 3579
Cdd:PRK06147 123 EPGSAVIARGRVSGAVALAQARRLIAAGGCPRVLVAGVDSLLTGPTLAHY------EARDRLLT-SQNSNGFIPGEAAAA 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3580 VMLKKLEDAERDGNHIYGVIRGTAENHGGRANTLTSpnpkaQADLLVRAYRQAgIDPSTVTYieaHGTGTELGDpieING 3659
Cdd:PRK06147 196 VLLGRPAGGEAPGLPLLGLGLGREPAPVGESEDLPL-----RGDGLTQAIRAA-LAEAGCGL---EDMDYRIAD---LNG 263
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1776025254 3660 LKAAFKE--LSNMRGESQPD-VPDHRC---GIGSVKSNIGHLELAAGISGLIK 3706
Cdd:PRK06147 264 EQYRFKEaaLAEMRLFRVRKeFFDLWHpaeCIGEIGAAIGPALLGVALAASRK 316
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
142-467 |
2.69e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 56.96 E-value: 2.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 142 VITDRGmHQEMLDwakEQGLEGFRAIIVED-----LLSAEADTDWHQS-SPEDLALLLLTSGSTGTPKAVMLNHRNIMSM 215
Cdd:PRK13388 103 LVTDAE-HRPLLD---GLDLPGVRVLDVDTpayaeLVAAAGALTPHREvDAMDPFMLIFTSGTTGAPKAVRCSHGRLAFA 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 216 VKGIIQMQGFTREDITFNWMPfdhvggigMLHLRDVYLGCQEINVSSETILMEPlkwldwidHYRASvtwapnfafGLVT 295
Cdd:PRK13388 179 GRALTERFGLTRDDVCYVSMP--------LFHSNAVMAGWAPAVASGAAVALPA--------KFSAS---------GFLD 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 296 DFaeeikdRKWDLSSMRYmlnggeamvakVGRRILELLEPHGLPADA---IRPAWGmSETSSGVIfsHEFTRA------- 365
Cdd:PRK13388 234 DV------RRYGATYFNY-----------VGKPLAYILATPERPDDAdnpLRVAFG-NEASPRDI--AEFSRRfgcqved 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 366 --GTSD-------DDHFVE--IGSPIPGfsMRIVNDhnELVEEGEIGRFQVSG-----------LSVT------SGYYQR 417
Cdd:PRK13388 294 gyGSSEgavivvrEPGTPPgsIGRGAPG--VAIYNP--ETLTECAVARFDAHGallnadeaigeLVNTagagffEGYYNN 369
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1776025254 418 PDLNESVFtEDGWFETGDLGFL-RNGRLTITGRTKDAIIINGINYYSHAIE 467
Cdd:PRK13388 370 PEATAERM-RHGMYWSGDLAYRdADGWIYFAGRTADWMRVDGENLSAAPIE 419
|
|
| PRK06198 |
PRK06198 |
short chain dehydrogenase; Provisional |
2847-2938 |
3.01e-07 |
|
short chain dehydrogenase; Provisional
Pssm-ID: 180462 [Multi-domain] Cd Length: 260 Bit Score: 55.40 E-value: 3.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2847 DEGVYLITGGAGSLGLLFAKEIANRtGRSTIVLTGRS-VLSEDKENELEALrsiGAEVVYREADVSDQHAVHHLFEEIKE 2925
Cdd:PRK06198 5 DGKVALVTGGTQGLGAAIARAFAER-GAAGLVICGRNaEKGEAQAAELEAL---GAKAVFVQADLSDVEDCRRVVAAADE 80
|
90
....*....|...
gi 1776025254 2926 RYGTLNGIIHGAG 2938
Cdd:PRK06198 81 AFGRLDALVNAAG 93
|
|
| MDH-like_SDR_c |
cd05352 |
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ... |
4169-4341 |
3.33e-07 |
|
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes the conversion of fructose to mannitol, an acyclic 6-carbon sugar. MDH is a tetrameric member of the SDR family. This subgroup also includes various other tetrameric SDRs, including Pichia stipitis D-arabinitol dehydrogenase (aka polyol dehydrogenase), Candida albicans Sou1p, a sorbose reductase, and Candida parapsilosis (S)-specific carbonyl reductase (SCR, aka S-specific alcohol dehydrogenase) which catalyzes the enantioselective reduction of 2-hydroxyacetophenone into (S)-1-phenyl-1,2-ethanediol. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser).
Pssm-ID: 187610 [Multi-domain] Cd Length: 252 Bit Score: 55.03 E-value: 3.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4169 KDHVLLITGGTRGIGLLCARHFAEcYGVKKLVLTGREqlpPREEWArfktsntslAEKIQavrelEAKGVQVEMLSLTLS 4248
Cdd:cd05352 7 KGKVAIVTGGSRGIGLAIARALAE-AGADVAIIYNSA---PRAEEK---------AEELA-----KKYGVKTKAYKCDVS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4249 DDAQVEQTLQHIKRTLGPIGGVIHCAGLTdmDTLAFIRKTSDDIQRVMEPKVSGLTtlyrHVCNEPLQFF--------VL 4320
Cdd:cd05352 69 SQESVEKTFKQIQKDFGKIDILIANAGIT--VHKPALDYTYEQWNKVIDVNLNGVF----NCAQAAAKIFkkqgkgslII 142
|
170 180
....*....|....*....|.
gi 1776025254 4321 FSSVSAIIPELSAGQADYAMA 4341
Cdd:cd05352 143 TASMSGTIVNRPQPQAAYNAS 163
|
|
| PT_fungal_PKS |
TIGR04532 |
iterative type I PKS product template domain; Sequences found by this model are the so-called ... |
2381-2580 |
3.99e-07 |
|
iterative type I PKS product template domain; Sequences found by this model are the so-called product template (PT) domain of various fungal iterative type I polyketide synthases. This domain resembles pfam14765, designated polyketide synthase dehydratase by Pfam, but members of that family are primarily bacterial, where type I PKS are predominantly modular, not iterative. The dehydratase active site residues well-conserved in pfam14765 (His in the first hot dog domain, Asp in the second hot dog domain) seem well conserved in this family also.
Pssm-ID: 275325 Cd Length: 324 Bit Score: 55.71 E-value: 3.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2381 SDFSEQKFSSVFTGdefflrdHVVRGKPVLPGVAYLEMAYAAIN----QAAGSEIGQDVRIRLNHTVWVQPVVVD----- 2451
Cdd:TIGR04532 23 SDLSDPDLLAAIQG-------HRVNGVPLCPSSVYADMALTAAKyllkRLRGSKDAADVGLDVRDMEVDKPLVADpsdsd 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2452 ----RHSAQVDISLfpeeDGKITFDIYSTQEDGDDPVIHSQGSAELASAAETPVAD----LTEISRRC---------GKG 2514
Cdd:TIGR04532 96 pqllRVTATADAST----SSRVSISFSSSSSSGKKTEEHATCTVRFGDPAAAWLAEwsrtAYLVKSRIdalrqsakeGSA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1776025254 2515 -KMSPDQFYEegrsrgMF-----HGPAFQGIKNVNI--GNREVLAQLQLPEIVSGTNeqFVLHPSIMDSALQTA 2580
Cdd:TIGR04532 172 hRLSRRMAYK------LFsslvdYSPKYRGMQEVVLdsDGLEATATVKLPTDPPDGG--FTVSPYWIDSLLHLA 237
|
|
| adh_short_C2 |
pfam13561 |
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ... |
2863-3017 |
4.08e-07 |
|
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) reductases.
Pssm-ID: 433310 [Multi-domain] Cd Length: 236 Bit Score: 54.36 E-value: 4.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2863 LFAKEIANrtgrstIVLTGRSvlsEDKENELEAL-RSIGAEVVyrEADVSDQHAVHHLFEEIKERYGTLNGIIHGAG-SI 2940
Cdd:pfam13561 15 ALAEEGAE------VVLTDLN---EALAKRVEELaEELGAAVL--PCDVTDEEQVEALVAAAVEKFGRLDILVNNAGfAP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2941 KDHFIIHKTN-EEFQEVLQPKVSGLLHvdeCSKDFpLDFF------IFFSSVSGCLGNAGQADYAAANSFMDAFAeyrRS 3013
Cdd:pfam13561 84 KLKGPFLDTSrEDFDRALDVNLYSLFL---LAKAA-LPLMkeggsiVNLSSIGAERVVPNYNAYGAAKAALEALT---RY 156
|
....
gi 1776025254 3014 LAAS 3017
Cdd:pfam13561 157 LAVE 160
|
|
| PRK08277 |
PRK08277 |
D-mannonate oxidoreductase; Provisional |
2850-2938 |
5.45e-07 |
|
D-mannonate oxidoreductase; Provisional
Pssm-ID: 236216 [Multi-domain] Cd Length: 278 Bit Score: 54.52 E-value: 5.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGLLFAKEIAnRTGRSTIVLtGRSVlsEDKENELEALRSIGAEVVYREADVSDQHAVHHLFEEIKERYGT 2929
Cdd:PRK08277 12 VAVITGGGGVLGGAMAKELA-RAGAKVAIL-DRNQ--EKAEAVVAEIKAAGGEALAVKADVLDKESLEQARQQILEDFGP 87
|
....*....
gi 1776025254 2930 LNGIIHGAG 2938
Cdd:PRK08277 88 CDILINGAG 96
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
1174-1340 |
5.76e-07 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 55.76 E-value: 5.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1174 YEGQTLTYRELDERSTQLAIYLQAH-GVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLEDSEVF 1252
Cdd:cd05938 1 FEGETYTYRDVDRRSNQAARALLAHaGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1253 ITLTTSELVNT-------LSWNGV-------------TTALLDQdwdeiAQTASDRKV---LTRTVTPENLAYVIYTSGS 1309
Cdd:cd05938 81 VLVVAPELQEAveevlpaLRADGVsvwylshtsntegVISLLDK-----VDAASDEPVpasLRAHVTIKSPALYIYTSGT 155
|
170 180 190
....*....|....*....|....*....|....
gi 1776025254 1310 TGKPKGVMIPHK---ALTNFLvsmgETPGLTAED 1340
Cdd:cd05938 156 TGLPKAARISHLrvlQCSGFL----SLCGVTADD 185
|
|
| PRK08213 |
PRK08213 |
gluconate 5-dehydrogenase; Provisional |
4174-4310 |
6.99e-07 |
|
gluconate 5-dehydrogenase; Provisional
Pssm-ID: 181295 [Multi-domain] Cd Length: 259 Bit Score: 54.18 E-value: 6.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4174 LITGGTRGIGLLCARHFAEcYGVkKLVLTGREQlppreewarfktsntslAEKIQAVRELEAKGVQVEMLSLTLSDDAQV 4253
Cdd:PRK08213 16 LVTGGSRGLGLQIAEALGE-AGA-RVVLSARKA-----------------EELEEAAAHLEALGIDALWIAADVADEADI 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1776025254 4254 EQTLQHIKRTLGPIGGVIHCAGLT------DMDTLAFirktsddiQRVMEPKVSGLTTLYRHV 4310
Cdd:PRK08213 77 ERLAEETLERFGHVDILVNNAGATwgapaeDHPVEAW--------DKVMNLNVRGLFLLSQAV 131
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
3909-4006 |
7.68e-07 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 56.03 E-value: 7.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3909 LADLWVKGVSIQWNTLYGETKPRLISLPSYPFAKDHYWVPAKEHSERDKKELVNAIEDRAACFLTKQWSLSPIGSAVPGT 3988
Cdd:COG3321 837 LAQLWVAGVPVDWSALYPGRGRRRVPLPTYPFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAA 916
|
90
....*....|....*...
gi 1776025254 3989 RTVAILCCQETADLAAEV 4006
Cdd:COG3321 917 AALALAAAALAALLALVA 934
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
1175-1563 |
8.41e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 55.39 E-value: 8.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1175 EGQTLTYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYP----------AERLEY 1244
Cdd:PRK07768 26 APVRHTWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTMLHQPTPrtdlavwaedTLRVIG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1245 MLEDSEVFITLTTSELVNTLSWNGVTTALLDQDWDEiaqtASDRKVLTrtvTPENLAYVIYTSGSTGKPKGVMIPHKALT 1324
Cdd:PRK07768 106 MIGAKAVVVGEPFLAAAPVLEEKGIRVLTVADLLAA----DPIDPVET---GEDDLALMQLTSGSTGSPKAVQITHGNLY 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1325 NFLVSMGETPGLTAE-DKMLAVTTYCFDIAALE-LFLPLIKGAhcyicqtehtkdveklkrDIRTIKPTVMQATPATWKM 1402
Cdd:PRK07768 179 ANAEAMFVAAEFDVEtDVMVSWLPLFHDMGMVGfLTVPMYFGA------------------ELVKVTPMDFLRDPLLWAE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1403 LF--------------YS------------GWENEENVKI-LCGGEAL-PETLKRyFLDTG------SEAW-NMFGPTET 1447
Cdd:PRK07768 241 LIskyrgtmtaapnfaYAllarrlrrqakpGAFDLSSLRFaLNGAEPIdPADVED-LLDAGarfglrPEAIlPAYGMAEA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1448 TI------WSAVQRINDEC-------------------SRATIGRPIANTQIYITDSQLAPVPAGVPGELCIAGDGVAKG 1502
Cdd:PRK07768 320 TLavsfspCGAGLVVDEVDadllaalrravpatkgntrRLATLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRGESVTPG 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1776025254 1503 YykkeeLTDSRFIdnPFEPGSKLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIE 1563
Cdd:PRK07768 400 Y-----LTMDGFI--PAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIE 453
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
2313-2347 |
1.02e-06 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 55.65 E-value: 1.02e-06
10 20 30
....*....|....*....|....*....|....*
gi 1776025254 2313 LAEMWSKGAHIDWMQLYKGERPNRMSLPTYPFAKE 2347
Cdd:COG3321 837 LAQLWVAGVPVDWSALYPGRGRRRVPLPTYPFQRE 871
|
|
| PRK07791 |
PRK07791 |
short chain dehydrogenase; Provisional |
2850-3000 |
1.18e-06 |
|
short chain dehydrogenase; Provisional
Pssm-ID: 236099 [Multi-domain] Cd Length: 286 Bit Score: 53.91 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLG----LLFAKEIA----NRTGRStivLTGRSVLSEDKENELEALRSIGAEVVYREADVSDQHAVHHLFE 2921
Cdd:PRK07791 8 VVIVTGAGGGIGrahaLAFAAEGArvvvNDIGVG---LDGSASGGSAAQAVVDEIVAAGGEAVANGDDIADWDGAANLVD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2922 EIKERYGTLNGIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSG---LLHV------DECSKDFPLDFFIF-FSSVSGCLGN 2991
Cdd:PRK07791 85 AAVETFGGLDVLVNNAGILRDRMIANMSEEEWDAVIAVHLKGhfaTLRHaaaywrAESKAGRAVDARIInTSSGAGLQGS 164
|
....*....
gi 1776025254 2992 AGQADYAAA 3000
Cdd:PRK07791 165 VGQGNYSAA 173
|
|
| PRK12826 |
PRK12826 |
SDR family oxidoreductase; |
4172-4303 |
1.52e-06 |
|
SDR family oxidoreductase;
Pssm-ID: 183775 [Multi-domain] Cd Length: 251 Bit Score: 53.00 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4172 VLLITGGTRGIGLLCARHFAEcYGVKKLVLTgreqlppreewarfkTSNTSLAEkiqAVRELEAKGVQVEMLSLTLSDDA 4251
Cdd:PRK12826 8 VALVTGAARGIGRAIAVRLAA-DGAEVIVVD---------------ICGDDAAA---TAELVEAAGGKARARQVDVRDRA 68
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1776025254 4252 QVEQTLQHIKRTLGPIGGVIHCAGLTDMDTLAFIrkTSDDIQRVMEPKVSGL 4303
Cdd:PRK12826 69 ALKAAVAAGVEDFGRLDILVANAGIFPLTPFAEM--DDEQWERVIDVNLTGT 118
|
|
| PRK07109 |
PRK07109 |
short chain dehydrogenase; Provisional |
4172-4297 |
2.09e-06 |
|
short chain dehydrogenase; Provisional
Pssm-ID: 235935 [Multi-domain] Cd Length: 334 Bit Score: 53.39 E-value: 2.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4172 VLLITGGTRGIGLLCARHFAEcYGVKKLVLtgreqlppreewARfktSNTSLAEkiqAVRELEAKGVQVEMLSLTLSDDA 4251
Cdd:PRK07109 10 VVVITGASAGVGRATARAFAR-RGAKVVLL------------AR---GEEGLEA---LAAEIRAAGGEALAVVADVADAE 70
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1776025254 4252 QVEQTLQHIKRTLGPIGGVIHCAGLTDMDTlaFIRKTSDDIQRVME 4297
Cdd:PRK07109 71 AVQAAADRAEEELGPIDTWVNNAMVTVFGP--FEDVTPEEFRRVTE 114
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
1168-1639 |
2.13e-06 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 53.97 E-value: 2.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1168 DRAAVSYEGQTL-----TYRELDERSTQLAIYLQAHGVGPDRLAGIYVDRSLDMLVGLLAILKAGGAYVPLDPSYPAERL 1242
Cdd:cd05915 9 GRKEVVSRLHTGevhrtTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1243 EYMLEDSEVFITLTTSE----------LVNTLSWNGVTTALLDQdWDEIAQTASDRKVLTRTVTPENLAYVIYTSGSTGK 1312
Cdd:cd05915 89 AYILNHAEDKVLLFDPNllplveairgELKTVQHFVVMDEKAPE-GYLAYEEALGEEADPVRVPERAACGMAYTTGTTGL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1313 PKGVMIPHKALTNFLVSMG--------ETPGLTAEDKMLAVTTYCFdIAALELFLPLIkgahcyICQTEHTKDvEKLKRD 1384
Cdd:cd05915 168 PKGVVYSHRALVLHSLAASlvdgtalsEKDVVLPVVPMFHVNAWCL-PYAATLVGAKQ------VLPGPRLDP-ASLVEL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1385 IRTIKPTVMQATPATWKMLFYSGWENEEN----VKILCGGEALPET------LKRYFLDTGSEAWNMFGPTETTIW-SAV 1453
Cdd:cd05915 240 FDGEGVTFTAGVPTVWLALADYLESTGHRlktlRRLVVGGSAAPRSliarfeRMGVEVRQGYGLTETSPVVVQNFVkSHL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1454 QRINDECSRATIGRPIANTQIYITDSqLAPVPAGVPGE------LCIAGDGVAKGYYKKEELTDSrfidNPFEPGskLYR 1527
Cdd:cd05915 320 ESLSEEEKLTLKAKTGLPIPLVRLRV-ADEEGRPVPKDgkalgeVQLKGPWITGGYYGNEEATRS----ALTPDG--FFR 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1528 TGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMD-----NLAAYYTAKHANASltAREL 1602
Cdd:cd05915 393 TGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHpkwqeRPLAVVVPRGEKPT--PEEL 470
|
490 500 510
....*....|....*....|....*....|....*...
gi 1776025254 1603 RHFVKNALPAY-MVPSYFIQLDHMPLTPNGKIDRNSLK 1639
Cdd:cd05915 471 NEHLLKAGFAKwQLPDAYVFAEEIPRTSAGKFLKRALR 508
|
|
| carb_red_PTCR-like_SDR_c |
cd05324 |
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ... |
2850-3008 |
2.15e-06 |
|
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR which catalyzes the NADPH-dependent reduction of ketones on steroids and prostaglandins. Unlike most SDRs, PTCR functions as a monomer. This subgroup also includes human carbonyl reductase 1 (CBR1) and CBR3. CBR1 is an NADPH-dependent SDR with broad substrate specificity and may be responsible for the in vivo reduction of quinones, prostaglandins, and other carbonyl-containing compounds. In addition it includes poppy NADPH-dependent salutaridine reductase which catalyzes the stereospecific reduction of salutaridine to 7(S)-salutaridinol in the biosynthesis of morphine, and Arabidopsis SDR1,a menthone reductase, which catalyzes the reduction of menthone to neomenthol, a compound with antimicrobial activity; SDR1 can also carry out neomenthol oxidation. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.
Pssm-ID: 187585 [Multi-domain] Cd Length: 225 Bit Score: 52.24 E-value: 2.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGLLFAKEIANRtGRSTIVLTGRSVlsEDKENELEALRSIGAEVVYREADVSDQHAVHHLFEEIKERYGT 2929
Cdd:cd05324 2 VALVTGANRGIGFEIVRQLAKS-GPGTVILTARDV--ERGQAAVEKLRAEGLSVRFHQLDVTDDASIEAAADFVEEKYGG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2930 LNGIIHGAGSIKDHFIIHKTN-EEFQEVLQPKVSGLLHVDECS----KDFPLDFFIFFSSVSGCLGNAGQADYAAANSFM 3004
Cdd:cd05324 79 LDILVNNAGIAFKGFDDSTPTrEQARETMKTNFFGTVDVTQALlpllKKSPAGRIVNVSSGLGSLTSAYGVSKAALNALT 158
|
....
gi 1776025254 3005 DAFA 3008
Cdd:cd05324 159 RILA 162
|
|
| omega_3_PfaA |
TIGR02813 |
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ... |
2398-2647 |
2.27e-06 |
|
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this alignment are involved in omega-3 polyunsaturated fatty acid biosynthesis, such as the protein PfaA from the eicosapentaenoic acid biosynthesis operon in Photobacterium profundum strain SS9. PfaA is encoded together with PfaB, PfaC, and PfaD, and the functions of the individual polypeptides have not yet been described. More distant homologs of PfaA, also included with the reach of this model, appear to be involved in polyketide-like biosynthetic mechanisms of polyunsaturated fatty acid biosynthesis, an alternative to the more familiar iterated mechanism of chain extension and desaturation, and in most cases are encoded near genes for homologs of PfaB, PfaC, and/or PfaD.
Pssm-ID: 274311 [Multi-domain] Cd Length: 2582 Bit Score: 54.63 E-value: 2.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2398 FLRDHVVRGKPVLPGVAylemAYAAINQAAGSEIGQDVRIRlNHTVwVQPVVVDRHSAQVDISLFPEEDGKITFD---IY 2474
Cdd:TIGR02813 2310 FIADHCIGGDKVLPTVC----AIAWMREAAMVALGAFVGVA-DYKL-LKGVIFDGSEATEYIDMILQLELTPLVVdtkIS 2383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2475 STQEDGDdPVIHSQGSAELASAAET---PVADL---TEISRRCGKGKMSPDQFYEEGRSRG-MFHGPAFQGIKNVNIGNR 2547
Cdd:TIGR02813 2384 TTNEQAL-ISFHYRPQYTAVLVAERkeaPTAELflpEALPELLPETVLSSIEEAGALYSNGtLFHGPRLQGIKAVLAFDD 2462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2548 E-VLAQLQLPEIVSGTNEQFVlhPSIMDSALQT-------ATICIMQELTDQKLILPFALEELEVIKGCSSSMWAYARLS 2619
Cdd:TIGR02813 2463 QgLLAKCQLPAVASLDCGEFP--PSPLNSGSQPfaedillQAMLVWARLKYGAASLPSSIGEFVSYRPVSLGEKFYLKLD 2540
|
250 260
....*....|....*....|....*...
gi 1776025254 2620 DSDHSGGVVQkADIDVIDESGSVCVRIK 2647
Cdd:TIGR02813 2541 VVKSSGRSLV-ANIELYHQDGRLSSEMK 2567
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
51-467 |
2.98e-06 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 53.54 E-value: 2.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 51 LQPDGTEVyqSYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNSQLLPAFWG---------CVLTGVVPAPLAvpptYA 121
Cdd:PRK13391 18 MASTGEVV--TYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAaersglyytCVNSHLTPAEAA----YI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 122 ESSSGTQKLKDAWTLLDKPAVITD---RGMHQEMLDWAKEqgLEGFRAiiVEDLLSAEADTDWHQSSPEDLalLLLTSGS 198
Cdd:PRK13391 92 VDDSGARALITSAAKLDVARALLKqcpGVRHRLVLDGDGE--LEGFVG--YAEAVAGLPATPIADESLGTD--MLYSSGT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 199 TGTPKAVM--LNHRNI---MSMVKGIIQMQGFTREDITFNWMPFDHVGGigmlhLRDVYLGcqeINVSSETILME---PL 270
Cdd:PRK13391 166 TGRPKGIKrpLPEQPPdtpLPLTAFLQRLWGFRSDMVYLSPAPLYHSAP-----QRAVMLV---IRLGGTVIVMEhfdAE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 271 KWLDWIDHYRASVT-WAPNFaFGLVTDFAEEIKDRkWDLSSMRYMLNGGEAMVAKVGRRILELLEPhglpadAIRPAWGM 349
Cdd:PRK13391 238 QYLALIEEYGVTHTqLVPTM-FSRMLKLPEEVRDK-YDLSSLEVAIHAAAPCPPQVKEQMIDWWGP------IIHEYYAA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 350 SEtSSGVIF--SHEF-TRAGTsdddhfveIGSPIPGfSMRIVNDHNELVEEGEIGRFQVSGLSVTSgYYQRPD-LNESVF 425
Cdd:PRK13391 310 TE-GLGFTAcdSEEWlAHPGT--------VGRAMFG-DLHILDDDGAELPPGEPGTIWFEGGRPFE-YLNDPAkTAEARH 378
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1776025254 426 TEDGWFETGDLGFL-RNGRLTITGRTKDAIIINGINYYSHAIE 467
Cdd:PRK13391 379 PDGTWSTVGDIGYVdEDGYLYLTDRAAFMIISGGVNIYPQEAE 421
|
|
| THN_reductase-like_SDR_c |
cd05362 |
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ... |
2850-3015 |
3.13e-06 |
|
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6,8-tetrahydroxynaphthalene reductase (4HNR) of Magnaporthe grisea and the related 1,3,8-trihydroxynaphthalene reductase (3HNR) are typical members of the SDR family containing the canonical glycine rich NAD(P)-binding site and active site tetrad, and function in fungal melanin biosynthesis. This subgroup also includes an SDR from Norway spruce that may function to protect against both biotic and abitoic stress. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.
Pssm-ID: 187620 [Multi-domain] Cd Length: 243 Bit Score: 51.89 E-value: 3.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGLLFAKEIANRtGRSTIVLTGRSvlSEDKENELEALRSIGAEVVYREADVSDQHAVHHLFEEIKERYGT 2929
Cdd:cd05362 5 VALVTGASRGIGRAIAKRLARD-GASVVVNYASS--KAAAEEVVAEIEAAGGKAIAVQADVSDPSQVARLFDAAEKAFGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2930 LNGIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSGLLHV-DECSKDF-PLDFFIFFSSVSGCLGNAGQADYAAANSFMDAF 3007
Cdd:cd05362 82 VDILVNNAGVMLKKPIAETSEEEFDRMFTVNTKGAFFVlQEAAKRLrDGGRIINISSSLTAAYTPNYGAYAGSKAAVEAF 161
|
....*...
gi 1776025254 3008 AeyrRSLA 3015
Cdd:cd05362 162 T---RVLA 166
|
|
| HetN_like_SDR_c |
cd08932 |
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ... |
4172-4340 |
3.60e-06 |
|
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC 7120 HetN, a putative oxidoreductase involved in heterocyst differentiation, and related proteins. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.
Pssm-ID: 212493 [Multi-domain] Cd Length: 223 Bit Score: 51.59 E-value: 3.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4172 VLLITGGTRGIGLLCARHFAECYgvKKLVLTGREQlppreewarfktsntslaekiQAVRELEAKGVQVEMLSLTLSDDA 4251
Cdd:cd08932 2 VALVTGASRGIGIEIARALARDG--YRVSLGLRNP---------------------EDLAALSASGGDVEAVPYDARDPE 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4252 QVEQTLQHIKRTLGPIGGVIHCAGLTDMDTLAFIrkTSDDIQRVMEPKVSGLTTLYR----HVCNEPLQFFVLFSSVSAI 4327
Cdd:cd08932 59 DARALVDALRDRFGRIDVLVHNAGIGRPTTLREG--SDAELEAHFSINVIAPAELTRallpALREAGSGRVVFLNSLSGK 136
|
170
....*....|...
gi 1776025254 4328 IPElsAGQADYAM 4340
Cdd:cd08932 137 RVL--AGNAGYSA 147
|
|
| HSD10-like_SDR_c |
cd05371 |
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ... |
4169-4339 |
4.24e-06 |
|
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as amyloid-peptide-binding alcohol dehydrogenase (ABAD), was previously identified as a L-3-hydroxyacyl-CoA dehydrogenase, HADH2. In fatty acid metabolism, HADH2 catalyzes the third step of beta-oxidation, the conversion of a hydroxyl to a keto group in the NAD-dependent oxidation of L-3-hydroxyacyl CoA. In addition to alcohol dehydrogenase and HADH2 activites, HSD10 has steroid dehydrogenase activity. Although the mechanism is unclear, HSD10 is implicated in the formation of amyloid beta-petide in the brain (which is linked to the development of Alzheimer's disease). Although HSD10 is normally concentrated in the mitochondria, in the presence of amyloid beta-peptide it translocates into the plasma membrane, where it's action may generate cytotoxic aldehydes and may lower estrogen levels through its use of 17-beta-estradiol as a substrate. HSD10 is a member of the SRD family, but differs from other SDRs by the presence of two insertions of unknown function. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.
Pssm-ID: 187629 [Multi-domain] Cd Length: 252 Bit Score: 51.52 E-value: 4.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4169 KDHVLLITGGTRGIGLLCARHFAEcYGVKKLVLtgreQLPPreewarfktsntslaEKIQAVRELEAKGVQVEmlsLTLS 4248
Cdd:cd05371 1 KGLVAVVTGGASGLGLATVERLLA-QGAKVVIL----DLPN---------------SPGETVAKLGDNCRFVP---VDVT 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4249 DDAQVEQTLQHIKRTLGPIGGVIHCAGLtdmdTLAFirKT----------SDDIQRVMEPKVSGLTTLYRHVC-----NE 4313
Cdd:cd05371 58 SEKDVKAALALAKAKFGRLDIVVNCAGI----AVAA--KTynkkgqqphsLELFQRVINVNLIGTFNVIRLAAgamgkNE 131
|
170 180 190
....*....|....*....|....*....|.
gi 1776025254 4314 PLQF-----FVLFSSVSAIipELSAGQADYA 4339
Cdd:cd05371 132 PDQGgergvIINTASVAAF--EGQIGQAAYS 160
|
|
| KDSR-like_SDR_c |
cd08939 |
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ... |
4171-4339 |
5.04e-06 |
|
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These proteins include members identified as KDSR, ribitol type dehydrogenase, and others. The group shows strong conservation of the active site tetrad and glycine rich NAD-binding motif of the classical SDRs. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.
Pssm-ID: 187643 [Multi-domain] Cd Length: 239 Bit Score: 51.10 E-value: 5.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4171 HVLlITGGTRGIGLLCARHFAEcYGvKKLVLTGReqlppreewarfktSNTSLAEKIQAVR-ELEAKGVQVEMLSLTLSD 4249
Cdd:cd08939 3 HVL-ITGGSSGIGKALAKELVK-EG-ANVIIVAR--------------SESKLEEAVEEIEaEANASGQKVSYISADLSD 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4250 DAQVEQTLQHIKRTLGPIGGVIHCAG------LTDMdtlafirkTSDDIQRVMEpkVSGLTTLY------RHVCNEPLQF 4317
Cdd:cd08939 66 YEEVEQAFAQAVEKGGPPDLVVNCAGisipglFEDL--------TAEEFERGMD--VNYFGSLNvahavlPLMKEQRPGH 135
|
170 180
....*....|....*....|..
gi 1776025254 4318 FVLFSSVSAIIPelSAGQADYA 4339
Cdd:cd08939 136 IVFVSSQAALVG--IYGYSAYC 155
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
1168-1641 |
5.10e-06 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 52.84 E-value: 5.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1168 DRAAVSYEG------QTLTYRELDERSTQLAIYLQAHGVGP-DRLAgIYvdrsLDMLV-GLLAILKA-----------GG 1228
Cdd:PRK00174 82 DKVAIIWEGddpgdsRKITYRELHREVCRFANALKSLGVKKgDRVA-IY----MPMIPeAAVAMLACarigavhsvvfGG 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1229 ayvpldpsYPAERLEYMLEDSE--VFIT--------------------LTTSELVNT---LSWNGVTTALL---DQDWDE 1280
Cdd:PRK00174 157 --------FSAEALADRIIDAGakLVITadegvrggkpiplkanvdeaLANCPSVEKvivVRRTGGDVDWVegrDLWWHE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1281 IAQTASDrkvltrTVTPENLA-----YVIYTSGSTGKPKGVMipHkaltnflvsmgeTPG--LTaedkmLAVTT--YCFD 1351
Cdd:PRK00174 229 LVAGASD------ECEPEPMDaedplFILYTSGSTGKPKGVL--H------------TTGgyLV-----YAAMTmkYVFD 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1352 IAALELF-----LPLIKGaHCYIcqtehtkdveklkrdirTIKPTVMQATpatwkMLFYSG----------WE--NEENV 1414
Cdd:PRK00174 284 YKDGDVYwctadVGWVTG-HSYI-----------------VYGPLANGAT-----TLMFEGvpnypdpgrfWEviDKHKV 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1415 KILC-----------GGEALPetlKRYFLDT----GS-------EAWNMFgptettiwsavqrindecsRATIGR---PI 1469
Cdd:PRK00174 341 TIFYtaptairalmkEGDEHP---KKYDLSSlrllGSvgepinpEAWEWY-------------------YKVVGGercPI 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1470 ANT-------QIYIT-------------------------DSQLAPVPAGVPGELCIAGD--GVAKGYYKKEEltdsRFI 1515
Cdd:PRK00174 399 VDTwwqtetgGIMITplpgatplkpgsatrplpgiqpavvDEEGNPLEGGEGGNLVIKDPwpGMMRTIYGDHE----RFV 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1516 DNPFEPGSKLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMDNLA-----AYYTA 1590
Cdd:PRK00174 475 KTYFSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKgqgiyAFVTL 554
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 1776025254 1591 KH---ANASLtARELRHFVKNALPAYMVPSyFIQL-DHMPLTPNGKIDRNSLKNI 1641
Cdd:PRK00174 555 KGgeePSDEL-RKELRNWVRKEIGPIAKPD-VIQFaPGLPKTRSGKIMRRILRKI 607
|
|
| PRK06484 |
PRK06484 |
short chain dehydrogenase; Validated |
2850-3015 |
5.64e-06 |
|
short chain dehydrogenase; Validated
Pssm-ID: 168574 [Multi-domain] Cd Length: 520 Bit Score: 52.54 E-value: 5.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGLLFAKEIANrtgrstivlTGRSVLSEDKENE--LEALRSIGAEVVYREADVSDQHAVHHLFEEIKERY 2927
Cdd:PRK06484 7 VVLVTGAAGGIGRAACQRFAR---------AGDQVVVADRNVEraRERADSLGPDHHALAMDVSDEAQIREGFEQLHREF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2928 GTLNGIIHGAGsIKDHF---IIHKTNEEFQEVLQPKVSG-LLHVDECSK----DFPLDFFIFFSSVSGCLGNAGQADYAA 2999
Cdd:PRK06484 78 GRIDVLVNNAG-VTDPTmtaTLDTTLEEFARLQAINLTGaYLVAREALRlmieQGHGAAIVNVASGAGLVALPKRTAYSA 156
|
170
....*....|....*.
gi 1776025254 3000 ANSFMDAFAeyrRSLA 3015
Cdd:PRK06484 157 SKAAVISLT---RSLA 169
|
|
| hydroxyacyl-CoA-like_DH_SDR_c-like |
cd05353 |
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ... |
2847-3025 |
7.15e-06 |
|
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids in eukaryotes occurs by a four-reaction cycle, that may take place in mitochondria or in peroxisomes. (3R)-hydroxyacyl-CoA dehydrogenase is part of rat peroxisomal multifunctional MFE-2, it is a member of the NAD-dependent SDRs, but contains an additional small C-terminal domain that completes the active site pocket and participates in dimerization. The atypical, additional C-terminal extension allows for more extensive dimerization contact than other SDRs. MFE-2 catalyzes the second and third reactions of the peroxisomal beta oxidation cycle. Proteins in this subgroup have a typical catalytic triad, but have a His in place of the usual upstream Asn. This subgroup also contains members identified as 17-beta-hydroxysteroid dehydrogenases, including human peroxisomal 17-beta-hydroxysteroid dehydrogenase type 4 (17beta-HSD type 4, aka MFE-2, encoded by HSD17B4 gene) which is involved in fatty acid beta-oxidation and steroid metabolism. This subgroup also includes two SDR domains of the Neurospora crassa and Saccharomyces cerevisiae multifunctional beta-oxidation protein (MFP, aka Fox2). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.
Pssm-ID: 187611 [Multi-domain] Cd Length: 250 Bit Score: 50.78 E-value: 7.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2847 DEGVYLITGGAGSLGLLFAKEIANRtGRSTIV------LTGRSVLSEDKENELEALRSIGAEVVYREADVSDQHAvhhLF 2920
Cdd:cd05353 4 DGRVVLVTGAGGGLGRAYALAFAER-GAKVVVndlggdRKGSGKSSSAADKVVDEIKAAGGKAVANYDSVEDGEK---IV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2921 EEIKERYGTLNGIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSGLLHVDECS----KDFPLDFFIFFSSVSGCLGNAGQAD 2996
Cdd:cd05353 80 KTAIDAFGRVDILVNNAGILRDRSFAKMSEEDWDLVMRVHLKGSFKVTRAAwpymRKQKFGRIINTSSAAGLYGNFGQAN 159
|
170 180
....*....|....*....|....*....
gi 1776025254 2997 YAAANSFMDAFAEyrrSLAASKKRFGSTI 3025
Cdd:cd05353 160 YSAAKLGLLGLSN---TLAIEGAKYNITC 185
|
|
| PRK12744 |
PRK12744 |
SDR family oxidoreductase; |
2850-2955 |
7.27e-06 |
|
SDR family oxidoreductase;
Pssm-ID: 183716 [Multi-domain] Cd Length: 257 Bit Score: 50.89 E-value: 7.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGLLFAKEIANRtGRSTIVLTGRSVLSE-DKENELEALRSIGAEVVYREADVSDQHAVHHLFEEIKERYG 2928
Cdd:PRK12744 10 VVLIAGGAKNLGGLIARDLAAQ-GAKAVAIHYNSAASKaDAEETVAAVKAAGAKAVAFQADLTTAAAVEKLFDDAKAAFG 88
|
90 100
....*....|....*....|....*..
gi 1776025254 2929 TLNGIIHGAGSIKDHFIIHKTNEEFQE 2955
Cdd:PRK12744 89 RPDIAINTVGKVLKKPIVEISEAEYDE 115
|
|
| PRK12936 |
PRK12936 |
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed |
2852-3056 |
7.40e-06 |
|
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
Pssm-ID: 171820 [Multi-domain] Cd Length: 245 Bit Score: 50.68 E-value: 7.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2852 LITGGAGSLGLLFAKeIANRTGrSTIVLTGRSVlsedkeNELEALRS-IGAEVVYREADVSDQHAVHHLFEEIKERYGTL 2930
Cdd:PRK12936 10 LVTGASGGIGEEIAR-LLHAQG-AIVGLHGTRV------EKLEALAAeLGERVKIFPANLSDRDEVKALGQKAEADLEGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2931 NGIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSGLLHVD-ECSKDFPLDFF---IFFSSVSGCLGNAGQADYAAANSFMDA 3006
Cdd:PRK12936 82 DILVNNAGITKDGLFVRMSDEDWDSVLEVNLTATFRLTrELTHPMMRRRYgriINITSVVGVTGNPGQANYCASKAGMIG 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3007 FAeyrRSLAASKKRFGSTISFNWPLWEEGGMqVGAEDEKRMLKTTGMVPM 3056
Cdd:PRK12936 162 FS---KSLAQEIATRNVTVNCVAPGFIESAM-TGKLNDKQKEAIMGAIPM 207
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
1302-1639 |
7.42e-06 |
|
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.
Pssm-ID: 341252 [Multi-domain] Cd Length: 473 Bit Score: 51.99 E-value: 7.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1302 YVIYTSGSTGKPKGVM--IPHKALTNFLVSMGETP-GLTAEDKMLAVT----TYCFDIAALELFLplikGAHCYI----C 1370
Cdd:cd05929 129 KMLYSGGTTGRPKGIKrgLPGGPPDNDTLMAAALGfGPGADSVYLSPAplyhAAPFRWSMTALFM----GGTLVLmekfD 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1371 QTEHTKDVEKLKRDIRTIKPTVMQatpatwKML-FYSGWENEENV---KILCGGEA-LPETLKRYFLDTGSEA-WNMFGP 1444
Cdd:cd05929 205 PEEFLRLIERYRVTFAQFVPTMFV------RLLkLPEAVRNAYDLsslKRVIHAAApCPPWVKEQWIDWGGPIiWEYYGG 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1445 TETtiwSAVQRINDE---CSRATIGRPIANtQIYITDSQLAPVPAGVPGELCIAGdGVAKGYYKKEELTDSRFIDNPFEP 1521
Cdd:cd05929 279 TEG---QGLTIINGEewlTHPGSVGRAVLG-KVHILDEDGNEVPPGEIGEVYFAN-GPGFEYTNDPEKTAAARNEGGWST 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1522 gsklyrTGDMArWLPGGRIEYIG-RIDNQVKIRGFRIELGDIESRLSEHPGILECVVV----ADMDN--LAAYYTAKHAN 1594
Cdd:cd05929 354 ------LGDVG-YLDEDGYLYLTdRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVgvpdEELGQrvHAVVQPAPGAD 426
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1776025254 1595 AS-LTARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLK 1639
Cdd:cd05929 427 AGtALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLR 472
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
23-243 |
7.45e-06 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 52.57 E-value: 7.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 23 ISEKQPATIPEVLYRTAAELGDTKGIIYlqpDGTEVyqSYRRLWDDGLRIVKGLRQSGLKAKQSVILQLGDNSQLLPAFW 102
Cdd:PRK08279 31 ITPDSKRSLGDVFEEAAARHPDRPALLF---EDQSI--SYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 103 GCVLTGVVPAPLavpptyaeSSSGTQK-LKDAWTLLDKPAVITDR-----------GMHQEMLDWAkEQGLEGFRAIIVE 170
Cdd:PRK08279 106 GLAKLGAVVALL--------NTQQRGAvLAHSLNLVDAKHLIVGEelveafeearaDLARPPRLWV-AGGDTLDDPEGYE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 171 DL--LSAEADTDWHQSSP----EDLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDH-VGGI 243
Cdd:PRK08279 177 DLaaAAAGAPTTNPASRSgvtaKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDVLYCCLPLYHnTGGT 256
|
|
| carb_red_PTCR-like_SDR_c |
cd05324 |
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ... |
4171-4372 |
9.76e-06 |
|
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR which catalyzes the NADPH-dependent reduction of ketones on steroids and prostaglandins. Unlike most SDRs, PTCR functions as a monomer. This subgroup also includes human carbonyl reductase 1 (CBR1) and CBR3. CBR1 is an NADPH-dependent SDR with broad substrate specificity and may be responsible for the in vivo reduction of quinones, prostaglandins, and other carbonyl-containing compounds. In addition it includes poppy NADPH-dependent salutaridine reductase which catalyzes the stereospecific reduction of salutaridine to 7(S)-salutaridinol in the biosynthesis of morphine, and Arabidopsis SDR1,a menthone reductase, which catalyzes the reduction of menthone to neomenthol, a compound with antimicrobial activity; SDR1 can also carry out neomenthol oxidation. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.
Pssm-ID: 187585 [Multi-domain] Cd Length: 225 Bit Score: 50.31 E-value: 9.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4171 HVLLITGGTRGIGLLCARHFAECYGVKkLVLTGReqlppreewarfktsNTSLAEkiQAVRELEAKGVQVEMLSLTLSDD 4250
Cdd:cd05324 1 KVALVTGANRGIGFEIVRQLAKSGPGT-VILTAR---------------DVERGQ--AAVEKLRAEGLSVRFHQLDVTDD 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4251 AQVEQTLQHIKRTLGPIGGVIHCAGLTdMDTLAFIRKTSDDIQRVMEPKVSGLttlyRHVCNE--PLqffvLFSSVSAII 4328
Cdd:cd05324 63 ASIEAAADFVEEKYGGLDILVNNAGIA-FKGFDDSTPTREQARETMKTNFFGT----VDVTQAllPL----LKKSPAGRI 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1776025254 4329 PELSAG----QADYAMA----NSYMDYFAEAHQK---HVPIISvqwPNWKETGMG 4372
Cdd:cd05324 134 VNVSSGlgslTSAYGVSkaalNALTRILAKELKEtgiKVNACC---PGWVKTDMG 185
|
|
| fabG |
PRK07666 |
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional |
2852-3000 |
1.01e-05 |
|
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
Pssm-ID: 236074 [Multi-domain] Cd Length: 239 Bit Score: 50.46 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2852 LITGGAGSLG----LLFAKEIANrtgrstIVLTGRSvlSEDKENELEALRSIGAEVVYREADVSDQHAVHHLFEEIKERY 2927
Cdd:PRK07666 11 LITGAGRGIGravaIALAKEGVN------VGLLART--EENLKAVAEEVEAYGVKVVIATADVSDYEEVTAAIEQLKNEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2928 GTLNGIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSGLLHV---------DECSKDfpldfFIFFSSVSGCLGNAGQADYA 2998
Cdd:PRK07666 83 GSIDILINNAGISKFGKFLELDPAEWEKIIQVNLMGVYYAtravlpsmiERQSGD-----IINISSTAGQKGAAVTSAYS 157
|
..
gi 1776025254 2999 AA 3000
Cdd:PRK07666 158 AS 159
|
|
| PRK12939 |
PRK12939 |
short chain dehydrogenase; Provisional |
4172-4302 |
1.36e-05 |
|
short chain dehydrogenase; Provisional
Pssm-ID: 183833 [Multi-domain] Cd Length: 250 Bit Score: 49.97 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4172 VLLITGGTRGIGllcaRHFAEcygvkKLVLTGreqlppreewARFKTSNTSLAEKIQAVRELEAKGVQVEMLSLTLSDDA 4251
Cdd:PRK12939 9 RALVTGAARGLG----AAFAE-----ALAEAG----------ATVAFNDGLAAEARELAAALEAAGGRAHAIAADLADPA 69
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1776025254 4252 QVEQTLQHIKRTLGPIGGVIHCAGLTDMDTLAFIrkTSDDIQRVMEPKVSG 4302
Cdd:PRK12939 70 SVQRFFDAAAAALGGLDGLVNNAGITNSKSATEL--DIDTWDAVMNVNVRG 118
|
|
| adh_short_C2 |
pfam13561 |
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ... |
4180-4310 |
1.44e-05 |
|
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) reductases.
Pssm-ID: 433310 [Multi-domain] Cd Length: 236 Bit Score: 49.74 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4180 RGIGLLCARHFAECyGVKkLVLTGReqlppreewarfktsNTSLAEKIQAVreleAKGVQVEMLSLTLSDDAQVEQTLQH 4259
Cdd:pfam13561 6 SGIGWAIARALAEE-GAE-VVLTDL---------------NEALAKRVEEL----AEELGAAVLPCDVTDEEQVEALVAA 64
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1776025254 4260 IKRTLGPIGGVIHCAGLTDMDTLAFIRKTSDDIQRVMEPKVSGLTTLYRHV 4310
Cdd:pfam13561 65 AVEKFGRLDILVNNAGFAPKLKGPFLDTSREDFDRALDVNLYSLFLLAKAA 115
|
|
| mannonate_red_SDR_c |
cd08935 |
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ... |
2850-2938 |
1.45e-05 |
|
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes the NAD-dependent interconversion of D-mannonate and D-fructuronate. This subgroup includes Bacillus subtitils UxuB/YjmF, a putative D-mannonate oxidoreductase; the B. subtilis UxuB gene is part of a putative ten-gene operon (the Yjm operon) involved in hexuronate catabolism. Escherichia coli UxuB does not belong to this subgroup. This subgroup has a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.
Pssm-ID: 187640 [Multi-domain] Cd Length: 271 Bit Score: 50.15 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGLLFAKEIAnRTGRSTIVLTGRSVLSEDKENELEALrsiGAEVVYREADVSDQHAVHHLFEEIKERYGT 2929
Cdd:cd08935 7 VAVITGGTGVLGGAMARALA-QAGAKVAALGRNQEKGDKVAKEITAL---GGRAIALAADVLDRASLERAREEIVAQFGT 82
|
....*....
gi 1776025254 2930 LNGIIHGAG 2938
Cdd:cd08935 83 VDILINGAG 91
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
400-555 |
1.64e-05 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 51.17 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 400 IGRFQVSGLSVTSGYYQRPDLNESVFtEDGWFETGDLGFLR-NGRLTITGRTKDAIIINGINYYSHAIESAVEELSEI-E 477
Cdd:PLN03102 392 MGEIVIKGSSIMKGYLKNPKATSEAF-KHGWLNTGDVGVIHpDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVlE 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 478 TSYTAACAVRLGQnsTDQLAIFFVTSAKLNDEQMSQLLRNIQSHVSQVIGVTPEYLLP---VQKEEIPKTAIGKIQRTQL 554
Cdd:PLN03102 471 TAVVAMPHPTWGE--TPCAFVVLEKGETTKEDRVDKLVTRERDLIEYCRENLPHFMCPrkvVFLQELPKNGNGKILKPKL 548
|
.
gi 1776025254 555 K 555
Cdd:PLN03102 549 R 549
|
|
| carb_red_sniffer_like_SDR_c |
cd05325 |
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ... |
2851-2967 |
1.78e-05 |
|
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl reductase of the classical SDR family. Studies in Drosophila melanogaster implicate Sniffer in the prevention of neurodegeneration due to aging and oxidative-stress. This subgroup also includes Rhodococcus sp. AD45 IsoH, which is an NAD-dependent 1-hydroxy-2-glutathionyl-2-methyl-3-butene dehydrogenase involved in isoprene metabolism, Aspergillus nidulans StcE encoded by a gene which is part of a proposed sterigmatocystin biosynthesis gene cluster, Bacillus circulans SANK 72073 BtrF encoded by a gene found in the butirosin biosynthesis gene cluster, and Aspergillus parasiticus nor-1 involved in the biosynthesis of aflatoxins. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.
Pssm-ID: 187586 [Multi-domain] Cd Length: 233 Bit Score: 49.60 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2851 YLITGGAGSLGLLFAKEIANRtGRSTIVLTGRSVlseDKENELEALRSIGAEVVYREADVSD--QHAVhhlfEEIKERYG 2928
Cdd:cd05325 1 VLITGASRGIGLELVRQLLAR-GNNTVIATCRDP---SAATELAALGASHSRLHILELDVTDeiAESA----EAVAERLG 72
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1776025254 2929 T--LNGIIHGAGsikdhfIIHKTN-------EEFQEVLQPKVSGLLHV 2967
Cdd:cd05325 73 DagLDVLINNAG------ILHSYGpasevdsEDLLEVFQVNVLGPLLL 114
|
|
| PRK08063 |
PRK08063 |
enoyl-[acyl-carrier-protein] reductase FabL; |
2850-2939 |
2.00e-05 |
|
enoyl-[acyl-carrier-protein] reductase FabL;
Pssm-ID: 236145 [Multi-domain] Cd Length: 250 Bit Score: 49.72 E-value: 2.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGLLFAKEIANRTGRSTIVLTGRSVLSEDKENELEALrsiGAEVVYREADVSDQHAVHHLFEEIKERYGT 2929
Cdd:PRK08063 6 VALVTGSSRGIGKAIALRLAEEGYDIAVNYARSRKAAEETAEEIEAL---GRKALAVKANVGDVEKIKEMFAQIDEEFGR 82
|
90
....*....|
gi 1776025254 2930 LNGIIHGAGS 2939
Cdd:PRK08063 83 LDVFVNNAAS 92
|
|
| DH-DHB-DH_SDR_c |
cd05331 |
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ... |
4174-4312 |
2.05e-05 |
|
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 dihydrozybenzoate dehydrogenase shares the characteristics of the classical SDRs. This subgroup includes Escherichai coli EntA which catalyzes the NAD+-dependent oxidation of 2,3-dihydro-2,3-dihydroxybenzoate to 2,3-dihydroxybenzoate during biosynthesis of the siderophore Enterobactin. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.
Pssm-ID: 187592 [Multi-domain] Cd Length: 244 Bit Score: 49.39 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4174 LITGGTRGIGLLCARHFAECyGVKKLVLTGREQlppreewarfktsntslaekiqavrELEAKGVQVEMLSLTLSDDAQV 4253
Cdd:cd05331 2 IVTGAAQGIGRAVARHLLQA-GATVIALDLPFV-------------------------LLLEYGDPLRLTPLDVADAAAV 55
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1776025254 4254 EQTLQHIKRTLGPIGGVIHCAGLTDMDtlAFIRKTSDDIQRVMEPKVSGLTTLYRHVCN 4312
Cdd:cd05331 56 REVCSRLLAEHGPIDALVNCAGVLRPG--ATDPLSTEDWEQTFAVNVTGVFNLLQAVAP 112
|
|
| cyclohexanol_reductase_SDR_c |
cd05330 |
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ... |
2850-3045 |
2.16e-05 |
|
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol reductases,including (6R)-2,2,6-trimethyl-1,4-cyclohexanedione (levodione) reductase of Corynebacterium aquaticum, catalyze the reversible oxidoreduction of hydroxycyclohexanone derivatives. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.
Pssm-ID: 187591 [Multi-domain] Cd Length: 257 Bit Score: 49.44 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGLLFAKEIANRTGRSTIVLTGRSVLSEDKENELEALRSigAEVVYREADVSDQHAVHHLFEEIKERYGT 2929
Cdd:cd05330 5 VVLITGGGSGLGLATAVRLAKEGAKLSLVDLNEEGLEAAKAALLEIAPD--AEVLLIKADVSDEAQVEAYVDATVEQFGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2930 LNGIIHGAG-SIKDHFIIHKTNEEFQEVLQPKVS----GLLHVDECSKDFPLDFFIFFSSVSGCLGNAGQADYAAANSfm 3004
Cdd:cd05330 83 IDGFFNNAGiEGKQNLTEDFGADEFDKVVSINLRgvfyGLEKVLKVMREQGSGMIVNTASVGGIRGVGNQSGYAAAKH-- 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1776025254 3005 dAFAEYRRSLAASKKRFGSTI------SFNWPLWEEGGMQVGAEDEK 3045
Cdd:cd05330 161 -GVVGLTRNSAVEYGQYGIRInaiapgAILTPMVEGSLKQLGPENPE 206
|
|
| SDR_c6 |
cd05350 |
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ... |
2852-3069 |
2.31e-05 |
|
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a canonical active site tetrad and a fairly well conserved typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.
Pssm-ID: 187608 [Multi-domain] Cd Length: 239 Bit Score: 49.25 E-value: 2.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2852 LITGGAGSLGLLFAKEIANRtGRStIVLTGRsvlsedKENELEALRS------IGAEVVyrEADVSDQHAVHHLFEEIKE 2925
Cdd:cd05350 2 LITGASSGIGRALAREFAKA-GYN-VALAAR------RTDRLDELKAellnpnPSVEVE--ILDVTDEERNQLVIAELEA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2926 RYGTLNGIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSGLLHVDECSkdfpLDFF--------IFFSSVSGCLGNAGQADY 2997
Cdd:cd05350 72 ELGGLDLVIINAGVGKGTSLGDLSFKAFRETIDTNLLGAAAILEAA----LPQFrakgrghlVLISSVAALRGLPGAAAY 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1776025254 2998 AAANSFMDAFAEyrrSLAASKKRFGSTISFNWPlweegGMqVGAEDEKRMLKTTGMvpMPTDSGLKAFYQGI 3069
Cdd:cd05350 148 SASKAALSSLAE---SLRYDVKKRGIRVTVINP-----GF-IDTPLTANMFTMPFL--MSVEQAAKRIYKAI 208
|
|
| PRK09072 |
PRK09072 |
SDR family oxidoreductase; |
4169-4297 |
2.70e-05 |
|
SDR family oxidoreductase;
Pssm-ID: 236372 [Multi-domain] Cd Length: 263 Bit Score: 49.17 E-value: 2.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4169 KDHVLLITGGTRGIGLLCARHFAECyGVkKLVLTGREqlppreewarfktsntslAEKIQAVRELEAKGVQVEMLSLTLS 4248
Cdd:PRK09072 4 KDKRVLLTGASGGIGQALAEALAAA-GA-RLLLVGRN------------------AEKLEALAARLPYPGRHRWVVADLT 63
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1776025254 4249 DDAQVEQTLQHIKRtLGPIGGVIHCAGLTDMDTLAfiRKTSDDIQRVME 4297
Cdd:PRK09072 64 SEAGREAVLARARE-MGGINVLINNAGVNHFALLE--DQDPEAIERLLA 109
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
1175-1345 |
2.77e-05 |
|
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.
Pssm-ID: 341231 [Multi-domain] Cd Length: 571 Bit Score: 50.42 E-value: 2.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1175 EGQTLTYRELDERSTQLAIYLQAH-GVGP-DRLAGIYVDrSLDMLVGLLAILKAGGAYVPLDPSYPAERLEYMLEDSEVF 1252
Cdd:cd05905 11 EATTLTWGKLLSRAEKIAAVLQKKvGLKPgDRVALMYPD-PLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLLGTCKVR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1253 ITLTTsELVNT----LSWNGVTTALLDQD--WDEIAQTASDRKVLTRTVTP---------ENLAYVIYTSGSTGKPKGVM 1317
Cdd:cd05905 90 VALTV-EACLKglpkKLLKSKTAAEIAKKkgWPKILDFVKIPKSKRSKLKKwgphpptrdGDTAYIEYSFSSDGSLSGVA 168
|
170 180
....*....|....*....|....*...
gi 1776025254 1318 IPHKALTNFLVSMGETPGLTAEDKMLAV 1345
Cdd:cd05905 169 VSHSSLLAHCRALKEACELYESRPLVTV 196
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
1512-1651 |
2.99e-05 |
|
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.
Pssm-ID: 341265 [Multi-domain] Cd Length: 629 Bit Score: 50.35 E-value: 2.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1512 SRFIDNPFE--PGskLYRTGDMARWLPGGRIEYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVA----DMDNLA 1585
Cdd:cd05943 472 SRYRAAYFAkyPG--VWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGqewkDGDERV 549
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1776025254 1586 AYYTAKHANASLT---ARELRHFVKNALPAYMVPSYFIQLDHMPLTPNGKIDRNSLKNIdLSGEQLKQR 1651
Cdd:cd05943 550 ILFVKLREGVELDdelRKRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGKKVEVAVKKI-IAGRPVKNA 617
|
|
| PRK08085 |
PRK08085 |
gluconate 5-dehydrogenase; Provisional |
4173-4276 |
3.22e-05 |
|
gluconate 5-dehydrogenase; Provisional
Pssm-ID: 181225 [Multi-domain] Cd Length: 254 Bit Score: 48.98 E-value: 3.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4173 LLITGGTRGIGLLCARHFAEcYGVKKLVltgreqlppreewarfktsNTSLAEKIQ-AVRELEAKGVQVEMLSLTLSDDA 4251
Cdd:PRK08085 12 ILITGSAQGIGFLLATGLAE-YGAEIII-------------------NDITAERAElAVAKLRQEGIKAHAAPFNVTHKQ 71
|
90 100
....*....|....*....|....*
gi 1776025254 4252 QVEQTLQHIKRTLGPIGGVIHCAGL 4276
Cdd:PRK08085 72 EVEAAIEHIEKDIGPIDVLINNAGI 96
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
398-555 |
3.24e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 50.33 E-value: 3.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 398 GE-IGRFQVSGLSVTSGYYQRPDLNESVFtEDGWFETGDLGFLR-NGRLTITGRTKDAIIINGINYYSHAIESAVEELSE 475
Cdd:PRK08162 385 GEtIGEIMFRGNIVMKGYLKNPKATEEAF-AGGWFHTGDLAVLHpDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPA 463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 476 IETSYTAA----------CA-VRLGQNSTdqlaiffVTSAKlndeqmsqllrnIQSHVSQVIgvtPEYLLP--VQKEEIP 542
Cdd:PRK08162 464 VLVAAVVAkpdpkwgevpCAfVELKDGAS-------ATEEE------------IIAHCREHL---AGFKVPkaVVFGELP 521
|
170
....*....|...
gi 1776025254 543 KTAIGKIQRTQLK 555
Cdd:PRK08162 522 KTSTGKIQKFVLR 534
|
|
| retinol-DH_like_SDR_c_like |
cd05327 |
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ... |
4172-4275 |
3.87e-05 |
|
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) OxidoReductase (LPOR) and related proteins, classical (c) SDRs; Classical SDR subgroup containing retinol-DHs, LPORs, and related proteins. Retinol is processed by a medium chain alcohol dehydrogenase followed by retinol-DHs. Pchlide reductases act in chlorophyll biosynthesis. There are distinct enzymes that catalyze Pchlide reduction in light or dark conditions. Light-dependent reduction is via an NADP-dependent SDR, LPOR. Proteins in this subfamily share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. This subgroup includes the human proteins: retinol dehydrogenase -12, -13 ,and -14, dehydrogenase/reductase SDR family member (DHRS)-12 , -13 and -X (a DHRS on chromosome X), and WWOX (WW domain-containing oxidoreductase), as well as a Neurospora crassa SDR encoded by the blue light inducible bli-4 gene. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.
Pssm-ID: 212492 [Multi-domain] Cd Length: 269 Bit Score: 48.76 E-value: 3.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4172 VLLITGGTRGIGLLCARHFAEcYGVkKLVLTGREQlppreewarfktsntslaEKIQAVRE---LEAKGVQVEMLSLTLS 4248
Cdd:cd05327 3 VVVITGANSGIGKETARELAK-RGA-HVIIACRNE------------------EKGEEAAAeikKETGNAKVEVIQLDLS 62
|
90 100
....*....|....*....|....*..
gi 1776025254 4249 DDAQVEQTLQHIKRTLGPIGGVIHCAG 4275
Cdd:cd05327 63 SLASVRQFAEEFLARFPRLDILINNAG 89
|
|
| BKR_like_SDR_like |
cd05344 |
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ... |
2850-2966 |
4.08e-05 |
|
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup resembles the SDR family, but does not have a perfect match to the NAD-binding motif or the catalytic tetrad characteristic of the SDRs. It includes the SDRs, Q9HYA2 from Pseudomonas aeruginosa PAO1 and APE0912 from Aeropyrum pernix K1. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.
Pssm-ID: 187602 [Multi-domain] Cd Length: 253 Bit Score: 48.81 E-value: 4.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGLLFAKEIAnRTGrSTIVLTGRSVlsEDKENELEALRSIGAEVVYREADVSDQHAVHHLFEEIKERYGT 2929
Cdd:cd05344 3 VALVTAASSGIGLAIARALA-REG-ARVAICARNR--ENLERAASELRAGGAGVLAVVADLTDPEDIDRLVEKAGDAFGR 78
|
90 100 110
....*....|....*....|....*....|....*..
gi 1776025254 2930 LNGIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSGLLH 2966
Cdd:cd05344 79 VDILVNNAGGPPPGPFAELTDEDWLEAFDLKLLSVIR 115
|
|
| PRK05875 |
PRK05875 |
short chain dehydrogenase; Provisional |
2847-2938 |
4.26e-05 |
|
short chain dehydrogenase; Provisional
Pssm-ID: 180300 [Multi-domain] Cd Length: 276 Bit Score: 48.65 E-value: 4.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2847 DEGVYLITGGAGSLGLLFAKEIANRTGRSTIVltGRSvlsEDK----ENELEALRSIGAeVVYREADVSDQHAVHHLFEE 2922
Cdd:PRK05875 6 QDRTYLVTGGGSGIGKGVAAGLVAAGAAVMIV--GRN---PDKlaaaAEEIEALKGAGA-VRYEPADVTDEDQVARAVDA 79
|
90
....*....|....*.
gi 1776025254 2923 IKERYGTLNGIIHGAG 2938
Cdd:PRK05875 80 ATAWHGRLHGVVHCAG 95
|
|
| BKR_2_SDR_c |
cd05349 |
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ... |
2850-3025 |
4.81e-05 |
|
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) SDR; This subgroup includes Rhizobium sp. NGR234 FabG1. The Escherichai coli K12 BKR, FabG, belongs to a different subgroup. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.
Pssm-ID: 187607 [Multi-domain] Cd Length: 246 Bit Score: 48.22 E-value: 4.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGLLFAKEIAnRTGRSTIVLTGRSVLSEDKeneleALRSIGAEVVYREADVSDQHAVHHLFEEIKERYGT 2929
Cdd:cd05349 2 VVLVTGASRGLGAAIARSFA-REGARVVVNYYRSTESAEA-----VAAEAGERAIAIQADVRDRDQVQAMIEEAKNHFGP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2930 LNGIIHGA-GSIKDHFIIHKTNEE-----FQEVLQPKVSGLLHV-DECSKDFPldffiffSSVSGCLGNAGQ-------- 2994
Cdd:cd05349 76 VDTIVNNAlIDFPFDPDQRKTFDTidwedYQQQLEGAVKGALNLlQAVLPDFK-------ERGSGRVINIGTnlfqnpvv 148
|
170 180 190
....*....|....*....|....*....|...
gi 1776025254 2995 --ADYAAANSFMDAFAeyrRSLAASKKRFGSTI 3025
Cdd:cd05349 149 pyHDYTTAKAALLGFT---RNMAKELGPYGITV 178
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
3413-3537 |
6.20e-05 |
|
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl synthase (pfam00109), and also chalcone synthase.
Pssm-ID: 459676 [Multi-domain] Cd Length: 260 Bit Score: 48.07 E-value: 6.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 3413 FGISPREADYVDpqqrLLMTYVWKALEDAGCPPQSLSGtgtgIFIGTGNTGYKD------LFHRANLPieghaatgHMIP 3486
Cdd:pfam00108 14 FGGSLKDVSAVE----LGAEAIKAALERAGVDPEDVDE----VIVGNVLQAGEGqnparqAALKAGIP--------DSAP 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1776025254 3487 SVGPNRMsyflnihgpsepvetaCSSSLVAIHRAVTAMQNGDCEMAIAGGV 3537
Cdd:pfam00108 78 AVTINKV----------------CGSGLKAVYLAAQSIASGDADVVLAGGV 112
|
|
| PRK08628 |
PRK08628 |
SDR family oxidoreductase; |
4169-4278 |
7.29e-05 |
|
SDR family oxidoreductase;
Pssm-ID: 181508 [Multi-domain] Cd Length: 258 Bit Score: 48.03 E-value: 7.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4169 KDHVLLITGGTRGIGLLCARHFAECYGVKklVLTGREqlppreewarfktsntslAEKIQAVRELEAKGVQVEMLSLTLS 4248
Cdd:PRK08628 6 KDKVVIVTGGASGIGAAISLRLAEEGAIP--VIFGRS------------------APDDEFAEELRALQPRAEFVQVDLT 65
|
90 100 110
....*....|....*....|....*....|
gi 1776025254 4249 DDAQVEQTLQHIKRTLGPIGGVIHCAGLTD 4278
Cdd:PRK08628 66 DDAQCRDAVEQTVAKFGRIDGLVNNAGVND 95
|
|
| PRK06483 |
PRK06483 |
dihydromonapterin reductase; Provisional |
2852-2937 |
7.81e-05 |
|
dihydromonapterin reductase; Provisional
Pssm-ID: 180586 [Multi-domain] Cd Length: 236 Bit Score: 47.62 E-value: 7.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2852 LITGGAGSLGLLFAKEIANRtgRSTIVLTGRSvlsedKENELEALRSIGAEVVYreADVSDQHAVHHLFEEIKERYGTLN 2931
Cdd:PRK06483 6 LITGAGQRIGLALAWHLLAQ--GQPVIVSYRT-----HYPAIDGLRQAGAQCIQ--ADFSTNAGIMAFIDELKQHTDGLR 76
|
....*.
gi 1776025254 2932 GIIHGA 2937
Cdd:PRK06483 77 AIIHNA 82
|
|
| AcpA |
COG3433 |
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ... |
4393-4531 |
8.49e-05 |
|
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442659 [Multi-domain] Cd Length: 295 Bit Score: 48.21 E-value: 8.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4393 LRFLDQIVSKMFGPVVLPAManqtnwEPELLMKRRKPHEGGLQEAALQSPPARDIEEADevskcdGLLSETQSWLIDLFT 4472
Cdd:COG3433 162 LAALDKVPPDVVAASAVVAL------DALLLLALKVVARAAPALAAAEALLAAASPAPA------LETALTEEELRADVA 229
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1776025254 4473 EELRIDREDFEIDGLFQDYGVDSIILAQVLQRInRKLEAALDPSILYEYPTIQRFTDWL 4531
Cdd:COG3433 230 ELLGVDPEEIDPDDNLFDLGLDSIRLMQLVERW-RKAGLDVSFADLAEHPTLAAWWALL 287
|
|
| PRK06181 |
PRK06181 |
SDR family oxidoreductase; |
2850-2961 |
8.64e-05 |
|
SDR family oxidoreductase;
Pssm-ID: 235726 [Multi-domain] Cd Length: 263 Bit Score: 47.67 E-value: 8.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGLLFAKEIAnRTGRStIVLTGRSvlsEDKENEL-EALRSIGAEVVYREADVSDQHAVHHLFEEIKERYG 2928
Cdd:PRK06181 3 VVIITGASEGIGRALAVRLA-RAGAQ-LVLAARN---ETRLASLaQELADHGGEALVVPTDVSDAEACERLIEAAVARFG 77
|
90 100 110
....*....|....*....|....*....|...
gi 1776025254 2929 TLNGIIHGAGsikdhfIIHKTNeeFQEVLQPKV 2961
Cdd:PRK06181 78 GIDILVNNAG------ITMWSR--FDELTDLSV 102
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
1466-1641 |
1.06e-04 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 48.45 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1466 GRPIANTQIYITDSQLapvpagvpGELCIAGDGVAKGYYKKeeltdsrFIDNPfepgsKLYRTGDMARWLPGGRIEYIGR 1545
Cdd:PRK07445 286 GQVLPHAQITIPANQT--------GNITIQAQSLALGYYPQ-------ILDSQ-----GIFETDDLGYLDAQGYLHILGR 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1546 IDNQVKIRGFRIELGDIESRLSEhPGILE--CVV-VADMD---NLAAYYTAKHANASLtaRELRHFVKNALPAYMVPSYF 1619
Cdd:PRK07445 346 NSQKIITGGENVYPAEVEAAILA-TGLVQdvCVLgLPDPHwgeVVTAIYVPKDPSISL--EELKTAIKDQLSPFKQPKHW 422
|
170 180
....*....|....*....|..
gi 1776025254 1620 IQLDHMPLTPNGKIDRNSLKNI 1641
Cdd:PRK07445 423 IPVPQLPRNPQGKINRQQLQQI 444
|
|
| PRK08213 |
PRK08213 |
gluconate 5-dehydrogenase; Provisional |
2852-2964 |
1.25e-04 |
|
gluconate 5-dehydrogenase; Provisional
Pssm-ID: 181295 [Multi-domain] Cd Length: 259 Bit Score: 47.25 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2852 LITGGAGSLGLlfakEIANRTGR--STIVLTGRsvlsedKENELEA----LRSIGAEVVYREADVSDQHAVHHLFEEIKE 2925
Cdd:PRK08213 16 LVTGGSRGLGL----QIAEALGEagARVVLSAR------KAEELEEaaahLEALGIDALWIAADVADEADIERLAEETLE 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1776025254 2926 RYGTLNGIIHGAGS-----IKDHFIihktnEEFQEVLQPKVSGL 2964
Cdd:PRK08213 86 RFGHVDILVNNAGAtwgapAEDHPV-----EAWDKVMNLNVRGL 124
|
|
| PRK07454 |
PRK07454 |
SDR family oxidoreductase; |
4174-4296 |
1.27e-04 |
|
SDR family oxidoreductase;
Pssm-ID: 180984 [Multi-domain] Cd Length: 241 Bit Score: 46.88 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4174 LITGGTRGIGLLCARHFAECyGVKkLVLTGREQlppreewarfktsntslaEKIQAVR-ELEAKGVQVEMLSLTLSDDAQ 4252
Cdd:PRK07454 10 LITGASSGIGKATALAFAKA-GWD-LALVARSQ------------------DALEALAaELRSTGVKAAAYSIDLSNPEA 69
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1776025254 4253 VEQTLQHIKRTLGPIGGVIHCAGLTDMDTLAfirKTS-DDIQRVM 4296
Cdd:PRK07454 70 IAPGIAELLEQFGCPDVLINNAGMAYTGPLL---EMPlSDWQWVI 111
|
|
| PRK07067 |
PRK07067 |
L-iditol 2-dehydrogenase; |
2850-2965 |
1.63e-04 |
|
L-iditol 2-dehydrogenase;
Pssm-ID: 235925 [Multi-domain] Cd Length: 257 Bit Score: 46.94 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGLLFAKEIANRTGRSTIVltgrsvlSEDKENELEALRSIGAEVVYREADVSDQHAVHHLFEEIKERYGT 2929
Cdd:PRK07067 8 VALLTGAASGIGEAVAERYLAEGARVVIA-------DIKPARARLAALEIGPAAIAVSLDVTRQDSIDRIVAAAVERFGG 80
|
90 100 110
....*....|....*....|....*....|....*.
gi 1776025254 2930 LNGIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSGLL 2965
Cdd:PRK07067 81 IDILFNNAALFDMAPILDISRDSYDRLFAVNVKGLF 116
|
|
| PRK07677 |
PRK07677 |
short chain dehydrogenase; Provisional |
4172-4274 |
1.67e-04 |
|
short chain dehydrogenase; Provisional
Pssm-ID: 181077 [Multi-domain] Cd Length: 252 Bit Score: 46.60 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4172 VLLITGGTRGIGLLCARHFAEcYGVKkLVLTGREQlppreewarfktsntslaEKI-QAVRELEAKGVQVEMLSLTLSDD 4250
Cdd:PRK07677 3 VVIITGGSSGMGKAMAKRFAE-EGAN-VVITGRTK------------------EKLeEAKLEIEQFPGQVLTVQMDVRNP 62
|
90 100
....*....|....*....|....
gi 1776025254 4251 AQVEQTLQHIKRTLGPIGGVIHCA 4274
Cdd:PRK07677 63 EDVQKMVEQIDEKFGRIDALINNA 86
|
|
| PRK08251 |
PRK08251 |
SDR family oxidoreductase; |
2852-2938 |
1.73e-04 |
|
SDR family oxidoreductase;
Pssm-ID: 181324 [Multi-domain] Cd Length: 248 Bit Score: 46.47 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2852 LITGGAGSLGLLFAKEIANRtGRStIVLTGRSV--LSEDKEnELEAlRSIGAEVVYREADVSDQHAVHHLFEEIKERYGT 2929
Cdd:PRK08251 6 LITGASSGLGAGMAREFAAK-GRD-LALCARRTdrLEELKA-ELLA-RYPGIKVAVAALDVNDHDQVFEVFAEFRDELGG 81
|
....*....
gi 1776025254 2930 LNGIIHGAG 2938
Cdd:PRK08251 82 LDRVIVNAG 90
|
|
| PRK06484 |
PRK06484 |
short chain dehydrogenase; Validated |
4172-4302 |
1.81e-04 |
|
short chain dehydrogenase; Validated
Pssm-ID: 168574 [Multi-domain] Cd Length: 520 Bit Score: 47.92 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4172 VLLITGGTRGIGLLCARHFAECYGVkkLVLTGREQLPPREEWARFKTSNTSLAekiqavreleakgvqvemlsLTLSDDA 4251
Cdd:PRK06484 7 VVLVTGAAGGIGRAACQRFARAGDQ--VVVADRNVERARERADSLGPDHHALA--------------------MDVSDEA 64
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1776025254 4252 QVEQTLQHIKRTLGPIGGVIHCAGLTDMDTLAFIRKTSDDIQRVMEPKVSG 4302
Cdd:PRK06484 65 QIREGFEQLHREFGRIDVLVNNAGVTDPTMTATLDTTLEEFARLQAINLTG 115
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
61-258 |
1.83e-04 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 47.67 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 61 SYRRLWDDGLRIVKGL-RQSGLKAKQSVILQLGdNSQLLPAFW------GCVLTGVVPAPLAVPPTYAESSSGTQKLKDA 133
Cdd:cd05938 7 TYRDVDRRSNQAARALlAHAGLRPGDTVALLLG-NEPAFLWIWlglaklGCPVAFLNTNIRSKSLLHCFRCCGAKVLVVA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 134 WTLLDkpAVitdrgmhQEMLDWAKEQGL-----------EGFRAIIveDLLSAEADT----DWH-QSSPEDLALLLLTSG 197
Cdd:cd05938 86 PELQE--AV-------EEVLPALRADGVsvwylshtsntEGVISLL--DKVDAASDEpvpaSLRaHVTIKSPALYIYTSG 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1776025254 198 STGTPKAVMLNHRNIMsMVKGIIQMQGFTREDITFNWMPFDHVGG--IGMlhlrdvyLGCQEI 258
Cdd:cd05938 155 TTGLPKAARISHLRVL-QCSGFLSLCGVTADDVIYITLPLYHSSGflLGI-------GGCIEL 209
|
|
| SDR_c8 |
cd08930 |
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ... |
2850-2957 |
1.91e-04 |
|
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad and domain size of the classical SDRs, but has an atypical NAD-binding motif ([ST]G[GA]XGXXG). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.
Pssm-ID: 187635 [Multi-domain] Cd Length: 250 Bit Score: 46.56 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGLLFAKEIANRTGRstIVLTGRSVLS-EDKENELEALRsiGAEVVYREADVSDQHAVHHLFEEIKERYG 2928
Cdd:cd08930 4 IILITGAAGLIGKAFCKALLSAGAR--LILADINAPAlEQLKEELTNLY--KNRVIALELDITSKESIKELIESYLEKFG 79
|
90 100 110
....*....|....*....|....*....|..
gi 1776025254 2929 TLNGIIHGAG-SIKDHFI--IHKTNEEFQEVL 2957
Cdd:cd08930 80 RIDILINNAYpSPKVWGSrfEEFPYEQWNEVL 111
|
|
| PRK06125 |
PRK06125 |
short chain dehydrogenase; Provisional |
4174-4308 |
2.10e-04 |
|
short chain dehydrogenase; Provisional
Pssm-ID: 235703 [Multi-domain] Cd Length: 259 Bit Score: 46.58 E-value: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4174 LITGGTRGIGLLCARHFAE--CYgvkkLVLTGREqlppreewarfktsntslAEKI-QAVRELEAK-GVQVEMLSLTLSD 4249
Cdd:PRK06125 11 LITGASKGIGAAAAEAFAAegCH----LHLVARD------------------ADALeALAADLRAAhGVDVAVHALDLSS 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1776025254 4250 DAQVEQtlqhIKRTLGPI------GGVIHCAGLTDMDTLAFirktsddiQRVMEPKVSGLTTLYR 4308
Cdd:PRK06125 69 PEAREQ----LAAEAGDIdilvnnAGAIPGGGLDDVDDAAW--------RAGWELKVFGYIDLTR 121
|
|
| PRK05872 |
PRK05872 |
short chain dehydrogenase; Provisional |
2850-2938 |
2.15e-04 |
|
short chain dehydrogenase; Provisional
Pssm-ID: 235633 [Multi-domain] Cd Length: 296 Bit Score: 46.89 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGLLFAKEIANRTGRstIVLTGrsvLSEDKENELEALRSIGAEVVYREADVSDQHAVHHLFEEIKERYGT 2929
Cdd:PRK05872 11 VVVVTGAARGIGAELARRLHARGAK--LALVD---LEEAELAALAAELGGDDRVLTVVADVTDLAAMQAAAEEAVERFGG 85
|
....*....
gi 1776025254 2930 LNGIIHGAG 2938
Cdd:PRK05872 86 IDVVVANAG 94
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
188-243 |
2.15e-04 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 47.35 E-value: 2.15e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1776025254 188 DLALLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDH-VGGI 243
Cdd:cd05940 82 DAALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGALPSDVLYTCLPLYHsTALI 138
|
|
| fabG |
PRK07666 |
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional |
4169-4302 |
2.25e-04 |
|
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
Pssm-ID: 236074 [Multi-domain] Cd Length: 239 Bit Score: 46.22 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4169 KDHVLLITGGTRGIGLLCARHFAEcYGVKkLVLTGREqlppreewarfktsntslAEKIQAV-RELEAKGVQVEMLSLTL 4247
Cdd:PRK07666 6 QGKNALITGAGRGIGRAVAIALAK-EGVN-VGLLART------------------EENLKAVaEEVEAYGVKVVIATADV 65
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1776025254 4248 SDDAQVEQTLQHIKRTLGPIGGVIHCAGLTDMDTlaFIRKTSDDIQRVMEPKVSG 4302
Cdd:PRK07666 66 SDYEEVTAAIEQLKNELGSIDILINNAGISKFGK--FLELDPAEWEKIIQVNLMG 118
|
|
| 17beta-HSDXI-like_SDR_c |
cd05339 |
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ... |
4172-4340 |
2.28e-04 |
|
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid dehydrogenases (17betaHSD) are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. 17betaHSD type XI, a classical SDR, preferentially converts 3alpha-Adiol to androsterone but not numerous other tested steroids. This subgroup of classical SDRs also includes members identified as retinol dehydrogenases, which convert retinol to retinal, a property that overlaps with 17betaHSD activity. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.
Pssm-ID: 187598 [Multi-domain] Cd Length: 243 Bit Score: 46.08 E-value: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4172 VLLITGGTRGIGLLCARHFAECYGvkKLVLtgreqlppreeWARFKTSNTSLAEKIqavrelEAKGVQVEMLSLTLSDDA 4251
Cdd:cd05339 1 IVLITGGGSGIGRLLALEFAKRGA--KVVI-----------LDINEKGAEETANNV------RKAGGKVHYYKCDVSKRE 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4252 QVEQTLQHIKRTLGPIGGVIHCAGLtdMDTLAFIRKTSDDIQRVMEPKVSGLTTLYRHVCNEPLQ----FFVLFSSVSAI 4327
Cdd:cd05339 62 EVYEAAKKIKKEVGDVTILINNAGV--VSGKKLLELPDEEIEKTFEVNTLAHFWTTKAFLPDMLErnhgHIVTIASVAGL 139
|
170
....*....|...
gi 1776025254 4328 IPelSAGQADYAM 4340
Cdd:cd05339 140 IS--PAGLADYCA 150
|
|
| PRK13394 |
PRK13394 |
3-hydroxybutyrate dehydrogenase; Provisional |
2850-3000 |
2.38e-04 |
|
3-hydroxybutyrate dehydrogenase; Provisional
Pssm-ID: 184025 [Multi-domain] Cd Length: 262 Bit Score: 46.43 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGLLFAKEIAnRTGrSTIVLTGrsvLSEDKENE-LEALRSIGAEVVYREADVSDQHAVHHLFEEIKERYG 2928
Cdd:PRK13394 9 TAVVTGAASGIGKEIALELA-RAG-AAVAIAD---LNQDGANAvADEINKAGGKAIGVAMDVTNEDAVNAGIDKVAERFG 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1776025254 2929 TLNGIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSGLLHVDECS-----KDFPLDFFIFFSSVSGCLGNAGQADYAAA 3000
Cdd:PRK13394 84 SVDILVSNAGIQIVNPIENYSFADWKKMQAIHVDGAFLTTKAAlkhmyKDDRGGVVIYMGSVHSHEASPLKSAYVTA 160
|
|
| KAsynt_C_assoc |
pfam16197 |
Ketoacyl-synthetase C-terminal extension; KAsynt_C_assoc represents the very C-terminus of a ... |
4973-5010 |
2.77e-04 |
|
Ketoacyl-synthetase C-terminal extension; KAsynt_C_assoc represents the very C-terminus of a subset of proteins from the keto-acyl-synthetase 2 family. It is found in proteins ranging from bacteria to human.
Pssm-ID: 465059 [Multi-domain] Cd Length: 111 Bit Score: 43.30 E-value: 2.77e-04
10 20 30
....*....|....*....|....*....|....*...
gi 1776025254 4973 AAINCFADGGTNVHVIVEAWEKdeKHAIKRSPKSPPQL 5010
Cdd:pfam16197 27 VGVNSFGFGGANAHVILKSNPK--PKIPPESPDNLPRL 62
|
|
| AcpA |
COG3433 |
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ... |
576-666 |
3.32e-04 |
|
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442659 [Multi-domain] Cd Length: 295 Bit Score: 46.28 E-value: 3.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 576 AVQDEEMQQADHVKRV---REEIQEHLLTCLTEELHVSRDWVEPNANIQSLGVNSIKMMKLIRSIEKNyHIKLTAREIHQ 652
Cdd:COG3433 198 ALAAAEALLAAASPAPaleTALTEEELRADVAELLGVDPEEIDPDDNLFDLGLDSIRLMQLVERWRKA-GLDVSFADLAE 276
|
90
....*....|....
gi 1776025254 653 YPTIERLASYLSEH 666
Cdd:COG3433 277 HPTLAAWWALLAAA 290
|
|
| SDR |
cd02266 |
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ... |
2852-3077 |
3.46e-04 |
|
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase (KR) domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.
Pssm-ID: 187535 [Multi-domain] Cd Length: 186 Bit Score: 44.81 E-value: 3.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2852 LITGGAGSLGLLFAKEIANRTGRSTIVLTGRSVLsedkenelealrsigaevvyreadvsdqhavhhlfeeikerygtln 2931
Cdd:cd02266 2 LVTGGSGGIGGAIARWLASRGSPKVLVVSRRDVV---------------------------------------------- 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2932 giIHGAGSIKDHFIIHKTNEEFQEVLQPKVSGLLHVDECSKdfPLDF------FIFFSSVSGCLGNAGQADYAAANSFMD 3005
Cdd:cd02266 36 --VHNAAILDDGRLIDLTGSRIERAIRANVVGTRRLLEAAR--ELMKakrlgrFILISSVAGLFGAPGLGGYAASKAALD 111
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1776025254 3006 AFAEYRRSLAASkkrFGSTISF-NWPLWEEGGM-QVGAEDEKRMLKTT-GMVPMPTDSGLKAFYQGIASDKPQVF 3077
Cdd:cd02266 112 GLAQQWASEGWG---NGLPATAvACGTWAGSGMaKGPVAPEEILGNRRhGVRTMPPEEVARALLNALDRPKAGVC 183
|
|
| PRK06194 |
PRK06194 |
hypothetical protein; Provisional |
2849-2938 |
3.56e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 180458 [Multi-domain] Cd Length: 287 Bit Score: 46.16 E-value: 3.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2849 GVYLITGGAGSLGLLFAKeIANRTGRStIVLTgrSVLSEDKENELEALRSIGAEVVYREADVSDQHAVHHLFEEIKERYG 2928
Cdd:PRK06194 7 KVAVITGAASGFGLAFAR-IGAALGMK-LVLA--DVQQDALDRAVAELRAQGAEVLGVRTDVSDAAQVEALADAALERFG 82
|
90
....*....|
gi 1776025254 2929 TLNGIIHGAG 2938
Cdd:PRK06194 83 AVHLLFNNAG 92
|
|
| CAD_SDR_c |
cd08934 |
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ... |
2850-3012 |
3.67e-04 |
|
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent reduction of clavulanate-9-aldehyde to clavulanic acid, a beta-lactamase inhibitor. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.
Pssm-ID: 187639 [Multi-domain] Cd Length: 243 Bit Score: 45.61 E-value: 3.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGLLFAKEIANRtGRSTIVLTGRSVLSEDKENELEALrsiGAEVVYREADVSDQHAVHHLFEEIKERYGT 2929
Cdd:cd08934 5 VALVTGASSGIGEATARALAAE-GAAVAIAARRVDRLEALADELEAE---GGKALVLELDVTDEQQVDAAVERTVEALGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2930 LNGIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSGLLHVDECSkdFPLDF------FIFFSSVSGCLGNAGQADYAAANSF 3003
Cdd:cd08934 81 LDILVNNAGIMLLGPVEDADTTDWTRMIDTNLLGLMYTTHAA--LPHHLlrnkgtIVNISSVAGRVAVRNSAVYNATKFG 158
|
....*....
gi 1776025254 3004 MDAFAEYRR 3012
Cdd:cd08934 159 VNAFSEGLR 167
|
|
| TER_DECR_SDR_a |
cd05369 |
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ... |
4169-4275 |
3.67e-04 |
|
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER is a peroxisomal protein with a proposed role in fatty acid elongation. Fatty acid synthesis is known to occur in the both endoplasmic reticulum and mitochondria; peroxisomal TER has been proposed as an additional fatty acid elongation system, it reduces the double bond at C-2 as the last step of elongation. This system resembles the mitochondrial system in that acetyl-CoA is used as a carbon donor. TER may also function in phytol metabolism, reducting phytenoyl-CoA to phytanoyl-CoA in peroxisomes. DECR processes double bonds in fatty acids to increase their utility in fatty acid metabolism; it reduces 2,4-dienoyl-CoA to an enoyl-CoA. DECR is active in mitochondria and peroxisomes. This subgroup has the Gly-rich NAD-binding motif of the classical SDR family, but does not display strong identity to the canonical active site tetrad, and lacks the characteristic Tyr at the usual position. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.
Pssm-ID: 187627 [Multi-domain] Cd Length: 249 Bit Score: 45.66 E-value: 3.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4169 KDHVLLITGGTRGIGLLCARHFAECyGVkKLVLTGReqlppREEwarfKTSNTslAEKIQAVRELEAKGVQVEmlsltLS 4248
Cdd:cd05369 2 KGKVAFITGGGTGIGKAIAKAFAEL-GA-SVAIAGR-----KPE----VLEAA--AEEISSATGGRAHPIQCD-----VR 63
|
90 100
....*....|....*....|....*..
gi 1776025254 4249 DDAQVEQTLQHIKRTLGPIGGVIHCAG 4275
Cdd:cd05369 64 DPEAVEAAVDETLKEFGKIDILINNAA 90
|
|
| PRK08220 |
PRK08220 |
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated |
4172-4312 |
3.68e-04 |
|
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
Pssm-ID: 236190 [Multi-domain] Cd Length: 252 Bit Score: 45.65 E-value: 3.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4172 VLLITGGTRGIGLLCARHFAECyGVKklvLTGREQlppreewarfktsntslaekiqavRELEAKGVQVEMLSLTLSDDA 4251
Cdd:PRK08220 10 TVWVTGAAQGIGYAVALAFVEA-GAK---VIGFDQ------------------------AFLTQEDYPFATFVLDVSDAA 61
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1776025254 4252 QVEQTLQHIKRTLGPIGGVIHCAGLTDM---DTLafirkTSDDIQRVMEPKVSGLTTLYRHVCN 4312
Cdd:PRK08220 62 AVAQVCQRLLAETGPLDVLVNAAGILRMgatDSL-----SDEDWQQTFAVNAGGAFNLFRAVMP 120
|
|
| PRK07201 |
PRK07201 |
SDR family oxidoreductase; |
4172-4297 |
3.99e-04 |
|
SDR family oxidoreductase;
Pssm-ID: 235962 [Multi-domain] Cd Length: 657 Bit Score: 46.87 E-value: 3.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4172 VLLITGGTRGIGLLCARHFAECYGvkKLVLTGREqlppreewarfktsntslAEKIQAVR-ELEAKGVQVEMLSLTLSDD 4250
Cdd:PRK07201 373 VVLITGASSGIGRATAIKVAEAGA--TVFLVARN------------------GEALDELVaEIRAKGGTAHAYTCDLTDS 432
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1776025254 4251 AQVEQTLQHIKRTLGPIGGVIHCAGLTdmdtlafIRKTSD-------DIQRVME 4297
Cdd:PRK07201 433 AAVDHTVKDILAEHGHVDYLVNNAGRS-------IRRSVEnstdrfhDYERTMA 479
|
|
| PRK12429 |
PRK12429 |
3-hydroxybutyrate dehydrogenase; Provisional |
2850-2938 |
4.40e-04 |
|
3-hydroxybutyrate dehydrogenase; Provisional
Pssm-ID: 237100 [Multi-domain] Cd Length: 258 Bit Score: 45.65 E-value: 4.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGLLFAKEIAnRTGrSTIVLTGrsVLSEDKENELEALRSIGAEVVYREADVSDQHAVHHLFEEIKERYGT 2929
Cdd:PRK12429 6 VALVTGAASGIGLEIALALA-KEG-AKVVIAD--LNDEAAAAAAEALQKAGGKAIGVAMDVTDEEAINAGIDYAVETFGG 81
|
....*....
gi 1776025254 2930 LNGIIHGAG 2938
Cdd:PRK12429 82 VDILVNNAG 90
|
|
| PRK06483 |
PRK06483 |
dihydromonapterin reductase; Provisional |
4173-4296 |
4.96e-04 |
|
dihydromonapterin reductase; Provisional
Pssm-ID: 180586 [Multi-domain] Cd Length: 236 Bit Score: 44.92 E-value: 4.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4173 LLITGGTRGIGLLCARHFAEcYGvKKLVLTGREQLPpreewarfktsntslaeKIQAVRELEAKGVQVEmlsltLSDDAQ 4252
Cdd:PRK06483 5 ILITGAGQRIGLALAWHLLA-QG-QPVIVSYRTHYP-----------------AIDGLRQAGAQCIQAD-----FSTNAG 60
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1776025254 4253 VEQTLQHIKRTLGPIGGVIHCAGLTDMDTLAFirKTSDDIQRVM 4296
Cdd:PRK06483 61 IMAFIDELKQHTDGLRAIIHNASDWLAEKPGA--PLADVLARMM 102
|
|
| PRK09186 |
PRK09186 |
flagellin modification protein A; Provisional |
2847-2937 |
5.10e-04 |
|
flagellin modification protein A; Provisional
Pssm-ID: 236399 [Multi-domain] Cd Length: 256 Bit Score: 45.37 E-value: 5.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2847 DEGVYLITGGAGSLGLLFAKEIANRTGRSTIVLTGRSVLSEDKENELEALRSIGAEVVyrEADVSDQHAVHHLFEEIKER 2926
Cdd:PRK09186 3 KGKTILITGAGGLIGSALVKAILEAGGIVIAADIDKEALNELLESLGKEFKSKKLSLV--ELDITDQESLEEFLSKSAEK 80
|
90
....*....|.
gi 1776025254 2927 YGTLNGIIHGA 2937
Cdd:PRK09186 81 YGKIDGAVNCA 91
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
376-555 |
5.65e-04 |
|
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.
Pssm-ID: 341270 [Multi-domain] Cd Length: 608 Bit Score: 46.40 E-value: 5.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 376 IGSPIPGFSMRIVNDHnelveegeiGRFQVSGLSVTSGYYqrpdlnesvFTEDGWFETGDlgflrnGRLTITGRTKDAII 455
Cdd:cd05966 441 IKRPWPGMARTIYGDH---------ERYEDTYFSKFPGYY---------FTGDGARRDED------GYYWITGRVDDVIN 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 456 INGINYYSHAIESAVEELSEIetsytAACAVrLGQNstDQL---AIF-FVTsakLND-EQMSQLLRN-IQSHVSQVIG-- 527
Cdd:cd05966 497 VSGHRLGTAEVESALVAHPAV-----AEAAV-VGRP--HDIkgeAIYaFVT---LKDgEEPSDELRKeLRKHVRKEIGpi 565
|
170 180
....*....|....*....|....*...
gi 1776025254 528 VTPEYLLPVqkEEIPKTAIGKIQRTQLK 555
Cdd:cd05966 566 ATPDKIQFV--PGLPKTRSGKIMRRILR 591
|
|
| 11beta-HSD1_like_SDR_c |
cd05332 |
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ... |
4172-4329 |
5.95e-04 |
|
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human 11beta_HSD1 catalyzes the NADP(H)-dependent interconversion of cortisone and cortisol. This subgroup also includes human dehydrogenase/reductase SDR family member 7C (DHRS7C) and DHRS7B. These proteins have the GxxxGxG nucleotide binding motif and S-Y-K catalytic triad characteristic of the SDRs, but have an atypical C-terminal domain that contributes to homodimerization contacts. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.
Pssm-ID: 187593 [Multi-domain] Cd Length: 257 Bit Score: 45.27 E-value: 5.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4172 VLLITGGTRGIGLLCARHFAE--CygvkKLVLTGReqlppREEwarfktsntSLAEKIQAVRELEAKgvQVEMLSLTLSD 4249
Cdd:cd05332 5 VVIITGASSGIGEELAYHLARlgA----RLVLSAR-----REE---------RLEEVKSECLELGAP--SPHVVPLDMSD 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4250 DAQVEQTLQHIKRTLGPIGGVIHCAGltdMDTLAFIRKTSDDIQR-VMEPKVSGLTTLYRHVcnEP-LQF-----FVLFS 4322
Cdd:cd05332 65 LEDAEQVVEEALKLFGGLDILINNAG---ISMRSLFHDTSIDVDRkIMEVNYFGPVALTKAA--LPhLIErsqgsIVVVS 139
|
....*..
gi 1776025254 4323 SVSAIIP 4329
Cdd:cd05332 140 SIAGKIG 146
|
|
| fabG |
PRK05565 |
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional |
4172-4310 |
6.04e-04 |
|
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
Pssm-ID: 235506 [Multi-domain] Cd Length: 247 Bit Score: 44.83 E-value: 6.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4172 VLLITGGTRGIGLLCARHFAECyGVKKLVLTGReqlppREEWARfktsntslaekiQAVRELEAKGVQVEMLSLTLSDDA 4251
Cdd:PRK05565 7 VAIVTGASGGIGRAIAELLAKE-GAKVVIAYDI-----NEEAAQ------------ELLEEIKEEGGDAIAVKADVSSEE 68
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1776025254 4252 QVEQTLQHIKRTLGPIGGVIHCAGLtdMDTLAFIRKTSDDIQRVMEPKVSGLTTLYRHV 4310
Cdd:PRK05565 69 DVENLVEQIVEKFGKIDILVNNAGI--SNFGLVTDMTDEEWDRVIDVNLTGVMLLTRYA 125
|
|
| PRK12429 |
PRK12429 |
3-hydroxybutyrate dehydrogenase; Provisional |
4169-4276 |
6.30e-04 |
|
3-hydroxybutyrate dehydrogenase; Provisional
Pssm-ID: 237100 [Multi-domain] Cd Length: 258 Bit Score: 44.88 E-value: 6.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4169 KDHVLLITGGTRGIGLLCARHFAEcYGvKKLVLTGREQlppreewarfktsntslAEKIQAVRELEAKGVQVEMLSLTLS 4248
Cdd:PRK12429 3 KGKVALVTGAASGIGLEIALALAK-EG-AKVVIADLND-----------------EAAAAAAEALQKAGGKAIGVAMDVT 63
|
90 100
....*....|....*....|....*...
gi 1776025254 4249 DDAQVEQTLQHIKRTLGPIGGVIHCAGL 4276
Cdd:PRK12429 64 DEEAINAGIDYAVETFGGVDILVNNAGI 91
|
|
| PRK05872 |
PRK05872 |
short chain dehydrogenase; Provisional |
4172-4302 |
6.66e-04 |
|
short chain dehydrogenase; Provisional
Pssm-ID: 235633 [Multi-domain] Cd Length: 296 Bit Score: 45.35 E-value: 6.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4172 VLLITGGTRGIGLLCARHFAECyGVkKLVLTGREQLPPREEWARFKTSNTSLaEKIQAVRELEAkgvqvemlsltlsdda 4251
Cdd:PRK05872 11 VVVVTGAARGIGAELARRLHAR-GA-KLALVDLEEAELAALAAELGGDDRVL-TVVADVTDLAA---------------- 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1776025254 4252 qVEQTLQHIKRTLGPIGGVIHCAGLT------DMDTLAFirktsddiQRVMEPKVSG 4302
Cdd:PRK05872 72 -MQAAAEEAVERFGGIDVVVANAGIAsggsvaQVDPDAF--------RRVIDVNLLG 119
|
|
| ENR_SDR |
cd05372 |
Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ... |
2851-2935 |
7.63e-04 |
|
Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ENRs includes Escherichia coli ENR. ENR catalyzes the NAD(P)H-dependent reduction of enoyl-ACP in the last step of fatty acid biosynthesis. De novo fatty acid biosynthesis is catalyzed by the fatty acid synthetase complex, through the serial addition of 2-carbon subunits. In bacteria and plants,ENR catalyzes one of six synthetic steps in this process. Oilseed rape ENR, and also apparently the NADH-specific form of Escherichia coli ENR, is tetrameric. Although similar to the classical SDRs, this group does not have the canonical catalytic tetrad, nor does it have the typical Gly-rich NAD-binding pattern. Such so-called divergent SDRs have a GXXXXXSXA NAD-binding motif and a YXXMXXXK (or YXXXMXXXK) active site motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.
Pssm-ID: 187630 [Multi-domain] Cd Length: 250 Bit Score: 44.49 E-value: 7.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2851 YLITGGAGSLGLLF--AKEIANRTGrsTIVLTGRSVLSEDKENELEALRSIGAEVVyrEADVSDQHAVHHLFEEIKERYG 2928
Cdd:cd05372 4 ILITGIANDRSIAWgiAKALHEAGA--ELAFTYQPEALRKRVEKLAERLGESALVL--PCDVSNDEEIKELFAEVKKDWG 79
|
....*..
gi 1776025254 2929 TLNGIIH 2935
Cdd:cd05372 80 KLDGLVH 86
|
|
| PRK08277 |
PRK08277 |
D-mannonate oxidoreductase; Provisional |
4169-4329 |
8.46e-04 |
|
D-mannonate oxidoreductase; Provisional
Pssm-ID: 236216 [Multi-domain] Cd Length: 278 Bit Score: 44.89 E-value: 8.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4169 KDHVLLITGGTrgiGLLC---ARHFAECyGVKKLVLtGREQlppreewarfktsntslaEKIQA-VRELEAKGVQVEMLS 4244
Cdd:PRK08277 9 KGKVAVITGGG---GVLGgamAKELARA-GAKVAIL-DRNQ------------------EKAEAvVAEIKAAGGEALAVK 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4245 LTLSDDAQVEQTLQHIKRTLGPIGGVIHCAG------LTDMDTLAFIRKT-------SDDIQRVMEPKVSGltTLYrhvc 4311
Cdd:PRK08277 66 ADVLDKESLEQARQQILEDFGPCDILINGAGgnhpkaTTDNEFHELIEPTktffdldEEGFEFVFDLNLLG--TLL---- 139
|
170 180 190
....*....|....*....|....*....|
gi 1776025254 4312 nePLQFF------------VLFSSVSAIIP 4329
Cdd:PRK08277 140 --PTQVFakdmvgrkggniINISSMNAFTP 167
|
|
| PRK08219 |
PRK08219 |
SDR family oxidoreductase; |
4174-4310 |
8.56e-04 |
|
SDR family oxidoreductase;
Pssm-ID: 181298 [Multi-domain] Cd Length: 227 Bit Score: 44.15 E-value: 8.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4174 LITGGTRGIGLLCARHFAECYgvkKLVLTGREQlppreewarfktsntslaekiQAVRELEAKGVQVEMLSLTLSDDAQV 4253
Cdd:PRK08219 7 LITGASRGIGAAIARELAPTH---TLLLGGRPA---------------------ERLDELAAELPGATPFPVDLTDPEAI 62
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1776025254 4254 EQTLQHIKRtlgpIGGVIHCAGLTDMDTLAfiRKTSDDIQRVMEPKVSGLTTLYRHV 4310
Cdd:PRK08219 63 AAAVEQLGR----LDVLVHNAGVADLGPVA--ESTVDEWRATLEVNVVAPAELTRLL 113
|
|
| Ycik_SDR_c |
cd05340 |
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ... |
4169-4277 |
8.72e-04 |
|
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related proteins have a canonical classical SDR nucleotide-binding motif and active site tetrad. They are predicted oxoacyl-(acyl carrier protein/ACP) reductases. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.
Pssm-ID: 187599 [Multi-domain] Cd Length: 236 Bit Score: 44.49 E-value: 8.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4169 KDHVLLITGGTRGIGLLCARHFAEcYGVkKLVLTGReqlppREEwarfktsntSLAEKIQAVRELEAKGVQVEMLSLTLS 4248
Cdd:cd05340 3 NDRIILVTGASDGIGREAALTYAR-YGA-TVILLGR-----NEE---------KLRQVADHINEEGGRQPQWFILDLLTC 66
|
90 100
....*....|....*....|....*....
gi 1776025254 4249 DDAQVEQTLQHIKRTLGPIGGVIHCAGLT 4277
Cdd:cd05340 67 TSENCQQLAQRIAVNYPRLDGVLHNAGLL 95
|
|
| DHRS1_HSDL2-like_SDR_c |
cd05338 |
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ... |
4172-4364 |
8.78e-04 |
|
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup includes human DHRS1 and human HSDL2 and related proteins. These are members of the classical SDR family, with a canonical Gly-rich NAD-binding motif and the typical YXXXK active site motif. However, the rest of the catalytic tetrad is not strongly conserved. DHRS1 mRNA has been detected in many tissues, liver, heart, skeletal muscle, kidney and pancreas; a longer transcript is predominantly expressed in the liver , a shorter one in the heart. HSDL2 may play a part in fatty acid metabolism, as it is found in peroxisomes. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.
Pssm-ID: 187597 [Multi-domain] Cd Length: 246 Bit Score: 44.31 E-value: 8.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4172 VLLITGGTRGIGLLCARHFAEC-YGVkklVLTGREQLPPReewarfKTSNTSLAEKIQ-AVRELEAKGVQVEMLSLTLSD 4249
Cdd:cd05338 5 VAFVTGASRGIGRAIALRLAKAgATV---VVAAKTASEGD------NGSAKSLPGTIEeTAEEIEAAGGQALPIVVDVRD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4250 DAQVEQTLQHIKRTLGPIGGVIHCAGLTDMD-TLAFIRKTSDDIQRVMePKVSGLTTLY--RHVCNEPLQFFVLFSSVSA 4326
Cdd:cd05338 76 EDQVRALVEATVDQFGRLDILVNNAGAIWLSlVEDTPAKRFDLMQRVN-LRGTYLLSQAalPHMVKAGQGHILNISPPLS 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1776025254 4327 IIPelSAGQADYAMANSYMDYF----AEAHQKHVPIISVQWP 4364
Cdd:cd05338 155 LRP--ARGDVAYAAGKAGMSRLtlglAAELRRHGIAVNSLWP 194
|
|
| PRK06914 |
PRK06914 |
SDR family oxidoreductase; |
2850-3069 |
8.89e-04 |
|
SDR family oxidoreductase;
Pssm-ID: 180744 [Multi-domain] Cd Length: 280 Bit Score: 44.63 E-value: 8.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGLLFAKEIANRTGRstIVLTGRSVLSEDKENELEALRSIGAEVVYREADVSDQHAVHHlFEEIKERYGT 2929
Cdd:PRK06914 5 IAIVTGASSGFGLLTTLELAKKGYL--VIATMRNPEKQENLLSQATQLNLQQNIKVQQLDVTDQNSIHN-FQLVLKEIGR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2930 LNGIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSGLLHVDEC----------SKdfpldfFIFFSSVSGCLGNAGQADYAA 2999
Cdd:PRK06914 82 IDLLVNNAGYANGGFVEEIPVEEYRKQFETNVFGAISVTQAvlpymrkqksGK------IINISSISGRVGFPGLSPYVS 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1776025254 3000 ANSFMDAFAEyrrSLAASKKRFGSTI------SFNWPLWEEGgmqvgaedekrmlKTTGMVPMPTDSGLKAFYQGI 3069
Cdd:PRK06914 156 SKYALEGFSE---SLRLELKPFGIDValiepgSYNTNIWEVG-------------KQLAENQSETTSPYKEYMKKI 215
|
|
| ChcA_like_SDR_c |
cd05359 |
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ... |
4174-4293 |
9.50e-04 |
|
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup contains classical SDR proteins, including members identified as 1-cyclohexenylcarbonyl coenzyme A reductase. ChcA of Streptomyces collinus is implicated in the final reduction step of shikimic acid to ansatrienin. ChcA shows sequence similarity to the SDR family of NAD-binding proteins, but it lacks the conserved Tyr of the characteristic catalytic site. This subgroup also contains the NADH-dependent enoyl-[acyl-carrier-protein(ACP)] reductase FabL from Bacillus subtilis. This enzyme participates in bacterial fatty acid synthesis, in type II fatty-acid synthases and catalyzes the last step in each elongation cycle. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.
Pssm-ID: 187617 [Multi-domain] Cd Length: 242 Bit Score: 44.27 E-value: 9.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4174 LITGGTRGIGLLCARHFAEcYGVkKLVLTGREqlppreewarfktsntSLAEKIQAVRELEAKGVQVEMLSLTLSDDAQV 4253
Cdd:cd05359 2 LVTGGSRGIGKAIALRLAE-RGA-DVVINYRK----------------SKDAAAEVAAEIEELGGKAVVVRADVSQPQDV 63
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1776025254 4254 EQTLQHIKRTLGPIGGVIHCAG------LTDMDTLAFIRKTSDDIQ 4293
Cdd:cd05359 64 EEMFAAVKERFGRLDVLVSNAAagafrpLSELTPAHWDAKMNTNLK 109
|
|
| HBDH_SDR_c |
cd08940 |
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ... |
4169-4281 |
9.73e-04 |
|
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, catalyzes the interconversion of D-3-hydroxybutyrate and acetoacetate. It is a classical SDR, with the canonical NAD-binding motif and active site tetrad. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.
Pssm-ID: 187644 [Multi-domain] Cd Length: 258 Bit Score: 44.36 E-value: 9.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4169 KDHVLLITGGTRGIGLLCARHFAECYGvkKLVLTGREQlppreewarfktsntslAEKIQAVRE--LEAKGVQVEMLSLT 4246
Cdd:cd08940 1 KGKVALVTGSTSGIGLGIARALAAAGA--NIVLNGFGD-----------------AAEIEAVRAglAAKHGVKVLYHGAD 61
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1776025254 4247 LSDDAQVEQTLQHIKRTLGPI------GGVIHCAGLTDMDT 4281
Cdd:cd08940 62 LSKPAAIEDMVAYAQRQFGGVdilvnnAGIQHVAPIEDFPT 102
|
|
| AcpA |
COG3433 |
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ... |
3115-3190 |
1.00e-03 |
|
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442659 [Multi-domain] Cd Length: 295 Bit Score: 44.74 E-value: 1.00e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1776025254 3115 LEAALIQMVGAILKVNTDDIDVNTELSEYGFDSVTFTVFTNKInEKFQLELTPTIFFEYGSVQSLAEYVVAAYQGE 3190
Cdd:COG3433 220 TEEELRADVAELLGVDPEEIDPDDNLFDLGLDSIRLMQLVERW-RKAGLDVSFADLAEHPTLAAWWALLAAAQAAA 294
|
|
| PRK12449 |
PRK12449 |
acyl carrier protein; Provisional |
592-666 |
1.02e-03 |
|
acyl carrier protein; Provisional
Pssm-ID: 183533 [Multi-domain] Cd Length: 80 Bit Score: 40.84 E-value: 1.02e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1776025254 592 REEIQEHLLTCLTEELHVSRDWVEPNANIQS-LGVNSIKMMKLIRSIEKNYHIKLTAREIHQYPTIERLASYLSEH 666
Cdd:PRK12449 3 REEIFERLINLIQKQRSYLSLAITEQTHLKDdLAVDSIELVEFIINVEDEFHIAIPDEDVEDMVSMGDLLDYLVQR 78
|
|
| SDR_c3 |
cd05360 |
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ... |
2849-3012 |
1.04e-03 |
|
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a canonical active site triad (and also active site Asn) and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.
Pssm-ID: 187618 [Multi-domain] Cd Length: 233 Bit Score: 44.30 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2849 GVYLITGGAGSLGLLFAKEIANRtgRSTIVLTGRSvlSEDKENELEALRSIGAEVVYREADVSDQHAVHHLFEEIKERYG 2928
Cdd:cd05360 1 QVVVITGASSGIGRATALAFAER--GAKVVLAARS--AEALHELAREVRELGGEAIAVVADVADAAQVERAADTAVERFG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2929 TLNGIIHGAG-SIKDHFiIHKTNEEFQEVLqpKVSGLLHVDECSKDFPL------DFFIFFSSVSGCLGNAGQADYAAAN 3001
Cdd:cd05360 77 RIDTWVNNAGvAVFGRF-EDVTPEEFRRVF--DVNYLGHVYGTLAALPHlrrrggGALINVGSLLGYRSAPLQAAYSASK 153
|
170
....*....|.
gi 1776025254 3002 SFMDAFAEYRR 3012
Cdd:cd05360 154 HAVRGFTESLR 164
|
|
| PRK08628 |
PRK08628 |
SDR family oxidoreductase; |
2850-2958 |
1.04e-03 |
|
SDR family oxidoreductase;
Pssm-ID: 181508 [Multi-domain] Cd Length: 258 Bit Score: 44.18 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLG----LLFAKEIAnrtgrsTIVLTGRSvlseDKENE-LEALRSIGAEVVYREADVSDQHAVHHLFEEIK 2924
Cdd:PRK08628 9 VVIVTGGASGIGaaisLRLAEEGA------IPVIFGRS----APDDEfAEELRALQPRAEFVQVDLTDDAQCRDAVEQTV 78
|
90 100 110
....*....|....*....|....*....|....
gi 1776025254 2925 ERYGTLNGIIHGAGsIKDHFIIHKTNEEFQEVLQ 2958
Cdd:PRK08628 79 AKFGRIDGLVNNAG-VNDGVGLEAGREAFVASLE 111
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
1275-1641 |
1.05e-03 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 45.32 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1275 DQDWDEIAQTASDRKVLTRTVTPENLAYVIYTSGSTGKPKGVMiphkaltnflvsmGETPGLTaedkmLAVTT---YCFD 1351
Cdd:PRK10524 210 DVDYATLRAQHLGARVPVEWLESNEPSYILYTSGTTGKPKGVQ-------------RDTGGYA-----VALATsmdTIFG 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1352 IAALELFL-----------------PLIKGAHCYICQ-TEHTKD-------VEKLKRDIRTIKPT---VMQATPATW--- 1400
Cdd:PRK10524 272 GKAGETFFcasdigwvvghsyivyaPLLAGMATIMYEgLPTRPDagiwwriVEKYKVNRMFSAPTairVLKKQDPALlrk 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1401 ------KMLFYSGweneenvkilcggEALPETLKRYFldtgSEAWNM-----FGPTET--TIWSAVQRINDECSR-ATIG 1466
Cdd:PRK10524 352 hdlsslRALFLAG-------------EPLDEPTASWI----SEALGVpvidnYWQTETgwPILAIARGVEDRPTRlGSPG 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1467 RPIA--NTQIyITDSQLAPVPAGVPGELCIAGD---GVAKGYYKKeeltDSRFIDNPFEP-GSKLYRTGDMARWLPGGRI 1540
Cdd:PRK10524 415 VPMYgyNVKL-LNEVTGEPCGPNEKGVLVIEGPlppGCMQTVWGD----DDRFVKTYWSLfGRQVYSTFDWGIRDADGYY 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 1541 EYIGRIDNQVKIRGFRIELGDIESRLSEHPGILECVVVADMDNL-----AAYYTAKHANASLTA-------RELRHFVKN 1608
Cdd:PRK10524 490 FILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALkgqvaVAFVVPKDSDSLADRearlaleKEIMALVDS 569
|
410 420 430
....*....|....*....|....*....|....*
gi 1776025254 1609 ALPAYMVPS--YFIQLdhMPLTPNGKIDRNSLKNI 1641
Cdd:PRK10524 570 QLGAVARPArvWFVSA--LPKTRSGKLLRRAIQAI 602
|
|
| PRK07677 |
PRK07677 |
short chain dehydrogenase; Provisional |
2850-2937 |
1.06e-03 |
|
short chain dehydrogenase; Provisional
Pssm-ID: 181077 [Multi-domain] Cd Length: 252 Bit Score: 44.28 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGLLFAKEIANRTGRstIVLTGRS--VLSEDKeNELEAlrsIGAEVVYREADVSDQHAVHHLFEEIKERY 2927
Cdd:PRK07677 3 VVIITGGSSGMGKAMAKRFAEEGAN--VVITGRTkeKLEEAK-LEIEQ---FPGQVLTVQMDVRNPEDVQKMVEQIDEKF 76
|
90
....*....|
gi 1776025254 2928 GTLNGIIHGA 2937
Cdd:PRK07677 77 GRIDALINNA 86
|
|
| CAD_SDR_c |
cd08934 |
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ... |
4171-4356 |
1.13e-03 |
|
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent reduction of clavulanate-9-aldehyde to clavulanic acid, a beta-lactamase inhibitor. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.
Pssm-ID: 187639 [Multi-domain] Cd Length: 243 Bit Score: 44.07 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4171 HVLLITGGTRGIGLLCARHFAEcYGVKkLVLTGREqlppreewarfktsntslAEKIQAV-RELEAKGVQVEMLSLTLSD 4249
Cdd:cd08934 4 KVALVTGASSGIGEATARALAA-EGAA-VAIAARR------------------VDRLEALaDELEAEGGKALVLELDVTD 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4250 DAQVEQTLQHIKRTLGPIGGVIHCAGL------TDMDTLafirktsdDIQRVMEPKVSGLttLYRHVCNEPLQF------ 4317
Cdd:cd08934 64 EQQVDAAVERTVEALGRLDILVNNAGImllgpvEDADTT--------DWTRMIDTNLLGL--MYTTHAALPHHLlrnkgt 133
|
170 180 190
....*....|....*....|....*....|....*....
gi 1776025254 4318 FVLFSSVSAIIpeLSAGQADYAMANSYMDYFAEAHQKHV 4356
Cdd:cd08934 134 IVNISSVAGRV--AVRNSAVYNATKFGVNAFSEGLRQEV 170
|
|
| SDR_c12 |
cd08944 |
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ... |
2850-3013 |
1.29e-03 |
|
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site tetrad and glycine-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.
Pssm-ID: 187648 [Multi-domain] Cd Length: 246 Bit Score: 44.02 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGLLFAKEIANRTGRstIVLTGRsvlseDKENELEALRSIGAEVVYREADVSDQHAVHHLFEEIKERYGT 2929
Cdd:cd08944 5 VAIVTGAGAGIGAACAARLAREGAR--VVVADI-----DGGAAQAVVAQIAGGALALRVDVTDEQQVAALFERAVEEFGG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2930 LNGIIHGAGSIK-DHFIIHKTNEEFQEVLQPKVSGLLHVdeCSKDFPL------DFFIFFSSVSGCLGNAGQADYAAANS 3002
Cdd:cd08944 78 LDLLVNNAGAMHlTPAIIDTDLAVWDQTMAINLRGTFLC--CRHAAPRmiarggGSIVNLSSIAGQSGDPGYGAYGASKA 155
|
170
....*....|....*.
gi 1776025254 3003 FMD-----AFAEYRRS 3013
Cdd:cd08944 156 AIRnltrtLAAELRHA 171
|
|
| FabI |
COG0623 |
Enoyl-[acyl-carrier-protein] reductase FabI [Lipid transport and metabolism]; Enoyl- ... |
2876-2940 |
1.39e-03 |
|
Enoyl-[acyl-carrier-protein] reductase FabI [Lipid transport and metabolism]; Enoyl-[acyl-carrier-protein] reductase FabI is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440388 [Multi-domain] Cd Length: 254 Bit Score: 43.86 E-value: 1.39e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1776025254 2876 TIVLTGRSVLSEDKENELeaLRSIGAEVVYrEADVSDQHAVHHLFEEIKERYGTLNGIIHgagSI 2940
Cdd:COG0623 33 ELAFTYQGEALKKRVEPL--AEELGSALVL-PCDVTDDEQIDALFDEIKEKWGKLDFLVH---SI 91
|
|
| PRK05876 |
PRK05876 |
short chain dehydrogenase; Provisional |
2852-3058 |
1.46e-03 |
|
short chain dehydrogenase; Provisional
Pssm-ID: 135637 [Multi-domain] Cd Length: 275 Bit Score: 44.18 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2852 LITGGAGSLGLLFAKEIANRTGRSTIVLTGRSVLsedkENELEALRSIGAEVVYREADVSDQHAVHHLFEEIKERYGTLN 2931
Cdd:PRK05876 10 VITGGASGIGLATGTEFARRGARVVLGDVDKPGL----RQAVNHLRAEGFDVHGVMCDVRHREEVTHLADEAFRLLGHVD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2932 GIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSGLLHVDECSKDFPLD-----FFIFFSSVSGCLGNAGQADYAAANSFMDA 3006
Cdd:PRK05876 86 VVFSNAGIVVGGPIVEMTHDDWRWVIDVDLWGSIHTVEAFLPRLLEqgtggHVVFTASFAGLVPNAGLGAYGVAKYGVVG 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1776025254 3007 FAEyrrSLAASKKRFGSTISFNWPLWEEGGMQVGAEDEK----RMLKTTG-MVPMPT 3058
Cdd:PRK05876 166 LAE---TLAREVTADGIGVSVLCPMVVETNLVANSERIRgaacAQSSTTGsPGPLPL 219
|
|
| WcaG |
COG0451 |
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis]; |
2852-2986 |
1.47e-03 |
|
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440220 [Multi-domain] Cd Length: 295 Bit Score: 44.20 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2852 LITGGAGSLGLLFAKEIANRtGRSTIVLtgrsVLSEDKENELEALRsiGAEVVyrEADVSDQHAVHHLFEEIkerygtlN 2931
Cdd:COG0451 3 LVTGGAGFIGSHLARRLLAR-GHEVVGL----DRSPPGAANLAALP--GVEFV--RGDLRDPEALAAALAGV-------D 66
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1776025254 2932 GIIHGAGsikdhfIIHKTNEEFQEVLQPKVSGLLHVDECSKDFPLDFFIFFSSVS 2986
Cdd:COG0451 67 AVVHLAA------PAGVGEEDPDETLEVNVEGTLNLLEAARAAGVKRFVYASSSS 115
|
|
| meso-BDH-like_SDR_c |
cd05366 |
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ... |
2850-2999 |
1.59e-03 |
|
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases (BDHs) catalyze the NAD+ dependent conversion of 2,3-butanediol to acetonin; BDHs are classified into types according to their stereospecificity as to substrates and products. Included in this subgroup are Klebsiella pneumonia meso-BDH which catalyzes meso-2,3-butanediol to D(-)-acetonin, and Corynebacterium glutamicum L-BDH which catalyzes lX+)-2,3-butanediol to L(+)-acetonin. This subgroup is comprised of classical SDRs with the characteristic catalytic triad and NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.
Pssm-ID: 187624 [Multi-domain] Cd Length: 257 Bit Score: 43.90 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGLLFAKEIANRTGRSTIVLTGRSVLSEDKENELEALrsiGAEVVYREADVSDQHAVHHLFEEIKERYGT 2929
Cdd:cd05366 4 VAIITGAAQGIGRAIAERLAADGFNIVLADLNLEEAAKSTIQEISEA---GYNAVAVGADVTDKDDVEALIDQAVEKFGS 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1776025254 2930 LNGIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSG-LLHVDECSKDFpLDF-----FIFFSSVSGCLGNAGQADYAA 2999
Cdd:cd05366 81 FDVMVNNAGIAPITPLLTITEEDLKKVYAVNVFGvLFGIQAAARQF-KKLghggkIINASSIAGVQGFPNLGAYSA 155
|
|
| PRK07109 |
PRK07109 |
short chain dehydrogenase; Provisional |
2841-2938 |
1.97e-03 |
|
short chain dehydrogenase; Provisional
Pssm-ID: 235935 [Multi-domain] Cd Length: 334 Bit Score: 44.14 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2841 LHMPWRDEGVYLITGGAGSLGLLFAKEIANRTGRstIVLTGRSvlsEDKENELEA-LRSIGAEVVYREADVSDQHAVHHL 2919
Cdd:PRK07109 1 MMLKPIGRQVVVITGASAGVGRATARAFARRGAK--VVLLARG---EEGLEALAAeIRAAGGEALAVVADVADAEAVQAA 75
|
90
....*....|....*....
gi 1776025254 2920 FEEIKERYGTLNGIIHGAG 2938
Cdd:PRK07109 76 ADRAEEELGPIDTWVNNAM 94
|
|
| fabG |
PRK08642 |
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional |
2847-2967 |
2.03e-03 |
|
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
Pssm-ID: 181517 [Multi-domain] Cd Length: 253 Bit Score: 43.54 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2847 DEGVYLITGGAGSLGLLFAKEIAnRTGRSTIVLTGRSvlsEDKENELeaLRSIGAEVVYREADVSDQHAVHHLFEEIKER 2926
Cdd:PRK08642 4 SEQTVLVTGGSRGLGAAIARAFA-REGARVVVNYHQS---EDAAEAL--ADELGDRAIALQADVTDREQVQAMFATATEH 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1776025254 2927 YG-TLNGIIHGA-------GSIKDHFiIHKTNEEFQEVLQPKVSGLLHV 2967
Cdd:PRK08642 78 FGkPITTVVNNAladfsfdGDARKKA-DDITWEDFQQQLEGSVKGALNT 125
|
|
| ChcA_like_SDR_c |
cd05359 |
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ... |
2852-2939 |
2.06e-03 |
|
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup contains classical SDR proteins, including members identified as 1-cyclohexenylcarbonyl coenzyme A reductase. ChcA of Streptomyces collinus is implicated in the final reduction step of shikimic acid to ansatrienin. ChcA shows sequence similarity to the SDR family of NAD-binding proteins, but it lacks the conserved Tyr of the characteristic catalytic site. This subgroup also contains the NADH-dependent enoyl-[acyl-carrier-protein(ACP)] reductase FabL from Bacillus subtilis. This enzyme participates in bacterial fatty acid synthesis, in type II fatty-acid synthases and catalyzes the last step in each elongation cycle. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.
Pssm-ID: 187617 [Multi-domain] Cd Length: 242 Bit Score: 43.11 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2852 LITGGAGSLGLLFAKEIANRTgrSTIVLTGRSvlSEDKENELEA-LRSIGAEVVYREADVSDQHAVHHLFEEIKERYGTL 2930
Cdd:cd05359 2 LVTGGSRGIGKAIALRLAERG--ADVVINYRK--SKDAAAEVAAeIEELGGKAVVVRADVSQPQDVEEMFAAVKERFGRL 77
|
....*....
gi 1776025254 2931 NGIIHGAGS 2939
Cdd:cd05359 78 DVLVSNAAA 86
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
1898-1963 |
2.28e-03 |
|
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; SCP-2 has multiple roles in intracellular lipid circulation and metabolism. The N-terminal presequence in the SCP-x isoform represents a peroxisomal 3-ketacyl-Coa thiolase specific for branched-chain acyl CoAs, which is proteolytically cleaved from the sterol carrier protein.
Pssm-ID: 238425 [Multi-domain] Cd Length: 375 Bit Score: 43.79 E-value: 2.28e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1776025254 1898 GYVSWVLAQSgTIPTMISHKLGLRG-PSYFVHANCSSSLIGLHSAYKSLLSAESDYALVGGATLHTE 1963
Cdd:cd00829 44 GNAAGGRFQS-FPGALIAEYLGLLGkPATRVEAAGASGSAAVRAAAAAIASGLADVVLVVGAEKMSD 109
|
|
| Ga5DH-like_SDR_c |
cd05347 |
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ... |
4172-4276 |
2.31e-03 |
|
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent conversion of carbon source D-gluconate and 5-keto-D-gluconate. This SDR subgroup has a classical Gly-rich NAD(P)-binding motif and a conserved active site tetrad pattern. However, it has been proposed that Arg104 (Streptococcus suis Ga5DH numbering), as well as an active site Ca2+, play a critical role in catalysis. In addition to Ga5DHs this subgroup contains Erwinia chrysanthemi KduD which is involved in pectin degradation, and is a putative 2,5-diketo-3-deoxygluconate dehydrogenase. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107,15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.
Pssm-ID: 187605 [Multi-domain] Cd Length: 248 Bit Score: 43.12 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4172 VLLITGGTRGIGLLCARHFAEcYGVKkLVLTGReqlppreewarfktsNTSLAEKIQAvrELEAKGVQVEMLSLTLSDDA 4251
Cdd:cd05347 7 VALVTGASRGIGFGIASGLAE-AGAN-IVINSR---------------NEEKAEEAQQ--LIEKEGVEATAFTCDVSDEE 67
|
90 100
....*....|....*....|....*
gi 1776025254 4252 QVEQTLQHIKRTLGPIGGVIHCAGL 4276
Cdd:cd05347 68 AIKAAVEAIEEDFGKIDILVNNAGI 92
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
165-243 |
2.41e-03 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 43.95 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 165 RAIIVEDLLSAEADTDWHQSSPEDLA-----LLLLTSGSTGTPKAVMLNHRNIMSMVKGIIQMQGFTREDITFNWMPFDH 239
Cdd:cd05939 77 KALIFNLLDPLLTQSSTEPPSQDDVNfrdklFYIYTSGTTGLPKAAVIVHSRYYRIAAGAYYAFGMRPEDVVYDCLPLYH 156
|
....*
gi 1776025254 240 -VGGI 243
Cdd:cd05939 157 sAGGI 161
|
|
| PRK06123 |
PRK06123 |
SDR family oxidoreductase; |
2850-3005 |
2.46e-03 |
|
SDR family oxidoreductase;
Pssm-ID: 180411 [Multi-domain] Cd Length: 248 Bit Score: 43.23 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGLLFAKeIANRTGRSTIVLTGRSvlSEDKENELEALRSIGAEVVYREADVSDQHAVHHLFEEIKERYGT 2929
Cdd:PRK06123 4 VMIITGASRGIGAATAL-LAAERGYAVCLNYLRN--RDAAEAVVQAIRRQGGEALAVAADVADEADVLRLFEAVDRELGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2930 LNGIIHGAGSIKDHFII-HKTNEEFQEVLQPKVSG-LLHVDECSKDFPLDF------FIFFSSVSGCLGNAGQ-ADYAAA 3000
Cdd:PRK06123 81 LDALVNNAGILEAQMRLeQMDAARLTRIFATNVVGsFLCAREAVKRMSTRHggrggaIVNVSSMAARLGSPGEyIDYAAS 160
|
....*
gi 1776025254 3001 NSFMD 3005
Cdd:PRK06123 161 KGAID 165
|
|
| PRK08340 |
PRK08340 |
SDR family oxidoreductase; |
2852-2941 |
2.62e-03 |
|
SDR family oxidoreductase;
Pssm-ID: 169390 [Multi-domain] Cd Length: 259 Bit Score: 43.25 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2852 LITGGAGSLGLLFAKEIANRTGRstIVLTGRSvlSEDKENELEALRSIGaEVVYREADVSDQHAVHHLFEEIKERYGTLN 2931
Cdd:PRK08340 4 LVTASSRGIGFNVARELLKKGAR--VVISSRN--EENLEKALKELKEYG-EVYAVKADLSDKDDLKNLVKEAWELLGGID 78
|
90
....*....|
gi 1776025254 2932 GIIHGAGSIK 2941
Cdd:PRK08340 79 ALVWNAGNVR 88
|
|
| Mgc4172-like_SDR_c |
cd05343 |
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ... |
2845-2964 |
2.63e-03 |
|
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These proteins are members of the SDR family, with a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.
Pssm-ID: 187601 [Multi-domain] Cd Length: 250 Bit Score: 42.89 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2845 WRDEgVYLITGGAGSLGLLFAKEIANRTGRstIVLTGRSVlseDKENELEA-LRSIG-AEVVYREADVSDQHAVHHLFEE 2922
Cdd:cd05343 4 WRGR-VALVTGASVGIGAAVARALVQHGMK--VVGCARRV---DKIEALAAeCQSAGyPTLFPYQCDLSNEEQILSMFSA 77
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1776025254 2923 IKERYGTLNGIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSGL 2964
Cdd:cd05343 78 IRTQHQGVDVCINNAGLARPEPLLSGKTEGWKEMFDVNVLAL 119
|
|
| TER_DECR_SDR_a |
cd05369 |
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ... |
2850-2938 |
2.71e-03 |
|
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER is a peroxisomal protein with a proposed role in fatty acid elongation. Fatty acid synthesis is known to occur in the both endoplasmic reticulum and mitochondria; peroxisomal TER has been proposed as an additional fatty acid elongation system, it reduces the double bond at C-2 as the last step of elongation. This system resembles the mitochondrial system in that acetyl-CoA is used as a carbon donor. TER may also function in phytol metabolism, reducting phytenoyl-CoA to phytanoyl-CoA in peroxisomes. DECR processes double bonds in fatty acids to increase their utility in fatty acid metabolism; it reduces 2,4-dienoyl-CoA to an enoyl-CoA. DECR is active in mitochondria and peroxisomes. This subgroup has the Gly-rich NAD-binding motif of the classical SDR family, but does not display strong identity to the canonical active site tetrad, and lacks the characteristic Tyr at the usual position. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.
Pssm-ID: 187627 [Multi-domain] Cd Length: 249 Bit Score: 42.96 E-value: 2.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGllfaKEIANRTGR--STIVLTGRS--VLSEDKEnELEALRsiGAEVVYREADVSDQHAVHHLFEEIKE 2925
Cdd:cd05369 5 VAFITGGGTGIG----KAIAKAFAElgASVAIAGRKpeVLEAAAE-EISSAT--GGRAHPIQCDVRDPEAVEAAVDETLK 77
|
90
....*....|...
gi 1776025254 2926 RYGTLNGIIHGAG 2938
Cdd:cd05369 78 EFGKIDILINNAA 90
|
|
| UDP_invert_4-6DH_SDR_e |
cd05237 |
UDP-Glcnac (UDP-linked N-acetylglucosamine) inverting 4,6-dehydratase, extended (e) SDRs; ... |
2852-2984 |
2.80e-03 |
|
UDP-Glcnac (UDP-linked N-acetylglucosamine) inverting 4,6-dehydratase, extended (e) SDRs; UDP-Glcnac inverting 4,6-dehydratase was identified in Helicobacter pylori as the hexameric flaA1 gene product (FlaA1). FlaA1 is hexameric, possesses UDP-GlcNAc-inverting 4,6-dehydratase activity, and catalyzes the first step in the creation of a pseudaminic acid derivative in protein glycosylation. Although this subgroup has the NADP-binding motif characteristic of extended SDRs, its members tend to have a Met substituted for the active site Tyr found in most SDR families. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187548 [Multi-domain] Cd Length: 287 Bit Score: 43.38 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2852 LITGGAGSLGLLFAKEIAnRTGRSTIVLTGRsvlSEDKENELE---ALRSIGAEVVYREADVSDQHAVHHLFEEIKERYg 2928
Cdd:cd05237 6 LVTGGAGSIGSELVRQIL-KFGPKKLIVFDR---DENKLHELVrelRSRFPHDKLRFIIGDVRDKERLRRAFKERGPDI- 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1776025254 2929 tlngIIHgAGSIKdhfiiHKTNEE--FQEVLQPKVSGLLHVDECSKDFPLDFFIFFSS 2984
Cdd:cd05237 81 ----VFH-AAALK-----HVPSMEdnPEEAIKTNVLGTKNVIDAAIENGVEKFVCIST 128
|
|
| Qor |
COG0604 |
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ... |
2852-2913 |
3.00e-03 |
|
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and conversion, General function prediction only];
Pssm-ID: 440369 [Multi-domain] Cd Length: 322 Bit Score: 43.21 E-value: 3.00e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1776025254 2852 LITGGAGSLGlLFAKEIANRTGRSTIVLTGrsvlSEDKeneLEALRSIGAEVV--YREADVSDQ 2913
Cdd:COG0604 144 LVHGAAGGVG-SAAVQLAKALGARVIATAS----SPEK---AELLRALGADHVidYREEDFAER 199
|
|
| fabG |
PRK06463 |
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional |
2850-2938 |
3.22e-03 |
|
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
Pssm-ID: 180576 [Multi-domain] Cd Length: 255 Bit Score: 42.85 E-value: 3.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGLLFAKEIAnRTGRSTIVLTGRSvlsedkENELEALRSIGAEVVyrEADVSDQHAVHHLFEEIKERYGT 2929
Cdd:PRK06463 9 VALITGGTRGIGRAIAEAFL-REGAKVAVLYNSA------ENEAKELREKGVFTI--KCDVGNRDQVKKSKEVVEKEFGR 79
|
....*....
gi 1776025254 2930 LNGIIHGAG 2938
Cdd:PRK06463 80 VDVLVNNAG 88
|
|
| PRK06124 |
PRK06124 |
SDR family oxidoreductase; |
4172-4310 |
3.55e-03 |
|
SDR family oxidoreductase;
Pssm-ID: 235702 [Multi-domain] Cd Length: 256 Bit Score: 42.78 E-value: 3.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4172 VLLITGGTRGIGLLCARHFAECyGVKKLVlTGREqlppreewarfktsntslAEKIQ-AVRELEAKGVQVEMLSLTLSDD 4250
Cdd:PRK06124 13 VALVTGSARGLGFEIARALAGA-GAHVLV-NGRN------------------AATLEaAVAALRAAGGAAEALAFDIADE 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4251 AQVEQTLQHIKRTLGPIGGVIHCAGLTDMDTLAFIrkTSDDIQRVMEPKVSGLTTLYRHV 4310
Cdd:PRK06124 73 EAVAAAFARIDAEHGRLDILVNNVGARDRRPLAEL--DDAAIRALLETDLVAPILLSRLA 130
|
|
| THN_reductase-like_SDR_c |
cd05362 |
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ... |
4172-4290 |
3.63e-03 |
|
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6,8-tetrahydroxynaphthalene reductase (4HNR) of Magnaporthe grisea and the related 1,3,8-trihydroxynaphthalene reductase (3HNR) are typical members of the SDR family containing the canonical glycine rich NAD(P)-binding site and active site tetrad, and function in fungal melanin biosynthesis. This subgroup also includes an SDR from Norway spruce that may function to protect against both biotic and abitoic stress. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.
Pssm-ID: 187620 [Multi-domain] Cd Length: 243 Bit Score: 42.65 E-value: 3.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4172 VLLITGGTRGIGLLCARHFAECyGVKKLVLTGreqlppreewarfktSNTSLAEKIqaVRELEAKGVQVEMLSLTLSDDA 4251
Cdd:cd05362 5 VALVTGASRGIGRAIAKRLARD-GASVVVNYA---------------SSKAAAEEV--VAEIEAAGGKAIAVQADVSDPS 66
|
90 100 110
....*....|....*....|....*....|....*....
gi 1776025254 4252 QVEQTLQHIKRTLGPIGGVIHCAGLTDMdtlAFIRKTSD 4290
Cdd:cd05362 67 QVARLFDAAEKAFGGVDILVNNAGVMLK---KPIAETSE 102
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
4734-4780 |
4.67e-03 |
|
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl synthase (pfam00109), and also chalcone synthase.
Pssm-ID: 459676 [Multi-domain] Cd Length: 260 Bit Score: 42.29 E-value: 4.67e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1776025254 4734 PSVVVDTACSSALVGMNMAIQALRGGDIQSAIVGGVSLLsSDASHRL 4780
Cdd:pfam00108 77 PAVTINKVCGSGLKAVYLAAQSIASGDADVVLAGGVESM-SHAPYAL 122
|
|
| dTDP_GD_SDR_e |
cd05246 |
dTDP-D-glucose 4,6-dehydratase, extended (e) SDRs; This subgroup contains dTDP-D-glucose 4, ... |
2851-2996 |
4.85e-03 |
|
dTDP-D-glucose 4,6-dehydratase, extended (e) SDRs; This subgroup contains dTDP-D-glucose 4,6-dehydratase and related proteins, members of the extended-SDR family, with the characteristic Rossmann fold core region, active site tetrad and NAD(P)-binding motif. dTDP-D-glucose 4,6-dehydratase is closely related to other sugar epimerases of the SDR family. dTDP-D-dlucose 4,6,-dehydratase catalyzes the second of four steps in the dTDP-L-rhamnose pathway (the dehydration of dTDP-D-glucose to dTDP-4-keto-6-deoxy-D-glucose) in the synthesis of L-rhamnose, a cell wall component of some pathogenic bacteria. In many gram negative bacteria, L-rhamnose is an important constituent of lipopoylsaccharide O-antigen. The larger N-terminal portion of dTDP-D-Glucose 4,6-dehydratase forms a Rossmann fold NAD-binding domain, while the C-terminus binds the sugar substrate. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187557 [Multi-domain] Cd Length: 315 Bit Score: 42.54 E-value: 4.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2851 YLITGGAGSLGLLFAKEIANRTGRSTIVltgrsVLseDKEN---ELEALRSIGAEVVYR--EADVSDQHAVHHLFEEIKe 2925
Cdd:cd05246 3 ILVTGGAGFIGSNFVRYLLNKYPDYKII-----NL--DKLTyagNLENLEDVSSSPRYRfvKGDICDAELVDRLFEEEK- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2926 rygtLNGIIHGAG------SIKDHFIIHKTNeefqevlqpkVSG---LLhvdECSKDFPLDFFIFFSS--VSGCLGNAGQ 2994
Cdd:cd05246 75 ----IDAVIHFAAeshvdrSISDPEPFIRTN----------VLGtytLL---EAARKYGVKRFVHISTdeVYGDLLDDGE 137
|
..
gi 1776025254 2995 AD 2996
Cdd:cd05246 138 FT 139
|
|
| PRK12745 |
PRK12745 |
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional |
4172-4341 |
5.02e-03 |
|
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
Pssm-ID: 237188 [Multi-domain] Cd Length: 256 Bit Score: 42.26 E-value: 5.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4172 VLLITGGTRGIGLLCARHFAecygvkklvltgreqlppREEWARFKTSNTSLAEKIQAVRELEAKGVQVEMLSLTLSDDA 4251
Cdd:PRK12745 4 VALVTGGRRGIGLGIARALA------------------AAGFDLAINDRPDDEELAATQQELRALGVEVIFFPADVADLS 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4252 QVEQTLQHIKRTLGPIGGVIHCAGLTDMDTLAFIRKTSDDIQRVMEPKVSG---LTTLY-------RHVCNEPLQFFVLF 4321
Cdd:PRK12745 66 AHEAMLDAAQAAWGRIDCLVNNAGVGVKVRGDLLDLTPESFDRVLAINLRGpffLTQAVakrmlaqPEPEELPHRSIVFV 145
|
170 180
....*....|....*....|
gi 1776025254 4322 SSVSAIIpeLSAGQADYAMA 4341
Cdd:PRK12745 146 SSVNAIM--VSPNRGEYCIS 163
|
|
| ADH_SDR_c_like |
cd05323 |
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ... |
2850-2943 |
5.20e-03 |
|
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains insect type ADH, and 15-hydroxyprostaglandin dehydrogenase (15-PGDH) type I; these proteins are classical SDRs. ADH catalyzes the NAD+-dependent oxidation of alcohols to aldehydes/ketones. This subgroup is distinct from the zinc-dependent alcohol dehydrogenases of the medium chain dehydrogenase/reductase family, and evolved in fruit flies to allow the digestion of fermenting fruit. 15-PGDH catalyzes the NAD-dependent interconversion of (5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-13-enoate and (5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-13-enoate, and has a typical SDR glycine-rich NAD-binding motif, which is not fully present in ADH. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.
Pssm-ID: 187584 [Multi-domain] Cd Length: 244 Bit Score: 41.90 E-value: 5.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGLLFAKEIANRtgrstivltGRSVLSEDKENELEALRSIGA-----EVVYREADVSDQHAVHHLFEEIK 2924
Cdd:cd05323 2 VAIITGGASGIGLATAKLLLKK---------GAKVAILDRNENPGAAAELQAinpkvKATFVQCDVTSWEQLAAAFKKAI 72
|
90
....*....|....*....
gi 1776025254 2925 ERYGTLNGIIHGAGSIKDH 2943
Cdd:cd05323 73 EKFGRVDILINNAGILDEK 91
|
|
| PRK07067 |
PRK07067 |
L-iditol 2-dehydrogenase; |
4169-4303 |
5.87e-03 |
|
L-iditol 2-dehydrogenase;
Pssm-ID: 235925 [Multi-domain] Cd Length: 257 Bit Score: 41.94 E-value: 5.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 4169 KDHVLLITGGTRGIGllcaRHFAECYGvkklvltgreqlpprEEWARFKTSNTSLAEKIQAVRELeakGVQVEMLSLTLS 4248
Cdd:PRK07067 5 QGKVALLTGAASGIG----EAVAERYL---------------AEGARVVIADIKPARARLAALEI---GPAAIAVSLDVT 62
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1776025254 4249 DDAQVEQTLQHIKRTLGPIGGVIHCAGLTDMDTLAFIrkTSDDIQRVMEPKVSGL 4303
Cdd:PRK07067 63 RQDSIDRIVAAAVERFGGIDILFNNAALFDMAPILDI--SRDSYDRLFAVNVKGL 115
|
|
| PRK07856 |
PRK07856 |
SDR family oxidoreductase; |
2850-2938 |
7.94e-03 |
|
SDR family oxidoreductase;
Pssm-ID: 236116 [Multi-domain] Cd Length: 252 Bit Score: 41.46 E-value: 7.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGLLFAKEIAnRTGrSTIVLTGRSVLSEDKenelealrsiGAEVVYREADVSDQHAVHHLFEEIKERYGT 2929
Cdd:PRK07856 8 VVLVTGGTRGIGAGIARAFL-AAG-ATVVVCGRRAPETVD----------GRPAEFHAADVRDPDQVAALVDAIVERHGR 75
|
....*....
gi 1776025254 2930 LNGIIHGAG 2938
Cdd:PRK07856 76 LDVLVNNAG 84
|
|
| PRK12384 |
PRK12384 |
sorbitol-6-phosphate dehydrogenase; Provisional |
2850-2963 |
9.30e-03 |
|
sorbitol-6-phosphate dehydrogenase; Provisional
Pssm-ID: 183489 [Multi-domain] Cd Length: 259 Bit Score: 41.56 E-value: 9.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776025254 2850 VYLITGGAGSLGLLFAKEIANRTGRSTIV-LTGRSV--LSEDKENELEALRSIGAEVvyreaDVSDQHAVHHLFEEIKER 2926
Cdd:PRK12384 4 VAVVIGGGQTLGAFLCHGLAEEGYRVAVAdINSEKAanVAQEINAEYGEGMAYGFGA-----DATSEQSVLALSRGVDEI 78
|
90 100 110
....*....|....*....|....*....|....*..
gi 1776025254 2927 YGTLNGIIHGAGSIKDHFIIHKTNEEFQEVLQPKVSG 2963
Cdd:PRK12384 79 FGRVDLLVYNAGIAKAAFITDFQLGDFDRSLQVNLVG 115
|
|
|