|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
1-659 |
0e+00 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 1368.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 1 MAVYTVKVADSIPATEERPSAGPVYRCIYAENGLLEVPKGMESPWEFFSDSVERNPKNQMLGRRQIINSKAGPYVWLTYR 80
Cdd:PLN02861 2 AETYTVKVEESRPATGGKPSAGPVYRSIYAKDGLLDLPADIDSPWQFFSDAVKKYPNNQMLGRRQVTDSKVGPYVWLTYK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 81 EAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQAIPYVPLYDSLGANAVEFIINHAEVSIAFVQESKIP 160
Cdd:PLN02861 82 EVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSIAFVQESKIS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 161 AMLTCLPKCTSYLKTIISFGKISSSQKEEAEELGVSCFSWEEFALLGSLDCELPPKQKTDICTIMYTSGTTGEPKGVVLS 240
Cdd:PLN02861 162 SILSCLPKCSSNLKTIVSFGDVSSEQKEEAEELGVSCFSWEEFSLMGSLDCELPPKQKTDICTIMYTSGTTGEPKGVILT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 241 NEAIMAEVLSTDQLLLETDKVATEEDTYFSFLPLAHVFDQIMETYCIYKGSSIGFWGADVRYLMEDIQELKPTIFCGVPR 320
Cdd:PLN02861 242 NRAIIAEVLSTDHLLKVTDRVATEEDSYFSYLPLAHVYDQVIETYCISKGASIGFWQGDIRYLMEDVQALKPTIFCGVPR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 321 VYERIYGGAIAKISSGGALRKALFQYAYNYKLRNLEKGLRQDEAAPRLDRLIFDKIKQGFGGRVRLLFSGAAPLSRHVEE 400
Cdd:PLN02861 322 VYDRIYTGIMQKISSGGMLRKKLFDFAYNYKLGNLRKGLKQEEASPRLDRLVFDKIKEGLGGRVRLLLSGAAPLPRHVEE 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 401 FLRVTSCSVLSQGYGLTESCGGCLTSIVNEFSMMGTVGVPYPTIEARLESVPEMGYDALSNVPRGEICLRGKTLFSGYFK 480
Cdd:PLN02861 402 FLRVTSCSVLSQGYGLTESCGGCFTSIANVFSMVGTVGVPMTTIEARLESVPEMGYDALSDVPRGEICLRGNTLFSGYHK 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 481 RQDLTESALVDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSQGEYVAVENLENTYSRCPLITSIWVYGNSFESFLVAVVV 560
Cdd:PLN02861 482 RQDLTEEVLIDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSQGEYVAVENLENTYSRCPLIASIWVYGNSFESFLVAVVV 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 561 PDKKALEDWAENHNVTGDFKSLCENLEARKYILDELNNTGQNHQLKGFERLKAVHLDPNPFDIERDLVTPTFKLKRPQLL 640
Cdd:PLN02861 562 PDRQALEDWAANNNKTGDFKSLCKNLKARKYILDELNSTGKKLQLRGFEMLKAIHLEPNPFDIERDLITPTFKLKRPQLL 641
|
650
....*....|....*....
gi 225428594 641 KYYKDIIDRLYSEAKGTKS 659
Cdd:PLN02861 642 KYYKDCIDQLYSEAKGGKA 660
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
4-655 |
0e+00 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 880.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 4 YTVKVADSIPATEERPSAGPVYRCIYAENGLLEVPKGMESPWEFFSDSVERNPKNQMLGRRQIINSKAGPYVWLTYREAY 83
Cdd:PLN02614 7 FIFQVEEGKEGSDGRPSVGPVYRSIFAKDGFPNPIEGMDSCWDVFRMSVEKYPNNPMLGRREIVDGKPGKYVWQTYQEVY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 84 DAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQAIPYVPLYDSLGANAVEFIINHAEVSIAFVQESKIPAML 163
Cdd:PLN02614 87 DIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVEEKKISELF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 164 TCLPKCTSYLKTIISFGKISSSQKEEAEELGVSCFSWEEFALLGS-LDCELPPKQKTDICTIMYTSGTTGEPKGVVLSNE 242
Cdd:PLN02614 167 KTCPNSTEYMKTVVSFGGVSREQKEEAETFGLVIYAWDEFLKLGEgKQYDLPIKKKSDICTIMYTSGTTGDPKGVMISNE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 243 AIMAEVLSTDQLLLETDKVATEEDTYFSFLPLAHVFDQIMETYCIYKGSSIGFWGADVRYLMEDIQELKPTIFCGVPRVY 322
Cdd:PLN02614 247 SIVTLIAGVIRLLKSANAALTVKDVYLSYLPLAHIFDRVIEECFIQHGAAIGFWRGDVKLLIEDLGELKPTIFCAVPRVL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 323 ERIYGGAIAKISSGGALRKALFQYAYNYKLRNLEKGLRQDEAAPRLDRLIFDKIKQGFGGRVRLLFSGAAPLSRHVEEFL 402
Cdd:PLN02614 327 DRVYSGLQKKLSDGGFLKKFVFDSAFSYKFGNMKKGQSHVEASPLCDKLVFNKVKQGLGGNVRIILSGAAPLASHVESFL 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 403 RVTSCSVLSQGYGLTESCGGCLTSIVNEFSMMGTVGVPYPTIEARLESVPEMGYDALSNVPRGEICLRGKTLFSGYFKRQ 482
Cdd:PLN02614 407 RVVACCHVLQGYGLTESCAGTFVSLPDELDMLGTVGPPVPNVDIRLESVPEMEYDALASTPRGEICIRGKTLFSGYYKRE 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 483 DLTESALVDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSQGEYVAVENLENTYSRCPLITSIWVYGNSFESFLVAVVVPD 562
Cdd:PLN02614 487 DLTKEVLIDGWLHTGDVGEWQPNGSMKIIDRKKNIFKLSQGEYVAVENIENIYGEVQAVDSVWVYGNSFESFLVAIANPN 566
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 563 KKALEDWAENHNVTGDFKSLCENLEARKYILDELNNTGQNHQLKGFERLKAVHLDPNPFDIERDLVTPTFKLKRPQLLKY 642
Cdd:PLN02614 567 QQILERWAAENGVSGDYNALCQNEKAKEFILGELVKMAKEKKMKGFEIIKAIHLDPVPFDMERDLLTPTFKKKRPQLLKY 646
|
650
....*....|...
gi 225428594 643 YKDIIDRLYSEAK 655
Cdd:PLN02614 647 YQSVIDEMYKTTN 659
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
72-652 |
0e+00 |
|
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: 812.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 72 GPYVWLTYREAYDAALRMGSAMRSRGVN--PGDRCGIYGSNCPEWIIAMEACNSQAIPYVPLYDSLGANAVEFIINHAEV 149
Cdd:cd05927 1 GPYEWISYKEVAERADNIGSALRSLGGKpaPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 150 SIAFVQEskipamltclpkctsylktiisfgkisssqkeeaeelGVSCFSWEEFALLGSLD-CELPPKQKTDICTIMYTS 228
Cdd:cd05927 81 SIVFCDA-------------------------------------GVKVYSLEEFEKLGKKNkVPPPPPKPEDLATICYTS 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 229 GTTGEPKGVVLSNEAIMAEVLSTDQLLLETDKVaTEEDTYFSFLPLAHVFDQIMETYCIYKGSSIGFWGADVRYLMEDIQ 308
Cdd:cd05927 124 GTTGNPKGVMLTHGNIVSNVAGVFKILEILNKI-NPTDVYISYLPLAHIFERVVEALFLYHGAKIGFYSGDIRLLLDDIK 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 309 ELKPTIFCGVPRVYERIYGGAIAKISSGGALRKALFQYAYNYKLRNLEKGlrQDEAAPRLDRLIFDKIKQGFGGRVRLLF 388
Cdd:cd05927 203 ALKPTVFPGVPRVLNRIYDKIFNKVQAKGPLKRKLFNFALNYKLAELRSG--VVRASPFWDKLVFNKIKQALGGNVRLML 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 389 SGAAPLSRHVEEFLRVTSCSVLSQGYGLTESCGGCLTSIVNEFSMmGTVGVPYPTIEARLESVPEMGYDALSNVPRGEIC 468
Cdd:cd05927 281 TGSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATLTLPGDTSV-GHVGGPLPCAEVKLVDVPEMNYDAKDPNPRGEVC 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 469 LRGKTLFSGYFKRQDLTESAL-VDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSQGEYVAVENLENTYSRCPLITSIWVY 547
Cdd:cd05927 360 IRGPNVFSGYYKDPEKTAEALdEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLSQGEYVAPEKIENIYARSPFVAQIFVY 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 548 GNSFESFLVAVVVPDKKALEDWA-ENHNVTGDFKSLCENLEARKYILDELNNTGQNHQLKGFERLKAVHLDPNPFDIERD 626
Cdd:cd05927 440 GDSLKSFLVAIVVPDPDVLKEWAaSKGGGTGSFEELCKNPEVKKAILEDLVRLGKENGLKGFEQVKAIHLEPEPFSVENG 519
|
570 580
....*....|....*....|....*.
gi 225428594 627 LVTPTFKLKRPQLLKYYKDIIDRLYS 652
Cdd:cd05927 520 LLTPTFKLKRPQLKKYYKKQIDEMYK 545
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
1-659 |
0e+00 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 805.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 1 MAVYTVKVADSIPATEERPSAGPVYRCIYAENGLLEVPKGMESPWEFFSDSVERNPKNQMLGRRQIINSKAGPYVWLTYR 80
Cdd:PLN02430 1 MKSFAAQVEEGVKGKDGKPSVGPVYRNLLSKKGFPPIDSDITTAWDIFSKSVEKYPDNKMLGWRRIVDGKVGPYMWKTYK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 81 EAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQAIPYVPLYDSLGANAVEFIINHAEVSIAFVQESKIP 160
Cdd:PLN02430 81 EVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVAMEACAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVFVQDKKIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 161 AMLTCLPKCTSYLKTIISFGKISSSQKEEAEELGVSCFSWEEFALLGSLD-CELPPKQKTDICTIMYTSGTTGEPKGVVL 239
Cdd:PLN02430 161 ELLEPDCKSAKRLKAIVSFTSVTEEESDKASQIGVKTYSWIDFLHMGKENpSETNPPKPLDICTIMYTSGTSGDPKGVVL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 240 SNEAIMAEVLSTDQLLLETDKVATEEDTYFSFLPLAHVFDQIMETYCIYKGSSIGFWGADVRYLMEDIQELKPTIFCGVP 319
Cdd:PLN02430 241 THEAVATFVRGVDLFMEQFEDKMTHDDVYLSFLPLAHILDRMIEEYFFRKGASVGYYHGDLNALRDDLMELKPTLLAGVP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 320 RVYERIYGGAIAKISSGGALRKALFQYAYNYKLRNLEKGLRQDEAAPRLDRLIFDKIKQGFGGRVRLLFSGAAPLSRHVE 399
Cdd:PLN02430 321 RVFERIHEGIQKALQELNPRRRLIFNALYKYKLAWMNRGYSHKKASPMADFLAFRKVKAKLGGRLRLLISGGAPLSTEIE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 400 EFLRVTSCSVLSQGYGLTESCGGCLTSIVNEFSMMGTVGVPYPTIEARLESVPEMGYDALSNVPRGEICLRGKTLFSGYF 479
Cdd:PLN02430 401 EFLRVTSCAFVVQGYGLTETLGPTTLGFPDEMCMLGTVGAPAVYNELRLEEVPEMGYDPLGEPPRGEICVRGKCLFSGYY 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 480 KRQDLTESALVDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSQGEYVAVENLENTYSRCPLITSIWVYGNSFESFLVAVV 559
Cdd:PLN02430 481 KNPELTEEVMKDGWFHTGDIGEILPNGVLKIIDRKKNLIKLSQGEYVALEYLENVYGQNPIVEDIWVYGDSFKSMLVAVV 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 560 VPDKKALEDWAENHNVTGDFKSLCENLEARKYILDELNNTGQNHQLKGFERLKAVHLDPNPFDIERDLVTPTFKLKRPQL 639
Cdd:PLN02430 561 VPNEENTNKWAKDNGFTGSFEELCSLPELKEHILSELKSTAEKNKLRGFEYIKGVILETKPFDVERDLVTATLKKRRNNL 640
|
650 660
....*....|....*....|
gi 225428594 640 LKYYKDIIDRLYSEAKGTKS 659
Cdd:PLN02430 641 LKYYQVEIDEMYRKLAEKRI 660
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
48-653 |
0e+00 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 615.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 48 FSDSVERNPKNQMLGRRQIINSKAGPYVWLTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQAIP 127
Cdd:PLN02736 50 FVYAVETFRDYKYLGTRIRVDGTVGEYKWMTYGEAGTARTAIGSGLVQHGIPKGACVGLYFINRPEWLIVDHACSAYSYV 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 128 YVPLYDSLGANAVEFIINHAEVSIAFVQESKIPAMLTCLPKCTSyLKTIISFGKISSSQKEEAEELGVSCFSWEEFALLG 207
Cdd:PLN02736 130 SVPLYDTLGPDAVKFIVNHAEVAAIFCVPQTLNTLLSCLSEIPS-VRLIVVVGGADEPLPSLPSGTGVEIVTYSKLLAQG 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 208 SLDCE--LPPKQkTDICTIMYTSGTTGEPKGVVLSNEAIMAEVLSTDQLLLetdkvATEEDTYFSFLPLAHVFDQIMETY 285
Cdd:PLN02736 209 RSSPQpfRPPKP-EDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTK-----FYPSDVHISYLPLAHIYERVNQIV 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 286 CIYKGSSIGFWGADVRYLMEDIQELKPTIFCGVPRVYERIYGGAIAKISSGGALRKALFQYAYNYKLRNLEKGlrqDEAA 365
Cdd:PLN02736 283 MLHYGVAVGFYQGDNLKLMDDLAALRPTIFCSVPRLYNRIYDGITNAVKESGGLKERLFNAAYNAKKQALENG---KNPS 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 366 PRLDRLIFDKIKQGFGGRVRLLFSGAAPLSRHVEEFLRVTSCSVLSQGYGLTEScgGCLTSIVNEF-SMMGTVGVPYPTI 444
Cdd:PLN02736 360 PMWDRLVFNKIKAKLGGRVRFMSSGASPLSPDVMEFLRICFGGRVLEGYGMTET--SCVISGMDEGdNLSGHVGSPNPAC 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 445 EARLESVPEMGY-DALSNVPRGEICLRGKTLFSGYFKRQDLTESAL-VDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSQ 522
Cdd:PLN02736 438 EVKLVDVPEMNYtSEDQPYPRGEICVRGPIIFKGYYKDEVQTREVIdEDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLAQ 517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 523 GEYVAVENLENTYSRCPLITSIWVYGNSFESFLVAVVVPDKKALEDWAENHNV-TGDFKSLCENLEARKYILDELNNTGQ 601
Cdd:PLN02736 518 GEYIAPEKIENVYAKCKFVAQCFVYGDSLNSSLVAVVVVDPEVLKAWAASEGIkYEDLKQLCNDPRVRAAVLADMDAVGR 597
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 225428594 602 NHQLKGFERLKAVHLDPNPFDIERDLVTPTFKLKRPQLLKYYKDIIDRLYSE 653
Cdd:PLN02736 598 EAQLRGFEFAKAVTLVPEPFTVENGLLTPTFKVKRPQAKAYFAKAISDMYAE 649
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
46-654 |
4.29e-179 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 521.97 E-value: 4.29e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 46 EFFSDSVERNPKNQMLGRRqiinsKAGPYVWLTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEACNS-Q 124
Cdd:COG1022 15 DLLRRRAARFPDRVALREK-----EDGIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAaG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 125 AIPyVPLYDSLGANAVEFIINHAEVSIAFVQESKI-PAMLTCLPKCTSyLKTIISFgkisssqKEEAEELGVSCFSWEEF 203
Cdd:COG1022 90 AVT-VPIYPTSSAEEVAYILNDSGAKVLFVEDQEQlDKLLEVRDELPS-LRHIVVL-------DPRGLRDDPRLLSLDEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 204 ALLGS-------LDCELPPKQKTDICTIMYTSGTTGEPKGVVLSNEAIMAEVLSTDQLLLetdkvATEEDTYFSFLPLAH 276
Cdd:COG1022 161 LALGRevadpaeLEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLP-----LGPGDRTLSFLPLAH 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 277 VFDQIMETYCIYKGSSIGFWgADVRYLMEDIQELKPTIFCGVPRVYERIYGGAIAKISSGGALRKALFQYAYNYKLRNLE 356
Cdd:COG1022 236 VFERTVSYYALAAGATVAFA-ESPDTLAEDLREVKPTFMLAVPRVWEKVYAGIQAKAEEAGGLKRKLFRWALAVGRRYAR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 357 KGLRQDEAAPRL-------DRLIFDKIKQGFGGRVRLLFSGAAPLSRHVEEFLR---VTscsvLSQGYGLTESCGgclTS 426
Cdd:COG1022 315 ARLAGKSPSLLLrlkhalaDKLVFSKLREALGGRLRFAVSGGAALGPELARFFRalgIP----VLEGYGLTETSP---VI 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 427 IVNEFS--MMGTVGVPYPTIEARLEsvpemgydalsnvPRGEICLRGKTLFSGYFKRQDLTESAL-VDGWFHTGDIGEWQ 503
Cdd:COG1022 388 TVNRPGdnRIGTVGPPLPGVEVKIA-------------EDGEILVRGPNVMKGYYKNPEATAEAFdADGWLHTGDIGELD 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 504 PNGAMKIIDRKKNIFKLSQGEYVAVENLENTYSRCPLITSIWVYGNSfESFLVAVVVPDKKALEDWAENHNVT-GDFKSL 582
Cdd:COG1022 455 EDGFLRITGRKKDLIVTSGGKNVAPQPIENALKASPLIEQAVVVGDG-RPFLAALIVPDFEALGEWAEENGLPyTSYAEL 533
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 225428594 583 CENLEARKYILDELNNTgqNHQLKGFERLKAVHLDPNPFDIERDLVTPTFKLKRPQLLKYYKDIIDRLYSEA 654
Cdd:COG1022 534 AQDPEVRALIQEEVDRA--NAGLSRAEQIKRFRLLPKEFTIENGELTPTLKLKRKVILEKYADLIEALYAGA 603
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
72-636 |
1.20e-173 |
|
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: 504.44 E-value: 1.20e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 72 GPYVWLTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQAIPYVPLYDSLGANAVEFIINHAEVSi 151
Cdd:cd17639 1 GEYKYMSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECS- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 152 afvqeskipamltclpkctsylkTIISFGKisssqkeeaeelgvscfsweefallgsldcelppkqKTDICTIMYTSGTT 231
Cdd:cd17639 80 -----------------------AIFTDGK------------------------------------PDDLACIMYTSGST 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 232 GEPKGVVLSNEAIMAEVLSTDQLLletDKVATEEDTYFSFLPLAHVFDQIMETYCIYKGSSIGFwgADVRYLME------ 305
Cdd:cd17639 101 GNPKGVMLTHGNLVAGIAGLGDRV---PELLGPDDRYLAYLPLAHIFELAAENVCLYRGGTIGY--GSPRTLTDkskrgc 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 306 --DIQELKPTIFCGVPRVYERIYGGAIAKISSGGALRKALFQYAYNYKLRNLEKGLrqdeAAPRLDRLIFDKIKQGFGGR 383
Cdd:cd17639 176 kgDLTEFKPTLMVGVPAIWDTIRKGVLAKLNPMGGLKRTLFWTAYQSKLKALKEGP----GTPLLDELVFKKVRAALGGR 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 384 VRLLFSGAAPLSRHVEEFLRVTSCSVLsQGYGLTESCGGCLTSIVNEFSMmGTVGVPYPTIEARLESVPEMGYDALSNVP 463
Cdd:cd17639 252 LRYMLSGGAPLSADTQEFLNIVLCPVI-QGYGLTETCAGGTVQDPGDLET-GRVGPPLPCCEIKLVDWEEGGYSTDKPPP 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 464 RGEICLRGKTLFSGYFKRQDLTESALV-DGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSQGEYVAVENLENTYSRCPLIT 542
Cdd:cd17639 330 RGEILIRGPNVFKGYYKNPEKTKEAFDgDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQNGEYIALEKLESIYRSNPLVN 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 543 SIWVYGNSFESFLVAVVVPDKKALEDWAENHNV-TGDFKSLCENLEARKYILDELNNTGQNHQLKGFERLKAVHLDPNPF 621
Cdd:cd17639 410 NICVYADPDKSYPVAIVVPNEKHLTKLAEKHGViNSEWEELCEDKKLQKAVLKSLAETARAAGLEKFEIPQGVVLLDEEW 489
|
570
....*....|....*
gi 225428594 622 DIERDLVTPTFKLKR 636
Cdd:cd17639 490 TPENGLVTAAQKLKR 504
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
72-639 |
8.28e-135 |
|
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: 403.13 E-value: 8.28e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 72 GPYVWLTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQAIPYVPLYDSLGANAVEFIINHAEVSI 151
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 152 AFVQEskipamltclpkctsylktiisfgkisssqkeeaeelgvscfsweefallgsldcelppkqKTDICTIMYTSGTT 231
Cdd:cd05907 81 LFVED-------------------------------------------------------------PDDLATIIYTSGTT 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 232 GEPKGVVLSNEAIMAEVLSTDQLLletdkVATEEDTYFSFLPLAHVFDQIM-ETYCIYKGSSIGFWgADVRYLMEDIQEL 310
Cdd:cd05907 100 GRPKGVMLSHRNILSNALALAERL-----PATEGDRHLSFLPLAHVFERRAgLYVPLLAGARIYFA-SSAETLLDDLSEV 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 311 KPTIFCGVPRVYERIYggAIAKISSGGALRKALFQYAYnyklrnlekglrqdeaaprldrlifdkikqgfGGRVRLLFSG 390
Cdd:cd05907 174 RPTVFLAVPRVWEKVY--AAIKVKAVPGLKRKLFDLAV--------------------------------GGRLRFAASG 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 391 AAPLSRHVEEFLRVTSCSVLsQGYGLTESCGGCLTSIVNEFSMmGTVGVPYPTIEARLesvpemgydalsnVPRGEICLR 470
Cdd:cd05907 220 GAPLPAELLHFFRALGIPVY-EGYGLTETSAVVTLNPPGDNRI-GTVGKPLPGVEVRI-------------ADDGEILVR 284
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 471 GKTLFSGYFKRQDLTESALV-DGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSQGEYVAVENLENTYSRCPLITSIWVYGN 549
Cdd:cd05907 285 GPNVMLGYYKNPEATAEALDaDGWLHTGDLGEIDEDGFLHITGRKKDLIITSGGKNISPEPIENALKASPLISQAVVIGD 364
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 550 SfESFLVAVVVPDKKALEDWAENHNVTG-DFKSLCENLEARKYILDELNNTgqNHQLKGFERLKAVHLDPNPFDIERDLV 628
Cdd:cd05907 365 G-RPFLVALIVPDPEALEAWAEEHGIAYtDVAELAANPAVRAEIEAAVEAA--NARLSRYEQIKKFLLLPEPFTIENGEL 441
|
570
....*....|.
gi 225428594 629 TPTFKLKRPQL 639
Cdd:cd05907 442 TPTLKLKRPVI 452
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
38-652 |
1.05e-124 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 385.24 E-value: 1.05e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 38 PKGMESPWE-------FFSDSVERNPKNQMLGRRQIINSKA--------------GPYVWLTYREAYDAALRMGSAMRSR 96
Cdd:PLN02387 47 PELVETPWEgattlaaLFEQSCKKYSDKRLLGTRKLISREFetssdgrkfeklhlGEYEWITYGQVFERVCNFASGLVAL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 97 GVNPGDRCGIYGSNCPEWIIAMEACNSQAIPYVPLYDSLGANAVEFIINHAEVSIAFV---QESKIPAMLTCLpkctSYL 173
Cdd:PLN02387 127 GHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICdskQLKKLIDISSQL----ETV 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 174 KTIISFGKISSSQKEEAEELG---VSCFS-WEEFALLGSLDCELPpkQKTDICTIMYTSGTTGEPKGVVLSNEAIMAEVL 249
Cdd:PLN02387 203 KRVIYMDDEGVDSDSSLSGSSnwtVSSFSeVEKLGKENPVDPDLP--SPNDIAVIMYTSGSTGLPKGVMMTHGNIVATVA 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 250 STDQLLLETDKvateEDTYFSFLPLAHVFDQIMETYCIYKGSSIGFWGA----DV-----RYLMEDIQELKPTIFCGVPR 320
Cdd:PLN02387 281 GVMTVVPKLGK----NDVYLAYLPLAHILELAAESVMAAVGAAIGYGSPltltDTsnkikKGTKGDASALKPTLMTAVPA 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 321 VYERIYGGAIAKISSGGALRKALFQYAYNYKLRNLEKGLRQDEAAPRL--DRLIFDKIKQGFGGRVRLLFSGAAPLSRHV 398
Cdd:PLN02387 357 ILDRVRDGVRKKVDAKGGLAKKLFDIAYKRRLAAIEGSWFGAWGLEKLlwDALVFKKIRAVLGGRIRFMLSGGAPLSGDT 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 399 EEFLRVTSCSVLSQGYGLTESCGGCLTSIVNEFSMmGTVGVPYPTIEARLESVPEMGYDAL-SNVPRGEICLRGKTLFSG 477
Cdd:PLN02387 437 QRFINICLGAPIGQGYGLTETCAGATFSEWDDTSV-GRVGPPLPCCYVKLVSWEEGGYLISdKPMPRGEIVIGGPSVTLG 515
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 478 YFKRQDLT-ESALVDG----WFHTGDIGEWQPNGAMKIIDRKKNIFKLSQGEYVAVENLENTYSRCPLITSIWVYGNSFE 552
Cdd:PLN02387 516 YFKNQEKTdEVYKVDErgmrWFYTGDIGQFHPDGCLEIIDRKKDIVKLQHGEYVSLGKVEAALSVSPYVDNIMVHADPFH 595
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 553 SFLVAVVVPDKKALEDWAENHNVT-GDFKSLCENLEARKYILDELNNTGQNHQLKGFERLKAVHLDPNPFDIERDLVTPT 631
Cdd:PLN02387 596 SYCVALVVPSQQALEKWAKKAGIDySNFAELCEKEEAVKEVQQSLSKAAKAARLEKFEIPAKIKLLPEPWTPESGLVTAA 675
|
650 660
....*....|....*....|.
gi 225428594 632 FKLKRPQLLKYYKDIIDRLYS 652
Cdd:PLN02387 676 LKLKREQIRKKFKDDLKKLYE 696
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
72-521 |
3.10e-108 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 333.51 E-value: 3.10e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 72 GPYVWLTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQAIPYVPLYDSLGANAVEFIINHAEVSI 151
Cdd:pfam00501 17 GEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSGAKV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 152 AFVQES-KIPAMLTCLPKCTS-YLKTIISFGKISSSQKEEAEELgvscfsweefaLLGSLDCELPPKQKTDICTIMYTSG 229
Cdd:pfam00501 97 LITDDAlKLEELLEALGKLEVvKLVLVLDRDPVLKEEPLPEEAK-----------PADVPPPPPPPPDPDDLAYIIYTSG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 230 TTGEPKGVVLSNEAIMAEVLSTDQLLLETDKVaTEEDTYFSFLPLAHVFDQIMETYC-IYKGSSIGFWG----ADVRYLM 304
Cdd:pfam00501 166 TTGKPKGVMLTHRNLVANVLSIKRVRPRGFGL-GPDDRVLSTLPLFHDFGLSLGLLGpLLAGATVVLPPgfpaLDPAALL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 305 EDIQELKPTIFCGVPRVYERIYggaiakissggalrkalfqyaynyklrnlekglrqdeAAPRLDRLIFdkikqgfgGRV 384
Cdd:pfam00501 245 ELIERYKVTVLYGVPTLLNMLL-------------------------------------EAGAPKRALL--------SSL 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 385 RLLFSGAAPLSRHVEEFLRVTSCSVLSQGYGLTESCGGCLTSI--VNEFSMMGTVGVPYPTIEARLESVPEMGYDALSNV 462
Cdd:pfam00501 280 RLVLSGGAPLPPELARRFRELFGGALVNGYGLTETTGVVTTPLplDEDLRSLGSVGRPLPGTEVKIVDDETGEPVPPGEP 359
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 463 prGEICLRGKTLFSGYFKRQDLTESALV-DGWFHTGDIGEWQPNGAMKIIDRKKNIFKLS 521
Cdd:pfam00501 360 --GELCVRGPGVMKGYLNDPELTAEAFDeDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
75-653 |
3.84e-102 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 326.55 E-value: 3.84e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 75 VWLTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQAIPYVPLYDSLGANAVEFIINHAEVSIAFV 154
Cdd:PTZ00216 120 RYITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAIVC 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 155 QESKIPAMLTCLPKCTSYLKTIISFGKISSSQKEEaeelGVSCFSWEEFALLGSL--DCELP--PKQKTDICTIMYTSGT 230
Cdd:PTZ00216 200 NGKNVPNLLRLMKSGGMPNTTIIYLDSLPASVDTE----GCRLVAWTDVVAKGHSagSHHPLniPENNDDLALIMYTSGT 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 231 TGEPKGVVLSNEAIMAEVLSTDQLLLETDKVATEEDTYFSFLPLAHVFDQIMETYCIYKGSSIGFwgADVRYLME----- 305
Cdd:PTZ00216 276 TGDPKGVMHTHGSLTAGILALEDRLNDLIGPPEEDETYCSYLPLAHIMEFGVTNIFLARGALIGF--GSPRTLTDtfarp 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 306 --DIQELKPTIFCGVPRVYERIYGGAIAKISSGGALRKALFQYAYNYKLRNLEKGlrqdEAAPRLDRLIFDKIKQGFGGR 383
Cdd:PTZ00216 354 hgDLTEFRPVFLIGVPRIFDTIKKAVEAKLPPVGSLKRRVFDHAYQSRLRALKEG----KDTPYWNEKVFSAPRAVLGGR 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 384 VRLLFSGAAPLSRHVEEFLRVTSCSVLsQGYGLTESCggCLTSIVNEFSM-MGTVGVPYPTIEARLESVPEMGY-DALSn 461
Cdd:PTZ00216 430 VRAMLSGGGPLSAATQEFVNVVFGMVI-QGWGLTETV--CCGGIQRTGDLePNAVGQLLKGVEMKLLDTEEYKHtDTPE- 505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 462 vPRGEICLRGKTLFSGYFKRQDLTESALV-DGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSQGEYVAVENLENTYSRCPL 540
Cdd:PTZ00216 506 -PRGEILLRGPFLFKGYYKQEELTREVLDeDGWFHTGDVGSIAANGTLRIIGRVKALAKNCLGEYIALEALEALYGQNEL 584
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 541 IT--SIWVYGNSFESFLVAVVVPDKKALEDWAENHNVTGDFKSLCENLEARKYILDELNNTGQNHQLKGFERLKAVHLDP 618
Cdd:PTZ00216 585 VVpnGVCVLVHPARSYICALVLTDEAKAMAFAKEHGIEGEYPAILKDPEFQKKATESLQETARAAGRKSFEIVRHVRVLS 664
|
570 580 590
....*....|....*....|....*....|....*
gi 225428594 619 NPFDIERDLVTPTFKLKRPQLLKYYKDIIDRLYSE 653
Cdd:PTZ00216 665 DEWTPENGVLTAAMKLKRRVIDERYADLIKELFAD 699
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
72-637 |
1.19e-75 |
|
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: 249.97 E-value: 1.19e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 72 GPYVWLTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAmeacnSQAIPyvplydSLGA-NAV---------- 140
Cdd:cd17640 1 KPPKRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIA-----DQGIM------ALGAvDVVrgsdssveel 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 141 EFIINHAEVSIAFVQESkipamltclpkctsylktiisfgkisssqkeeaeelgvscfsweefallgsldcelpPKqktD 220
Cdd:cd17640 70 LYILNHSESVALVVEND---------------------------------------------------------SD---D 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 221 ICTIMYTSGTTGEPKGVVLSNEAIMAEVlstDQLLLETDKVATeeDTYFSFLPLAHVFDQIMETYCIYKGSSIGFwgADV 300
Cdd:cd17640 90 LATIIYTSGTTGNPKGVMLTHANLLHQI---RSLSDIVPPQPG--DRFLSILPIWHSYERSAEYFIFACGCSQAY--TSI 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 301 RYLMEDIQELKPTIFCGVPRVYERIYGGAIAKISSGGALRKALFQYAYnyklrnlekglrqdeaaprldrlifdkikqgF 380
Cdd:cd17640 163 RTLKDDLKRVKPHYIVSVPRLWESLYSGIQKQVSKSSPIKQFLFLFFL-------------------------------S 211
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 381 GGRVRLLFSGAAPLSRHVEEFLRVTSCSVLsQGYGLTESCGGcltSIVNEFS--MMGTVGVPYPTIEARLesvpemgYDA 458
Cdd:cd17640 212 GGIFKFGISGGGALPPHVDTFFEAIGIEVL-NGYGLTETSPV---VSARRLKcnVRGSVGRPLPGTEIKI-------VDP 280
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 459 LSNVP-----RGEICLRGKTLFSGYFKRQDLTESAL-VDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSQGEYVAVENLE 532
Cdd:cd17640 281 EGNVVlppgeKGIVWVRGPQVMKGYYKNPEATSKVLdSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSNGENVEPQPIE 360
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 533 NTYSRCPLITSIWVYGNSfESFLVAVVVPDKKALEDWAENHNV--TGDFKSLCENLEARKYILDELNNTGQNHQL-KGFE 609
Cdd:cd17640 361 EALMRSPFIEQIMVVGQD-QKRLGALIVPNFEELEKWAKESGVklANDRSQLLASKKVLKLYKNEIKDEISNRPGfKSFE 439
|
570 580
....*....|....*....|....*...
gi 225428594 610 RLKAVHLDPNPFdIERDLVTPTFKLKRP 637
Cdd:cd17640 440 QIAPFALLEEPF-IENGEMTQTMKIKRN 466
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
72-643 |
2.53e-74 |
|
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: 247.77 E-value: 2.53e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 72 GPYVWLTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQAIPYVPLYDSLGANAVEFIINHAEVSI 151
Cdd:cd05932 2 GQVVEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 152 AFV-----QESKIPAMLTCLPKCTSYLKTIISFGkisssqkeeaeelgvscFSWEEFALLGSLDCELPPKQKTDICTIMY 226
Cdd:cd05932 82 LFVgklddWKAMAPGVPEGLISISLPPPSAANCQ-----------------YQWDDLIAQHPPLEERPTRFPEQLATLIY 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 227 TSGTTGEPKGVVLSneaiMAEVLSTDQLLLETDKVaTEEDTYFSFLPLAHVFDQI-METYCIYKGSSIGFwGADVRYLME 305
Cdd:cd05932 145 TSGTTGQPKGVMLT----FGSFAWAAQAGIEHIGT-EENDRMLSYLPLAHVTERVfVEGGSLYGGVLVAF-AESLDTFVE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 306 DIQELKPTIFCGVPRVYERIYGGAIAKISSGgalrkalfqyaynyKLRNLEKglrqdeaAPRLDRLIFDKIKQGFG-GRV 384
Cdd:cd05932 219 DVQRARPTLFFSVPRLWTKFQQGVQDKIPQQ--------------KLNLLLK-------IPVVNSLVKRKVLKGLGlDQC 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 385 RLLFSGAAPLSRHVEEFLRVTSCSVLsQGYGLTESCGgclTSIVNE--FSMMGTVGVPYPTIEARLEsvpemgydalsnv 462
Cdd:cd05932 278 RLAGCGSAPVPPALLEWYRSLGLNIL-EAYGMTENFA---YSHLNYpgRDKIGTVGNAGPGVEVRIS------------- 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 463 PRGEICLRGKTLFSGYFKRQDLTESALV-DGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSQGEYVAVENLENTYSRCPLI 541
Cdd:cd05932 341 EDGEILVRSPALMMGYYKDPEATAEAFTaDGFLRTGDKGELDADGNLTITGRVKDIFKTSKGKYVAPAPIENKLAEHDRV 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 542 TSIWVYGNSFESFLVAVVvpdkkaLEDWAENHNVTGDFKSLCENLEArkyILDELNNTGQNHqlkgfERLKAVHLDPNPF 621
Cdd:cd05932 421 EMVCVIGSGLPAPLALVV------LSEEARLRADAFARAELEASLRA---HLARVNSTLDSH-----EQLAGIVVVKDPW 486
|
570 580
....*....|....*....|..
gi 225428594 622 DIERDLVTPTFKLKRPQLLKYY 643
Cdd:cd05932 487 SIDNGILTPTLKIKRNVLEKAY 508
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
77-651 |
9.52e-71 |
|
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: 240.72 E-value: 9.52e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 77 LTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIA-MEACNSQAIpYVPLYDSLGANAVEFIINHAEVSIAFV- 154
Cdd:cd05933 9 LTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAaVGAIFAGGI-AVGIYTTNSPEACQYVAETSEANILVVe 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 155 ---QESKIPAMLTCLPKctsyLKTIISFgkisssqKEEAEELGVSCFSWEEFALLGSldcELPPKQKTDI---------C 222
Cdd:cd05933 88 nqkQLQKILQIQDKLPH----LKAIIQY-------KEPLKEKEPNLYSWDEFMELGR---SIPDEQLDAIissqkpnqcC 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 223 TIMYTSGTTGEPKGVVLSNEAIM--AEVLSTDQLLLETDKvatEEDTYFSFLPLAHVFDQIMETY-CIYKGSSIGFWGAD 299
Cdd:cd05933 154 TLIYTSGTTGMPKGVMLSHDNITwtAKAASQHMDLRPATV---GQESVVSYLPLSHIAAQILDIWlPIKVGGQVYFAQPD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 300 VR--YLMEDIQELKPTIFCGVPRVYERIYGGAIAKISSGGALRKALFQYAYNYKLRNLEKGLRQDEAAPR----LDRLIF 373
Cdd:cd05933 231 ALkgTLVKTLREVRPTAFMGVPRVWEKIQEKMKAVGAKSGTLKRKIASWAKGVGLETNLKLMGGESPSPLfyrlAKKLVF 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 374 DKIKQGFG-GRVRLLFSGAAPLSRHVEEFLrvtsCSV---LSQGYGLTESCGGCLTSIVNEFSmMGTVGVPYPTIEARLE 449
Cdd:cd05933 311 KKVRKALGlDRCQKFFTGAAPISRETLEFF----LSLnipIMELYGMSETSGPHTISNPQAYR-LLSCGKALPGCKTKIH 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 450 SVPEMGYdalsnvprGEICLRGKTLFSGYFKRQDLTESAL-VDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSQGEYVAV 528
Cdd:cd05933 386 NPDADGI--------GEICFWGRHVFMGYLNMEDKTEEAIdEDGWLHSGDLGKLDEDGFLYITGRIKELIITAGGENVPP 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 529 ENLENTY-SRCPLITSIWVYGNS--FESFLVAV---VVPDKKALEDwaenhNVTGDFKSLCENLEARKYILDELNNtGQN 602
Cdd:cd05933 458 VPIEDAVkKELPIISNAMLIGDKrkFLSMLLTLkceVNPETGEPLD-----ELTEEAIEFCRKLGSQATRVSEIAG-GKD 531
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 225428594 603 HQL-----KGFERL--KAVH---------LDPNPFDIERDLVTPTFKLKRPQLLKYYKDIIDRLY 651
Cdd:cd05933 532 PKVyeaieEGIKRVnkKAISnaqkiqkwvILEKDFSVPGGELGPTMKLKRPVVAKKYKDEIDKLY 596
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
77-571 |
1.76e-67 |
|
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: 227.77 E-value: 1.76e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 77 LTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQAIPYVPLYDSLGANAVEFIINHAEVSIAFVqe 156
Cdd:COG0318 25 LTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEELAYILEDSGARALVT-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 157 skipamltclpkctsylktiisfgkisssqkeeaeelgvscfsweefallgsldcelppkqktdiCTIMYTSGTTGEPKG 236
Cdd:COG0318 103 -----------------------------------------------------------------ALILYTSGTTGRPKG 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 237 VVLSNEAIMAEVLSTDQLLLetdkvATEEDTYFSFLPLAHVFDQIMETY-CIYKGSSI----GFWGADVrylMEDIQELK 311
Cdd:COG0318 118 VMLTHRNLLANAAAIAAALG-----LTPGDVVLVALPLFHVFGLTVGLLaPLLAGATLvllpRFDPERV---LELIERER 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 312 PTIFCGVPRVYERIyggaiakissggalrkalfqyaynyklrnlekgLRQDEAAPR-LDRLifdkikqgfggrvRLLFSG 390
Cdd:COG0318 190 VTVLFGVPTMLARL---------------------------------LRHPEFARYdLSSL-------------RLVVSG 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 391 AAPLSRHV-EEFLRVTSCsVLSQGYGLTESCGGCLTSIVNEF-SMMGTVGVPYPTIEARLesVPEMGYDalsnVPR---G 465
Cdd:COG0318 224 GAPLPPELlERFEERFGV-RIVEGYGLTETSPVVTVNPEDPGeRRPGSVGRPLPGVEVRI--VDEDGRE----LPPgevG 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 466 EICLRGKTLFSGYFKRQDLTESALVDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSqGEYVAVENLENTYSRCPLITSiw 545
Cdd:COG0318 297 EIVVRGPNVMKGYWNDPEATAEAFRDGWLRTGDLGRLDEDGYLYIVGRKKDMIISG-GENVYPAEVEEVLAAHPGVAE-- 373
|
490 500
....*....|....*....|....*..
gi 225428594 546 vygnsfesflVAVV-VPDkkalEDWAE 571
Cdd:COG0318 374 ----------AAVVgVPD----EKWGE 386
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
187-648 |
1.38e-60 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 216.12 E-value: 1.38e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 187 KEEAEELGVSCFSWEEFALLGSLDCELPPKQKTDICTIMYTSGTTGEPKGVVLSNEAIMAEVLS-TDQLLLETDKVatee 265
Cdd:PTZ00342 272 KEKAKKLGISIILFDDMTKNKTTNYKIQNEDPDFITSIVYTSGTSGKPKGVMLSNKNLYNTVVPlCKHSIFKKYNP---- 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 266 DTYFSFLPLAHVFDQIMETYCIYKGSSIGFWGADVRYLMEDIQELKPTIFCGVPRVYERIYGGAIAKISSGGALRKALFQ 345
Cdd:PTZ00342 348 KTHLSYLPISHIYERVIAYLSFMLGGTINIWSKDINYFSKDIYNSKGNILAGVPKVFNRIYTNIMTEINNLPPLKRFLVK 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 346 YAYNYKLRNLEKGLRQdeaapRLDRL--IFDKIKQGFGGRVRLLFSGAAPLSRHVEEFLRVTSCSVLSQGYGLTESCGGC 423
Cdd:PTZ00342 428 KILSLRKSNNNGGFSK-----FLEGIthISSKIKDKVNPNLEVILNGGGKLSPKIAEELSVLLNVNYYQGYGLTETTGPI 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 424 LTSIVNEFSMMgTVGVPY-PTIEARLESVPEmgYDALSNVPRGEICLRGKTLFSGYFKRQDLTESALV-DGWFHTGDIGE 501
Cdd:PTZ00342 503 FVQHADDNNTE-SIGGPIsPNTKYKVRTWET--YKATDTLPKGELLIKSDSIFSGYFLEKEQTKNAFTeDGYFKTGDIVQ 579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 502 WQPNGAMKIIDRKKNIFKLSQGEYVAVENLENTYSRCPLITSIWVYGNSFESFLVAVVVPDKKALEDWAENHNV---TG- 577
Cdd:PTZ00342 580 INKNGSLTFLDRSKGLVKLSQGEYIETDMLNNLYSQISFINFCVVYGDDSMDGPLAIISVDKYLLFKCLKDDNMlesTGi 659
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 225428594 578 DFKSLCENL--------EARKYILDELNNTGQNHQLKGFERLKAVHLDPNPFDIERDLvTPTFKLKRPQLLKYYKDIID 648
Cdd:PTZ00342 660 NEKNYLEKLtdetinnnIYVDYVKGKMLEVYKKTNLNRYNIINDIYLTSKVWDTNNYL-TPTFKVKRFYVFKDYAFFID 737
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
77-636 |
6.73e-58 |
|
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: 202.29 E-value: 6.73e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 77 LTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQAIPYVPLYDSLGANAVEFIINHAEVSIAFVQE 156
Cdd:cd05914 8 LTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFVSD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 157 skipamltclpkctsylktiisfgkisssqkeeaeelgvscfsweefallgsldcelppkqKTDICTIMYTSGTTGEPKG 236
Cdd:cd05914 88 -------------------------------------------------------------EDDVALINYTSGTTGNSKG 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 237 VVLSNEAIMAEVLSTDQLLLetdkvATEEDTYFSFLPLAHV----FDQIMETYciyKGSSIGFWG--ADVRYLMEDIQEL 310
Cdd:cd05914 107 VMLTYRNIVSNVDGVKEVVL-----LGKGDKILSILPLHHIypltFTLLLPLL---NGAHVVFLDkiPSAKIIALAFAQV 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 311 KPTIFCGVPRVYERIYGGAIAKISSGGALRKALFQYAYNYKLRNLekglrqdeaaprldrlIFDKIKQGFGGRVRLLFSG 390
Cdd:cd05914 179 TPTLGVPVPLVIEKIFKMDIIPKLTLKKFKFKLAKKINNRKIRKL----------------AFKKVHEAFGGNIKEFVIG 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 391 AAPLSRHVEEFLRVTSCSVlSQGYGLTEsCGGCLTSIVNEFSMMGTVGVPYPTIEARLESVPEMGYDalsnvprGEICLR 470
Cdd:cd05914 243 GAKINPDVEEFLRTIGFPY-TIGYGMTE-TAPIISYSPPNRIRLGSAGKVIDGVEVRIDSPDPATGE-------GEIIVR 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 471 GKTLFSGYFKRQDLTESALV-DGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSQGEYVAVENLENTYSRCP--LITSIWVy 547
Cdd:cd05914 314 GPNVMKGYYKNPEATAEAFDkDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSSGKNIYPEEIEAKINNMPfvLESLVVV- 392
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 548 gnsFESFLVAVVVPDKKALEDWAEnhNVTGDFKSLCENLearkyiLDELNNtgqnhQLKGFERLKAVHLDPNPFDierdl 627
Cdd:cd05914 393 ---QEKKLVALAYIDPDFLDVKAL--KQRNIIDAIKWEV------RDKVNQ-----KVPNYKKISKVKIVKEEFE----- 451
|
....*....
gi 225428594 628 VTPTFKLKR 636
Cdd:cd05914 452 KTPKGKIKR 460
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
75-575 |
4.76e-57 |
|
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: 202.65 E-value: 4.76e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 75 VW--LTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEACNS-QAIPyVPLYDSLGANAVEFIINHAEVSI 151
Cdd:cd17641 8 IWqeFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAiGALS-LGIYQDSMAEEVAYLLNYTGARV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 152 AFVQ-ESKIPAMLTCLPKCTSYLKTIISFGKISSSQK-------EEAEELGVSCFSWEEfallGSLDCELPPKQKTDICT 223
Cdd:cd17641 87 VIAEdEEQVDKLLEIADRIPSVRYVIYCDPRGMRKYDdprlisfEDVVALGRALDRRDP----GLYEREVAAGKGEDVAV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 224 IMYTSGTTGEPKGVVLSNEAImaevLSTDQLLLETDKVATEEDtYFSFLPLAHVFDQIMET-YCIYKGSSIGFwGADVRY 302
Cdd:cd17641 163 LCTTSGTTGKPKLAMLSHGNF----LGHCAAYLAADPLGPGDE-YVSVLPLPWIGEQMYSVgQALVCGFIVNF-PEEPET 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 303 LMEDIQELKPTIFCGVPRVYERIYGGAIAKISSGGALRKALFQYAYNYKLRNLEKGLRQDEAAPRL-------DRLIFDK 375
Cdd:cd17641 237 MMEDLREIGPTFVLLPPRVWEGIAADVRARMMDATPFKRFMFELGMKLGLRALDRGKRGRPVSLWLrlaswlaDALLFRP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 376 IKQGFG-GRVRLLFSGAAPLSRHVEEFLRVTSCSvLSQGYGLTESCGgcLTSIVNEFSM-MGTVGVPYPTIEARLESVpe 453
Cdd:cd17641 317 LRDRLGfSRLRSAATGGAALGPDTFRFFHAIGVP-LKQLYGQTELAG--AYTVHRDGDVdPDTVGVPFPGTEVRIDEV-- 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 454 mgydalsnvprGEICLRGKTLFSGYFKRQDLTESALV-DGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSQGEYVAVENLE 532
Cdd:cd17641 392 -----------GEILVRSPGVFVGYYKNPEATAEDFDeDGWLHTGDAGYFKENGHLVVIDRAKDVGTTSDGTRFSPQFIE 460
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 225428594 533 NTYSRCPLITSIWVYGNSFEsFLVAVVVPDKKALEDWAENHNV 575
Cdd:cd17641 461 NKLKFSPYIAEAVVLGAGRP-YLTAFICIDYAIVGKWAEQRGI 502
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
77-519 |
4.81e-56 |
|
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: 197.82 E-value: 4.81e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 77 LTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQAIPYVPLYDSLGANAVEFIINHAEVSIAFVQE 156
Cdd:cd05911 11 LTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTDP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 157 SKIPAMLTCLpKCTSYLKTIISFGkiSSSQKEEAEELGVSCFSWEEFALLgsldcELPPKQ-KTDICTIMYTSGTTGEPK 235
Cdd:cd05911 91 DGLEKVKEAA-KELGPKDKIIVLD--DKPDGVLSIEDLLSPTLGEEDEDL-----PPPLKDgKDDTAAILYSSGTTGLPK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 236 GVVLSNEAIMAEVLSTDQLLLETDKVateEDTYFSFLPLAHVFDQIMETYCIYKGSSI----GFwgaDVRYLMEDIQELK 311
Cdd:cd05911 163 GVCLSHRNLIANLSQVQTFLYGNDGS---NDVILGFLPLYHIYGLFTTLASLLNGATViimpKF---DSELFLDLIEKYK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 312 PTIFCGVPRVyeriyggaIAKISSGGALRKalfqyaynYKLRNLekglrqdeaaprldrlifdkikqgfggrvRLLFSGA 391
Cdd:cd05911 237 ITFLYLVPPI--------AAALAKSPLLDK--------YDLSSL-----------------------------RVILSGG 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 392 APLSRHVEEFL-RVTSCSVLSQGYGLTESCGGCLTSIVNEFSMmGTVGVPYPTIEARLesVPEMGYDALSNVPRGEICLR 470
Cdd:cd05911 272 APLSKELQELLaKRFPNATIKQGYGMTETGGILTVNPDGDDKP-GSVGRLLPNVEAKI--VDDDGKDSLGPNEPGEICVR 348
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 225428594 471 GKTLFSGYFKRQDLTESALV-DGWFHTGDIGEWQPNGAMKIIDRKKNIFK 519
Cdd:cd05911 349 GPQVMKGYYNNPEATKETFDeDGWLHTGDIGYFDEDGYLYIVDRKKELIK 398
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
78-571 |
2.17e-55 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 196.95 E-value: 2.17e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 78 TYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQAIPYVPLYDSLGANAVEFIINHAEVSIAFVQES 157
Cdd:PRK06187 33 TYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIRLKPEEIAYILNDAEDRVVLVDSE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 158 KIPAMLTCLPKCTSyLKTIISFGKisssqkEEAEELGVSCFSWEEFALLGSLDCELPPKQKTDICTIMYTSGTTGEPKGV 237
Cdd:PRK06187 113 FVPLLAAILPQLPT-VRTVIVEGD------GPAAPLAPEVGEYEELLAAASDTFDFPDIDENDAAAMLYTSGTTGHPKGV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 238 VLSNeaimaevlstDQLLLETDKVA-----TEEDTYFSFLPLAHVFdqimETYC----IYKGSSIGFWGA-DVRYLMEDI 307
Cdd:PRK06187 186 VLSH----------RNLFLHSLAVCawlklSRDDVYLVIVPMFHVH----AWGLpylaLMAGAKQVIPRRfDPENLLDLI 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 308 QELKPTIFCGVPRVYeriyggaiakissgGALRKALFQYAYNYklrnlekglrqdeaaprldrlifdkikqgfgGRVRLL 387
Cdd:PRK06187 252 ETERVTFFFAVPTIW--------------QMLLKAPRAYFVDF-------------------------------SSLRLV 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 388 FSGAAPLSRH-VEEFLRVTSCSVLsQGYGLTEsCGGCLT------SIVNEFSMMGTVGVPYPTIEARL-----ESVPEMG 455
Cdd:PRK06187 287 IYGGAALPPAlLREFKEKFGIDLV-QGYGMTE-TSPVVSvlppedQLPGQWTKRRSAGRPLPGVEARIvdddgDELPPDG 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 456 YDAlsnvprGEICLRGKTLFSGYFKRQDLTESALVDGWFHTGDIGEWQPNGAMKIIDRKKNIFKlSQGEYV-AVEnLENT 534
Cdd:PRK06187 365 GEV------GEIIVRGPWLMQGYWNRPEATAETIDGGWLHTGDVGYIDEDGYLYITDRIKDVII-SGGENIyPRE-LEDA 436
|
490 500 510
....*....|....*....|....*....|....*...
gi 225428594 535 YSRCPLITSiwvygnsfesflVAVV-VPDKKaledWAE 571
Cdd:PRK06187 437 LYGHPAVAE------------VAVIgVPDEK----WGE 458
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
220-565 |
6.52e-54 |
|
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: 187.88 E-value: 6.52e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 220 DICTIMYTSGTTGEPKGVVLSNEAIMAEVLSTDQLLLETdkvatEEDTYFSFLPLAHVFDQIMETYCIYKGSSI----GF 295
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLT-----EGDVFLSTLPLFHIGGLFGLLGALLAGGTVvllpKF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 296 wgaDVRYLMEDIQELKPTIFCGVPRVYERIyggaiakissggalrkalfqyaynyklrnlekgLRQDEAAPR-LDRLifd 374
Cdd:cd04433 76 ---DPEAALELIEREKVTILLGVPTLLARL---------------------------------LKAPESAGYdLSSL--- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 375 kikqgfggrvRLLFSGAAPLSRHVEEFLRVTSCSVLSQGYGLTESCGG-CLTSIVNEFSMMGTVGVPYPTIEARLesVPE 453
Cdd:cd04433 117 ----------RALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTvATGPPDDDARKPGSVGRPVPGVEVRI--VDP 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 454 MGYDALSNVPrGEICLRGKTLFSGYFKRQDLTESALVDGWFHTGDIGEWQPNGAMKIIDRKKNIFKlSQGEYVAVENLEN 533
Cdd:cd04433 185 DGGELPPGEI-GELVVRGPSVMKGYWNNPEATAAVDEDGWYRTGDLGRLDEDGYLYIVGRLKDMIK-SGGENVYPAEVEA 262
|
330 340 350
....*....|....*....|....*....|....*
gi 225428594 534 TYSRCPLITSIWVYG---NSFESFLVAVVVPDKKA 565
Cdd:cd04433 263 VLLGHPGVAEAAVVGvpdPEWGERVVAVVVLRPGA 297
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
75-517 |
5.82e-53 |
|
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: 188.93 E-value: 5.82e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 75 VWLTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEAC---NSQAIPYVPLYdslGANAVEFIINHAEVSI 151
Cdd:cd05936 23 RKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGAlkaGAVVVPLNPLY---TPRELEHILNDSGAKA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 152 AFVqeskipamltclpkctsylktIISFgkisssqkeeaEELGvscfsweEFALLGSLDCELPPkqkTDICTIMYTSGTT 231
Cdd:cd05936 100 LIV---------------------AVSF-----------TDLL-------AAGAPLGERVALTP---EDVAVLQYTSGTT 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 232 GEPKGVVLSNEAIMAEVLSTDQLLLETDkvaTEEDTYFSFLPLAHVFDQ-IMETYCIYKGSSIGFW-GADVRYLMEDIQE 309
Cdd:cd05936 138 GVPKGAMLTHRNLVANALQIKAWLEDLL---EGDDVVLAALPLFHVFGLtVALLLPLALGATIVLIpRFRPIGVLKEIRK 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 310 LKPTIFCGVPRVYERIYGgaiakissggalrkalfqyaynyklrnlekglrqdeaAPRLDRLIFdkikqgfgGRVRLLFS 389
Cdd:cd05936 215 HRVTIFPGVPTMYIALLN-------------------------------------APEFKKRDF--------SSLRLCIS 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 390 GAAPLSRHV-EEFLRVTSCSVLsQGYGLTESC-GGCLTSIVNEfSMMGTVGVPYPTIEARLesvpemgYDALSN-VPR-- 464
Cdd:cd05936 250 GGAPLPVEVaERFEELTGVPIV-EGYGLTETSpVVAVNPLDGP-RKPGSIGIPLPGTEVKI-------VDDDGEeLPPge 320
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 225428594 465 -GEICLRGKTLFSGYFKRQDLTESALVDGWFHTGDIGEWQPNGAMKIIDRKKNI 517
Cdd:cd05936 321 vGELWVRGPQVMKGYWNRPEETAEAFVDGWLRTGDIGYMDEDGYFFIVDRKKDM 374
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
74-629 |
1.40e-52 |
|
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: 190.74 E-value: 1.40e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 74 YVWLTYREAYDAALRMGSAMRS-RGVNPGDRCGIYGSNCPEWIIAMEACNSQAIPYVPLYDSLGANAVEFIINHAEVSIA 152
Cdd:cd17632 65 FETITYAELWERVGAVAAAHDPeQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 153 FVQESKIPAMLTCLPKCTSyLKTIISFG---------KISSSQKEEAEELGVSCFSWEEFALLG---SLDCELPPKQKTD 220
Cdd:cd17632 145 AVSAEHLDLAVEAVLEGGT-PPRLVVFDhrpevdahrAALESARERLAAVGIPVTTLTLIAVRGrdlPPAPLFRPEPDDD 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 221 -ICTIMYTSGTTGEPKGVVLsneaimaevlsTDQLLLE--TDKVATEEDT-----YFSFLPLAHVFDQIMETYCIYKGSS 292
Cdd:cd17632 224 pLALLIYTSGSTGTPKGAMY-----------TERLVATfwLKVSSIQDIRppasiTLNFMPMSHIAGRISLYGTLARGGT 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 293 IGFWGA-DVRYLMEDIQELKPTIFCGVPRVYEriyggaiakissggalrkALFQYAYNYKLRNLEKGLRQDEAAPRLDRL 371
Cdd:cd17632 293 AYFAAAsDMSTLFDDLALVRPTELFLVPRVCD------------------MLFQRYQAELDRRSVAGADAETLAERVKAE 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 372 IFDKIkqgFGGRVRLLFSGAAPLSRHVEEFLRVTSCSVLSQGYGLTESCGgcltSIVNefsmmGTVGVPyPTIEARLESV 451
Cdd:cd17632 355 LRERV---LGGRLLAAVCGSAPLSAEMKAFMESLLDLDLHDGYGSTEAGA----VILD-----GVIVRP-PVLDYKLVDV 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 452 PEMGYDAL-SNVPRGEICLRGKTLFSGYFKRQDLTESAL-VDGWFHTGDI-GEWQPNgAMKIIDRKKNIFKLSQGEYVAV 528
Cdd:cd17632 422 PELGYFRTdRPHPRGELLVKTDTLFPGYYKRPEVTAEVFdEDGFYRTGDVmAELGPD-RLVYVDRRNNVLKLSQGEFVTV 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 529 ENLENTYSRCPLITSIWVYGNSFESFLVAVVVPDKKALEDWAENhnvtgdfkslcenlEARKYILDELNNTGQNHQLKGF 608
Cdd:cd17632 501 ARLEAVFAASPLVRQIFVYGNSERAYLLAVVVPTQDALAGEDTA--------------RLRAALAESLQRIAREAGLQSY 566
|
570 580
....*....|....*....|.
gi 225428594 609 ERLKAVHLDPNPFDIERDLVT 629
Cdd:cd17632 567 EIPRDFLIETEPFTIANGLLS 587
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
77-518 |
5.39e-49 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 179.33 E-value: 5.39e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 77 LTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQAIPYVPLYDSLGANAVEFIINHAEVSIAFVQE 156
Cdd:PRK07656 31 LTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYILARGDAKALFVLG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 157 SKIP---AMLTCLPKctsyLKTIISFgkisssQKEEAEELGVSCFSWEEFALLGSLDCELPPKQKTDICTIMYTSGTTGE 233
Cdd:PRK07656 111 LFLGvdySATTRLPA----LEHVVIC------ETEEDDPHTEKMKTFTDFLAAGDPAERAPEVDPDDVADILFTSGTTGR 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 234 PKGVV------LSNEAIMAEVLSTdqllletdkvaTEEDTYFSFLPLAHVFdqimeTY------CIYKGSSI----GFwg 297
Cdd:PRK07656 181 PKGAMlthrqlLSNAADWAEYLGL-----------TEGDRYLAANPFFHVF-----GYkagvnaPLMRGATIlplpVF-- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 298 aDVRYLMEDIQELKPTIFCGVPRVYeriyggaiakissggalrkalfQYAYNYklrnlEKGLRQDEAAprldrlifdkik 377
Cdd:PRK07656 243 -DPDEVFRLIETERITVLPGPPTMY----------------------NSLLQH-----PDRSAEDLSS------------ 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 378 qgfggrVRLLFSGAA----PLSRHVEEFLRVtscSVLSQGYGLTESCG-GCLTSIVNEFSMM-GTVGVPYPTIEARLesV 451
Cdd:PRK07656 283 ------LRLAVTGAAsmpvALLERFESELGV---DIVLTGYGLSEASGvTTFNRLDDDRKTVaGTIGTAIAGVENKI--V 351
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 225428594 452 PEMGYDALSNVPrGEICLRGKTLFSGYFKRQDLTESAL-VDGWFHTGDIGEWQPNGAMKIIDRKKNIF 518
Cdd:PRK07656 352 NELGEEVPVGEV-GELLVRGPNVMKGYYDDPEATAAAIdADGWLHTGDLGRLDEEGYLYIVDRKKDMF 418
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
77-571 |
2.82e-43 |
|
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: 161.24 E-value: 2.82e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 77 LTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQAIPYVPLYDSLGANAVEFIINHAEVSIAFvqe 156
Cdd:cd17631 21 LTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAYILADSGAKVLF--- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 157 skipamltclpkctsylktiisfgkisssqkeeaeelgvscfsweefallgsldcelppkqkTDICTIMYTSGTTGEPKG 236
Cdd:cd17631 98 --------------------------------------------------------------DDLALLMYTSGTTGRPKG 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 237 VVLSNEAIMAEVLSTdqlLLETDkvATEEDTYFSFLPLAHVfdQIMETYCI---YKGSSI----GFwgaDVRYLMEDIQE 309
Cdd:cd17631 116 AMLTHRNLLWNAVNA---LAALD--LGPDDVLLVVAPLFHI--GGLGVFTLptlLRGGTVvilrKF---DPETVLDLIER 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 310 LKPTIFCGVPRVYEriyggaiakissggalrkalfqyaynyklrnlekGLRQDEAAPRLDRLifdkikqgfggRVRLLFS 389
Cdd:cd17631 186 HRVTSFFLVPTMIQ----------------------------------ALLQHPRFATTDLS-----------SLRAVIY 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 390 GAAPLSRHVEEFLRVTSCsVLSQGYGLTESCGG-CLTSIVNEFSMMGTVGVPYPTIEARLesVPEMGYDALSNVPrGEIC 468
Cdd:cd17631 221 GGAPMPERLLRALQARGV-KFVQGYGMTETSPGvTFLSPEDHRRKLGSAGRPVFFVEVRI--VDPDGREVPPGEV-GEIV 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 469 LRGKTLFSGYFKRQDLTESALVDGWFHTGDIGEWQPNGAMKIIDRKKNIFKlSQGEYVAVENLENTYSRCPLItsiwvyg 548
Cdd:cd17631 297 VRGPHVMAGYWNRPEATAAAFRDGWFHTGDLGRLDEDGYLYIVDRKKDMII-SGGENVYPAEVEDVLYEHPAV------- 368
|
490 500
....*....|....*....|....
gi 225428594 549 nsfesFLVAVV-VPDkkalEDWAE 571
Cdd:cd17631 369 -----AEVAVIgVPD----EKWGE 383
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
14-517 |
1.42e-41 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 159.40 E-value: 1.42e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 14 ATEERPsagpvYRCIYAENGLLEVPKGMESPWEFFSDSVERNPKNQML---GRRQiinskagpyvwlTYREAYDAALRMG 90
Cdd:PRK05605 9 AFADKP-----WLQSYAPWTPHDLDYGDTTLVDLYDNAVARFGDRPALdffGATT------------TYAELGKQVRRAA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 91 SAMRSRGVNPGDRCGIYGSNCPEWIIAMEACNSqaipyvplydsLGANAVE-------------FIINHAEVSIAFvqeS 157
Cdd:PRK05605 72 AGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLR-----------LGAVVVEhnplytahelehpFEDHGARVAIVW---D 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 158 KIPAMLTCLPKCTSyLKTIISFGKISS--------------SQKEEAEELGVSC---FSWEEF---ALLGSLDCELPPK- 216
Cdd:PRK05605 138 KVAPTVERLRRTTP-LETIVSVNMIAAmpllqrlalrlpipALRKARAALTGPApgtVPWETLvdaAIGGDGSDVSHPRp 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 217 QKTDICTIMYTSGTTGEPKGVVLSNEAIMAEVLstdQLLLETDKVATEEDTYFSFLPLAHVFDQimeTYCIYKGSSIG-- 294
Cdd:PRK05605 217 TPDDVALILYTSGTTGKPKGAQLTHRNLFANAA---QGKAWVPGLGDGPERVLAALPMFHAYGL---TLCLTLAVSIGge 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 295 ---FWGADVRYLMEDIQELKPTIFCGVPRVYERIYGGAIAK---ISSggalrkalfqyaynyklrnlekglrqdeaaprl 368
Cdd:PRK05605 291 lvlLPAPDIDLILDAMKKHPPTWLPGVPPLYEKIAEAAEERgvdLSG--------------------------------- 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 369 drlifdkikqgfggrVRLLFSGAAPLSRH-VEEFLRVTScSVLSQGYGLTESCGGCLTSIVNEFSMMGTVGVPYPTIEAR 447
Cdd:PRK05605 338 ---------------VRNAFSGAMALPVStVELWEKLTG-GLLVEGYGLTETSPIIVGNPMSDDRRPGYVGVPFPDTEVR 401
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 225428594 448 LESvPEmgyDALSNVP---RGEICLRGKTLFSGYFKRQDLTESALVDGWFHTGDIGEWQPNGAMKIIDRKKNI 517
Cdd:PRK05605 402 IVD-PE---DPDETMPdgeEGELLVRGPQVFKGYWNRPEETAKSFLDGWFRTGDVVVMEEDGFIRIVDRIKEL 470
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
62-571 |
3.19e-41 |
|
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: 157.41 E-value: 3.19e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 62 GRRQIIN-SKAGPYVWLTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEAcnsqaipyVPlydslGANAV 140
Cdd:cd12119 10 GDREIVSrTHEGEVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYA--------VP-----GMGAV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 141 -------------EFIINHAEVSIAFVQESKIPAMLTCLPKCTSYLKTIISFGKIsssqkEEAEELGVSCFSWEEFALLG 207
Cdd:cd12119 77 lhtinprlfpeqiAYIINHAEDRVVFVDRDFLPLLEAIAPRLPTVEHVVVMTDDA-----AMPEPAGVGVLAYEELLAAE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 208 SLDCELPPKQKTDICTIMYTSGTTGEPKGVVLSNEAI----MAeVLSTDQLLLEtdkvatEEDTYFSFLPLAHVFDQIME 283
Cdd:cd12119 152 SPEYDWPDFDENTAAAICYTSGTTGNPKGVVYSHRSLvlhaMA-ALLTDGLGLS------ESDVVLPVVPMFHVNAWGLP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 284 TYCIYKGSSIGFWGADVRY--LMEDIQELKPTIFCGVPRVYEriyggaiakissggalrkalfqyaynyklrnlekGLRQ 361
Cdd:cd12119 225 YAAAMVGAKLVLPGPYLDPasLAELIEREGVTFAAGVPTVWQ----------------------------------GLLD 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 362 DEAAPRLDRlifdkikqgFGGRvRLLFSGAAPLSRHVEEF----LRVTscsvlsQGYGLTESCGGCLTSIVN-------- 429
Cdd:cd12119 271 HLEANGRDL---------SSLR-RVVIGGSAVPRSLIEAFeergVRVI------HAWGMTETSPLGTVARPPsehsnlse 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 430 --EFSMMGTVGVPYPTIEARLESvPEMGYDALSNVPRGEICLRGKTLFSGYFKRQDLTESALVDGWFHTGDIGEWQPNGA 507
Cdd:cd12119 335 deQLALRAKQGRPVPGVELRIVD-DDGRELPWDGKAVGELQVRGPWVTKSYYKNDEESEALTEDGWLRTGDVATIDEDGY 413
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 225428594 508 MKIIDRKKNIFKlSQGEYVAVENLENTYSRCPLItsiwvygnsfesFLVAVV-VPDKKaledWAE 571
Cdd:cd12119 414 LTITDRSKDVIK-SGGEWISSVELENAIMAHPAV------------AEAAVIgVPHPK----WGE 461
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
77-506 |
1.94e-38 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 150.26 E-value: 1.94e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 77 LTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQAIPYVPLYDSLGANAVEFIINHAEVSIAFVQE 156
Cdd:COG0365 40 LTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITAD 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 157 ---------SKIPAMLTCLPKCTSyLKTIISFGKISSSQKEEAEelgvscFSWEEFALLGSLDCELPPKQKTDICTIMYT 227
Cdd:COG0365 120 gglrggkviDLKEKVDEALEELPS-LEHVIVVGRTGADVPMEGD------LDWDELLAAASAEFEPEPTDADDPLFILYT 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 228 SGTTGEPKGVVLSNEAIMAEVLSTDQLLLEtdkvATEEDTYFS--------------FLPLAH---VFdqimetycIYKG 290
Cdd:COG0365 193 SGTTGKPKGVVHTHGGYLVHAATTAKYVLD----LKPGDVFWCtadigwatghsyivYGPLLNgatVV--------LYEG 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 291 sSIGFWGADVryLMEDIQELKPTIFCGVPRVYeRiyggaiakissggALRKALFQYAYNYKLRNLekglrqdeaaprldr 370
Cdd:COG0365 261 -RPDFPDPGR--LWELIEKYGVTVFFTAPTAI-R-------------ALMKAGDEPLKKYDLSSL--------------- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 371 lifdkikqgfggrvRLLFSGAAPLSRHV-EEFLRVTSCSVLSqGYGLTESCGGCLTSIVNEFSMMGTVGVPYPTIEARLe 449
Cdd:COG0365 309 --------------RLLGSAGEPLNPEVwEWWYEAVGVPIVD-GWGQTETGGIFISNLPGLPVKPGSMGKPVPGYDVAV- 372
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 225428594 450 sVPEMGYDALSNVPrGEICLRGK--TLFSGYFKRQDLTESALVD---GWFHTGDIGEWQPNG 506
Cdd:COG0365 373 -VDEDGNPVPPGEE-GELVIKGPwpGMFRGYWNDPERYRETYFGrfpGWYRTGDGARRDEDG 432
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
78-568 |
2.98e-38 |
|
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: 147.05 E-value: 2.98e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 78 TYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQAIPYVPLYDSLGANAVEFIINHAEVSIAFvqes 157
Cdd:cd05934 5 TYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 158 kipamltclpkctsylktiisfgkisssqkeeaeelgvscfsweefallgsldcelppkqkTDICTIMYTSGTTGEPKGV 237
Cdd:cd05934 81 -------------------------------------------------------------VDPASILYTSGTTGPPKGV 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 238 VLSN-EAIMAEVLSTDQLlletdkVATEEDTYFSFLPLAHVFDQIMETY-CIYKGSSI---------GFWGadvrylmeD 306
Cdd:cd05934 100 VITHaNLTFAGYYSARRF------GLGEDDVYLTVLPLFHINAQAVSVLaALSVGATLvllprfsasRFWS--------D 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 307 IQELKPTIFcgvprvyeriyggaiakiSSGGALRKALfqyaynyklrnlekgLRQDEAAPRLDrlifdkikqgfgGRVRL 386
Cdd:cd05934 166 VRRYGATVT------------------NYLGAMLSYL---------------LAQPPSPDDRA------------HRLRA 200
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 387 LFSGAAPLSRHvEEFLRVTSCSVLsQGYGLTESCGgCLTSIVNEFSMMGTVGVPYPTIEARLesVPEMGYDALSNVPrGE 466
Cdd:cd05934 201 AYGAPNPPELH-EEFEERFGVRLL-EGYGMTETIV-GVIGPRDEPRRPGSIGRPAPGYEVRI--VDDDGQELPAGEP-GE 274
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 467 ICLR---GKTLFSGYFKRQDLTESALVDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSqGEYVAVENLENTYSRCPLITS 543
Cdd:cd05934 275 LVIRglrGWGFFKGYYNMPEATAEAMRNGWFHTGDLGYRDADGFFYFVDRKKDMIRRR-GENISSAEVERAILRHPAVRE 353
|
490 500
....*....|....*....|....*
gi 225428594 544 IWVYGnsfesflvavvVPDKKALED 568
Cdd:cd05934 354 AAVVA-----------VPDEVGEDE 367
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
77-573 |
1.62e-37 |
|
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: 145.13 E-value: 1.62e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 77 LTYREAYDAALRMGSAM-RSRGVNPGDRCGIYGSNCPEWIIAMEACNSQAIPYVPLYDSLGANAVEFIINHAEVSIAFvq 155
Cdd:cd05941 12 ITYADLVARAARLANRLlALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDSEPSLVL-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 156 eskipamltclpkctsylktiisfgkisssqkeeaeelgvscfsweefallgsldcelppkqktDICTIMYTSGTTGEPK 235
Cdd:cd05941 90 ----------------------------------------------------------------DPALILYTSGTTGRPK 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 236 GVVLSNEAIMAEVlstdQLLLETDKVaTEEDTYFSFLPLAHV---FDQIMETycIYKGSSIGFWGADVRYLMEDIQELKP 312
Cdd:cd05941 106 GVVLTHANLAANV----RALVDAWRW-TEDDVLLHVLPLHHVhglVNALLCP--LFAGASVEFLPKFDPKEVAISRLMPS 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 313 -TIFCGVPRVYERIYGGAIAKISSGGALRKALFqyaynyklrnlekglrqdeaaprldrlifdkikqgfgGRVRLLFSGA 391
Cdd:cd05941 179 iTVFMGVPTIYTRLLQYYEAHFTDPQFARAAAA-------------------------------------ERLRLMVSGS 221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 392 APLSRHV-EEFLRVTSCSVLSQgYGLTEScGGCLTSIVNEFSMMGTVGVPYPTIEARLesVPEMGYDALSNVPRGEICLR 470
Cdd:cd05941 222 AALPVPTlEEWEAITGHTLLER-YGMTEI-GMALSNPLDGERRPGTVGMPLPGVQARI--VDEETGEPLPRGEVGEIQVR 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 471 GKTLFSGYFKRQDLTESALV-DGWFHTGDIGEWQPNGAMKIIDRKK-NIFKlSQGEYVAVENLENTYSRCPLITSIWVYG 548
Cdd:cd05941 298 GPSVFKEYWNKPEATKEEFTdDGWFKTGDLGVVDEDGYYWILGRSSvDIIK-SGGYKVSALEIERVLLAHPGVSECAVIG 376
|
490 500 510
....*....|....*....|....*....|....*
gi 225428594 549 NSFESF---LVAVVVPDKKA-------LEDWAENH 573
Cdd:cd05941 377 VPDPDWgerVVAVVVLRAGAaalsleeLKEWAKQR 411
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
77-561 |
4.80e-37 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 145.46 E-value: 4.80e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 77 LTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQAIPYVPLYDSLGANAVEFIINHAEVSIAFVQe 156
Cdd:PRK08316 37 WTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAFLVD- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 157 skiPAMLTCLPKCTSYLKTiisfGKISSSQKEEAEELGVSCFSWEEFALLGSLDCELPPKQKTDICTIMYTSGTTGEPKG 236
Cdd:PRK08316 116 ---PALAPTAEAALALLPV----DTLILSLVLGGREAPGGWLDFADWAEAGSVAEPDVELADDDLAQILYTSGTESLPKG 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 237 VVLSNEAIMAEVLSTdqlLLETDkvATEEDTYFSFLPLAH-----VFdqiMETYCIYKGSSIGFWGADVRYLMEDIQELK 311
Cdd:PRK08316 189 AMLTHRALIAEYVSC---IVAGD--MSADDIPLHALPLYHcaqldVF---LGPYLYVGATNVILDAPDPELILRTIEAER 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 312 PTIFCGVPRVYeriyggaiakISsggALRKALFQyayNYKLRNLEKGlrqdeaaprldrlifdkikqgfggrvrllFSGA 391
Cdd:PRK08316 261 ITSFFAPPTVW----------IS---LLRHPDFD---TRDLSSLRKG-----------------------------YYGA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 392 APLSRHV-EEF------LRVTSCsvlsqgYGLTEScgGCLTSIVN---EFSMMGTVGVPYPTIEARLESvpemgyDALSN 461
Cdd:PRK08316 296 SIMPVEVlKELrerlpgLRFYNC------YGQTEI--APLATVLGpeeHLRRPGSAGRPVLNVETRVVD------DDGND 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 462 VPR---GEICLRGKTLFSGYFKRQDLTESALVDGWFHTGDIGEWQPNGAMKIIDRKKNIFKlSQGEYVAVENLENTYSRC 538
Cdd:PRK08316 362 VAPgevGEIVHRSPQLMLGYWDDPEKTAEAFRGGWFHSGDLGVMDEEGYITVVDRKKDMIK-TGGENVASREVEEALYTH 440
|
490 500
....*....|....*....|....*.
gi 225428594 539 PLITSIWVYGNSFESFL---VAVVVP 561
Cdd:PRK08316 441 PAVAEVAVIGLPDPKWIeavTAVVVP 466
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
78-573 |
1.49e-35 |
|
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: 139.51 E-value: 1.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 78 TYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEACnsqaipyvplydsLGANAVEFIINHA--EVSIAFVQ 155
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHAC-------------LLLGAEIAMLNTRltENERTNQL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 156 ESKIPAMLTCLPKCTSYLKTIISFGKISSSQkEEAEELGVScFSWEefallgsldcelppkqktDICTIMYTSGTTGEPK 235
Cdd:TIGR01923 68 EDLDVQLLLTDSLLEEKDFQADSLDRIEAAG-RYETSLSAS-FNMD------------------QIATLMFTSGTTGKPK 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 236 GVVLSNEAIMAEVLSTDQLLletdkVATEEDTYFSFLPLAHVFDQIMETYCIYKGSSIGFWGADVRyLMEDIQELKPTIF 315
Cdd:TIGR01923 128 AVPHTFRNHYASAVGSKENL-----GFTEDDNWLLSLPLYHISGLSILFRWLIEGATLRIVDKFNQ-LLEMIANERVTHI 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 316 CGVPRVYERIyggaiakissggaLRKALFQYaynyklrNLEKGLRQDEAAPrldrlifdkikqgfggrvrllfsgaAPLS 395
Cdd:TIGR01923 202 SLVPTQLNRL-------------LDEGGHNE-------NLRKILLGGSAIP-------------------------APLI 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 396 RHVEEfLRVTscsvLSQGYGLTESCGGCLTSIVNEFSMMGTVGVPYPTIEARLESVPEMGYdalsnvprGEICLRGKTLF 475
Cdd:TIGR01923 237 EEAQQ-YGLP----IYLSYGMTETCSQVTTATPEMLHARPDVGRPLAGREIKIKVDNKEGH--------GEIMVKGANLM 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 476 SGYFKRQDLTESALVDGWFHTGDIGEWQPNGAMKIIDRKKNIFkLSQGEYVAVENLENTYSRCPLITSIWV-------YG 548
Cdd:TIGR01923 304 KGYLYQGELTPAFEQQGWFNTGDIGELDGEGFLYVLGRRDDLI-ISGGENIYPEEIETVLYQHPGIQEAVVvpkpdaeWG 382
|
490 500
....*....|....*....|....*
gi 225428594 549 NSFESFLVAVVVPDKKALEDWAENH 573
Cdd:TIGR01923 383 QVPVAYIVSESDISQAKLIAYLTEK 407
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
75-571 |
3.26e-34 |
|
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: 136.66 E-value: 3.26e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 75 VWLTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPewiiAM-EAcnSQAIPY-----VPLYDSLGANAVEFIINHAE 148
Cdd:cd12118 28 RRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTP----AMyEL--HFGVPMagavlNALNTRLDAEEIAFILRHSE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 149 VSIAFVQESkipamltclpkctsylktiisfgkisssqkeeaeelgvscFSWEEFALLGSLDCE-LPPKQKTDICTIMYT 227
Cdd:cd12118 102 AKVLFVDRE----------------------------------------FEYEDLLAEGDPDFEwIPPADEWDPIALNYT 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 228 SGTTGEPKGVVLSNEAIMAEVLSTdQLLLETDKVATeedtYFSFLPLAH---------VFDQIMETYCIYKGSSIGFWGA 298
Cdd:cd12118 142 SGTTGRPKGVVYHHRGAYLNALAN-ILEWEMKQHPV----YLWTLPMFHcngwcfpwtVAAVGGTNVCLRKVDAKAIYDL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 299 dvrylmedIQELKPTIFCGVPRVYEriyggAIAKissggalrkalfqyaynyklrnlekglrqdeaAPRLDRlifdkikQ 378
Cdd:cd12118 217 --------IEKHKVTHFCGAPTVLN-----MLAN--------------------------------APPSDA-------R 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 379 GFGGRVRLLFSGAAP----LSRHVEEFLRVTscsvlsQGYGLTESCGgclTSIVNEFS-------------MMGTVGVPY 441
Cdd:cd12118 245 PLPHRVHVMTAGAPPpaavLAKMEELGFDVT------HVYGLTETYG---PATVCAWKpewdelpteerarLKARQGVRY 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 442 PTIEarlesvPEMGYDA--LSNVPR-----GEICLRGKTLFSGYFKRQDLTESALVDGWFHTGDIGEWQPNGAMKIIDRK 514
Cdd:cd12118 316 VGLE------EVDVLDPetMKPVPRdgktiGEIVFRGNIVMKGYLKNPEATAEAFRGGWFHSGDLAVIHPDGYIEIKDRS 389
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 225428594 515 KNIFkLSQGEYVAVENLENTYSRCPLItsiwvygnsfesFLVAVV-VPDKKaledWAE 571
Cdd:cd12118 390 KDII-ISGGENISSVEVEGVLYKHPAV------------LEAAVVaRPDEK----WGE 430
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
77-564 |
1.58e-31 |
|
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: 128.60 E-value: 1.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 77 LTYREAYDAALRMGSAMRsRGVNPGDRCGIYGSNCPEWIIAMEAcnSQAIPYVP--LYDSLGANAVEFIINHAEV----- 149
Cdd:cd05909 8 LTYRKLLTGAIALARKLA-KMTKEGENVGVMLPPSAGGALANFA--LALSGKVPvmLNYTAGLRELRACIKLAGIktvlt 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 150 SIAFVQESKIPAMLTCLPKCT-SYLKTIIsfGKISSSQKEEAEeLGVSCFSWEEFALLGsldceLPPKQKTDICTIMYTS 228
Cdd:cd05909 85 SKQFIEKLKLHHLFDVEYDARiVYLEDLR--AKISKADKCKAF-LAGKFPPKWLLRIFG-----VAPVQPDDPAVILFTS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 229 GTTGEPKGVVLSNEAIMAEVlstDQLLLETDkvATEEDTYFSFLPLAHVFdqimetyciykGSSIGFW-----GADV--- 300
Cdd:cd05909 157 GSEGLPKGVVLSHKNLLANV---EQITAIFD--PNPEDVVFGALPFFHSF-----------GLTGCLWlpllsGIKVvfh 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 301 ------RYLMEDIQELKPTIFCGVPrVYERIYggaiakissggaLRkalfqYAYNYKLRNLekglrqdeaaprldrlifd 374
Cdd:cd05909 221 pnpldyKKIPELIYDKKATILLGTP-TFLRGY------------AR-----AAHPEDFSSL------------------- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 375 kikqgfggrvRLLFSGAAPLSRHVEEFLRVTSCSVLSQGYGLTESCGGCLTSIVNEFSMMGTVGVPYPTIEARLESVPem 454
Cdd:cd05909 264 ----------RLVVAGAEKLKDTLRQEFQEKFGIRILEGYGTTECSPVISVNTPQSPNKEGTVGRPLPGMEVKIVSVE-- 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 455 GYDALSNVPRGEICLRGKTLFSGYFKRQDLTESALVDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSqGEYVAVENLEN- 533
Cdd:cd05909 332 THEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAFGDGWYDTGDIGKIDGEGFLTITGRLSRFAKIA-GEMVSLEAIEDi 410
|
490 500 510
....*....|....*....|....*....|..
gi 225428594 534 TYSRCPlitsiwvygnsfESFLVAVV-VPDKK 564
Cdd:cd05909 411 LSEILP------------EDNEVAVVsVPDGR 430
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
77-596 |
3.25e-31 |
|
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: 126.73 E-value: 3.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 77 LTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQAIPYVPLYDSLGANAVEFIINHAEVSIAFVQE 156
Cdd:cd05903 2 LTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 157 SkipamltclpkctsylktiisFGKISssqkeeaeelgvscfsweefallgsldcelPPKQKTDICTIMYTSGTTGEPKG 236
Cdd:cd05903 82 R---------------------FRQFD------------------------------PAAMPDAVALLLFTSGTTGEPKG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 237 VVLSNEAIMAEVLSTDQLLLetdkvATEEDTYFSFLPLAHVfdqimetyciykgssIGFWGADVRYLMEdiqelkptifc 316
Cdd:cd05903 111 VMHSHNTLSASIRQYAERLG-----LGPGDVFLVASPMAHQ---------------TGFVYGFTLPLLL----------- 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 317 GVPRVYERIYGG--AIAKISSGGALrkalFQYAYNYKLRNLEKGLrqDEAAPRLDRLifdkikqgfggrvRLLFSGAAP- 393
Cdd:cd05903 160 GAPVVLQDIWDPdkALALMREHGVT----FMMGATPFLTDLLNAV--EEAGEPLSRL-------------RTFVCGGATv 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 394 ---LSRHVEEFLRVTSCSVlsqgYGLTESCGgCLTSI--VNEFSMMGTVGVPYPTIEARLesVPEMGyDALSNVPRGEIC 468
Cdd:cd05903 221 prsLARRAAELLGAKVCSA----YGSTECPG-AVTSItpAPEDRRLYTDGRPLPGVEIKV--VDDTG-ATLAPGVEGELL 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 469 LRGKTLFSGYFKRQDLTESALVDGWFHTGDIGEWQPNGAMKIIDRKKNIFkLSQGEYVAVENLENTYSRCPLITSIWVYG 548
Cdd:cd05903 293 SRGPSVFLGYLDRPDLTADAAPEGWFRTGDLARLDEDGYLRITGRSKDII-IRGGENIPVLEVEDLLLGHPGVIEAAVVA 371
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 225428594 549 NSFESF---LVAVVVPDKKALEDWAEnhnvtgdfksLCENLE----ARKYILDEL 596
Cdd:cd05903 372 LPDERLgerACAVVVTKSGALLTFDE----------LVAYLDrqgvAKQYWPERL 416
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
75-571 |
3.58e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 128.14 E-value: 3.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 75 VWLTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEAcnsqaipyVP--------LYDSLGANAVEFIINH 146
Cdd:PRK08162 42 RRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFG--------VPmagavlntLNTRLDAASIAFMLRH 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 147 AEVSIAFVQE---SKIPAMLTCLPKctsylKTIISFGkISSSQKEEAEELGVscFSWEEFALLGSLDCEL-PPKQKTDIC 222
Cdd:PRK08162 114 GEAKVLIVDTefaEVAREALALLPG-----PKPLVID-VDDPEYPGGRFIGA--LDYEAFLASGDPDFAWtLPADEWDAI 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 223 TIMYTSGTTGEPKGVVLSNE--AIMAevLSTdqlLLETDkvATEEDTYFSFLPLAHV----FDQIMetyCIYKGSSIGFW 296
Cdd:PRK08162 186 ALNYTSGTTGNPKGVVYHHRgaYLNA--LSN---ILAWG--MPKHPVYLWTLPMFHCngwcFPWTV---AARAGTNVCLR 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 297 GADVRYLMEDIQELKPTIFCGVPRVYeriygGAIAKissggalrkalfqyaynyklrnlekglrqdeaAPrldrlifDKI 376
Cdd:PRK08162 256 KVDPKLIFDLIREHGVTHYCGAPIVL-----SALIN--------------------------------AP-------AEW 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 377 KQGFGGRVRLLFSGAAP----LSRHVEEFLRVTscsvlsQGYGLTESCGG---CLT-------SIVNEFSMMGTVGVPYP 442
Cdd:PRK08162 292 RAGIDHPVHAMVAGAAPpaavIAKMEEIGFDLT------HVYGLTETYGPatvCAWqpewdalPLDERAQLKARQGVRYP 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 443 TiearLESVPEMGYDALSNVPR-----GEICLRGKTLFSGYFKRQDLTESALVDGWFHTGDIGEWQPNGAMKIIDRKKNI 517
Cdd:PRK08162 366 L----QEGVTVLDPDTMQPVPAdgetiGEIMFRGNIVMKGYLKNPKATEEAFAGGWFHTGDLAVLHPDGYIKIKDRSKDI 441
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 225428594 518 FkLSQGEYVAVENLENTYSRCPLItsiwvygnsfesfLVAVVV--PDKKaledWAE 571
Cdd:PRK08162 442 I-ISGGENISSIEVEDVLYRHPAV-------------LVAAVVakPDPK----WGE 479
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
77-519 |
7.70e-31 |
|
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: 126.97 E-value: 7.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 77 LTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQAIPYVPLYDSLGANAVEFIINHAEVSIAFVQE 156
Cdd:cd05904 33 LTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFTTA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 157 SKipamltcLPKCTSYLKTIISFGkisssqkeeaEELGVSCFSWEEFALLGSLDCELPPKQKTDICTIMYTSGTTGEPKG 236
Cdd:cd05904 113 EL-------AEKLASLALPVVLLD----------SAEFDSLSFSDLLFEADEAEPPVVVIKQDDVAALLYSSGTTGRSKG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 237 VVLSNEAIMAEVLSTDQLlleTDKVATEEDTYFSFLPLAHVFDQIMETYCIYK-GSSI----GFwgaDVRYLMEDIQELK 311
Cdd:cd05904 176 VMLTHRNLIAMVAQFVAG---EGSNSDSEDVFLCVLPMFHIYGLSSFALGLLRlGATVvvmpRF---DLEELLAAIERYK 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 312 PTIFCGVPRVYEriyggAIAKISSGGalrkalfqyayNYKLRNLEKglrqdeaaprldrlifdkikqgfggrvrlLFSGA 391
Cdd:cd05904 250 VTHLPVVPPIVL-----ALVKSPIVD-----------KYDLSSLRQ-----------------------------IMSGA 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 392 APLSRHVEE-FLRVTSCSVLSQGYGLTESCGGCLTSIVNEFSMM--GTVGVPYPTIEARLESvPEMGyDALSNVPRGEIC 468
Cdd:cd05904 285 APLGKELIEaFRAKFPNVDLGQGYGMTESTGVVAMCFAPEKDRAkyGSVGRLVPNVEAKIVD-PETG-ESLPPNQTGELW 362
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 225428594 469 LRGKTLFSGYFKRQDLTESALV-DGWFHTGDIGEWQPNGAMKIIDRKKNIFK 519
Cdd:cd05904 363 IRGPSIMKGYLNNPEATAATIDkEGWLHTGDLCYIDEDGYLFIVDRLKELIK 414
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
72-600 |
5.12e-30 |
|
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: 124.35 E-value: 5.12e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 72 GPYVWLTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQAIPYVPLYDSLGANAVEFIINHAEVSI 151
Cdd:cd05926 10 GSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 152 AFVQESKIPAMLTCLPKCTSYLKTIiSFGKISSSQKEEAEELGVSCFsweefalLGSLDCELPPKQKTDICTIMYTSGTT 231
Cdd:cd05926 90 VLTPKGELGPASRAASKLGLAILEL-ALDVGVLIRAPSAESLSNLLA-------DKKNAKSEGVPLPDDLALILHTSGTT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 232 GEPKGVVLSNEAIMAEVL---STDQLlletdkvaTEEDTYFSFLPLAHVFDQI---METycIYKGSSI---------GFW 296
Cdd:cd05926 162 GRPKGVPLTHRNLAASATnitNTYKL--------TPDDRTLVVMPLFHVHGLVaslLST--LAAGGSVvlpprfsasTFW 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 297 GadvrylmeDIQELKPTIFCGVPrvyeriyggAIAKIssggalrkalfqyaynykLRNLEKGLRQDEAAPrldrlifdki 376
Cdd:cd05926 232 P--------DVRDYNATWYTAVP---------TIHQI------------------LLNRPEPNPESPPPK---------- 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 377 kqgfggrVRLLFSGAAPLS-RHVEEFLRVTSCSVLsQGYGLTESCGGcLTSivNEFSMM----GTVGVPYPTiEARLesV 451
Cdd:cd05926 267 -------LRFIRSCSASLPpAVLEALEATFGAPVL-EAYGMTEAAHQ-MTS--NPLPPGprkpGSVGKPVGV-EVRI--L 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 452 PEMGyDALSNVPRGEICLRGKTLFSGYFKRQDLT-ESALVDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSqGEYVAVEN 530
Cdd:cd05926 333 DEDG-EILPPGVVGEICLRGPNVTRGYLNNPEANaEAAFKDGWFRTGDLGYLDADGYLFLTGRIKELINRG-GEKISPLE 410
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 531 LENTYSRCPLITSIWVYGNSFESF---LVAVVVP------DKKALEDWAENHnvTGDFKslcenLEARKYILDEL--NNT 599
Cdd:cd05926 411 VDGVLLSHPAVLEAVAFGVPDEKYgeeVAAAVVLregasvTEEELRAFCRKH--LAAFK-----VPKKVYFVDELpkTAT 483
|
.
gi 225428594 600 G 600
Cdd:cd05926 484 G 484
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
77-569 |
6.61e-29 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 121.42 E-value: 6.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 77 LTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQAIPYVPLYDSLGANAVEFIINHAEVSIAFVQE 156
Cdd:PRK07786 43 TTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVVTEA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 157 SKIPaMLTCLPKCTSYLKTIISFGKISSSQKEEAEELgvscfsweefallgsLDCELPPKQKTDI-----CTIMYTSGTT 231
Cdd:PRK07786 123 ALAP-VATAVRDIVPLLSTVVVAGGSSDDSVLGYEDL---------------LAEAGPAHAPVDIpndspALIMYTSGTT 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 232 GEPKGVVLSNEAIMAEVLStdqlLLETDKVATEEDTYFSFLPLAHV--------FDQIMETYCIYKgssigfWGA-DVRY 302
Cdd:PRK07786 187 GRPKGAVLTHANLTGQAMT----CLRTNGADINSDVGFVGVPLFHIagigsmlpGLLLGAPTVIYP------LGAfDPGQ 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 303 LMEDIQELKPT-IFCgVPRVYERIYGGAIAKissggalrkalfqyAYNYKLRNLEKGlrqdeAAPRLDRLIfDKIKQGFG 381
Cdd:PRK07786 257 LLDVLEAEKVTgIFL-VPAQWQAVCAEQQAR--------------PRDLALRVLSWG-----AAPASDTLL-RQMAATFP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 382 GRVRLLFSGAAPLSRhveeflrVTsCSVLSQgygltescggcltsivNEFSMMGTVGVPYPTIEARLESvpemgyDALSN 461
Cdd:PRK07786 316 EAQILAAFGQTEMSP-------VT-CMLLGE----------------DAIRKLGSVGKVIPTVAARVVD------ENMND 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 462 VPRG---EICLRGKTLFSGYFKRQDLTESALVDGWFHTGDIGEWQPNGAMKIIDRKKNIFkLSQGEYVAVENLENTYSRC 538
Cdd:PRK07786 366 VPVGevgEIVYRAPTLMSGYWNNPEATAEAFAGGWFHSGDLVRQDEEGYVWVVDRKKDMI-ISGGENIYCAEVENVLASH 444
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 225428594 539 PLITSIWVYGNSFESF---LVAVVVPDK-------KALEDW 569
Cdd:PRK07786 445 PDIVEVAVIGRADEKWgevPVAVAAVRNddaaltlEDLAEF 485
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
77-517 |
3.88e-28 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 119.37 E-value: 3.88e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 77 LTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEA---CNSQAIPYVPLYDSlgaNAVEFIINHAEVSIAF 153
Cdd:PRK06710 50 ITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGtllAGGIVVQTNPLYTE---RELEYQLHDSGAKVIL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 154 VQESKIPAMLTClpKCTSYLKTII--------SFGK--ISSSQKEEAEELGVSCFSWEEFALLGSLD------CELPPKQ 217
Cdd:PRK06710 127 CLDLVFPRVTNV--QSATKIEHVIvtriadflPFPKnlLYPFVQKKQSNLVVKVSESETIHLWNSVEkevntgVEVPCDP 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 218 KTDICTIMYTSGTTGEPKGVVLSNEAIMAEVLSTDQLLLETDKvatEEDTYFSFLPLAHVFDQ--IMETYCIYKGSSIGF 295
Cdd:PRK06710 205 ENDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYNCKE---GEEVVLGVLPFFHVYGMtaVMNLSIMQGYKMVLI 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 296 WGADVRYLMEDIQELKPTIFCGVPRVYeriyggaIAKISSggalrkalfqyaynyklrnlekglrqdeaaPRLDRLIFDK 375
Cdd:PRK06710 282 PKFDMKMVFEAIKKHKVTLFPGAPTIY-------IALLNS------------------------------PLLKEYDISS 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 376 IkqgfggrvRLLFSGAAPLSRHVEEFLRVTSCSVLSQGYGLTESCGGCLTSIVNEFSMMGTVGVPYPTIEARLESVpEMG 455
Cdd:PRK06710 325 I--------RACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSPVTHSNFLWEKRVPGSIGVPWPDTEAMIMSL-ETG 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 225428594 456 yDALSNVPRGEICLRGKTLFSGYFKRQDLTESALVDGWFHTGDIGEWQPNGAMKIIDRKKNI 517
Cdd:PRK06710 396 -EALPPGEIGEIVVKGPQIMKGYWNKPEETAAVLQDGWLHTGDVGYMDEDGFFYVKDRKKDM 456
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
77-548 |
6.94e-28 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 117.65 E-value: 6.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 77 LTYREAYDAALRMGSAMRSR-GVNPGDRCGIYGSNCPEWIIAMEACNSQAIPYVPLYDSLGANAVEFIINHAEVSIAFVQ 155
Cdd:PRK06839 28 MTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTTVLFVE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 156 ESKIPAMLtcLPKCTSYLKTIISFGKISSSqkEEAEELGvscfsweefallgsldceLPPKQKTDICTIMYTSGTTGEPK 235
Cdd:PRK06839 108 KTFQNMAL--SMQKVSYVQRVISITSLKEI--EDRKIDN------------------FVEKNESASFIICYTSGTTGKPK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 236 GVVLSNEAIMAEVLSTdqlLLETDkvATEEDTYFSFLPLAHVfdqimetyciykgSSIGF-----WGADVRYLMED---- 306
Cdd:PRK06839 166 GAVLTQENMFWNALNN---TFAID--LTMHDRSIVLLPLFHI-------------GGIGLfafptLFAGGVIIVPRkfep 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 307 ------IQELKPTIFCGVPRVYEriyggaiakissggALRKALfqyaynyklrnlekglrqDEAAPRLDRlifdkikqgf 380
Cdd:PRK06839 228 tkalsmIEKHKVTVVMGVPTIHQ--------------ALINCS------------------KFETTNLQS---------- 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 381 ggrVRLLFSGAAP----LSRHVEE--FLrvtscsvLSQGYGLTESCGGCLTSIVNEFSM-MGTVGVPYPTIEARLESvpe 453
Cdd:PRK06839 266 ---VRWFYNGGAPcpeeLMREFIDrgFL-------FGQGFGMTETSPTVFMLSEEDARRkVGSIGKPVLFCDYELID--- 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 454 mgyDALSNVPRG---EICLRGKTLFSGYFKRQDLTESALVDGWFHTGDIGEWQPNGAMKIIDRKKNIFkLSQGEYVAVEN 530
Cdd:PRK06839 333 ---ENKNKVEVGevgELLIRGPNVMKEYWNRPDATEETIQDGWLCTGDLARVDEDGFVYIVGRKKEMI-ISGGENIYPLE 408
|
490
....*....|....*...
gi 225428594 531 LENTYSRCPLITSIWVYG 548
Cdd:PRK06839 409 VEQVINKLSDVYEVAVVG 426
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
46-568 |
8.54e-28 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 118.34 E-value: 8.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 46 EFFSDSVERNPknqmlGRRQIINSKAGpyVWLTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQA 125
Cdd:PRK12583 22 DAFDATVARFP-----DREALVVRHQA--LRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 126 IPYVPLYDSLGANAVEFIINHAEVS-------------IAFVQE------SKIPAMLTC--LPKctsyLKTIISFGKISS 184
Cdd:PRK12583 95 AILVNINPAYRASELEYALGQSGVRwvicadafktsdyHAMLQEllpglaEGQPGALACerLPE----LRGVVSLAPAPP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 185 S-----QKEEAEELGVScfSWEEFALLGSLDCElppkqktDICTIMYTSGTTGEPKGVVLS------NEAIMAEVLSTdq 253
Cdd:PRK12583 171 PgflawHELQARGETVS--REALAERQASLDRD-------DPINIQYTSGTTGFPKGATLShhnilnNGYFVAESLGL-- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 254 llletdkvaTEEDTYFSFLPLAHVFDQIMETY-CIYKGSSIGFWGA--DVRYLMEDIQELKPTIFCGVPRVYeriyggaI 330
Cdd:PRK12583 240 ---------TEHDRLCVPVPLYHCFGMVLANLgCMTVGACLVYPNEafDPLATLQAVEEERCTALYGVPTMF-------I 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 331 AKISSGgalrkalfQYAyNYKLRNLEKGLRQDEAAPRldrlifdkikqgfggrvrllfsgaAPLSRHVEEFlrvtSCSVL 410
Cdd:PRK12583 304 AELDHP--------QRG-NFDLSSLRTGIMAGAPCPI------------------------EVMRRVMDEM----HMAEV 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 411 SQGYGLTEScggcltsivnefSMMGTVGVPYPTIEARLESV----P--EMGY-DALSN-VPRGEI---CLRGKTLFSGYF 479
Cdd:PRK12583 347 QIAYGMTET------------SPVSLQTTAADDLERRVETVgrtqPhlEVKVvDPDGAtVPRGEIgelCTRGYSVMKGYW 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 480 KRQDLT-ESALVDGWFHTGDIGEWQPNGAMKIIDRKKNIFkLSQGEYVAVENLENTYSRCPLITSIWVYGNSFESF---L 555
Cdd:PRK12583 415 NNPEATaESIDEDGWMHTGDLATMDEQGYVRIVGRSKDMI-IRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYgeeI 493
|
570
....*....|....*
gi 225428594 556 VAVVV--PDKKALED 568
Cdd:PRK12583 494 VAWVRlhPGHAASEE 508
|
|
| PTZ00297 |
PTZ00297 |
pantothenate kinase; Provisional |
27-657 |
1.15e-27 |
|
pantothenate kinase; Provisional
Pssm-ID: 140318 [Multi-domain] Cd Length: 1452 Bit Score: 119.57 E-value: 1.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 27 CIYAENGLLEVPKGMESPWEFFSDSVERNPKNQMLGRrqiiNSKAGPYVWLTYREAYDAALRMGSAMRSRGVNPGDRCGI 106
Cdd:PTZ00297 412 FALNLPREYNPLAGVRSLGEMWERSVTRHSTFRCLGQ----TSESGESEWLTYGTVDARARELGSGLLALGVRPGDVIGV 487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 107 YGSNCPEWIIAMEACNSQAIPYVPLYDSlgANAVEFIINHAEVSIAFVQESKIPAMLTCLpkcTSYLKTIISfgkISSSQ 186
Cdd:PTZ00297 488 DCEASRNIVILEVACALYGFTTLPLVGK--GSTMRTLIDEHKIKVVFADRNSVAAILTCR---SRKLETVVY---THSFY 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 187 KEE----AEELGVSCFSWEEFALLGSLDCELPPKQKTDICTIMYTSGTTGEPKGvvlSNEAIM----AEVLSTDQLLLET 258
Cdd:PTZ00297 560 DEDdhavARDLNITLIPYEFVEQKGRLCPVPLKEHVTTDTVFTYVVDNTTSASG---DGLAVVrvthADVLRDISTLVMT 636
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 259 DKVAT--EEDTYFSFLPLAHVFDQIMETYCIYKGSSIGfwGADVRYLMEDIQELKPTIFCGVPRVYEriyggaiakiSSG 336
Cdd:PTZ00297 637 GVLPSsfKKHLMVHFTPFAMLFNRVFVLGLFAHGSAVA--TVDAAHLQRAFVKFQPTILVAAPSLFS----------TSR 704
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 337 GALRKA----------LFQYAYNYKLRnLEKGLRQDEAAPRLdrLIFDKIKQGFGGRVRLLfsgaaplsrhveeflrVTS 406
Cdd:PTZ00297 705 LQLSRAnerysavyswLFERAFQLRSR-LINIHRRDSSLLRF--IFFRATQELLGGCVEKI----------------VLC 765
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 407 CSVLSQGYGLTESCGGCLTSIVNEFSMMGTVGV------PYPTIEARLESVPEM----GYDALSNVPRGEiclrgktlfs 476
Cdd:PTZ00297 766 VSEESTSFSLLEHISVCYVPCLREVFFLPSEGVfcvdgtPAPSLQVDLEPFDEPsdgaGIGQLVLAKKGE---------- 835
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 477 gyfKRQDLTESAlvdgwfhtgdigEWQPNGAMKIIDRKKNIFKLSQGEYVAVENLENTYSRCPLITSIWVYGNSFESfLV 556
Cdd:PTZ00297 836 ---PRRTLPIAA------------QWKRDRTLRLLGPPLGILLPVAYEYVIAAELERIFSQSRYVNDIFLYADPSRP-II 899
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 557 AVVVPDKKALE-DWAENHNV-TGDFKSLCENLE-----ARKYILDELNNTGQNHQLKGFERLKAVHLDPNPFDIERDLVT 629
Cdd:PTZ00297 900 AIVSPNRDTVEfEWRQSHCMgEGGGPARQLGWTelvayASSLLTADFACIAKENGLHPSNVPEYVHLHPHAFKDHSTFLT 979
|
650 660
....*....|....*....|....*...
gi 225428594 630 PTFKLKRPQLLKYYKDIIDRLYSEAKGT 657
Cdd:PTZ00297 980 PYGKIRRDAVHSYFSSVIERFYSDVETT 1007
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
77-571 |
6.88e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 115.08 E-value: 6.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 77 LTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQAIPYVPLY--DSLGANAveFIINHAEVSIAFV 154
Cdd:PRK06188 38 LTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHplGSLDDHA--YVLEDAGISTLIV 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 155 QESKIPA-MLTCLPKCTSyLKTIISFGKIsssqkEEAEELgvscfsWEEFALLGSLDCElPPKQKTDICTIMYTSGTTGE 233
Cdd:PRK06188 116 DPAPFVErALALLARVPS-LKHVLTLGPV-----PDGVDL------LAAAAKFGPAPLV-AAALPPDIAGLAYTGGTTGK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 234 PKGVVLSNEAI--MAEVLSTDQLLletdkvaTEEDTYFSFLPLAHV---FdqIMETycIYKGSSI----GFWGADVrylM 304
Cdd:PRK06188 183 PKGVMGTHRSIatMAQIQLAEWEW-------PADPRFLMCTPLSHAggaF--FLPT--LLRGGTVivlaKFDPAEV---L 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 305 EDIQELKPTIFCGVPRVyerIYggaiaKISSGGALRKAlfqyaynyKLRNLEkglrqdeaaprldrlifdkikqgfggrv 384
Cdd:PRK06188 249 RAIEEQRITATFLVPTM---IY-----ALLDHPDLRTR--------DLSSLE---------------------------- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 385 rLLFSGAAPLS--RHVEEFLRVTscSVLSQGYGLTEsCGGCLTSIVNEFSM------MGTVGVPYPTIEARLESvpemgy 456
Cdd:PRK06188 285 -TVYYGASPMSpvRLAEAIERFG--PIFAQYYGQTE-APMVITYLRKRDHDpddpkrLTSCGRPTPGLRVALLD------ 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 457 DALSNVPR---GEICLRGKTLFSGYFKRQDLTESALVDGWFHTGDIGEWQPNGAMKIIDRKKNIFkLSQGEYVAVENLEN 533
Cdd:PRK06188 355 EDGREVAQgevGEICVRGPLVMDGYWNRPEETAEAFRDGWLHTGDVAREDEDGFYYIVDRKKDMI-VTGGFNVFPREVED 433
|
490 500 510
....*....|....*....|....*....|....*....
gi 225428594 534 TYSRCPLITSiwvygnsfesflVAVV-VPDKKaledWAE 571
Cdd:PRK06188 434 VLAEHPAVAQ------------VAVIgVPDEK----WGE 456
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
77-607 |
1.00e-26 |
|
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: 113.21 E-value: 1.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 77 LTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQAIPYVPLYDSLGANAVEFIINHAEVsiafvqe 156
Cdd:cd05912 2 YTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDV------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 157 skipamltclpkctsylktiisfgkisssqkeeaeelgvscfsweefallgsldcelppkQKTDICTIMYTSGTTGEPKG 236
Cdd:cd05912 75 ------------------------------------------------------------KLDDIATIMYTSGTTGKPKG 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 237 VVLSNEAIMAEVLSTdQLLLEtdkvATEEDTYFSFLPLAHV--FDQIMETycIYKGSSIGFWGA-DVRYLMEDIQELKPT 313
Cdd:cd05912 95 VQQTFGNHWWSAIGS-ALNLG----LTEDDNWLCALPLFHIsgLSILMRS--VIYGMTVYLVDKfDAEQVLHLINSGKVT 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 314 IFCGVPRVYERIyggaiakissggaLRKALFQYAYNyklrnlekglrqdeaaprldrlifdkikqgfggrVRLLFSGAAP 393
Cdd:cd05912 168 IISVVPTMLQRL-------------LEILGEGYPNN----------------------------------LRCILLGGGP 200
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 394 LSRHVEEFLRVTSCSVLsQGYGLTESCGGCLTsIVNEFSM--MGTVGVPYPTIEARLE--SVPEMGYdalsnvprGEICL 469
Cdd:cd05912 201 APKPLLEQCKEKGIPVY-QSYGMTETCSQIVT-LSPEDALnkIGSAGKPLFPVELKIEddGQPPYEV--------GEILL 270
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 470 RGKTLFSGYFKRQDLTESALVDGWFHTGDIGEWQPNGAMKIIDRKKNIFkLSQGEYVAVENLENTYSRCPLITSIWVYGN 549
Cdd:cd05912 271 KGPNVTKGYLNRPDATEESFENGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIEEVLLSHPAIKEAGVVGI 349
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 550 SFESF---LVAVVVPDKKALEDWAENHnvtgdfksLCENLEARK-----YILDEL--NNTG--QNHQLKG 607
Cdd:cd05912 350 PDDKWgqvPVAFVVSERPISEEELIAY--------CSEKLAKYKvpkkiYFVDELprTASGklLRHELKQ 411
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
224-514 |
5.61e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 111.62 E-value: 5.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 224 IMYTSGTTGEPKGVVLSNEAIMAEVlstdqllletDKVA-----TEEDTYFSFLPLAHVFDQIMETY-CIYKGSSIGFWG 297
Cdd:PRK07787 133 IVYTSGTTGPPKGVVLSRRAIAADL----------DALAeawqwTADDVLVHGLPLFHVHGLVLGVLgPLRIGNRFVHTG 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 298 --ADVRYLMEdiQELKPTIFCGVPRVYERIyggaIAKISSGGALRKAlfqyaynyklrnlekglrqdeaaprldrlifdk 375
Cdd:PRK07787 203 rpTPEAYAQA--LSEGGTLYFGVPTVWSRI----AADPEAARALRGA--------------------------------- 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 376 ikqgfggrvRLLFSGAAPLSRHVEEFLRVTSCSVLSQGYGLTESCGGCLTSIVNEfSMMGTVGVPYPTIEARL--ESVPE 453
Cdd:PRK07787 244 ---------RLLVSGSAALPVPVFDRLAALTGHRPVERYGMTETLITLSTRADGE-RRPGWVGLPLAGVETRLvdEDGGP 313
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 225428594 454 MGYDALSnvpRGEICLRGKTLFSGYFKRQDLTESALV-DGWFHTGDIGEWQPNGAMKIIDRK 514
Cdd:PRK07787 314 VPHDGET---VGELQVRGPTLFDGYLNRPDATAAAFTaDGWFRTGDVAVVDPDGMHRIVGRE 372
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
77-606 |
2.54e-25 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 110.05 E-value: 2.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 77 LTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQAIPYVPLYDSLGANAVEFIINHAEVSIAFVQE 156
Cdd:PRK03640 28 VTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKCLITDD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 157 SKIPAMltclpkctsYLKTIISFGKISSSQKEEAEELgvscfswEEFALlgsldcelppkqkTDICTIMYTSGTTGEPKG 236
Cdd:PRK03640 108 DFEAKL---------IPGISVKFAELMNGPKEEAEIQ-------EEFDL-------------DEVATIMYTSGTTGKPKG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 237 VVLSNEA-IMAEVLSTDQLLLetdkvaTEEDTYFSFLPLAHV--FDQIMETyCIYkGSSI----GFwgaDVRYLMEDIQE 309
Cdd:PRK03640 159 VIQTYGNhWWSAVGSALNLGL------TEDDCWLAAVPIFHIsgLSILMRS-VIY-GMRVvlveKF---DAEKINKLLQT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 310 LKPTIFCGVPRVYERIyggaIAKISSGGalrkalfqyaYNYKLRNLekglrqdeaaprldrlifdkikqgfggrvrLLFS 389
Cdd:PRK03640 228 GGVTIISVVSTMLQRL----LERLGEGT----------YPSSFRCM------------------------------LLGG 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 390 GAAPLS-------RHVEEFlrvtscsvlsQGYGLTESCggclTSIVN---EFSM--MGTVGVPYPTIEARLESvpemgyD 457
Cdd:PRK03640 264 GPAPKPlleqckeKGIPVY----------QSYGMTETA----SQIVTlspEDALtkLGSAGKPLFPCELKIEK------D 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 458 ALSNVPR--GEICLRGKTLFSGYFKRQDLTESALVDGWFHTGDIGEWQPNGAMKIIDRKKNIFkLSQGEYVAVENLENTY 535
Cdd:PRK03640 324 GVVVPPFeeGEIVVKGPNVTKGYLNREDATRETFQDGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIEEVL 402
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 536 SRCPLITSIWVYGNSFE---SFLVAVVVPDKKALEDwaenhnvtgDFKSLC-ENLE-----ARKYILDELNNTG----QN 602
Cdd:PRK03640 403 LSHPGVAEAGVVGVPDDkwgQVPVAFVVKSGEVTEE---------ELRHFCeEKLAkykvpKRFYFVEELPRNAsgklLR 473
|
....
gi 225428594 603 HQLK 606
Cdd:PRK03640 474 HELK 477
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
78-506 |
3.37e-25 |
|
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: 108.51 E-value: 3.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 78 TYREAYDAALRMGSAMRSR-GVNPGDRCGIYGSNCPEWIIAMEACNSQAIPYVPLYDSLGANAVEFIINHAEVSIAFVQE 156
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 157 SKIPAMLTCLPkctsylktiisfgkisssqkeeaeelGVSCFSWEEFALLGSLDCELPPKQK---TDICTIMYTSGTTGE 233
Cdd:TIGR01733 81 ALASRLAGLVL--------------------------PVILLDPLELAALDDAPAPPPPDAPsgpDDLAYVIYTSGSTGR 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 234 PKGVVLSNEAIMAEVLSTDQLLletdkVATEEDTYFSFLPLAhvFDQIME----------TYCIYKGSSIGFWGADVRYL 303
Cdd:TIGR01733 135 PKGVVVTHRSLVNLLAWLARRY-----GLDPDDRVLQFASLS--FDASVEeifgallagaTLVVPPEDEERDDAALLAAL 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 304 MEdiqELKPTIFCGVPRVYERIyggAIAKISSGGALRkalfqyaynyklrnlekglrqdeaaprldrlifdkikqgfggr 383
Cdd:TIGR01733 208 IA---EHPVTVLNLTPSLLALL---AAALPPALASLR------------------------------------------- 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 384 vRLLFSGAAPLSRHVEEFLRVTSCSVLSQGYGLTEscgGCLTSIVNEFSMMGT-------VGVPYPTIEARLESvpemgy 456
Cdd:TIGR01733 239 -LVILGGEALTPALVDRWRARGPGARLINLYGPTE---TTVWSTATLVDPDDAprespvpIGRPLANTRLYVLD------ 308
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 225428594 457 DALSNVPR---GEICLRGKTLFSGYFKRQDLTESALVDGWF---------HTGDIGEWQPNG 506
Cdd:TIGR01733 309 DDLRPVPVgvvGELYIGGPGVARGYLNRPELTAERFVPDPFaggdgarlyRTGDLVRYLPDG 370
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
66-548 |
6.86e-25 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 109.00 E-value: 6.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 66 IINSKAGPYVWLTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQAIPYVPLYDSLGANAVEFIIN 145
Cdd:PRK08008 27 IFESSGGVVRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 146 HAEVSIAFVQESKIPAMLTCLPKCTSYLKTIIsfgkISSSQKEEAEelGVSCFSWEEFALLGSLdCELPPKQKTDICTIM 225
Cdd:PRK08008 107 NSQASLLVTSAQFYPMYRQIQQEDATPLRHIC----LTRVALPADD--GVSSFTQLKAQQPATL-CYAPPLSTDDTAEIL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 226 YTSGTTGEPKGVVLSNEAIM-AEVLSTDQLLLetdkvaTEEDTYFSFLPLAHVFDQI---METYC-------IYKGSSIG 294
Cdd:PRK08008 180 FTSGTTSRPKGVVITHYNLRfAGYYSAWQCAL------RDDDVYLTVMPAFHIDCQCtaaMAAFSagatfvlLEKYSARA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 295 FWGadvrylmeDIQELKPTIFCGVPRVyeriyggaiakissggaLRKALFQYAynyklrnlekglRQDEAAPRLDRLIF- 373
Cdd:PRK08008 254 FWG--------QVCKYRATITECIPMM-----------------IRTLMVQPP------------SANDRQHCLREVMFy 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 374 ----DKIKQGFGGR--VRLLFSgaaplsrhveeflrvtscsvlsqgYGLTESCGGCLTSivnefsmmgtvgvpYPTIEAR 447
Cdd:PRK08008 297 lnlsDQEKDAFEERfgVRLLTS------------------------YGMTETIVGIIGD--------------RPGDKRR 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 448 LESV--PEMGYDA---------LSNVPRGEICLRG---KTLFSGYFKRQDLTESAL-VDGWFHTGDIGEWQPNGAMKIID 512
Cdd:PRK08008 339 WPSIgrPGFCYEAeirddhnrpLPAGEIGEICIKGvpgKTIFKEYYLDPKATAKVLeADGWLHTGDTGYVDEEGFFYFVD 418
|
490 500 510
....*....|....*....|....*....|....*.
gi 225428594 513 RKKNIFKLSqGEYVAVENLENTYSRCPLITSIWVYG 548
Cdd:PRK08008 419 RRCNMIKRG-GENVSCVELENIIATHPKIQDIVVVG 453
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
77-515 |
1.25e-24 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 108.04 E-value: 1.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 77 LTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQAIPYVPLYDSLGANAVEFIINHAEvsiafvqe 156
Cdd:PRK07514 29 YTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAE-------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 157 skiPAMLTCLPKCTSYLKTIisfgkisssqkeeAEELGVSCF---------SWEEFALLGSLDCELPPKQKTDICTIMYT 227
Cdd:PRK07514 101 ---PALVVCDPANFAWLSKI-------------AAAAGAPHVetldadgtgSLLEAAAAAPDDFETVPRGADDLAAILYT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 228 SGTTGEPKGVVLS--NEAIMAEVLstdqllletdKVA---TEEDTYFSFLPLAHVFDQIMETYCI-YKGSSIgFWGAdvR 301
Cdd:PRK07514 165 SGTTGRSKGAMLShgNLLSNALTL----------VDYwrfTPDDVLIHALPIFHTHGLFVATNVAlLAGASM-IFLP--K 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 302 YLMEDIQELKP--TIFCGVPRVYERiyggaiakissggalrkalfqyaynyklrnlekgLRQDeaaPRLDRLIfdkikqg 379
Cdd:PRK07514 232 FDPDAVLALMPraTVMMGVPTFYTR----------------------------------LLQE---PRLTREA------- 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 380 fGGRVRLLFSGAAPL--SRHVEeFLRVTSCSVLSQgYGLTEScgGCLTSivNEFS---MMGTVGVPYPTIEARLESvPEM 454
Cdd:PRK07514 268 -AAHMRLFISGSAPLlaETHRE-FQERTGHAILER-YGMTET--NMNTS--NPYDgerRAGTVGFPLPGVSLRVTD-PET 339
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 225428594 455 GYDalsnVPRGEIC---LRGKTLFSGYFKRQDLTESAL-VDGWFHTGDIGEWQPNGAMKIIDRKK 515
Cdd:PRK07514 340 GAE----LPPGEIGmieVKGPNVFKGYWRMPEKTAEEFrADGFFITGDLGKIDERGYVHIVGRGK 400
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
59-567 |
1.54e-24 |
|
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: 108.00 E-value: 1.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 59 QMLGRRQIINSKAGpyVWLTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQAIPYVPLYDSLGAN 138
Cdd:cd17642 29 SVPGTIAFTDAHTG--VNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNER 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 139 AVEFIINHAEVSIAFVQESKIPAMLTCLPKCTsYLKTIISFGKISSSQKEEAEE----------LGVSCFSWEEFallgs 208
Cdd:cd17642 107 ELDHSLNISKPTIVFCSKKGLQKVLNVQKKLK-IIKTIIILDSKEDYKGYQCLYtfitqnlppgFNEYDFKPPSF----- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 209 ldcelppKQKTDICTIMYTSGTTGEPKGVVLSNEAIMAEVLSTDQLLLETDkvATEEDTYFSFLPLAHVFDqiMETyciy 288
Cdd:cd17642 181 -------DRDEQVALIMNSSGSTGLPKGVQLTHKNIVARFSHARDPIFGNQ--IIPDTAILTVIPFHHGFG--MFT---- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 289 kgsSIGFWGADVRYLMediqelkptifcgVPRVYERIYGGAIAKISSGGA-LRKALFQYaynyklrnLEKglrqdeaAPR 367
Cdd:cd17642 246 ---TLGYLICGFRVVL-------------MYKFEEELFLRSLQDYKVQSAlLVPTLFAF--------FAK-------STL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 368 LDRLIFDKIKQgfggrvrlLFSGAAPLSRHVEEFL-RVTSCSVLSQGYGLTESCGGCLtsIVNE-FSMMGTVGVPYPTIE 445
Cdd:cd17642 295 VDKYDLSNLHE--------IASGGAPLSKEVGEAVaKRFKLPGIRQGYGLTETTSAIL--ITPEgDDKPGAVGKVVPFFY 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 446 ARLESvPEMGyDALSNVPRGEICLRGKTLFSGYFKRQDLTESALV-DGWFHTGDIGEWQPNGAMKIIDRKKNIFKLsQGE 524
Cdd:cd17642 365 AKVVD-LDTG-KTLGPNERGELCVKGPMIMKGYVNNPEATKALIDkDGWLHSGDIAYYDEDGHFFIVDRLKSLIKY-KGY 441
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 225428594 525 YVAVENLENTYSRCPLITSIWVYGnsfesflvavvVPDKKALE 567
Cdd:cd17642 442 QVPPAELESILLQHPKIFDAGVAG-----------IPDEDAGE 473
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
220-568 |
5.55e-24 |
|
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: 103.18 E-value: 5.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 220 DICTIMYTSGTTGEPKGVVLSNEAIMAEVLSTDQLLletdkVATEEDTYFSFLPLAHVfdqimetyciykgSSIGFWgad 299
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRL-----GFGGGDSWLLSLPLYHV-------------GGLAIL--- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 300 VRYLMEdiqelkptifcgvprvyeriyGGAIAKISSGGALRKALFQYAYNY------KLRNLekgLRQDEAAPRLDRLif 373
Cdd:cd17630 60 VRSLLA---------------------GAELVLLERNQALAEDLAPPGVTHvslvptQLQRL---LDSGQGPAALKSL-- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 374 dkikqgfggrvRLLFSGAAPLSRhveEFLRVTSCS--VLSQGYGLTESCGGCLTSIVNEFSMmGTVGVPYPTIEARLesv 451
Cdd:cd17630 114 -----------RAVLLGGAPIPP---ELLERAADRgiPLYTTYGMTETASQVATKRPDGFGR-GGVGVLLPGRELRI--- 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 452 pemgydalsnVPRGEICLRGKTLFSGYFKRQdLTESALVDGWFHTGDIGEWQPNGAMKIIDRKKNIFkLSQGEYVAVENL 531
Cdd:cd17630 176 ----------VEDGEIWVGGASLAMGYLRGQ-LVPEFNEDGWFTTKDLGELHADGRLTVLGRADNMI-ISGGENIQPEEI 243
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 225428594 532 ENTYSRCPLITSIWVYGNSFESF---LVAVVVPDKKALED 568
Cdd:cd17630 244 EAALAAHPAVRDAFVVGVPDEELgqrPVAVIVGRGPADPA 283
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
76-567 |
5.94e-24 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 106.38 E-value: 5.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 76 WLTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQAIPYVPLYDSLGANAVEFIINHAEVSIAFVQ 155
Cdd:PRK06155 46 RWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVVE 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 156 ESKIPAMLTCLPKCTSyLKTIISFGKISSSQKEEAeelgvscFSWEEFALLGSLDCELPPkQKTDICTIMYTSGTTGEPK 235
Cdd:PRK06155 126 AALLAALEAADPGDLP-LPAVWLLDAPASVSVPAG-------WSTAPLPPLDAPAPAAAV-QPGDTAAILYTSGTTGPSK 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 236 GVVLSNeaimAE-----VLSTDQLLLETDkvateeDTYFSFLPLAHV-----FDQIMETYCIY----KGSSIGFW----- 296
Cdd:PRK06155 197 GVCCPH----AQfywwgRNSAEDLEIGAD------DVLYTTLPLFHTnalnaFFQALLAGATYvlepRFSASGFWpavrr 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 297 -GADVRYLMediqelkptifcgvprvyeriygGAIAKIssggalrkalfqyaynyklrnlekgLRQDEAAPRlDRlifdk 375
Cdd:PRK06155 267 hGATVTYLL-----------------------GAMVSI-------------------------LLSQPARES-DR----- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 376 ikqgfGGRVRLLFSGAAPLSRHVEEFLRvtsCSV-LSQGYGLTES---CGGCLTSivnefSMMGTVGVPYPTIEARLesV 451
Cdd:PRK06155 293 -----AHRVRVALGPGVPAALHAAFRER---FGVdLLDGYGSTETnfvIAVTHGS-----QRPGSMGRLAPGFEARV--V 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 452 PEMGYDALSNVPrGEICLRGKTLF---SGYFKRQDLTESALVDGWFHTGDIGEWQPNGAMKIIDRKKNIFKlSQGEYVAV 528
Cdd:PRK06155 358 DEHDQELPDGEP-GELLLRADEPFafaTGYFGMPEKTVEAWRNLWFHTGDRVVRDADGWFRFVDRIKDAIR-RRGENISS 435
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 225428594 529 ENLENTYSRCPLITSIWVYGNSFE----SFLVAVVVPDKKALE 567
Cdd:PRK06155 436 FEVEQVLLSHPAVAAAAVFPVPSElgedEVMAAVVLRDGTALE 478
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
77-561 |
6.21e-24 |
|
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: 105.41 E-value: 6.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 77 LTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQAIPYVPLYDSLGANAVEFIINHAEvsiafvqe 156
Cdd:cd05945 17 LTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIREILDAAK-------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 157 skiPAMLTCLPKCTSYlktiisfgkisssqkeeaeelgvscfsweefallgsldcelppkqktdictIMYTSGTTGEPKG 236
Cdd:cd05945 89 ---PALLIADGDDNAY---------------------------------------------------IIFTSGSTGRPKG 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 237 VVLSNEAIMA--EVLSTDQLLLETDKVATEEDtyFSFlPLAhVFDqimetycIYKGSSIGfwG----------ADVRYLM 304
Cdd:cd05945 115 VQISHDNLVSftNWMLSDFPLGPGDVFLNQAP--FSF-DLS-VMD-------LYPALASG--AtlvpvprdatADPKQLF 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 305 EDIQELKPTIFCGVPRVYERiyggaiakissggALRKALFqyaynyklrnlekglrqdeAAPRLDRLIfdkikqGFggrv 384
Cdd:cd05945 182 RFLAEHGITVWVSTPSFAAM-------------CLLSPTF-------------------TPESLPSLR------HF---- 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 385 rlLFSGAAPLSRHVEEFLRVTSCSVLSQGYGLTESCGGCLTSIVNEFSMMG----TVGVPYPtiEARLESVPEMGyDALS 460
Cdd:cd05945 220 --LFCGEVLPHKTARALQQRFPDARIYNTYGPTEATVAVTYIEVTPEVLDGydrlPIGYAKP--GAKLVILDEDG-RPVP 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 461 NVPRGEICLRGKTLFSGYFKRQDLTESALVD----GWFHTGDIGEWQPNGAMKIIDRKKNIFKLsQGEYVAVENLENTYS 536
Cdd:cd05945 295 PGEKGELVISGPSVSKGYLNNPEKTAAAFFPdegqRAYRTGDLVRLEADGLLFYRGRLDFQVKL-NGYRIELEEIEAALR 373
|
490 500
....*....|....*....|....*...
gi 225428594 537 RCPLITS---IWVYGNSFESFLVAVVVP 561
Cdd:cd05945 374 QVPGVKEavvVPKYKGEKVTELIAFVVP 401
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
213-567 |
6.70e-24 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 106.11 E-value: 6.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 213 LPPKQ--KTDICTIMYTSGTTGEPKGVVLSNEAIMAEVLSTDQLLLETDKVATEEDTYFSFLPLAHVFDQIMETYCIYKG 290
Cdd:PRK08751 200 MPTLQiePDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWLAGTGKLEEGCEVVITALPLYHIFALTANGLVFMKI 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 291 SSIGFWGADVRYLMEDIQELKPTIFCGVPRVyeriyggaiakissggalrKALFQYAYNyklrnlekglrqdeaAPRLDR 370
Cdd:PRK08751 280 GGCNHLISNPRDMPGFVKELKKTRFTAFTGV-------------------NTLFNGLLN---------------TPGFDQ 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 371 LIFDKIKQGFGGrvrllfsGAApLSRHVEEFLRVTSCSVLSQGYGLTE-SCGGCLTSI-VNEFSmmGTVGVPYPTIEARL 448
Cdd:PRK08751 326 IDFSSLKMTLGG-------GMA-VQRSVAERWKQVTGLTLVEAYGLTEtSPAACINPLtLKEYN--GSIGLPIPSTDACI 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 449 ESvpemgyDALSNVPRGEI---CLRGKTLFSGYFKRQDLTESAL-VDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSqGE 524
Cdd:PRK08751 396 KD------DAGTVLAIGEIgelCIKGPQVMKGYWKRPEETAKVMdADGWLHTGDIARMDEQGFVYIVDRKKDMILVS-GF 468
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 225428594 525 YVAVENLENTYSRCPLITSIwvygnsfesflVAVVVPDKKALE 567
Cdd:PRK08751 469 NVYPNEIEDVIAMMPGVLEV-----------AAVGVPDEKSGE 500
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
76-548 |
8.01e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 105.27 E-value: 8.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 76 WlTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQAIPYVPLYDSLGANAVEFIINHAEVsiAFVQ 155
Cdd:PRK09088 23 W-TYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEP--RLLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 156 ESKIPAMLTCLPKCTSYLktiisfgkissSQKEEAEELgvscfsweefALLGSLDCELPPkqktdicTIMYTSGTTGEPK 235
Cdd:PRK09088 100 GDDAVAAGRTDVEDLAAF-----------IASADALEP----------ADTPSIPPERVS-------LILFTSGTSGQPK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 236 GVVLSNEAIMAEVLSTDqllletdkVATEEDTYFSFL---PLAHVfdqimetyciykgssIGFwgadvrylmedIQELKP 312
Cdd:PRK09088 152 GVMLSERNLQQTAHNFG--------VLGRVDAHSSFLcdaPMFHI---------------IGL-----------ITSVRP 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 313 TIfcgvprvyerIYGGAIaKISSGGALRKALfqyaynYKLRNLEKGLRQDEAAPRLDRLIFDKikQGFGG----RVRLLF 388
Cdd:PRK09088 198 VL----------AVGGSI-LVSNGFEPKRTL------GRLGDPALGITHYFCVPQMAQAFRAQ--PGFDAaalrHLTALF 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 389 SGAAPlsrHVEEFLR--VTSCSVLSQGYGLTEScGGCLTSIVNE---FSMMGTVGVPYPTIEARLesVPEMGYDALSNVP 463
Cdd:PRK09088 259 TGGAP---HAAEDILgwLDDGIPMVDGFGMSEA-GTVFGMSVDCdviRAKAGAAGIPTPTVQTRV--VDDQGNDCPAGVP 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 464 rGEICLRGKTLFSGYFKRQDLTESALV-DGWFHTGDIGEWQPNGAMKIIDRKKNIFkLSQGEYVAVENLENTYSRCPLIT 542
Cdd:PRK09088 333 -GELLLRGPNLSPGYWRRPQATARAFTgDGWFRTGDIARRDADGFFWVVDRKKDMF-ISGGENVYPAEIEAVLADHPGIR 410
|
....*.
gi 225428594 543 SIWVYG 548
Cdd:PRK09088 411 ECAVVG 416
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
77-541 |
1.40e-23 |
|
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: 104.08 E-value: 1.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 77 LTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEACnsqaipyvplydsLGANAVEFIINhaevsiafvQE 156
Cdd:cd05919 11 VTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGC-------------LARGAIAVVIN---------PL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 157 SKIPAMLTCLPKCtsylktiisfgkisssqkeeaeelgvscfsweefallgslDCELPPKQKTDICTIMYTSGTTGEPKG 236
Cdd:cd05919 69 LHPDDYAYIARDC----------------------------------------EARLVVTSADDIAYLLYSSGTTGPPKG 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 237 VV--LSNEAIMAEVLSTDQL-LLETDKVATEEDTYFSFlPLAHVFdqimeTYCIYKGSS-IGFWGA-DVRYLMEDIQELK 311
Cdd:cd05919 109 VMhaHRDPLLFADAMAREALgLTPGDRVFSSAKMFFGY-GLGNSL-----WFPLAVGASaVLNPGWpTAERVLATLARFR 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 312 PTIFCGVPRVYERIyggaiakissggalrkalfqyaynyklrnlekgLRQDEAAPRLDRlifdkikqgfggRVRLLFSGA 391
Cdd:cd05919 183 PTVLYGVPTFYANL---------------------------------LDSCAGSPDALR------------SLRLCVSAG 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 392 APLSRHVEEFLRVTSCSVLSQGYGLTESCGGCLTSIVNEFSMmGTVGVPYPTIEARLesVPEMGYDALSNVPrGEICLRG 471
Cdd:cd05919 218 EALPRGLGERWMEHFGGPILDGIGATEVGHIFLSNRPGAWRL-GSTGRPVPGYEIRL--VDEEGHTIPPGEE-GDLLVRG 293
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 472 KTLFSGYFKRQDLTESALVDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSqGEYVAVENLENTYSRCPLI 541
Cdd:cd05919 294 PSAAVGYWNNPEKSRATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVG-GQWVSPVEVESLIIQHPAV 362
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
71-528 |
2.26e-23 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 104.96 E-value: 2.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 71 AGPYVWLTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQAIPYVPL---YDSLGAN--AVEFIIN 145
Cdd:PRK08180 64 DGGWRRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMYAGVPYAPVspaYSLVSQDfgKLRHVLE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 146 HAEVSIAFVQESKI--PAMLTCLPKCTsylKTIISFGkisssqkeeaEELGVSCFSWEEFA---LLGSLDCELPPKQKTD 220
Cdd:PRK08180 144 LLTPGLVFADDGAAfaRALAAVVPADV---EVVAVRG----------AVPGRAATPFAALLatpPTAAVDAAHAAVGPDT 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 221 ICTIMYTSGTTGEPKGVVL------SNEAIMAEVLstdQLLLETDKVateedtYFSFLPLAHVF--DQIMeTYCIYKGSS 292
Cdd:PRK08180 211 IAKFLFTSGSTGLPKAVINthrmlcANQQMLAQTF---PFLAEEPPV------LVDWLPWNHTFggNHNL-GIVLYNGGT 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 293 I---------GFWGADVRYLmediQELKPTIFCGVPRVYEriyggaiakissggALRKAlfqyaynyklrnlekgLRQDE 363
Cdd:PRK08180 281 LyiddgkptpGGFDETLRNL----REISPTVYFNVPKGWE--------------MLVPA----------------LERDA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 364 AaprLDRLIFdkikqgfgGRVRLLFSGAAPLSRHVEEFL----------RVTSCSvlsqGYGLTESCGGClTSIVNEFSM 433
Cdd:PRK08180 327 A---LRRRFF--------SRLKLLFYAGAALSQDVWDRLdrvaeatcgeRIRMMT----GLGMTETAPSA-TFTTGPLSR 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 434 MGTVGVPYPTIEARLesVPEMGydalsnvpRGEICLRGKTLFSGYFKRQDLTESALVD-GWFHTGDigewqpngAMKIID 512
Cdd:PRK08180 391 AGNIGLPAPGCEVKL--VPVGG--------KLEVRVKGPNVTPGYWRAPELTAEAFDEeGYYRSGD--------AVRFVD 452
|
490 500
....*....|....*....|....*...
gi 225428594 513 ------------RKKNIFKLSQGEYVAV 528
Cdd:PRK08180 453 padperglmfdgRIAEDFKLSSGTWVSV 480
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
78-571 |
8.44e-23 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 103.00 E-value: 8.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 78 TYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPewiiameaCNSQAIPYVPLYDS--------LGANAVEFIINHAEV 149
Cdd:PLN02479 47 TWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIP--------AMYEAHFGVPMAGAvvncvnirLNAPTIAFLLEHSKS 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 150 SIAFVQESKIP----AMLTCLPKCTSYLKT--IISFGKISSSQKEEAEELGVSCFSWEEFalLGSLDCEL---PPKQKTD 220
Cdd:PLN02479 119 EVVMVDQEFFTlaeeALKILAEKKKSSFKPplLIVIGDPTCDPKSLQYALGKGAIEYEKF--LETGDPEFawkPPADEWQ 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 221 ICTIMYTSGTTGEPKGVVLSNEAIMAEVLStDQLLLETDKVATeedtYFSFLPLAHV----FDQIMETYCiykGSSIGFW 296
Cdd:PLN02479 197 SIALGYTSGTTASPKGVVLHHRGAYLMALS-NALIWGMNEGAV----YLWTLPMFHCngwcFTWTLAALC---GTNICLR 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 297 GADVRYLMEDIQELKPTIFCGVPRVyeriyggaiakissggalrkalfqyaynykLRNLEKGLRQDEAAPrLDRLifdki 376
Cdd:PLN02479 269 QVTAKAIYSAIANYGVTHFCAAPVV------------------------------LNTIVNAPKSETILP-LPRV----- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 377 kqgfggrVRLLFSGAAP----LSRHVEEFLRVTSCSVLSQGYGLTESCG-----GCLTSIVNEfSMMGTVGVPYPTIEaR 447
Cdd:PLN02479 313 -------VHVMTAGAAPppsvLFAMSEKGFRVTHTYGLSETYGPSTVCAwkpewDSLPPEEQA-RLNARQGVRYIGLE-G 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 448 LESVpemgyDALSNVP-------RGEICLRGKTLFSGYFKRQDLTESALVDGWFHTGDIGEWQPNGAMKIIDRKKNIFkL 520
Cdd:PLN02479 384 LDVV-----DTKTMKPvpadgktMGEIVMRGNMVMKGYLKNPKANEEAFANGWFHSGDLGVKHPDGYIEIKDRSKDII-I 457
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 225428594 521 SQGEYVAVENLENTYSRCPLItsiwvygnsFESFLVAvvvpdkKALEDWAE 571
Cdd:PLN02479 458 SGGENISSLEVENVVYTHPAV---------LEASVVA------RPDERWGE 493
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
214-567 |
9.74e-23 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 102.41 E-value: 9.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 214 PPKQKTDICTIMYTSGTTGEPKGVVLSNEAIMAEVLSTDQLLLETDKVATEEDTYFSF--LPLAHVFdqiMETYCIYKGS 291
Cdd:PRK07059 199 VKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQMEAWLQPAFEKKPRPDQLNFVcaLPLYHIF---ALTVCGLLGM 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 292 SIGFWGA------DVRYLMEDIQELKPTIFCGVPRVYeriyggaiakissggalrkalfqyayNYKLRNlekglrqdeaa 365
Cdd:PRK07059 276 RTGGRNIlipnprDIPGFIKELKKYQVHIFPAVNTLY--------------------------NALLNN----------- 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 366 PRLDRLIFDKIKQGFGGrvrllfsGAApLSRHV-EEFLRVTSCSVLsQGYGLTES--CGGCLTSIVNEFSmmGTVGVPYP 442
Cdd:PRK07059 319 PDFDKLDFSKLIVANGG-------GMA-VQRPVaERWLEMTGCPIT-EGYGLSETspVATCNPVDATEFS--GTIGLPLP 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 443 TIEARLESvpemgyDALSNVPRG---EICLRGKTLFSGYFKRQDltESALV---DGWFHTGDIGEWQPNGAMKIIDRKKN 516
Cdd:PRK07059 388 STEVSIRD------DDGNDLPLGepgEICIRGPQVMAGYWNRPD--ETAKVmtaDGFFRTGDVGVMDERGYTKIVDRKKD 459
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 225428594 517 IFKLSqGEYVAVENLENTYSRCPLItsiwvygnsFEsflVAVV-VPDKKALE 567
Cdd:PRK07059 460 MILVS-GFNVYPNEIEEVVASHPGV---------LE---VAAVgVPDEHSGE 498
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
83-560 |
1.99e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 101.12 E-value: 1.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 83 YDAALRMGSAM-RSRGVNPGDRCGIYGSNCPEWIIAMEACNSQAIPYVPLYDSLGANAVEFIINHAEVSIAFVQE--SKI 159
Cdd:PRK06145 33 FHQRILQAAGMlHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYILGDAGAKLLLVDEefDAI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 160 PAMLTclpkctsylKTIIsfgkISSSQKEEAEELGVscfsweefallGSLDC-ELPPKQKTDICTIMYTSGTTGEPKGVV 238
Cdd:PRK06145 113 VALET---------PKIV----IDAAAQADSRRLAQ-----------GGLEIpPQAAVAPTDLVRLMYTSGTTDRPKGVM 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 239 LSNEAIMAEvlSTDQLLLETdkvATEEDTYFSFLPLAHVfdqimeTYCIYKGSSIGFWGADVRYLmediQELKP-TIFCG 317
Cdd:PRK06145 169 HSYGNLHWK--SIDHVIALG---LTASERLLVVGPLYHV------GAFDLPGIAVLWVGGTLRIH----REFDPeAVLAA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 318 VPRvyERIYGGAIAKISSGGALrkalfqyaynyklrnlekglrqdeAAPRLDRLIFDKIKQGFGGRVRllfsgaAPLSRh 397
Cdd:PRK06145 234 IER--HRLTCAWMAPVMLSRVL------------------------TVPDRDRFDLDSLAWCIGGGEK------TPESR- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 398 VEEFLRVTSCSVLSQGYGLTESCGG-CLTSIVNEFSMMGTVGVPYPTIEARLESvpEMGYDALSNVpRGEICLRGKTLFS 476
Cdd:PRK06145 281 IRDFTRVFTRARYIDAYGLTETCSGdTLMEAGREIEKIGSTGRALAHVEIRIAD--GAGRWLPPNM-KGEICMRGPKVTK 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 477 GYFKRQDLTESALVDGWFHTGDIGEWQPNGAMKIIDRKKNIFkLSQGEYVAVENLENTYSRCPLITSIWVYG---NSFES 553
Cdd:PRK06145 358 GYWKDPEKTAEAFYGDWFRSGDVGYLDEEGFLYLTDRKKDMI-ISGGENIASSEVERVIYELPEVAEAAVIGvhdDRWGE 436
|
....*..
gi 225428594 554 FLVAVVV 560
Cdd:PRK06145 437 RITAVVV 443
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
76-571 |
1.57e-21 |
|
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: 98.13 E-value: 1.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 76 WLTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQAIPYVPLYDSLGANAVEFIINHAEVSIAFVQ 155
Cdd:cd12116 12 SLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALVLTD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 156 eskiPAMLTCLPKCtsylktiisfgkisssqkeeaeeLGVSCFSWEefALLGSLDCELPPKQKTDICTIMYTSGTTGEPK 235
Cdd:cd12116 92 ----DALPDRLPAG-----------------------LPVLLLALA--AAAAAPAAPRTPVSPDDLAYVIYTSGSTGRPK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 236 GVVLSNEAI------MAEVLST---DQLLLETdkvateedTY-FS------FLPL---AHVfdQIMETYCIYkgssigfw 296
Cdd:cd12116 143 GVVVSHRNLvnflhsMRERLGLgpgDRLLAVT--------TYaFDisllelLLPLlagARV--VIAPRETQR-------- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 297 gaDVRYLMEDIQELKPTIFcgvprvyeriyggaiakissggalrkalfqyaynyklrnlekglrqdEAAPRLDRLIFDki 376
Cdd:cd12116 205 --DPEALARLIEAHSITVM-----------------------------------------------QATPATWRMLLD-- 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 377 kQGFGGR--VRLLFSGAApLSRHVEEFLRVTSCSvLSQGYGLTEscggclTSI------VNEFSMMGTVGVPYP-----T 443
Cdd:cd12116 234 -AGWQGRagLTALCGGEA-LPPDLAARLLSRVGS-LWNLYGPTE------TTIwstaarVTAAAGPIPIGRPLAntqvyV 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 444 IEARLESVPEmgydalsNVPrGEICLRGKTLFSGYFKRQDLTESALVDG--------WFHTGDIGEWQPNGAMKIIDRKK 515
Cdd:cd12116 305 LDAALRPVPP-------GVP-GELYIGGDGVAQGYLGRPALTAERFVPDpfagpgsrLYRTGDLVRRRADGRLEYLGRAD 376
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 225428594 516 NIFKLsQGEYVAVENLENTYSRCPLIT--SIWVYGNSFESFLVAVVVPDKKALEDWAE 571
Cdd:cd12116 377 GQVKI-RGHRIELGEIEAALAAHPGVAqaAVVVREDGGDRRLVAYVVLKAGAAPDAAA 433
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
72-515 |
2.21e-21 |
|
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: 98.12 E-value: 2.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 72 GPYVWLTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEACN-SQAIPyVPLydslGANAVEFIINHAEVS 150
Cdd:cd05906 35 GSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVlAGFVP-APL----TVPPTYDEPNARLRK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 151 IAFVqeSKI---PAMLTclpkctsylktiisfgkiSSSQKEEAEELgVSCFSWEEFALLGS---LDCE----LPPKQKTD 220
Cdd:cd05906 110 LRHI--WQLlgsPVVLT------------------DAELVAEFAGL-ETLSGLPGIRVLSIeelLDTAadhdLPQSRPDD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 221 ICTIMYTSGTTGEPKGVVLSNEAIMAEVLSTDQllletDKVATEEDTYFSFLPLAHVfdqimetyciykGSSIGFWGADV 300
Cdd:cd05906 169 LALLMLTSGSTGFPKAVPLTHRNILARSAGKIQ-----HNGLTPQDVFLNWVPLDHV------------GGLVELHLRAV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 301 RYLMEDIQELKPTIFCGVPRVYERI--YGGAIAkissggalrkalF--QYAYNYKLRNLEKGLRQDeaaprldrliFDKi 376
Cdd:cd05906 232 YLGCQQVHVPTEEILADPLRWLDLIdrYRVTIT------------WapNFAFALLNDLLEEIEDGT----------WDL- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 377 kqgfgGRVRLLFSGAAPLSRHV-EEFLRVTS-----CSVLSQGYGLTESCGGCLTSIV---------NEFSmmgTVGVPY 441
Cdd:cd05906 289 -----SSLRYLVNAGEAVVAKTiRRLLRLLEpyglpPDAIRPAFGMTETCSGVIYSRSfptydhsqaLEFV---SLGRPI 360
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 225428594 442 PTIEARLesVPEMGyDALSNVPRGEICLRGKTLFSGYFKRQDLTESALV-DGWFHTGDIGeWQPNGAMKIIDRKK 515
Cdd:cd05906 361 PGVSMRI--VDDEG-QLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTeDGWFRTGDLG-FLDNGNLTITGRTK 431
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
220-517 |
2.47e-21 |
|
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: 95.79 E-value: 2.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 220 DICTIMYTSGTTGEPKGVVLSNEAIMAEvlsTDQLLLETdKVATEEDTYFSFLPLAHVFDQIMETYCIYKGSSIGFWGAD 299
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTFFAV---PDILQKEG-LNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 300 VRY--LMEDIQELKPTIFCGVPRVYEriyggaiakissggalrkalfqyaynyKLRNLEKGLRQDeaAPRLdRLIfdkik 377
Cdd:cd17635 78 TTYksLFKILTTNAVTTTCLVPTLLS---------------------------KLVSELKSANAT--VPSL-RLI----- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 378 qGFGGrvrllfsgAAPLSRHVEEFLrVTSCSVLSQGYGLTESCGGCLTSIVNEFSMMGTVGVPYPTIEARLESVPEMgyd 457
Cdd:cd17635 123 -GYGG--------SRAIAADVRFIE-ATGLTNTAQVYGLSETGTALCLPTDDDSIEINAVGRPYPGVDVYLAATDGI--- 189
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 458 ALSNVPRGEICLRGKTLFSGYFKRQDLTESALVDGWFHTGDIGEWQPNGAMKIIDRKKNI 517
Cdd:cd17635 190 AGPSASFGTIWIKSPANMLGYWNNPERTAEVLIDGWVNTGDLGERREDGFLFITGRSSES 249
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
77-532 |
3.86e-21 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 97.36 E-value: 3.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 77 LTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIA------MEACNSQAIP-YVP--LYDSLGANAVEFIINHA 147
Cdd:PLN02246 51 YTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAflgasrRGAVTTTANPfYTPaeIAKQAKASGAKLIITQS 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 148 ---EVSIAFVQESKIPAMLT------CLpkctsylktiiSFGKISSSQKEEAEELGVScfsweefallgsldcelppkqK 218
Cdd:PLN02246 131 cyvDKLKGLAEDDGVTVVTIddppegCL-----------HFSELTQADENELPEVEIS---------------------P 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 219 TDICTIMYTSGTTGEPKGVVLSNEAIMAEVlsTDQLLLETDKVA-TEEDTYFSFLPLAHVF--DQIMetYC-IYKGSSI- 293
Cdd:PLN02246 179 DDVVALPYSSGTTGLPKGVMLTHKGLVTSV--AQQVDGENPNLYfHSDDVILCVLPMFHIYslNSVL--LCgLRVGAAIl 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 294 ---GFwgaDVRYLMEDIQELKPTIFCGVPRVYEriyggAIAKissggalrkalfqyaynyklrnlekglrqdeaAPRLDR 370
Cdd:PLN02246 255 impKF---EIGALLELIQRHKVTIAPFVPPIVL-----AIAK--------------------------------SPVVEK 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 371 liFDKikqgfgGRVRLLFSGAAPLSRHVEEFLRVT-SCSVLSQGYGLTEScGGCLtsivnefSM-MGTVGVPYP------ 442
Cdd:PLN02246 295 --YDL------SSIRMVLSGAAPLGKELEDAFRAKlPNAVLGQGYGMTEA-GPVL-------AMcLAFAKEPFPvksgsc 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 443 -TI--EARLESV-PEMGYDALSNVPrGEICLRGKTLFSGYFKRQDLTESAL-VDGWFHTGDIGEWQPNGAMKIIDRKKNI 517
Cdd:PLN02246 359 gTVvrNAELKIVdPETGASLPRNQP-GEICIRGPQIMKGYLNDPEATANTIdKDGWLHTGDIGYIDDDDELFIVDRLKEL 437
|
490
....*....|....*
gi 225428594 518 FKLsQGEYVAVENLE 532
Cdd:PLN02246 438 IKY-KGFQVAPAELE 451
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
70-567 |
4.39e-21 |
|
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: 97.50 E-value: 4.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 70 KAGPYVW--LTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQAIPYVPL---YDSLGANAVEF-- 142
Cdd:cd05921 17 REGNGGWrrVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVspaYSLMSQDLAKLkh 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 143 IINHAEVSIAFVQESkipamltclPKCTSYLKTIISFGK-ISSSQKEEAEELGVSCFSWEEFALLGSLDCELPPKQKTDI 221
Cdd:cd05921 97 LFELLKPGLVFAQDA---------APFARALAAIFPLGTpLVVSRNAVAGRGAISFAELAATPPTAAVDAAFAAVGPDTV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 222 CTIMYTSGTTGEPKGVVlSNEAIMAevlSTDQLLLETDKVATEED-TYFSFLPLAHVFdqimetyciykGSSIGF----W 296
Cdd:cd05921 168 AKFLFTSGSTGLPKAVI-NTQRMLC---ANQAMLEQTYPFFGEEPpVLVDWLPWNHTF-----------GGNHNFnlvlY 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 297 GADVRYL-------------MEDIQELKPTIFCGVPRVYEriyggaiakissggalrkALFQYaynyklrnlekgLRQDE 363
Cdd:cd05921 233 NGGTLYIddgkpmpggfeetLRNLREISPTVYFNVPAGWE------------------MLVAA------------LEKDE 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 364 AaprLDRLIFDkikqgfggRVRLLFSGAAPLSRHVEEflRVTSCSV--------LSQGYGLTESCGGClTSIVNEFSMMG 435
Cdd:cd05921 283 A---LRRRFFK--------RLKLMFYAGAGLSQDVWD--RLQALAVatvgeripMMAGLGATETAPTA-TFTHWPTERSG 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 436 TVGVPYPTIEARLesVPEMGydalsnvpRGEICLRGKTLFSGYFKRQDLTESAL-VDGWFHTGDIGEW----QPNGAMKI 510
Cdd:cd05921 349 LIGLPAPGTELKL--VPSGG--------KYEVRVKGPNVTPGYWRQPELTAQAFdEEGFYCLGDAAKLadpdDPAKGLVF 418
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 225428594 511 IDRKKNIFKLSQGEYVAVENLEN-TYSRC-PLITSIWVYGNSFEsFLVAVVVPDKKALE 567
Cdd:cd05921 419 DGRVAEDFKLASGTWVSVGPLRArAVAACaPLVHDAVVAGEDRA-EVGALVFPDLLACR 476
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
48-600 |
6.26e-21 |
|
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: 96.67 E-value: 6.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 48 FSDSVERNpKNQMLGRRQIINSKAGPyvwLTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIA-MEACNSQAI 126
Cdd:cd05959 5 AATLVDLN-LNEGRGDKTAFIDDAGS---LTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAfLGAIRAGIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 127 PyVPLYDSLGANAVEFIINHAEVSIAFVQESKIPAMLTCLPKCTSYLKTIISFGkisssqkEEAEELGVSCFSweefALL 206
Cdd:cd05959 81 P-VPVNTLLTPDDYAYYLEDSRARVVVVSGELAPVLAAALTKSEHTLVVLIVSG-------GAGPEAGALLLA----ELV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 207 GSLDCELPP--KQKTDICTIMYTSGTTGEPKGVV--LSNEAIMAEVLSTDQLLLetdkvaTEEDTYFSFLPLAHvfdqim 282
Cdd:cd05959 149 AAEAEQLKPaaTHADDPAFWLYSSGSTGRPKGVVhlHADIYWTAELYARNVLGI------REDDVCFSAAKLFF------ 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 283 eTYCIYKGSSIGFW-GADVrYLM----------EDIQELKPTIFCGVPRVYeriyggaiakissggalrkalfqyaynyk 351
Cdd:cd05959 217 -AYGLGNSLTFPLSvGATT-VLMperptpaavfKRIRRYRPTVFFGVPTLY----------------------------- 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 352 lrnleKGLRQDEAAPRLDrlifdkikqgfGGRVRLLFSGAAPLSRHV-EEFLRVTSCSVLsQGYGLTESCGGCLTSIVNE 430
Cdd:cd05959 266 -----AAMLAAPNLPSRD-----------LSSLRLCVSAGEALPAEVgERWKARFGLDIL-DGIGSTEMLHIFLSNRPGR 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 431 fSMMGTVGVPYPTIEARLesVPEMGYDALSNVPrGEICLRGKTLFSGYFKRQDLTESALVDGWFHTGDIGEWQPNGAMKI 510
Cdd:cd05959 329 -VRYGTTGKPVPGYEVEL--RDEDGGDVADGEP-GELYVRGPSSATMYWNNRDKTRDTFQGEWTRTGDKYVRDDDGFYTY 404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 511 IDRKKNIFKLSqGEYVAVENLENTYSRCPLITSIWVYGNSFESFL---VAVVVPDKKAledwAENHNVTGDFKSLCEN-L 586
Cdd:cd05959 405 AGRADDMLKVS-GIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLtkpKAFVVLRPGY----EDSEALEEELKEFVKDrL 479
|
570
....*....|....*....
gi 225428594 587 EARKY-----ILDELNNTG 600
Cdd:cd05959 480 APYKYprwivFVDELPKTA 498
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
220-567 |
8.66e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 96.37 E-value: 8.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 220 DICTIMYTSGTTGEPKGVVLSNEAIMAEVLSTDQLLleTDKVATEEDTYFSFLPLAHVFDQIMETYCIYKGSSIGFWGAD 299
Cdd:PRK05677 208 DVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCRALM--GSNLNEGCEILIAPLPLYHIYAFTFHCMAMMLIGNHNILISN 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 300 VRYLMEDIQELKPTIFCGvprvyeriYGGaiakissggalrkalfqyaynykLRNLEKGLRQDEAAPRLDrliFDKIKQG 379
Cdd:PRK05677 286 PRDLPAMVKELGKWKFSG--------FVG-----------------------LNTLFVALCNNEAFRKLD---FSALKLT 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 380 FGGRVRLLFSGAaplsrhvEEFLRVTSCSVLsQGYGLTEscggclTS---IVNEFS--MMGTVGVPYPTIEARLESvpem 454
Cdd:PRK05677 332 LSGGMALQLATA-------ERWKEVTGCAIC-EGYGMTE------TSpvvSVNPSQaiQVGTIGIPVPSTLCKVID---- 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 455 gyDALSNVPRGEI---CLRGKTLFSGYFKRQDLTESAL-VDGWFHTGDIGEWQPNGAMKIIDRKKNIFklsqgeyvaven 530
Cdd:PRK05677 394 --DDGNELPLGEVgelCVKGPQVMKGYWQRPEATDEILdSDGWLKTGDIALIQEDGYMRIVDRKKDMI------------ 459
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 225428594 531 lentysrcpLITSIWVYGNSFESFLV---------AVVVPDKKALE 567
Cdd:PRK05677 460 ---------LVSGFNVYPNELEDVLAalpgvlqcaAIGVPDEKSGE 496
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
77-561 |
9.83e-21 |
|
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: 96.04 E-value: 9.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 77 LTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEACN-SQAIPyVPLYDSLGANAVEFIINHAEVSIAFVQ 155
Cdd:cd05923 29 LTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHrLGAVP-ALINPRLKAAELAELIERGEMTAAVIA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 156 ESKIPAMltclpkctsylktiisfGKISSSQKEEAEELGVSCFSWEEFALLgsldCELPPKQKTDICTIMYTSGTTGEPK 235
Cdd:cd05923 108 VDAQVMD-----------------AIFQSGVRVLALSDLVGLGEPESAGPL----IEDPPREPEQPAFVFYTSGTTGLPK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 236 GVVLSNEAIMAEVL--STDQLLLETDkvateEDTYFSFLPLAHVfdqiMETYCIYKGSSI--GFWgADVRYL-----MED 306
Cdd:cd05923 167 GAVIPQRAAESRVLfmSTQAGLRHGR-----HNVVLGLMPLYHV----IGFFAVLVAALAldGTY-VVVEEFdpadaLKL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 307 IQELKPTIFCGVPRVYERIyggaIAKISSGGAlrkalfqyaynyKLRNLEKglrqdeaaprldrlifdkikqgfggrvrL 386
Cdd:cd05923 237 IEQERVTSLFATPTHLDAL----AAAAEFAGL------------KLSSLRH----------------------------V 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 387 LFSGAA---PLSRHVEEFLRVTSCSVlsqgYGLTEScggcLTSIVNEFSMMGTVGVPYPTIEARLESVPEMGYDALSNVP 463
Cdd:cd05923 273 TFAGATmpdAVLERVNQHLPGEKVNI----YGTTEA----MNSLYMRDARTGTEMRPGFFSEVRIVRIGGSPDEALANGE 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 464 RGEIC--LRGKTLFSGYFKRQDLTESALVDGWFHTGDIGEWQPNGAMKIIDRKKNIFkLSQGEYVAVENLENTYSRCPLI 541
Cdd:cd05923 345 EGELIvaAAADAAFTGYLNQPEATAKKLQDGWYRTGDVGYVDPSGDVRILGRVDDMI-ISGGENIHPSEIERVLSRHPGV 423
|
490 500
....*....|....*....|...
gi 225428594 542 TSIWVYGNSFESF---LVAVVVP 561
Cdd:cd05923 424 TEVVVIGVADERWgqsVTACVVP 446
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
46-564 |
1.28e-20 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 96.03 E-value: 1.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 46 EFFSDSVERNPKNQML-----GRRqiinskagpyvwLTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEA 120
Cdd:PRK08315 20 QLLDRTAARYPDREALvyrdqGLR------------WTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 121 CNSQAIPYV---PLYDSlgaNAVEFIINHAEVS-------------IAFVQESkIPAMLTCLPKCTS-----YLKTIISF 179
Cdd:PRK08315 88 TAKIGAILVtinPAYRL---SELEYALNQSGCKaliaadgfkdsdyVAMLYEL-APELATCEPGQLQsarlpELRRVIFL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 180 GkisssqkeeaEELGVSCFSWEEFALLGS--LDCELPPKQKT----DICTIMYTSGTTGEPKGVVLSNEAIM------AE 247
Cdd:PRK08315 164 G----------DEKHPGMLNFDELLALGRavDDAELAARQATldpdDPINIQYTSGTTGFPKGATLTHRNILnngyfiGE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 248 VlstdQLLLETDKVATEedtyfsfLPLAHVFDQIMETY-CIYKGSSI-----GFwgaDVRYLMEDIQELKPTIFCGVPRV 321
Cdd:PRK08315 234 A----MKLTEEDRLCIP-------VPLYHCFGMVLGNLaCVTHGATMvypgeGF---DPLATLAAVEEERCTALYGVPTM 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 322 YeriyggaIAKissggaLRKALFQyayNYKLRNLEKGLRQDEAAP-RLDRLIFDKIkqgfggrvrllfsgaaplsrHVEE 400
Cdd:PRK08315 300 F-------IAE------LDHPDFA---RFDLSSLRTGIMAGSPCPiEVMKRVIDKM--------------------HMSE 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 401 flrVTSCsvlsqgYGLTE-SCGGCLTSIVNEFSM-MGTVGVPYPTIEARLesV-PEMGYDalsnVPR---GEICLRGKTL 474
Cdd:PRK08315 344 ---VTIA------YGMTEtSPVSTQTRTDDPLEKrVTTVGRALPHLEVKI--VdPETGET----VPRgeqGELCTRGYSV 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 475 FSGYFKRQDLTESAL-VDGWFHTGDIGEWQPNGAMKIIDRKKNIfkLSQGEyvavenlENTYSRcplitsiwvygnSFES 553
Cdd:PRK08315 409 MKGYWNDPEKTAEAIdADGWMHTGDLAVMDEEGYVNIVGRIKDM--IIRGG-------ENIYPR------------EIEE 467
|
570 580
....*....|....*....|
gi 225428594 554 FL--------VAVV-VPDKK 564
Cdd:PRK08315 468 FLythpkiqdVQVVgVPDEK 487
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
77-567 |
1.38e-20 |
|
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: 94.85 E-value: 1.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 77 LTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQAIPYVPLYDSLGANAVEFIINHAEVSIAFVqe 156
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVV-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 157 skipamltclpkctsylktiisfgkisssqkeeaeelgvscfsweefalLGSLDcelppkqktDICTIMYTSGTTGEPKG 236
Cdd:cd05935 80 -------------------------------------------------GSELD---------DLALIPYTSGTTGLPKG 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 237 VVLSNEAIMAEVLStdqllLETDKVATEEDTYFSFLPLAHV--FDQIMETyCIYKGSSI---GFWGADVryLMEDIQELK 311
Cdd:cd05935 102 CMHTHFSAAANALQ-----SAVWTGLTPSDVILACLPLFHVtgFVGSLNT-AVYVGGTYvlmARWDRET--ALELIEKYK 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 312 PTIFCGVPRVyeriyggAIAKISSggalrkalfqyaYNYKLRNLEKglrqdeaaprldrlifdkikqgfggrVRLLFSGA 391
Cdd:cd05935 174 VTFWTNIPTM-------LVDLLAT------------PEFKTRDLSS--------------------------LKVLTGGG 208
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 392 APLSRHVEEFLRVTSCSVLSQGYGLTESCGGCLTSIVNEFSMMgTVGVPYPTIEARLESvPEMGYDALSNVpRGEICLRG 471
Cdd:cd05935 209 APMPPAVAEKLLKLTGLRFVEGYGLTETMSQTHTNPPLRPKLQ-CLGIP*FGVDARVID-IETGRELPPNE-VGEIVVRG 285
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 472 KTLFSGYFKRQDLTESAL--VDG--WFHTGDIGEWQPNGAMKIIDRKKNIFKLSqGEYVAVENLENTYSRCPLITSIWVY 547
Cdd:cd05935 286 PQIFKGYWNRPEETEESFieIKGrrFFRTGDLGYMDEEGYFFFVDRVKRMINVS-GFKVWPAEVEAKLYKHPAI*EVCVI 364
|
490 500
....*....|....*....|
gi 225428594 548 GnsfesflvavvVPDKKALE 567
Cdd:cd05935 365 S-----------VPDERVGE 373
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
219-564 |
1.66e-20 |
|
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: 93.50 E-value: 1.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 219 TDICTIMYTSGTTGEPKGV------VLSNEAIMAEVLSTdqllletdkvaTEEDTYFSFLPLAHVFDQIMETY-CIYKGS 291
Cdd:cd05917 2 DDVINIQFTSGTTGSPKGAtlthhnIVNNGYFIGERLGL-----------TEQDRLCIPVPLFHCFGSVLGVLaCLTHGA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 292 SIGFWGA--DVRYLMEDIQELKPTIFCGVPRVYeriyggaIAKISSggalrkalfqyaynyklrnlekglrqdeaaPRLD 369
Cdd:cd05917 71 TMVFPSPsfDPLAVLEAIEKEKCTALHGVPTMF-------IAELEH------------------------------PDFD 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 370 RLIFDKIKQGFGGrvrllfsGA---APLSRHVEEFLRVTSCSVlsqGYGLTESCGGCLTSIVNE--FSMMGTVGVPYPTI 444
Cdd:cd05917 114 KFDLSSLRTGIMA-------GApcpPELMKRVIEVMNMKDVTI---AYGMTETSPVSTQTRTDDsiEKRVNTVGRIMPHT 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 445 EARL-----ESVPEMGYdalsnvpRGEICLRGKTLFSGYFKRQDLT-ESALVDGWFHTGDIGEWQPNGAMKIIDRKKNIF 518
Cdd:cd05917 184 EAKIvdpegGIVPPVGV-------PGELCIRGYSVMKGYWNDPEKTaEAIDGDGWLHTGDLAVMDEDGYCRIVGRIKDMI 256
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 225428594 519 kLSQGEYVAVENLENTYSRCPLITSIWVYGnsfesflvavvVPDKK 564
Cdd:cd05917 257 -IRGGENIYPREIEEFLHTHPKVSDVQVVG-----------VPDER 290
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
77-521 |
3.12e-20 |
|
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: 93.56 E-value: 3.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 77 LTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQAIPYVPLYDSLGANAVEFIINHAEVSIAFVQE 156
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 157 SkipamltclpkctsylktiisfgkisssqkeeaeelgvscfsweefallgsldcelppkqktDICTIMYTSGTTGEPKG 236
Cdd:cd05972 81 E--------------------------------------------------------------DPALIYFTSGTTGLPKG 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 237 VVLSNEAIMAeVLSTDQLLL---ETDKVATEEDT------YFSFL-PLAHVFDQIMETYciykgssIGFwgaDVRYLMED 306
Cdd:cd05972 99 VLHTHSYPLG-HIPTAAYWLglrPDDIHWNIADPgwakgaWSSFFgPWLLGATVFVYEG-------PRF---DAERILEL 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 307 IQELKPTIFCGVPRVYERIyggaiakissggalrkalfqyaynyklrnlekglrqdeAAPRLDRLIFdkikqgfgGRVRL 386
Cdd:cd05972 168 LERYGVTSFCGPPTAYRML--------------------------------------IKQDLSSYKF--------SHLRL 201
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 387 LFSGAAPLSRHVEEFLRVTSCSVLSQGYGLTEScggclTSIVNEFSMM----GTVGVPYPTIEARLesVPEMGYDALSNV 462
Cdd:cd05972 202 VVSAGEPLNPEVIEWWRAATGLPIRDGYGQTET-----GLTVGNFPDMpvkpGSMGRPTPGYDVAI--IDDDGRELPPGE 274
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 225428594 463 PrGEICLRGKT--LFSGYFKRQDLTESALVDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLS 521
Cdd:cd05972 275 E-GDIAIKLPPpgLFLGYVGDPEKTEASIRGDYYLTGDRAYRDEDGYFWFVGRADDIIKSS 334
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
205-567 |
3.96e-20 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 94.52 E-value: 3.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 205 LLGSLDCEL-PPKQKTDICTIMYTSGTTGEPKGVVLSNEAIMAEVLSTDQLLLETDKVATEEDTYFSFLPLAHVFD-QIM 282
Cdd:PLN02574 183 IKEDFDFVPkPVIKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVRFEASQYEYPGSDNVYLAALPMFHIYGlSLF 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 283 ETYCIYKGSSIGFWGA-DVRYLMEDIQELKPTIFCGVPRVyeriyggaiakissggalrkalfqyaynykLRNLEKGLRQ 361
Cdd:PLN02574 263 VVGLLSLGSTIVVMRRfDASDMVKVIDRFKVTHFPVVPPI------------------------------LMALTKKAKG 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 362 DEAAPrldrliFDKIKQgfggrvrlLFSGAAPLSRH-VEEFLRVTSCSVLSQGYGLTESCG-GCLTSIVNEFSMMGTVGV 439
Cdd:PLN02574 313 VCGEV------LKSLKQ--------VSCGAAPLSGKfIQDFVQTLPHVDFIQGYGMTESTAvGTRGFNTEKLSKYSSVGL 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 440 PYPTIEARlesVPEMGYDALsnVP---RGEICLRGKTLFSGYFKRQDLTESALV-DGWFHTGDIGEWQPNGAMKIIDRKK 515
Cdd:PLN02574 379 LAPNMQAK---VVDWSTGCL--LPpgnCGELWIQGPGVMKGYLNNPKATQSTIDkDGWLRTGDIAYFDEDGYLYIVDRLK 453
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 225428594 516 NIFKLsQGEYVAVENLENTYSRCPLITSIWVYGnsfesflvavvVPDKKALE 567
Cdd:PLN02574 454 EIIKY-KGFQIAPADLEAVLISHPEIIDAAVTA-----------VPDKECGE 493
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
77-563 |
9.33e-20 |
|
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: 92.59 E-value: 9.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 77 LTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEACnSQA-IPYVPLYDSLGANAVEFIINHAEVSIAFVQ 155
Cdd:cd05930 13 LTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAV-LKAgAAYVPLDPSYPAERLAYILEDSGAKLVLTD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 156 ESkipamltclpkctsylktiisfgkisssqkeeaeelgvscfsweefallgsldcelppkqktDICTIMYTSGTTGEPK 235
Cdd:cd05930 92 PD--------------------------------------------------------------DLAYVIYTSGSTGKPK 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 236 GVVLSNEAIMAEVLSTDQLLLetdkvATEEDTYFSFLPLAhvFDQ-IMETYC-IYKGSSIGFWGADVRYLMEDIQEL--- 310
Cdd:cd05930 110 GVMVEHRGLVNLLLWMQEAYP-----LTPGDRVLQFTSFS--FDVsVWEIFGaLLAGATLVVLPEEVRKDPEALADLlae 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 311 -KPTIFCGVPrvyeriyggaiakissggALRKALFQYAynyklrnlekglrQDEAAPRLDRLIFdkikqgfggrvrllfS 389
Cdd:cd05930 183 eGITVLHLTP------------------SLLRLLLQEL-------------ELAALPSLRLVLV---------------G 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 390 GAAPLSRHVEEFLRVTSCSVLSQGYGLTESCGGCLTSIVNEFSMMG---TVGVPYPTIEAR-----LESVPEmgydalsN 461
Cdd:cd05930 217 GEALPPDLVRRWRELLPGARLVNLYGPTEATVDATYYRVPPDDEEDgrvPIGRPIPNTRVYvldenLRPVPP-------G 289
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 462 VPrGEICLRGKTLFSGYFKRQDLTESALVDGWFH-------TGDIGEWQPNGAMKIIDRKKNIFKLSqGEYVAVENLENT 534
Cdd:cd05930 290 VP-GELYIGGAGLARGYLNRPELTAERFVPNPFGpgermyrTGDLVRWLPDGNLEFLGRIDDQVKIR-GYRIELGEIEAA 367
|
490 500 510
....*....|....*....|....*....|..
gi 225428594 535 YSRCPLITS---IWVYGNSFESFLVAVVVPDK 563
Cdd:cd05930 368 LLAHPGVREaavVAREDGDGEKRLVAYVVPDE 399
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
77-531 |
1.21e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 89.63 E-value: 1.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 77 LTYREAYDAALRM-GSAMRSRGVNPGDRCGIYGSNCPEWIIAMEA---CNSQAIPYVPLydsLGANAVEFIINHAEVSIA 152
Cdd:PRK08314 36 ISYRELLEEAERLaGYLQQECGVRKGDRVLLYMQNSPQFVIAYYAilrANAVVVPVNPM---NREEELAHYVTDSGARVA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 153 FVQESKIPAMLTCLPK-------CTSYLKTIISFGKIS-----SSQKEEAEELGVSCFSWEEfallgSLDCELPPKQKT- 219
Cdd:PRK08314 113 IVGSELAPKVAPAVGNlrlrhviVAQYSDYLPAEPEIAvpawlRAEPPLQALAPGGVVAWKE-----ALAAGLAPPPHTa 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 220 ---DICTIMYTSGTTGEPKGVVLSNEAIMAEVLSTdQLLLEtdkvATEEDTYFSFLPLAHV--FDQIMETyCIYKGSSIg 294
Cdd:PRK08314 188 gpdDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGS-VLWSN----STPESVVLAVLPLFHVtgMVHSMNA-PIYAGATV- 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 295 fwgadvrYLMediqelkptifcgvPRVYERIYGGAIA--KISSGGALRKALFQYAynyklrnlekglrqdeAAPRLDRli 372
Cdd:PRK08314 261 -------VLM--------------PRWDREAAARLIEryRVTHWTNIPTMVVDFL----------------ASPGLAE-- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 373 FDKIKqgfggrVRLLFSGAAPLSRHVEEFLRVTSCSVLSQGYGLTESCGGcltSIVNEFSM--MGTVGVPYPTIEARLes 450
Cdd:PRK08314 302 RDLSS------LRYIGGGGAAMPEAVAERLKELTGLDYVEGYGLTETMAQ---THSNPPDRpkLQCLGIPTFGVDARV-- 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 451 vpeMGYDALSNVPR---GEICLRGKTLFSGYFKRQDLTESALV--DG--WFHTGDIGEWQPNGAMKIIDRKKNI-----F 518
Cdd:PRK08314 371 ---IDPETLEELPPgevGEIVVHGPQVFKGYWNRPEATAEAFIeiDGkrFFRTGDLGRMDEEGYFFITDRLKRMinasgF 447
|
490
....*....|...
gi 225428594 519 KLSQGEyvaVENL 531
Cdd:PRK08314 448 KVWPAE---VENL 457
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
220-548 |
1.42e-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: 87.17 E-value: 1.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 220 DICTIMYTSGTTGEPKGVVLSNEaimaEVLSTDQLLLETDKVaTEEDTYFSFLPLAHVFDqimetY------CIYKGSSI 293
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHR----QTLRAAAAWADCADL-TEDDRYLIINPFFHTFG-----YkagivaCLLTGATV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 294 ----GFwgaDVRYLMEDIQELKPTIFCGVPRVYERIYGGAIAKissggalrkalfqyayNYKLRNLekglrqdeaaprld 369
Cdd:cd17638 71 vpvaVF---DVDAILEAIERERITVLPGPPTLFQSLLDHPGRK----------------KFDLSSL-------------- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 370 rlifdkikqgfggrvRLLFSGAAP----LSRHVEEFLrvtSCSVLSQGYGLTESCGGCLTSIVNEFSMMG-TVGVPYPTI 444
Cdd:cd17638 118 ---------------RAAVTGAATvpveLVRRMRSEL---GFETVLTAYGLTEAGVATMCRPGDDAETVAtTCGRACPGF 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 445 EARLESvpemgydalsnvpRGEICLRGKTLFSGYFKRQDLTESAL-VDGWFHTGDIGEWQPNGAMKIIDRKKNIFkLSQG 523
Cdd:cd17638 180 EVRIAD-------------DGEVLVRGYNVMQGYLDDPEATAEAIdADGWLHTGDVGELDERGYLRITDRLKDMY-IVGG 245
|
330 340
....*....|....*....|....*
gi 225428594 524 EYVAVENLENTYSRCPLITSIWVYG 548
Cdd:cd17638 246 FNVYPAEVEGALAEHPGVAQVAVIG 270
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
77-561 |
1.66e-18 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 89.31 E-value: 1.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 77 LTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEwIIAMEAcnsqAIPYV-----PLYDSLGANAVEFIINHAEVSI 151
Cdd:PLN03102 40 FTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPA-MYEMHF----AVPMAgavlnPINTRLDATSIAAILRHAKPKI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 152 AFVQESKIP---AMLTCLPKCTSYLK-TIISFGKISSSQKEEAEELGVSCFSWEEFALLGSLDCELPPKQKTDICTIMYT 227
Cdd:PLN03102 115 LFVDRSFEPlarEVLHLLSSEDSNLNlPVIFIHEIDFPKRPSSEELDYECLIQRGEPTPSLVARMFRIQDEHDPISLNYT 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 228 SGTTGEPKGVVLSNEAIMAEVLSTdqllletdKVATEEDT---YFSFLPLAHVfDQIMETYCIYK--GSSIGFWGADVRY 302
Cdd:PLN03102 195 SGTTADPKGVVISHRGAYLSTLSA--------IIGWEMGTcpvYLWTLPMFHC-NGWTFTWGTAArgGTSVCMRHVTAPE 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 303 LMEDIQELKPTIFCGVPRVYeriyggaiakissggalrkalfqyaynyklRNLEKGLRQDEAaPRldrlifdkikqgfGG 382
Cdd:PLN03102 266 IYKNIEMHNVTHMCCVPTVF------------------------------NILLKGNSLDLS-PR-------------SG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 383 RVRLLFSGAAPLSRHVEEFLRVtSCSVLsQGYGLTESCGGCL----------TSIVNEFSMMGTVGVPYPTiearLESVP 452
Cdd:PLN03102 302 PVHVLTGGSPPPAALVKKVQRL-GFQVM-HAYGLTEATGPVLfcewqdewnrLPENQQMELKARQGVSILG----LADVD 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 453 EMGYDALSNVPR-----GEICLRGKTLFSGYFKRQDLTESALVDGWFHTGDIGEWQPNGAMKIIDRKKNIFkLSQGEYVA 527
Cdd:PLN03102 376 VKNKETQESVPRdgktmGEIVIKGSSIMKGYLKNPKATSEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDII-ISGGENIS 454
|
490 500 510
....*....|....*....|....*....|....
gi 225428594 528 VENLENTysrcplitsIWVYGNSFESFLVAVVVP 561
Cdd:PLN03102 455 SVEVENV---------LYKYPKVLETAVVAMPHP 479
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
77-573 |
5.38e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 87.79 E-value: 5.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 77 LTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQAIPYVPLYDSLGANAVEFIINHAEVSIAFVQE 156
Cdd:PRK06178 59 ITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLALD 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 157 SKIPAMLTCLPKCTsyLKTII--SFGKISSSQ-----KEEAEELGVSCFSWEEfaLLGSLDCE-----LPPKQKTDICTI 224
Cdd:PRK06178 139 QLAPVVEQVRAETS--LRHVIvtSLADVLPAEptlplPDSLRAPRLAAAGAID--LLPALRACtapvpLPPPALDALAAL 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 225 MYTSGTTGEPKGVVLSNEAIMAEVLSTDQLLLetdkVATEEDTYFSFLPLahvfdqimetyciykgssigFWGADvrylm 304
Cdd:PRK06178 215 NYTGGTTGMPKGCEHTQRDMVYTAAAAYAVAV----VGGEDSVFLSFLPE--------------------FWIAG----- 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 305 EDIQELKPtIFCGVPRVYeriyggaIAKISSGGALrkALFQyayNYKLRNLekGLRQDEAA-----PRLDRLIFDKIKQg 379
Cdd:PRK06178 266 ENFGLLFP-LFSGATLVL-------LARWDAVAFM--AAVE---RYRVTRT--VMLVDNAVelmdhPRFAEYDLSSLRQ- 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 380 fggrvrllfSGAAPLSRHVEEFLR-----VTSCSVLSQGYGLTES--CGGCLTSI-VNEFSMMGT---VGVPYPTIEARL 448
Cdd:PRK06178 330 ---------VRVVSFVKKLNPDYRqrwraLTGSVLAEAAWGMTEThtCDTFTAGFqDDDFDLLSQpvfVGLPVPGTEFKI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 449 ESvpemgYDALSNVP---RGEICLRGKTLFSGYFKRQDLTESALVDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSqGEY 525
Cdd:PRK06178 401 CD-----FETGELLPlgaEGEIVVRTPSLLKGYWNKPEATAEALRDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVN-GMS 474
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 225428594 526 VAVENLENTYSRCPLITSIWVYGNSFE---SFLVAVVVP------DKKALEDWAENH 573
Cdd:PRK06178 475 VFPSEVEALLGQHPAVLGSAVVGRPDPdkgQVPVAFVQLkpgadlTAAALQAWCREN 531
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
77-533 |
5.52e-18 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 87.92 E-value: 5.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 77 LTYREAYDAALRMGSAMRSR-GVNPGDRCGIYGSNCPEWIIAMEACNSQAIPYVPLYDSLGANAVEFIINHAEVSIAFVQ 155
Cdd:PRK05620 39 TTFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVAD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 156 ESKIPAMLTCLPKCTSyLKTIISFGKiSSSQKEEAEEL-GVSCFSWEEFALLGSLDCELPPKQKTDICTIMYTSGTTGEP 234
Cdd:PRK05620 119 PRLAEQLGEILKECPC-VRAVVFIGP-SDADSAAAHMPeGIKVYSYEALLDGRSTVYDWPELDETTAAAICYSTGTTGAP 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 235 KGVVLSNEAIMAEVLStdqlLLETDKVATEEDTyfSFL---PLAHVFDQIMETYCIYKGSSIGFWGADVR--YLMEDIQE 309
Cdd:PRK05620 197 KGVVYSHRSLYLQSLS----LRTTDSLAVTHGE--SFLccvPIYHVLSWGVPLAAFMSGTPLVFPGPDLSapTLAKIIAT 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 310 LKPTIFCGVPRVYERIyggaiakissggalrkaLFQYAYNyklrnlekglrqdeaAPRLDRLifdkikqgfggrvRLLFS 389
Cdd:PRK05620 271 AMPRVAHGVPTLWIQL-----------------MVHYLKN---------------PPERMSL-------------QEIYV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 390 GAAPLSRHV----EEFLRVTSCSVlsqgYGLTEScggcltsivnefSMMGTVGVPYPTI--EARLESVPEMGY------- 456
Cdd:PRK05620 306 GGSAVPPILikawEERYGVDVVHV----WGMTET------------SPVGTVARPPSGVsgEARWAYRVSQGRfpasley 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 457 ------DALSNVPR--GEICLRGKTLFSGYFKR-----------------QDLTESALVDGWFHTGDIGEWQPNGAMKII 511
Cdd:PRK05620 370 rivndgQVMESTDRneGEIQVRGNWVTASYYHSpteegggaastfrgedvEDANDRFTADGWLRTGDVGSVTRDGFLTIH 449
|
490 500
....*....|....*....|..
gi 225428594 512 DRKKNIFKlSQGEYVAVENLEN 533
Cdd:PRK05620 450 DRARDVIR-SGGEWIYSAQLEN 470
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
78-541 |
8.47e-18 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 87.11 E-value: 8.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 78 TYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQAIPYVPLYDSLGANAVEFIIN--HAEVSIAFVQ 155
Cdd:PRK06087 51 TYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNkcQAKMFFAPTL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 156 ESKIPAMLTCLP--KCTSYLKTIISFGKISSSQKEEAeeLGVSCFSWEEFAllgsldcELPPKQKTDICTIMYTSGTTGE 233
Cdd:PRK06087 131 FKQTRPVDLILPlqNQLPQLQQIVGVDKLAPATSSLS--LSQIIADYEPLT-------TAITTHGDELAAVLFTSGTEGL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 234 PKGVVLS-NEAIMAEVLSTDQLLLetdkvaTEEDTYFSFLPLAHV---FDQIMETYCIykgssigfwGAdvRYLMEDIqe 309
Cdd:PRK06087 202 PKGVMLThNNILASERAYCARLNL------TWQDVFMMPAPLGHAtgfLHGVTAPFLI---------GA--RSVLLDI-- 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 310 LKPTifcgvprvyeriygGAIAKIS------SGGAlrkALFQYaynyklrNLEKGLRQDEaaPRLDRLifdkikqgfggr 383
Cdd:PRK06087 263 FTPD--------------ACLALLEqqrctcMLGA---TPFIY-------DLLNLLEKQP--ADLSAL------------ 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 384 vRLLFSGAAPL-SRHVEEFLR--VTSCSVlsqgYGLTESCGGCLTSIVNEFS-MMGTVGVPYPTIEARLESvpemgyDAL 459
Cdd:PRK06087 305 -RFFLCGGTTIpKKVARECQQrgIKLLSV----YGSTESSPHAVVNLDDPLSrFMHTDGYAAAGVEIKVVD------EAR 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 460 SNVPRG---EICLRGKTLFSGYFKRQDLTESAL-VDGWFHTGDIGEWQPNGAMKIIDRKKNIFkLSQGEYVAVENLENTY 535
Cdd:PRK06087 374 KTLPPGcegEEASRGPNVFMGYLDEPELTARALdEEGWYYSGDLCRMDEAGYIKITGRKKDII-VRGGENISSREVEDIL 452
|
....*.
gi 225428594 536 SRCPLI 541
Cdd:PRK06087 453 LQHPKI 458
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
77-565 |
8.74e-18 |
|
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: 86.56 E-value: 8.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 77 LTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQAIPYVPLYDSLGANAVEFIINHAEVSIAfvqe 156
Cdd:cd12114 13 LTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLV---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 157 skipamLTCLPKCtsylktiisfgkisssqkeeAEELGVSCFSWEEFALLGSLDCELPPK-QKTDICTIMYTSGTTGEPK 235
Cdd:cd12114 89 ------LTDGPDA--------------------QLDVAVFDVLILDLDALAAPAPPPPVDvAPDDLAYVIFTSGSTGTPK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 236 GVVLSNEAIMAEVLSTDQLLletdkVATEEDTYFSFLPLAhvFDqiMETYCIYKGSSIGfwGA----------DVRYLME 305
Cdd:cd12114 143 GVMISHRAALNTILDINRRF-----AVGPDDRVLALSSLS--FD--LSVYDIFGALSAG--ATlvlpdearrrDPAHWAE 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 306 DIQELKPTIFCGVPrvyeriyggaiakissggalrkALFQYAYNYklrnlekgLRQDEAAPRLDRLIF---DKIKQGFGG 382
Cdd:cd12114 212 LIERHGVTLWNSVP----------------------ALLEMLLDV--------LEAAQALLPSLRLVLlsgDWIPLDLPA 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 383 RVRLLFSGAAplsrhveeflrvtscsVLSQGyGLTEscggclTSI-VNEFSM----MGTVGVPY--PTIEARLESVPEMG 455
Cdd:cd12114 262 RLRALAPDAR----------------LISLG-GATE------ASIwSIYHPIdevpPDWRSIPYgrPLANQRYRVLDPRG 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 456 YDALSNVPrGEICLRGKTLFSGYFKRQDLTESALVD-----GWFHTGDIGEWQPNGAMKIIDRKKNIFKLsQGEYVAVEN 530
Cdd:cd12114 319 RDCPDWVP-GELWIGGRGVALGYLGDPELTAARFVThpdgeRLYRTGDLGRYRPDGTLEFLGRRDGQVKV-RGYRIELGE 396
|
490 500 510
....*....|....*....|....*....|....*..
gi 225428594 531 LENTYSRCPLITS--IWVYGNSFESFLVAVVVPDKKA 565
Cdd:cd12114 397 IEAALQAHPGVARavVVVLGDPGGKRLAAFVVPDNDG 433
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
77-279 |
1.27e-17 |
|
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: 86.37 E-value: 1.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 77 LTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQAIPYVPLYDSLGANAVEFIINHAEVSIAFVQE 156
Cdd:TIGR03098 26 LTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQVAHILADCNVRLLVTSS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 157 SKIPAMLTCLPKCTSyLKTIISFGkisSSQKEEAEELGVSCFSWEEFALLGSLDcELPPKQKTDICTIMYTSGTTGEPKG 236
Cdd:TIGR03098 106 ERLDLLHPALPGCHD-LRTLIIVG---DPAHASEGHPGEEPASWPKLLALGDAD-PPHPVIDSDMAAILYTSGSTGRPKG 180
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 225428594 237 VVLSNEAIMAEVLSTDQLLLEtdkvaTEEDTYFSFLPLAhvFD 279
Cdd:TIGR03098 181 VVLSHRNLVAGAQSVATYLEN-----RPDDRLLAVLPLS--FD 216
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
220-521 |
2.46e-17 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 85.64 E-value: 2.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 220 DICTIMYTSGTTGEPKGVVLSNEAIMAEVLSTDQLLLETDK-----VATEEDTYFSFLPLAHVFDQIMETYCIYKGSSIG 294
Cdd:PRK12492 208 DIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSQLGPdgqplMKEGQEVMIAPLPLYHIYAFTANCMCMMVSGNHN 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 295 FWGADVRYLMEDIQELKPTIFCGVPRVyeriyggaiakissgGALRKALFQYaynyklrnlekglrqdeaaPRLDRLIFD 374
Cdd:PRK12492 288 VLITNPRDIPGFIKELGKWRFSALLGL---------------NTLFVALMDH-------------------PGFKDLDFS 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 375 KIKQGFGGrvrllfsGAAPLSRHVEEFLRVTSCSVLsQGYGLTESCGGCLTSIVNEFSMMGTVGVPYPTieARLESVPEM 454
Cdd:PRK12492 334 ALKLTNSG-------GTALVKATAERWEQLTGCTIV-EGYGLTETSPVASTNPYGELARLGTVGIPVPG--TALKVIDDD 403
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 225428594 455 GyDALSNVPRGEICLRGKTLFSGYFKRQDLTESAL-VDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLS 521
Cdd:PRK12492 404 G-NELPLGERGELCIKGPQVMKGYWQQPEATAEALdAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVS 470
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
214-577 |
5.44e-17 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 84.72 E-value: 5.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 214 PPKQKTDICTIMYTSGTTGEPKGVVLSNEAIMAEVLSTD----QLLLE-TDKVATEedtyfsfLPLAHVFDQIMEtyC-- 286
Cdd:PRK08974 201 PELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQAKaaygPLLHPgKELVVTA-------LPLYHIFALTVN--Cll 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 287 -IYKGSSiGFWGADVRYLMEDIQELKPTIFCGVPRVyeriyggaiakissggalrKALFqyayNYKLRNlekglrqdeaa 365
Cdd:PRK08974 272 fIELGGQ-NLLITNPRDIPGFVKELKKYPFTAITGV-------------------NTLF----NALLNN----------- 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 366 PRLDRLIFDKIKQGFGGrvrllfsgAAPLSRHV-EEFLRVTSCSVLsQGYGLTEsCGGCLT-SIVNEFSMMGTVGVPYPT 443
Cdd:PRK08974 317 EEFQELDFSSLKLSVGG--------GMAVQQAVaERWVKLTGQYLL-EGYGLTE-CSPLVSvNPYDLDYYSGSIGLPVPS 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 444 IEARLesVPEMGYDaLSNVPRGEICLRGKTLFSGYFKRQDLTESALVDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSqG 523
Cdd:PRK08974 387 TEIKL--VDDDGNE-VPPGEPGELWVKGPQVMLGYWQRPEATDEVIKDGWLATGDIAVMDEEGFLRIVDRKKDMILVS-G 462
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 225428594 524 EYVAVENLENTYSRCPLITSIWVYG----NSFESFLVAVVVPDKKALEDWAENH---NVTG 577
Cdd:PRK08974 463 FNVYPNEIEDVVMLHPKVLEVAAVGvpseVSGEAVKIFVVKKDPSLTEEELITHcrrHLTG 523
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
62-533 |
6.57e-17 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 84.42 E-value: 6.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 62 GRRQIIN-SKAGPYVWLTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPE----WIIAM---EACNSqaipyvpLYD 133
Cdd:PRK06018 24 GNREVVTrSVEGPIVRTTYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRhleaWYGIMgigAICHT-------VNP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 134 SLGANAVEFIINHAEVSIAFVQESKIPAMLTCLPKCTSYLKTIISFGKISSSQKEEAEELgvscfSWEEFALLGSLDCEL 213
Cdd:PRK06018 97 RLFPEQIAWIINHAEDRVVITDLTFVPILEKIADKLPSVERYVVLTDAAHMPQTTLKNAV-----AYEEWIAEADGDFAW 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 214 PPKQKTDICTIMYTSGTTGEPKGVVLSNEAIMAEVLSTDQllleTDKV-ATEEDTYFSFLPLAHVFDQIMETYCIYKGSS 292
Cdd:PRK06018 172 KTFDENTAAGMCYTSGTTGDPKGVLYSHRSNVLHALMANN----GDALgTSAADTMLPVVPLFHANSWGIAFSAPSMGTK 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 293 IGFWGA--DVRYLMEDIQELKPTIFCGVPRVYEriyggaiakissggalrkALFQY--AYNYKLRNLEKGLRQDEAAPRL 368
Cdd:PRK06018 248 LVMPGAklDGASVYELLDTEKVTFTAGVPTVWL------------------MLLQYmeKEGLKLPHLKMVVCGGSAMPRS 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 369 DRLIFDKikqgFGGRVRllfsgaaplsrhveeflrvtscsvlsQGYGLTEScggcltsivnefSMMGTVGVPYP-----T 443
Cdd:PRK06018 310 MIKAFED----MGVEVR--------------------------HAWGMTEM------------SPLGTLAALKPpfsklP 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 444 IEARLESVPEMGY-----------DALSNVPR-----GEICLRGKTLFSGYFKRQD--LTEsalvDGWFHTGDIGEWQPN 505
Cdd:PRK06018 348 GDARLDVLQKQGYppfgvemkitdDAGKELPWdgktfGRLKVRGPAVAAAYYRVDGeiLDD----DGFFDTGDVATIDAY 423
|
490 500
....*....|....*....|....*...
gi 225428594 506 GAMKIIDRKKNIFKlSQGEYVAVENLEN 533
Cdd:PRK06018 424 GYMRITDRSKDVIK-SGGEWISSIDLEN 450
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
77-244 |
6.66e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 84.17 E-value: 6.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 77 LTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEAC-NSQAIP------YVP-----LYDSLGANAVefiI 144
Cdd:PRK07798 29 LTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAfKARAVPvnvnyrYVEdelryLLDDSDAVAL---V 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 145 NHAEVSiafvqeskiPAMLTCLPKCTSyLKTIISFGKISSsqkEEAEELGVscfSWEEFALLGSLDCELPPKQKTDIcTI 224
Cdd:PRK07798 106 YEREFA---------PRVAEVLPRLPK-LRTLVVVEDGSG---NDLLPGAV---DYEDALAAGSPERDFGERSPDDL-YL 168
|
170 180
....*....|....*....|
gi 225428594 225 MYTSGTTGEPKGVVLSNEAI 244
Cdd:PRK07798 169 LYTGGTTGMPKGVMWRQEDI 188
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
77-506 |
1.88e-16 |
|
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: 83.75 E-value: 1.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 77 LTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMeacnsQAI-----PYVPLYDSLGANAVEFIINHAEVSI 151
Cdd:COG1020 502 LTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVAL-----LAVlkagaAYVPLDPAYPAERLAYMLEDAGARL 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 152 AFVQEskipAMLTCLPkctsylktiisfgkisssqkeeaeELGVSCFSWEEFALLGSLDCELPPKQK-TDICTIMYTSGT 230
Cdd:COG1020 577 VLTQS----ALAARLP------------------------ELGVPVLALDALALAAEPATNPPVPVTpDDLAYVIYTSGS 628
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 231 TGEPKGVVLSNEAIMAEVLSTDQLLLetdkvATEEDTYFSFLPLAhvFDqimetyciykGSSIGFWGA------------ 298
Cdd:COG1020 629 TGRPKGVMVEHRALVNLLAWMQRRYG-----LGPGDRVLQFASLS--FD----------ASVWEIFGAllsgatlvlapp 691
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 299 ----DVRYLMEDIQELKPTIFCGVPrvyeriyggaiakissggalrkALFQyaynyklrnlekGLRqDEAAPRLDRLifd 374
Cdd:COG1020 692 earrDPAALAELLARHRVTVLNLTP----------------------SLLR------------ALL-DAAPEALPSL--- 733
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 375 kikqgfggRvRLLFSGAAPLSRHVEEFLRVTSCSVLSQGYGLTESCGGCLTSIVNEFSMMG---TVGVPYPTIE-----A 446
Cdd:COG1020 734 --------R-LVLVGGEALPPELVRRWRARLPGARLVNLYGPTETTVDSTYYEVTPPDADGgsvPIGRPIANTRvyvldA 804
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 225428594 447 RLESVPEmgydalsNVPrGEICLRGKTLFSGYFKRQDLTESALVDG--------WFHTGDIGEWQPNG 506
Cdd:COG1020 805 HLQPVPV-------GVP-GELYIGGAGLARGYLNRPELTAERFVADpfgfpgarLYRTGDLARWLPDG 864
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
213-564 |
2.53e-16 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 83.09 E-value: 2.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 213 LPPKQKTDICTIMYTSGTTGEPKGVVLSNEAIMAEVLstdQLLLETDkvATEEDTYFSFLPLAHVFdqimetyciykgss 292
Cdd:PRK06814 787 FCNRDPDDPAVILFTSGSEGTPKGVVLSHRNLLANRA---QVAARID--FSPEDKVFNALPVFHSF-------------- 847
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 293 iGFWGADVRYLMEDIqelkPTIFCGVPRVY----ERIYG-GAIAKIS-----SGGAlrkalfQYAYNYKLRNLekglrqd 362
Cdd:PRK06814 848 -GLTGGLVLPLLSGV----KVFLYPSPLHYriipELIYDtNATILFGtdtflNGYA------RYAHPYDFRSL------- 909
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 363 eaaprldrlifdkikqgfggrvRLLFSGAAPL---SRHV--EEF-LRVTscsvlsQGYGLTESCGG--CLTSIVNEFsmm 434
Cdd:PRK06814 910 ----------------------RYVFAGAEKVkeeTRQTwmEKFgIRIL------EGYGVTETAPViaLNTPMHNKA--- 958
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 435 GTVGVPYPTIEARLESVP--EMGydalsnvprGEICLRGKTLFSGYFKrqdlTES-----ALVDGWFHTGDIGEWQPNGA 507
Cdd:PRK06814 959 GTVGRLLPGIEYRLEPVPgiDEG---------GRLFVRGPNVMLGYLR----AENpgvlePPADGWYDTGDIVTIDEEGF 1025
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 508 MKIIDRKKNIFKLSqGEYV---AVENLENTysrcplitsIWVYGNSfesflVAVVVPDKK 564
Cdd:PRK06814 1026 ITIKGRAKRFAKIA-GEMIslaAVEELAAE---------LWPDALH-----AAVSIPDAR 1070
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
214-515 |
2.54e-16 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 82.70 E-value: 2.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 214 PPKQKTDICTIMYTSGTTGEPKGVVLS--NEAIMAEVLSTDQLLletdkvaTEEDTYFSFLPLAHVFD---QIMETycIY 288
Cdd:PRK07529 208 RPIGPDDVAAYFHTGGTTGMPKLAQHThgNEVANAWLGALLLGL-------GPGDTVFCGLPLFHVNAllvTGLAP--LA 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 289 KGSSI------GFWGADV-RYLMEDIQELKPTIFCGVPRVYeriygGAIAKISSGGAlrkalfqyaynyklrNLekglrq 361
Cdd:PRK07529 279 RGAHVvlatpqGYRGPGViANFWKIVERYRINFLSGVPTVY-----AALLQVPVDGH---------------DI------ 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 362 deaaprldrlifdkikqgfgGRVRLLFSGAAPLSRHV-EEFLRVTSCSVLsQGYGLTEscGGCLTSI--VNEFSMMGTVG 438
Cdd:PRK07529 333 --------------------SSLRYALCGAAPLPVEVfRRFEAATGVRIV-EGYGLTE--ATCVSSVnpPDGERRIGSVG 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 439 VPYPTIEARLESVPEMGyDALSNVPR---GEICLRGKTLFSGYFKRQDLTESALVDGWFHTGDIGEWQPNGAMKIIDRKK 515
Cdd:PRK07529 390 LRLPYQRVRVVILDDAG-RYLRDCAVdevGVLCIAGPNVFSGYLEAAHNKGLWLEDGWLNTGDLGRIDADGYFWLTGRAK 468
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
72-571 |
5.54e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 81.24 E-value: 5.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 72 GPYVWlTYREaYDAAL-RMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQAIPYVPlydslganaVEFIINHAEVs 150
Cdd:PRK07470 29 GDRSW-TWRE-IDARVdALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVP---------TNFRQTPDEV- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 151 iAFVQESKIPAMLTCLPKCTSYLKTIisfgKISSSQKEEAEELGVSCFSWEEFALLGS-LDCELPPKQ--KTDICTIMYT 227
Cdd:PRK07470 97 -AYLAEASGARAMICHADFPEHAAAV----RAASPDLTHVVAIGGARAGLDYEALVARhLGARVANAAvdHDDPCWFFFT 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 228 SGTTGEPKGVVLSNeAIMAEVLsTDQLlleTDKV--ATEEDTYFSFLPLAHvfdqimetyciykgssigfwGADVRYLme 305
Cdd:PRK07470 172 SGTTGRPKAAVLTH-GQMAFVI-TNHL---ADLMpgTTEQDASLVVAPLSH--------------------GAGIHQL-- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 306 diqelkptifCGVPRvyeriygGAIAKISSGGALRKA-LFQYAYNYKLRNL------EKGLRQDEAAPRLDRlifdkikq 378
Cdd:PRK07470 225 ----------CQVAR-------GAATVLLPSERFDPAeVWALVERHRVTNLftvptiLKMLVEHPAVDRYDH-------- 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 379 gfgGRVRLLFSGAAPLSRHVEEFLRVTSCSVLSQGYGLTEsCGGCLTSIVNEF--------SMMGTVGVPYPTIEARLES 450
Cdd:PRK07470 280 ---SSLRYVIYAGAPMYRADQKRALAKLGKVLVQYFGLGE-VTGNITVLPPALhdaedgpdARIGTCGFERTGMEVQIQD 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 451 vpemgyDALSNVP---RGEICLRGKTLFSGYFKRQDLTESALVDGWFHTGDIGEWQPNGAMKIIDRKKNIFkLSQGEYVA 527
Cdd:PRK07470 356 ------DEGRELPpgeTGEICVIGPAVFAGYYNNPEANAKAFRDGWFRTGDLGHLDARGFLYITGRASDMY-ISGGSNVY 428
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 225428594 528 VENLENTYSRCPLITSIWVYGnsfesflvavvVPDKKaledWAE 571
Cdd:PRK07470 429 PREIEEKLLTHPAVSEVAVLG-----------VPDPV----WGE 457
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
77-599 |
5.61e-16 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 81.25 E-value: 5.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 77 LTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQAI---PYVPLYDSlgaNAVEFIINHAEVSIAF 153
Cdd:PRK13295 56 FTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAvlnPLMPIFRE---RELSFMLKHAESKVLV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 154 VQES----KIPAMLTCLPKCTSYLKTII--------SFGKISSSQKeeaeelgvscfsWEEFALLGSLDCELPPKQKtDI 221
Cdd:PRK13295 133 VPKTfrgfDHAAMARRLRPELPALRHVVvvggdgadSFEALLITPA------------WEQEPDAPAILARLRPGPD-DV 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 222 CTIMYTSGTTGEPKGVVLSNEAIMAEVLS-TDQLLLETDKVAteedtyFSFLPLAHVfdqimetyciykgssIGFwgadv 300
Cdd:PRK13295 200 TQLIYTSGTTGEPKGVMHTANTLMANIVPyAERLGLGADDVI------LMASPMAHQ---------------TGF----- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 301 RYLMediqeLKPTIFcGVPRVYERIYGG--AIAKISSGGALrkalFQYAYNYKLRNLEKGlrQDEAAPRLDRLifdkikq 378
Cdd:PRK13295 254 MYGL-----MMPVML-GATAVLQDIWDParAAELIRTEGVT----FTMASTPFLTDLTRA--VKESGRPVSSL------- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 379 gfggrvRLLFSGAAPLSRH-VEEFLRVTSCSVLSqGYGLTEScgGCLTSIVNEFS---MMGTVGVPYPTIEARLESvpem 454
Cdd:PRK13295 315 ------RTFLCAGAPIPGAlVERARAALGAKIVS-AWGMTEN--GAVTLTKLDDPderASTTDGCPLPGVEVRVVD---- 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 455 gyDALSNVPRGEI---CLRGKTLFSGYFKRQDLTESAlVDGWFHTGDIGEWQPNGAMKIIDRKKNIFkLSQGEYVAVENL 531
Cdd:PRK13295 382 --ADGAPLPAGQIgrlQVRGCSNFGGYLKRPQLNGTD-ADGWFDTGDLARIDADGYIRISGRSKDVI-IRGGENIPVVEI 457
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 225428594 532 ENTYSRCPLITSIWVYGNSFESF---LVAVVVP------DKKALEDWAENHNVTGDFksLCENLEarkyILDELNNT 599
Cdd:PRK13295 458 EALLYRHPAIAQVAIVAYPDERLgerACAFVVPrpgqslDFEEMVEFLKAQKVAKQY--IPERLV----VRDALPRT 528
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
78-533 |
1.06e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 80.52 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 78 TYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEACN-SQAIPYVpLYDSLGANAVEFIINHAEVSIAFVQE 156
Cdd:PRK07008 41 TYRDCERRAKQLAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVSgSGAVCHT-INPRLFPEQIAYIVNHAEDRYVLFDL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 157 SKIPAMLTCLPKCtsylKTIISFGKISSSQKEEAEELGVSCFswEEFALLGSLDCELPPKQKTDICTIMYTSGTTGEPKG 236
Cdd:PRK07008 120 TFLPLVDALAPQC----PNVKGWVAMTDAAHLPAGSTPLLCY--ETLVGAQDGDYDWPRFDENQASSLCYTSGTTGNPKG 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 237 VVLSNEAIM----AEVLStDQLLLetdkvaTEEDTYFSFLPLAHVFDQIMETYCIYKGSSIGFWGADV--RYLMEDIQEL 310
Cdd:PRK07008 194 ALYSHRSTVlhayGAALP-DAMGL------SARDAVLPVVPMFHVNAWGLPYSAPLTGAKLVLPGPDLdgKSLYELIEAE 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 311 KPTIFCGVPRVYEriyggaiakissggalrkALFQYAYnyklrnlEKGLRqdeaaprldrliFDKIKqgfggrvRLLFSG 390
Cdd:PRK07008 267 RVTFSAGVPTVWL------------------GLLNHMR-------EAGLR------------FSTLR-------RTVIGG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 391 AAPLSRHVEEFLRVTSCSVLsQGYGLTE-SCGGCLTSIVNEFSMM------------GTV--GVPYPTIEARLESVPEMG 455
Cdd:PRK07008 303 SACPPAMIRTFEDEYGVEVI-HAWGMTEmSPLGTLCKLKWKHSQLpldeqrkllekqGRViyGVDMKIVGDDGRELPWDG 381
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 225428594 456 ydalsnVPRGEICLRGKTLFSGYFKRQDlteSALVDGWFHTGDIGEWQPNGAMKIIDRKKNIFKlSQGEYVAVENLEN 533
Cdd:PRK07008 382 ------KAFGDLQVRGPWVIDRYFRGDA---SPLVDGWFPTGDVATIDADGFMQITDRSKDVIK-SGGEWISSIDIEN 449
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
75-518 |
3.98e-15 |
|
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: 78.82 E-value: 3.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 75 VWLTYREAYDAALRMGSAMRSRGvNPGDRCGIYGSNCPEWIIAMEAC-NSQAIPyVPLYDSLGANAVE---FIINHAEVS 150
Cdd:cd05931 23 ETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGClYAGAIA-VPLPPPTPGRHAErlaAILADAGPR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 151 IAFVQESKIPAMltclpkctsylktiisfgKISSSQKEEAEELGVSCfsWEEFALLGSLDCELPPKQKTDICTIMYTSGT 230
Cdd:cd05931 101 VVLTTAAALAAV------------------RAFAASRPAAGTPRLLV--VDLLPDTSAADWPPPSPDPDDIAYLQYTSGS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 231 TGEPKGVVLSNEAIMAEVLSTDQLLLetdkvATEEDTYFSFLPLAHvfDQIMetyciykgssIGFWGAdvrylmediqel 310
Cdd:cd05931 161 TGTPKGVVVTHRNLLANVRQIRRAYG-----LDPGDVVVSWLPLYH--DMGL----------IGGLLT------------ 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 311 kpTIFCGVPRVY--------------ERI--YGGAIakisSGGAlrkalfQYAYNYKLRNLEkglrqDEAAPRLDrLifd 374
Cdd:cd05931 212 --PLYSGGPSVLmspaaflrrplrwlRLIsrYRATI----SAAP------NFAYDLCVRRVR-----DEDLEGLD-L--- 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 375 kikqgfgGRVRLLFSGAAPLSRH-VEEFLRVTS-----CSVLSQGYGLTESC----------GGCLTSIVNEFSMMGTVG 438
Cdd:cd05931 271 -------SSWRVALNGAEPVRPAtLRRFAEAFApfgfrPEAFRPSYGLAEATlfvsggppgtGPVVLRVDRDALAGRAVA 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 439 VPYPTIEARL-----ESVPEMGY---DALSNVPR-----GEICLRGKTLFSGYFKRQDLTESALV-------DGWFHTGD 498
Cdd:cd05931 344 VAADDPAARElvscgRPLPDQEVrivDPETGRELpdgevGEIWVRGPSVASGYWGRPEATAETFGalaatdeGGWLRTGD 423
|
490 500
....*....|....*....|....*..
gi 225428594 499 IG-----EWQPNGAMK--IIDRKKNIF 518
Cdd:cd05931 424 LGflhdgELYITGRLKdlIIVRGRNHY 450
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
78-548 |
5.11e-15 |
|
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: 77.86 E-value: 5.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 78 TYREAYDAALRMGSAMRS-RGVNPGDRCGIYGSNCPEWIIAMEAcnsqaipyvplYDSLGAnaVEFIINHAEVSIAFVQe 156
Cdd:cd05937 7 TYSETYDLVLRYAHWLHDdLGVQAGDFVAIDLTNSPEFVFLWLG-----------LWSIGA--APAFINYNLSGDPLIH- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 157 skipamltCLPKCTSylKTIISfgkisssqkeeaeelgvscfsweefallgsldcelppkQKTDICTIMYTSGTTGEPKG 236
Cdd:cd05937 73 --------CLKLSGS--RFVIV--------------------------------------DPDDPAILIYTSGTTGLPKA 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 237 VVLSneaiMAEVLSTDQlLLETDKVATEEDTYFSFLPLAHVFDQIMET-YCIYKGSSIG---------FWgadvrylmED 306
Cdd:cd05937 105 AAIS----WRRTLVTSN-LLSHDLNLKNGDRTYTCMPLYHGTAAFLGAcNCLMSGGTLAlsrkfsasqFW--------KD 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 307 IQELKPTIFCGVPRVYERIYGGAIAKissggalrkalfqYAYNYKLR----NlekGLRQDeaaprldrlIFDKIKQGFGG 382
Cdd:cd05937 172 VRDSGATIIQYVGELCRYLLSTPPSP-------------YDRDHKVRvawgN---GLRPD---------IWERFRERFNV 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 383 RVrllfsgaaplsrhVEEFlrvtscsvlsqgYGLTESCGGCLTSIVNEFSmMGTVGVPYPTIEARLESV-------PEMG 455
Cdd:cd05937 227 PE-------------IGEF------------YAATEGVFALTNHNVGDFG-AGAIGHHGLIRRWKFENQvvlvkmdPETD 280
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 456 YDALSN-------VPRGE-------ICLRGKTLFSGYFKRQDLTESALV-------DGWFHTGDIGEWQPNGAMKIIDRK 514
Cdd:cd05937 281 DPIRDPktgfcvrAPVGEpgemlgrVPFKNREAFQGYLHNEDATESKLVrdvfrkgDIYFRTGDLLRQDADGRWYFLDRL 360
|
490 500 510
....*....|....*....|....*....|....
gi 225428594 515 KNIFKLsQGEYVAVENLENTYSRCPLITSIWVYG 548
Cdd:cd05937 361 GDTFRW-KSENVSTTEVADVLGAHPDIAEANVYG 393
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
56-578 |
7.26e-15 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 78.16 E-value: 7.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 56 PKNQMLGRRqiiNSKAGPYVWLTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQAIPYVPlydsl 135
Cdd:PRK12582 63 PDRPWLAQR---EPGHGQWRKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPAAP----- 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 136 ganavefiinhaeVSIAFvqeSKIPAMLTCLPKCTSYLKTIISF---GKISSSQKEEAEELGVSCFSWE---------EF 203
Cdd:PRK12582 135 -------------VSPAY---SLMSHDHAKLKHLFDLVKPRVVFaqsGAPFARALAALDLLDVTVVHVTgpgegiasiAF 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 204 ALLGSLdcelPPKQKTD----------ICTIMYTSGTTGEPKGVvLSNEAIMAEVLSTdQLLLETDKVATEEDTYFSFLP 273
Cdd:PRK12582 199 ADLAAT----PPTAAVAaaiaaitpdtVAKYLFTSGSTGMPKAV-INTQRMMCANIAM-QEQLRPREPDPPPPVSLDWMP 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 274 LAHVFdqimetyciykGSSIGF----WGADVRYL-------------MEDIQELKPTIFCGVPRVYeriyggaiakissg 336
Cdd:PRK12582 273 WNHTM-----------GGNANFngllWGGGTLYIddgkplpgmfeetIRNLREISPTVYGNVPAGY-------------- 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 337 GALRKALfqyaynyklrnlekglRQDEAaprldrlifdkIKQGFGGRVRLLFSGAAPLSRHVEEFLRVTSCS------VL 410
Cdd:PRK12582 328 AMLAEAM----------------EKDDA-----------LRRSFFKNLRLMAYGGATLSDDLYERMQALAVRttghriPF 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 411 SQGYGLTEScGGCLTSIVNEFSMMGTVGVPYPTIEARLesvpemgydalsnVPRG---EICLRGKTLFSGYFKRQDLTES 487
Cdd:PRK12582 381 YTGYGATET-APTTTGTHWDTERVGLIGLPLPGVELKL-------------APVGdkyEVRVKGPNVTPGYHKDPELTAA 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 488 AL-VDGWFHTGDIGEW----QPNGAMKIIDRKKNIFKLSQGEYVAVENLE-NTYSRC-PLITSIWVYGNSfESFLVAVVV 560
Cdd:PRK12582 447 AFdEEGFYRLGDAARFvdpdDPEKGLIFDGRVAEDFKLSTGTWVSVGTLRpDAVAACsPVIHDAVVAGQD-RAFIGLLAW 525
|
570
....*....|....*...
gi 225428594 561 PDKKALEDWAENHNVTGD 578
Cdd:PRK12582 526 PNPAACRQLAGDPDAAPE 543
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
77-562 |
1.13e-14 |
|
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: 76.86 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 77 LTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQAIPYVPLYDSLGANAVEFIINHAEVSIAFVQE 156
Cdd:cd12117 23 LTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAERLAFMLADAGAKVLLTDR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 157 SkIPAMLTCLPkctsylkTIISFGKISSSQKEEAEELGVScfsweefallgsldcelppkqKTDICTIMYTSGTTGEPKG 236
Cdd:cd12117 103 S-LAGRAGGLE-------VAVVIDEALDAGPAGNPAVPVS---------------------PDDLAYVMYTSGSTGRPKG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 237 VVLSNEAIMAEVLSTDQLLLetdkvaTEEDTYFSFLPLAhvFDqimetyciykGSSIGFWGADV---------RYLMEDI 307
Cdd:cd12117 154 VAVTHRGVVRLVKNTNYVTL------GPDDRVLQTSPLA--FD----------ASTFEIWGALLngarlvlapKGTLLDP 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 308 QELKptifcgvprvyERIYGGAIAKIssggALRKALFqyaynyklrnlekglrqdeaaprldRLIFDKIKQGFGGRVRLL 387
Cdd:cd12117 216 DALG-----------ALIAEEGVTVL----WLTAALF-------------------------NQLADEDPECFAGLRELL 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 388 FSGAAPLSRHVEEFLRVTSCSVLSQGYGLTESCGGCLTSIVNEFSMMGT---VGVPYPTIEARLesVPEMGYDALSNVPr 464
Cdd:cd12117 256 TGGEVVSPPHVRRVLAACPGLRLVNGYGPTENTTFTTSHVVTELDEVAGsipIGRPIANTRVYV--LDEDGRPVPPGVP- 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 465 GEICLRGKTLFSGYFKRQDLTESALV-----DG--WFHTGDIGEWQPNGAMKIIDRKKNIFKLsQGEYVAVENLENTYSR 537
Cdd:cd12117 333 GELYVGGDGLALGYLNRPALTAERFVadpfgPGerLYRTGDLARWLPDGRLEFLGRIDDQVKI-RGFRIELGEIEAALRA 411
|
490 500
....*....|....*....|....*...
gi 225428594 538 CPLITSIWVY---GNSFESFLVAVVVPD 562
Cdd:cd12117 412 HPGVREAVVVvreDAGGDKRLVAYVVAE 439
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
218-616 |
1.75e-14 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 76.56 E-value: 1.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 218 KTDICTIMYTSGTTGEPKGVVLSNEAIMAEVLSTdqlLLETDKVATEEDTYFSFLPLAHVFDqIMETYCIY---KGSSIG 294
Cdd:PLN02330 183 QTDLCALPFSSGTTGISKGVMLTHRNLVANLCSS---LFSVGPEMIGQVVTLGLIPFFHIYG-ITGICCATlrnKGKVVV 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 295 FWGADVRYLMEDIQELKPTIFCGVPRVyeriyggaiakissggalrkalfqyaynykLRNLEKGlrqdeaaPRLDRLIFD 374
Cdd:PLN02330 259 MSRFELRTFLNALITQEVSFAPIVPPI------------------------------ILNLVKN-------PIVEEFDLS 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 375 KIKqgfggrVRLLFSGAAPLSRHVEEFLRVTSCSV-LSQGYGLTEScgGCLTSIVNE------FSMMGTVGVPYPTIEAR 447
Cdd:PLN02330 302 KLK------LQAIMTAAAPLAPELLTAFEAKFPGVqVQEAYGLTEH--SCITLTHGDpekghgIAKKNSVGFILPNLEVK 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 448 LESvPEMGYDALSNVPrGEICLRGKTLFSGYFKRQDLTESAL-VDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLsQGEYV 526
Cdd:PLN02330 374 FID-PDTGRSLPKNTP-GELCVRSQCVMQGYYNNKEETDRTIdEDGWLHTGDIGYIDDDGDIFIVDRIKELIKY-KGFQV 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 527 AVENLEntysrcplitSIWVYGNSFESflVAVV-VPDKKAledwaenhnvtGDFKSLCE--NLEARKYILDELNNTGQNh 603
Cdd:PLN02330 451 APAELE----------AILLTHPSVED--AAVVpLPDEEA-----------GEIPAACVviNPKAKESEEDILNFVAAN- 506
|
410
....*....|...
gi 225428594 604 qLKGFERLKAVHL 616
Cdd:PLN02330 507 -VAHYKKVRVVQF 518
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
213-513 |
2.88e-14 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 76.50 E-value: 2.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 213 LPPKQKTDICTIMYTSGTTGEPKGVVLSNEAIMAEVLSTDQLLLetdkvATEEDTYFSFLPLAHVFdqimetyciykGSS 292
Cdd:PRK08633 776 GPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFN-----LRNDDVILSSLPFFHSF-----------GLT 839
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 293 IGFWG--------------ADVRYLMEDIQELKPTIFCGVPrVYERIYggaiakissggalrkalfqyaynykLRNlekg 358
Cdd:PRK08633 840 VTLWLpllegikvvyhpdpTDALGIAKLVAKHRATILLGTP-TFLRLY-------------------------LRN---- 889
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 359 lrqdeaaPRLDRLIFDKIkqgfggrvRLLFSGAAPLSRHVEEFLRVTSCSVLSQGYGLTESCGGCLTSIVNE-------- 430
Cdd:PRK08633 890 -------KKLHPLMFASL--------RLVVAGAEKLKPEVADAFEEKFGIRILEGYGATETSPVASVNLPDVlaadfkrq 954
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 431 -FSMMGTVGVPYPTIEARLesV-PEmgydALSNVPRGE---ICLRGKTLFSGYFKRQDLTESALVD----GWFHTGDIGE 501
Cdd:PRK08633 955 tGSKEGSVGMPLPGVAVRI--VdPE----TFEELPPGEdglILIGGPQVMKGYLGDPEKTAEVIKDidgiGWYVTGDKGH 1028
|
330
....*....|..
gi 225428594 502 WQPNGAMKIIDR 513
Cdd:PRK08633 1029 LDEDGFLTITDR 1040
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
46-513 |
3.83e-14 |
|
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: 75.44 E-value: 3.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 46 EFFSDSVERNPKNQML--GRRQiinskagpyvwLTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEACNS 123
Cdd:cd17655 1 ELFEEQAEKTPDHTAVvfEDQT-----------LTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 124 QAIPYVPLYDSLGANAVEFIINHAEVSIAFVQESkipamltcLPKCTSYLKTIISFgKISSSQKEEAEELGvscfsweef 203
Cdd:cd17655 70 AGGAYLPIDPDYPEERIQYILEDSGADILLTQSH--------LQPPIAFIGLIDLL-DEDTIYHEESENLE--------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 204 allgsldcelPPKQKTDICTIMYTSGTTGEPKGVVLSNEAIMAEVLSTDQLLletdkVATEEDTYFSFLPLAhvFD---- 279
Cdd:cd17655 132 ----------PVSKSDDLAYVIYTSGSTGKPKGVMIEHRGVVNLVEWANKVI-----YQGEHLRVALFASIS--FDasvt 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 280 QIM------ETYCIYKGSSIGfwgaDVRYLMEDIQELKPTIFCGVPRV-----YERIYGG-AIAKISSGGalrkalfqya 347
Cdd:cd17655 195 EIFasllsgNTLYIVRKETVL----DGQALTQYIRQNRITIIDLTPAHlklldAADDSEGlSLKHLIVGG---------- 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 348 ynyklrnlekglrqDEAAPRLdrliFDKIKQGFGGRVRLLFSgaaplsrhveeflrvtscsvlsqgYGLTESCGGCLTSI 427
Cdd:cd17655 261 --------------EALSTEL----AKKIIELFGTNPTITNA------------------------YGPTETTVDASIYQ 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 428 VNEfSMMGTVGVPY--PTIEARLESVPEMGYDALSNVPrGEICLRGKTLFSGYFKRQDLTESALVDGWF-------HTGD 498
Cdd:cd17655 299 YEP-ETDQQVSVPIgkPLGNTRIYILDQYGRPQPVGVA-GELYIGGEGVARGYLNRPELTAEKFVDDPFvpgermyRTGD 376
|
490
....*....|....*
gi 225428594 499 IGEWQPNGAMKIIDR 513
Cdd:cd17655 377 LARWLPDGNIEFLGR 391
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
77-513 |
4.79e-14 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 75.04 E-value: 4.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 77 LTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEACNSqaipyvplydsLGANAVEFIINHAEVSIAFVQE 156
Cdd:PRK05857 42 LRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAK-----------LGAIAVMADGNLPIAAIERFCQ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 157 SKIPAMLTCLPKC---TSYLKTIISfgKISSSQKEEAEELGVSCFSWEEFALLGSLDcelppKQKTDICTIMYTSGTTGE 233
Cdd:PRK05857 111 ITDPAAALVAPGSkmaSSAVPEALH--SIPVIAVDIAAVTRESEHSLDAASLAGNAD-----QGSEDPLAMIFTSGTTGE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 234 PKGVVLSNEAIMA--EVLSTDQLLLeTDKVATEedTYFSFLPLAHVFDQIMETYCIYKGSSIGFWGADVRYLMEDIQELK 311
Cdd:PRK05857 184 PKAVLLANRTFFAvpDILQKEGLNW-VTWVVGE--TTYSPLPATHIGGLWWILTCLMHGGLCVTGGENTTSLLEILTTNA 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 312 PTIFCGVPRVYERIyggaIAKISSGGALRKALfqyaynyklrnlekglrqdeaaprldRLIfdkikqGFGGrvrllfsga 391
Cdd:PRK05857 261 VATTCLVPTLLSKL----VSELKSANATVPSL--------------------------RLV------GYGG--------- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 392 aplSRHVEEFLRVTSCSVL--SQGYGLTES-CGG-CLTSIVNEFSMM--GTVGVPYPTIEARLEsvPEMG-----YDALS 460
Cdd:PRK05857 296 ---SRAIAADVRFIEATGVrtAQVYGLSETgCTAlCLPTDDGSIVKIeaGAVGRPYPGVDVYLA--ATDGigptaPGAGP 370
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 225428594 461 NVPRGEICLRGKTLFSGYFKRQDLTESALVDGWFHTGDIGEWQPNGAMKIIDR 513
Cdd:PRK05857 371 SASFGTLWIKSPANMLGYWNNPERTAEVLIDGWVNTGDLLERREDGFFYIKGR 423
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
224-571 |
5.92e-14 |
|
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: 73.46 E-value: 5.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 224 IMYTSGTTGEPKGVVLSNEAIMAEVLSTDQLLletdkVATEEDTYFSFLPLAHVFDQIMETYCIYKGssigfwGADV--- 300
Cdd:cd17637 5 IIHTAAVAGRPRGAVLSHGNLIAANLQLIHAM-----GLTEADVYLNMLPLFHIAGLNLALATFHAG------GANVvme 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 301 RY----LMEDIQELKPTIFCGVPRVYERIYGGAIAKISSGGALRKALfqyaynyklrnlekGLRQDEAaprldrlifdki 376
Cdd:cd17637 74 KFdpaeALELIEEEKVTLMGSFPPILSNLLDAAEKSGVDLSSLRHVL--------------GLDAPET------------ 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 377 kqgfggrvrllfsgaaplsrhVEEFLRVTSCSVLSqGYGLTESCGGCLTSIVNEFSmmGTVGVPYPTIEARLesVPEMGY 456
Cdd:cd17637 128 ---------------------IQRFEETTGATFWS-LYGQTETSGLVTLSPYRERP--GSAGRPGPLVRVRI--VDDNDR 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 457 DalsnVPR---GEICLRGKTLFSGYFKRQDLTESALVDGWFHTGDIGEWQPNGAMKIIDRK--KNIFKlSQGEYVAVENL 531
Cdd:cd17637 182 P----VPAgetGEIVVRGPLVFQGYWNLPELTAYTFRNGWHHTGDLGRFDEDGYLWYAGRKpeKELIK-PGGENVYPAEV 256
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 225428594 532 ENTYSRCPLITSIWVYGnsfesflvavvVPDKKaledWAE 571
Cdd:cd17637 257 EKVILEHPAIAEVCVIG-----------VPDPK----WGE 281
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
77-607 |
1.07e-13 |
|
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: 73.54 E-value: 1.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 77 LTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEACNSqaipyvplydsLGAnavefiinhaevsiafvqe 156
Cdd:cd05940 4 LTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVK-----------IGA------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 157 skIPAMltclpkctsylktiisfgkISSSQKEEAeelgvscfsweefaLLGSLDCELPPKQKTDICTIMYTSGTTGEPKG 236
Cdd:cd05940 54 --VAAL-------------------INYNLRGES--------------LAHCLNVSSAKHLVVDAALYIYTSGTTGLPKA 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 237 VVLSNEAI--MAEVLSTDQLLLEtdkvateEDTYFSFLPLAHVFDQIME-TYCIYKGSSI---------GFWgadvrylm 304
Cdd:cd05940 99 AIISHRRAwrGGAFFAGSGGALP-------SDVLYTCLPLYHSTALIVGwSACLASGATLvirkkfsasNFW-------- 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 305 EDIQELKPTIFcgvprvyerIYGGAIakissggaLRKALFQYAYNY----KLRN-LEKGLRQDeaaprldrlIFDKIKQG 379
Cdd:cd05940 164 DDIRKYQATIF---------QYIGEL--------CRYLLNQPPKPTerkhKVRMiFGNGLRPD---------IWEEFKER 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 380 FGgrvrllfsgaaplSRHVEEFlrvtscsvlsqgYGLTEscggCLTSIVNEFSMMGTVGV---------PYPTIEARLES 450
Cdd:cd05940 218 FG-------------VPRIAEF------------YAATE----GNSGFINFFGKPGAIGRnpsllrkvaPLALVKYDLES 268
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 451 V----PEMGYdaLSNVPRGE----IC-LRGKTLFSGYFKRQDLTESALV------DGWFHTGDIGEWQPNGAMKIIDRKK 515
Cdd:cd05940 269 GepirDAEGR--CIKVPRGEpgllISrINPLEPFDGYTDPAATEKKILRdvfkkgDAWFNTGDLMRLDGEGFWYFVDRLG 346
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 516 NIFKLsQGEYVAVENLENTYSRCPLITSIWVYGnsfesflvaVVVPDKK------ALEDWAENH-NVTGDFKSLCENLE- 587
Cdd:cd05940 347 DTFRW-KGENVSTTEVAAVLGAFPGVEEANVYG---------VQVPGTDgragmaAIVLQPNEEfDLSALAAHLEKNLPg 416
|
570 580
....*....|....*....|....
gi 225428594 588 -ARKY---ILDELNNTGQNHQLKG 607
Cdd:cd05940 417 yARPLflrLQPEMEITGTFKQQKV 440
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
30-271 |
1.54e-13 |
|
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: 73.84 E-value: 1.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 30 AENGLLEVPKGMESPwEFFSDSvERNPKNQMLGRRQ------IINSKAGPYVWLTYREAYDAALRMGSAMRSRGVNPGDR 103
Cdd:cd05943 48 PYDVVVVSGRIMPGA-RWFPGA-RLNYAENLLRHADaddpaaIYAAEDGERTEVTWAELRRRVARLAAALRALGVKPGDR 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 104 CGIYGSNCPEWIIAMEACNS----------------------QAIPYVplydSLGANAVEF---IINHAEvsiafvqesK 158
Cdd:cd05943 126 VAGYLPNIPEAVVAMLATASigaiwsscspdfgvpgvldrfgQIEPKV----LFAVDAYTYngkRHDVRE---------K 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 159 IPAMLTCLPkctSYLKTIIsfgkISSSQKEEAEELGVS--CFSWEEFALLGSlDCELPPKQK--TDICTIMYTSGTTGEP 234
Cdd:cd05943 193 VAELVKGLP---SLLAVVV----VPYTVAAGQPDLSKIakALTLEDFLATGA-AGELEFEPLpfDHPLYILYSSGTTGLP 264
|
250 260 270
....*....|....*....|....*....|....*..
gi 225428594 235 KGVVLSNEAIMAEVLStdQLLLETDkvATEEDTYFSF 271
Cdd:cd05943 265 KCIVHGAGGTLLQHLK--EHILHCD--LRPGDRLFYY 297
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
220-517 |
2.03e-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: 72.13 E-value: 2.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 220 DICTIMYTSGTTGEPKGV--VLSNEAIMAEVLSTDQLLletdkvaTEEDTYFSFLPLAHVFDQIMETYC-IYKGSSI--- 293
Cdd:cd05944 3 DVAAYFHTGGTTGTPKLAqhTHSNEVYNAWMLALNSLF-------DPDDVLLCGLPLFHVNGSVVTLLTpLASGAHVvla 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 294 ------------GFWGADVRYlmediqelKPTIFCGVPRVYeriyggaiakissggalrKALFQYAYNYKLRNLekglrq 361
Cdd:cd05944 76 gpagyrnpglfdNFWKLVERY--------RITSLSTVPTVY------------------AALLQVPVNADISSL------ 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 362 deaaprldrlifdkikqgfggrvRLLFSGAAPLS----RHVEEFLRVTSCsvlsQGYGLTEscGGCLTSIV--NEFSMMG 435
Cdd:cd05944 124 -----------------------RFAMSGAAPLPvelrARFEDATGLPVV----EGYGLTE--ATCLVAVNppDGPKRPG 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 436 TVGVPYPTIEARLESVpemgyDALSNVPR-------GEICLRGKTLFSGYFKRQDLTESALVDGWFHTGDIGEWQPNGAM 508
Cdd:cd05944 175 SVGLRLPYARVRIKVL-----DGVGRLLRdcapdevGEICVAGPGVFGGYLYTEGNKNAFVADGWLNTGDLGRLDADGYL 249
|
....*....
gi 225428594 509 KIIDRKKNI 517
Cdd:cd05944 250 FITGRAKDL 258
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
215-532 |
2.24e-13 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 73.59 E-value: 2.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 215 PKQKTDICTIMYTSGTTGEPKGVVLSNEAIMAEVlstDQLLLETDkvATEEDTYFSFLPLAHVFdqimetyciykGSSIG 294
Cdd:PRK08043 361 KQQPEDAALILFTSGSEGHPKGVVHSHKSLLANV---EQIKTIAD--FTPNDRFMSALPLFHSF-----------GLTVG 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 295 FW-----GADVrYLMEdiqelKPTIFCGVPR-VYER----IYGgaiakiSSGGALRKALFQYAYN-YKLRNLEKGlrQDE 363
Cdd:PRK08043 425 LFtplltGAEV-FLYP-----SPLHYRIVPElVYDRnctvLFG------TSTFLGNYARFANPYDfARLRYVVAG--AEK 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 364 AAPRLDRLIFDKikqgFGgrVRLLfsgaaplsrhveeflrvtscsvlsQGYGLTEsCGGCLTSIVNEFSMMGTVGVPYPT 443
Cdd:PRK08043 491 LQESTKQLWQDK----FG--LRIL------------------------EGYGVTE-CAPVVSINVPMAAKPGTVGRILPG 539
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 444 IEARLESVP--EMGydalsnvprGEICLRGKTLFSGYFKRQ----------DLTESALVDGWFHTGDIGEWQPNGAMKII 511
Cdd:PRK08043 540 MDARLLSVPgiEQG---------GRLQLKGPNIMNGYLRVEkpgvlevptaENARGEMERGWYDTGDIVRFDEQGFVQIQ 610
|
330 340
....*....|....*....|.
gi 225428594 512 DRKKNIFKLSqGEYVAVENLE 532
Cdd:PRK08043 611 GRAKRFAKIA-GEMVSLEMVE 630
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
91-568 |
3.50e-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: 341246 [Multi-domain] Cd Length: 457 Bit Score: 72.09 E-value: 3.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 91 SAMRSRGVNPGDRCGIYGSNCPEWI-----IAMEACNSQAIpYVPLYDSLGANAVEFIINHAEVSIAFVQE---SKIPAM 162
Cdd:cd05922 8 SALLEAGGVRGERVVLILPNRFTYIelsfaVAYAGGRLGLV-FVPLNPTLKESVLRYLVADAGGRIVLADAgaaDRLRDA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 163 LTCLPKCTSYLKT--IISFGKISSSQKEEAEELGVscfsweefallgsldcelppkqktdictIMYTSGTTGEPKGVVLS 240
Cdd:cd05922 87 LPASPDPGTVLDAdgIRAARASAPAHEVSHEDLAL----------------------------LLYTSGSTGSPKLVRLS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 241 NEAIMAEVLSTDQLLletdkVATEEDTYFSFLPLAHVFDQIMETYCIYKGSSI----------GFWgadvrylmEDIQEL 310
Cdd:cd05922 139 HQNLLANARSIAEYL-----GITADDRALTVLPLSYDYGLSVLNTHLLRGATLvltndgvlddAFW--------EDLREH 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 311 KPTIFCGVPRVYEriyggaiakissggalrkalfqyaynyklrnlekglrqdeaapRLDRLIFDKIK-------QGFGGR 383
Cdd:cd05922 206 GATGLAGVPSTYA-------------------------------------------MLTRLGFDPAKlpslrylTQAGGR 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 384 VRllfsgAAPLSRhVEEFLRVTSCSVLsqgYGLTEsCGGCLTSIVNE--FSMMGTVGVPYPtiEARLESVPEMGYDALSN 461
Cdd:cd05922 243 LP-----QETIAR-LRELLPGAQVYVM---YGQTE-ATRRMTYLPPEriLEKPGSIGLAIP--GGEFEILDDDGTPTPPG 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 462 VPrGEICLRGKTLFSGYFKR-QDLTESALVDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSqGEYVAVENLENTYSRCPL 540
Cdd:cd05922 311 EP-GEIVHRGPNVMKGYWNDpPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLF-GNRISPTEIEAAARSIGL 388
|
490 500 510
....*....|....*....|....*....|.
gi 225428594 541 ITSIWVYG---NSFESFLVAVVVPDKKALED 568
Cdd:cd05922 389 IIEAAAVGlpdPLGEKLALFVTAPDKIDPKD 419
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
77-571 |
3.76e-13 |
|
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: 71.99 E-value: 3.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 77 LTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQAIPYVPLYDSLGANAVEFIINHAEVSIAFVQE 156
Cdd:cd17651 21 LTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFMLADAGPVLVLTHP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 157 SKIPAMltclpkctsylktiisfgkisssqkeEAEELGVSCFSWEEFALLGSLDCElPPKQKTDICTIMYTSGTTGEPKG 236
Cdd:cd17651 101 ALAGEL--------------------------AVELVAVTLLDQPGAAAGADAEPD-PALDADDLAYVIYTSGSTGRPKG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 237 VVLSNeaimAEVLSTDQLLletdkvateeDTYFSFLPLAHVFdQImetyciykgSSIGFwgaDVrylmeDIQELKPTIFC 316
Cdd:cd17651 154 VVMPH----RSLANLVAWQ----------ARASSLGPGARTL-QF---------AGLGF---DV-----SVQEIFSTLCA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 317 G----VPRVYERIYGGAIAKISSGGALRKALFQYAYnykLRNLekglrqDEAAPRLDRlifdkikqgFGGRVRLLFSGAA 392
Cdd:cd17651 202 GatlvLPPEEVRTDPPALAAWLDEQRISRVFLPTVA---LRAL------AEHGRPLGV---------RLAALRYLLTGGE 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 393 PLSRH--VEEFLRVTSCSVLSQGYGLTES---CGGCLTSIVNEFSMMGTVGVPYPTIE-----ARLESVPemgydalSNV 462
Cdd:cd17651 264 QLVLTedLREFCAGLPGLRLHNHYGPTEThvvTALSLPGDPAAWPAPPPIGRPIDNTRvyvldAALRPVP-------PGV 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 463 PrGEICLRGKTLFSGYFKRQDLTESALVDGWF-------HTGDIGEWQPNGAMKIIDR-----KKNIFKLSQGEyvaven 530
Cdd:cd17651 337 P-GELYIGGAGLARGYLNRPELTAERFVPDPFvpgarmyRTGDLARWLPDGELEFLGRaddqvKIRGFRIELGE------ 409
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 225428594 531 LENTYSRCPLITSIWVYG---NSFESFLVAVVVPDKKALEDWAE 571
Cdd:cd17651 410 IEAALARHPGVREAVVLAredRPGEKRLVAYVVGDPEAPVDAAE 453
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
220-639 |
4.47e-13 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 72.14 E-value: 4.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 220 DICTIMYTSGTTGEPKGVVLSNEAIMAEVLStdqllletdKVA----TEEDTYFSFLPLAHV--FDQIMeTYCIYKGSSI 293
Cdd:PLN02860 173 DAVLICFTSGTTGRPKGVTISHSALIVQSLA---------KIAivgyGEDDVYLHTAPLCHIggLSSAL-AMLMVGACHV 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 294 GFWGADVRYLMEDIQELKPTIFCGVPrvyeriyggaiakissggALRKALFQYAYNYKLRNLEKGLRqdeaaprldrlif 373
Cdd:PLN02860 243 LLPKFDAKAALQAIKQHNVTSMITVP------------------AMMADLISLTRKSMTWKVFPSVR------------- 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 374 dKIKQGFGGRVRLLFSGAaplsrhVEEFlrvtSCSVLSQGYGLTESCGG----------CLTSIVNEFSMMGT------- 436
Cdd:PLN02860 292 -KILNGGGSLSSRLLPDA------KKLF----PNAKLFSAYGMTEACSSltfmtlhdptLESPKQTLQTVNQTksssvhq 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 437 -----VGVPYPTIEARLesvpemGYDALSNVprGEICLRGKTLFSGYFKRQDLTESALV-DGWFHTGDIGEWQPNGAMKI 510
Cdd:PLN02860 361 pqgvcVGKPAPHVELKI------GLDESSRV--GRILTRGPHVMLGYWGQNSETASVLSnDGWLDTGDIGWIDKAGNLWL 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 511 IDRKKNIFKlSQGEYVAVENLENTYSRCPLITSIWVYGNSfESFLVAVVVPDKKALEDWAENHNVTGDFK---SLCEnle 587
Cdd:PLN02860 433 IGRSNDRIK-TGGENVYPEEVEAVLSQHPGVASVVVVGVP-DSRLTEMVVACVRLRDGWIWSDNEKENAKknlTLSS--- 507
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 225428594 588 arkyilDELNNTGQNHQLKGFERLKAVHLDPNPFDierdlVTPTFKLKRPQL 639
Cdd:PLN02860 508 ------ETLRHHCREKNLSRFKIPKLFVQWRKPFP-----LTTTGKIRRDEV 548
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
78-548 |
5.52e-13 |
|
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: 71.31 E-value: 5.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 78 TYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIA-MEACNSQAIPyVPLYDSLGANAVEFIINHAEVSIAFVQE 156
Cdd:cd05971 8 TFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAhIAILRSGAIA-VPLFALFGPEALEYRLSNSGASALVTDG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 157 SKIPAMltclpkctsylktiisfgkisssqkeeaeelgvscfsweefallgsldcelppkqktdictIMYTSGTTGEPKG 236
Cdd:cd05971 87 SDDPAL-------------------------------------------------------------IIYTSGTTGPPKG 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 237 VVLSNEAIMAEvLSTDQLlletdkvateedtYFSFLPlahvfdqiMETYCIYKGSSIGFWGA--DVrylmediqeLKPTI 314
Cdd:cd05971 106 ALHAHRVLLGH-LPGVQF-------------PFNLFP--------RDGDLYWTPADWAWIGGllDV---------LLPSL 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 315 FCGVPRVYERiyggaIAKISSggalrKALFQYAYNYKLRN--LEKglrqdeAAPRLDRLIFDKIKQgFGGRVRLLFSGAA 392
Cdd:cd05971 155 YFGVPVLAHR-----MTKFDP-----KAALDLMSRYGVTTafLPP------TALKMMRQQGEQLKH-AQVKLRAIATGGE 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 393 PLSRHVEEFLRVTSCSVLSQGYGLTEsCGGCLTSIVNEFSMM-GTVGVPYPTIEARLESvpemgyDALSNVP---RGEIC 468
Cdd:cd05971 218 SLGEELLGWAREQFGVEVNEFYGQTE-CNLVIGNCSALFPIKpGSMGKPIPGHRVAIVD------DNGTPLPpgeVGEIA 290
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 469 LR--GKTLFSGYFKRQDLTESALVDGWFHTGDIGEWQPNGAMKIIDRKKNIFKlSQGEYVAVENLENTYSRCPLITSIWV 546
Cdd:cd05971 291 VElpDPVAFLGYWNNPSATEKKMAGDWLLTGDLGRKDSDGYFWYVGRDDDVIT-SSGYRIGPAEIEECLLKHPAVLMAAV 369
|
..
gi 225428594 547 YG 548
Cdd:cd05971 370 VG 371
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
72-517 |
1.43e-12 |
|
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: 70.21 E-value: 1.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 72 GPYVWLTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQAIPYVPLydSLGANAvefiiNHAEVSI 151
Cdd:cd05908 11 KKEKFVSYRHLREEALGYLGALQELGIKPGQEVVFQITHNNKFLYLFWACLLGGMIAVPV--SIGSNE-----EHKLKLN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 152 AFVQESKIPAMLTCLPKctsylktiisfgkisssQKEEAEELGVscfsweefallgsldcelppkqktdictIMYTSGTT 231
Cdd:cd05908 84 KVWNTLKNPYLITEEEV-----------------LCELADELAF----------------------------IQFSSGST 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 232 GEPKGVVLSNEAIMAEVLStdqLLLETDkvATEEDTYFSFLPLAHVFDQI-METYCIYKGSSigfwgadvRYLMediqel 310
Cdd:cd05908 119 GDPKGVMLTHENLVHNMFA---ILNSTE--WKTKDRILSWMPLTHDMGLIaFHLAPLIAGMN--------QYLM------ 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 311 kPT-IFCGVPRVYeriyggaIAKISSGGALRKALFQYAYNYKLRNLekglrQDEAAPRLDRlifdkikqgfgGRVRLLFS 389
Cdd:cd05908 180 -PTrLFIRRPILW-------LKKASEHKATIVSSPNFGYKYFLKTL-----KPEKANDWDL-----------SSIRMILN 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 390 GAAPLSRHV-EEFLRVTSCSVLSQG-----YGLTE-SCGGCLTSIVNEFSMMG------TVGVPYPTI---EARLESVPE 453
Cdd:cd05908 236 GAEPIDYELcHEFLDHMSKYGLKRNailpvYGLAEaSVGASLPKAQSPFKTITlgrrhvTHGEPEPEVdkkDSECLTFVE 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 454 MGYdALSN------------VPR---GEICLRGKTLFSGYFKRQDLTESALV-DGWFHTGDIGeWQPNGAMKIIDRKKNI 517
Cdd:cd05908 316 VGK-PIDEtdiricdednkiLPDgyiGHIQIRGKNVTPGYYNNPEATAKVFTdDGWLKTGDLG-FIRNGRLVITGREKDI 393
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
77-565 |
1.51e-12 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 70.30 E-value: 1.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 77 LTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQAIPYVPLYDSLGANAVEFIINHAEVSIAFVQE 156
Cdd:PRK05852 44 ISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLIDA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 157 S----KIPAMLTCLPKCTSYLKTIISFGKISSSQKEEAEELGVscfsweefallgslDCELPPKQKTDICTIMYTSGTTG 232
Cdd:PRK05852 124 DgphdRAEPTTRWWPLTVNVGGDSGPSGGTLSVHLDAATEPTP--------------ATSTPEGLRPDDAMIMFTGGTTG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 233 EPKGVVLSNEAIMAEVLStdqllLETDKVATEEDTYFSFLPLAHVFDQIMETYCIYKGSSIGFWGADVRY----LMEDIQ 308
Cdd:PRK05852 190 LPKMVPWTHANIASSVRA-----IITGYRLSPRDATVAVMPLYHGHGLIAALLATLASGGAVLLPARGRFsahtFWDDIK 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 309 ELKPTIFCGVPrvyeriyggAIAKIssggalrkaLFQyaynyklRNLEKGLRQDEAAPRLDRlifdkikqgfggrvrllf 388
Cdd:PRK05852 265 AVGATWYTAVP---------TIHQI---------LLE-------RAATEPSGRKPAALRFIR------------------ 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 389 SGAAPLSRHVEEFLRVTSCSVLSQGYGLTESCGGCLTSIVNEFSM----MGTVGVPYPTIEARLESVpemGYDALSNVPR 464
Cdd:PRK05852 302 SCSAPLTAETAQALQTEFAAPVVCAFGMTEATHQVTTTQIEGIGQtenpVVSTGLVGRSTGAQIRIV---GSDGLPLPAG 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 465 --GEICLRGKTLFSGYFKRQDLTESALVDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSqGEYVAVENLENTYSRCPLIT 542
Cdd:PRK05852 379 avGEVWLRGTTVVRGYLGDPTITAANFTDGWLRTGDLGSLSAAGDLSIRGRIKELINRG-GEKISPERVEGVLASHPNVM 457
|
490 500
....*....|....*....|....*.
gi 225428594 543 SIWVYGNSFESF---LVAVVVPDKKA 565
Cdd:PRK05852 458 EAAVFGVPDQLYgeaVAAVIVPRESA 483
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
77-517 |
1.57e-12 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 70.42 E-value: 1.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 77 LTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEACN-SQAIPY-VPLYDSLGANAvefiinhaevsiAFV 154
Cdd:PRK09192 50 LPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQyAGLVPVpLPLPMGFGGRE------------SYI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 155 QesKIPAMLT-CLPKCTSYLKTIISF-GKISSSQKeeaeelGVSCFSWEEFALLGSLDCELPPKQKTDICTIMYTSGTTG 232
Cdd:PRK09192 118 A--QLRGMLAsAQPAAIITPDELLPWvNEATHGNP------LLHVLSHAWFKALPEADVALPRPTPDDIAYLQYSSGSTR 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 233 EPKGVVLSNEAIMAEV--LSTDQLLLEtdkvatEEDTYFSFLPLAHvfDQIMetyciykgssIGFWGA------DVRYLm 304
Cdd:PRK09192 190 FPRGVIITHRALMANLraISHDGLKVR------PGDRCVSWLPFYH--DMGL----------VGFLLTpvatqlSVDYL- 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 305 ediqelkPT-IFCGVPRVYERIYGGAIAKISsggalrkalFQYAYNYKL--RNLEKglrQDEAAprLD----RLifdkik 377
Cdd:PRK09192 251 -------PTrDFARRPLQWLDLISRNRGTIS---------YSPPFGYELcaRRVNS---KDLAE--LDlscwRV------ 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 378 QGFGGR-VRllfsgAAPLSRHVEEFLRVT-SCSVLSQGYGLTESC---------GGCLTSIVNEFSMMGT-VGVPYPTIE 445
Cdd:PRK09192 304 AGIGADmIR-----PDVLHQFAEAFAPAGfDDKAFMPSYGLAEATlavsfsplgSGIVVEEVDRDRLEYQgKAVAPGAET 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 446 ARLES-------VPEMGY----DALSNVPR---GEICLRGKTLFSGYFKRQDLTESALVDGWFHTGDIGeWQPNGAMKII 511
Cdd:PRK09192 379 RRVRTfvncgkaLPGHEIeirnEAGMPLPErvvGHICVRGPSLMSGYFRDEESQDVLAADGWLDTGDLG-YLLDGYLYIT 457
|
....*.
gi 225428594 512 DRKKNI 517
Cdd:PRK09192 458 GRAKDL 463
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
77-571 |
1.62e-12 |
|
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: 69.80 E-value: 1.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 77 LTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQAIPYVPLYDSLGANAVEFIINHAEVSIAFVQe 156
Cdd:cd17650 13 LTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLEDSGAKLLLTQ- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 157 skipamltclPKCTSYlktiisfgkisssqkeeaeelgvscfsweefallgsldcelppkqktdictIMYTSGTTGEPKG 236
Cdd:cd17650 92 ----------PEDLAY---------------------------------------------------VIYTSGTTGKPKG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 237 VVLSNEAIMAEVLSTDQLL-LETDKVATEEDTYFSFLPLAHVFDQIMETyciykGSSIGFWGADVRY----LMEDIQELK 311
Cdd:cd17650 111 VMVEHRNVAHAAHAWRREYeLDSFPVRLLQMASFSFDVFAGDFARSLLN-----GGTLVICPDEVKLdpaaLYDLILKSR 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 312 PTIFCGVPrvyeriyggaiakissggALRKALFQYAYNYKLRnlekglrqdeaaprLDRLifdkikqgfggRVRLLFSGA 391
Cdd:cd17650 186 ITLMESTP------------------ALIRPVMAYVYRNGLD--------------LSAM-----------RLLIVGSDG 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 392 APLSRHVEEFLRVTSCSVLSQGYGLTESCggcLTSIVNEFSM-------MGTVGVPYPT-----IEARLESVPEMGYdal 459
Cdd:cd17650 223 CKAQDFKTLAARFGQGMRIINSYGVTEAT---IDSTYYEEGRdplgdsaNVPIGRPLPNtamyvLDERLQPQPVGVA--- 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 460 snvprGEICLRGKTLFSGYFKRQDLTESALVDGWF-------HTGDIGEWQPNGAMKIIDRKKNIFKLsQGEYVAVENLE 532
Cdd:cd17650 297 -----GELYIGGAGVARGYLNRPELTAERFVENPFapgermyRTGDLARWRADGNVELLGRVDHQVKI-RGFRIELGEIE 370
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 225428594 533 NTYSRCPLITSIWV---YGNSFESFLVAVVVPDKKAleDWAE 571
Cdd:cd17650 371 SQLARHPAIDEAVVavrEDKGGEARLCAYVVAAATL--NTAE 410
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
220-563 |
3.50e-12 |
|
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: 67.82 E-value: 3.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 220 DICTIMYTSGTTGEPKGVVLSNEAIMAEVLSTDQLLLetdkvATEEDTYFSFLPLAHVFDQIMETYCIYKGSS-IGFWGA 298
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERSWIESFVCNEDLFN-----ISGEDAILAPGPLSHSLFLYGAISALYLGGTfIGQRKF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 299 DVRYLMEDIQELKPTIFCGVP-------RVYERIYggAIAKISSGGALrkalfqyaynyklrnlekglrqdeaaprLDRL 371
Cdd:cd17633 76 NPKSWIRKINQYNATVIYLVPtmlqalaRTLEPES--KIKSIFSSGQK----------------------------LFES 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 372 IFDKIKQGFGGRVRLLFSGAAPLSrhveeFLrvtscsvlsqgygltescggclTSIVNEFSM-MGTVGVPYPTIEARLEs 450
Cdd:cd17633 126 TKKKLKNIFPKANLIEFYGTSELS-----FI----------------------TYNFNQESRpPNSVGRPFPNVEIEIR- 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 451 vpemgydALSNVPRGEICLRGKTLFSGYFKRQDLTesalVDGWFHTGDIGEWQPNGAMKIIDRKKNIFkLSQGEYVAVEN 530
Cdd:cd17633 178 -------NADGGEIGKIFVKSEMVFSGYVRGGFSN----PDGWMSVGDIGYVDEEGYLYLVGRESDMI-IIGGINIFPTE 245
|
330 340 350
....*....|....*....|....*....|....*.
gi 225428594 531 LENTYSRCPLITSIWVYGNSFESF---LVAVVVPDK 563
Cdd:cd17633 246 IESVLKAIPGIEEAIVVGIPDARFgeiAVALYSGDK 281
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
77-548 |
2.09e-11 |
|
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: 66.37 E-value: 2.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 77 LTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQAIPYVPLYDSLGANAVEFIINHAEVSIAFVQE 156
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 157 SkipamltclpkctsylktiisfgkisssqkeeaeelgvscfsweefaLLGSLDCElppkqktDICTIMYTSGTTGEPKG 236
Cdd:cd05969 81 E-----------------------------------------------LYERTDPE-------DPTLLHYTSGTTGTPKG 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 237 VVLSNEAIMAEVLSTDQLLletDKVatEEDTYFsflplaHVFDQIMETyciykGSSIGFWGA--------------DVRY 302
Cdd:cd05969 107 VLHVHDAMIFYYFTGKYVL---DLH--PDDIYW------CTADPGWVT-----GTVYGIWAPwlngvtnvvyegrfDAES 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 303 LMEDIQELKPTIFCGVPRVYERIYGgaiakisSGGALrkalfqyAYNYKLRNLekglrqdeaaprldrlifdkikqgfgg 382
Cdd:cd05969 171 WYGIIERVKVTVWYTAPTAIRMLMK-------EGDEL-------ARKYDLSSL--------------------------- 209
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 383 rvRLLFSGAAPLSRHV----EEFLRVTscsvLSQGYGLTEScGGCLtsIVNEFSM---MGTVGVPYPTIEARLesVPEMG 455
Cdd:cd05969 210 --RFIHSVGEPLNPEAirwgMEVFGVP----IHDTWWQTET-GSIM--IANYPCMpikPGSMGKPLPGVKAAV--VDENG 278
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 456 yDALSNVPRGEICLRG--KTLFSGYFKRQDLTESALVDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSqGEYVAVENLEN 533
Cdd:cd05969 279 -NELPPGTKGILALKPgwPSMFRGIWNDEERYKNSFIDGWYLTGDLAYRDEDGYFWFVGRADDIIKTS-GHRVGPFEVES 356
|
490
....*....|....*
gi 225428594 534 TYSRCPLITSIWVYG 548
Cdd:cd05969 357 ALMEHPAVAEAGVIG 371
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
77-571 |
2.70e-11 |
|
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: 66.18 E-value: 2.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 77 LTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQAIPYVPLyDslganavefiINHAEVSIAFVQE 156
Cdd:cd17643 13 LTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPI-D----------PAYPVERIAFILA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 157 SKIPAMLTCLPKCTSYlktiisfgkisssqkeeaeelgvscfsweefallgsldcelppkqktdictIMYTSGTTGEPKG 236
Cdd:cd17643 82 DSGPSLLLTDPDDLAY---------------------------------------------------VIYTSGSTGRPKG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 237 VVLSNeaimAEVLStdqLLLETDKV--ATEEDTYFSFLPLAhvFD-QIMEtyciykgssigFWGA------------DVR 301
Cdd:cd17643 111 VVVSH----ANVLA---LFAATQRWfgFNEDDVWTLFHSYA--FDfSVWE-----------IWGAllhggrlvvvpyEVA 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 302 YLMEDIQEL----KPTIFCGVPrvyeriyggaiakissgGALRkalfqyaynyklRNLEKGLRQDEAAPRLdRLIFdkik 377
Cdd:cd17643 171 RSPEDFARLlrdeGVTVLNQTP-----------------SAFY------------QLVEAADRDGRDPLAL-RYVI---- 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 378 qgFGGRvRLLFSGAAPLSRHVEEflrvtSCSVLSQGYGLTEscggclTSIVNEF----------SMMGTVGVPYPTIEAR 447
Cdd:cd17643 217 --FGGE-ALEAAMLRPWAGRFGL-----DRPQLVNMYGITE------TTVHVTFrpldaadlpaAAASPIGRPLPGLRVY 282
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 448 LesvpemgYDA-LSNVPR---GEICLRGKTLFSGYFKRQDLTESALVDGWF--------HTGDIGEWQPNGAMKIIDR-- 513
Cdd:cd17643 283 V-------LDAdGRPVPPgvvGELYVSGAGVARGYLGRPELTAERFVANPFggpgsrmyRTGDLARRLPDGELEYLGRad 355
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 225428594 514 ---KKNIFKLSQGEyvavenLENTYSRCPLITSIWVYGNSFE---SFLVAVVVPDKKALEDWAE 571
Cdd:cd17643 356 eqvKIRGFRIELGE------IEAALATHPSVRDAAVIVREDEpgdTRLVAYVVADDGAAADIAE 413
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
77-573 |
6.59e-11 |
|
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: 65.02 E-value: 6.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 77 LTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQAIPYVPLYDSLGANAVEFIINHAEVSIAfvqe 156
Cdd:cd17653 23 LTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARIQAILRTSGATLL---- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 157 skipamltclpkctsylktiisfgkisssqkeeaeelgvscfsweefallgsldceLPPKQKTDICTIMYTSGTTGEPKG 236
Cdd:cd17653 99 --------------------------------------------------------LTTDSPDDLAYIIFTSGSTGIPKG 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 237 VVLSNEAIMAEVLSTDQLLLET--DKVAteedtyfSFLPLAhvFD----QIMETYC-----IYKGSSiGFWGADVRYLme 305
Cdd:cd17653 123 VMVPHRGVLNYVSQPPARLDVGpgSRVA-------QVLSIA--FDacigEIFSTLCnggtlVLADPS-DPFAHVARTV-- 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 306 DIQELKPTIFCGV-PRVYERIyggaiAKISSGGalrkalfqyaynyklrnlekglrqdEAAPR--LDRlifdkikqgFGG 382
Cdd:cd17653 191 DALMSTPSILSTLsPQDFPNL-----KTIFLGG-------------------------EAVPPslLDR---------WSP 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 383 RVRLLfsgaaplsrhveeflrvtscsvlsQGYGLTE-SCGGCLTSIvnefsMMG---TVGVPYPT-----IEARLESVPE 453
Cdd:cd17653 232 GRRLY------------------------NAYGPTEcTISSTMTEL-----LPGqpvTIGKPIPNstcyiLDADLQPVPE 282
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 454 MgydalsnvPRGEICLRGKTLFSGYFKRQDLTESALV-----DGW--FHTGDIGEWQPNGAMKIIDRKKNIFKLsQGEYV 526
Cdd:cd17653 283 G--------VVGEICISGVQVARGYLGNPALTASKFVpdpfwPGSrmYRTGDYGRWTEDGGLEFLGREDNQVKV-RGFRI 353
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 225428594 527 AVENLENT-YSRCPLITSiwVYGNSFESFLVAVVVP---DKKALEDWAENH 573
Cdd:cd17653 354 NLEEIEEVvLQSQPEVTQ--AAAIVVNGRLVAFVTPetvDVDGLRSELAKH 402
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
78-241 |
7.94e-11 |
|
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: 64.91 E-value: 7.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 78 TYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQAIPYVPLYDSLGANAVEFIINHAEVSI-----A 152
Cdd:cd17634 86 SYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLlitadG 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 153 FVQESKIPAMLTCL-----PKCTSYLKTIISFGKISSSQKEEAEElgvscFSWEEFALLGSLDCELPPKQKTDICTIMYT 227
Cdd:cd17634 166 GVRAGRSVPLKKNVddalnPNVTSVEHVIVLKRTGSDIDWQEGRD-----LWWRDLIAKASPEHQPEAMNAEDPLFILYT 240
|
170
....*....|....
gi 225428594 228 SGTTGEPKGVVLSN 241
Cdd:cd17634 241 SGTTGKPKGVLHTT 254
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
78-521 |
8.20e-11 |
|
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: 64.82 E-value: 8.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 78 TYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQAIPYVPLYDSLGANAVEFIINHAEVS-IAFVQE 156
Cdd:cd05970 49 TFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKmIVAIAE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 157 SKIPAML-TCLPKCTSYLKTIisfgKISSSQKEeaeelgvscfSWEEF-ALLGSLDCELPPKQKT------DICTIMYTS 228
Cdd:cd05970 129 DNIPEEIeKAAPECPSKPKLV----WVGDPVPE----------GWIDFrKLIKNASPDFERPTANsypcgeDILLVYFSS 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 229 GTTGEPKGVVLSNEAIMAEVLSTD--QLLLETDKVATEEDT----------YFSFLPLAHVFDQIMETYciykgssigfw 296
Cdd:cd05970 195 GTTGMPKMVEHDFTYPLGHIVTAKywQNVREGGLHLTVADTgwgkavwgkiYGQWIAGAAVFVYDYDKF----------- 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 297 gaDVRYLMEDIQELKPTIFCGVPRVYERIYGGAIAKissggalrkalfqyaynYKLRNLEKGLRQDEAaprLDRLIFDKI 376
Cdd:cd05970 264 --DPKALLEKLSKYGVTTFCAPPTIYRFLIREDLSR-----------------YDLSSLRYCTTAGEA---LNPEVFNTF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 377 KQGFGGRVRllfsgaaplsrhveeflrvtscsvlsQGYGLTEscggcLTSIVNEFSMM----GTVGVPYPTIEARLesvp 452
Cdd:cd05970 322 KEKTGIKLM--------------------------EGFGQTE-----TTLTIATFPWMepkpGSMGKPAPGYEIDL---- 366
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 225428594 453 eMGYDAlSNVP---RGEICLR---GKT--LFSGYFKRQDLTESALVDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLS 521
Cdd:cd05970 367 -IDREG-RSCEageEGEIVIRtskGKPvgLFGGYYKDAEKTAEVWHDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSS 441
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
77-238 |
8.25e-11 |
|
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: 65.20 E-value: 8.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 77 LTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQAIPYVPLYDSLGANAVEFIINHAEVSIAFVQE 156
Cdd:cd05968 92 LTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALITAD 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 157 SkipamltclpkcTSYLKTIISFgkisssqKEEAEELGVSCFSWEEFALLGSLDCELPPKQKTDI--------------- 221
Cdd:cd05968 172 G------------FTRRGREVNL-------KEEADKACAQCPTVEKVVVVRHLGNDFTPAKGRDLsydeeketagdgaer 232
|
170 180
....*....|....*....|...
gi 225428594 222 ------CTIMYTSGTTGEPKGVV 238
Cdd:cd05968 233 tesedpLMIIYTSGTTGKPKGTV 255
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
77-562 |
1.80e-10 |
|
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: 63.83 E-value: 1.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 77 LTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQAIPYVPLYDSLGANAVEFIINHAEVSIAFVQE 156
Cdd:cd17646 24 LTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAYMLADAGPAVVLTTA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 157 SKIPAMltclpkctsylktiisfgkisssqkeeAEELGVSCFSWEEFALLGSLDCELPPKQKTDICTImYTSGTTGEPKG 236
Cdd:cd17646 104 DLAARL---------------------------PAGGDVALLGDEALAAPPATPPLVPPRPDNLAYVI-YTSGSTGRPKG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 237 VVLSNEAImAEVLSTDQ---LLLETDKVAteEDTYFSF--------LPLAHvfdqimetyciykGSSI------GfwGAD 299
Cdd:cd17646 156 VMVTHAGI-VNRLLWMQdeyPLGPGDRVL--QKTPLSFdvsvwelfWPLVA-------------GARLvvarpgG--HRD 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 300 VRYLMEDIQELKPTIFCGVPRVyeriyggaiakissggaLRKALfqyaynyklrnlekglrQDEAAPRLDRLifdkikqg 379
Cdd:cd17646 218 PAYLAALIREHGVTTCHFVPSM-----------------LRVFL-----------------AEPAAGSCASL-------- 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 380 fggrvRLLFSGAAPLSRHV-EEFLRVTSCSvLSQGYGLTEScggcltsivnefsmmgTVGVPYPTIEARLE--SVPeMGY 456
Cdd:cd17646 256 -----RRVFCSGEALPPELaARFLALPGAE-LHNLYGPTEA----------------AIDVTHWPVRGPAEtpSVP-IGR 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 457 -----------DALSNVPRG---EICLRGKTLFSGYFKRQDLTESALVDGWF-------HTGDIGEWQPNGAMKIIDRKK 515
Cdd:cd17646 313 pvpntrlyvldDALRPVPVGvpgELYLGGVQLARGYLGRPALTAERFVPDPFgpgsrmyRTGDLARWRPDGALEFLGRSD 392
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 225428594 516 NIFKLsQGEYVAVENLENTYSRCPLITSIWVY---GNSFESFLVAVVVPD 562
Cdd:cd17646 393 DQVKI-RGFRVEPGEIEAALAAHPAVTHAVVVaraAPAGAARLVGYVVPA 441
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
413-532 |
3.49e-10 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 62.58 E-value: 3.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 413 GYGLTEscggcLTSIV--NEFSMMGTVGVPYPTIEARLESvpemgydalsnvprGEICLRGKTLFSGYF---KRQDLTES 487
Cdd:PRK09029 270 GYGLTE-----MASTVcaKRADGLAGVGSPLPGREVKLVD--------------GEIWLRGASLALGYWrqgQLVPLVND 330
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 225428594 488 alvDGWFHTGDIGEWQpNGAMKIIDRKKNIFkLSQGEYVAVENLE 532
Cdd:PRK09029 331 ---EGWFATRDRGEWQ-NGELTILGRLDNLF-FSGGEGIQPEEIE 370
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
77-513 |
8.05e-10 |
|
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: 61.62 E-value: 8.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 77 LTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQAIPYVPLYDSLGANAVEFIInhaevsiafvQE 156
Cdd:cd17649 13 LSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML----------ED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 157 SKIPAMLTCLPKCTSYlktiisfgkisssqkeeaeelgvscfsweefallgsldcelppkqktdictIMYTSGTTGEPKG 236
Cdd:cd17649 83 SGAGLLLTHHPRQLAY---------------------------------------------------VIYTSGSTGTPKG 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 237 VVLSNEaimaevlstdqllletdkvateedtyfsflPLAHVFDQIMETY------CIYKGSSIGFWGAdvrylmedIQEL 310
Cdd:cd17649 112 VAVSHG------------------------------PLAAHCQATAERYgltpgdRELQFASFNFDGA--------HEQL 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 311 KPTIFCG---VPRVYERIYG-GAIAKISSGGALRKALFQYAYNYKLrnlekglrqdeaaprldRLIFDKIKQGFGGRVRL 386
Cdd:cd17649 154 LPPLICGacvVLRPDELWASaDELAEMVRELGVTVLDLPPAYLQQL-----------------AEEADRTGDGRPPSLRL 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 387 LFSGAAPLSrhVEEFLRVTSCSV-LSQGYGLTEscgGCLTSIVNEFSMMGTVGVPYPTIEARLESVPEMGYDA----LSN 461
Cdd:cd17649 217 YIFGGEALS--PELLRRWLKAPVrLFNAYGPTE---ATVTPLVWKCEAGAARAGASMPIGRPLGGRSAYILDAdlnpVPV 291
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 462 VPRGEICLRGKTLFSGYFKRQDLTESALVDG--------WFHTGDIGEWQPNGAMKIIDR 513
Cdd:cd17649 292 GVTGELYIGGEGLARGYLGRPELTAERFVPDpfgapgsrLYRTGDLARWRDDGVIEYLGR 351
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
222-530 |
1.21e-09 |
|
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: 60.39 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 222 CTIMYTSGTTGEPKGVVLSNEAIMAEVLstdQLLLETDkvATEEDTYFSFLPLAHvfdqimetyciykgssIGFWGADVr 301
Cdd:cd17636 3 VLAIYTAAFSGRPNGALLSHQALLAQAL---VLAVLQA--IDEGTVFLNSGPLFH----------------IGTLMFTL- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 302 ylmediqelkPTIFCG-----VPRVYERIYGGAIA--KISSGGALRKALFQyaynykLRNLEKGLRQDEAAPRLDRlifd 374
Cdd:cd17636 61 ----------ATFHAGgtnvfVRRVDAEEVLELIEaeRCTHAFLLPPTIDQ------IVELNADGLYDLSSLRSSP---- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 375 kikqGFGGRVRLLFSGAAPLSRHVeeflrvtscsvlsQGYGLTEsCGGCLTSIVNEFSMMGTVGVPYPTIEARLesVPEM 454
Cdd:cd17636 121 ----AAPEWNDMATVDTSPWGRKP-------------GGYGQTE-VMGLATFAALGGGAIGGAGRPSPLVQVRI--LDED 180
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 225428594 455 GYDalsnVPRG---EICLRGKTLFSGYFKRQDLTESALVDGWFHTGDIGEWQPNGAMKIIDRKKNIFKlsqgeyVAVEN 530
Cdd:cd17636 181 GRE----VPDGevgEIVARGPTVMAGYWNRPEVNARRTRGGWHHTNDLGRREPDGSLSFVGPKTRMIK------SGAEN 249
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
77-238 |
2.82e-09 |
|
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: 60.02 E-value: 2.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 77 LTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEACNS-QAIPYVpLYDSLGANAVEFIINHAE----VSI 151
Cdd:cd05967 83 YTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARiGAIHSV-VFGGFAAKELASRIDDAKpkliVTA 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 152 AF-VQESKIPAMLTCLPKCTSY-----LKTIIsfgkISSSQKEEAEELGVSCFSW-EEFALLGSLDCelPPKQKTDICTI 224
Cdd:cd05967 162 SCgIEPGKVVPYKPLLDKALELsghkpHHVLV----LNRPQVPADLTKPGRDLDWsELLAKAEPVDC--VPVAATDPLYI 235
|
170
....*....|....
gi 225428594 225 MYTSGTTGEPKGVV 238
Cdd:cd05967 236 LYTSGTTGKPKGVV 249
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
48-548 |
3.62e-09 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 59.89 E-value: 3.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 48 FSDSVERNPKNQML--GRRQIinskagpyvwlTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEACNSqa 125
Cdd:PRK08279 43 FEEAAARHPDRPALlfEDQSI-----------SYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAK-- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 126 ipyvplydsLGAnaVEFIINHAEV------SIAFVQeskiPAMLTCLPKCTSYLKTIISFGKISSSQKEEAEELGVSCFS 199
Cdd:PRK08279 110 ---------LGA--VVALLNTQQRgavlahSLNLVD----AKHLIVGEELVEAFEEARADLARPPRLWVAGGDTLDDPEG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 200 WEEFALLGSLDCELPPK-----QKTDICTIMYTSGTTGEPKGVVLSNEAIMaevLSTDQLLLETDkvATEEDTYFSFLPL 274
Cdd:PRK08279 175 YEDLAAAAAGAPTTNPAsrsgvTAKDTAFYIYTSGTTGLPKAAVMSHMRWL---KAMGGFGGLLR--LTPDDVLYCCLPL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 275 AH------VFDQIMETyciykGSSI---------GFWgadvrylmEDIQELKPTIFCgvprvyeriYGGAIakissggaL 339
Cdd:PRK08279 250 YHntggtvAWSSVLAA-----GATLalrrkfsasRFW--------DDVRRYRATAFQ---------YIGEL--------C 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 340 RkalfqYAYNYKLRNLEK----------GLRQDeaaprldrlIFDKIKQGFGgrvrllfsgaaplSRHVEEFlrvtscsv 409
Cdd:PRK08279 300 R-----YLLNQPPKPTDRdhrlrlmignGLRPD---------IWDEFQQRFG-------------IPRILEF-------- 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 410 lsqgYGLTEscggCLTSIVNEFSMMGTVG-------VPYPTIEARLES-VPEMGYDA-LSNVPRGEICL-----RGKTLF 475
Cdd:PRK08279 345 ----YAASE----GNVGFINVFNFDGTVGrvplwlaHPYAIVKYDVDTgEPVRDADGrCIKVKPGEVGLligriTDRGPF 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 476 SGYFKRQDlTESALV-------DGWFHTGDIGEWQPNGAMKIIDRKKNIFKLsQGEYVAVENLENTYSRCPLITSIWVYG 548
Cdd:PRK08279 417 DGYTDPEA-SEKKILrdvfkkgDAWFNTGDLMRDDGFGHAQFVDRLGDTFRW-KGENVATTEVENALSGFPGVEEAVVYG 494
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
73-561 |
2.48e-08 |
|
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: 56.72 E-value: 2.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 73 PYVWLTYREAYDAALRMGSAMRSRGVN-PGDRCGIYGSNCPEWIIAMEACNSQAIPYVPLYDSLGANAVEFIINHAEVSI 151
Cdd:cd05958 7 PEREWTYRDLLALANRIANVLVGELGIvPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKARITV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 152 AFVQEskipamltclpkctsylktiisfgkisssqKEEAEElgvscfsweefallgsldcelppkqktDICTIMYTSGTT 231
Cdd:cd05958 87 ALCAH------------------------------ALTASD---------------------------DICILAFTSGTT 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 232 GEPKGVV--LSNEAIMAEVLSTDQLLLEtdkvatEEDTYFSFLPLAHVFDQ-IMETYCIYKGSS-IGFWGADVRYLMEDI 307
Cdd:cd05958 110 GAPKATMhfHRDPLASADRYAVNVLRLR------EDDRFVGSPPLAFTFGLgGVLLFPFGVGASgVLLEEATPDLLLSAI 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 308 QELKPTIFCGVPRVYERIYGGAIAKISSGGALRKALfqyaynyklrnlekglrqdEAAPRLDRLIFDKIKQGFGgrvrll 387
Cdd:cd05958 184 ARYKPTVLFTAPTAYRAMLAHPDAAGPDLSSLRKCV-------------------SAGEALPAALHRAWKEATG------ 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 388 fsgaaplsrhveeflrvtscSVLSQGYGLTESCgGCLTSIVNEFSMMGTVGVPYPTIEARLesVPEMGYDalsnVPRGEI 467
Cdd:cd05958 239 --------------------IPIIDGIGSTEMF-HIFISARPGDARPGATGKPVPGYEAKV--VDDEGNP----VPDGTI 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 468 ---CLRGKTLFSGYF-KRQdltESALVDGWFHTGDIGEWQPNGAMKIIDRKKNIFKlSQGEYVAVENLENTYSRCPLITS 543
Cdd:cd05958 292 grlAVRGPTGCRYLAdKRQ---RTYVQGGWNITGDTYSRDPDGYFRHQGRSDDMIV-SGGYNIAPPEVEDVLLQHPAVAE 367
|
490 500
....*....|....*....|.
gi 225428594 544 IWVYGNSFESFLV---AVVVP 561
Cdd:cd05958 368 CAVVGHPDESRGVvvkAFVVL 388
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
77-240 |
3.11e-08 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 56.44 E-value: 3.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 77 LTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQAIPYVPLYDSLGANAVEFIINHAEVSIAFvqe 156
Cdd:PRK04813 28 LTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVDVSSPAERIEMIIEVAKPSLII--- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 157 skipamltclpkCTSYLKTIISFGKISSsqkeeAEELGvscfswEEFALLGSLDCELPPKQkTDICTIMYTSGTTGEPKG 236
Cdd:PRK04813 105 ------------ATEELPLEILGIPVIT-----LDELK------DIFATGNPYDFDHAVKG-DDNYYIIFTSGTTGKPKG 160
|
....
gi 225428594 237 VVLS 240
Cdd:PRK04813 161 VQIS 164
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
216-533 |
3.53e-08 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 56.36 E-value: 3.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 216 KQKTDICTIMYTSGTTGEPKGVVLSNEAIMAEVLSTDQLLletdkVATEEDTYFSFLPLAHVFD-QIMETYCIYKGSSIG 294
Cdd:PRK06334 180 KDPEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFF-----SPKEDDVMMSFLPPFHAYGfNSCTLFPLLSGVPVV 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 295 FWGADV--RYLMEDIQELKPTIFCGVPRVYERIYGGAIAKISSGGALRKALFqyaynyklrnlekglrqdeaaprldrli 372
Cdd:PRK06334 255 FAYNPLypKKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQESCLPSLRFVVI---------------------------- 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 373 fdkikqgfGGRV--RLLFSGAAPLSRHVeeflrvtscsVLSQGYGLTEsCGGCLTsIVNEFS--MMGTVGVPYPTIEARL 448
Cdd:PRK06334 307 --------GGDAfkDSLYQEALKTFPHI----------QLRQGYGTTE-CSPVIT-INTVNSpkHESCVGMPIRGMDVLI 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 449 esVPEMGYDALSNVPRGEICLRGKTLFSGYFKrQDLTESALV---DGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSqGEY 525
Cdd:PRK06334 367 --VSEETKVPVSSGETGLVLTRGTSLFSGYLG-EDFGQGFVElggETWYVTGDLGYVDRHGELFLKGRLSRFVKIG-AEM 442
|
....*...
gi 225428594 526 VAVENLEN 533
Cdd:PRK06334 443 VSLEALES 450
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
77-246 |
7.34e-08 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 55.67 E-value: 7.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 77 LTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPE-WIIAMEACNSQAIpYVPLYDSLGANAVefiinHAEVSIAfvq 155
Cdd:PRK04319 74 YTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPElYFALLGALKNGAI-VGPLFEAFMEEAV-----RDRLEDS--- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 156 ESKI----PAMLTCLPKC-TSYLKTIISFGkisssqkeEAEELGVSCFSWEEFALLGSLDCELPPKQKTDICTIMYTSGT 230
Cdd:PRK04319 145 EAKVlittPALLERKPADdLPSLKHVLLVG--------EDVEEGPGTLDFNALMEQASDEFDIEWTDREDGAILHYTSGS 216
|
170
....*....|....*.
gi 225428594 231 TGEPKGVVLSNEAIMA 246
Cdd:PRK04319 217 TGKPKGVLHVHNAMLQ 232
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
77-238 |
1.81e-07 |
|
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: 54.49 E-value: 1.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 77 LTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQAIPYVPLYDSLGANAVEFIINHAEVSI----- 151
Cdd:cd05966 85 ITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFAGFSAESLADRINDAQCKLvitad 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 152 AFVQESKI----PAMLTCLPKCTSyLKTIISF----GKISSSQKEEaeelgvscFSWEEFALLGSLDCELPPKQKTDICT 223
Cdd:cd05966 165 GGYRGGKViplkEIVDEALEKCPS-VEKVLVVkrtgGEVPMTEGRD--------LWWHDLMAKQSPECEPEWMDSEDPLF 235
|
170
....*....|....*
gi 225428594 224 IMYTSGTTGEPKGVV 238
Cdd:cd05966 236 ILYTSGSTGKPKGVV 250
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
220-562 |
4.50e-07 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 52.35 E-value: 4.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 220 DICTIMYTSGTTGEPKGVVLSNEAIMAEVLSTDQLLletdkvaTEEDTYFSFLPLAHVFDQIMETYCIYKGS-------S 292
Cdd:PRK07824 36 DVALVVATSGTTGTPKGAMLTAAALTASADATHDRL-------GGPGQWLLALPAHHIAGLQVLVRSVIAGSepveldvS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 293 IGFwgaDVRYLMEDIQELKPtifcgvprvyERIYGGAIAKissggalrkalfqyaynyklrNLEKGLRQDEAAPRLDRli 372
Cdd:PRK07824 109 AGF---DPTALPRAVAELGG----------GRRYTSLVPM---------------------QLAKALDDPAATAALAE-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 373 FDKIkqgfggrvrLLfsGAAPLSRHVEEFLRVTSCSVLSQgYGLTESCGGCLTSivnefsmmgtvGVPYPTIEARLESvp 452
Cdd:PRK07824 153 LDAV---------LV--GGGPAPAPVLDAAAAAGINVVRT-YGMSETSGGCVYD-----------GVPLDGVRVRVED-- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 453 emgydalsnvprGEICLRGKTLFSGYfkRQDLTESALVD-GWFHTGDIGEWQpNGAMKIIDRKKNIFKlSQGEYVAVENL 531
Cdd:PRK07824 208 ------------GRIALGGPTLAKGY--RNPVDPDPFAEpGWFRTDDLGALD-DGVLTVLGRADDAIS-TGGLTVLPQVV 271
|
330 340 350
....*....|....*....|....*....|....
gi 225428594 532 ENTYSRCPLITSIWVYGNSFESF---LVAVVVPD 562
Cdd:PRK07824 272 EAALATHPAVADCAVFGLPDDRLgqrVVAAVVGD 305
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
77-571 |
4.52e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 52.82 E-value: 4.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 77 LTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEACNSqaipyvplydsLGAN--AVEFIINHAEVsiAFV 154
Cdd:PRK06164 36 LSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACAR-----------LGATviAVNTRYRSHEV--AHI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 155 QESKIPAMLTCLPKctsyLKTIISFGKISSSQKEE---AEELGVSCFSWEE--------------FALLGSLDCELPPKQ 217
Cdd:PRK06164 103 LGRGRARWLVVWPG----FKGIDFAAILAAVPPDAlppLRAIAVVDDAADAtpapapgarvqlfaLPDPAPPAAAGERAA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 218 KTDICTIMYT-SGTTGEPKGV------VLSNEAIMAEVLSTDQllletdkvateEDTYFSFLPLAHVFdqimetyciykg 290
Cdd:PRK06164 179 DPDAGALLFTtSGTTSGPKLVlhrqatLLRHARAIARAYGYDP-----------GAVLLAALPFCGVF------------ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 291 ssiGFWGadvrylmediqeLKPTIFCGVPRVYERIYGGAIAkissGGALRKALFQYAY--NYKLRNLEKGLRQDEAAPRL 368
Cdd:PRK06164 236 ---GFST------------LLGALAGGAPLVCEPVFDAART----ARALRRHRVTHTFgnDEMLRRILDTAGERADFPSA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 369 DRLifdkikqGFGGrvrllFSGAaplSRHVEEFLRVTScSVLSQGYGLTE----SCGGCLTSIVNEFSMMGtvGVP-YPT 443
Cdd:PRK06164 297 RLF-------GFAS-----FAPA---LGELAALARARG-VPLTGLYGSSEvqalVALQPATDPVSVRIEGG--GRPaSPE 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 444 IEARLESvPEMGyDALSNVPRGEICLRGKTLFSGYFKRQDLTESALV-DGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSq 522
Cdd:PRK06164 359 ARVRARD-PQDG-ALLPDGESGEIEIRAPSLMRGYLDNPDATARALTdDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLG- 435
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 225428594 523 GEYVAVENLENTYSRCPLITSIWVYGNSFESFLVAV--VVPDKKALEDWAE 571
Cdd:PRK06164 436 GFLVNPAEIEHALEALPGVAAAQVVGATRDGKTVPVafVIPTDGASPDEAG 486
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
209-592 |
4.65e-07 |
|
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: 52.93 E-value: 4.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 209 LDCELPPKQKTDICT-----------------IMYTSGTTGEPKGVVLSNEAIMAEVLSTDQLLLetdkvATEEDTYFSF 271
Cdd:cd05918 79 LDPSHPLQRLQEILQdtgakvvltsspsdaayVIFTSGSTGKPKGVVIEHRALSTSALAHGRALG-----LTSESRVLQF 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 272 LplAHVFD-QIMETY---------CIykgssigfwGADVRyLMED----IQELKPTIFCGVPRVyeriyggaiakissgg 337
Cdd:cd05918 154 A--SYTFDvSILEIFttlaaggclCI---------PSEED-RLNDlagfINRLRVTWAFLTPSV---------------- 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 338 alrkalfqyaynykLRNLekglrQDEAAPRLDRLIF--DKIKQG----FGGRVRLLfsgaaplsrhveeflrvtscsvls 411
Cdd:cd05918 206 --------------ARLL-----DPEDVPSLRTLVLggEALTQSdvdtWADRVRLI------------------------ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 412 QGYGLTESCGGCLTSIVNEFSMMGTVGVPYPtieARLESVPEMGYDALsnVPR---GEICLRGKTLFSGYFKRQDLTESA 488
Cdd:cd05918 243 NAYGPAECTIAATVSPVVPSTDPRNIGRPLG---ATCWVVDPDNHDRL--VPIgavGELLIEGPILARGYLNDPEKTAAA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 489 LVDG--W------------FHTGDIGEWQPNGAMKIIDRKKNIFKLsQGEYVAVENLENTYSRC-PLITS-----IWVYG 548
Cdd:cd05918 318 FIEDpaWlkqegsgrgrrlYRTGDLVRYNPDGSLEYVGRKDTQVKI-RGQRVELGEIEHHLRQSlPGAKEvvvevVKPKD 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 225428594 549 NSFESFLVAVVVPDKkaledwAENHNVTGDFKSLCENLEARKYI 592
Cdd:cd05918 397 GSSSPQLVAFVVLDG------SSSGSGDGDSLFLEPSDEFRALV 434
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
77-121 |
1.14e-06 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 51.68 E-value: 1.14e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 225428594 77 LTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEAC 121
Cdd:PRK00174 99 ITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLAC 143
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
467-554 |
1.49e-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: 51.28 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 467 ICLRGKTLFSGYFKRQDLTES-ALVDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSqGEYVAVENLENTYSRCPLITSIW 545
Cdd:cd05915 363 VQLKGPWITGGYYGNEEATRSaLTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSG-GEWISSVDLENALMGHPKVKEAA 441
|
....*....
gi 225428594 546 VYGNSFESF 554
Cdd:cd05915 442 VVAIPHPKW 450
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
217-528 |
3.30e-06 |
|
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: 50.13 E-value: 3.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 217 QKTDICTIMYTSGTTGEPKGVVLSNEAIMAEVLSTDQLLLETDKVATEEDTYFSFLPLAhvfDQIMETycIYKGSSIGFW 296
Cdd:cd17644 104 QPENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAA---EEIYVT--LLSGATLVLR 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 297 GADVRYLMED----IQELKPTIFcGVPRVY--ERIYGGAIAKISSGGALRKALfqyaynyklrnlekgLRQDEAAPRLDR 370
Cdd:cd17644 179 PEEMRSSLEDfvqyIQQWQLTVL-SLPPAYwhLLVLELLLSTIDLPSSLRLVI---------------VGGEAVQPELVR 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 371 LIFdkikQGFGGRVRLLfSGAAPlsrhveeflrvTSCSVLSQGYGLTESCGGCLTSIvnefsmmgTVGVPYPTIEA---- 446
Cdd:cd17644 243 QWQ----KNVGNFIQLI-NVYGP-----------TEATIAATVCRLTQLTERNITSV--------PIGRPIANTQVyild 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 447 -RLESVPemgydalSNVPrGEICLRGKTLFSGYFKRQDLTESALVDGWFH---------TGDIGEWQPNGAMKIIDR--- 513
Cdd:cd17644 299 eNLQPVP-------VGVP-GELHIGGVGLARGYLNRPELTAEKFISHPFNsseserlykTGDLARYLPDGNIEYLGRidn 370
|
330
....*....|....*..
gi 225428594 514 --KKNIFKLSQGEYVAV 528
Cdd:cd17644 371 qvKIRGFRIELGEIEAV 387
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
210-518 |
6.54e-06 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 49.38 E-value: 6.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 210 DCELPPKQKTDICTIMYTSGTTGEPKGVVLSNEAimaeVLSTDQLLLETDKVATEEDTYFSFLPLAHVFDQIMETYCIYK 289
Cdd:PRK05851 143 SASLTPPDSGGPAVLQGTAGSTGTPRTAILSPGA----VLSNLRGLNARVGLDAATDVGCSWLPLYHDMGLAFLLTAALA 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 290 GSSIgfWgadvrylmediqeLKPT-IFCGVPRVYeriyggaIAKISSGGALRKALFQYAYN----YKLRNLEKGLrqdea 364
Cdd:PRK05851 219 GAPL--W-------------LAPTtAFSASPFRW-------LSWLSDSRATLTAAPNFAYNligkYARRVSDVDL----- 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 365 aprldrlifdkikqgfgGRVRLLFSGAAP-----LSRHVEEFLRVT-SCSVLSQGYGLTES--------CGGCLtsIVNE 430
Cdd:PRK05851 272 -----------------GALRVALNGGEPvdcdgFERFATAMAPFGfDAGAAAPSYGLAEStcavtvpvPGIGL--RVDE 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 431 FSMMGT--------VGVPYPTIEARLESvpemGYDALSNVPR--GEICLRGKTLFSGYFKRQDLTEsalvDGWFHTGDIG 500
Cdd:PRK05851 333 VTTDDGsgarrhavLGNPIPGMEVRISP----GDGAAGVAGReiGEIEIRGASMMSGYLGQAPIDP----DDWFPTGDLG 404
|
330 340
....*....|....*....|....*.
gi 225428594 501 eWQPNGAMKIIDRKK--------NIF 518
Cdd:PRK05851 405 -YLVDGGLVVCGRAKelitvagrNIF 429
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
77-564 |
8.01e-06 |
|
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: 49.01 E-value: 8.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 77 LTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQAIPYVPLYDSLGANAVEFIINHAEVSIAFVQE 156
Cdd:cd17656 14 LTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRVVLTQR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 157 SkIPAMLTclpkcTSYLKTIISFGKISssqKEEAEELGVScfsweefallgsldcelppKQKTDICTIMYTSGTTGEPKG 236
Cdd:cd17656 94 H-LKSKLS-----FNKSTILLEDPSIS---QEDTSNIDYI-------------------NNSDDLLYIIYTSGTTGKPKG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 237 VVLSNEAIMAevlstdqlLLETDKVATEEDTYFSFLPLAHV-FD----QIMETYCiykgssigfWGADVRYLMEDIQElk 311
Cdd:cd17656 146 VQLEHKNMVN--------LLHFEREKTNINFSDKVLQFATCsFDvcyqEIFSTLL---------SGGTLYIIREETKR-- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 312 ptifcGVPRVYERIYGGAIAKISSGGALRKALFQyaynyklrnlekglrQDEAAPRLdrliFDKIKQGFGGRVRLLfsga 391
Cdd:cd17656 207 -----DVEQLFDLVKRHNIEVVFLPVAFLKFIFS---------------EREFINRF----PTCVKHIITAGEQLV---- 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 392 apLSRHVEEFLRVTSCSvLSQGYGLTEscggclTSIVNEFSMMGTVGVP-YPTIEARLESVPEMGYD-ALSNVPRG---E 466
Cdd:cd17656 259 --ITNEFKEMLHEHNVH-LHNHYGPSE------THVVTTYTINPEAEIPeLPPIGKPISNTWIYILDqEQQLQPQGivgE 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 467 ICLRGKTLFSGYFKRQDLTESALVDGWF-------HTGDIGEWQPNGAMKIIDRKKNIFKLsQGEYVAVENLENTYSRCP 539
Cdd:cd17656 330 LYISGASVARGYLNRQELTAEKFFPDPFdpnermyRTGDLARYLPDGNIEFLGRADHQVKI-RGYRIELGEIEAQLLNHP 408
|
490 500
....*....|....*....|....*...
gi 225428594 540 LITS--IWVYGNSF-ESFLVAVVVPDKK 564
Cdd:cd17656 409 GVSEavVLDKADDKgEKYLCAYFVMEQE 436
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
46-520 |
1.01e-05 |
|
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: 48.47 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 46 EFFSDSVERNPKNQML--GRRQiinskagpyvwLTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEACNS 123
Cdd:cd12115 3 DLVEAQAARTPDAIALvcGDES-----------LTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 124 QAIPYVPLYDSLGANAVEFIINHAEVSIAFVQeskipamltclPKCTSYlktiisfgkisssqkeeaeelgvscfsweef 203
Cdd:cd12115 72 AGAAYVPLDPAYPPERLRFILEDAQARLVLTD-----------PDDLAY------------------------------- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 204 allgsldcelppkqktdictIMYTSGTTGEPKGVVLS--NEAIM----AEVLSTDQL--LLETDKVATEEDTYFSFLPLA 275
Cdd:cd12115 110 --------------------VIYTSGSTGRPKGVAIEhrNAAAFlqwaAAAFSAEELagVLASTSICFDLSVFELFGPLA 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 276 HvfdqimetyciykGSSIgFWGADVRYLMEDIQELKPTIFCGVPrvyeriyggaiakiSSGGALrkalfqyaynyklrnl 355
Cdd:cd12115 170 T-------------GGKV-VLADNVLALPDLPAAAEVTLINTVP--------------SAAAEL---------------- 205
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 356 ekgLRQDeaaprldrlifdkikqGFGGRVRLLFSGAAPLSRH-VEEFLRVTSCSVLSQGYGLTEscggclTSIVNEFSMM 434
Cdd:cd12115 206 ---LRHD----------------ALPASVRVVNLAGEPLPRDlVQRLYARLQVERVVNLYGPSE------DTTYSTVAPV 260
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 435 GTVGVPYPTI------------EARLESVPemgydalSNVPrGEICLRGKTLFSGYFKRQDLT-ESALVDGW------FH 495
Cdd:cd12115 261 PPGASGEVSIgrplantqayvlDRALQPVP-------LGVP-GELYIGGAGVARGYLGRPGLTaERFLPDPFgpgarlYR 332
|
490 500
....*....|....*....|....*
gi 225428594 496 TGDIGEWQPNGAMKIIDRKKNIFKL 520
Cdd:cd12115 333 TGDLVRWRPDGLLEFLGRADNQVKV 357
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
77-562 |
1.02e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 48.52 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 77 LTYREAYDAALRMGSAMRSRgVNPGDRC--GIYGSNCPEWIIAMEACNSQAIPYVPLYDSLGANAVEFIINHAEVSIAFV 154
Cdd:PRK07867 29 TSWREHIRGSAARAAALRAR-LDPTRPPhvGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIAHADCQLVLT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 155 qESKIPAMLTCLPKctsylktiisfgkisssqkeEAEELGVSCFSWEEfALLGSLDCELPPK--QKTDICTIMYTSGTTG 232
Cdd:PRK07867 108 -ESAHAELLDGLDP--------------------GVRVINVDSPAWAD-ELAAHRDAEPPFRvaDPDDLFMLIFTSGTSG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 233 EPKGVVLSNEAI-MAEVLSTDQLLLETDKVAteedtYFSfLPLAHVfDQIMETYCiykgssigfwgadvrylmediqelk 311
Cdd:PRK07867 166 DPKAVRCTHRKVaSAGVMLAQRFGLGPDDVC-----YVS-MPLFHS-NAVMAGWA------------------------- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 312 PTIFCGvprvyeriygGAIA---KISSGGAL---RKALFQYAyNYKLRNLEKGL----RQDEAAPRLdrlifdkiKQGFG 381
Cdd:PRK07867 214 VALAAG----------ASIAlrrKFSASGFLpdvRRYGATYA-NYVGKPLSYVLatpeRPDDADNPL--------RIVYG 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 382 GRvrllfsgAAPlsRHVEEFLRVTSCSVLsQGYGLTEscGGclTSIVNEFSM-MGTVGVPYPTI-----EARLESVP-EM 454
Cdd:PRK07867 275 NE-------GAP--GDIARFARRFGCVVV-DGFGSTE--GG--VAITRTPDTpPGALGPLPPGVaivdpDTGTECPPaED 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 455 GYDALSNVPR--GEIC-LRGKTLFSGYFKRQDLTESALVDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSqGEYVAVENL 531
Cdd:PRK07867 341 ADGRLLNADEaiGELVnTAGPGGFEGYYNDPEADAERMRGGVYWSGDLAYRDADGYAYFAGRLGDWMRVD-GENLGTAPI 419
|
490 500 510
....*....|....*....|....*....|.
gi 225428594 532 ENTYSRCPLITSIWVYGnsfesflvavvVPD 562
Cdd:PRK07867 420 ERILLRYPDATEVAVYA-----------VPD 439
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
77-237 |
1.45e-05 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 48.02 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 77 LTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEAC----------------------------------- 121
Cdd:PRK10524 85 YTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACarigaihsvvfggfashslaariddakpvlivsad 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 122 ----NSQAIPYVPLYDSlganAVEFIinhaevsiafvqESKIPAMLtclpkctsylktIISFGkISSSQKEEAEELgvsc 197
Cdd:PRK10524 165 agsrGGKVVPYKPLLDE----AIALA------------QHKPRHVL------------LVDRG-LAPMARVAGRDV---- 211
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 225428594 198 fsweEFALL--GSLDCELPPK--QKTDICTIMYTSGTTGEPKGV 237
Cdd:PRK10524 212 ----DYATLraQHLGARVPVEwlESNEPSYILYTSGTTGKPKGV 251
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
211-276 |
3.32e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 46.86 E-value: 3.32e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 211 CELPPKQKTDICTIMYTSGTTGEPKGVVLSNEAIMAEVlstDQLL----LETDKVATEEDTYFSFLPLAH 276
Cdd:PRK05850 152 SDARPRDLPSTAYLQYTSGSTRTPAGVMVSHRNVIANF---EQLMsdyfGDTGGVPPPDTTVVSWLPFYH 218
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
77-251 |
3.88e-05 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 46.81 E-value: 3.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 77 LTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEACNSqaipyvplydsLGANavefiinHAEVSIAFVQE 156
Cdd:PLN02654 121 LTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACAR-----------IGAV-------HSVVFAGFSAE 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 157 SKIPAMLTCLPK----CTSYLK--TIISFGKISSSQKEEAEELGVS---CFS---------------------WEEFALL 206
Cdd:PLN02654 183 SLAQRIVDCKPKvvitCNAVKRgpKTINLKDIVDAALDESAKNGVSvgiCLTyenqlamkredtkwqegrdvwWQDVVPN 262
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 225428594 207 GSLDCELPPKQKTDICTIMYTSGTTGEPKGVVLSNEAIMAEVLST 251
Cdd:PLN02654 263 YPTKCEVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMVYTATT 307
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
205-517 |
6.14e-05 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 46.14 E-value: 6.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 205 LLGSLDCELPPKQKTDICTIMYTSGTTGEPKGVVLSN-------EAIMAEVlstdQLLLETDKVAteedtyfSFLPLAHv 277
Cdd:PRK07768 138 LLAADPIDPVETGEDDLALMQLTSGSTGSPKAVQITHgnlyanaEAMFVAA----EFDVETDVMV-------SWLPLFH- 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 278 fDQIMetyciykgssIGF------WGADVRYLmediqelKPTIFCGVPRVYERI---YGGAIAkissggalrkALFQYAY 348
Cdd:PRK07768 206 -DMGM----------VGFltvpmyFGAELVKV-------TPMDFLRDPLLWAELiskYRGTMT----------AAPNFAY 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 349 NYKLRNLEKGlrQDEAAPRLDRLifdkikqgfggrvRLLFSGAAPLS-RHVEEFLRVT-----SCSVLSQGYGLTES--- 419
Cdd:PRK07768 258 ALLARRLRRQ--AKPGAFDLSSL-------------RFALNGAEPIDpADVEDLLDAGarfglRPEAILPAYGMAEAtla 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 420 -----CGGCLTsiVNE-----FSMMG--------------TVGVPYPTIEARLesVPEMGydalsNV--PR--GEICLRG 471
Cdd:PRK07768 323 vsfspCGAGLV--VDEvdadlLAALRravpatkgntrrlaTLGPPLPGLEVRV--VDEDG-----QVlpPRgvGVIELRG 393
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 225428594 472 KTLFSGYfkrqdLTESALV-----DGWFHTGDIGEWQPNGAMKIIDRKKNI 517
Cdd:PRK07768 394 ESVTPGY-----LTMDGFIpaqdaDGWLDTGDLGYLTEEGEVVVCGRVKDV 439
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
77-244 |
6.37e-05 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 46.19 E-value: 6.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 77 LTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQAIPYVPLyDSlganavefiiNHAEVSIAFVQE 156
Cdd:PRK10252 484 FSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPL-DT----------GYPDDRLKMMLE 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 157 SKIPAMLtclpkctsylktiISfgkiSSSQKEEAEELGVSCFSWEEFALLGSLDCELPPKQKTDICTIMYTSGTTGEPKG 236
Cdd:PRK10252 553 DARPSLL-------------IT----TADQLPRFADVPDLTSLCYNAPLAPQGAAPLQLSQPHHTAYIIFTSGSTGRPKG 615
|
....*...
gi 225428594 237 VVLSNEAI 244
Cdd:PRK10252 616 VMVGQTAI 623
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
462-562 |
1.70e-04 |
|
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: 44.75 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 462 VPRGEI---CLRGKTLFSGYFKRQDLTESAL-VDGWFHTGDIGEWQPNGAMKIIDRKKNifklsQ----GEYVAVENLEN 533
Cdd:COG1021 375 VPPGEVgelLTRGPYTIRGYYRAPEHNARAFtPDGFYRTGDLVRRTPDGYLVVEGRAKD-----QinrgGEKIAAEEVEN 449
|
90 100 110
....*....|....*....|....*....|
gi 225428594 534 TYSRCPLITSiwvygnsfesflVAVV-VPD 562
Cdd:COG1021 450 LLLAHPAVHD------------AAVVaMPD 467
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
364-521 |
2.09e-04 |
|
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: 44.10 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 364 AAPRLDRLIFDKIKQGFGGRVRLLFSGAAPLSRHVEEFLRVTSCSVLSQGYGLTESCggCLTS-IVNEFSMMGTVGVPYP 442
Cdd:cd05974 182 APPTVWRMLIQQDLASFDVKLREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETT--ALVGnSPGQPVKAGSMGRPLP 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 443 TIEARLesvpemgYDALSN-VPRGEICL-----RGKTLFSGYFKRQDLTESALVDGWFHTGDIGEWQPNGAMKIIDRKKN 516
Cdd:cd05974 260 GYRVAL-------LDPDGApATEGEVALdlgdtRPVGLMKGYAGDPDKTAHAMRGGYYRTGDIAMRDEDGYLTYVGRADD 332
|
....*
gi 225428594 517 IFKLS 521
Cdd:cd05974 333 VFKSS 337
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
465-565 |
3.80e-04 |
|
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: 43.31 E-value: 3.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 465 GEICLRGKTLFSGYFKRQDLTESALV-------DGWFHTGDIGEWQPNGAMKIIDRKKNIFKLsQGEYVAVENLENTYSR 537
Cdd:cd17645 289 GELCIAGEGLARGYLNRPELTAEKFIvhpfvpgERMYRTGDLAKFLPDGNIEFLGRLDQQVKI-RGYRIEPGEIEPFLMN 367
|
90 100 110
....*....|....*....|....*....|.
gi 225428594 538 CPLI---TSIWVYGNSFESFLVAVVVPDKKA 565
Cdd:cd17645 368 HPLIelaAVLAKEDADGRKYLVAYVTAPEEI 398
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
72-123 |
4.10e-04 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 43.63 E-value: 4.10e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 225428594 72 GPYVWLTYREAYDAALRMGSAMRSRGVNPGDRCGIYGSNCPEWIIAMEACNS 123
Cdd:PRK03584 110 GPRRELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATAS 161
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
385-567 |
4.80e-04 |
|
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: 43.09 E-value: 4.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 385 RLLFSGAAPLS----RHVEEFLRVTscsvLSQGYGLTEscgG--CLTSIVN-EFSMMGTVGVPY-PTIEARLesVPEMGY 456
Cdd:cd05920 258 RLLQVGGARLSpalaRRVPPVLGCT----LQQVFGMAE---GllNYTRLDDpDEVIIHTQGRPMsPDDEIRV--VDEEGN 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 457 DalsnVPRGEI---CLRGKTLFSGYFKRQDLTESALV-DGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSqGEYVAVENLE 532
Cdd:cd05920 329 P----VPPGEEgelLTRGPYTIRGYYRAPEHNARAFTpDGFYRTGDLVRRTPDGYLVVEGRIKDQINRG-GEKIAAEEVE 403
|
170 180 190
....*....|....*....|....*....|....*....
gi 225428594 533 NTYSRCPLITSIWVYGNSfESFL----VAVVVPDKKALE 567
Cdd:cd05920 404 NLLLRHPAVHDAAVVAMP-DELLgersCAFVVLRDPPPS 441
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
224-548 |
2.27e-03 |
|
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: 40.82 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 224 IMYTSGTTGEPKGVV--LSNEAIMAEVLSTDQLLLEtdkvATEEDTYFSFLPLAHVFDQ--------------IMETYCi 287
Cdd:cd05929 130 MLYSGGTTGRPKGIKrgLPGGPPDNDTLMAAALGFG----PGADSVYLSPAPLYHAAPFrwsmtalfmggtlvLMEKFD- 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 288 ykgsSIGFWGADVRYLMEDIQeLKPTIFCGVPRVYEriyggaiakissggALRKAlfqyaynYKLRNLEKglrqdeaapr 367
Cdd:cd05929 205 ----PEEFLRLIERYRVTFAQ-FVPTMFVRLLKLPE--------------AVRNA-------YDLSSLKR---------- 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 368 ldrlifdkikqgfggrvrlLFSGAAPLSRHVEEFLRVTSCSVLSQGYGLTESCGGCLTSIVNEFSMMGTVGVPyptIEAR 447
Cdd:cd05929 249 -------------------VIHAAAPCPPWVKEQWIDWGGPIIWEYYGGTEGQGLTIINGEEWLTHPGSVGRA---VLGK 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 448 LESVPEMGydalSNVPRGEIclrGKTLFSG-----YFKRQDLTESALV-DGWFHTGDIGEWQPNGAMKIIDRKKNIFkLS 521
Cdd:cd05929 307 VHILDEDG----NEVPPGEI---GEVYFANgpgfeYTNDPEKTAAARNeGGWSTLGDVGYLDEDGYLYLTDRRSDMI-IS 378
|
330 340
....*....|....*....|....*..
gi 225428594 522 QGEYVAVENLENTYSRCPLITSIWVYG 548
Cdd:cd05929 379 GGVNIYPQEIENALIAHPKVLDAAVVG 405
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
462-601 |
4.45e-03 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 40.13 E-value: 4.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225428594 462 VPRGE---ICLRGKTLFSGYFKRQDlteSALVDGWFHTGDIGEWQPNGAMKIIDRKKNIFkLSQGEYVAVENLENTYSRC 538
Cdd:PRK13382 386 VPTGEvgtIFVRNDTQFDGYTSGST---KDFHDGFMASGDVGYLDENGRLFVVGRDDEMI-VSGGENVYPIEVEKTLATH 461
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 225428594 539 PLITSIWVYGNSFESF---LVAVVVPD----------KKALEDWAENHNVTGDFKslcenlearkyILDEL--NNTGQ 601
Cdd:PRK13382 462 PDVAEAAVIGVDDEQYgqrLAAFVVLKpgasatpetlKQHVRDNLANYKVPRDIV-----------VLDELprGATGK 528
|
|
| |
