|
Name |
Accession |
Description |
Interval |
E-value |
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
117-695 |
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: 941.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 117 QPYEWISYKQVAEMAECIGSALIQKGFKPCSEQFIGIFSQNRPEWVTIEQGCFTYSMVVVPLYDTLGTDAITYIVNKAEL 196
Cdd:cd05927 1 GPYEWISYKEVAERADNIGSALRSLGGKPAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 197 SVIFADKpekaklllegvenkltpclkiivimdsydndlvergqkcGVEIIGLKALEDLGRVNRTKPKPPEPEDLAIICF 276
Cdd:cd05927 81 SIVFCDA---------------------------------------GVKVYSLEEFEKLGKKNKVPPPPPKPEDLATICY 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 277 TSGTTGNPKGAMVTHQNIMNDCSGFIKATESAFIASPEDVLISFLPLAHMFETVVECVMLCHGAKIGFFQGDIRLLMDDL 356
Cdd:cd05927 122 TSGTTGNPKGVMLTHGNIVSNVAGVFKILEILNKINPTDVYISYLPLAHIFERVVEALFLYHGAKIGFYSGDIRLLLDDI 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 357 KVLQPTIFPVVPRLLNRMFDRIFG--QANTSVKRWLLDFASKRKEAELRSGIVRNNSLWDKLIFHKIQSSLGGKVRLMIT 434
Cdd:cd05927 202 KALKPTVFPGVPRVLNRIYDKIFNkvQAKGPLKRKLFNFALNYKLAELRSGVVRASPFWDKLVFNKIKQALGGNVRLMLT 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 435 GAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYIKLVDVEDMNYQAA--KGEGEVCVK 512
Cdd:cd05927 282 GSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAEVKLVDVPEMNYDAKdpNPRGEVCIR 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 513 GANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYLRSEAVAQVFVHGE 592
Cdd:cd05927 362 GPNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLSQGEYVAPEKIENIYARSPFVAQIFVYGD 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 593 SLQAFLIAIVVPDVEILPSWA-QKRGFQGSFEELCRNKDINKAILEDMVKLGKNAGLKPFEQVKGIAVHPELFSIDNGLL 671
Cdd:cd05927 442 SLKSFLVAIVVPDPDVLKEWAaSKGGGTGSFEELCKNPEVKKAILEDLVRLGKENGLKGFEQVKAIHLEPEPFSVENGLL 521
|
570 580
....*....|....*....|....
gi 564389119 672 TPTLKAKRPELRNYFRSQIDELYS 695
Cdd:cd05927 522 TPTFKLKRPQLKKYYKKQIDEMYK 545
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
87-697 |
0e+00 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 702.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 87 YDDVRTMYDGFQRGIQVSNDGPCLGSRKPNQ----PYEWISYKQVAEMAECIGSALIQKGFKPcsEQFIGIFSQNRPEWV 162
Cdd:PLN02736 40 HPEIGTLHDNFVYAVETFRDYKYLGTRIRVDgtvgEYKWMTYGEAGTARTAIGSGLVQHGIPK--GACVGLYFINRPEWL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 163 TIEQGCFTYSMVVVPLYDTLGTDAITYIVNKAELSVIFAdKPEKAKLLLEGVENklTPCLKIIVIMDSYDNDLVERGQKC 242
Cdd:PLN02736 118 IVDHACSAYSYVSVPLYDTLGPDAVKFIVNHAEVAAIFC-VPQTLNTLLSCLSE--IPSVRLIVVVGGADEPLPSLPSGT 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 243 GVEIIGLKALEDLGRVNRTKPKPPEPEDLAIICFTSGTTGNPKGAMVTHQNIMNDCSGFIKATESafiaSPEDVLISFLP 322
Cdd:PLN02736 195 GVEIVTYSKLLAQGRSSPQPFRPPKPEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKF----YPSDVHISYLP 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 323 LAHMFETVVECVMLCHGAKIGFFQGDIRLLMDDLKVLQPTIFPVVPRLLNRMFDRIFGQANTS--VKRWLLDFASKRKEA 400
Cdd:PLN02736 271 LAHIYERVNQIVMLHYGVAVGFYQGDNLKLMDDLAALRPTIFCSVPRLYNRIYDGITNAVKESggLKERLFNAAYNAKKQ 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 401 ELRSGivRNNS-LWDKLIFHKIQSSLGGKVRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTEctAGCCLSL--PGDWT 477
Cdd:PLN02736 351 ALENG--KNPSpMWDRLVFNKIKAKLGGRVRFMSSGASPLSPDVMEFLRICFGGRVLEGYGMTE--TSCVISGmdEGDNL 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 478 AGHVGAPMPCNYIKLVDVEDMNYQAAKG---EGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKII 554
Cdd:PLN02736 427 SGHVGSPNPACEVKLVDVPEMNYTSEDQpypRGEICVRGPIIFKGYYKDEVQTREVIDEDGWLHTGDIGLWLPGGRLKII 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 555 DRKKHIFKLAQGEYIAPEKIENIYLRSEAVAQVFVHGESLQAFLIAIVVPDVEILPSWAQKRGFQ-GSFEELCRNKDINK 633
Cdd:PLN02736 507 DRKKNIFKLAQGEYIAPEKIENVYAKCKFVAQCFVYGDSLNSSLVAVVVVDPEVLKAWAASEGIKyEDLKQLCNDPRVRA 586
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564389119 634 AILEDMVKLGKNAGLKPFEQVKGIAVHPELFSIDNGLLTPTLKAKRPELRNYFRSQIDELYSTI 697
Cdd:PLN02736 587 AVLADMDAVGREAQLRGFEFAKAVTLVPEPFTVENGLLTPTFKVKRPQAKAYFAKAISDMYAEL 650
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
87-695 |
0e+00 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 529.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 87 YDDVRTMYDGFQRGIQVSNDGPCLgSRKPNQPYEWISYKQVAEMAECIGSALIQKGFKPcsEQFIGIFSQNRPEWVTIEQ 166
Cdd:COG1022 7 VPPADTLPDLLRRRAARFPDRVAL-REKEDGIWQSLTWAEFAERVRALAAGLLALGVKP--GDRVAILSDNRPEWVIADL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 167 GCFTYSMVVVPLYDTLGTDAITYIVNKAELSVIFADKPEKAKLLLEGVENklTPCLKIIVIMDsydndlvERGQKCGVEI 246
Cdd:COG1022 84 AILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQEQLDKLLEVRDE--LPSLRHIVVLD-------PRGLRDDPRL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 247 IGLKALEDLGRvNRTKPKPPE-------PEDLAIICFTSGTTGNPKGAMVTHQNIMNDCsgfiKATESAFIASPEDVLIS 319
Cdd:COG1022 155 LSLDELLALGR-EVADPAELEarraavkPDDLATIIYTSGTTGRPKGVMLTHRNLLSNA----RALLERLPLGPGDRTLS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 320 FLPLAHMFETVVECVMLCHGAKIGFfQGDIRLLMDDLKVLQPTIFPVVPRLLNRMFDRIFGQANTS--VKRWLLDFA--- 394
Cdd:COG1022 230 FLPLAHVFERTVSYYALAAGATVAF-AESPDTLAEDLREVKPTFMLAVPRVWEKVYAGIQAKAEEAggLKRKLFRWAlav 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 395 SKRKEAELRSGivRNNSLW--------DKLIFHKIQSSLGGKVRLMITGAAPVSATVLTFLRAaLGCQFYEGYGQTECTA 466
Cdd:COG1022 309 GRRYARARLAG--KSPSLLlrlkhalaDKLVFSKLREALGGRLRFAVSGGAALGPELARFFRA-LGIPVLEGYGLTETSP 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 467 GCCLSLPGDWTAGHVGAPMPCNYIKLVDvedmnyqaakgEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWL 546
Cdd:COG1022 386 VITVNRPGDNRIGTVGPPLPGVEVKIAE-----------DGEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELD 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 547 PNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYLRSEAVAQVFVHGESlQAFLIAIVVPDVEILPSWAQKRGFQ-GSFEEL 625
Cdd:COG1022 455 EDGFLRITGRKKDLIVTSGGKNVAPQPIENALKASPLIEQAVVVGDG-RPFLAALIVPDFEALGEWAEENGLPyTSYAEL 533
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 626 CRNKDINKAILEDMVKLgkNAGLKPFEQVKGIAVHPELFSIDNGLLTPTLKAKRPELRNYFRSQIDELYS 695
Cdd:COG1022 534 AQDPEVRALIQEEVDRA--NAGLSRAEQIKRFRLLPKEFTIENGELTPTLKLKRKVILEKYADLIEALYA 601
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
117-682 |
3.67e-169 |
|
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: 492.50 E-value: 3.67e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 117 QPYEWISYKQVAEMAECIGSALIQKGFKPcsEQFIGIFSQNRPEWVTIEQGCFTYSMVVVPLYDTLGTDAITYIVNKAEL 196
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLIALGVEP--GDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 197 SVIFADKPEkaklllegvenkltpclkiivimdsydndlvergqkcgveiiglkaledlgrvnrtkpkppepeDLAIICF 276
Cdd:cd05907 79 KALFVEDPD----------------------------------------------------------------DLATIIY 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 277 TSGTTGNPKGAMVTHQNIMNDCSGFIKATEsafiASPEDVLISFLPLAHMFETV-VECVMLCHGAKIGFFQgDIRLLMDD 355
Cdd:cd05907 95 TSGTTGRPKGVMLSHRNILSNALALAERLP----ATEGDRHLSFLPLAHVFERRaGLYVPLLAGARIYFAS-SAETLLDD 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 356 LKVLQPTIFPVVPRLLNRMFDRIFGQANTSVKRWLLDFASkrkeaelrsgivrnnslwdklifhkiqsslGGKVRLMITG 435
Cdd:cd05907 170 LSEVRPTVFLAVPRVWEKVYAAIKVKAVPGLKRKLFDLAV------------------------------GGRLRFAASG 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 436 AAPVSATVLTFLRAaLGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYIKLVDvedmnyqaakgEGEVCVKGAN 515
Cdd:cd05907 220 GAPLPAELLHFFRA-LGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVEVRIAD-----------DGEILVRGPN 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 516 VFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYLRSEAVAQVFVHGESlQ 595
Cdd:cd05907 288 VMLGYYKNPEATAEALDADGWLHTGDLGEIDEDGFLHITGRKKDLIITSGGKNISPEPIENALKASPLISQAVVIGDG-R 366
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 596 AFLIAIVVPDVEILPSWAQKRG-FQGSFEELCRNKDINKAILEDMVKLgkNAGLKPFEQVKGIAVHPELFSIDNGLLTPT 674
Cdd:cd05907 367 PFLVALIVPDPEALEAWAEEHGiAYTDVAELAANPAVRAEIEAAVEAA--NARLSRYEQIKKFLLLPEPFTIENGELTPT 444
|
....*...
gi 564389119 675 LKAKRPEL 682
Cdd:cd05907 445 LKLKRPVI 452
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
118-698 |
8.15e-157 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 468.55 E-value: 8.15e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 118 PYEWISYKQVAEMAECIGSALIQKGFKPCSEqfIGIFSQNRPEWVTIEQGCFTYSMVVVPLYDTLGTDAITYIVNKAELS 197
Cdd:PLN02861 74 PYVWLTYKEVYDAAIRIGSAIRSRGVNPGDR--CGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVS 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 198 VIFADKPEKAKLLleGVENKLTPCLKIIVIMDSYDNDLVERGQKCGVEIIGLKALEDLGRVNRTKPkPPEPEDLAIICFT 277
Cdd:PLN02861 152 IAFVQESKISSIL--SCLPKCSSNLKTIVSFGDVSSEQKEEAEELGVSCFSWEEFSLMGSLDCELP-PKQKTDICTIMYT 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 278 SGTTGNPKGAMVTHQNIMNDC---SGFIKATESAfiASPEDVLISFLPLAHMFETVVECVMLCHGAKIGFFQGDIRLLMD 354
Cdd:PLN02861 229 SGTTGEPKGVILTNRAIIAEVlstDHLLKVTDRV--ATEEDSYFSYLPLAHVYDQVIETYCISKGASIGFWQGDIRYLME 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 355 DLKVLQPTIFPVVPRLlnrmFDRIFG------QANTSVKRWLLDFASKRKEAELRSGIVRNNS--LWDKLIFHKIQSSLG 426
Cdd:PLN02861 307 DVQALKPTIFCGVPRV----YDRIYTgimqkiSSGGMLRKKLFDFAYNYKLGNLRKGLKQEEAspRLDRLVFDKIKEGLG 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 427 GKVRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLSLPGDWT-AGHVGAPMPCNYIKLVDVEDMNYQAAKG 505
Cdd:PLN02861 383 GRVRLLLSGAAPLPRHVEEFLRVTSCSVLSQGYGLTESCGGCFTSIANVFSmVGTVGVPMTTIEARLESVPEMGYDALSD 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 506 --EGEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYLRSEA 583
Cdd:PLN02861 463 vpRGEICLRGNTLFSGYHKRQDLTEEVL-IDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSQGEYVAVENLENTYSRCPL 541
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 584 VAQVFVHGESLQAFLIAIVVPDVEILPSWAQKRGFQGSFEELCRNKDINKAILEDMVKLGKNAGLKPFEQVKGIAVHPEL 663
Cdd:PLN02861 542 IASIWVYGNSFESFLVAVVVPDRQALEDWAANNNKTGDFKSLCKNLKARKYILDELNSTGKKLQLRGFEMLKAIHLEPNP 621
|
570 580 590
....*....|....*....|....*....|....*
gi 564389119 664 FSIDNGLLTPTLKAKRPELRNYFRSQIDELYSTIK 698
Cdd:PLN02861 622 FDIERDLITPTFKLKRPQLLKYYKDCIDQLYSEAK 656
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
118-679 |
9.34e-157 |
|
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: 462.84 E-value: 9.34e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 118 PYEWISYKQVAEMAECIGSALIQKGFKPcsEQFIGIFSQNRPEWVTIEQGCFTYSMVVVPLYDTLGTDAITYIVNKAELS 197
Cdd:cd17639 2 EYKYMSYAEVWERVLNFGRGLVELGLKP--GDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 198 VIFADkpekaklllegvenkltpclkiivimdsydndlvergqkcgveiiglkaledlgrvnrtkpkpPEPEDLAIICFT 277
Cdd:cd17639 80 AIFTD---------------------------------------------------------------GKPDDLACIMYT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 278 SGTTGNPKGAMVTHQNIMNDCSGFIKATeSAFIaSPEDVLISFLPLAHMFETVVECVMLCHGAKIGFfqGDIRLLMD--- 354
Cdd:cd17639 97 SGSTGNPKGVMLTHGNLVAGIAGLGDRV-PELL-GPDDRYLAYLPLAHIFELAAENVCLYRGGTIGY--GSPRTLTDksk 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 355 -----DLKVLQPTIFPVVPRLLNRMFDRIFGQANT--SVKRWLLDFASKRKEAELRSGIvrNNSLWDKLIFHKIQSSLGG 427
Cdd:cd17639 173 rgckgDLTEFKPTLMVGVPAIWDTIRKGVLAKLNPmgGLKRTLFWTAYQSKLKALKEGP--GTPLLDELVFKKVRAALGG 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 428 KVRLMITGAAPVSATVLTFLrAALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYIKLVDVEDMNYQAAKGE- 506
Cdd:cd17639 251 RLRYMLSGGAPLSADTQEFL-NIVLCPVIQGYGLTETCAGGTVQDPGDLETGRVGPPLPCCEIKLVDWEEGGYSTDKPPp 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 507 -GEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYLRSEAVA 585
Cdd:cd17639 330 rGEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQNGEYIALEKLESIYRSNPLVN 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 586 QVFVHGESLQAFLIAIVVPDVEILPSWAQKRGF-QGSFEELCRNKDINKAILEDMVKLGKNAGLKPFEQVKGIAVHPELF 664
Cdd:cd17639 410 NICVYADPDKSYPVAIVVPNEKHLTKLAEKHGViNSEWEELCEDKKLQKAVLKSLAETARAAGLEKFEIPQGVVLLDEEW 489
|
570
....*....|....*
gi 564389119 665 SIDNGLLTPTLKAKR 679
Cdd:cd17639 490 TPENGLVTAAQKLKR 504
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
88-698 |
6.16e-156 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 466.42 E-value: 6.16e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 88 DDVRTMYDGFQRGIQVSNDGPCLGSR-----KPNQpYEWISYKQVAEMAECIGSALIQKGFKpcSEQFIGIFSQNRPEWV 162
Cdd:PLN02614 42 EGMDSCWDVFRMSVEKYPNNPMLGRReivdgKPGK-YVWQTYQEVYDIVIKLGNSLRSVGVK--DEAKCGIYGANSPEWI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 163 TIEQGCFTYSMVVVPLYDTLGTDAITYIVNKAELSVIFADKpEKAKLLLEGVENKlTPCLKIIVIMDSYDNDLVERGQKC 242
Cdd:PLN02614 119 ISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVEE-KKISELFKTCPNS-TEYMKTVVSFGGVSREQKEEAETF 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 243 GVEIIGLKALEDLGRVNRTKPKPPEPEDLAIICFTSGTTGNPKGAMVTHQNIMNDCSGFIKATESAFIA-SPEDVLISFL 321
Cdd:PLN02614 197 GLVIYAWDEFLKLGEGKQYDLPIKKKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLKSANAAlTVKDVYLSYL 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 322 PLAHMFETVVECVMLCHGAKIGFFQGDIRLLMDDLKVLQPTIFPVVPRLLNRMFDRIfgQANTS----VKRWLLDFASKR 397
Cdd:PLN02614 277 PLAHIFDRVIEECFIQHGAAIGFWRGDVKLLIEDLGELKPTIFCAVPRVLDRVYSGL--QKKLSdggfLKKFVFDSAFSY 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 398 KEAELRSGI--VRNNSLWDKLIFHKIQSSLGGKVRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLSLPGD 475
Cdd:PLN02614 355 KFGNMKKGQshVEASPLCDKLVFNKVKQGLGGNVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTESCAGTFVSLPDE 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 476 W-TAGHVGAPMPCNYIKLVDVEDMNYQA--AKGEGEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLK 552
Cdd:PLN02614 435 LdMLGTVGPPVPNVDIRLESVPEMEYDAlaSTPRGEICIRGKTLFSGYYKREDLTKEVL-IDGWLHTGDVGEWQPNGSMK 513
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 553 IIDRKKHIFKLAQGEYIAPEKIENIYLRSEAVAQVFVHGESLQAFLIAIVVPDVEILPSWAQKRGFQGSFEELCRNKDIN 632
Cdd:PLN02614 514 IIDRKKNIFKLSQGEYVAVENIENIYGEVQAVDSVWVYGNSFESFLVAIANPNQQILERWAAENGVSGDYNALCQNEKAK 593
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564389119 633 KAILEDMVKLGKNAGLKPFEQVKGIAVHPELFSIDNGLLTPTLKAKRPELRNYFRSQIDELYSTIK 698
Cdd:PLN02614 594 EFILGELVKMAKEKKMKGFEIIKAIHLDPVPFDMERDLLTPTFKKKRPQLLKYYQSVIDEMYKTTN 659
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
89-697 |
8.95e-154 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 460.44 E-value: 8.95e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 89 DVRTMYDGFQRGIQVSNDGPCLGSRKPNQ----PYEWISYKQVAEMAECIGSALIQKGFKPCSEqfIGIFSQNRPEWVTI 164
Cdd:PLN02430 40 DITTAWDIFSKSVEKYPDNKMLGWRRIVDgkvgPYMWKTYKEVYEEVLQIGSALRASGAEPGSR--VGIYGSNCPQWIVA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 165 EQGCFTYSMVVVPLYDTLGTDAITYIVNKAELSVIFA-DKpeKAKLLLEGvENKLTPCLKIIVIMDSYDNDLVERGQKCG 243
Cdd:PLN02430 118 MEACAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVFVqDK--KIKELLEP-DCKSAKRLKAIVSFTSVTEEESDKASQIG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 244 VEIIGLKALEDLGRVNRTKPKPPEPEDLAIICFTSGTTGNPKGAMVTHQNIMNDCSG---FIKATESAFiaSPEDVLISF 320
Cdd:PLN02430 195 VKTYSWIDFLHMGKENPSETNPPKPLDICTIMYTSGTSGDPKGVVLTHEAVATFVRGvdlFMEQFEDKM--THDDVYLSF 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 321 LPLAHMFETVVECVMLCHGAKIGFFQGDIRLLMDDLKVLQPTIFPVVPRLLNRMFDRIFG--QANTSVKRWLLDFASKRK 398
Cdd:PLN02430 273 LPLAHILDRMIEEYFFRKGASVGYYHGDLNALRDDLMELKPTLLAGVPRVFERIHEGIQKalQELNPRRRLIFNALYKYK 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 399 EAELRSGIVRNNS--LWDKLIFHKIQSSLGGKVRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLSLPGDW 476
Cdd:PLN02430 353 LAWMNRGYSHKKAspMADFLAFRKVKAKLGGRLRLLISGGAPLSTEIEEFLRVTSCAFVVQGYGLTETLGPTTLGFPDEM 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 477 TA-GHVGAPMPCNYIKLVDVEDMNYQAAkGE---GEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLK 552
Cdd:PLN02430 433 CMlGTVGAPAVYNELRLEEVPEMGYDPL-GEpprGEICVRGKCLFSGYYKNPELTEEVM-KDGWFHTGDIGEILPNGVLK 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 553 IIDRKKHIFKLAQGEYIAPEKIENIYLRSEAVAQVFVHGESLQAFLIAIVVPDVEILPSWAQKRGFQGSFEELCRNKDIN 632
Cdd:PLN02430 511 IIDRKKNLIKLSQGEYVALEYLENVYGQNPIVEDIWVYGDSFKSMLVAVVVPNEENTNKWAKDNGFTGSFEELCSLPELK 590
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564389119 633 KAILEDMVKLGKNAGLKPFEQVKGIAVHPELFSIDNGLLTPTLKAKRPELRNYFRSQIDELYSTI 697
Cdd:PLN02430 591 EHILSELKSTAEKNKLRGFEYIKGVILETKPFDVERDLVTATLKKRRNNLLKYYQVEIDEMYRKL 655
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
118-695 |
1.14e-132 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 407.20 E-value: 1.14e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 118 PYEWISYKQVAEMAECIGSALIQKGFKpcSEQFIGIFSQNRPEWVTIEQGCFTYSMVVVPLYDTLGTDAITYIVNKAELS 197
Cdd:PLN02387 103 EYEWITYGQVFERVCNFASGLVALGHN--KEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVT 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 198 VIFADKPEKAKLLleGVENKLTPCLKIIVIMDSYDNDLVERGQKCGVEIIGLKALEDLGRVNRTKPKPPEPEDLAIICFT 277
Cdd:PLN02387 181 TVICDSKQLKKLI--DISSQLETVKRVIYMDDEGVDSDSSLSGSSNWTVSSFSEVEKLGKENPVDPDLPSPNDIAVIMYT 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 278 SGTTGNPKGAMVTHQNIMndcsgfikATESAFIA-----SPEDVLISFLPLAHMFETVVECVMLCHGAKIGFfqGDIRLL 352
Cdd:PLN02387 259 SGSTGLPKGVMMTHGNIV--------ATVAGVMTvvpklGKNDVYLAYLPLAHILELAAESVMAAVGAAIGY--GSPLTL 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 353 MD-----------DLKVLQPTIFPVVPRLLNRMFDRIFGQANTS---VKRwLLDFASKRKEAELR------SGIVRnnSL 412
Cdd:PLN02387 329 TDtsnkikkgtkgDASALKPTLMTAVPAILDRVRDGVRKKVDAKgglAKK-LFDIAYKRRLAAIEgswfgaWGLEK--LL 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 413 WDKLIFHKIQSSLGGKVRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYIKL 492
Cdd:PLN02387 406 WDALVFKKIRAVLGGRIRFMLSGGAPLSGDTQRFINICLGAPIGQGYGLTETCAGATFSEWDDTSVGRVGPPLPCCYVKL 485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 493 VDVEDMNYQAAKG---EGEVCVKGANVFKGYLKDPARTAEA--LDKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLAQ 565
Cdd:PLN02387 486 VSWEEGGYLISDKpmpRGEIVIGGPSVTLGYFKNQEKTDEVykVDERGmrWFYTGDIGQFHPDGCLEIIDRKKDIVKLQH 565
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 566 GEYIAPEKIENIYLRSEAVAQVFVHGESLQAFLIAIVVPDVEILPSWAQKRGFQ-GSFEELCRNKDINKAILEDMVKLGK 644
Cdd:PLN02387 566 GEYVSLGKVEAALSVSPYVDNIMVHADPFHSYCVALVVPSQQALEKWAKKAGIDySNFAELCEKEEAVKEVQQSLSKAAK 645
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 564389119 645 NAGLKPFEQVKGIAVHPELFSIDNGLLTPTLKAKRPELRNYFRSQIDELYS 695
Cdd:PLN02387 646 AARLEKFEIPAKIKLLPEPWTPESGLVTAALKLKREQIRKKFKDDLKKLYE 696
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
118-564 |
2.47e-128 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 386.28 E-value: 2.47e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 118 PYEWISYKQVAEMAECIGSALIQKGFKPcsEQFIGIFSQNRPEWVTIEQGCFTYSMVVVPLYDTLGTDAITYIVNKAELS 197
Cdd:pfam00501 18 EGRRLTYRELDERANRLAAGLRALGVGK--GDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSGAK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 198 VIFADKPEKAKLLLEGVENKLTPCLKIIVIMDSydndlvergqkcGVEIIGLKALEDLGRVNRTKPKPPEPEDLAIICFT 277
Cdd:pfam00501 96 VLITDDALKLEELLEALGKLEVVKLVLVLDRDP------------VLKEEPLPEEAKPADVPPPPPPPPDPDDLAYIIYT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 278 SGTTGNPKGAMVTHQNIMNDCSGFIKATESAFIASPEDVLISFLPLAHMFETVVEC-VMLCHGAKIGFFQGDIRL----L 352
Cdd:pfam00501 164 SGTTGKPKGVMLTHRNLVANVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSLGLlGPLLAGATVVLPPGFPALdpaaL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 353 MDDLKVLQPTIFPVVPRLLNRMFDrifgqantsvkrwlldfaSKRKEAELRSGivrnnslwdklifhkiqsslggkVRLM 432
Cdd:pfam00501 244 LELIERYKVTVLYGVPTLLNMLLE------------------AGAPKRALLSS-----------------------LRLV 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 433 ITGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLSLPGDW---TAGHVGAPMPCNYIKLVDVEDMNYQAAKGEGEV 509
Cdd:pfam00501 283 LSGGAPLPPELARRFRELFGGALVNGYGLTETTGVVTTPLPLDEdlrSLGSVGRPLPGTEVKIVDDETGEPVPPGEPGEL 362
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 564389119 510 CVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLA 564
Cdd:pfam00501 363 CVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
122-694 |
4.42e-98 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 316.92 E-value: 4.42e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 122 ISYKQVAEMAECIGSALIQKGFKPCSEqfIGIFSQNRPEWVTIEQGCFTYSMVVVPLYDTLGTDAITYIVNKAELSVIFA 201
Cdd:PTZ00216 122 ITYAELWERIVNFGRGLAELGLTKGSN--VAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAIVC 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 202 DKpEKAKLLLEGVENKLTPCLKIIvimdsYDNDLVERGQKCGVEIIGLKALEDLGRVNRTKPKPPEPE---DLAIICFTS 278
Cdd:PTZ00216 200 NG-KNVPNLLRLMKSGGMPNTTII-----YLDSLPASVDTEGCRLVAWTDVVAKGHSAGSHHPLNIPEnndDLALIMYTS 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 279 GTTGNPKGAMVTHQNIMNDCSGF-IKATESAFIASPEDVLISFLPLAHMFETVVECVMLCHGAKIGFfqGDIRLLMD--- 354
Cdd:PTZ00216 274 GTTGDPKGVMHTHGSLTAGILALeDRLNDLIGPPEEDETYCSYLPLAHIMEFGVTNIFLARGALIGF--GSPRTLTDtfa 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 355 ----DLKVLQPTIFPVVPRLlnrmFDRI----------FGqantSVKRWLLDFASKRKEAELRSGivRNNSLWDKLIFHK 420
Cdd:PTZ00216 352 rphgDLTEFRPVFLIGVPRI----FDTIkkaveaklppVG----SLKRRVFDHAYQSRLRALKEG--KDTPYWNEKVFSA 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 421 IQSSLGGKVRLMITGAAPVSATVLTFLRAALGCqFYEGYGQTECTagCC--LSLPGDWTAGHVGAPMPCNYIKLVDVEDM 498
Cdd:PTZ00216 422 PRAVLGGRVRAMLSGGGPLSAATQEFVNVVFGM-VIQGWGLTETV--CCggIQRTGDLEPNAVGQLLKGVEMKLLDTEEY 498
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 499 NY-QAAKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENI 577
Cdd:PTZ00216 499 KHtDTPEPRGEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVKALAKNCLGEYIALEALEAL 578
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 578 YLRSEAVAQ----VFVHgeSLQAFLIAIVVPDVEILPSWAQKRGFQGSFEELCRNKDINKAILEDMVKLGKNAGLKPFEQ 653
Cdd:PTZ00216 579 YGQNELVVPngvcVLVH--PARSYICALVLTDEAKAMAFAKEHGIEGEYPAILKDPEFQKKATESLQETARAAGRKSFEI 656
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 564389119 654 VKGIAVHPELFSIDNGLLTPTLKAKRPELRNYFRSQIDELY 694
Cdd:PTZ00216 657 VRHVRVLSDEWTPENGVLTAAMKLKRRVIDERYADLIKELF 697
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
117-680 |
1.73e-90 |
|
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: 290.03 E-value: 1.73e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 117 QPYEWISYKQVAEMAECIGSALIQKGFKPcsEQFIGIFSQNRPEWVTIEQGCFTYSMVVVPLYDTLGTDAITYIVNKAEL 196
Cdd:cd17640 1 KPPKRITYKDLYQEILDFAAGLRSLGVKA--GEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 197 SVIFadkpekaklllegVENkltpclkiivimdsydndlvergqkcgveiiglkaledlgrvnrtkpkppEPEDLAIICF 276
Cdd:cd17640 79 VALV-------------VEN--------------------------------------------------DSDDLATIIY 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 277 TSGTTGNPKGAMVTHQNIMNDCSGFikateSAFI-ASPEDVLISFLPLAHMFETVVECVMLCHGAKIGFfqGDIRLLMDD 355
Cdd:cd17640 96 TSGTTGNPKGVMLTHANLLHQIRSL-----SDIVpPQPGDRFLSILPIWHSYERSAEYFIFACGCSQAY--TSIRTLKDD 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 356 LKVLQPTIFPVVPRLlnrmfdrifgqantsvkrWlldfaskrkEAeLRSGI---VRNNSLWDKLIFHKIQSslGGKVRLM 432
Cdd:cd17640 169 LKRVKPHYIVSVPRL------------------W---------ES-LYSGIqkqVSKSSPIKQFLFLFFLS--GGIFKFG 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 433 ITGAAPVSATVLTFLRaALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYIKLVDVEDMNYQAAKGEGEVCVK 512
Cdd:cd17640 219 ISGGGALPPHVDTFFE-AIGIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIVDPEGNVVLPPGEKGIVWVR 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 513 GANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYLRSEAVAQVFVHGE 592
Cdd:cd17640 298 GPQVMKGYYKNPEATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSNGENVEPQPIEEALMRSPFIEQIMVVGQ 377
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 593 SlQAFLIAIVVPDVEILPSWAQKRG--FQGSFEELCRNKDINKAI-LEDMVKLGKNAGLKPFEQVKGIAVHPELFsIDNG 669
Cdd:cd17640 378 D-QKRLGALIVPNFEELEKWAKESGvkLANDRSQLLASKKVLKLYkNEIKDEISNRPGFKSFEQIAPFALLEEPF-IENG 455
|
570
....*....|.
gi 564389119 670 LLTPTLKAKRP 680
Cdd:cd17640 456 EMTQTMKIKRN 466
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
119-679 |
7.75e-81 |
|
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: 265.87 E-value: 7.75e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 119 YEWISYKQVAEMAECIGSALIQKGFKPCSEqfIGIFSQNRPEWVTIEQGCFTYSMVVVPLYDTLGTDAITYIVNKAELSV 198
Cdd:cd05932 4 VVEFTWGEVADKARRLAAALRALGLEPGSK--IALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 199 IFADK----PEKAKLLLEGVENKLTPCLKIIVIMDSYDnDLVERGQkcgveiiglkALEDlgrvnrtKPkPPEPEDLAII 274
Cdd:cd05932 82 LFVGKlddwKAMAPGVPEGLISISLPPPSAANCQYQWD-DLIAQHP----------PLEE-------RP-TRFPEQLATL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 275 CFTSGTTGNPKGAMVTHQNIMNDCSGFIKAtesaFIASPEDVLISFLPLAHMFETV-VECVMLCHGAKIgFFQGDIRLLM 353
Cdd:cd05932 143 IYTSGTTGQPKGVMLTFGSFAWAAQAGIEH----IGTEENDRMLSYLPLAHVTERVfVEGGSLYGGVLV-AFAESLDTFV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 354 DDLKVLQPTIFPVVPRLLNRMFDRIFGQANTSVKRWLLDFaskrkeaelrsgivrnnSLWDKLIFHKIQSSLG-GKVRLM 432
Cdd:cd05932 218 EDVQRARPTLFFSVPRLWTKFQQGVQDKIPQQKLNLLLKI-----------------PVVNSLVKRKVLKGLGlDQCRLA 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 433 ITGAAPVSATVLTFLRAaLGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYIKLVDvedmnyqaakgEGEVCVK 512
Cdd:cd05932 281 GCGSAPVPPALLEWYRS-LGLNILEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRISE-----------DGEILVR 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 513 GANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYLRSEAVAQVFVHGE 592
Cdd:cd05932 349 SPALMMGYYKDPEATAEAFTADGFLRTGDKGELDADGNLTITGRVKDIFKTSKGKYVAPAPIENKLAEHDRVEMVCVIGS 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 593 SLQAfLIAIVVPDVEILPSwaQKRGFQGSFEELCRnkdinkAILEDMvklgkNAGLKPFEQVKGIAVHPELFSIDNGLLT 672
Cdd:cd05932 429 GLPA-PLALVVLSEEARLR--ADAFARAELEASLR------AHLARV-----NSTLDSHEQLAGIVVVKDPWSIDNGILT 494
|
....*..
gi 564389119 673 PTLKAKR 679
Cdd:cd05932 495 PTLKIKR 501
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
122-616 |
8.98e-72 |
|
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: 240.10 E-value: 8.98e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 122 ISYKQVAEMAECIGSALIQKGFKPcsEQFIGIFSQNRPEWVTIEQGCFTYSMVVVPLYDTLGTDAITYIVNKAELSVIFA 201
Cdd:COG0318 25 LTYAELDARARRLAAALRALGVGP--GDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEELAYILEDSGARALVT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 202 dkpekaklllegvenkltpclkiivimdsydndlvergqkcgveiiglkaledlgrvnrtkpkppepedlAIICFTSGTT 281
Cdd:COG0318 103 ----------------------------------------------------------------------ALILYTSGTT 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 282 GNPKGAMVTHQNIMNDCSGFIKATEsafiASPEDVLISFLPLAHMFETVVECVM-LCHGAKI----GFfqgDIRLLMDDL 356
Cdd:COG0318 113 GRPKGVMLTHRNLLANAAAIAAALG----LTPGDVVLVALPLFHVFGLTVGLLApLLAGATLvllpRF---DPERVLELI 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 357 KVLQPTIFPVVPRLLNRMFDRifgqantsvkrwlldfaSKRKEAELRSgivrnnslwdklifhkiqsslggkVRLMITGA 436
Cdd:COG0318 186 ERERVTVLFGVPTMLARLLRH-----------------PEFARYDLSS------------------------LRLVVSGG 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 437 APVSATVLTFLRAALGCQFYEGYGQTECTAGCCLSLPGDWTA--GHVGAPMPCNYIKLVDvEDMNYQAAKGEGEVCVKGA 514
Cdd:COG0318 225 APLPPELLERFEERFGVRIVEGYGLTETSPVVTVNPEDPGERrpGSVGRPLPGVEVRIVD-EDGRELPPGEVGEIVVRGP 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 515 NVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYLRSEAVAQVFV----- 589
Cdd:COG0318 304 NVMKGYWNDPEATAEAF-RDGWLRTGDLGRLDEDGYLYIVGRKKDMIISG-GENVYPAEVEEVLAAHPGVAEAAVvgvpd 381
|
490 500 510
....*....|....*....|....*....|.
gi 564389119 590 --HGESLQAFLI--AIVVPDVEILPSWAQKR 616
Cdd:COG0318 382 ekWGERVVAFVVlrPGAELDAEELRAFLRER 412
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
114-694 |
8.84e-68 |
|
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: 233.40 E-value: 8.84e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 114 KPNQPYEWISYKQVAEMAECIGSALIQKGFkpcsEQF--IGIFSQNRPEWVTIEQGCFTYSMVVVPLYDTLGTDAITYIV 191
Cdd:cd05933 1 KRGDKWHTLTYKEYYEACRQAAKAFLKLGL----ERFhgVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 192 NKAELSVIFADKPEKAKLLLEgVENKLtPCLKIIVImdsYDNDLVERGQKcgveIIGLKALEDLGRvnrtkpKPPEPEDL 271
Cdd:cd05933 77 ETSEANILVVENQKQLQKILQ-IQDKL-PHLKAIIQ---YKEPLKEKEPN----LYSWDEFMELGR------SIPDEQLD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 272 AII-------C----FTSGTTGNPKGAMVTHQNIMNDCSGFIKATESAFIASPEDVLISFLPLAHMFETVVEcVMLC--H 338
Cdd:cd05933 142 AIIssqkpnqCctliYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLRPATVGQESVVSYLPLSHIAAQILD-IWLPikV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 339 GAKIGFFQGDIR--LLMDDLKVLQPTIFPVVPRLLNRMFDRI--FGQANTSVKRWLLDFAsKRKEAE-------LRSGIV 407
Cdd:cd05933 221 GGQVYFAQPDALkgTLVKTLREVRPTAFMGVPRVWEKIQEKMkaVGAKSGTLKRKIASWA-KGVGLEtnlklmgGESPSP 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 408 RNNSLWDKLIFHKIQSSLG-GKVRLMITGAAPVSATVLTFLrAALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMP 486
Cdd:cd05933 300 LFYRLAKKLVFKKVRKALGlDRCQKFFTGAAPISRETLEFF-LSLNIPIMELYGMSETSGPHTISNPQAYRLLSCGKALP 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 487 CNYIKLVDvedmnyQAAKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQG 566
Cdd:cd05933 379 GCKTKIHN------PDADGIGEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITAGG 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 567 EYIAPEKIEN-IYLRSEAVAQVFVHGESLQaFLIAIVVPDVEILP--------------SWAQKRGFQGS-FEELCRNKD 630
Cdd:cd05933 453 ENVPPVPIEDaVKKELPIISNAMLIGDKRK-FLSMLLTLKCEVNPetgepldelteeaiEFCRKLGSQATrVSEIAGGKD 531
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564389119 631 --INKAILEDMVKLGKNAGLKPfEQVKGIAVHPELFSIDNGLLTPTLKAKRPELRNYFRSQIDELY 694
Cdd:cd05933 532 pkVYEAIEEGIKRVNKKAISNA-QKIQKWVILEKDFSVPGGELGPTMKLKRPVVAKKYKDEIDKLY 596
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
122-679 |
7.01e-67 |
|
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: 230.39 E-value: 7.01e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 122 ISYKQVAEMAECIGSALIQKGFKPcsEQFIGIFSQNRPEWVTIEQGCFTYSMVVVPLYDTLGTDAITYIVNKAELSVIFA 201
Cdd:cd17641 12 FTWADYADRVRAFALGLLALGVGR--GDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 202 DKPEKAKLLLEgVENKLTPCLKIIVI----MDSYDN-------DLVERGQKCGVEIIGLkaLEDlgRVNRTKPkppepED 270
Cdd:cd17641 90 EDEEQVDKLLE-IADRIPSVRYVIYCdprgMRKYDDprlisfeDVVALGRALDRRDPGL--YER--EVAAGKG-----ED 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 271 LAIICFTSGTTGNPKGAMVTHQNIMNDCSGFIKATESafiaSPEDVLISFLPLAHMFETVVECVM-LCHGAKIGFFQgDI 349
Cdd:cd17641 160 VAVLCTTSGTTGKPKLAMLSHGNFLGHCAAYLAADPL----GPGDEYVSVLPLPWIGEQMYSVGQaLVCGFIVNFPE-EP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 350 RLLMDDLKVLQPTIFPVVPRLLNRM--FDRIFGQANTSVKRWLLDF--------ASKRKEAELRSGIVRNNS-LWDKLIF 418
Cdd:cd17641 235 ETMMEDLREIGPTFVLLPPRVWEGIaaDVRARMMDATPFKRFMFELgmklglraLDRGKRGRPVSLWLRLASwLADALLF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 419 HKIQSSLG-GKVRLMITGAAPVSATVLTFLRAaLGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYIKLVDVed 497
Cdd:cd17641 315 RPLRDRLGfSRLRSAATGGAALGPDTFRFFHA-IGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGTEVRIDEV-- 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 498 mnyqaakgeGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIEN- 576
Cdd:cd17641 392 ---------GEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTTSDGTRFSPQFIENk 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 577 ----IYLRsEAVaqVFVHGeslQAFLIAIVVPDVEILPSWAQKRGFQ-GSFEELCRNKDINKAILEDMVKLgkNAGLKPF 651
Cdd:cd17641 463 lkfsPYIA-EAV--VLGAG---RPYLTAFICIDYAIVGKWAEQRGIAfTTYTDLASRPEVYELIRKEVEKV--NASLPEA 534
|
570 580
....*....|....*....|....*...
gi 564389119 652 EQVKGIAVHPELFSIDNGLLTPTLKAKR 679
Cdd:cd17641 535 QRIRRFLLLYKELDADDGELTRTRKVRR 562
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
122-679 |
1.02e-66 |
|
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: 226.94 E-value: 1.02e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 122 ISYKQVAEMAECIGSALIQKGFKPCSEqfIGIFSQNRPEWVTIEQGCFTYSMVVVPLYDTLGTDAITYIVNKAELSVIFA 201
Cdd:cd05914 8 LTYKDLADNIAKFALLLKINGVGTGDR--VALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 202 DkpekaklllegvenkltpclkiivimdsydndlvergqkcgveiiglkaledlgrvnrtkpkppEPEDLAIICFTSGTT 281
Cdd:cd05914 86 S----------------------------------------------------------------DEDDVALINYTSGTT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 282 GNPKGAMVTHQNIMNDCSGfIKATEsafIASPEDVLISFLPLAHMFETVVECVM-LCHGAKIGFFQGDIRLLMDDLKVLQ 360
Cdd:cd05914 102 GNSKGVMLTYRNIVSNVDG-VKEVV---LLGKGDKILSILPLHHIYPLTFTLLLpLLNGAHVVFLDKIPSAKIIALAFAQ 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 361 PTIFPVVPRLLNRMFDRIFGQANTSVKRWLLdfaskrkeaeLRSGIVRNNSLWDKLIFHKIQSSLGGKVRLMITGAAPVS 440
Cdd:cd05914 178 VTPTLGVPVPLVIEKIFKMDIIPKLTLKKFK----------FKLAKKINNRKIRKLAFKKVHEAFGGNIKEFVIGGAKIN 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 441 ATVLTFLRAaLGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPmpcnyIKLVDVEDMNYQAAKGEGEVCVKGANVFKGY 520
Cdd:cd05914 248 PDVEEFLRT-IGFPYTIGYGMTETAPIISYSPPNRIRLGSAGKV-----IDGVEVRIDSPDPATGEGEIIVRGPNVMKGY 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 521 LKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYLRSEAVAQ--VFV-HGEslqaf 597
Cdd:cd05914 322 YKNPEATAEAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSSGKNIYPEEIEAKINNMPFVLEslVVVqEKK----- 396
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 598 LIAIVVPDVEILPSWAQKrgfqgsfeelcrNKDINKAILEDMVKlGKNAGLKPFEQVKGIAVHPELFSidnglLTPTLKA 677
Cdd:cd05914 397 LVALAYIDPDFLDVKALK------------QRNIIDAIKWEVRD-KVNQKVPNYKKISKVKIVKEEFE-----KTPKGKI 458
|
..
gi 564389119 678 KR 679
Cdd:cd05914 459 KR 460
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
270-604 |
5.12e-65 |
|
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: 218.31 E-value: 5.12e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 270 DLAIICFTSGTTGNPKGAMVTHQNIMndcsGFIKATESAFIASPEDVLISFLPLAHMFETVVECVMLCHGAKI----GFF 345
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLL----AAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVvllpKFD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 346 QGDIRLLMDDLKVlqpTIFPVVPRLLNRMFDRIfgqantsvkrwlldfasKRKEAELRSgivrnnslwdklifhkiqssl 425
Cdd:cd04433 77 PEAALELIEREKV---TILLGVPTLLARLLKAP-----------------ESAGYDLSS--------------------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 426 ggkVRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLSLPGDWT--AGHVGAPMPCNYIKLVDVEDmNYQAA 503
Cdd:cd04433 116 ---LRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTVATGPPDDDArkPGSVGRPVPGVEVRIVDPDG-GELPP 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 504 KGEGEVCVKGANVFKGYLKDPARTAEAlDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYLRSEA 583
Cdd:cd04433 192 GEIGELVVRGPSVMKGYWNNPEATAAV-DEDGWYRTGDLGRLDEDGYLYIVGRLKDMIK-SGGENVYPAEVEAVLLGHPG 269
|
330 340
....*....|....*....|....
gi 564389119 584 VAQVFVHG---ESLQAFLIAIVVP 604
Cdd:cd04433 270 VAEAAVVGvpdPEWGERVVAVVVL 293
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
148-672 |
5.36e-62 |
|
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: 217.71 E-value: 5.36e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 148 EQFIGIFSQNRPEWVTIEQGCFTYSMVVVPLYDTLGTDAITYIVNKAELSVIFADkPEKAKLLLEGVENKLTPclKIIVI 227
Cdd:cd17632 93 GDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAVS-AEHLDLAVEAVLEGGTP--PRLVV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 228 MDSYDNDLVER-----------GQKCGVEIIGLKALEDLGrVNRTKPKPPEPED--LAIICFTSGTTGNPKGAMVTHQNI 294
Cdd:cd17632 170 FDHRPEVDAHRaalesarerlaAVGIPVTTLTLIAVRGRD-LPPAPLFRPEPDDdpLALLIYTSGSTGTPKGAMYTERLV 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 295 MN---DCSGFIKATEsafiasPEDVLISFLPLAHMFETVVECVMLCHGAkIGFFQG--DIRLLMDDLKVLQPTIFPVVPR 369
Cdd:cd17632 249 ATfwlKVSSIQDIRP------PASITLNFMPMSHIAGRISLYGTLARGG-TAYFAAasDMSTLFDDLALVRPTELFLVPR 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 370 LLNRMFDRIfgQAntSVKRWLLDFA-----SKRKEAELRsgivrnnslwdklifhkiQSSLGGKVRLMITGAAPVSATVL 444
Cdd:cd17632 322 VCDMLFQRY--QA--ELDRRSVAGAdaetlAERVKAELR------------------ERVLGGRLLAAVCGSAPLSAEMK 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 445 TFLRAALGCQFYEGYGQTEctAGCCLSLpgdwtaGHVGAPMPCNYiKLVDVEDMNYQAAKG---EGEVCVKGANVFKGYL 521
Cdd:cd17632 380 AFMESLLDLDLHDGYGSTE--AGAVILD------GVIVRPPVLDY-KLVDVPELGYFRTDRphpRGELLVKTDTLFPGYY 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 522 KDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYLRSEAVAQVFVHGESLQAFLIAI 601
Cdd:cd17632 451 KRPEVTAEVFDEDGFYRTGDVMAELGPDRLVYVDRRNNVLKLSQGEFVTVARLEAVFAASPLVRQIFVYGNSERAYLLAV 530
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564389119 602 VVPdveilpswAQKRGFQGSFEELcrnkdiNKAILEDMVKLGKNAGLKPFEQVKGIAVHPELFSIDNGLLT 672
Cdd:cd17632 531 VVP--------TQDALAGEDTARL------RAALAESLQRIAREAGLQSYEIPRDFLIETEPFTIANGLLS 587
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
120-604 |
8.51e-59 |
|
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: 205.87 E-value: 8.51e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 120 EWISYKQVAEMAECIGSALIQKGFKPCSEqfIGIFSQNRPEWVTIEQGCFTYSMVVVPLYDTLGTDAITYIVNKAELSVI 199
Cdd:cd05936 23 RKLTYRELDALAEAFAAGLQNLGVQPGDR--VALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPRELEHILNDSGAKAL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 200 FADKPEKaklllegvenkltpclkiivimdsydnDLVERGQKcgveiiglkaledlgrvnRTKPKPPEPEDLAIICFTSG 279
Cdd:cd05936 101 IVAVSFT---------------------------DLLAAGAP------------------LGERVALTPEDVAVLQYTSG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 280 TTGNPKGAMVTHQNIMNDCSGFIKATESAFiaSPEDVLISFLPLAHMF-ETVVECVMLCHGAKIGFFQG-DIRLLMDDLK 357
Cdd:cd05936 136 TTGVPKGAMLTHRNLVANALQIKAWLEDLL--EGDDVVLAALPLFHVFgLTVALLLPLALGATIVLIPRfRPIGVLKEIR 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 358 VLQPTIFPVVPRLLNRMFDrifgqantsvkrwlldfASKRKEAELRSgivrnnslwdklifhkiqsslggkVRLMITGAA 437
Cdd:cd05936 214 KHRVTIFPGVPTMYIALLN-----------------APEFKKRDFSS------------------------LRLCISGGA 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 438 PVSATVLTFLRAALGCQFYEGYGQTECT-AGCCLSLPGDWTAGHVGAPMPCNYIKLVDVEDMnyQAAKGE-GEVCVKGAN 515
Cdd:cd05936 253 PLPVEVAERFEELTGVPIVEGYGLTETSpVVAVNPLDGPRKPGSIGIPLPGTEVKIVDDDGE--ELPPGEvGELWVRGPQ 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 516 VFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAVAQVFV------ 589
Cdd:cd05936 331 VMKGYWNRPEETAEAF-VDGWLRTGDIGYMDEDGYFFIVDRKKDMI-IVGGFNVYPREVEEVLYEHPAVAEAAVvgvpdp 408
|
490
....*....|....*.
gi 564389119 590 -HGESLQAFliaiVVP 604
Cdd:cd05936 409 ySGEAVKAF----VVL 420
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
122-591 |
3.87e-58 |
|
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: 204.37 E-value: 3.87e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 122 ISYKQVAEMAECIGSALIQKGFKPcsEQFIGIFSQNRPEWVTIEQGCFTYSMVVVPLYDTLGTDAITYIVNKAELSVIFA 201
Cdd:cd05911 11 LTYAQLRTLSRRLAAGLRKLGLKK--GDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 202 DKPEKAKLLleGVENKLTPCLKIIVIMDsydndlveRGQKCGVEIIGLKALEDLGRVNRTKPKPPEPEDLAIICFTSGTT 281
Cdd:cd05911 89 DPDGLEKVK--EAAKELGPKDKIIVLDD--------KPDGVLSIEDLLSPTLGEEDEDLPPPLKDGKDDTAAILYSSGTT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 282 GNPKGAMVTHQNIMNDCSGFIKATESAFiaSPEDVLISFLPLAHMFETVVECVMLCHGAK-IGFFQGDIRLLMDDLKVLQ 360
Cdd:cd05911 159 GLPKGVCLSHRNLIANLSQVQTFLYGND--GSNDVILGFLPLYHIYGLFTTLASLLNGATvIIMPKFDSELFLDLIEKYK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 361 PTIFPVVPRLLNRMFdrifgqantsvkrwlldfaskrkeaelRSGIVRNNSLwdklifhkiqSSLggkvRLMITGAAPVS 440
Cdd:cd05911 237 ITFLYLVPPIAAALA---------------------------KSPLLDKYDL----------SSL----RVILSGGAPLS 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 441 ATVLTFLRAALG-CQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPcNY-IKLVDVEDMNYQAAKGEGEVCVKGANVFK 518
Cdd:cd05911 276 KELQELLAKRFPnATIKQGYGMTETGGILTVNPDGDDKPGSVGRLLP-NVeAKIVDDDGKDSLGPNEPGEICVRGPQVMK 354
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564389119 519 GYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSEAVAQVFVHG 591
Cdd:cd05911 355 GYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKKELIKY-KGFQVAPAELEAVLLEHPGVADAAVIG 426
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
122-616 |
5.53e-57 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 202.06 E-value: 5.53e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 122 ISYKQVAEMAECIGSALIQKGFKPCSEqfIGIFSQNRPEWVTIEQGCFTYSMVVVPLYDTLGTDAITYIVNKAELSVIFA 201
Cdd:PRK07656 31 LTYAELNARVRRAAAALAALGIGKGDR--VAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYILARGDAKALFV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 202 dkpekAKLLLeGVENKLT---PCLKIIVIMDSYDNDLVERGQKCGVEIIGLKALEDLGRvnrtkpkPPEPEDLAIICFTS 278
Cdd:PRK07656 109 -----LGLFL-GVDYSATtrlPALEHVVICETEEDDPHTEKMKTFTDFLAAGDPAERAP-------EVDPDDVADILFTS 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 279 GTTGNPKGAMVTHQNIMNDcsgfikATESAFIAS--PEDVLISFLPLAHMF---ETVVECVMlcHGAKIgffqgDIRLLM 353
Cdd:PRK07656 176 GTTGRPKGAMLTHRQLLSN------AADWAEYLGltEGDRYLAANPFFHVFgykAGVNAPLM--RGATI-----LPLPVF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 354 DDLKVLQ------PTIFPVVPRLLNRMFDrifgqantsvkrwlldfASKRKEAELRSgivrnnslwdklifhkiqsslgg 427
Cdd:PRK07656 243 DPDEVFRlieterITVLPGPPTMYNSLLQ-----------------HPDRSAEDLSS----------------------- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 428 kVRLMITGAAPVSATVLTFLRAALGCQ-FYEGYGQTECTAGCCLSLPGD---WTAGHVGAPMPCNYIKLVDvEDMNYQAA 503
Cdd:PRK07656 283 -LRLAVTGAASMPVALLERFESELGVDiVLTGYGLSEASGVTTFNRLDDdrkTVAGTIGTAIAGVENKIVN-ELGEEVPV 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 504 KGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEA 583
Cdd:PRK07656 361 GEVGELLVRGPNVMKGYYDDPEATAAAIDADGWLHTGDLGRLDEEGYLYIVDRKKDMF-IVGGFNVYPAEVEEVLYEHPA 439
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 564389119 584 VAQVFV-------HGESLQAFliaiVVP------DVEILPSWAQKR 616
Cdd:PRK07656 440 VAEAAVigvpderLGEVGKAY----VVLkpgaelTEEELIAYCREH 481
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
122-592 |
1.59e-55 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 198.10 E-value: 1.59e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 122 ISYKQVAEMAECIGSALIQKGFKPcsEQFIGIFSQNRPEWVTIEQGCftySM---VVVPLYDTLGTDAITYIVNKAELSV 198
Cdd:PRK06187 32 TTYAELDERVNRLANALRALGVKK--GDRVAVFDWNSHEYLEAYFAV---PKigaVLHPINIRLKPEEIAYILNDAEDRV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 199 IFADkPEKAKLLlEGVENKLTPCLKIIVIMDSYDNDLVERGQkcgveiiglkALEDLgrVNRTKPKPPEPE----DLAII 274
Cdd:PRK06187 107 VLVD-SEFVPLL-AAILPQLPTVRTVIVEGDGPAAPLAPEVG----------EYEEL--LAAASDTFDFPDidenDAAAM 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 275 CFTSGTTGNPKGAMVTHQNI-MNdcsgfIKATESAFIASPEDVLISFLPLAHMFETVVECVMLCHGAKI---GFFqgDIR 350
Cdd:PRK06187 173 LYTSGTTGHPKGVVLSHRNLfLH-----SLAVCAWLKLSRDDVYLVIVPMFHVHAWGLPYLALMAGAKQvipRRF--DPE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 351 LLMDDLKVLQPTIFPVVPRLLNRMFdrifgQANTSVKRWLldfaskrkeaelrsgivrnnslwdklifhkiqSSLggkvR 430
Cdd:PRK06187 246 NLLDLIETERVTFFFAVPTIWQMLL-----KAPRAYFVDF--------------------------------SSL----R 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 431 LMITGAAPVSATVLTFLRAALGCQFYEGYGQTECT-AGCCL----SLPGDWT-AGHVGAPMPCNYIKLVDvEDMNYQAAK 504
Cdd:PRK06187 285 LVIYGGAALPPALLREFKEKFGIDLVQGYGMTETSpVVSVLppedQLPGQWTkRRSAGRPLPGVEARIVD-DDGDELPPD 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 505 GE--GEVCVKGANVFKGYLKDPARTAEALDkDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYLRSE 582
Cdd:PRK06187 364 GGevGEIIVRGPWLMQGYWNRPEATAETID-GGWLHTGDVGYIDEDGYLYITDRIKDVIISG-GENIYPRELEDALYGHP 441
|
490
....*....|
gi 564389119 583 AVAQVFVHGE 592
Cdd:PRK06187 442 AVAEVAVIGV 451
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
122-605 |
1.83e-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: 162.39 E-value: 1.83e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 122 ISYKQVAEMAECIGSALIQKGFKPCSEqfIGIFSQNRPEWVTIEQGCFTYSMVVVPLYDTLGTDAITYIVNKAELSVIFa 201
Cdd:cd17631 21 LTYAELDERVNRLAHALRALGVAKGDR--VAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAYILADSGAKVLF- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 202 dkpekaklllegvenkltpclkiivimdsydndlvergqkcgveiiglkaledlgrvnrtkpkppepEDLAIICFTSGTT 281
Cdd:cd17631 98 -------------------------------------------------------------------DDLALLMYTSGTT 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 282 GNPKGAMVTHQNIMNDCSGFIkateSAFIASPEDVLISFLPLAHMFETVVECVM-LCHGAKI----GFfqgDIRLLMDDL 356
Cdd:cd17631 111 GRPKGAMLTHRNLLWNAVNAL----AALDLGPDDVLLVVAPLFHIGGLGVFTLPtLLRGGTVvilrKF---DPETVLDLI 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 357 KVLQPTIFPVVPRLLNRMFDRifgqantsvkrwlldfaSKRKEAELrsgivrnnslwdklifhkiqSSLggkvRLMITGA 436
Cdd:cd17631 184 ERHRVTSFFLVPTMIQALLQH-----------------PRFATTDL--------------------SSL----RAVIYGG 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 437 APVSATVLTFLRAAlGCQFYEGYGQTECTAGCCLSLPGDW--TAGHVGAPMPCNYIKLVDvEDMNYQAAKGEGEVCVKGA 514
Cdd:cd17631 223 APMPERLLRALQAR-GVKFVQGYGMTETSPGVTFLSPEDHrrKLGSAGRPVFFVEVRIVD-PDGREVPPGEVGEIVVRGP 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 515 NVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYLRSEAVAQVFV----- 589
Cdd:cd17631 301 HVMAGYWNRPEATAAAF-RDGWFHTGDLGRLDEDGYLYIVDRKKDMII-SGGENVYPAEVEDVLYEHPAVAEVAVigvpd 378
|
490
....*....|....*...
gi 564389119 590 --HGESlqafLIAIVVPD 605
Cdd:cd17631 379 ekWGEA----VVAVVVPR 392
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
233-695 |
1.77e-42 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 164.51 E-value: 1.77e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 233 NDLVERGQKCGVEIIglkALEDLGRVNRT--KPKPPEPEDLAIICFTSGTTGNPKGAMVTHQNIMN------DCSGFIKA 304
Cdd:PTZ00342 269 KDLKEKAKKLGISII---LFDDMTKNKTTnyKIQNEDPDFITSIVYTSGTSGKPKGVMLSNKNLYNtvvplcKHSIFKKY 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 305 tesafiaSPEDVLiSFLPLAHMFETVVECVMLCHGAKIGFFQGDIRLLMDDLKVLQPTIFPVVPRLLNRMFDRIFGQAN- 383
Cdd:PTZ00342 346 -------NPKTHL-SYLPISHIYERVIAYLSFMLGGTINIWSKDINYFSKDIYNSKGNILAGVPKVFNRIYTNIMTEINn 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 384 -TSVKRWLLdfaskRKEAELRSGivRNNSLWDKL---IFH---KIQSSLGGKVRLMITGAAPVSATVLTFLRAALGCQFY 456
Cdd:PTZ00342 418 lPPLKRFLV-----KKILSLRKS--NNNGGFSKFlegITHissKIKDKVNPNLEVILNGGGKLSPKIAEELSVLLNVNYY 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 457 EGYGQTECTAGCCLSLPGDWTAGHVGAPM-PCNYIKLVDVEDMNYQAAKGEGEVCVKGANVFKGYLKDPARTAEALDKDG 535
Cdd:PTZ00342 491 QGYGLTETTGPIFVQHADDNNTESIGGPIsPNTKYKVRTWETYKATDTLPKGELLIKSDSIFSGYFLEKEQTKNAFTEDG 570
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 536 WLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYLRSEAVAQVFVHGESLQAFLIAIVVPDVEILPSWAQK 615
Cdd:PTZ00342 571 YFKTGDIVQINKNGSLTFLDRSKGLVKLSQGEYIETDMLNNLYSQISFINFCVVYGDDSMDGPLAIISVDKYLLFKCLKD 650
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 616 RGF---QGSFEELCRNK----DINKAILEDMVK-----LGKNAGLKPFEQVKGIAVHPELFSIDNgLLTPTLKAKRPEL- 682
Cdd:PTZ00342 651 DNMlesTGINEKNYLEKltdeTINNNIYVDYVKgkmleVYKKTNLNRYNIINDIYLTSKVWDTNN-YLTPTFKVKRFYVf 729
|
490
....*....|....*
gi 564389119 683 --RNYFRSQIDELYS 695
Cdd:PTZ00342 730 kdYAFFIDQVKKIYK 744
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
270-616 |
3.16e-41 |
|
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: 156.30 E-value: 3.16e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 270 DLAIICFTSGTTGNPKGAMVTHQNIMNDCSGFIKATEsafiASPEDVLISFLPLAHMFETVV----------ECVMLchg 339
Cdd:cd05941 90 DPALILYTSGTTGRPKGVVLTHANLAANVRALVDAWR----WTEDDVLLHVLPLHHVHGLVNallcplfagaSVEFL--- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 340 akiGFF---QGDIRLLMDDLkvlqpTIFPVVPRllnrMFDRIFGQANTSVKrwllDFASKRKEAElrsgivrnnslwdkl 416
Cdd:cd05941 163 ---PKFdpkEVAISRLMPSI-----TVFMGVPT----IYTRLLQYYEAHFT----DPQFARAAAA--------------- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 417 ifhkiqsslgGKVRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTEctAGCCLSLP--GDWTAGHVGAPMPCNYIKLVD 494
Cdd:cd05941 212 ----------ERLRLMVSGSAALPVPTLEEWEAITGHTLLERYGMTE--IGMALSNPldGERRPGTVGMPLPGVQARIVD 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 495 VEDMNYQAAKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKK-HIFKlAQGEYIAPEK 573
Cdd:cd05941 280 EETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGWFKTGDLGVVDEDGYYWILGRSSvDIIK-SGGYKVSALE 358
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 564389119 574 IENIYLRSEAVAQVFVHGESLQAF---LIAIVVP-------DVEILPSWAQKR 616
Cdd:cd05941 359 IERVLLAHPGVSECAVIGVPDPDWgerVVAVVVLragaaalSLEELKEWAKQR 411
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
206-589 |
2.17e-40 |
|
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: 155.09 E-value: 2.17e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 206 KAKLLL---EGVEnKLTPCLKIIVIMDSYDNDLvergqkcgveiiglkALEDLGRVNRTKPKPPEPE----DLAIICFTS 278
Cdd:cd05904 104 GAKLAFttaELAE-KLASLALPVVLLDSAEFDS---------------LSFSDLLFEADEAEPPVVVikqdDVAALLYSS 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 279 GTTGNPKGAMVTHQNIMNDCSGFIKATESAFiaSPEDVLISFLPLAHMFE-TVVECVMLCHGAKI----GFfqgDIRLLM 353
Cdd:cd05904 168 GTTGRSKGVMLTHRNLIAMVAQFVAGEGSNS--DSEDVFLCVLPMFHIYGlSSFALGLLRLGATVvvmpRF---DLEELL 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 354 DDLKVLQPTIFPVVPRLLNRMfdrifgqantsVKrwlldfaskrkeaelrSGIVRNNSLwdklifhkiqSSLggkvRLMI 433
Cdd:cd05904 243 AAIERYKVTHLPVVPPIVLAL-----------VK----------------SPIVDKYDL----------SSL----RQIM 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 434 TGAAPVSATVLTFLRAAL-GCQFYEGYGQTECTAG---CCLSLPGDWTAGHVGAPMPCNYIKLVDVEDMNYQAAKGEGEV 509
Cdd:cd05904 282 SGAAPLGKELIEAFRAKFpNVDLGQGYGMTESTGVvamCFAPEKDRAKYGSVGRLVPNVEAKIVDPETGESLPPNQTGEL 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 510 CVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSEAVAQVFV 589
Cdd:cd05904 362 WIRGPSIMKGYLNNPEATAATIDKEGWLHTGDLCYIDEDGYLFIVDRLKELIKY-KGFQVAPAELEALLLSHPEILDAAV 440
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
268-599 |
4.87e-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.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 144.73 E-value: 4.87e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 268 PEDLAIICFTSGTTGNPKGAMVTHQNIMNDcsGFIKATESAFiaSPEDVLISFLPLAHMFETVVEcVMLC--HGAKIGFf 345
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNIVNN--GYFIGERLGL--TEQDRLCIPVPLFHCFGSVLG-VLACltHGATMVF- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 346 qgdIRLLMDDLKVLQ-------------PTIFPvvpRLLNRMFDRIFgqantsvkrwllDFASkrkeaeLRSGIvrnnsl 412
Cdd:cd05917 75 ---PSPSFDPLAVLEaiekekctalhgvPTMFI---AELEHPDFDKF------------DLSS------LRTGI------ 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 413 wdklifhkiqsslggkvrlmiTGAAPVSATVLTFLRAALGC-QFYEGYGQTECTAGCCLSLPGDWT---AGHVGAPMPCN 488
Cdd:cd05917 125 ---------------------MAGAPCPPELMKRVIEVMNMkDVTIAYGMTETSPVSTQTRTDDSIekrVNTVGRIMPHT 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 489 YIKLVDVEDmNYQAAKGE-GEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGE 567
Cdd:cd05917 184 EAKIVDPEG-GIVPPVGVpGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLAVMDEDGYCRIVGRIKDMI-IRGGE 261
|
330 340 350
....*....|....*....|....*....|....*....
gi 564389119 568 YIAPEKIENIYLRSEAVAQVFV-------HGESLQAFLI 599
Cdd:cd05917 262 NIYPREIEEFLHTHPKVSDVQVvgvpderYGEEVCAWIR 300
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
120-599 |
1.01e-37 |
|
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: 147.07 E-value: 1.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 120 EWISYKQVAEMAECIGSALIQKGFKPCSEqfIGIFSQNRPEWV-----TIEQGCftysmVVVPLYDTLGTDAITYIVNKA 194
Cdd:cd05926 13 PALTYADLAELVDDLARQLAALGIKKGDR--VAIALPNGLEFVvaflaAARAGA-----VVAPLNPAYKKAEFEFYLADL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 195 ELSVIFADKPEkaklLLEGVENKLTPCLKII-VIMDSYDNDLVERGQKcgveiigLKALEDLGRVNRTkPKPPEPEDLAI 273
Cdd:cd05926 86 GSKLVLTPKGE----LGPASRAASKLGLAILeLALDVGVLIRAPSAES-------LSNLLADKKNAKS-EGVPLPDDLAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 274 ICFTSGTTGNPKGAMVTHQNIMNDcsgfIKATESAFIASPEDVLISFLPLAHMFETVVECV-MLCHGAKI----GFfqgD 348
Cdd:cd05926 154 ILHTSGTTGRPKGVPLTHRNLAAS----ATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLsTLAAGGSVvlppRF---S 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 349 IRLLMDDLKVLQPTIFPVVPRLLnrmfdrifgqantsvkRWLLDFASKRKEAELrsgivrnnslwdklifhkiqsslgGK 428
Cdd:cd05926 227 ASTFWPDVRDYNATWYTAVPTIH----------------QILLNRPEPNPESPP------------------------PK 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 429 VRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTE-CTAGCCLSLPGDW-TAGHVGAPMPcNYIKLVDvEDMNYQAAKGE 506
Cdd:cd05926 267 LRFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEaAHQMTSNPLPPGPrKPGSVGKPVG-VEVRILD-EDGEILPPGVV 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 507 GEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYLRSEAVAQ 586
Cdd:cd05926 345 GEICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADGYLFLTGRIKELINRG-GEKISPLEVDGVLLSHPAVLE 423
|
490 500
....*....|....*....|
gi 564389119 587 --VF-----VHGESLQAFLI 599
Cdd:cd05926 424 avAFgvpdeKYGEEVAAAVV 443
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
181-577 |
1.32e-37 |
|
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: 146.71 E-value: 1.32e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 181 TLGTDAITYIVNKAELSVIFADKP--EKAKLL-------------LEGVENKLTPCLKIIVIMDSYdndlvergqkcgve 245
Cdd:cd05909 64 TAGLRELRACIKLAGIKTVLTSKQfiEKLKLHhlfdveydarivyLEDLRAKISKADKCKAFLAGK-------------- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 246 IIGLKALEDLGRVNRtkpkppEPEDLAIICFTSGTTGNPKGAMVTHQNIMNDcsgfIKATESAFIASPEDVLISFLPLAH 325
Cdd:cd05909 130 FPPKWLLRIFGVAPV------QPDDPAVILFTSGSEGLPKGVVLSHKNLLAN----VEQITAIFDPNPEDVVFGALPFFH 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 326 MFetvvecvmlchgakiGFFQGDIRLLMDDLKVLQ---PTIFPVVPRLLNRMFDRIFGQANTsvkrwLLDFASKRKEAEL 402
Cdd:cd05909 200 SF---------------GLTGCLWLPLLSGIKVVFhpnPLDYKKIPELIYDKKATILLGTPT-----FLRGYARAAHPED 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 403 RSGIvrnnslwdklifhkiqsslggkvRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLSLPG-DWTAGHV 481
Cdd:cd05909 260 FSSL-----------------------RLVVAGAEKLKDTLRQEFQEKFGIRILEGYGTTECSPVISVNTPQsPNKEGTV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 482 GAPMPCNYIKLVDVEDMNYQAAKGEGEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIF 561
Cdd:cd05909 317 GRPLPGMEVKIVSVETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAF-GDGWYDTGDIGKIDGEGFLTITGRLSRFA 395
|
410
....*....|....*.
gi 564389119 562 KLAqGEYIAPEKIENI 577
Cdd:cd05909 396 KIA-GEMVSLEAIEDI 410
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
267-600 |
1.36e-36 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 145.20 E-value: 1.36e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 267 EPEDLAIICFTSGTTGNPKGAMVTHQNIMNDCSGfIKATESAFIASPEDVLISFLPLAHMFETVVECVMLCH-GAKigff 345
Cdd:PRK08974 204 VPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQ-AKAAYGPLLHPGKELVVTALPLYHIFALTVNCLLFIElGGQ---- 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 346 qgdirllmdDLKVLQPTIFP-VVPRLLNRMFDRIFGqANTSVKRWLldfaskrkeaelrsgivrNNSLWDKLIFhkiqSS 424
Cdd:PRK08974 279 ---------NLLITNPRDIPgFVKELKKYPFTAITG-VNTLFNALL------------------NNEEFQELDF----SS 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 425 LggkvRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECT---AGCCLSLPGdwTAGHVGAPMPCNYIKLVDvEDMNyQ 501
Cdd:PRK08974 327 L----KLSVGGGMAVQQAVAERWVKLTGQYLLEGYGLTECSplvSVNPYDLDY--YSGSIGLPVPSTEIKLVD-DDGN-E 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 502 AAKGE-GEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLR 580
Cdd:PRK08974 399 VPPGEpGELWVKGPQVMLGYWQRPEATDEVI-KDGWLATGDIAVMDEEGFLRIVDRKKDMI-LVSGFNVYPNEIEDVVML 476
|
330 340
....*....|....*....|....*..
gi 564389119 581 SEAVAQVF-------VHGESLQAFLIA 600
Cdd:PRK08974 477 HPKVLEVAavgvpseVSGEAVKIFVVK 503
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
122-591 |
1.37e-36 |
|
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: 144.59 E-value: 1.37e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 122 ISYKQVAEMAECIGSALIQKGFKpcSEQFIGIFSQNRPEWVTIEQGCFTYSMVVVPLYDTLGTDAITYIVNKAELSVIFA 201
Cdd:cd17642 45 YSYAEYLEMSVRLAEALKKYGLK--QNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFC 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 202 DKPEKAKLLleGVENKLtPCLKIIVIMDSyDNDLveRGQKCgveIIGLKALEDLGRVNRTKPKPPE---PEDLAIICFTS 278
Cdd:cd17642 123 SKKGLQKVL--NVQKKL-KIIKTIIILDS-KEDY--KGYQC---LYTFITQNLPPGFNEYDFKPPSfdrDEQVALIMNSS 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 279 GTTGNPKGAMVTHQNImndCSGFIKATESAFIA--SPEDVLISFLPLAHMFETVVECVMLCHGAKIGF---FQGDIRL-L 352
Cdd:cd17642 194 GSTGLPKGVQLTHKNI---VARFSHARDPIFGNqiIPDTAILTVIPFHHGFGMFTTLGYLICGFRVVLmykFEEELFLrS 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 353 MDDLKV----LQPTIFPVVPrllnrmfdrifgqantsvKRWLLDfaskrkeaelrsgivrnnsLWDKLIFHKIQSslggk 428
Cdd:cd17642 271 LQDYKVqsalLVPTLFAFFA------------------KSTLVD-------------------KYDLSNLHEIAS----- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 429 vrlmitGAAPVSATVLTFLRAALGCQFY-EGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYIKLVDVEDMNYQAAKGEG 507
Cdd:cd17642 309 ------GGAPLSKEVGEAVAKRFKLPGIrQGYGLTETTSAILITPEGDDKPGAVGKVVPFFYAKVVDLDTGKTLGPNERG 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 508 EVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSEAVAQV 587
Cdd:cd17642 383 ELCVKGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKY-KGYQVPPAELESILLQHPKIFDA 461
|
....
gi 564389119 588 FVHG 591
Cdd:cd17642 462 GVAG 465
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
270-591 |
1.20e-34 |
|
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: 136.65 E-value: 1.20e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 270 DLAIICFTSGTTGNPKGAMVTHQNIMNDCSGFIKAtesaFIASPEDVLISFLPLAHMFETVVEC-VMLCHGAKIgffqgd 348
Cdd:cd05934 82 DPASILYTSGTTGPPKGVVITHANLTFAGYYSARR----FGLGEDDVYLTVLPLFHINAQAVSVlAALSVGATL------ 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 349 irllmddlkVLQPTIfpvvprllnrmfdrifgqantSVKRWLLDFAskrkeaelRSGIVRNNSLWDKLIFHKIQ----SS 424
Cdd:cd05934 152 ---------VLLPRF---------------------SASRFWSDVR--------RYGATVTNYLGAMLSYLLAQppspDD 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 425 LGGKVRLmITGAAPVSATVLTFLRAaLGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYIKLVDveDMNYQAAK 504
Cdd:cd05934 194 RAHRLRA-AYGAPNPPELHEEFEER-FGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIVD--DDGQELPA 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 505 GE-GEVCVKGAN---VFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYLR 580
Cdd:cd05934 270 GEpGELVIRGLRgwgFFKGYYNMPEATAEAM-RNGWFHTGDLGYRDADGFFYFVDRKKDMIR-RRGENISSAEVERAILR 347
|
330
....*....|.
gi 564389119 581 SEAVAQVFVHG 591
Cdd:cd05934 348 HPAVREAAVVA 358
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
267-607 |
1.26e-34 |
|
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: 137.27 E-value: 1.26e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 267 EPEDLAIICFTSGTTGNPKGAMVTHQNIMNdcsgFIKATESAFIASPEDVLISFLPLA---HMFETvveCVMLCHGAKI- 342
Cdd:cd05930 91 DPDDLAYVIYTSGSTGKPKGVMVEHRGLVN----LLLWMQEAYPLTPGDRVLQFTSFSfdvSVWEI---FGALLAGATLv 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 343 ---GFFQGDIRLLMDDLKVLQPTIFPVVPRLLNRMFDRIFGQANTSVkrwlldfaskrkeaelrsgivrnnslwdklifh 419
Cdd:cd05930 164 vlpEEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQELELAALPSL--------------------------------- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 420 kiqsslggkvRLMITGAAPVSATVLT-FLRAALGCQFYEGYGQTECTAGCCL--SLPGDWTAGHV--GAPMPCNYIKLVD 494
Cdd:cd05930 211 ----------RLVLVGGEALPPDLVRrWRELLPGARLVNLYGPTEATVDATYyrVPPDDEEDGRVpiGRPIPNTRVYVLD 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 495 vEDMNYQAAKGEGEVCVKGANVFKGYLKDPARTAEA-----LDKDGWLH-TGDIGKWLPNGTLKIIDRKKHIFKLAqGEY 568
Cdd:cd05930 281 -ENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERfvpnpFGPGERMYrTGDLVRWLPDGNLEFLGRIDDQVKIR-GYR 358
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 564389119 569 IAPEKIENIYLRSEAVAQVFV---HGESLQAFLIAIVVPDVE 607
Cdd:cd05930 359 IELGEIEAALLAHPGVREAAVvarEDGDGEKRLVAYVVPDEG 400
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
255-605 |
1.61e-34 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 138.74 E-value: 1.61e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 255 LGRVNRTKPKPPEPEDLAIICFTSGTTGNPKGAMVTHQNI---MNDCsgfiKATESAFIASPEDVLISFLPLAHMFETVV 331
Cdd:PRK05677 193 KGAGQPVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLvanMLQC----RALMGSNLNEGCEILIAPLPLYHIYAFTF 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 332 ECVMLchgakigffqgdirLLMDDLKVLQPTifpvvPRLLNRMfdrifgqantsVKrwlldfaskrkeaELR----SGIV 407
Cdd:PRK05677 269 HCMAM--------------MLIGNHNILISN-----PRDLPAM-----------VK-------------ELGkwkfSGFV 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 408 RNNSLWDKLI----FHKIQSSlggKVRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGA 483
Cdd:PRK05677 306 GLNTLFVALCnneaFRKLDFS---ALKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETSPVVSVNPSQAIQVGTIGI 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 484 PMPCNYIKLVDveDMNYQAAKGE-GEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFk 562
Cdd:PRK05677 383 PVPSTLCKVID--DDGNELPLGEvGELCVKGPQVMKGYWQRPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMI- 459
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 564389119 563 LAQGEYIAPEKIENIYLRSEAVAQVfvhgeslqaflIAIVVPD 605
Cdd:PRK05677 460 LVSGFNVYPNELEDVLAALPGVLQC-----------AAIGVPD 491
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
255-591 |
3.12e-34 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 138.21 E-value: 3.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 255 LGRVNRTKPKPPEPEDLAIICFTSGTTGNPKGAMVTHQNIM-NDCSGfiKATESAFIASPEDVLiSFLPLAHMFE-TVVE 332
Cdd:PRK05605 205 GGDGSDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFaNAAQG--KAWVPGLGDGPERVL-AALPMFHAYGlTLCL 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 333 CVMLCHGAKIGFFQG-DIRLLMDDLKVLQPTIFPVVPRLlnrmFDRIfgqantsvkrwlldfaskRKEAELRsGIvrnns 411
Cdd:PRK05605 282 TLAVSIGGELVLLPApDIDLILDAMKKHPPTWLPGVPPL----YEKI------------------AEAAEER-GV----- 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 412 lwdklifhkiqsSLGGkVRLMITGAA--PVSaTVLTFlRAALGCQFYEGYGQTECTA-GCCLSLPGDWTAGHVGAPMPCN 488
Cdd:PRK05605 334 ------------DLSG-VRNAFSGAMalPVS-TVELW-EKLTGGLLVEGYGLTETSPiIVGNPMSDDRRPGYVGVPFPDT 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 489 YIKLVDVEDMNYQAAKGE-GEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGE 567
Cdd:PRK05605 399 EVRIVDPEDPDETMPDGEeGELLVRGPQVFKGYWNRPEETAKSF-LDGWFRTGDVVVMEEDGFIRIVDRIKELI-ITGGF 476
|
330 340
....*....|....*....|....
gi 564389119 568 YIAPEKIENIYLRSEAVAQVFVHG 591
Cdd:PRK05605 477 NVYPAEVEEVLREHPGVEDAAVVG 500
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
124-616 |
5.15e-34 |
|
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 162605 [Multi-domain] Cd Length: 436 Bit Score: 135.27 E-value: 5.15e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 124 YKQVAEMAECIGSALIQKGfkpcseQFIGIFSQNRPEWVTIEQGCFTYSMVVVPLYDTLGTDAITYIVNKAELSVIFADk 203
Cdd:TIGR01923 6 DCEAAHLAKALKAQGIRSG------SRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTD- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 204 pekAKLLLEGVEnkltpclkiIVIMDSydndlvergqkcgveiIGLKALEDLgRVNRTKPKppepEDLAIICFTSGTTGN 283
Cdd:TIGR01923 79 ---SLLEEKDFQ---------ADSLDR----------------IEAAGRYET-SLSASFNM----DQIATLMFTSGTTGK 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 284 PKGAMVTHQNIMNDcsgfIKATESAFIASPEDVLISFLPLAH------MFETVVEcvmlchGAKIGFFQGDIRLLmDDLK 357
Cdd:TIGR01923 126 PKAVPHTFRNHYAS----AVGSKENLGFTEDDNWLLSLPLYHisglsiLFRWLIE------GATLRIVDKFNQLL-EMIA 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 358 VLQPTIFPVVPRLLNRMFDRifGQANTSVKRWLLdfaskrkeaelrsgivrnnslwdklifhkiqsslggkvrlmitGAA 437
Cdd:TIGR01923 195 NERVTHISLVPTQLNRLLDE--GGHNENLRKILL-------------------------------------------GGS 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 438 PVSATVLTFLRAaLGCQFYEGYGQTE-CTAGCCLSLPGDWTAGHVGAPMPCNYIKLvDVEDMnyqaaKGEGEVCVKGANV 516
Cdd:TIGR01923 230 AIPAPLIEEAQQ-YGLPIYLSYGMTEtCSQVTTATPEMLHARPDVGRPLAGREIKI-KVDNK-----EGHGEIMVKGANL 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 517 FKGYLkDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAVAQVFV------- 589
Cdd:TIGR01923 303 MKGYL-YQGELTPAFEQQGWFNTGDIGELDGEGFLYVLGRRDDLI-ISGGENIYPEEIETVLYQHPGIQEAVVvpkpdae 380
|
490 500
....*....|....*....|....*..
gi 564389119 590 HGESLQAFLIAIVVPDVEILPSWAQKR 616
Cdd:TIGR01923 381 WGQVPVAYIVSESDISQAKLIAYLTEK 407
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
223-589 |
7.86e-34 |
|
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: 134.32 E-value: 7.86e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 223 KIIVIMDSYDNDLVERGQKCGVEIIGLKALEDLGRVNRTKPKPPEPEDLAIICFTSGTTGNPKGAMVTHQNIMNdcsgFI 302
Cdd:TIGR01733 74 RLLLTDSALASRLAGLVLPVILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVN----LL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 303 KATESAFIASPEDVLISFLPLAH------MFETvvecvmLCHGAK--------IGFFQGDIRLLMDDLKVlqpTIFPVVP 368
Cdd:TIGR01733 150 AWLARRYGLDPDDRVLQFASLSFdasveeIFGA------LLAGATlvvppedeERDDAALLAALIAEHPV---TVLNLTP 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 369 RLLNRMFDRIFGQANTsvkrwlldfaskrkeaelrsgivrnnslwdklifhkiqsslggkVRLMITGA-APVSATVLTFL 447
Cdd:TIGR01733 221 SLLALLAAALPPALAS--------------------------------------------LRLVILGGeALTPALVDRWR 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 448 RAALGCQFYEGYGQTECTAGC-CLSLPGDWTAGHV----GAPMPCNYIKLVDvEDMNYQAAKGEGEVCVKGANVFKGYLK 522
Cdd:TIGR01733 257 ARGPGARLINLYGPTETTVWStATLVDPDDAPRESpvpiGRPLANTRLYVLD-DDLRPVPVGVVGELYIGGPGVARGYLN 335
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564389119 523 DPARTAE--------ALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSEAVAQVFV 589
Cdd:TIGR01733 336 RPELTAErfvpdpfaGGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKI-RGYRIELGEIEAALLRHPGVREAVV 409
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
123-629 |
8.99e-34 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 136.44 E-value: 8.99e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 123 SYKQVAEMAECIGSALIQKGFKPCSEqfIGIFSQNRPEWVTIEQGCFTYSMVVVPLYDTLGTDAITYIVNKAELS-VIFA 201
Cdd:PRK12583 47 TWRQLADAVDRLARGLLALGVQPGDR--VGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRwVICA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 202 DK--------------PEKAKLLLEGVENKLTPCLKIIVIMDSYD-------NDLVERGqkcgvEIIGLKALEdlgrvnr 260
Cdd:PRK12583 125 DAfktsdyhamlqellPGLAEGQPGALACERLPELRGVVSLAPAPppgflawHELQARG-----ETVSREALA------- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 261 TKPKPPEPEDLAIICFTSGTTGNPKGAMVTHQNIMNDcsGFIKATESAFiaSPEDVLISFLPLAHMFETVVeCVMLC--H 338
Cdd:PRK12583 193 ERQASLDRDDPINIQYTSGTTGFPKGATLSHHNILNN--GYFVAESLGL--TEHDRLCVPVPLYHCFGMVL-ANLGCmtV 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 339 GAKIgFFQGDirlLMDDLKVLQ-------------PTIFpvVPRLLNRMFDRifgqantsvkrwlLDFASkrkeaeLRSG 405
Cdd:PRK12583 268 GACL-VYPNE---AFDPLATLQaveeerctalygvPTMF--IAELDHPQRGN-------------FDLSS------LRTG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 406 IVrnnslwdklifhkiqsslggkvrlmitGAAPVSATVLTFLRAALGC-QFYEGYGQTECTAGCCLSLPGD---WTAGHV 481
Cdd:PRK12583 323 IM---------------------------AGAPCPIEVMRRVMDEMHMaEVQIAYGMTETSPVSLQTTAADdleRRVETV 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 482 GAPMPCNYIKLVDVEDMNyqAAKGE-GEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHI 560
Cdd:PRK12583 376 GRTQPHLEVKVVDPDGAT--VPRGEiGELCTRGYSVMKGYWNNPEATAESIDEDGWMHTGDLATMDEQGYVRIVGRSKDM 453
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564389119 561 FkLAQGEYIAPEKIENIYLRSEAVAQVFVHGeslqafliaivVPDV---EILPSWAQKR-GFQGSFEEL---CRNK 629
Cdd:PRK12583 454 I-IRGGENIYPREIEEFLFTHPAVADVQVFG-----------VPDEkygEEIVAWVRLHpGHAASEEELrefCKAR 517
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
255-684 |
1.23e-33 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 136.16 E-value: 1.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 255 LGRVNRTKPKPPEPEDLAIICFTSGTTGNPKGAMVTHQNI---MNDCSGFIKATESafIASPEDVLISFLPLAHMFETVV 331
Cdd:PRK08751 194 LGRKHSMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLvanMQQAHQWLAGTGK--LEEGCEVVITALPLYHIFALTA 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 332 ECVMLchgAKIGFFQG------DIRLLMDDLKVLQPTIFPVVPRLLNRMFdrifgqantsvkrwlldfaskrkeaelrsg 405
Cdd:PRK08751 272 NGLVF---MKIGGCNHlisnprDMPGFVKELKKTRFTAFTGVNTLFNGLL------------------------------ 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 406 ivrNNSLWDKLIFHKIQSSLGGkvrlmitGAApVSATVLTFLRAALGCQFYEGYGQTECTAGCCLS-LPGDWTAGHVGAP 484
Cdd:PRK08751 319 ---NTPGFDQIDFSSLKMTLGG-------GMA-VQRSVAERWKQVTGLTLVEAYGLTETSPAACINpLTLKEYNGSIGLP 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 485 MPCNYIKLVDveDMNYQAAKGE-GEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkL 563
Cdd:PRK08751 388 IPSTDACIKD--DAGTVLAIGEiGELCIKGPQVMKGYWKRPEETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMI-L 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 564 AQGEYIAPEKIENIYLRSEAVAQVfvhgeslqaflIAIVVPDveilpswaQKRGfqgsfeELCRNKDINK--AILEDMVK 641
Cdd:PRK08751 465 VSGFNVYPNEIEDVIAMMPGVLEV-----------AAVGVPD--------EKSG------EIVKVVIVKKdpALTAEDVK 519
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 564389119 642 LGKNAGLKPFEQVKGIAVHPELFSIDNGlltptlKAKRPELRN 684
Cdd:PRK08751 520 AHARANLTGYKQPRIIEFRKELPKTNVG------KILRRELRD 556
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
247-600 |
1.76e-33 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 135.72 E-value: 1.76e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 247 IGLKALEDLGRVNRTKPKPPEPEDLAIICFTSGTTGNPKGAMVTHQNIMND------CSGFIKATESAFIASPEDVLISF 320
Cdd:PRK12492 185 VPFKQALRQGRGLSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANmlqvraCLSQLGPDGQPLMKEGQEVMIAP 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 321 LPLAHMFETVVECVMLchgakigFFQGDIRLLMDDlkvlqptifpvvPRLLNRMFDRIfgqantsvKRWLLdfaskrkea 400
Cdd:PRK12492 265 LPLYHIYAFTANCMCM-------MVSGNHNVLITN------------PRDIPGFIKEL--------GKWRF--------- 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 401 elrSGIVRNNSLWDKLIFHKIQSSLGGKvRLMIT---GAAPVSATVLTFlRAALGCQFYEGYGQTECTAGCCLSLPGDWT 477
Cdd:PRK12492 309 ---SALLGLNTLFVALMDHPGFKDLDFS-ALKLTnsgGTALVKATAERW-EQLTGCTIVEGYGLTETSPVASTNPYGELA 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 478 A-GHVGAPMPCNYIKLVDvEDMNYQAAKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDR 556
Cdd:PRK12492 384 RlGTVGIPVPGTALKVID-DDGNELPLGERGELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDR 462
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 564389119 557 KKHIFkLAQGEYIAPEKIENIYLRSEAVAQVFV-------HGESLQAFLIA 600
Cdd:PRK12492 463 KKDLI-IVSGFNVYPNEIEDVVMAHPKVANCAAigvpderSGEAVKLFVVA 512
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
123-599 |
4.49e-33 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 134.55 E-value: 4.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 123 SYKQVAEMAECIGSALIQKGFKPCSEqfIGIFSQNRPEWVTIEQGCFTYSMVVV---PLYDTlgtDAITYIVNKAELSVI 199
Cdd:PRK08315 45 TYREFNEEVDALAKGLLALGIEKGDR--VGIWAPNVPEWVLTQFATAKIGAILVtinPAYRL---SELEYALNQSGCKAL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 200 F-ADK--------------PEKAKLLLEGVENKLTPCLKIIVIMDSYD-------NDLVERGQkcGVEIIGLKALED-Lg 256
Cdd:PRK08315 120 IaADGfkdsdyvamlyelaPELATCEPGQLQSARLPELRRVIFLGDEKhpgmlnfDELLALGR--AVDDAELAARQAtL- 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 257 rvnrtkpkppEPEDLAIICFTSGTTGNPKGAMVTHQNIMNDcsGFikatesaFIA-----SPEDVLISFLPLAHMFEtvv 331
Cdd:PRK08315 197 ----------DPDDPINIQYTSGTTGFPKGATLTHRNILNN--GY-------FIGeamklTEEDRLCIPVPLYHCFG--- 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 332 eCVM-----LCHGAKI-----GFfqgdirllmDDLKVLQ-------------PTIFpvVPRLLNRMFDRifgqantsvkr 388
Cdd:PRK08315 255 -MVLgnlacVTHGATMvypgeGF---------DPLATLAaveeerctalygvPTMF--IAELDHPDFAR----------- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 389 wlLDFASkrkeaeLRSGIvrnnslwdklifhkiqssLGGK---VRLM-----------ITGAapvsatvltflraalgcq 454
Cdd:PRK08315 312 --FDLSS------LRTGI------------------MAGSpcpIEVMkrvidkmhmseVTIA------------------ 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 455 fyegYGQTECTAGCCLSLPGD------WTaghVGAPMPCNYIKLVDvEDMNYQAAKGE-GEVCVKGANVFKGYLKDPART 527
Cdd:PRK08315 348 ----YGMTETSPVSTQTRTDDplekrvTT---VGRALPHLEVKIVD-PETGETVPRGEqGELCTRGYSVMKGYWNDPEKT 419
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564389119 528 AEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAV--AQVF-V----HGESLQAFLI 599
Cdd:PRK08315 420 AEAIDADGWMHTGDLAVMDEEGYVNIVGRIKDMI-IRGGENIYPREIEEFLYTHPKIqdVQVVgVpdekYGEEVCAWII 497
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
185-591 |
9.99e-33 |
|
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: 132.75 E-value: 9.99e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 185 DAITYIVNKAELSVIFADkPEKAKLLlEGVENKLtPCLKIIVIMDSYDNDLVERGqkcgveiIGLKALEDLgrVNRTKPK 264
Cdd:cd12119 87 EQIAYIINHAEDRVVFVD-RDFLPLL-EAIAPRL-PTVEHVVVMTDDAAMPEPAG-------VGVLAYEEL--LAAESPE 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 265 PPEPE----DLAIICFTSGTTGNPKGAMVTHQNI--------MNDCSGFikatesafiaSPEDVlisFLPLAHMFE---- 328
Cdd:cd12119 155 YDWPDfdenTAAAICYTSGTTGNPKGVVYSHRSLvlhamaalLTDGLGL----------SESDV---VLPVVPMFHvnaw 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 329 -TVVECVMLchGAKI----GFFQGDIRL-LMDDLKVlqpTIFPVVPRLLNRMFDrifgqantSVKRWLLDFASKRkeael 402
Cdd:cd12119 222 gLPYAAAMV--GAKLvlpgPYLDPASLAeLIEREGV---TFAAGVPTVWQGLLD--------HLEANGRDLSSLR----- 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 403 rsgivrnnslwdklifhkiqsslggkvRLMITGAAPVSATVLTFlrAALGCQFYEGYGQTE-CTAGCCLSLPGDWTAGHV 481
Cdd:cd12119 284 ---------------------------RVVIGGSAVPRSLIEAF--EERGVRVIHAWGMTEtSPLGTVARPPSEHSNLSE 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 482 ----------GAPMPCNYIKLVDvEDMNYQAAKGE--GEVCVKGANVFKGYLKDPaRTAEALDKDGWLHTGDIGKWLPNG 549
Cdd:cd12119 335 deqlalrakqGRPVPGVELRIVD-DDGRELPWDGKavGELQVRGPWVTKSYYKND-EESEALTEDGWLRTGDVATIDEDG 412
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 564389119 550 TLKIIDRKKHIFKLAqGEYIAPEKIENIYLRSEAVAQVFVHG 591
Cdd:cd12119 413 YLTITDRSKDVIKSG-GEWISSVELENAIMAHPAVAEAAVIG 453
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
270-591 |
2.98e-31 |
|
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: 124.92 E-value: 2.98e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 270 DLAIICFTSGTTGNPKGAMVTHQNIMndcSGFIKATESAFIASPEDVLIsFLPLAHMFETVVECVM-LCHGAKI---GFF 345
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTL---RAAAAWADCADLTEDDRYLI-INPFFHTFGYKAGIVAcLLTGATVvpvAVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 346 qgDIRLLMDDLKVLQPTIFPVVPRLLNRMFDRifgqantsvkrwlldfaSKRKEAELrsgivrnnslwdklifhkiqSSL 425
Cdd:cd17638 77 --DVDAILEAIERERITVLPGPPTLFQSLLDH-----------------PGRKKFDL--------------------SSL 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 426 ggkvRLMITGAAPVSATVLTFLRAALGCQ-FYEGYGQTECTAGCcLSLPGD---WTAGHVGAPMPCNYIKLVDvedmnyq 501
Cdd:cd17638 118 ----RAAVTGAATVPVELVRRMRSELGFEtVLTAYGLTEAGVAT-MCRPGDdaeTVATTCGRACPGFEVRIAD------- 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 502 aakgEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRS 581
Cdd:cd17638 186 ----DGEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGELDERGYLRITDRLKDMY-IVGGFNVYPAEVEGALAEH 260
|
330
....*....|
gi 564389119 582 EAVAQVFVHG 591
Cdd:cd17638 261 PGVAQVAVIG 270
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
268-575 |
7.03e-31 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 127.79 E-value: 7.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 268 PEDLAIICFTSGTTGNPKGAMVTHQNIMNDCSGFIKATESAFIASPEDVLISFLPLAHMFEtvVECVMLCH---GAKIGF 344
Cdd:PLN02246 178 PDDVVALPYSSGTTGLPKGVMLTHKGLVTSVAQQVDGENPNLYFHSDDVILCVLPMFHIYS--LNSVLLCGlrvGAAILI 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 345 FQG-DIRLLMDDLKVLQPTIFPVVPRLLnrmfdrifgqantsvkrwlLDFAskrkeaelRSGIVRNNSLwdklifhkiqS 423
Cdd:PLN02246 256 MPKfEIGALLELIQRHKVTIAPFVPPIV-------------------LAIA--------KSPVVEKYDL----------S 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 424 SlggkVRLMITGAAPVSATVLTFLRAAL-GCQFYEGYGQTEctAGCCLSL-------PGDWTAGHVGAPMPCNYIKLVDV 495
Cdd:PLN02246 299 S----IRMVLSGAAPLGKELEDAFRAKLpNAVLGQGYGMTE--AGPVLAMclafakePFPVKSGSCGTVVRNAELKIVDP 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 496 EDMNYQAAKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIE 575
Cdd:PLN02246 373 ETGASLPRNQPGEICIRGPQIMKGYLNDPEATANTIDKDGWLHTGDIGYIDDDDELFIVDRLKELIKY-KGFQVAPAELE 451
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
265-616 |
1.06e-29 |
|
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: 122.42 E-value: 1.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 265 PPEPEDLAIICFTSGTTGNPKGAMVTHQNIMNdcsgFIKATESAFIASPEDVLISFLPLA------HMFETvvecvmLCH 338
Cdd:cd17653 101 TDSPDDLAYIIFTSGSTGIPKGVMVPHRGVLN----YVSQPPARLDVGPGSRVAQVLSIAfdacigEIFST------LCN 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 339 GAKIgFFQGDIRLLMDDLKVLqpTIFPVVPRLLnrmfdrifgqantsvkrwlldfaSKRKEAELRSgivrnnslwdklif 418
Cdd:cd17653 171 GGTL-VLADPSDPFAHVARTV--DALMSTPSIL-----------------------STLSPQDFPN-------------- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 419 hkiqsslggkVRLMITGAAPVSATVLTflRAALGCQFYEGYGQTECTAGCCLS--LPGDWTagHVGAPMPCNYIKLVDvE 496
Cdd:cd17653 211 ----------LKTIFLGGEAVPPSLLD--RWSPGRRLYNAYGPTECTISSTMTelLPGQPV--TIGKPIPNSTCYILD-A 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 497 DMNYQAAKGEGEVCVKGANVFKGYLKDPARTAEAL----DKDGWLH--TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIA 570
Cdd:cd17653 276 DLQPVPEGVVGEICISGVQVARGYLGNPALTASKFvpdpFWPGSRMyrTGDYGRWTEDGGLEFLGREDNQVKV-RGFRIN 354
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 564389119 571 PEKIENIYLRSEAVAQ---VFVHGEslqaFLIAIVVP---DVEILPSWAQKR 616
Cdd:cd17653 355 LEEIEEVVLQSQPEVTqaaAIVVNG----RLVAFVTPetvDVDGLRSELAKH 402
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
114-579 |
1.71e-29 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 123.70 E-value: 1.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 114 KPNQPYEWiSYKQVAEMAECIGSALIQKGFKPCSeqfigIFSQNRPEW---VTIEQGCFTYSMVVVPLYDTLGTDAITYI 190
Cdd:PRK06087 43 VDNHGASY-TYSALDHAASRLANWLLAKGIEPGD-----RVAFQLPGWcefTIIYLACLKVGAVSVPLLPSWREAELVWV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 191 VNKAELSVIFADKPEKA----KLLLEgVENKLtPCLKIIVimdsydndLVERGQKCGVEIIGLKALEDLGRVNrtKPKPP 266
Cdd:PRK06087 117 LNKCQAKMFFAPTLFKQtrpvDLILP-LQNQL-PQLQQIV--------GVDKLAPATSSLSLSQIIADYEPLT--TAITT 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 267 EPEDLAIICFTSGTTGNPKGAMVTHQNIMndcsgfikATESAFIA----SPEDVLISFLPLAHmfetvvecvmlchgaKI 342
Cdd:PRK06087 185 HGDELAAVLFTSGTEGLPKGVMLTHNNIL--------ASERAYCArlnlTWQDVFMMPAPLGH---------------AT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 343 GFFQGDIR-LLMDDLKVLQPTIFPVVP-RLLNRmfdrifgQANTsvkrWLL-------DFASKRKEAELRSgivrnnslw 413
Cdd:PRK06087 242 GFLHGVTApFLIGARSVLLDIFTPDAClALLEQ-------QRCT----CMLgatpfiyDLLNLLEKQPADL--------- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 414 dklifhkiqSSLggkvRLMITGAAPVSATVLtflRAAL--GCQFYEGYGQTECTAGCCLSL--PGDWTAGHVGAPMPCNY 489
Cdd:PRK06087 302 ---------SAL----RFFLCGGTTIPKKVA---RECQqrGIKLLSVYGSTESSPHAVVNLddPLSRFMHTDGYAAAGVE 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 490 IKLVDvEDMNYQAAKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYI 569
Cdd:PRK06087 366 IKVVD-EARKTLPPGCEGEEASRGPNVFMGYLDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDII-VRGGENI 443
|
490
....*....|
gi 564389119 570 APEKIENIYL 579
Cdd:PRK06087 444 SSREVEDILL 453
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
256-577 |
2.09e-29 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 123.21 E-value: 2.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 256 GRVNRTKPKPPEPEDLAIICFTSGTTGNPKGAMVTHQNIMNDCSGFIKATESAFIASPED---VLISFLPLAHMFETVVE 332
Cdd:PRK07059 191 GARQTFKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQMEAWLQPAFEKKPRPdqlNFVCALPLYHIFALTVC 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 333 CVMlchGAKIGffqG---------DIRLLMDDLKVLQPTIFPVVPRLLNRMFdrifgqantsvkrwlldfaskrkeaelr 403
Cdd:PRK07059 271 GLL---GMRTG---GrnilipnprDIPGFIKELKKYQVHIFPAVNTLYNALL---------------------------- 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 404 sgivrNNSLWDKLIFHKIQSSLGGkvrlmitGAApVSATVLTFLRAALGCQFYEGYGQTEcTAGCCLSLPGDWTA--GHV 481
Cdd:PRK07059 317 -----NNPDFDKLDFSKLIVANGG-------GMA-VQRPVAERWLEMTGCPITEGYGLSE-TSPVATCNPVDATEfsGTI 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 482 GAPMPCNYIKLVDvEDMNYQAAKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIF 561
Cdd:PRK07059 383 GLPLPSTEVSIRD-DDGNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKDMI 461
|
330
....*....|....*.
gi 564389119 562 kLAQGEYIAPEKIENI 577
Cdd:PRK07059 462 -LVSGFNVYPNEIEEV 476
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
266-627 |
2.70e-29 |
|
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: 121.33 E-value: 2.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 266 PEPEDLAIICFTSGTTGNPKGAMVTHQNIMndcsgfikATESAFIA----SPEDVLISFLPLAHMFETVvecvmlcHGAK 341
Cdd:cd05903 90 AMPDAVALLLFTSGTTGEPKGVMHSHNTLS--------ASIRQYAErlglGPGDVFLVASPMAHQTGFV-------YGFT 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 342 IGFFQGDIRLLMDdlkVLQPTifpVVPRLLNRmfDRI-FGQANTSVKRWLLDfASKRKEAELRSgivrnnslwdklifhk 420
Cdd:cd05903 155 LPLLLGAPVVLQD---IWDPD---KALALMRE--HGVtFMMGATPFLTDLLN-AVEEAGEPLSR---------------- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 421 iqsslggkVRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTEC--TAGCCLSLPGDWTAGHVGAPMPCNYIKLVDvEDM 498
Cdd:cd05903 210 --------LRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECpgAVTSITPAPEDRRLYTDGRPLPGVEIKVVD-DTG 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 499 NYQAAKGEGEVCVKGANVFKGYLKDPARTAEALDkDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIY 578
Cdd:cd05903 281 ATLAPGVEGELLSRGPSVFLGYLDRPDLTADAAP-EGWFRTGDLARLDEDGYLRITGRSKDII-IRGGENIPVLEVEDLL 358
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 564389119 579 LRSEAVAQVFVHG---ESLQAFLIAIVVPdveilpswaqKRGFQGSFEELCR 627
Cdd:cd05903 359 LGHPGVIEAAVVAlpdERLGERACAVVVT----------KSGALLTFDELVA 400
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
122-604 |
3.45e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 122.40 E-value: 3.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 122 ISYKQVAEMAECIGSALIQKGFKPCSEqfIGIFSQNRPE-WVTIEQGCfTYSMVVVPLYDTLGTDAITYIVNKAELSVIF 200
Cdd:PRK06188 38 LTYGQLADRISRYIQAFEALGLGTGDA--VALLSLNRPEvLMAIGAAQ-LAGLRRTALHPLGSLDDHAYVLEDAGISTLI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 201 ADkpekaklllegvenkltpclkiivimdsyDNDLVERGQKCGVEIIGLKALEDLGRVN----------RTKPKPPEPE- 269
Cdd:PRK06188 115 VD-----------------------------PAPFVERALALLARVPSLKHVLTLGPVPdgvdllaaaaKFGPAPLVAAa 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 270 ---DLAIICFTSGTTGNPKGAMVTHQNImndcsgfikATESAFIAS----PEDvlISFL---PLAHMFETVVECVMLCHG 339
Cdd:PRK06188 166 lppDIAGLAYTGGTTGKPKGVMGTHRSI---------ATMAQIQLAewewPAD--PRFLmctPLSHAGGAFFLPTLLRGG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 340 AKI---GFfqgDIRLLMDDLKVLQPTIFPVVPRLLNRmfdrifgqantsvkrwLLDFASKRKeAELrsgivrnnslwdkl 416
Cdd:PRK06188 235 TVIvlaKF---DPAEVLRAIEEQRITATFLVPTMIYA----------------LLDHPDLRT-RDL-------------- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 417 ifhkiqSSLggkvRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLSLPGDWTAGHV------GAPMPCNYI 490
Cdd:PRK06188 281 ------SSL----ETVYYGASPMSPVRLAEAIERFGPIFAQYYGQTEAPMVITYLRKRDHDPDDPkrltscGRPTPGLRV 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 491 KLVDvEDMNyQAAKGE-GEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYI 569
Cdd:PRK06188 351 ALLD-EDGR-EVAQGEvGEICVRGPLVMDGYWNRPEETAEAF-RDGWLHTGDVAREDEDGFYYIVDRKKDMI-VTGGFNV 426
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 564389119 570 APEKIENIYLRSEAVAQVFV-------HGESLQafliAIVVP 604
Cdd:PRK06188 427 FPREVEDVLAEHPAVAQVAVigvpdekWGEAVT----AVVVL 464
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
266-611 |
3.85e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 121.64 E-value: 3.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 266 PEPEDLAIICFTSGTTGNPKGAMVTHQNIMNDcsgfIKATESAFIASPEDVLISFLPLAHMfetvvecvmlcHGAKIGff 345
Cdd:PRK07787 125 PDPDAPALIVYTSGTTGPPKGVVLSRRAIAAD----LDALAEAWQWTADDVLVHGLPLFHV-----------HGLVLG-- 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 346 qgdirllmddlkVLQPTifpvvpRLLNRMfdrifgqantsvkRWLLDFASKRKEAELRSG-------------IVRNNSL 412
Cdd:PRK07787 188 ------------VLGPL------RIGNRF-------------VHTGRPTPEAYAQALSEGgtlyfgvptvwsrIAADPEA 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 413 WDKLifhkiqsslgGKVRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYIKL 492
Cdd:PRK07787 237 ARAL----------RGARLLVSGSAALPVPVFDRLAALTGHRPVERYGMTETLITLSTRADGERRPGWVGLPLAGVETRL 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 493 VDvEDMNYQAAKGE--GEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDR------KKHIFKLA 564
Cdd:PRK07787 307 VD-EDGGPVPHDGEtvGELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDPDGMHRIVGRestdliKSGGYRIG 385
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 564389119 565 QGEyiapekIENIYLRSEAVAQVFVHGE---SLQAFLIAIVVPDVEILPS 611
Cdd:PRK07787 386 AGE------IETALLGHPGVREAAVVGVpddDLGQRIVAYVVGADDVAAD 429
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
118-558 |
6.20e-29 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 121.62 E-value: 6.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 118 PYEWISYKQVAEMAECIGSALIQKGFKPcSEQFIGIFSQNRpEWVTIEQGCFTYSMVVVPLydtlgTDAITYivnkaels 197
Cdd:cd05906 36 SEEFQSYQDLLEDARRLAAGLRQLGLRP-GDSVILQFDDNE-DFIPAFWACVLAGFVPAPL-----TVPPTY-------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 198 vifaDKPEKAKLLLEGVENKLTPClkiIVIMDSydnDLVE--RGQKC--GVEIIGLKALEDLGRVNRTKPKPP-EPEDLA 272
Cdd:cd05906 101 ----DEPNARLRKLRHIWQLLGSP---VVLTDA---ELVAefAGLETlsGLPGIRVLSIEELLDTAADHDLPQsRPDDLA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 273 IICFTSGTTGNPKGAMVTHQNIMNDCSGfikaTESAFIASPEDVLISFLPLAHmfetVVECVMlCHGAkigffqgDIRLL 352
Cdd:cd05906 171 LLMLTSGSTGFPKAVPLTHRNILARSAG----KIQHNGLTPQDVFLNWVPLDH----VGGLVE-LHLR-------AVYLG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 353 MDDLKVLQPTIFPVVPRLLnRMFDRiFGQANTsvkrWLLDFA-SKRKEAELRsgivRNNSLWDklifhkiQSSLggkvRL 431
Cdd:cd05906 235 CQQVHVPTEEILADPLRWL-DLIDR-YRVTIT----WAPNFAfALLNDLLEE----IEDGTWD-------LSSL----RY 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 432 MITGAAPVSA-TVLTFLR--AALGCQ---FYEGYGQTECTAGC--CLSLP-GDWTAGH----VGAPMPCNYIKLVDVEDm 498
Cdd:cd05906 294 LVNAGEAVVAkTIRRLLRllEPYGLPpdaIRPAFGMTETCSGViySRSFPtYDHSQALefvsLGRPIPGVSMRIVDDEG- 372
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 499 NYQAAKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGkWLPNGTLKIIDRKK 558
Cdd:cd05906 373 QLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLG-FLDNGNLTITGRTK 431
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
233-589 |
8.97e-29 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 121.24 E-value: 8.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 233 NDLVERGQKCGVEIIGLKALEdlgrvnrtkpkppepEDLAIICFTSGTTGNPKGAMVTHQN-IMNDCSgfikateSAFIA 311
Cdd:PLN02330 163 KELLEAADRAGDTSDNEEILQ---------------TDLCALPFSSGTTGISKGVMLTHRNlVANLCS-------SLFSV 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 312 SPEDV----LISFLPLAHMFETVVEC--VMLCHGAKIGFFQGDIRLLMDDLKVLQPTIFPVVPRLLNRMfdrifgqants 385
Cdd:PLN02330 221 GPEMIgqvvTLGLIPFFHIYGITGICcaTLRNKGKVVVMSRFELRTFLNALITQEVSFAPIVPPIILNL----------- 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 386 VKrwlldfaskrkeaelrsgivrnNSLWDKLIFHKIqsslggKVRLMITGAAPVSATVLTFLRAAL-GCQFYEGYGQTEC 464
Cdd:PLN02330 290 VK----------------------NPIVEEFDLSKL------KLQAIMTAAAPLAPELLTAFEAKFpGVQVQEAYGLTEH 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 465 TagcCLSLP-GDWTAGH-------VGAPMPCNYIKLVDVEDMNYQAAKGEGEVCVKGANVFKGYLKDPARTAEALDKDGW 536
Cdd:PLN02330 342 S---CITLThGDPEKGHgiakknsVGFILPNLEVKFIDPDTGRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGW 418
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 564389119 537 LHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSEAVAQVFV 589
Cdd:PLN02330 419 LHTGDIGYIDDDGDIFIVDRIKELIKY-KGFQVAPAELEAILLTHPSVEDAAV 470
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
174-659 |
9.60e-29 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 123.11 E-value: 9.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 174 VVVPLYDTLGTDAITYIVNKAELSVIFADKPEKAKLLLEGVENKLTPCLKIIvimdsYDNDLVERGQKcgVEII--GLKA 251
Cdd:PRK08633 691 VPVNLNYTASEAALKSAIEQAQIKTVITSRKFLEKLKNKGFDLELPENVKVI-----YLEDLKAKISK--VDKLtaLLAA 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 252 ----LEDLGRVNRTKPKPpepEDLAIICFTSGTTGNPKGAMVTHQNIMNDcsgfIKATESAFIASPEDVLISFLPLAHMF 327
Cdd:PRK08633 764 rllpARLLKRLYGPTFKP---DDTATIIFSSGSEGEPKGVMLSHHNILSN----IEQISDVFNLRNDDVILSSLPFFHSF 836
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 328 ETVVECVM-LCHGAKIGFFQGDirllMDDLKVLQ-------------PTIFpvvprllnRMFDRifgqaNTSVKRwlLDF 393
Cdd:PRK08633 837 GLTVTLWLpLLEGIKVVYHPDP----TDALGIAKlvakhratillgtPTFL--------RLYLR-----NKKLHP--LMF 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 394 ASkrkeaelrsgivrnnslwdklifhkiqsslggkVRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLSLP 473
Cdd:PRK08633 898 AS---------------------------------LRLVVAGAEKLKPEVADAFEEKFGIRILEGYGATETSPVASVNLP 944
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 474 -----GDWT-----AGHVGAPMPCNYIKLVDVEDMNYQAAKGEGEVCVKGANVFKGYLKDPARTAEAL---DKDGWLHTG 540
Cdd:PRK08633 945 dvlaaDFKRqtgskEGSVGMPLPGVAVRIVDPETFEELPPGEDGLILIGGPQVMKGYLGDPEKTAEVIkdiDGIGWYVTG 1024
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 541 DIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIEniylrsEAVAQVFvHGESLQafLIAIVVPDveilpswaQKRGFQ- 619
Cdd:PRK08633 1025 DKGHLDEDGFLTITDRYSRFAKIG-GEMVPLGAVE------EELAKAL-GGEEVV--FAVTAVPD--------EKKGEKl 1086
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 564389119 620 --------GSFEELCR---NKDINKA-------ILEDMVKLGknAGLKPFEQVKGIAV 659
Cdd:PRK08633 1087 vvlhtcgaEDVEELKRaikESGLPNLwkpsryfKVEALPLLG--SGKLDLKGLKELAL 1142
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
174-611 |
1.09e-28 |
|
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: 119.85 E-value: 1.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 174 VVVPLYDTLGTDAITYIVNKAELSVIFADkpekaklllEGVENKLTPCLkiiviMDSYDNDLVergqkcgveiIGLKALE 253
Cdd:cd05922 48 VFVPLNPTLKESVLRYLVADAGGRIVLAD---------AGAADRLRDAL-----PASPDPGTV----------LDADGIR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 254 DLGRvnRTKPKPPEPEDLAIICFTSGTTGNPKGAMVTHQNIMndcsgfikaTESAFIAS-----PEDVLISFLPLAHMFE 328
Cdd:cd05922 104 AARA--SAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLL---------ANARSIAEylgitADDRALTVLPLSYDYG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 329 TVVECVMLCHGAKIgFFQGDIRL---LMDDLKVLQPTIFPVVPRLLNrMFDRifgqantsvkrwlLDFAsKRKEAELRsg 405
Cdd:cd05922 173 LSVLNTHLLRGATL-VLTNDGVLddaFWEDLREHGATGLAGVPSTYA-MLTR-------------LGFD-PAKLPSLR-- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 406 ivrnnslwdklifhkIQSSLGGKVRlmitgaapvSATVLTFLRAALGCQFYEGYGQTECTAGCCLsLPGDWTA---GHVG 482
Cdd:cd05922 235 ---------------YLTQAGGRLP---------QETIARLRELLPGAQVYVMYGQTEATRRMTY-LPPERILekpGSIG 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 483 APMPCNYIkLVDVEDMNYQAAKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFK 562
Cdd:cd05922 290 LAIPGGEF-EILDDDGTPTPPGEPGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIK 368
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 564389119 563 LAqGEYIAPEKIENIyLRSEA---VAQVFVHGESLQAFLIAIVVPDVEILPS 611
Cdd:cd05922 369 LF-GNRISPTEIEAA-ARSIGliiEAAAVGLPDPLGEKLALFVTAPDKIDPK 418
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
112-616 |
2.06e-28 |
|
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: 119.35 E-value: 2.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 112 SRKPNQPY-----EWISYKQVAEMAECIGSALIQKGFKPcsEQFIGIFSQNRPEWVTIEQGCFTYSMVVVPLYDTLGTDA 186
Cdd:cd17655 8 EKTPDHTAvvfedQTLTYRELNERANQLARTLREKGVGP--DTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEER 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 187 ITYIVNKAELSVIFADKPEKAKLLLEGvenkltpclkiivimdsyDNDLVERGQkcgveiIGLKALEDLGRVNRtkpkpp 266
Cdd:cd17655 86 IQYILEDSGADILLTQSHLQPPIAFIG------------------LIDLLDEDT------IYHEESENLEPVSK------ 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 267 ePEDLAIICFTSGTTGNPKGAMVTHQNIMNdcsgFIKATESAFIASPEDVLISFLPLAhmfetvvecvmlchgakigfFq 346
Cdd:cd17655 136 -SDDLAYVIYTSGSTGKPKGVMIEHRGVVN----LVEWANKVIYQGEHLRVALFASIS--------------------F- 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 347 gdirllmdDLKVLQptIFPvvPRLL-NRMFdrIFGQANTSVKRWLLDFASKRkeaelRSGIVRNNSLWDKLIFHkIQSSL 425
Cdd:cd17655 190 --------DASVTE--IFA--SLLSgNTLY--IVRKETVLDGQALTQYIRQN-----RITIIDLTPAHLKLLDA-ADDSE 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 426 GGKVRLMITGAAPVSATVLTFL--RAALGCQFYEGYGQTECTAGCCLSL--PGDWTAGHV--GAPMPCNYIKLVDvEDMN 499
Cdd:cd17655 250 GLSLKHLIVGGEALSTELAKKIieLFGTNPTITNAYGPTETTVDASIYQyePETDQQVSVpiGKPLGNTRIYILD-QYGR 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 500 YQAAKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWL------HTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEK 573
Cdd:cd17655 329 PQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVpgermyRTGDLARWLPDGNIEFLGRIDHQVKI-RGYRIELGE 407
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 564389119 574 IENIYLRSEAVAQ--VFVH-GESLQAFLIAIVVPDVEILPSWAQKR 616
Cdd:cd17655 408 IEARLLQHPDIKEavVIARkDEQGQNYLCAYIVSEKELPVAQLREF 453
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
120-616 |
3.04e-28 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 121.89 E-value: 3.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 120 EWISYKQVAEMAECIGSALIQKGFKPcsEQFIGIFSQNRPEwvtieqgcftysMVV------------VPLYDTLGTDAI 187
Cdd:COG1020 500 QSLTYAELNARANRLAHHLRALGVGP--GDLVGVCLERSLE------------MVVallavlkagaayVPLDPAYPAERL 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 188 TYIVNKAELSVIfadkpekaklllegvenkLTpclkiivimdsyDNDLVERGQKCGVEIIGLKALEdLGRVNRTKPKPP- 266
Cdd:COG1020 566 AYMLEDAGARLV------------------LT------------QSALAARLPELGVPVLALDALA-LAAEPATNPPVPv 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 267 EPEDLAIICFTSGTTGNPKGAMVTHQNIMNdcsgFIKATESAFIASPEDVLISFLPLAhmFE-TVVECVM-LCHGAKIGF 344
Cdd:COG1020 615 TPDDLAYVIYTSGSTGRPKGVMVEHRALVN----LLAWMQRRYGLGPGDRVLQFASLS--FDaSVWEIFGaLLSGATLVL 688
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 345 FQGDIRLLMDDLKVL----QPTIFPVVPRLLNRMFDrifgqantsvkrwlldfaskrkeaelrsgivrnnSLWDKLifhk 420
Cdd:COG1020 689 APPEARRDPAALAELlarhRVTVLNLTPSLLRALLD----------------------------------AAPEAL---- 730
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 421 iqSSLggkvRLMITG--AAPVsATVLTFLRAALGCQFYEGYGQTECTAGCCLSL--PGDWTAGHV--GAPMPCNYIKLVD 494
Cdd:COG1020 731 --PSL----RLVLVGgeALPP-ELVRRWRARLPGARLVNLYGPTETTVDSTYYEvtPPDADGGSVpiGRPIANTRVYVLD 803
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 495 vEDMNYQAAKGEGEVCVKGANVFKGYLKDPARTAEA-----LDKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGE 567
Cdd:COG1020 804 -AHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERfvadpFGFPGarLYRTGDLARWLPDGNLEFLGRADDQVKI-RGF 881
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 564389119 568 YIAPEKIENIYLRSEAVAQ--VFVHGESLQA-FLIAIVVPDVEILPSWAQKR 616
Cdd:COG1020 882 RIELGEIEAALLQHPGVREavVVAREDAPGDkRLVAYVVPEAGAAAAAALLR 933
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
269-592 |
6.41e-28 |
|
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: 116.68 E-value: 6.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 269 EDLAIICFTSGTTGNPKGAMVTHQNIMNdcsgfikateSAfIASPE-------DVLISFLPLAH------MFETVVE-CV 334
Cdd:cd05912 77 DDIATIMYTSGTTGKPKGVQQTFGNHWW----------SA-IGSALnlgltedDNWLCALPLFHisglsiLMRSVIYgMT 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 335 MLCHGAkigFFQGDIRLLMDDLKVlqpTIFPVVPRLLNRMFDRIFGQANTSVkrwlldfaskrkeaelrsgivrnnslwd 414
Cdd:cd05912 146 VYLVDK---FDAEQVLHLINSGKV---TIISVVPTMLQRLLEILGEGYPNNL---------------------------- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 415 klifhkiqsslggkvRLMITGAAPVSATVLTFLRAaLGCQFYEGYGQTE-CTAGCCLSlPGDWTA--GHVGAPMPCNYIK 491
Cdd:cd05912 192 ---------------RCILLGGGPAPKPLLEQCKE-KGIPVYQSYGMTEtCSQIVTLS-PEDALNkiGSAGKPLFPVELK 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 492 LVDvedmNYQAAKGEGEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAP 571
Cdd:cd05912 255 IED----DGQPPYEVGEILLKGPNVTKGYLNRPDATEESF-ENGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYP 328
|
330 340
....*....|....*....|.
gi 564389119 572 EKIENIYLRSEAVAQVFVHGE 592
Cdd:cd05912 329 AEIEEVLLSHPAIKEAGVVGI 349
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
265-558 |
3.87e-27 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 115.74 E-value: 3.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 265 PPEPEDLAIICFTSGTTGNPKGAMVTHQNI------MNDCSGFikatesafiaSPEDVLISFLPLAH---MFetVVECVM 335
Cdd:PRK07514 152 PRGADDLAAILYTSGTTGRSKGAMLSHGNLlsnaltLVDYWRF----------TPDDVLIHALPIFHthgLF--VATNVA 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 336 LCHGAKIGFFQG-DIRLLMDDLKvlQPTIFPVVP----RLL-NRMFDRifgqantsvkrwlldfaskrkEAelrsgiVRN 409
Cdd:PRK07514 220 LLAGASMIFLPKfDPDAVLALMP--RATVMMGVPtfytRLLqEPRLTR---------------------EA------AAH 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 410 nslwdklifhkiqsslggkVRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTEctAGCCLSLP--GDWTAGHVGAPMPC 487
Cdd:PRK07514 271 -------------------MRLFISGSAPLLAETHREFQERTGHAILERYGMTE--TNMNTSNPydGERRAGTVGFPLPG 329
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564389119 488 NYIKLVDVEDMNYQAAKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKK 558
Cdd:PRK07514 330 VSLRVTDPETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGFFITGDLGKIDERGYVHIVGRGK 400
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
263-585 |
6.55e-27 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 116.21 E-value: 6.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 263 PKPPEPEDLAIICFTSGTTGNPKGAMVTHQNIMNDcsGFIKATESAFiaSPEDVLISFLPLAHMFETVVEC-VMLCHGAK 341
Cdd:PRK07529 207 GRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVAN--AWLGALLLGL--GPGDTVFCGLPLFHVNALLVTGlAPLARGAH 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 342 IGFF--QG--DIRLLMDDLKVL---QPTIFPVVPRLLNRMFDRIFGQANTSvkrwlldfaskrkeaelrsgivrnnslwd 414
Cdd:PRK07529 283 VVLAtpQGyrGPGVIANFWKIVeryRINFLSGVPTVYAALLQVPVDGHDIS----------------------------- 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 415 klifhkiqsSLggkvRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLSLP-GDWTAGHVGAPMPCNYIKLV 493
Cdd:PRK07529 334 ---------SL----RYALCGAAPLPVEVFRRFEAATGVRIVEGYGLTEATCVSSVNPPdGERRIGSVGLRLPYQRVRVV 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 494 DV-EDMNYQ--AAKGE-GEVCVKGANVFKGYLkDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYI 569
Cdd:PRK07529 401 ILdDAGRYLrdCAVDEvGVLCIAGPNVFSGYL-EAAHNKGLWLEDGWLNTGDLGRIDADGYFWLTGRAKDLI-IRGGHNI 478
|
330
....*....|....*.
gi 564389119 570 APEKIENIYLRSEAVA 585
Cdd:PRK07529 479 DPAAIEEALLRHPAVA 494
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
106-672 |
7.33e-27 |
|
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: 115.61 E-value: 7.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 106 DGPCLGSRKPNQPYEWISYKQVAEMAECIGSALIQKGFKPcsEQFIGIFSQNRPEWVTIEQGCFTY---SMVVVPLYDTL 182
Cdd:cd05921 10 DRTWLAEREGNGGWRRVTYAEALRQVRAIAQGLLDLGLSA--ERPLLILSGNSIEHALMALAAMYAgvpAAPVSPAYSLM 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 183 GTD--AITYIVNKAELSVIFADKPEKAKLLLEGVENKLTPclkIIVIMdsydNDLVERGQkcgVEIIGLKALEDLGRVNR 260
Cdd:cd05921 88 SQDlaKLKHLFELLKPGLVFAQDAAPFARALAAIFPLGTP---LVVSR----NAVAGRGA---ISFAELAATPPTAAVDA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 261 TKPKPpEPEDLAIICFTSGTTGNPKGAMVTHQNIMNDCSGfiKATESAFIASPEDVLISFLPLAHMFetvvecvmlchGA 340
Cdd:cd05921 158 AFAAV-GPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAM--LEQTYPFFGEEPPVLVDWLPWNHTF-----------GG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 341 KIGF-----------------FQGDIRLLMDDLKVLQPTIFPVVPrllnrmfdrifgqantsvKRWLLDFASKRKEAELR 403
Cdd:cd05921 224 NHNFnlvlynggtlyiddgkpMPGGFEETLRNLREISPTVYFNVP------------------AGWEMLVAALEKDEALR 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 404 SGIVRNnslwdklifhkiqsslggkVRLMITGAAPVSATVLTFLRAaLGCQ-------FYEGYGQTEcTAGCCLSLPGDW 476
Cdd:cd05921 286 RRFFKR-------------------LKLMFYAGAGLSQDVWDRLQA-LAVAtvgeripMMAGLGATE-TAPTATFTHWPT 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 477 T-AGHVGAPMPCNYIKLVDVEdmnyqaakGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWL----PNGTL 551
Cdd:cd05921 345 ErSGLIGLPAPGTELKLVPSG--------GKYEVRVKGPNVTPGYWRQPELTAQAFDEEGFYCLGDAAKLAdpddPAKGL 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 552 KIIDRKKHIFKLAQGEYIA--PekieniyLRSEAVAQ-------VFVHGESlQAFLIAIVVPDveILPSWAQKRGFQGSF 622
Cdd:cd05921 417 VFDGRVAEDFKLASGTWVSvgP-------LRARAVAAcaplvhdAVVAGED-RAEVGALVFPD--LLACRRLVGLQEASD 486
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 564389119 623 EELCRNKDInKAILEDMVKLGKNAGLKPFEQVKGIAVHPELFSIDNGLLT 672
Cdd:cd05921 487 AEVLRHAKV-RAAFRDRLAALNGEATGSSSRIARALLLDEPPSIDKGEIT 535
|
|
| PTZ00297 |
PTZ00297 |
pantothenate kinase; Provisional |
90-695 |
7.87e-27 |
|
pantothenate kinase; Provisional
Pssm-ID: 140318 [Multi-domain] Cd Length: 1452 Bit Score: 117.26 E-value: 7.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 90 VRTMYDGFQRGIQVSNDGPCLGSRKPNQPYEWISYKQVAEMAECIGSALIQKGFKPcsEQFIGIFSQNRPEWVTIEQGCF 169
Cdd:PTZ00297 426 VRSLGEMWERSVTRHSTFRCLGQTSESGESEWLTYGTVDARARELGSGLLALGVRP--GDVIGVDCEASRNIVILEVACA 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 170 TYSMVVVPLYDTLGTdaITYIVNKAELSVIFADKPEKAKLLlegvenkltPC----LKIIVIMDS-YDNDLVERGQKCGV 244
Cdd:PTZ00297 504 LYGFTTLPLVGKGST--MRTLIDEHKIKVVFADRNSVAAIL---------TCrsrkLETVVYTHSfYDEDDHAVARDLNI 572
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 245 EIIGLKALEDLGRVNRTKPKPPEPED----LAIICFTSGTTGNPKGAMVTHQNIMNDCSGFIkATESAFIASPEDVLISF 320
Cdd:PTZ00297 573 TLIPYEFVEQKGRLCPVPLKEHVTTDtvftYVVDNTTSASGDGLAVVRVTHADVLRDISTLV-MTGVLPSSFKKHLMVHF 651
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 321 LPLAHMFETVVECVMLCHGAKIGffQGDIRLLMDDLKVLQPTIFPVVPRL-------LNRMFDRifgqaNTSVKRWLLDf 393
Cdd:PTZ00297 652 TPFAMLFNRVFVLGLFAHGSAVA--TVDAAHLQRAFVKFQPTILVAAPSLfstsrlqLSRANER-----YSAVYSWLFE- 723
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 394 askrKEAELRSGIV----RNNSLWDKLIFHKIQSSLGGKVRLMITGAAPVSaTVLTFLRAALGCQ-------FYegygqT 462
Cdd:PTZ00297 724 ----RAFQLRSRLInihrRDSSLLRFIFFRATQELLGGCVEKIVLCVSEES-TSFSLLEHISVCYvpclrevFF-----L 793
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 463 ECTAGCCLSlpgdwtaghvGAPMPCNYIKLVDVEDMNYQAAKGEGEVCVKGanvfkgylkDPARTAEAldkdgwlhtgdI 542
Cdd:PTZ00297 794 PSEGVFCVD----------GTPAPSLQVDLEPFDEPSDGAGIGQLVLAKKG---------EPRRTLPI-----------A 843
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 543 GKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYLRSEAVAQVFVHGESLQAfLIAIVVPDVEILP-SWAQKRGF--- 618
Cdd:PTZ00297 844 AQWKRDRTLRLLGPPLGILLPVAYEYVIAAELERIFSQSRYVNDIFLYADPSRP-IIAIVSPNRDTVEfEWRQSHCMgeg 922
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 619 -----QGSFEELCRNKdiNKAILEDMVKLGKNAGLKPFEQVKGIAVHPELFSIDNGLLTPTLKAKRPELRNYFRSQIDEL 693
Cdd:PTZ00297 923 ggparQLGWTELVAYA--SSLLTADFACIAKENGLHPSNVPEYVHLHPHAFKDHSTFLTPYGKIRRDAVHSYFSSVIERF 1000
|
..
gi 564389119 694 YS 695
Cdd:PTZ00297 1001 YS 1002
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
120-591 |
9.88e-27 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 114.57 E-value: 9.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 120 EWISYKQVAEMAECIGSALIQK-GFKPCSEqfIGIFSQNRPEWVTIEQGCFTYSMVVVPLYDTLGTDAITYIVNKAELSV 198
Cdd:PRK06839 26 EEMTYKQLHEYVSKVAAYLIYElNVKKGER--IAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTTV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 199 IFADKpekaklllegvenkltpclkiivimdSYDNDLVERGQKCGVE----IIGLKALEDLGRVNRtkpKPPEPEDLAII 274
Cdd:PRK06839 104 LFVEK--------------------------TFQNMALSMQKVSYVQrvisITSLKEIEDRKIDNF---VEKNESASFII 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 275 CFTSGTTGNPKGAMVTHQNImndcsgFIKATESAFIA--SPEDVLISFLPLAHMfetvvecvmlchgAKIGFFQgdirll 352
Cdd:PRK06839 155 CYTSGTTGKPKGAVLTQENM------FWNALNNTFAIdlTMHDRSIVLLPLFHI-------------GGIGLFA------ 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 353 mddlkvlQPTIFP----VVPRLLN-----RMFDR-----IFGQAntSVKRWLLDfASKRKEAELRSgivrnnslwdklif 418
Cdd:PRK06839 210 -------FPTLFAggviIVPRKFEptkalSMIEKhkvtvVMGVP--TIHQALIN-CSKFETTNLQS-------------- 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 419 hkiqsslggkVRLMITGAAPVSATVLTFLRAAlGCQFYEGYGQTECTAGCCLSLPGDW--TAGHVGAPMPCNYIKLVDvE 496
Cdd:PRK06839 266 ----------VRWFYNGGAPCPEELMREFIDR-GFLFGQGFGMTETSPTVFMLSEEDArrKVGSIGKPVLFCDYELID-E 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 497 DMNYQAAKGEGEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIEN 576
Cdd:PRK06839 334 NKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETI-QDGWLCTGDLARVDEDGFVYIVGRKKEMI-ISGGENIYPLEVEQ 411
|
490
....*....|....*
gi 564389119 577 IYLRSEAVAQVFVHG 591
Cdd:PRK06839 412 VINKLSDVYEVAVVG 426
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
123-604 |
1.53e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 114.26 E-value: 1.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 123 SYKQVAEMAECIGSALIQKGFKPCSEqfIGIFSQNRPEWVTIEQGCFTYSMVVVPLYDTLGTDAITYIVNKAELSVIFAD 202
Cdd:PRK08316 38 TYAELDAAVNRVAAALLDLGLKKGDR--VAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAFLVD 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 203 kPEKAKLLLEGVEnkLTPCLKIIVimdsydnDLVERGQKCGVeiiGLKALEDLGRVNRTKPKPPEP--EDLAIICFTSGT 280
Cdd:PRK08316 116 -PALAPTAEAALA--LLPVDTLIL-------SLVLGGREAPG---GWLDFADWAEAGSVAEPDVELadDDLAQILYTSGT 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 281 TGNPKGAMVTHQNIMNDCSGFIKATEsafiASPEDVLISFLPLAHmfetvvecvmlChgAKIGFFqgdirlLMDDLKVLQ 360
Cdd:PRK08316 183 ESLPKGAMLTHRALIAEYVSCIVAGD----MSADDIPLHALPLYH-----------C--AQLDVF------LGPYLYVGA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 361 PTIFPVVPRLlNRMFDRIFGQANTS------VkrW--LL---DFAsKRKEAELRSGIVrnnslwdklifhkiqsslggkv 429
Cdd:PRK08316 240 TNVILDAPDP-ELILRTIEAERITSffapptV--WisLLrhpDFD-TRDLSSLRKGYY---------------------- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 430 rlmitGAAPVSATVLTFLRAAL-GCQFYEGYGQTEcTAGCCLSLPGDWTAGHVG-APMPCNYI--KLVDvEDMNyQAAKG 505
Cdd:PRK08316 294 -----GASIMPVEVLKELRERLpGLRFYNCYGQTE-IAPLATVLGPEEHLRRPGsAGRPVLNVetRVVD-DDGN-DVAPG 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 506 E-GEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYLRSEAV 584
Cdd:PRK08316 366 EvGEIVHRSPQLMLGYWDDPEKTAEAF-RGGWFHSGDLGVMDEEGYITVVDRKKDMIKTG-GENVASREVEEALYTHPAV 443
|
490 500
....*....|....*....|....
gi 564389119 585 AQVFV----HGESLQAfLIAIVVP 604
Cdd:PRK08316 444 AEVAViglpDPKWIEA-VTAVVVP 466
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
265-599 |
1.80e-26 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 114.36 E-value: 1.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 265 PPEPE-DLAIICFTSGTTGNPKGAMVTHQNIMNDCSGFIKATESAfiASPEDVLISFLPLAHMF-ETVVECVMLCHGAKI 342
Cdd:PRK06710 201 PCDPEnDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYNC--KEGEEVVLGVLPFFHVYgMTAVMNLSIMQGYKM 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 343 GFF-QGDIRLLMDDLKVLQPTIFPVVPRLLNRMFDrifgqantsvkrwlldfASKRKEAELRSgivrnnslwdklifhki 421
Cdd:PRK06710 279 VLIpKFDMKMVFEAIKKHKVTLFPGAPTIYIALLN-----------------SPLLKEYDISS----------------- 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 422 qsslggkVRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLS-LPGDWTAGHVGAPMPCNYIKLVDVEDMNY 500
Cdd:PRK06710 325 -------IRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSPVTHSNfLWEKRVPGSIGVPWPDTEAMIMSLETGEA 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 501 QAAKGEGEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLR 580
Cdd:PRK06710 398 LPPGEIGEIVVKGPQIMKGYWNKPEETAAVL-QDGWLHTGDVGYMDEDGFFYVKDRKKDMI-VASGFNVYPREVEEVLYE 475
|
330 340
....*....|....*....|....*.
gi 564389119 581 SEAVAQVFV-------HGESLQAFLI 599
Cdd:PRK06710 476 HEKVQEVVTigvpdpyRGETVKAFVV 501
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
121-629 |
1.96e-26 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.
Pssm-ID: 341283 [Multi-domain] Cd Length: 486 Bit Score: 113.55 E-value: 1.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 121 WISYKQVAEMAECIGSALIQKGFKPcsEQFIGIFSQNRPEWVTIEQGCFTYSMVVVPLYDTLGTDAITYIVNKAELSVIF 200
Cdd:cd12118 29 RYTWRQTYDRCRRLASALAALGISR--GDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVLF 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 201 ADKPekakllLEGvenkltpclkiivimdsydNDLVERGQKcgveiiglkaledlgrvnRTKPKPPEPEDLAI-ICFTSG 279
Cdd:cd12118 107 VDRE------FEY-------------------EDLLAEGDP------------------DFEWIPPADEWDPIaLNYTSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 280 TTGNPKGAMVTHQnimndcSGFIKATESA--FIASPEDVLISFLPLAHmfetvveCVMLCHGAKIGFFQG--------DI 349
Cdd:cd12118 144 TTGRPKGVVYHHR------GAYLNALANIleWEMKQHPVYLWTLPMFH-------CNGWCFPWTVAAVGGtnvclrkvDA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 350 RLLMDDLKVLQPTIFPVVPRLLNRMfdrifgqANTSvkrwlldfaskrkeaelrsgivrnnslwdklifHKIQSSLGGKV 429
Cdd:cd12118 211 KAIYDLIEKHKVTHFCGAPTVLNML-------ANAP---------------------------------PSDARPLPHRV 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 430 RLMITGAAPvSATVLtFLRAALGCQFYEGYGQTEcTAG---CCL------SLPGDWTAgHVGAPMPCNYIKL--VDVED- 497
Cdd:cd12118 251 HVMTAGAPP-PAAVL-AKMEELGFDVTHVYGLTE-TYGpatVCAwkpewdELPTEERA-RLKARQGVRYVGLeeVDVLDp 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 498 --MNYQAAKGE--GEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEK 573
Cdd:cd12118 327 etMKPVPRDGKtiGEIVFRGNIVMKGYLKNPEATAEAF-RGGWFHSGDLAVIHPDGYIEIKDRSKDII-ISGGENISSVE 404
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564389119 574 IENIYLRSEAVAQVFVH-------GESLQAFliaivvpdVEIlpswaqKRGFQGSFEEL---CRNK 629
Cdd:cd12118 405 VEGVLYKHPAVLEAAVVarpdekwGEVPCAF--------VEL------KEGAKVTEEEIiafCREH 456
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
91-545 |
2.03e-26 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 114.59 E-value: 2.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 91 RTMYDGFQRGIQVSNDGPCLGSRKPNQPYEWISYKQVAEMAECIGSALIQKGFKPcsEQFIGIFSQNRPEWVTIEQGCFT 170
Cdd:PRK08180 39 RRLTDRLVHWAQEAPDRVFLAERGADGGWRRLTYAEALERVRAIAQALLDRGLSA--ERPLMILSGNSIEHALLALAAMY 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 171 YSMVVVPL---YDTLGTD--AITYIVNKAELSVIFADKPEKAKLLLEGVEnklTPCLKIIVImdsydndlveRGQKCGVE 245
Cdd:PRK08180 117 AGVPYAPVspaYSLVSQDfgKLRHVLELLTPGLVFADDGAAFARALAAVV---PADVEVVAV----------RGAVPGRA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 246 IIGLKALEDLgrvnrtkPKPPE---------PEDLAIICFTSGTTGNPKGAMVTHQNImndCSG--FIKATeSAFIASPE 314
Cdd:PRK08180 184 ATPFAALLAT-------PPTAAvdaahaavgPDTIAKFLFTSGSTGLPKAVINTHRML---CANqqMLAQT-FPFLAEEP 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 315 DVLISFLPLAHMFETVVEC-VMLCHGAKI---------GFFQGDIRllmdDLKVLQPTIFPVVPR----LLNRMfdrifg 380
Cdd:PRK08180 253 PVLVDWLPWNHTFGGNHNLgIVLYNGGTLyiddgkptpGGFDETLR----NLREISPTVYFNVPKgwemLVPAL------ 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 381 qantsvkrwlldfaskRKEAELRSgivrnnslwdklifhkiqsSLGGKVRLMITGAAPVSATVLTFL----RAALGCQ-- 454
Cdd:PRK08180 323 ----------------ERDAALRR-------------------RFFSRLKLLFYAGAALSQDVWDRLdrvaEATCGERir 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 455 FYEGYGQTEcTAGCCLSL--PGDwTAGHVGAPMPCNYIKLVDVEdmnyqaakGEGEVCVKGANVFKGYLKDPARTAEALD 532
Cdd:PRK08180 368 MMTGLGMTE-TAPSATFTtgPLS-RAGNIGLPAPGCEVKLVPVG--------GKLEVRVKGPNVTPGYWRAPELTAEAFD 437
|
490
....*....|...
gi 564389119 533 KDGWLHTGDIGKW 545
Cdd:PRK08180 438 EEGYYRSGDAVRF 450
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
268-605 |
8.63e-26 |
|
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: 111.48 E-value: 8.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 268 PEDLAIICFTSGTTGNPKGAMVTHQNImndCSGfIKATESAFIASPED-VL----ISF-LPLAHMFETvvecvmLCHGAK 341
Cdd:cd05918 105 PSDAAYVIFTSGSTGKPKGVVIEHRAL---STS-ALAHGRALGLTSESrVLqfasYTFdVSILEIFTT------LAAGGC 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 342 IGffqgdI---RLLMDDLkvlqptifpvvPRLLNRMfdrifgQANT-----SVKRwLLDfaskrkEAELRSgivrnnslw 413
Cdd:cd05918 175 LC-----IpseEDRLNDL-----------AGFINRL------RVTWafltpSVAR-LLD------PEDVPS--------- 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 414 dklifhkiqsslggkVRLMITGAAPVSATVLTflRAALGCQFYEGYGQTECTAGCCLSLPG-DWTAGHVGAPMPCNyIKL 492
Cdd:cd05918 217 ---------------LRTLVLGGEALTQSDVD--TWADRVRLINAYGPAECTIAATVSPVVpSTDPRNIGRPLGAT-CWV 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 493 VDVEDMNYQAAKGE-GEVCVKGANVFKGYLKDPARTAEALDKD-GWLH------------TGDIGKWLPNGTLKIIDRKK 558
Cdd:cd05918 279 VDPDNHDRLVPIGAvGELLIEGPILARGYLNDPEKTAAAFIEDpAWLKqegsgrgrrlyrTGDLVRYNPDGSLEYVGRKD 358
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 564389119 559 HIFKLaQGEYIAPEKIENIYLRS-----EAVAQVFVH-GESLQAFLIAIVVPD 605
Cdd:cd05918 359 TQVKI-RGQRVELGEIEHHLRQSlpgakEVVVEVVKPkDGSSSPQLVAFVVLD 410
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
122-589 |
1.64e-25 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 111.36 E-value: 1.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 122 ISYKQVAEMAECIGSALIQKGFKPcsEQFIGIFSQNRPEWVTIEQGCftYSM--VVVPLYDTLGTDAITYIVNKAELSVI 199
Cdd:COG0365 40 LTYAELRREVNRFANALRALGVKK--GDRVAIYLPNIPEAVIAMLAC--ARIgaVHSPVFPGFGAEALADRIEDAEAKVL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 200 FAD-------KPEKAKLLLEGVENKLTPCLKIIVImdsydndlveRGQKCGVEIIGLKALEDL--GRVNRTKPKPPEPED 270
Cdd:COG0365 116 ITAdgglrggKVIDLKEKVDEALEELPSLEHVIVV----------GRTGADVPMEGDLDWDELlaAASAEFEPEPTDADD 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 271 LAIICFTSGTTGNPKGAMVTHQNIMNDCSGFIKATesaFIASPEDVLISFLPLA----HMFetvveCVM--LCHGAKIGF 344
Cdd:COG0365 186 PLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYV---LDLKPGDVFWCTADIGwatgHSY-----IVYgpLLNGATVVL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 345 FQGDI------RL--LMDDLKVlqpTIFPVVPRLLnRMFdrifgqantsvKRWLLDFASKRkeaelrsgivrnnSLwdkl 416
Cdd:COG0365 258 YEGRPdfpdpgRLweLIEKYGV---TVFFTAPTAI-RAL-----------MKAGDEPLKKY-------------DL---- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 417 ifhkiqSSLggkvRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLSLPGDWT-AGHVGAPMPCNYIKLVDv 495
Cdd:COG0365 306 ------SSL----RLLGSAGEPLNPEVWEWWYEAVGVPIVDGWGQTETGGIFISNLPGLPVkPGSMGKPVPGYDVAVVD- 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 496 EDMNYQAAKGEGEVCVKGAN--VFKGYLKDPARTAEAL--DKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAP 571
Cdd:COG0365 375 EDGNPVPPGEEGELVIKGPWpgMFRGYWNDPERYRETYfgRFPGWYRTGDGARRDEDGYFWILGRSDDVINVS-GHRIGT 453
|
490
....*....|....*...
gi 564389119 572 EKIENIYLRSEAVAQVFV 589
Cdd:COG0365 454 AEIESALVSHPAVAEAAV 471
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
153-616 |
2.12e-25 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 111.02 E-value: 2.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 153 IFSQNRPEWVTIEQGCFTYSMVVVPLYDTLGTDAITYIVNKAELSVIFADKPEKAklLLEGVENKLTPCLKIIVIMDSYD 232
Cdd:PRK07786 72 ILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVVTEAALAP--VATAVRDIVPLLSTVVVAGGSSD 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 233 NDLVergqkcgveiiglkALEDLgrVNRTKPKPPE---PEDL-AIICFTSGTTGNPKGAMVTHQNIMNDCSGFIKATEsa 308
Cdd:PRK07786 150 DSVL--------------GYEDL--LAEAGPAHAPvdiPNDSpALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNG-- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 309 fIASPEDVLISFLPLAHM--FETVVECVMLchGAKIgffqgdirllmddlkVLQPTifpvvprllnRMFDRifGQantsv 386
Cdd:PRK07786 212 -ADINSDVGFVGVPLFHIagIGSMLPGLLL--GAPT---------------VIYPL----------GAFDP--GQ----- 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 387 krwLLDFAskrkEAELRSGIVRNNSLWDKLIFHKIQSSLGGKVRLMITGAAPVSATVLTFLRAAL-GCQFYEGYGQTECT 465
Cdd:PRK07786 257 ---LLDVL----EAEKVTGIFLVPAQWQAVCAEQQARPRDLALRVLSWGAAPASDTLLRQMAATFpEAQILAAFGQTEMS 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 466 AGCCLSLPGDWTA--GHVGAPMPCNYIKLVDvEDMNyQAAKGE-GEVCVKGANVFKGYLKDPARTAEALDkDGWLHTGDI 542
Cdd:PRK07786 330 PVTCMLLGEDAIRklGSVGKVIPTVAARVVD-ENMN-DVPVGEvGEIVYRAPTLMSGYWNNPEATAEAFA-GGWFHSGDL 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 543 GKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAVAQVFVHGESLQAF---LIAIVVPD-------VEILPSW 612
Cdd:PRK07786 407 VRQDEEGYVWVVDRKKDMI-ISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWgevPVAVAAVRnddaaltLEDLAEF 485
|
....
gi 564389119 613 AQKR 616
Cdd:PRK07786 486 LTDR 489
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
124-608 |
2.63e-25 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 110.05 E-value: 2.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 124 YKQVAEMAECIGSALIQKGfkpcseQFIGIFSQNRPEWVTIEQGCFTYSMVVVPLYDTLGTDAITYIVNKAELSVIFADk 203
Cdd:PRK03640 34 HEAVVSVAGKLAALGVKKG------DRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKCLITD- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 204 pekaklllegvenkltpclkiivimDSYDNDLVERGQKcgveiiglkALEDLGRVNRTKPKPPEPEDL---AIICFTSGT 280
Cdd:PRK03640 107 -------------------------DDFEAKLIPGISV---------KFAELMNGPKEEAEIQEEFDLdevATIMYTSGT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 281 TGNPKGAMVTHQNimndcsGFIKATESAFIA--SPEDVLISFLPLAHM--FETVVECVMlcHGAKI----GFFQGDI-RL 351
Cdd:PRK03640 153 TGKPKGVIQTYGN------HWWSAVGSALNLglTEDDCWLAAVPIFHIsgLSILMRSVI--YGMRVvlveKFDAEKInKL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 352 LMDDlKVlqpTIFPVVPRLLNRMFDRIfGQANTsvkrwlldfaskrkeaelrsgivrNNSLwdklifhkiqsslggkvRL 431
Cdd:PRK03640 225 LQTG-GV---TIISVVSTMLQRLLERL-GEGTY------------------------PSSF-----------------RC 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 432 MITGAAPVSATVLTFLRAAlGCQFYEGYGQTEcTAGCCLSLPGDWTA---GHVGAPM-PCNyIKLVDveDMNYQAAKGEG 507
Cdd:PRK03640 259 MLLGGGPAPKPLLEQCKEK-GIPVYQSYGMTE-TASQIVTLSPEDALtklGSAGKPLfPCE-LKIEK--DGVVVPPFEEG 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 508 EVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAVAQV 587
Cdd:PRK03640 334 EIVVKGPNVTKGYLNREDATRETF-QDGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIEEVLLSHPGVAEA 411
|
490 500
....*....|....*....|....
gi 564389119 588 FVHGESLQ---AFLIAIVVPDVEI 608
Cdd:PRK03640 412 GVVGVPDDkwgQVPVAFVVKSGEV 435
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
128-591 |
5.50e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 109.13 E-value: 5.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 128 AEMAECIGSA---LIQKGFKPcsEQFIGIFSQNRPEWVTIEQGCFTYSMVVVPLYDTLGTDAITYIVNKAELSVIFADkp 204
Cdd:PRK09088 26 AELDALVGRLaavLRRRGCVD--GERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLLGD-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 205 ekaklllegvenkltpclkiivimdsydnDLVERGQKCGVEIIGLKALEDLGRVNRTKPKPPEpeDLAIICFTSGTTGNP 284
Cdd:PRK09088 102 -----------------------------DAVAAGRTDVEDLAAFIASADALEPADTPSIPPE--RVSLILFTSGTSGQP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 285 KGAMVTHQNIMNDCSGFIKATESafiaspeDVLISFLPLAHMFETV--VECV--MLCHGAKIGFFQGdirllmddlkvLQ 360
Cdd:PRK09088 151 KGVMLSERNLQQTAHNFGVLGRV-------DAHSSFLCDAPMFHIIglITSVrpVLAVGGSILVSNG-----------FE 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 361 PTifpvvpRLLNRMFDRIFGQANTsvkrwlldFASKRKEAELRSGIVRNNSLWDKLIfhkiqsslggkvrLMITGAAP-V 439
Cdd:PRK09088 213 PK------RTLGRLGDPALGITHY--------FCVPQMAQAFRAQPGFDAAALRHLT-------------ALFTGGAPhA 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 440 SATVLTFLraALGCQFYEGYGQTEctAGCCLSLPGDWT-----AGHVGAPMPCNYIKLVDVEDMNYQAakGE-GEVCVKG 513
Cdd:PRK09088 266 AEDILGWL--DDGIPMVDGFGMSE--AGTVFGMSVDCDvirakAGAAGIPTPTVQTRVVDDQGNDCPA--GVpGELLLRG 339
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564389119 514 ANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAVAQVFVHG 591
Cdd:PRK09088 340 PNLSPGYWRRPQATARAFTGDGWFRTGDIARRDADGFFWVVDRKKDMF-ISGGENVYPAEIEAVLADHPGIRECAVVG 416
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
263-577 |
8.13e-25 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 109.16 E-value: 8.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 263 PKPP-EPEDLAIICFTSGTTGNPKGAMVTHQNIMNDCSGFIKATESAFIAS-PEDVLISFLPLAHMFETVVECV-MLCHG 339
Cdd:PLN02574 191 PKPViKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVRFEASQYEYPgSDNVYLAALPMFHIYGLSLFVVgLLSLG 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 340 AKI----GFFQGDIRLLMDDLKVlqpTIFPVVPRLLNRMFDRIFGQANTSVKrwlldfaskrkeaelrsgivrnnslwdk 415
Cdd:PLN02574 271 STIvvmrRFDASDMVKVIDRFKV---THFPVVPPILMALTKKAKGVCGEVLK---------------------------- 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 416 lifhkiqsslggKVRLMITGAAPVSA-TVLTFLRAALGCQFYEGYGQTECTAGCCLSLPGDWTAGH--VGAPMPCNYIKL 492
Cdd:PLN02574 320 ------------SLKQVSCGAAPLSGkFIQDFVQTLPHVDFIQGYGMTESTAVGTRGFNTEKLSKYssVGLLAPNMQAKV 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 493 VDVEDMNYQAAKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPE 572
Cdd:PLN02574 388 VDWSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKY-KGFQIAPA 466
|
....*
gi 564389119 573 KIENI 577
Cdd:PLN02574 467 DLEAV 471
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
120-616 |
1.19e-24 |
|
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: 107.76 E-value: 1.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 120 EWISYKQVAEMAECIGSALIQKGFKPcsEQFIGIFSQNRPEWVTIEQGCFTYSMVVVPLYDTLGTDAITYIVNKAELSVI 199
Cdd:cd12116 11 RSLSYAELDERANRLAARLRARGVGP--GDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 200 fadkpekaklllegvenkLTpclkiivimdsyDNDLVERGQKCGVEIigLKALEDLGRVNRTKPKPPEPEDLAIICFTSG 279
Cdd:cd12116 89 ------------------LT------------DDALPDRLPAGLPVL--LLALAAAAAAPAAPRTPVSPDDLAYVIYTSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 280 TTGNPKGAMVTHQNIMNdcsgFIKATESAFIASPEDVLISFLPLAhmFE-TVVECVM-LCHGAKIGFFQGDI----RLLM 353
Cdd:cd12116 137 STGRPKGVVVSHRNLVN----FLHSMRERLGLGPGDRLLAVTTYA--FDiSLLELLLpLLAGARVVIAPRETqrdpEALA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 354 DDLKVLQPTIFpvvprllnrmfdrifgQANTSVKRWLLDfASKRKEAELRsgivrnnslwdklifhkiqsslggkvrlMI 433
Cdd:cd12116 211 RLIEAHSITVM----------------QATPATWRMLLD-AGWQGRAGLT----------------------------AL 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 434 TGAAPVSATVLTFLrAALGCQFYEGYGQTECT--AGCCLSLPGDwTAGHVGAPMPCNYIKLVDvEDMNYQAAKGEGEVCV 511
Cdd:cd12116 246 CGGEALPPDLAARL-LSRVGSLWNLYGPTETTiwSTAARVTAAA-GPIPIGRPLANTQVYVLD-AALRPVPPGVPGELYI 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 512 KGANVFKGYLKDPARTAEALDKDGWLH-------TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSEAV 584
Cdd:cd12116 323 GGDGVAQGYLGRPALTAERFVPDPFAGpgsrlyrTGDLVRRRADGRLEYLGRADGQVKI-RGHRIELGEIEAALAAHPGV 401
|
490 500 510
....*....|....*....|....*....|....
gi 564389119 585 AQ--VFVHGESLQAFLIAIVVPDVEILPSWAQKR 616
Cdd:cd12116 402 AQaaVVVREDGGDRRLVAYVVLKAGAAPDAAALR 435
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
122-599 |
2.42e-24 |
|
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: 106.41 E-value: 2.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 122 ISYKQVAEMAECIGSALIQKGFKPCSEqfIGIFSQNRPEWVTIEQGCFTYSMVVVPLYDTLGTDAITYIVNKAElsvifa 201
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDR--VGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSG------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 202 dkpekAKLLLEGvenkltpclkiivimdsydndlvergqkcgveiiglkaledlgrvnrtkpkpPEPEDLAIICFTSGTT 281
Cdd:cd05935 74 -----AKVAVVG----------------------------------------------------SELDDLALIPYTSGTT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 282 GNPKGAMVTHQNIMNDCSGfikaTESAFIASPEDVLISFLPLAHM--FETVVECVMLCHGAKIGFFQGDIRLLMDDLKVL 359
Cdd:cd05935 97 GLPKGCMHTHFSAAANALQ----SAVWTGLTPSDVILACLPLFHVtgFVGSLNTAVYVGGTYVLMARWDRETALELIEKY 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 360 QPTIFPVVPRLLNrmfdrifgqantsvkrwlldfaskrkeaelrsgivrnnslwDKLIFHKIQSSLGGKVRLMITGAAPV 439
Cdd:cd05935 173 KVTFWTNIPTMLV-----------------------------------------DLLATPEFKTRDLSSLKVLTGGGAPM 211
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 440 SATVLTFLRAALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYIKLVDVEDMNYQAAKGEGEVCVKGANVFKG 519
Cdd:cd05935 212 PPAVAEKLLKLTGLRFVEGYGLTETMSQTHTNPPLRPKLQCLGIP*FGVDARVIDIETGRELPPNEVGEIVVRGPQIFKG 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 520 YLKDPARTAEALDKDG---WLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYLRSEAVAQVFV------- 589
Cdd:cd05935 292 YWNRPEETEESFIEIKgrrFFRTGDLGYMDEEGYFFFVDRVKRMINVS-GFKVWPAEVEAKLYKHPAI*EVCVisvpder 370
|
490
....*....|
gi 564389119 590 HGESLQAFLI 599
Cdd:cd05935 371 VGEEVKAFIV 380
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
268-592 |
3.31e-24 |
|
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: 104.87 E-value: 3.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 268 PEDLAIICFTSGTTGNPKGAMVTHQNIMNDcsGFIKATESAFiaSPEDVLISFLPLAHMFETVVECVMLchgakigFFQG 347
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYN--AWMLALNSLF--DPDDVLLCGLPLFHVNGSVVTLLTP-------LASG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 348 DIRLLMDDLKVLQPTIFPVVPRLLNRMfdRIfgQANTSVKRWLLDFASKRKEAELrsgivrnnslwdklifhkiqSSLgg 427
Cdd:cd05944 70 AHVVLAGPAGYRNPGLFDNFWKLVERY--RI--TSLSTVPTVYAALLQVPVNADI--------------------SSL-- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 428 kvRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLSLP-GDWTAGHVGAPMPCNYIKLVDVE-DMNYQ--AA 503
Cdd:cd05944 124 --RFAMSGAAPLPVELRARFEDATGLPVVEGYGLTEATCLVAVNPPdGPKRPGSVGLRLPYARVRIKVLDgVGRLLrdCA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 504 KGE-GEVCVKGANVFKGYLKDpARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSE 582
Cdd:cd05944 202 PDEvGEICVAGPGVFGGYLYT-EGNKNAFVADGWLNTGDLGRLDADGYLFITGRAKDLI-IRGGHNIDPALIEEALLRHP 279
|
330
....*....|
gi 564389119 583 AVAQVFVHGE 592
Cdd:cd05944 280 AVAFAGAVGQ 289
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
266-604 |
3.31e-24 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 107.45 E-value: 3.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 266 PEPEDLAIICFTSGTTGNPKGAMVTHQNIMNDCSGFIKATEsafiASPEDVLISFLPLAHMfetvvecvmlchgakIGFF 345
Cdd:PRK13295 194 PGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLG----LGADDVILMASPMAHQ---------------TGFM 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 346 QGDIRLLMDDLK-VLQPTIFPVvprllnRMFDRI------FGQANTSvkrWLLDFASKRKEAELRSgivrnnslwdklif 418
Cdd:PRK13295 255 YGLMMPVMLGATaVLQDIWDPA------RAAELIrtegvtFTMASTP---FLTDLTRAVKESGRPV-------------- 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 419 hkiqSSLggkvRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTA--GCCLSLPGDWTAGHVGAPMPCNYIKLVDVE 496
Cdd:PRK13295 312 ----SSL----RTFLCAGAPIPGALVERARAALGAKIVSAWGMTENGAvtLTKLDDPDERASTTDGCPLPGVEVRVVDAD 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 497 DMNYQAAKgEGEVCVKGANVFKGYLKDPARTAEalDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIEN 576
Cdd:PRK13295 384 GAPLPAGQ-IGRLQVRGCSNFGGYLKRPQLNGT--DADGWFDTGDLARIDADGYIRISGRSKDVI-IRGGENIPVVEIEA 459
|
330 340 350
....*....|....*....|....*....|.
gi 564389119 577 IYLRSEAVAQVFVHG---ESLQAFLIAIVVP 604
Cdd:PRK13295 460 LLYRHPAIAQVAIVAypdERLGERACAFVVP 490
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
270-611 |
1.16e-23 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 102.41 E-value: 1.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 270 DLAIICFTSGTTGNPKGAMVTHQNIMNDCSGfikaTESAFIASPEDVLISFLPLAHM--FETVVECVMLchGAKIGFFQG 347
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAG----LHSRLGFGGGDSWLLSLPLYHVggLAILVRSLLA--GAELVLLER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 348 DiRLLMDDLKVLQPTIFPVVPRLLNRMFDRifGQANTSVKRwlldfaskrkeaelrsgivrnnslwdklifhkiqsslgg 427
Cdd:cd17630 75 N-QALAEDLAPPGVTHVSLVPTQLQRLLDS--GQGPAALKS--------------------------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 428 kVRLMITGAAPVSAtVLTFLRAALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYIKLVDvedmnyqaakgEG 507
Cdd:cd17630 113 -LRAVLLGGAPIPP-ELLERAADRGIPLYTTYGMTETASQVATKRPDGFGRGGVGVLLPGRELRIVE-----------DG 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 508 EVCVKGANVFKGYLKdpARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAVAQV 587
Cdd:cd17630 180 EIWVGGASLAMGYLR--GQLVPEFNEDGWFTTKDLGELHADGRLTVLGRADNMI-ISGGENIQPEEIEAALAAHPAVRDA 256
|
330 340
....*....|....*....|....*..
gi 564389119 588 FVHG---ESLQAFLIAIVVPDVEILPS 611
Cdd:cd17630 257 FVVGvpdEELGQRPVAVIVGRGPADPA 283
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
267-607 |
1.23e-23 |
|
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: 104.64 E-value: 1.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 267 EPEDLAIICFTSGTTGNPKGAMVTHQNIMNdcsgFIKATESAFIASPEDVLISFLPLAhmFETvveCVM-----LCHGAk 341
Cdd:cd05945 95 DGDDNAYIIFTSGSTGRPKGVQISHDNLVS----FTNWMLSDFPLGPGDVFLNQAPFS--FDL---SVMdlypaLASGA- 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 342 igffqgdirllmddlkvlqpTIFPVvPRLLNRMFDRIF-GQANTSVKRWlldfaskrkeaelrsgiVRNNSLWDKLIFHK 420
Cdd:cd05945 165 --------------------TLVPV-PRDATADPKQLFrFLAEHGITVW-----------------VSTPSFAAMCLLSP 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 421 --IQSSLGGKVRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCL------------SLPgdwtaghVGAPMP 486
Cdd:cd05945 207 tfTPESLPSLRHFLFCGEVLPHKTARALQQRFPDARIYNTYGPTEATVAVTYievtpevldgydRLP-------IGYAKP 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 487 CNYIKLVDvEDMNYQAAKGEGEVCVKGANVFKGYLKDPARTAEALDKD---GWLHTGDIGKWLPNGTLKIIDRKKHIFKL 563
Cdd:cd05945 280 GAKLVILD-EDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDegqRAYRTGDLVRLEADGLLFYRGRLDFQVKL 358
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 564389119 564 aQGEYIAPEKIENIYLRSEAVAQVFV----HGESLQAfLIAIVVPDVE 607
Cdd:cd05945 359 -NGYRIELEEIEAALRQVPGVKEAVVvpkyKGEKVTE-LIAFVVPKPG 404
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
232-608 |
1.56e-23 |
|
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: 104.59 E-value: 1.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 232 DNDLVERGQKCGVEIIGLKALEDLGRVNrtkPKPP-EPEDLAIICFTSGTTGNPKGAMVTHQNIMNdcsgfiKATESAFI 310
Cdd:cd12117 101 DRSLAGRAGGLEVAVVIDEALDAGPAGN---PAVPvSPDDLAYVMYTSGSTGRPKGVAVTHRGVVR------LVKNTNYV 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 311 A-SPEDVLISFLPL---AHMFETVVEcvmLCHGAKIgffqgdirllmddlkVLQPtifpvvprllnrmfdrifgqantsv 386
Cdd:cd12117 172 TlGPDDRVLQTSPLafdASTFEIWGA---LLNGARL---------------VLAP------------------------- 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 387 KRWLLDFAskrkeaELRSGIVRN--NSLWdkLI---FHKI----QSSLGGkVRLMITGAAPVS-ATVLTFLRAALGCQFY 456
Cdd:cd12117 209 KGTLLDPD------ALGALIAEEgvTVLW--LTaalFNQLadedPECFAG-LRELLTGGEVVSpPHVRRVLAACPGLRLV 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 457 EGYGQTECT--AGCCLSLPGDWTAGHV--GAPMPCNYIKLVDvEDMNYQAAKGEGEVCVKGANVFKGYLKDPARTAEALD 532
Cdd:cd12117 280 NGYGPTENTtfTTSHVVTELDEVAGSIpiGRPIANTRVYVLD-EDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFV 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 533 KDGWL------HTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSEAVAQVFV---HGESLQAFLIAIVV 603
Cdd:cd12117 359 ADPFGpgerlyRTGDLARWLPDGRLEFLGRIDDQVKI-RGFRIELGEIEAALRAHPGVREAVVvvrEDAGGDKRLVAYVV 437
|
....*
gi 564389119 604 PDVEI 608
Cdd:cd12117 438 AEGAL 442
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
265-618 |
3.64e-23 |
|
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: 103.58 E-value: 3.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 265 PPEPEDLAIICFTSGTTGNPKGAMVTHQNIMNdcsgFIKATESAFIASPEDVLISFLPLAhmFETVVECVM--LCHGAKI 342
Cdd:cd17651 132 ALDADDLAYVIYTSGSTGRPKGVVMPHRSLAN----LVAWQARASSLGPGARTLQFAGLG--FDVSVQEIFstLCAGATL 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 343 GFFQGDIRllMDDLKVLqptifpvvpRLLNRM-FDRIFgqANTSVKRWLLdfaskrkeAELRSGIVRNNSLwdklifhki 421
Cdd:cd17651 206 VLPPEEVR--TDPPALA---------AWLDEQrISRVF--LPTVALRALA--------EHGRPLGVRLAAL--------- 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 422 qsslggkvRLMITGAAPVSATVLT--FLRAALGCQFYEGYGQTECTAGCCLSLPGD---WTA-GHVGAPMPCNYIKLVDv 495
Cdd:cd17651 256 --------RYLLTGGEQLVLTEDLreFCAGLPGLRLHNHYGPTETHVVTALSLPGDpaaWPApPPIGRPIDNTRVYVLD- 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 496 EDMNyQAAKG-EGEVCVKGANVFKGYLKDPARTAEALDKDGWL------HTGDIGKWLPNGTLKIIDRKKHIFKLaQGEY 568
Cdd:cd17651 327 AALR-PVPPGvPGELYIGGAGLARGYLNRPELTAERFVPDPFVpgarmyRTGDLARWLPDGELEFLGRADDQVKI-RGFR 404
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 564389119 569 IAPEKIENIYLRSEAVAQ--VFVHGE-SLQAFLIAIVVPDVEILPSWAQKRGF 618
Cdd:cd17651 405 IELGEIEAALARHPGVREavVLAREDrPGEKRLVAYVVGDPEAPVDAAELRAA 457
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
123-683 |
2.42e-22 |
|
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.
Pssm-ID: 341276 [Multi-domain] Cd Length: 428 Bit Score: 100.49 E-value: 2.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 123 SYKQVAEMAECIGSALIQKGFKpcSEQFIGIFSQNRPEWVTIEQGCFTYSMVVVPLYDTLGTDAITYIVNKAELSVIFAD 202
Cdd:cd05972 2 SFRELKRESAKAANVLAKLGLR--KGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 203 KpekaklllegvenkltpclkiivimdsydndlvergqkcgveiiglkaledlgrvnrtkpkppepEDLAIICFTSGTTG 282
Cdd:cd05972 80 A-----------------------------------------------------------------EDPALIYFTSGTTG 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 283 NPKGAMVTHQNIMndcsGFIKATESAFIASPEDV-------------LISFL-PLAHMFetvveCVMLCHGAKIgffqgD 348
Cdd:cd05972 95 LPKGVLHTHSYPL----GHIPTAAYWLGLRPDDIhwniadpgwakgaWSSFFgPWLLGA-----TVFVYEGPRF-----D 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 349 IRLLMDDLKVLQPTIFPVVPrllnrmfdrifgqanTSVKRWLldfaskrkeAELRSGIVRnnslwdklifhkiqsslgGK 428
Cdd:cd05972 161 AERILELLERYGVTSFCGPP---------------TAYRMLI---------KQDLSSYKF------------------SH 198
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 429 VRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYIKLVDvEDMNYQAAKGEGE 508
Cdd:cd05972 199 LRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDVAIID-DDGRELPPGEEGD 277
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 509 VCVKGANV--FKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYLRSEAVAQ 586
Cdd:cd05972 278 IAIKLPPPglFLGYVGDPEKTEASI-RGDYYLTGDRAYRDEDGYFWFVGRADDIIK-SSGYRIGPFEVESALLEHPAVAE 355
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 587 VFV-------HGESLQAFLIAivvpdveilpswaqKRGFQGSfEELcrnkdinkaiLEDMVKLGKNAgLKPFEQVKGIAV 659
Cdd:cd05972 356 AAVvgspdpvRGEVVKAFVVL--------------TSGYEPS-EEL----------AEELQGHVKKV-LAPYKYPREIEF 409
|
570 580
....*....|....*....|....
gi 564389119 660 HPELfsidngLLTPTLKAKRPELR 683
Cdd:cd05972 410 VEEL------PKTISGKIRRVELR 427
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
122-591 |
5.40e-22 |
|
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: 99.89 E-value: 5.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 122 ISYKQVAEMAECIGSALIQKGFKPcsEQFIGIFSQNRPEWVTIEQGCFTYSMVVVPLYDTLGTDAITYIVNKAEL-SVIF 200
Cdd:cd05923 29 LTYSELRARIEAVAARLHARGLRP--GQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEMtAAVI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 201 ADkpekAKLLLEGvenkltpclkiivimdsyDNDLVERGQKCGVEIiGLKALEDLGRVnrTKPKPPEPEDLAIICFTSGT 280
Cdd:cd05923 107 AV----DAQVMDA------------------IFQSGVRVLALSDLV-GLGEPESAGPL--IEDPPREPEQPAFVFYTSGT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 281 TGNPKGAMVTHQNIMNDCSgFIkATESAFIASPEDVLISFLPLAHMfetvvecvmlchgakIGFFQgdirLLMDDLkVLQ 360
Cdd:cd05923 162 TGLPKGAVIPQRAAESRVL-FM-STQAGLRHGRHNVVLGLMPLYHV---------------IGFFA----VLVAAL-ALD 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 361 PTIFPVvprllnRMFDRIFgqantsvkrwlldfASKRKEAELRSGIVRNNSLWDKLIFHKIQSSLGGK-VRLMITGAAPV 439
Cdd:cd05923 220 GTYVVV------EEFDPAD--------------ALKLIEQERVTSLFATPTHLDALAAAAEFAGLKLSsLRHVTFAGATM 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 440 SATVLTFLRAALGCQFYEGYGQTEctAGCCLSLPgDWTAGHVGAPMPCNYIKLVDV-EDMNYQAAKG-EGEVCVK--GAN 515
Cdd:cd05923 280 PDAVLERVNQHLPGEKVNIYGTTE--AMNSLYMR-DARTGTEMRPGFFSEVRIVRIgGSPDEALANGeEGELIVAaaADA 356
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564389119 516 VFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAVAQVFVHG 591
Cdd:cd05923 357 AFTGYLNQPEATAKKL-QDGWYRTGDVGYVDPSGDVRILGRVDDMI-ISGGENIHPSEIERVLSRHPGVTEVVVIG 430
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
267-618 |
8.16e-22 |
|
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: 99.05 E-value: 8.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 267 EPEDLAIICFTSGTTGNPKGAMVTHQNIMNDCSGFIKATesaFIASPEDVLIsFLPLAhmFETVVE--CVMLCHGAKIgf 344
Cdd:cd17644 104 QPENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEY---GITSSDRVLQ-FASIA--FDVAAEeiYVTLLSGATL-- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 345 fqgdirllmddlkVLQPtifpvvprllNRMFdrifgqantsvkRWLLDFASKRKEAELRsgiVRN--NSLWDKLIFHKIQ 422
Cdd:cd17644 176 -------------VLRP----------EEMR------------SSLEDFVQYIQQWQLT---VLSlpPAYWHLLVLELLL 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 423 SSLGG--KVRLMITGAAPVSATVLTFLRAALG--CQFYEGYGQTECTAGCCLSLPGDWTAGH-----VGAPMPC------ 487
Cdd:cd17644 218 STIDLpsSLRLVIVGGEAVQPELVRQWQKNVGnfIQLINVYGPTEATIAATVCRLTQLTERNitsvpIGRPIANtqvyil 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 488 -NYIKLVDVEDMnyqaakgeGEVCVKGANVFKGYLKDPARTAEALDKDGWLH--------TGDIGKWLPNGTLKIIDRKK 558
Cdd:cd17644 298 dENLQPVPVGVP--------GELHIGGVGLARGYLNRPELTAEKFISHPFNSseserlykTGDLARYLPDGNIEYLGRID 369
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564389119 559 HIFKLaQGEYIAPEKIENIYLRSEAVAQVFV---HGESLQAFLIAIVVPDVEILPSWAQKRGF 618
Cdd:cd17644 370 NQVKI-RGFRIELGEIEAVLSQHNDVKTAVVivrEDQPGNKRLVAYIVPHYEESPSTVELRQF 431
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
267-605 |
8.86e-22 |
|
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: 98.92 E-value: 8.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 267 EPEDLAIICFTSGTTGNPKGAMVTHQNImndcSGFIKATESAFIASPEDVLISFLPLAHMFeTVVEcvM---LCHGAKIG 343
Cdd:cd17643 91 DPDDLAYVIYTSGSTGRPKGVVVSHANV----LALFAATQRWFGFNEDDVWTLFHSYAFDF-SVWE--IwgaLLHGGRLV 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 344 FFQGDIRLLMDDLkvlqptifpvvPRLLNRMFDRIFGQANTSVKRWLldfaskrkEAELRsgivrnnslwdkliFHKIQS 423
Cdd:cd17643 164 VVPYEVARSPEDF-----------ARLLRDEGVTVLNQTPSAFYQLV--------EAADR--------------DGRDPL 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 424 SLggkvRLMITGAAPVSATVLTFLRAALGC---QFYEGYGQTECTAGCCL------SLPGDwTAGHVGAPMPCNYIKLVD 494
Cdd:cd17643 211 AL----RYVIFGGEALEAAMLRPWAGRFGLdrpQLVNMYGITETTVHVTFrpldaaDLPAA-AASPIGRPLPGLRVYVLD 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 495 vEDMNYQAAKGEGEVCVKGANVFKGYLKDPARTAE-------ALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGE 567
Cdd:cd17643 286 -ADGRPVPPGVVGELYVSGAGVARGYLGRPELTAErfvanpfGGPGSRMYRTGDLARRLPDGELEYLGRADEQVKI-RGF 363
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 564389119 568 YIAPEKIENIYLRSEAVAQVFV---HGESLQAFLIAIVVPD 605
Cdd:cd17643 364 RIELGEIEAALATHPSVRDAAVivrEDEPGDTRLVAYVVAD 404
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
122-611 |
1.19e-21 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 99.19 E-value: 1.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 122 ISYKQVAEMAECIGSALIQKGFKPCSEqfIGIFSQNRPEWVTIEQGCFTYSMVVVPLYDTLGTDAITYIVNKAELSVIFA 201
Cdd:PRK05852 44 ISYRDLARLVDDLAGQLTRSGLLPGDR--VALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLI 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 202 DKpekaklllEGVENKLTPCLKIIVIMDSYDNDlveRGQKCGVEIIGLKALEDLGRVNRTkPKPPEPEDlAIICFTSGTT 281
Cdd:PRK05852 122 DA--------DGPHDRAEPTTRWWPLTVNVGGD---SGPSGGTLSVHLDAATEPTPATST-PEGLRPDD-AMIMFTGGTT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 282 GNPKGAMVTHQNImndcSGFIKATESAFIASPEDVLISFLPLAHMFETVVECV-MLCHGAKI-----GFFQGdiRLLMDD 355
Cdd:PRK05852 189 GLPKMVPWTHANI----ASSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALLaTLASGGAVllparGRFSA--HTFWDD 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 356 LKVLQPTIFPVVPRLLNRMFDRifgqANTSvkrwlldfASKRKEAELRsgIVRNNSlwdklifhkiqsslggkvrlmitg 435
Cdd:PRK05852 263 IKAVGATWYTAVPTIHQILLER----AATE--------PSGRKPAALR--FIRSCS------------------------ 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 436 aAPVSATVLTFLRAALGCQFYEGYGQTECT---------AGCCLSLPGDWT--AGHVGAPMpcnyIKLVDVEDMNYQAAK 504
Cdd:PRK05852 305 -APLTAETAQALQTEFAAPVVCAFGMTEAThqvtttqieGIGQTENPVVSTglVGRSTGAQ----IRIVGSDGLPLPAGA 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 505 gEGEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYLRSEAV 584
Cdd:PRK05852 380 -VGEVWLRGTTVVRGYLGDPTITAANF-TDGWLRTGDLGSLSAAGDLSIRGRIKELINRG-GEKISPERVEGVLASHPNV 456
|
490 500 510
....*....|....*....|....*....|
gi 564389119 585 AQVFVHGESLQAF---LIAIVVPDVEILPS 611
Cdd:PRK05852 457 MEAAVFGVPDQLYgeaVAAVIVPRESAPPT 486
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
270-607 |
1.25e-21 |
|
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: 96.57 E-value: 1.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 270 DLAIICFTSGTTGNPKGAMVTHQNIMndCSGFikATESAFIASPEDVLISFLPLAHMFETVVECVMLCHGAK---IGFFQ 346
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLI--AANL--QLIHAMGLTEADVYLNMLPLFHIAGLNLALATFHAGGAnvvMEKFD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 347 GDIRL-LMDDLKVlqpTIFPVVPRLLNRMFDRIfgqantsvkrwlldfasKRKEAELRSgiVRNnslwdklifhkiqssl 425
Cdd:cd17637 77 PAEALeLIEEEKV---TLMGSFPPILSNLLDAA-----------------EKSGVDLSS--LRH---------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 426 ggkvrlmITGA-APvsATVLTFLrAALGCQFYEGYGQTECTAGCCLSlPGDWTAGHVGAPMPCNYIKLVDVEDMnyQAAK 504
Cdd:cd17637 119 -------VLGLdAP--ETIQRFE-ETTGATFWSLYGQTETSGLVTLS-PYRERPGSAGRPGPLVRVRIVDDNDR--PVPA 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 505 GE-GEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRK--KHIFKlAQGEYIAPEKIENIYLRS 581
Cdd:cd17637 186 GEtGEIVVRGPLVFQGYWNLPELTAYTF-RNGWHHTGDLGRFDEDGYLWYAGRKpeKELIK-PGGENVYPAEVEKVILEH 263
|
330 340
....*....|....*....|....*.
gi 564389119 582 EAVAQVFVHGeslqafliaivVPDVE 607
Cdd:cd17637 264 PAIAEVCVIG-----------VPDPK 278
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
251-600 |
1.39e-21 |
|
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: 99.06 E-value: 1.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 251 ALEDLGRVNRTKPKP-PEPEDLAIICFTSGTTGNPKGAMVTHqnimND--CSgfikATESAFIA--SPEDVLISFLPLAH 325
Cdd:COG1021 165 SLDALLAAPADLSEPrPDPDDVAFFQLSGGTTGLPKLIPRTH----DDylYS----VRASAEICglDADTVYLAALPAAH 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 326 MFETVVECVM--LCHGAKIgffqgdirllmddlkVLQP-----TIFP-----------VVPRLLNRMfdrifgqantsvk 387
Cdd:COG1021 237 NFPLSSPGVLgvLYAGGTV---------------VLAPdpspdTAFPlierervtvtaLVPPLALLW------------- 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 388 rwlLDFASKRKeAELrsgivrnnslwdklifhkiqSSLggkvRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTEctaG 467
Cdd:COG1021 289 ---LDAAERSR-YDL--------------------SSL----RVLQVGGAKLSPELARRVRPALGCTLQQVFGMAE---G 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 468 --CCLSL--PGDWTAGHVGAPM-PCNYIKLVDVEDMnyQAAKGE-GEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGD 541
Cdd:COG1021 338 lvNYTRLddPEEVILTTQGRPIsPDDEVRIVDEDGN--PVPPGEvGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGD 415
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564389119 542 IGKWLPNGTLKIIDRKK-HIFKlaQGEYIAPEKIENIYLRSEAVAQVFV-------HGESLQAFLIA 600
Cdd:COG1021 416 LVRRTPDGYLVVEGRAKdQINR--GGEKIAAEEVENLLLAHPAVHDAAVvampdeyLGERSCAFVVP 480
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
267-618 |
1.47e-21 |
|
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: 98.31 E-value: 1.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 267 EPEDLAIICFTSGTTGNPKGAMVTHQNIMNDCSGFIKatESAFIASPEDVL----ISFLPLAHMFetvveCVMLCHGAKI 342
Cdd:cd17650 91 QPEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWRR--EYELDSFPVRLLqmasFSFDVFAGDF-----ARSLLNGGTL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 343 GFFQGDIRL----LMDDLKVLQPTIFPVVPRLLnrmfdrifgqantsvkRWLLDFASKRKE--AELRSGIVRNNSLWDKL 416
Cdd:cd17650 164 VICPDEVKLdpaaLYDLILKSRITLMESTPALI----------------RPVMAYVYRNGLdlSAMRLLIVGSDGCKAQD 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 417 iFHKIQSSLGGKVRLmITGAAPVSATVLTflraalgcQFYEGYGQTECTAGcclSLPgdwtaghVGAPMPCNYIKLVDvE 496
Cdd:cd17650 228 -FKTLAARFGQGMRI-INSYGVTEATIDS--------TYYEEGRDPLGDSA---NVP-------IGRPLPNTAMYVLD-E 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 497 DMNYQAAKGEGEVCVKGANVFKGYLKDPARTAEALDKDGW------LHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIA 570
Cdd:cd17650 287 RLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFapgermYRTGDLARWRADGNVELLGRVDHQVKI-RGFRIE 365
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 564389119 571 PEKIENIYLRSEAVAQVFV---HGESLQAFLIAIVVPDVEilPSWAQKRGF 618
Cdd:cd17650 366 LGEIESQLARHPAIDEAVVavrEDKGGEARLCAYVVAAAT--LNTAELRAF 414
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
113-607 |
1.80e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 98.88 E-value: 1.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 113 RKPNQPYEW-----ISYKQVAEMAECIGSALIQK-GFKPCSEqfIGIFSQNRPEWVTIEQGCFTYSMVVVPLYDTLGTDA 186
Cdd:PRK08314 22 RYPDKTAIVfygraISYRELLEEAERLAGYLQQEcGVRKGDR--VLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 187 ITYIVNKAELSVIFAdkpekAKLLLEGVE--NKLTPCLKIIVIM--DSYDND--------LVERGQKCGVEIIGLKALED 254
Cdd:PRK08314 100 LAHYVTDSGARVAIV-----GSELAPKVApaVGNLRLRHVIVAQysDYLPAEpeiavpawLRAEPPLQALAPGGVVAWKE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 255 -LGRVNRTKPKPPEPEDLAIICFTSGTTGNPKGAMVTHQNIMNDCSGFIKATESafiaSPEDVLISFLPLAHMfeTVVEC 333
Cdd:PRK08314 175 aLAAGLAPPPHTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNS----TPESVVLAVLPLFHV--TGMVH 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 334 VMlcHGAkigFFQGDIRLLMddlkvlqptifP-----VVPRLLNRMfdRIFGQANTSVKrwLLDF-ASKR-KEAELRsgi 406
Cdd:PRK08314 249 SM--NAP---IYAGATVVLM-----------PrwdreAAARLIERY--RVTHWTNIPTM--VVDFlASPGlAERDLS--- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 407 vrnnSLWdklifhkiqsSLGGkvrlmitGAAPVSATVLTFLRAALGCQFYEGYGQTECTAG-----------CCLSLPGD 475
Cdd:PRK08314 306 ----SLR----------YIGG-------GGAAMPEAVAERLKELTGLDYVEGYGLTETMAQthsnppdrpklQCLGIPTF 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 476 WTAGHV-----GAPMPCNyiklvdvedmnyqaakGEGEVCVKGANVFKGYLKDPARTAEA---LDKDGWLHTGDIGKWLP 547
Cdd:PRK08314 365 GVDARVidpetLEELPPG----------------EVGEIVVHGPQVFKGYWNRPEATAEAfieIDGKRFFRTGDLGRMDE 428
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564389119 548 NGTLKIIDRKKHIFKlAQGEYIAPEKIENIYLRSEAVAQVFV-------HGESLQAFliaiVVPDVE 607
Cdd:PRK08314 429 EGYFFITDRLKRMIN-ASGFKVWPAEVENLLYKHPAIQEACViatpdprRGETVKAV----VVLRPE 490
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
122-683 |
3.03e-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: 97.82 E-value: 3.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 122 ISYKQVAEMAECIGSALIQKGFKPcsEQFIGIFSQNRPEWVTIEQGCFTYSMVVVPLYDTLGTDAITYIVNKAELSVIFA 201
Cdd:cd05959 30 LTYAELEAEARRVAGALRALGVKR--EERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 202 DkPEKAKLLLEGVEnKLTPCLKIIVIMDSYDNdlvERGQKCGVEIIGlkALEDLGrvnrtKPKPPEPEDLAIICFTSGTT 281
Cdd:cd05959 108 S-GELAPVLAAALT-KSEHTLVVLIVSGGAGP---EAGALLLAELVA--AEAEQL-----KPAATHADDPAFWLYSSGST 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 282 GNPKGAMVTHQNIMNDCSGFIKATesaFIASPEDVLISFLPLAHMFEtvvecvmLCHGAKIGFFQGDIRLLM-------- 353
Cdd:cd05959 176 GRPKGVVHLHADIYWTAELYARNV---LGIREDDVCFSAAKLFFAYG-------LGNSLTFPLSVGATTVLMperptpaa 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 354 --DDLKVLQPTIFPVVPRLLNRMfdrifgqanTSVKRWlldfaskrkeaelrsgivrnnslwdklifhkiQSSLGGKVRL 431
Cdd:cd05959 246 vfKRIRRYRPTVFFGVPTLYAAM---------LAAPNL--------------------------------PSRDLSSLRL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 432 MITGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYIKLVDvEDMNYQAAKGEGEVCV 511
Cdd:cd05959 285 CVSAGEALPAEVGERWKARFGLDILDGIGSTEMLHIFLSNRPGRVRYGTTGKPVPGYEVELRD-EDGGDVADGEPGELYV 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 512 KGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYLRSEAVAQVFVHG 591
Cdd:cd05959 364 RGPSSATMYWNNRDKTRDTF-QGEWTRTGDKYVRDDDGFYTYAGRADDMLK-VSGIWVSPFEVESALVQHPAVLEAAVVG 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 592 ESLQAFLI---AIVVPdveilpswaqKRGFQGSfeelcrnkdinkAILEDMVKLGKNAGLKPFEQVKGIAVHPELFSidn 668
Cdd:cd05959 442 VEDEDGLTkpkAFVVL----------RPGYEDS------------EALEEELKEFVKDRLAPYKYPRWIVFVDELPK--- 496
|
570
....*....|....*
gi 564389119 669 gllTPTLKAKRPELR 683
Cdd:cd05959 497 ---TATGKIQRFKLR 508
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
267-619 |
4.69e-21 |
|
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: 96.35 E-value: 4.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 267 EPEDLAIICFTSGTTGNPKGAMVTHQNIMndcsGFIKATESAFIASPEDVLISFLPlahmfetvvecvmlchgAKIGFFQ 346
Cdd:cd05971 86 GSDDPALIIYTSGTTGPPKGALHAHRVLL----GHLPGVQFPFNLFPRDGDLYWTP-----------------ADWAWIG 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 347 GdirlLMDdlkVLQPTIFPVVPRLLNRM--FDRifGQANTSVKRWLLDFASKRKEAeLRsgIVRnnslwdkliFHKIQSS 424
Cdd:cd05971 145 G----LLD---VLLPSLYFGVPVLAHRMtkFDP--KAALDLMSRYGVTTAFLPPTA-LK--MMR---------QQGEQLK 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 425 LGG-KVRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTA--GCCLSLpGDWTAGHVGAPMPCNYIKLVDVEDMNyQ 501
Cdd:cd05971 204 HAQvKLRAIATGGESLGEELLGWAREQFGVEVNEFYGQTECNLviGNCSAL-FPIKPGSMGKPIPGHRVAIVDDNGTP-L 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 502 AAKGEGEVCVK--GANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYL 579
Cdd:cd05971 282 PPGEVGEIAVElpDPVAFLGYWNNPSATEKKM-AGDWLLTGDLGRKDSDGYFWYVGRDDDVITSS-GYRIGPAEIEECLL 359
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 564389119 580 RSEAVAQVFV-------HGESLQAFliaiVVPDVEILPSWAQKRGFQ 619
Cdd:cd05971 360 KHPAVLMAAVvgipdpiRGEIVKAF----VVLNPGETPSDALAREIQ 402
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
194-577 |
1.05e-20 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 97.73 E-value: 1.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 194 AELSVIFADKP--EKAKL--LLEGVENKLtpclKIIVIMDsydndlVERGQKCGVEIIGLKAledlGRVNRTKPKPPEPE 269
Cdd:PRK06814 728 AQVKTVLTSRAfiEKARLgpLIEALEFGI----RIIYLED------VRAQIGLADKIKGLLA----GRFPLVYFCNRDPD 793
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 270 DLAIICFTSGTTGNPKGAMVTHQNIMNDCsgfikATESAFI-ASPEDVLISFLPLAHMFetvvecvmlchgakiGFFQGD 348
Cdd:PRK06814 794 DPAVILFTSGSEGTPKGVVLSHRNLLANR-----AQVAARIdFSPEDKVFNALPVFHSF---------------GLTGGL 853
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 349 IRLLMDDLKVL---QPTIFPVVPRLlnrmfdrIFGQANT---SVKRWLLDFASKRKEAELRSgivrnnslwdklifhkiq 422
Cdd:PRK06814 854 VLPLLSGVKVFlypSPLHYRIIPEL-------IYDTNATilfGTDTFLNGYARYAHPYDFRS------------------ 908
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 423 sslggkVRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYIKLVDVEDMNyqa 502
Cdd:PRK06814 909 ------LRYVFAGAEKVKEETRQTWMEKFGIRILEGYGVTETAPVIALNTPMHNKAGTVGRLLPGIEYRLEPVPGID--- 979
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564389119 503 aKGeGEVCVKGANVFKGYLK-DPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENI 577
Cdd:PRK06814 980 -EG-GRLFVRGPNVMLGYLRaENPGVLEPP-ADGWYDTGDIVTIDEEGFITIKGRAKRFAKIA-GEMISLAAVEEL 1051
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
265-599 |
1.39e-20 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 95.90 E-value: 1.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 265 PPEPEDLAIICFTSGTTGNPKGAMVTHQNIMndCSGFIKATESAFIASpeDVLISFLPLAHM-FETVVECVMLCHGAKIG 343
Cdd:PRK08008 169 PLSTDDTAEILFTSGTTSRPKGVVITHYNLR--FAGYYSAWQCALRDD--DVYLTVMPAFHIdCQCTAAMAAFSAGATFV 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 344 F--------FQGDIRLLmddlkvlQPTIFPVVPRLLNRMfdrifgqantsvkrwLLDFASKRKeaelrsgivRNNSLWDK 415
Cdd:PRK08008 245 LlekysaraFWGQVCKY-------RATITECIPMMIRTL---------------MVQPPSAND---------RQHCLREV 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 416 LIFhkiqsslggkvrLMITgaapvSATVLTFLRAaLGCQFYEGYGQTECTAGCCLSLPGD---WTAghVGAPMPCNYIKL 492
Cdd:PRK08008 294 MFY------------LNLS-----DQEKDAFEER-FGVRLLTSYGMTETIVGIIGDRPGDkrrWPS--IGRPGFCYEAEI 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 493 VDVEdmNYQAAKGE-GEVCVKGA---NVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEY 568
Cdd:PRK08008 354 RDDH--NRPLPAGEiGEICIKGVpgkTIFKEYYLDPKATAKVLEADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRG-GEN 430
|
330 340 350
....*....|....*....|....*....|....*...
gi 564389119 569 IAPEKIENIYLRSEAVAQVFVHG-------ESLQAFLI 599
Cdd:PRK08008 431 VSCVELENIIATHPKIQDIVVVGikdsirdEAIKAFVV 468
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
268-697 |
4.94e-20 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 94.48 E-value: 4.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 268 PEDLAIICFTSGTTGNPKGAMVTHqnimndcSGFIkaTES-AFIA----SPEDVLISFLPLAHM--FETVVECVML--CH 338
Cdd:PLN02860 171 PDDAVLICFTSGTTGRPKGVTISH-------SALI--VQSlAKIAivgyGEDDVYLHTAPLCHIggLSSALAMLMVgaCH 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 339 GAKIGFfqgDIRLLMDDLKVLQPTIFPVVPRLL------NRMfdRIFGQANTSVKRwLLDFAskrkeaelrsGIVRNNSL 412
Cdd:PLN02860 242 VLLPKF---DAKAALQAIKQHNVTSMITVPAMMadlislTRK--SMTWKVFPSVRK-ILNGG----------GSLSSRLL 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 413 WD-KLIF--HKIQSSLGgkvrlmITGAApvsaTVLTFLRaaLGCQFYEGYGQTECTAGCCLSLPGDWTAGH-VGAPMPCN 488
Cdd:PLN02860 306 PDaKKLFpnAKLFSAYG------MTEAC----SSLTFMT--LHDPTLESPKQTLQTVNQTKSSSVHQPQGVcVGKPAPHV 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 489 YIKL-VDVEDMnyqaakgEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGE 567
Cdd:PLN02860 374 ELKIgLDESSR-------VGRILTRGPHVMLGYWGQNSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIK-TGGE 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 568 YIAPEKIENIYLRSEAVAQVFVHGeSLQAFLIAIVVPDVEILPSW--------AQKRGFQGSFEEL---CRNKdinkail 636
Cdd:PLN02860 446 NVYPEEVEAVLSQHPGVASVVVVG-VPDSRLTEMVVACVRLRDGWiwsdnekeNAKKNLTLSSETLrhhCREK------- 517
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564389119 637 edmvklgknaGLKPFEQVKGIAVHPELFSidnglLTPTLKAKRPELRNYFRSQIDELYSTI 697
Cdd:PLN02860 518 ----------NLSRFKIPKLFVQWRKPFP-----LTTTGKIRRDEVRREVLSHLQSLPSNL 563
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
267-600 |
9.99e-20 |
|
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: 92.52 E-value: 9.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 267 EPEDLAIICFTSGTTGNPKGAMVTHQNIMNDCSGFikATEsAFIASPEDVLISflpLAHMFETVvecvMLCHGAKIGFFQ 346
Cdd:cd05919 89 SADDIAYLLYSSGTTGPPKGVMHAHRDPLLFADAM--ARE-ALGLTPGDRVFS---SAKMFFGY----GLGNSLWFPLAV 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 347 GDIRLLMDD----------LKVLQPTIFPVVPRLLNRMFDrifgQANTSvkrwlldfaskrkEAELRSgivrnnslwdkl 416
Cdd:cd05919 159 GASAVLNPGwptaervlatLARFRPTVLYGVPTFYANLLD----SCAGS-------------PDALRS------------ 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 417 ifhkiqsslggkVRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYIKLVDvE 496
Cdd:cd05919 210 ------------LRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVGHIFLSNRPGAWRLGSTGRPVPGYEIRLVD-E 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 497 DMNYQAAKGEGEVCVKGANVFKGYLKDPaRTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIEN 576
Cdd:cd05919 277 EGHTIPPGEEGDLLVRGPSAAVGYWNNP-EKSRATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVG-GQWVSPVEVES 354
|
330 340 350
....*....|....*....|....*....|.
gi 564389119 577 IYLRSEAVAQVFV------HGES-LQAFLIA 600
Cdd:cd05919 355 LIIQHPAVAEAAVvavpesTGLSrLTAFVVL 385
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
55-606 |
1.97e-19 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 94.07 E-value: 1.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 55 CDLSMQSVEvtgttegvRRSAVLEDDKLLLYYYDDvRTMYDGFQRGIQVSNDGPCLGSRKpnqpyEWISYKQVAEMAECI 134
Cdd:PRK12467 485 GELPLLDAE--------ERARELVRWNAPATEYAP-DCVHQLIEAQARQHPERPALVFGE-----QVLSYAELNRQANRL 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 135 GSALIQKGFKPcsEQFIGIFSQNRPEWVTIEQGCFTYSMVVVPLYDTLGTDAITYIVNKAELSVIFADkPEKAKLLlegv 214
Cdd:PRK12467 551 AHVLIAAGVGP--DVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQ-SHLLAQL---- 623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 215 enkltpclkiivimdsydnDLVErgqkcGVEIIGLKALEDL--GRVNRTKPKPPEPEDLAIICFTSGTTGNPKGAMVTHQ 292
Cdd:PRK12467 624 -------------------PVPA-----GLRSLCLDEPADLlcGYSGHNPEVALDPDNLAYVIYTSGSTGQPKGVAISHG 679
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 293 NIMNdcsgFIKATESAFIASPEDVLISFLPLAHMFETVVECVMLCHGAKIgffqgdirLLMDDLKVLQPTIFpvvprlln 372
Cdd:PRK12467 680 ALAN----YVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATL--------HLLPPDCARDAEAF-------- 739
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 373 rmFDRIFGQANTsvkrwLLDFASkrkeaelrsgivrnnSLWDKLIFHKIQSSLGGKVRLMITGAA-PVSATVLTFlRAAL 451
Cdd:PRK12467 740 --AALMADQGVT-----VLKIVP---------------SHLQALLQASRVALPRPQRALVCGGEAlQVDLLARVR-ALGP 796
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 452 GCQFYEGYGQTECTAGC----CLSLPGDWTAGHVGAPMPCNYIKLVDvEDMNYQAAKGEGEVCVKGANVFKGYLKDPART 527
Cdd:PRK12467 797 GARLINHYGPTETTVGVstyeLSDEERDFGNVPIGQPLANLGLYILD-HYLNPVPVGVVGELYIGGAGLARGYHRRPALT 875
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 528 AEALDKD------GWLH-TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSEAVAQVFV--HGESLQAFL 598
Cdd:PRK12467 876 AERFVPDpfgadgGRLYrTGDLARYRADGVIEYLGRMDHQVKI-RGFRIELGEIEARLLAQPGVREAVVlaQPGDAGLQL 954
|
....*...
gi 564389119 599 IAIVVPDV 606
Cdd:PRK12467 955 VAYLVPAA 962
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
120-589 |
2.46e-19 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 92.13 E-value: 2.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 120 EWISYKQVAEMAECIGSALIQKGFKPCSEqfIGIFSQNRPEWVTIEQGCFTYSMVVVPLYDTLGTDAITYIVNKAELSVI 199
Cdd:PRK06155 45 TRWTYAEAARAAAAAAHALAAAGVKRGDR--VALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 200 FADkpekAKLL--LEGVENKLTPcLKIIVIMDSYDNDLVERGqkcgVEIIGLKALEDlgrvnRTKPKPPEPEDLAIICFT 277
Cdd:PRK06155 123 VVE----AALLaaLEAADPGDLP-LPAVWLLDAPASVSVPAG----WSTAPLPPLDA-----PAPAAAVQPGDTAAILYT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 278 SGTTGNPKGAMVTHQNImndcsgFIKATESAFI--ASPEDVLISFLPLAHMfetvvecvmlchGAKIGFFQGdirLLMDD 355
Cdd:PRK06155 189 SGTTGPSKGVCCPHAQF------YWWGRNSAEDleIGADDVLYTTLPLFHT------------NALNAFFQA---LLAGA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 356 LKVLQPTiFPVvprllNRMFDRIfgQANTSVKRWLLD-----FASKRKEAELRSgivrnnslwdklifHKIQSSLGGKVr 430
Cdd:PRK06155 248 TYVLEPR-FSA-----SGFWPAV--RRHGATVTYLLGamvsiLLSQPARESDRA--------------HRVRVALGPGV- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 431 lmitgaapvSATVLTFLRAALGCQFYEGYGQTECTAGCCLSLPGDwTAGHVGAPMPCNYIKLVDVEDMNYQAakGE-GEV 509
Cdd:PRK06155 305 ---------PAALHAAFRERFGVDLLDGYGSTETNFVIAVTHGSQ-RPGSMGRLAPGFEARVVDEHDQELPD--GEpGEL 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 510 CVKGANVF---KGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYLRSEAVAQ 586
Cdd:PRK06155 373 LLRADEPFafaTGYFGMPEKTVEAW-RNLWFHTGDRVVRDADGWFRFVDRIKDAIR-RRGENISSFEVEQVLLSHPAVAA 450
|
...
gi 564389119 587 VFV 589
Cdd:PRK06155 451 AAV 453
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
122-605 |
3.19e-19 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 93.10 E-value: 3.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 122 ISYKQVAEMAECIGSALIQKGFKPcsEQFIGIFSQNRPEWVTIEQGCFTYSMVVVPLYDTLGTDAITYIVNKAELSVIFA 201
Cdd:PRK12316 2029 LSYAELDSRANRLAHRLRARGVGP--EVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLT 2106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 202 DKPEKAKLLLEGvenkltpclkiivimdsydndlvergqkcGVEIIGLKALEDLGRVNRTKPKPP-EPEDLAIICFTSGT 280
Cdd:PRK12316 2107 QRHLLERLPLPA-----------------------------GVARLPLDRDAEWADYPDTAPAVQlAGENLAYVIYTSGS 2157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 281 TGNPKGAMVTHQNIMNdcsgFIKATESAFIASPEDVLISFLPLAhmFETVVECVM--LCHGAkigffqgdiRLLMDDLKV 358
Cdd:PRK12316 2158 TGLPKGVAVSHGALVA----HCQAAGERYELSPADCELQFMSFS--FDGAHEQWFhpLLNGA---------RVLIRDDEL 2222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 359 LQPtifpvvprllNRMFDRIFGQANTsvkrwLLDFASkrkeaelrsgivrnnSLWDKLIFHKIQSSLGGKVRLMITGAAP 438
Cdd:PRK12316 2223 WDP----------EQLYDEMERHGVT-----ILDFPP---------------VYLQQLAEHAERDGRPPAVRVYCFGGEA 2272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 439 VSATVLTFLRAALGCQF-YEGYGQTECTA-----GCCLSLPGDWTAGHVGAPMPCNYIKLVDvEDMNYQAAKGEGEVCVK 512
Cdd:PRK12316 2273 VPAASLRLAWEALRPVYlFNGYGPTEAVVtpllwKCRPQDPCGAAYVPIGRALGNRRAYILD-ADLNLLAPGMAGELYLG 2351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 513 GANVFKGYLKDPARTAEALDKDGWLH-------TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSEAVA 585
Cdd:PRK12316 2352 GEGLARGYLNRPGLTAERFVPDPFSAsgerlyrTGDLARYRADGVVEYLGRIDHQVKI-RGFRIELGEIEARLQAHPAVR 2430
|
490 500
....*....|....*....|...
gi 564389119 586 QVFV---HGESLQAfLIAIVVPD 605
Cdd:PRK12316 2431 EAVVvaqDGASGKQ-LVAYVVPD 2452
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
120-605 |
3.26e-19 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 91.53 E-value: 3.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 120 EWISYKQVAEMAECIGSALIQKGfkPCSEQFIGIFSQNrPEWVTIEQGCFTYSMVVVPLYDTLGTDA---ITYIVNKAEL 196
Cdd:cd05931 23 ETLTYAELDRRARAIAARLQAVG--KPGDRVLLLAPPG-LDFVAAFLGCLYAGAIAVPLPPPTPGRHaerLAAILADAGP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 197 SVIFADKPEKAKLLLEGVENKLTPCLKIIVImdsydnDLVErgqkcgveiiglkaledLGRVNRTKPKPPEPEDLAIICF 276
Cdd:cd05931 100 RVVLTTAAALAAVRAFAASRPAAGTPRLLVV------DLLP-----------------DTSAADWPPPSPDPDDIAYLQY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 277 TSGTTGNPKGAMVTHQNIMNDCsgfiKATESAFIASPEDVLISFLPLAH-M------FETVV---ECVMLchgAKIGFFQ 346
Cdd:cd05931 157 TSGSTGTPKGVVVTHRNLLANV----RQIRRAYGLDPGDVVVSWLPLYHdMgligglLTPLYsggPSVLM---SPAAFLR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 347 GDIRLLmddlkvlqptifpvvpRLLNRmfdrifGQANTSVKRwllDFA----SKRKEAELRSGIvrnnslwDkLifhkiq 422
Cdd:cd05931 230 RPLRWL----------------RLISR------YRATISAAP---NFAydlcVRRVRDEDLEGL-------D-L------ 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 423 sslgGKVRLMITGAAPVSATVLT-FLRAALGCQF-----YEGYGQTECT----------AGCCLSLPGDWTAGHV----- 481
Cdd:cd05931 271 ----SSWRVALNGAEPVRPATLRrFAEAFAPFGFrpeafRPSYGLAEATlfvsggppgtGPVVLRVDRDALAGRAvavaa 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 482 -----------GAPMPCNYIKLVDVEDMNYQAAKGEGEVCVKGANVFKGYLKDPARTAE------ALDKDGWLHTGDIGk 544
Cdd:cd05931 347 ddpaarelvscGRPLPDQEVRIVDPETGRELPDGEVGEIWVRGPSVASGYWGRPEATAEtfgalaATDEGGWLRTGDLG- 425
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564389119 545 WLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENiylrseAVAQvfVHGESLQAFLIAIVVPD 605
Cdd:cd05931 426 FLHDGELYITGRLKDLIIVR-GRNHYPQDIEA------TAEE--AHPALRPGCVAAFSVPD 477
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
269-577 |
4.34e-19 |
|
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: 89.24 E-value: 4.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 269 EDLAIICFTSGTTGNPKGAMVTHQNIMNDCSGFIKATESAfiaSPEDVLISFLPLAHMFETVVECVMLCHGAKIGFFQGD 348
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNW---VVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 349 IRL--LMDDLKVLQPTIFPVVPRLLNRMfdrifgqantsvkrwLLDFASKRKEAElrsgivrnnslwdklifhkiqsslg 426
Cdd:cd17635 78 TTYksLFKILTTNAVTTTCLVPTLLSKL---------------VSELKSANATVP------------------------- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 427 gKVRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLSLPGDWT-AGHVGAPMPCNYIKLVDVEDMNYQAAkG 505
Cdd:cd17635 118 -SLRLIGYGGSRAIAADVRFIEATGLTNTAQVYGLSETGTALCLPTDDDSIeINAVGRPYPGVDVYLAATDGIAGPSA-S 195
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564389119 506 EGEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENI 577
Cdd:cd17635 196 FGTIWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLGERREDGFLFITGRSSESINCG-GVKIAPDEVERI 265
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
174-591 |
4.39e-19 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 91.38 E-value: 4.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 174 VVVPLYDTLGTDAITYIVNKAELSVIFADkPEKAKLLLEGVENklTPCLKIIVIMDSYDNDLVERGQKCGVEIIGLKALE 253
Cdd:PRK05620 90 VFNPLNKQLMNDQIVHIINHAEDEVIVAD-PRLAEQLGEILKE--CPCVRAVVFIGPSDADSAAAHMPEGIKVYSYEALL 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 254 DlGRvNRTKPKPPEPEDLAI-ICFTSGTTGNPKGAMVTHQNIMNDCSGfIKATESAFIASPEdvliSFL---PLAHmfet 329
Cdd:PRK05620 167 D-GR-STVYDWPELDETTAAaICYSTGTTGAPKGVVYSHRSLYLQSLS-LRTTDSLAVTHGE----SFLccvPIYH---- 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 330 vvecvMLCHGAKIGFFQGDIRLLMDDLKVLQPTIFPVVPRLLNRmfdrifgQANTSvkrwlldfaskrkeaelrsgivrn 409
Cdd:PRK05620 236 -----VLSWGVPLAAFMSGTPLVFPGPDLSAPTLAKIIATAMPR-------VAHGV------------------------ 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 410 NSLWDKLIFHKIQS-----SLggkvRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGA- 483
Cdd:PRK05620 280 PTLWIQLMVHYLKNppermSL----QEIYVGGSAVPPILIKAWEERYGVDVVHVWGMTETSPVGTVARPPSGVSGEARWa 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 484 --------PMPCNYIKLVDVEDMNyQAAKGEGEVCVKGANVFKGYLKDPART----------------AEALDKDGWLHT 539
Cdd:PRK05620 356 yrvsqgrfPASLEYRIVNDGQVME-STDRNEGEIQVRGNWVTASYYHSPTEEgggaastfrgedvedaNDRFTADGWLRT 434
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 564389119 540 GDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYLRSEAVAQVFVHG 591
Cdd:PRK05620 435 GDVGSVTRDGFLTIHDRARDVIR-SGGEWIYSAQLENYIMAAPEVVECAVIG 485
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
186-589 |
5.20e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 91.16 E-value: 5.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 186 AITYIVNKAELSVIFADkPEKAKLLLEGVEnkLTPCLKIIVImdsyDNDLVERGqkcGVEIIGLKALEDLgrVNRTKP-- 263
Cdd:PRK08162 106 SIAFMLRHGEAKVLIVD-TEFAEVAREALA--LLPGPKPLVI----DVDDPEYP---GGRFIGALDYEAF--LASGDPdf 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 264 --KPPEPEDLAI-ICFTSGTTGNPKGaMVTHQN--IMNDCSGFIkatesAFIASPEDVLISFLPLAHmfetvveCVMLCH 338
Cdd:PRK08162 174 awTLPADEWDAIaLNYTSGTTGNPKG-VVYHHRgaYLNALSNIL-----AWGMPKHPVYLWTLPMFH-------CNGWCF 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 339 --------GAKIGFFQGDIRLLMDDLKVLQPTIF---PVVPRLLnrmfdrifgqANTsvkrwlldfaskrkEAELRSGIv 407
Cdd:PRK08162 241 pwtvaaraGTNVCLRKVDPKLIFDLIREHGVTHYcgaPIVLSAL----------INA--------------PAEWRAGI- 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 408 rnnslwdklifhkiqsslGGKVRLMITGAAPVSAtVLTFLRAAlGCQFYEGYGQTEC--TAGCCLSLPGdWTA------- 478
Cdd:PRK08162 296 ------------------DHPVHAMVAGAAPPAA-VIAKMEEI-GFDLTHVYGLTETygPATVCAWQPE-WDAlpldera 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 479 ---GHVGAPMPC-NYIKLVDVEDMNYQAAKGE--GEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLK 552
Cdd:PRK08162 355 qlkARQGVRYPLqEGVTVLDPDTMQPVPADGEtiGEIMFRGNIVMKGYLKNPKATEEAF-AGGWFHTGDLAVLHPDGYIK 433
|
410 420 430
....*....|....*....|....*....|....*..
gi 564389119 553 IIDRKKHIFkLAQGEYIAPEKIENIYLRSEAVAQVFV 589
Cdd:PRK08162 434 IKDRSKDII-ISGGENISSIEVEDVLYRHPAVLVAAV 469
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
169-591 |
5.55e-19 |
|
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: 91.02 E-value: 5.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 169 FTYSM--------VVVPLYDTLGTDAITYIVNKAELSVIFADKpekAKLLLEGVENKLTPC---LKIIVIMDSYDNDLVE 237
Cdd:cd05970 85 FWYSLlalhklgaIAIPATHQLTAKDIVYRIESADIKMIVAIA---EDNIPEEIEKAAPECpskPKLVWVGDPVPEGWID 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 238 RGQKCgveiigLKALEDLGRvnRTKPKPPEPEDLAIICFTSGTTGNPKgaMVTHQNIMndcsgfikatesafiaspedvl 317
Cdd:cd05970 162 FRKLI------KNASPDFER--PTANSYPCGEDILLVYFSSGTTGMPK--MVEHDFTY---------------------- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 318 isflPLAHMFETvvecvMLCHGAKigffQGDIRLLMDDLKVLQPtifpvvprllnrMFDRIFGQANTSVKRWLLDFASKR 397
Cdd:cd05970 210 ----PLGHIVTA-----KYWQNVR----EGGLHLTVADTGWGKA------------VWGKIYGQWIAGAAVFVYDYDKFD 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 398 KEAELRSgIVRNN--------SLWDKLIFHKIQSSLGGKVRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTAgCC 469
Cdd:cd05970 265 PKALLEK-LSKYGvttfcappTIYRFLIREDLSRYDLSSLRYCTTAGEALNPEVFNTFKEKTGIKLMEGFGQTETTL-TI 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 470 LSLPG-DWTAGHVGAPMPCNYIKLVDVEDMNYQAAKgEGEVCVKGAN-----VFKGYLKDPARTAEALdKDGWLHTGDIG 543
Cdd:cd05970 343 ATFPWmEPKPGSMGKPAPGYEIDLIDREGRSCEAGE-EGEIVIRTSKgkpvgLFGGYYKDAEKTAEVW-HDGYYHTGDAA 420
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 564389119 544 KWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYLRSEAVAQVFVHG 591
Cdd:cd05970 421 WMDEDGYLWFVGRTDDLIK-SSGYRIGPFEVESALIQHPAVLECAVTG 467
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
267-614 |
7.92e-19 |
|
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: 89.73 E-value: 7.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 267 EPEDLAIICFTSGTTGNPKGAMVTHQNImndcSGFIKATESAFIASPEDVLISFLPLAhmFETVVECVM--LCHGAkigf 344
Cdd:cd17649 92 HPRQLAYVIYTSGSTGTPKGVAVSHGPL----AAHCQATAERYGLTPGDRELQFASFN--FDGAHEQLLppLICGA---- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 345 fqgdiRLLMDDLKVLQPtifpvvPRLLNRMFDR----IFGQANTSVKRWLLDFASKrkeaelrsgivrnnslwdklifhk 420
Cdd:cd17649 162 -----CVVLRPDELWAS------ADELAEMVRElgvtVLDLPPAYLQQLAEEADRT------------------------ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 421 iQSSLGGKVRLMITGAAPVSAtvlTFLRAALGC--QFYEGYGQTEC--TAGCCLSLPGDWTAGH---VGAPMPCNYIKLV 493
Cdd:cd17649 207 -GDGRPPSLRLYIFGGEALSP---ELLRRWLKApvRLFNAYGPTEAtvTPLVWKCEAGAARAGAsmpIGRPLGGRSAYIL 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 494 DvEDMNYQAAKGEGEVCVKGANVFKGYLKDPARTAEAL--DKDG-----WLHTGDIGKWLPNGTLKIIDRKKHIFKLaQG 566
Cdd:cd17649 283 D-ADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFvpDPFGapgsrLYRTGDLARWRDDGVIEYLGRVDHQVKI-RG 360
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 564389119 567 EYIAPEKIENIYLRSEAVAQVFVHGES--LQAFLIAIVVP-DVEILPSWAQ 614
Cdd:cd17649 361 FRIELGEIEAALLEHPGVREAAVVALDgaGGKQLVAYVVLrAAAAQPELRA 411
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
106-672 |
1.33e-18 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 90.11 E-value: 1.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 106 DGPCLGSRKPNQ-PYEWISYKQVAEMAECIGSALIQKGFKPcsEQFIGIFSQNRPEWVTIEQGCFTYSMVVVPL---YDT 181
Cdd:PRK12582 64 DRPWLAQREPGHgQWRKVTYGEAKRAVDALAQALLDLGLDP--GRPVMILSGNSIEHALMTLAAMQAGVPAAPVspaYSL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 182 LGTD--AITYIVNKAELSVIFADKPEK-----AKLLLEGVEnkltpclkIIVIMDSYDN-------DLVERGQKCGVEii 247
Cdd:PRK12582 142 MSHDhaKLKHLFDLVKPRVVFAQSGAPfaralAALDLLDVT--------VVHVTGPGEGiasiafaDLAATPPTAAVA-- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 248 glKALEDLGrvnrtkpkppePEDLAIICFTSGTTGNPKGAMVTHQNIMndcsGFIKATESAFIASPED---VLISFLPLA 324
Cdd:PRK12582 212 --AAIAAIT-----------PDTVAKYLFTSGSTGMPKAVINTQRMMC----ANIAMQEQLRPREPDPpppVSLDWMPWN 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 325 HMFetvvecvmlchGAKIGFfQGDIR----LLMDDLKVLqPTIFPVVPRLLNRMFDRIFGqaNTSVKRWLLDFASKRKEA 400
Cdd:PRK12582 275 HTM-----------GGNANF-NGLLWgggtLYIDDGKPL-PGMFEETIRNLREISPTVYG--NVPAGYAMLAEAMEKDDA 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 401 ELRSgivrnnslwdkliFHKiqsslggKVRLMITGAAPVSATVLTFLRA----ALGCQ--FYEGYGQTEcTAGccLSLPG 474
Cdd:PRK12582 340 LRRS-------------FFK-------NLRLMAYGGATLSDDLYERMQAlavrTTGHRipFYTGYGATE-TAP--TTTGT 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 475 DWTA---GHVGAPMPCNYIKLVDVEDmNYqaakgegEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWL----P 547
Cdd:PRK12582 397 HWDTervGLIGLPLPGVELKLAPVGD-KY-------EVRVKGPNVTPGYHKDPELTAAAFDEEGFYRLGDAARFVdpddP 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 548 NGTLKIIDRKKHIFKLAQGEYIAPEKieniyLRSEAVA-------QVFVHGESlQAFLIAIVVPDVEILPSWAQKRGfqG 620
Cdd:PRK12582 469 EKGLIFDGRVAEDFKLSTGTWVSVGT-----LRPDAVAacspvihDAVVAGQD-RAFIGLLAWPNPAACRQLAGDPD--A 540
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 564389119 621 SFEELCRNKDINKAILEDMVKLGKNAGlKPFEQVKGIAVHPELFSIDNGLLT 672
Cdd:PRK12582 541 APEDVVKHPAVLAILREGLSAHNAEAG-GSSSRIARALLMTEPPSIDAGEIT 591
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
251-575 |
1.95e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 89.28 E-value: 1.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 251 ALEDLGRVNRTKPKPPEPEDLAIICFTSGTTGNPKGAMVTHQNIMNDCSGFIKATEsafiASPE-DVLISFLPLAH-Mfe 328
Cdd:PRK07768 134 TVADLLAADPIDPVETGEDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAE----FDVEtDVMVSWLPLFHdM-- 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 329 tvvecvmlchgAKIGFFQGDIRLLMDDLKVlQPTIFPVVPRLLNRMFDRIFGqANTSVKRWLLDFASKRkeaeLRSGIVR 408
Cdd:PRK07768 208 -----------GMVGFLTVPMYFGAELVKV-TPMDFLRDPLLWAELISKYRG-TMTAAPNFAYALLARR----LRRQAKP 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 409 NNslWDklifhkiQSSLggkvRLMITGAAPVS-ATVLTFLRA---------ALGCqfyeGYGQTECTAGCCLSLPGD--- 475
Cdd:PRK07768 271 GA--FD-------LSSL----RFALNGAEPIDpADVEDLLDAgarfglrpeAILP----AYGMAEATLAVSFSPCGAglv 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 476 -----------------WTAGHV------GAPMPCNYIKLVDvEDMNYQAAKGEGEVCVKGANVFKGYLkDPARTAEALD 532
Cdd:PRK07768 334 vdevdadllaalrravpATKGNTrrlatlGPPLPGLEVRVVD-EDGQVLPPRGVGVIELRGESVTPGYL-TMDGFIPAQD 411
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 564389119 533 KDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIE 575
Cdd:PRK07768 412 ADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMA-GRNIYPTDIE 453
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
265-591 |
6.32e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 87.79 E-value: 6.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 265 PPEPEDLAIICFTSGTTGNPKGAMVTHQNIMNDCSGFIKAtesAFIASPEDVLISFLPlahMFETVVEcvmlchgakigf 344
Cdd:PRK06178 205 PPALDALAALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAV---AVVGGEDSVFLSFLP---EFWIAGE------------ 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 345 fqgdirllmdDLKVLQPTIF--PVVprLLNRmfdrifgqantsvkrwlldfaskrkeaelrsgivrnnslWDKLIF---- 418
Cdd:PRK06178 267 ----------NFGLLFPLFSgaTLV--LLAR---------------------------------------WDAVAFmaav 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 419 --HKIQSSLG---GKVRLMITGAapVSATVLTFL--------------------RAALGCQFYEG-YGQTEcTAGCclsl 472
Cdd:PRK06178 296 erYRVTRTVMlvdNAVELMDHPR--FAEYDLSSLrqvrvvsfvkklnpdyrqrwRALTGSVLAEAaWGMTE-THTC---- 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 473 pGDWTAG-------------HVGAPMPCNYIKLVDVEDMNYQAAKGEGEVCVKGANVFKGYLKDPARTAEALdKDGWLHT 539
Cdd:PRK06178 369 -DTFTAGfqdddfdllsqpvFVGLPVPGTEFKICDFETGELLPLGAEGEIVVRTPSLLKGYWNKPEATAEAL-RDGWLHT 446
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 564389119 540 GDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSEAVAQVFVHG 591
Cdd:PRK06178 447 GDIGKIDEQGFLHYLGRRKEMLKV-NGMSVFPSEVEALLGQHPAVLGSAVVG 497
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
265-586 |
6.52e-18 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 88.23 E-value: 6.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 265 PPEPEDLAIICFTSGTTGNPKGAMVTHQNIMNDCSGfIKAtesafIA--SPEDVLISFLPLAHMFE-TVVECVMLCHGAK 341
Cdd:PRK08043 361 KQQPEDAALILFTSGSEGHPKGVVHSHKSLLANVEQ-IKT-----IAdfTPNDRFMSALPLFHSFGlTVGLFTPLLTGAE 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 342 IGFFQgdirllmddlkvlQPTIFPVVPRLLnrmFDR----IFGqanTSVkrWLLDFAskrkeaelrsgivRNNSLWDkli 417
Cdd:PRK08043 435 VFLYP-------------SPLHYRIVPELV---YDRnctvLFG---TST--FLGNYA-------------RFANPYD--- 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 418 FHKiqsslggkVRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYIKLVDVED 497
Cdd:PRK08043 478 FAR--------LRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSVPG 549
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 498 MnyqaAKGeGEVCVKGANVFKGYLK--DP-------ARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEY 568
Cdd:PRK08043 550 I----EQG-GRLQLKGPNIMNGYLRveKPgvlevptAENARGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIA-GEM 623
|
330
....*....|....*...
gi 564389119 569 IAPEKIENIYLRSEAVAQ 586
Cdd:PRK08043 624 VSLEMVEQLALGVSPDKQ 641
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
263-605 |
1.40e-17 |
|
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: 86.17 E-value: 1.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 263 PKPPEPEDLAIICFTSGTTGNPKGAMVTHQNIMNDcsgfIKATESAFIASPEDVLISFLPLAH------MFETvvecvmL 336
Cdd:cd12114 120 PVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNT----ILDINRRFAVGPDDRVLALSSLSFdlsvydIFGA------L 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 337 CHGAKIGFFQGDIR----LLMDDLKVLQPTIFPVVPRLLNrMfdrifgqantsvkrwLLDfaskrkeaELRSGIVRNNSL 412
Cdd:cd12114 190 SAGATLVLPDEARRrdpaHWAELIERHGVTLWNSVPALLE-M---------------LLD--------VLEAAQALLPSL 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 413 wdKLIFHK---IQSSLGGKVRLMITGAAPVSatvltflraaLGcqfyegyGQTEctaGCCLS-------LPGDWTAGHVG 482
Cdd:cd12114 246 --RLVLLSgdwIPLDLPARLRALAPDARLIS----------LG-------GATE---ASIWSiyhpideVPPDWRSIPYG 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 483 APMPCNYIKLVDvEDMNYQAAKGEGEVCVKGANVFKGYLKDPARTAEAL--DKDG--WLHTGDIGKWLPNGTLKIIDRKK 558
Cdd:cd12114 304 RPLANQRYRVLD-PRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFvtHPDGerLYRTGDLGRYRPDGTLEFLGRRD 382
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 564389119 559 HIFKLaQGEYIAPEKIENIYLRSEAVAQ--VFVHGESLQAFLIAIVVPD 605
Cdd:cd12114 383 GQVKV-RGYRIELGEIEAALQAHPGVARavVVVLGDPGGKRLAAFVVPD 430
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
174-604 |
1.73e-17 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 86.23 E-value: 1.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 174 VVVPLYDTLGTDAITYIVNKAELSVIFADKpEKAKLLLEGVE----NKLTPCLKIIVImdsYDNDLVERgqkcgveiIGL 249
Cdd:PLN03102 90 VLNPINTRLDATSIAAILRHAKPKILFVDR-SFEPLAREVLHllssEDSNLNLPVIFI---HEIDFPKR--------PSS 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 250 KALEDLGRVNRTKPKPP---------EPEDLAIICFTSGTTGNPKGAMVTHQnimndcsGFIKATESAFIASPEDVLISF 320
Cdd:PLN03102 158 EELDYECLIQRGEPTPSlvarmfriqDEHDPISLNYTSGTTADPKGVVISHR-------GAYLSTLSAIIGWEMGTCPVY 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 321 LPLAHMFEtvvecvmlCHGAKIGF---FQGDIRLLMDdlKVLQPTIFPVVprllnRMFDRIFGQANTSVKRWLLdfaskr 397
Cdd:PLN03102 231 LWTLPMFH--------CNGWTFTWgtaARGGTSVCMR--HVTAPEIYKNI-----EMHNVTHMCCVPTVFNILL------ 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 398 keaelrsgivRNNSLwdklifhkIQSSLGGKVRLMITGAAPVSATVLTFLRaaLGCQFYEGYGQTECTAGCCL------- 470
Cdd:PLN03102 290 ----------KGNSL--------DLSPRSGPVHVLTGGSPPPAALVKKVQR--LGFQVMHAYGLTEATGPVLFcewqdew 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 471 -SLPGDWTAgHVGAPMPCNYIKLVDVEDMNYQA-------AKGEGEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDI 542
Cdd:PLN03102 350 nRLPENQQM-ELKARQGVSILGLADVDVKNKETqesvprdGKTMGEIVIKGSSIMKGYLKNPKATSEAF-KHGWLNTGDV 427
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564389119 543 GKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIylrseavaqVFVHGESLQAFLIAIVVP 604
Cdd:PLN03102 428 GVIHPDGHVEIKDRSKDII-ISGGENISSVEVENV---------LYKYPKVLETAVVAMPHP 479
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
265-605 |
3.37e-17 |
|
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: 85.02 E-value: 3.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 265 PPEPEDLAIICFTSGTTGNPKGAMVTHQNIMNDCSGFikatESAFIASPEDVLISFLPLAhmFETVVECVM--LCHGAKI 342
Cdd:cd17646 134 PPRPDNLAYVIYTSGSTGRPKGVMVTHAGIVNRLLWM----QDEYPLGPGDRVLQKTPLS--FDVSVWELFwpLVAGARL 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 343 GFFQGD-------IRLLMDDLKVlqpTIFPVVPRLLnrmfdRIFGQantsvkrwlldfaskrkeaELRSGivRNNSLwdk 415
Cdd:cd17646 208 VVARPGghrdpayLAALIREHGV---TTCHFVPSML-----RVFLA-------------------EPAAG--SCASL--- 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 416 lifhkiqsslggkvRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTEC----TAGCClslPGDWTAGHV--GAPMPCNY 489
Cdd:cd17646 256 --------------RRVFCSGEALPPELAARFLALPGAELHNLYGPTEAaidvTHWPV---RGPAETPSVpiGRPVPNTR 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 490 IKLVDvEDMNYQAAKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLH------TGDIGKWLPNGTLKIIDRKKHIFKL 563
Cdd:cd17646 319 LYVLD-DALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFGPgsrmyrTGDLARWRPDGALEFLGRSDDQVKI 397
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 564389119 564 aQGEYIAPEKIENIYLRSEAVAQVFV---HGESLQAFLIAIVVPD 605
Cdd:cd17646 398 -RGFRVEPGEIEAALAAHPAVTHAVVvarAAPAGAARLVGYVVPA 441
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
270-600 |
7.95e-17 |
|
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: 83.92 E-value: 7.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 270 DLAIICFTSGTTGNPKGAMVTHqnimNDCSGFIKATESAFIASPEDVLISFLPLAHMFetVVEC-----VMLChGAKIGF 344
Cdd:cd05920 140 EVALFLLSGGTTGTPKLIPRTH----NDYAYNVRASAEVCGLDQDTVYLAVLPAAHNF--PLACpgvlgTLLA-GGRVVL 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 345 FQ----GDIRLLMDDLKVlqpTIFPVVPRLlnrmfdrifgqantsVKRWLlDFASKRKEAElrsgivrnnslwdklifhk 420
Cdd:cd05920 213 APdpspDAAFPLIEREGV---TVTALVPAL---------------VSLWL-DAAASRRADL------------------- 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 421 iqSSLggkvRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTE----CTAgccLSLPGDWTAGHVGAPM-PCNYIKLVDv 495
Cdd:cd05920 255 --SSL----RLLQVGGARLSPALARRVPPVLGCTLQQVFGMAEgllnYTR---LDDPDEVIIHTQGRPMsPDDEIRVVD- 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 496 EDMNYQAAKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIE 575
Cdd:cd05920 325 EEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRG-GEKIAAEEVE 403
|
330 340 350
....*....|....*....|....*....|..
gi 564389119 576 NIYLRSEAVAQVFV-------HGESLQAFLIA 600
Cdd:cd05920 404 NLLLRHPAVHDAAVvampdelLGERSCAFVVL 435
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
267-615 |
8.69e-17 |
|
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: 83.37 E-value: 8.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 267 EPEDLAIICFTSGTTGNPKGAMVTHQNIMNDCSGFikatESAFIASPED-----VLISFLPLA-HMFETvvecvmLCHGA 340
Cdd:cd17645 102 NPDDLAYVIYTSGSTGLPKGVMIEHHNLVNLCEWH----RPYFGVTPADkslvyASFSFDASAwEIFPH------LTAGA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 341 KIGFFQGDIRLLMDDLkvlqptifpvvprllnrmfDRIFGQANTSVKRWLLDFASKRKEAElrsgivrNNSLwdklifhk 420
Cdd:cd17645 172 ALHVVPSERRLDLDAL-------------------NDYFNQEGITISFLPTGAAEQFMQLD-------NQSL-------- 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 421 iqsslggkvRLMITGAAPVSATVLTflraalGCQFYEGYGQTECTAgCCLSLPGDWTAGH--VGAPMPCNYIKLVDvEDM 498
Cdd:cd17645 218 ---------RVLLTGGDKLKKIERK------GYKLVNNYGPTENTV-VATSFEIDKPYANipIGKPIDNTRVYILD-EAL 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 499 NYQAAKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWL------HTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPE 572
Cdd:cd17645 281 QLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVpgermyRTGDLAKFLPDGNIEFLGRLDQQVKI-RGYRIEPG 359
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 564389119 573 KIENIYLRSEAVAQVFV-------HGESLQAFLIAIVVPDVEILPSWAQK 615
Cdd:cd17645 360 EIEPFLMNHPLIELAAVlakedadGRKYLVAYVTAPEEIPHEELREWLKN 409
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
116-584 |
1.19e-16 |
|
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: 83.31 E-value: 1.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 116 NQPYEWISYKQVAEMAECIGSALIQKGFKPCSEQFIGIfsQNRPEWVTIEQGCFTYSMVVVPLydTLGTDaityivnkae 195
Cdd:cd05908 10 DKKEKFVSYRHLREEALGYLGALQELGIKPGQEVVFQI--THNNKFLYLFWACLLGGMIAVPV--SIGSN---------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 196 lsvifadkpEKAKLLLEGVENKLT-PCLkiivimdsydndlvergqkcgveIIGLKALEDLgrvnrtkpkppePEDLAII 274
Cdd:cd05908 76 ---------EEHKLKLNKVWNTLKnPYL-----------------------ITEEEVLCEL------------ADELAFI 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 275 CFTSGTTGNPKGAMVTHQNIMNDCSGFIKATESafiaSPEDVLISFLPLAHMFETVVecvmlCHGAKIgfFQGDIRLLMd 354
Cdd:cd05908 112 QFSSGSTGDPKGVMLTHENLVHNMFAILNSTEW----KTKDRILSWMPLTHDMGLIA-----FHLAPL--IAGMNQYLM- 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 355 dlkvlqPT-IFPVVPRLlnrmfdrifgqantsvkrWLLDfASKRKEAELRSGIVRNNSLWDKLIFHKIQSSLGGKVRLMI 433
Cdd:cd05908 180 ------PTrLFIRRPIL------------------WLKK-ASEHKATIVSSPNFGYKYFLKTLKPEKANDWDLSSIRMIL 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 434 TGAAPVSATVLTFLRAALGC------QFYEGYGQTECTAGCCL----------SLPGDWTAGHVGAPM------------ 485
Cdd:cd05908 235 NGAEPIDYELCHEFLDHMSKyglkrnAILPVYGLAEASVGASLpkaqspfktiTLGRRHVTHGEPEPEvdkkdsecltfv 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 486 ----PCNYIKLVDVEDMNYQAAKGE-GEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGkWLPNGTLKIIDRKKHI 560
Cdd:cd05908 315 evgkPIDETDIRICDEDNKILPDGYiGHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLG-FIRNGRLVITGREKDI 393
|
490 500
....*....|....*....|....
gi 564389119 561 FkLAQGEYIAPEKIENIYLRSEAV 584
Cdd:cd05908 394 I-FVNGQNVYPHDIERIAEELEGV 416
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
267-618 |
6.35e-16 |
|
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).
Pssm-ID: 341307 [Multi-domain] Cd Length: 436 Bit Score: 80.76 E-value: 6.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 267 EPEDLAIICFTSGTTGNPKGAMVTHQNIMNdcsgFIKATESAFIASPEDVLISFLPLAhmFETVV-ECVM-LCHGAkigf 344
Cdd:cd17652 91 TPDNLAYVIYTSGSTGRPKGVVVTHRGLAN----LAAAQIAAFDVGPGSRVLQFASPS--FDASVwELLMaLLAGA---- 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 345 fqgdiRLLMDDLKVLQPtifpvvprllnrmfdrifGQAntsvkrwLLDFaskrkeaelrsgivrnnsLWDKLIFHKIQS- 423
Cdd:cd17652 161 -----TLVLAPAEELLP------------------GEP-------LADL------------------LREHRITHVTLPp 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 424 ---------SLGGKVRLMITGAAPVSATVLtflRAALGCQFYEGYGQTECTAGCCLSLP-GDWTAGHVGAPMPCNYIKLV 493
Cdd:cd17652 193 aalaalppdDLPDLRTLVVAGEACPAELVD---RWAPGRRMINAYGPTETTVCATMAGPlPGGGVPPIGRPVPGTRVYVL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 494 DveDMNYQAAKGE-GEVCVKGANVFKGYLKDPARTAEALDKD------GWLH-TGDIGKWLPNGTLKIIDRKKHIFKLaQ 565
Cdd:cd17652 270 D--ARLRPVPPGVpGELYIAGAGLARGYLNRPGLTAERFVADpfgapgSRMYrTGDLARWRADGQLEFLGRADDQVKI-R 346
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 564389119 566 GEYIAPEKIENIYLRSEAVAQ--VFVHGESL-QAFLIAIVVPDVEILPSWAQKRGF 618
Cdd:cd17652 347 GFRIELGEVEAALTEHPGVAEavVVVRDDRPgDKRLVAYVVPAPGAAPTAAELRAH 402
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
268-627 |
1.37e-15 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 81.54 E-value: 1.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 268 PEDLAIICFTSGTTGNPKGAMVTHQNIMNdcsgFIKATESAFIASPEDVLISFLPLAhmFETVVECVM--LCHGAkigff 345
Cdd:PRK12316 4693 PDNLAYVIYTSGSTGRPKGVAVSHGSLVN----HLHATGERYELTPDDRVLQFMSFS--FDGSHEGLYhpLINGA----- 4761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 346 qgdiRLLMDDLKVLQPTifpvvpRLLNRMfdrifGQANTSVkrwlLDFASkrkeaelrsgivrnnSLWDKLIFHKIQSSL 425
Cdd:PRK12316 4762 ----SVVIRDDSLWDPE------RLYAEI-----HEHRVTV----LVFPP---------------VYLQQLAEHAERDGE 4807
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 426 GGKVRLMITG--AAPVSATVLTFlRAALGCQFYEGYGQTECTAG-CCLSLPGDWTAG----HVGAPMPCNYIKLVDVEdM 498
Cdd:PRK12316 4808 PPSLRVYCFGgeAVAQASYDLAW-RALKPVYLFNGYGPTETTVTvLLWKARDGDACGaaymPIGTPLGNRSGYVLDGQ-L 4885
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 499 NYQAAKGEGEVCVKGANVFKGYLKDPARTAE-----ALDKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAP 571
Cdd:PRK12316 4886 NPLPVGVAGELYLGGEGVARGYLERPALTAErfvpdPFGAPGgrLYRTGDLARYRADGVIDYLGRVDHQVKI-RGFRIEL 4964
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 564389119 572 EKIENIYLRSEAVAQVFVHGE--SLQAFLIAIVVP-DVEILPSWAQKRGFQGSFEELCR 627
Cdd:PRK12316 4965 GEIEARLREHPAVREAVVIAQegAVGKQLVGYVVPqDPALADADEAQAELRDELKAALR 5023
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
458-614 |
1.45e-15 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 78.50 E-value: 1.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 458 GYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYIKLVDVEDMnyQAAKGE-GEVCVKGANVFKGYLKDPARTAEALdKDGW 536
Cdd:cd17636 142 GYGQTEVMGLATFAALGGGAIGGAGRPSPLVQVRILDEDGR--EVPDGEvGEIVARGPTVMAGYWNRPEVNARRT-RGGW 218
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564389119 537 LHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYLRSEAVAQVFVhgeslqafliaIVVPDveilPSWAQ 614
Cdd:cd17636 219 HHTNDLGRREPDGSLSFVGPKTRMIKSG-AENIYPAEVERCLRQHPAVADAAV-----------IGVPD----PRWAQ 280
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
174-591 |
4.27e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 78.39 E-value: 4.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 174 VVVPLYDTLGTDAITYIVNKAelsvifadkpeKAKLLLEGVENKLTPCLKI-IVIMDSYDNDLVERGQKCGVEIiglkal 252
Cdd:PRK06145 78 VFLPINYRLAADEVAYILGDA-----------GAKLLLVDEEFDAIVALETpKIVIDAAAQADSRRLAQGGLEI------ 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 253 edlgrvnrTKPKPPEPEDLAIICFTSGTTGNPKGAMVTHQNIMNDCSGFIkateSAFIASPEDVLISFLPLAHmfetVVE 332
Cdd:PRK06145 141 --------PPQAAVAPTDLVRLMYTSGTTDRPKGVMHSYGNLHWKSIDHV----IALGLTASERLLVVGPLYH----VGA 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 333 C-----VMLCHGAKIGFFQG-DIRLLMDDLKVLQPTIFPVVPRLLNRMF-----DRIfgqaNTSVKRWLLDFASKRKEAE 401
Cdd:PRK06145 205 FdlpgiAVLWVGGTLRIHREfDPEAVLAAIERHRLTCAWMAPVMLSRVLtvpdrDRF----DLDSLAWCIGGGEKTPESR 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 402 LRSgivrnnslwdklifhkiqsslggkvrlmitgaapvsatvltFLRAALGCQFYEGYGQTECTAGCCLSLPGDWTA--G 479
Cdd:PRK06145 281 IRD-----------------------------------------FTRVFTRARYIDAYGLTETCSGDTLMEAGREIEkiG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 480 HVGAPMPCNYIKLVDvEDMNYQAAKGEGEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKH 559
Cdd:PRK06145 320 STGRALAHVEIRIAD-GAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAF-YGDWFRSGDVGYLDEEGFLYLTDRKKD 397
|
410 420 430
....*....|....*....|....*....|..
gi 564389119 560 IFkLAQGEYIAPEKIENIYLRSEAVAQVFVHG 591
Cdd:PRK06145 398 MI-ISGGENIASSEVERVIYELPEVAEAAVIG 428
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
119-598 |
1.40e-14 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 77.19 E-value: 1.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 119 YEWI-SYKQVAEMAecigSALIQKGFKPCSEqfIGIFSQNRPEWVTIEQGCFTYSMVVVPLYDTLGTDAITYIVNKAELS 197
Cdd:PLN02479 46 YTWAqTYQRCRRLA----SALAKRSIGPGST--VAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKSE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 198 VIFADKP------EKAKLLLEGVENKLTPCLKIIVIMDSYDNDLVERGQKCGveiiglkALEDLGRVNRTKP----KPPE 267
Cdd:PLN02479 120 VVMVDQEfftlaeEALKILAEKKKSSFKPPLLIVIGDPTCDPKSLQYALGKG-------AIEYEKFLETGDPefawKPPA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 268 PEDLAI-ICFTSGTTGNPKGAMVTHQnimndcSGFIKATESAFI-ASPED-VLISFLPLAHmfetvveCVMLCHGAKIGF 344
Cdd:PLN02479 193 DEWQSIaLGYTSGTTASPKGVVLHHR------GAYLMALSNALIwGMNEGaVYLWTLPMFH-------CNGWCFTWTLAA 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 345 FQG-DIRLLMDDLKVLQPTI-------FPVVPRLLNRMFdrifgqaNTSVKRWLLdfaskrkeaelrsgivrnnslwdkl 416
Cdd:PLN02479 260 LCGtNICLRQVTAKAIYSAIanygvthFCAAPVVLNTIV-------NAPKSETIL------------------------- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 417 ifhkiqsSLGGKVRLMITGAAPvSATVLtFLRAALGCQFYEGYGQTEcTAG----CCL-----SLPGDwTAGHVGAPMPC 487
Cdd:PLN02479 308 -------PLPRVVHVMTAGAAP-PPSVL-FAMSEKGFRVTHTYGLSE-TYGpstvCAWkpewdSLPPE-EQARLNARQGV 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 488 NYIKL-----VDVEDMNYQAAKGE--GEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHI 560
Cdd:PLN02479 377 RYIGLegldvVDTKTMKPVPADGKtmGEIVMRGNMVMKGYLKNPKANEEAF-ANGWFHSGDLGVKHPDGYIEIKDRSKDI 455
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 564389119 561 FkLAQGEYIAPEKIENIYLRSEAVAQVFV-------HGESLQAFL 598
Cdd:PLN02479 456 I-ISGGENISSLEVENVVYTHPAVLEASVvarpderWGESPCAFV 499
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
266-617 |
1.45e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 78.28 E-value: 1.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 266 PEPEDLAIICFTSGTTGNPKGAMVTHQNIMNdcsgFIKATESAFIASPEDVLISFLPLAhmFETVVECVM--LCHGAKIG 343
Cdd:PRK12467 1715 LAPQNLAYVIYTSGSTGRPKGAGNRHGALVN----RLCATQEAYQLSAADVVLQFTSFA--FDVSVWELFwpLINGARLV 1788
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 344 FFQGDIRL----LMDDLKVLQPTIFPVVPRLLNRmfdriFGQANTSVKRWLldfaskrkeaelrsgivrnnslwdklifh 419
Cdd:PRK12467 1789 IAPPGAHRdpeqLIQLIERQQVTTLHFVPSMLQQ-----LLQMDEQVEHPL----------------------------- 1834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 420 kiqsslggKVRLMITG--AAPVSATVLTFlrAALG-CQFYEGYGQTECTAG-----CCLSLPGDWTAGHVGAPMPCNYIK 491
Cdd:PRK12467 1835 --------SLRRVVCGgeALEVEALRPWL--ERLPdTGLFNLYGPTETAVDvthwtCRRKDLEGRDSVPIGQPIANLSTY 1904
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 492 LVDvEDMNYQAAKGEGEVCVKGANVFKGYLKDPARTAEAL------DKDGWLH-TGDIGKWLPNGTLKIIDRKKHIFKLa 564
Cdd:PRK12467 1905 ILD-ASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFvadpfgTVGSRLYrTGDLARYRADGVIEYLGRIDHQVKI- 1982
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 564389119 565 QGEYIAPEKIENIYLRSEAVAQ--VFVHGESLQAFLIAIVVPDVEILPSWAQKRG 617
Cdd:PRK12467 1983 RGFRIELGEIEARLREQGGVREavVIAQDGANGKQLVAYVVPTDPGLVDDDEAQV 2037
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
267-605 |
1.78e-14 |
|
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: 76.20 E-value: 1.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 267 EPEDLAIICFTSGTTGNPKGAMVTHQNIMNdcsgFIKATESAFiaSPED---VL----ISF-LPLAHMFETvvecvmLCH 338
Cdd:cd12115 103 DPDDLAYVIYTSGSTGRPKGVAIEHRNAAA----FLQWAAAAF--SAEElagVLastsICFdLSVFELFGP------LAT 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 339 GAKIgffqgdirLLMDDlkVLQPTIFPVVPR--LLNRMfdrifgqanTSVKRWLLDfaskrkeaelrsgivrnnslwdkl 416
Cdd:cd12115 171 GGKV--------VLADN--VLALPDLPAAAEvtLINTV---------PSAAAELLR------------------------ 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 417 ifhkiQSSLGGKVRLMITGAAPVSATVLTFLRAAL-GCQFYEGYGQTECT--AGCCLSLPGDWTAGHVGAPMPCNYIKLV 493
Cdd:cd12115 208 -----HDALPASVRVVNLAGEPLPRDLVQRLYARLqVERVVNLYGPSEDTtySTVAPVPPGASGEVSIGRPLANTQAYVL 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 494 DvEDMNYQAAKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWL------HTGDIGKWLPNGTLKIIDRKKHIFKLaQGE 567
Cdd:cd12115 283 D-RALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGpgarlyRTGDLVRWRPDGLLEFLGRADNQVKV-RGF 360
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 564389119 568 YIAPEKIENIYLRSEAVAQ--VFVHGESL-QAFLIAIVVPD 605
Cdd:cd12115 361 RIELGEIEAALRSIPGVREavVVAIGDAAgERRLVAYIVAE 401
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
421-589 |
1.91e-14 |
|
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: 76.07 E-value: 1.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 421 IQSSLGG---KVRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLSlPGD-WTAGHVGAPMPCNYIKLVDVE 496
Cdd:cd05974 191 IQQDLASfdvKLREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVGNS-PGQpVKAGSMGRPLPGYRVALLDPD 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 497 DmnyqAAKGEGEVCV-----KGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAP 571
Cdd:cd05974 270 G----APATEGEVALdlgdtRPVGLMKGYAGDPDKTAHAM-RGGYYRTGDIAMRDEDGYLTYVGRADDVFK-SSDYRISP 343
|
170
....*....|....*...
gi 564389119 572 EKIENIYLRSEAVAQVFV 589
Cdd:cd05974 344 FELESVLIEHPAVAEAAV 361
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
216-619 |
2.78e-14 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 75.68 E-value: 2.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 216 NKLTPCLKIIVIMDSYDNDLVergqkcgveiIGLKALeDLGRVNRTKPKPPEPEDLAIICFTSGTTGNPKGAMVTHQnim 295
Cdd:PRK09029 93 EELLPSLTLDFALVLEGENTF----------SALTSL-HLQLVEGAHAVAWQPQRLATMTLTSGSTGLPKAAVHTAQ--- 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 296 ndcsgfikatesAFIASPEDVL--ISF---------LPLAHmfetvvecV--------MLCHGAKIGFfqGDIRLLMDDL 356
Cdd:PRK09029 159 ------------AHLASAEGVLslMPFtaqdswllsLPLFH--------VsgqgivwrWLYAGATLVV--RDKQPLEQAL 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 357 kvLQPTIFPVVPRLLNRMFDRifGQANTSVKRWLLdfaskrkeaelrsgivrnnslwdklifhkiqsslGGKvrlMItga 436
Cdd:PRK09029 217 --AGCTHASLVPTQLWRLLDN--RSEPLSLKAVLL----------------------------------GGA---AI--- 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 437 apvsATVLTFLRAALGCQFYEGYGQTECTAGCCL----SLPGdwtaghVGAPMPCNYIKLVDvedmnyqaakgeGEVCVK 512
Cdd:PRK09029 253 ----PVELTEQAEQQGIRCWCGYGLTEMASTVCAkradGLAG------VGSPLPGREVKLVD------------GEIWLR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 513 GANVFKGYLKDPARTAeALDKDGWLHTGDIGKWLpNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAVAQVFVhge 592
Cdd:PRK09029 311 GASLALGYWRQGQLVP-LVNDEGWFATRDRGEWQ-NGELTILGRLDNLF-FSGGEGIQPEEIERVINQHPLVQQVFV--- 384
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 564389119 593 slqafliaIVVPDVE------------------ILPSWAQKR--GFQ 619
Cdd:PRK09029 385 --------VPVADAEfgqrpvavvesdseaavvNLAEWLQDKlaRFQ 423
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
276-612 |
2.97e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 75.85 E-value: 2.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 276 FTSGTTGNPKGAMVTHQN----IMNDCSGFIKATesafiaSPEDVLISFLPLAHMfETVVECVMLCHGAKigffqgDIRL 351
Cdd:PRK07470 170 FTSGTTGRPKAAVLTHGQmafvITNHLADLMPGT------TEQDASLVVAPLSHG-AGIHQLCQVARGAA------TVLL 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 352 LMDDLKVlqPTIFPVVPRL-LNRMFdrifgQANTSVKRWLLDFASKRKEaelrsgivrnnslwdklifhkiQSSLggkvR 430
Cdd:PRK07470 237 PSERFDP--AEVWALVERHrVTNLF-----TVPTILKMLVEHPAVDRYD----------------------HSSL----R 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 431 LMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTaGCCLSLP------GDWTAGHVGapmPCNY------IKLVDvEDM 498
Cdd:PRK07470 284 YVIYAGAPMYRADQKRALAKLGKVLVQYFGLGEVT-GNITVLPpalhdaEDGPDARIG---TCGFertgmeVQIQD-DEG 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 499 NYQAAKGEGEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIY 578
Cdd:PRK07470 359 RELPPGETGEICVIGPAVFAGYYNNPEANAKAF-RDGWFRTGDLGHLDARGFLYITGRASDMY-ISGGSNVYPREIEEKL 436
|
330 340 350
....*....|....*....|....*....|....
gi 564389119 579 LRSEAVAQVFVHGeslqafliaivVPDveilPSW 612
Cdd:PRK07470 437 LTHPAVSEVAVLG-----------VPD----PVW 455
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
265-605 |
8.21e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 74.78 E-value: 8.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 265 PPEPEDLAIICFT-SGTTGNPK------GAMVTHQNIMNDCSGFikatesafiaSPEDVLISFLPL--AHMFETVVecvm 335
Cdd:PRK06164 176 RAADPDAGALLFTtSGTTSGPKlvlhrqATLLRHARAIARAYGY----------DPGAVLLAALPFcgVFGFSTLL---- 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 336 lchgakiGFFQGDIRLLMDDLkvlqptiF--PVVPRLL-----------NRMFDRIFGQANTSVkrwllDFASKRkeael 402
Cdd:PRK06164 242 -------GALAGGAPLVCEPV-------FdaARTARALrrhrvthtfgnDEMLRRILDTAGERA-----DFPSAR----- 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 403 rsgivrnnslwdklifhkiqsslggkvRLMITGAAPVSATVLTFLRAAlGCQFYEGYGQTECTA-GCCLSLPGDWTAGHV 481
Cdd:PRK06164 298 ---------------------------LFGFASFAPALGELAALARAR-GVPLTGLYGSSEVQAlVALQPATDPVSVRIE 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 482 --GAPM-PCNYIKLVDVEDMNYQAAKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKK 558
Cdd:PRK06164 350 ggGRPAsPEARVRARDPQDGALLPDGESGEIEIRAPSLMRGYLDNPDATARALTDDGYFRTGDLGYTRGDGQFVYQTRMG 429
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 564389119 559 HIFKLAqGEYIAPEKIENIYLRSEAVAQVFVHGESL--QAFLIAIVVPD 605
Cdd:PRK06164 430 DSLRLG-GFLVNPAEIEHALEALPGVAAAQVVGATRdgKTVPVAFVIPT 477
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
267-577 |
1.64e-13 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 73.70 E-value: 1.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 267 EPEDLAIICFTSGTTGNPKGAMVTHQNIMND---CSGFIKATEsafiaspEDVLISFLPLAHMFetvvecvmlchgakiG 343
Cdd:PRK06334 181 DPEDVAVILFTSGTEKLPKGVPLTHANLLANqraCLKFFSPKE-------DDVMMSFLPPFHAY---------------G 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 344 FFQGDIRLLMDDLkvlqPTIF---PVVPRLLNRMFDR----IFGqaNTSVkrwLLDF---ASKRKEAELRS-------GI 406
Cdd:PRK06334 239 FNSCTLFPLLSGV----PVVFaynPLYPKKIVEMIDEakvtFLG--STPV---FFDYilkTAKKQESCLPSlrfvvigGD 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 407 VRNNSLWDKlifhkiqsslggkvrlmitgaapvsaTVLTFLRAALgcqfYEGYGQTECTAgcCLSLPGDWTAGH---VGA 483
Cdd:PRK06334 310 AFKDSLYQE--------------------------ALKTFPHIQL----RQGYGTTECSP--VITINTVNSPKHescVGM 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 484 PMPCNYIKLVDvEDMNYQAAKGE-GEVCVKGANVFKGYL-KDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIF 561
Cdd:PRK06334 358 PIRGMDVLIVS-EETKVPVSSGEtGLVLTRGTSLFSGYLgEDFGQGFVELGGETWYVTGDLGYVDRHGELFLKGRLSRFV 436
|
330
....*....|....*.
gi 564389119 562 KLAqGEYIAPEKIENI 577
Cdd:PRK06334 437 KIG-AEMVSLEALESI 451
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
151-608 |
2.16e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 73.18 E-value: 2.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 151 IGIFSQNRPEWVTIEQGCFTYSMVVVPLYDTLGTDAITYIVNKAELSVIFADKPEKAklLLEGVENkltpclkiivimds 230
Cdd:PRK07867 57 VGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIAHADCQLVLTESAHAE--LLDGLDP-------------- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 231 ydndlvergqkcGVEIIGLKALE-----DLGRVNRTKPKPPEPEDLAIICFTSGTTGNPKGAMVTHQNIMNdcSGFIKAT 305
Cdd:PRK07867 121 ------------GVRVINVDSPAwadelAAHRDAEPPFRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVAS--AGVMLAQ 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 306 EsaFIASPEDVLISFLPLAHMFETVVE-CVMLCHGAKI---------GFfqgdirllMDDLKVLQPTIFPVVPRLLNrmf 375
Cdd:PRK07867 187 R--FGLGPDDVCYVSMPLFHSNAVMAGwAVALAAGASIalrrkfsasGF--------LPDVRRYGATYANYVGKPLS--- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 376 drifgqantsvkrWLLDFASKRKEAElrsgivrnNSLwdklifhkiqsslggkvRLMI-TGAAPVSatVLTFlRAALGCQ 454
Cdd:PRK07867 254 -------------YVLATPERPDDAD--------NPL-----------------RIVYgNEGAPGD--IARF-ARRFGCV 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 455 FYEGYGQTEctAGCCLSLPGDWTAGHVGAPMPCnyIKLVDVE--------------DMNYQAAKGEgEVCVKGANVFKGY 520
Cdd:PRK07867 293 VVDGFGSTE--GGVAITRTPDTPPGALGPLPPG--VAIVDPDtgtecppaedadgrLLNADEAIGE-LVNTAGPGGFEGY 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 521 LKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSEAVAQVFVHGeslqaflia 600
Cdd:PRK07867 368 YNDPEADAERM-RGGVYWSGDLAYRDADGYAYFAGRLGDWMRV-DGENLGTAPIERILLRYPDATEVAVYA--------- 436
|
....*...
gi 564389119 601 ivVPDVEI 608
Cdd:PRK07867 437 --VPDPVV 442
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
267-610 |
8.70e-13 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 70.89 E-value: 8.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 267 EPEDLAIICFTSGTTGNPKGAMVTHQNIMNDCSGFIkatESAFIASPEDVLISFLPlAHMFETVVE--CVMLCHGAKIGF 344
Cdd:cd17648 92 NSTDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSLS---ERYFGRDNGDEAVLFFS-NYVFDFFVEqmTLALLNGQKLVV 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 345 FQGDIRL-------LMDDLKVlqpTIFPVVPRLLNRM-FDRIfgqanTSVKRWLL---DFASKRkeaelrsgivrnnslw 413
Cdd:cd17648 168 PPDEMRFdpdrfyaYINREKV---TYLSGTPSVLQQYdLARL-----PHLKRVDAageEFTAPV---------------- 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 414 dkliFHKIQSSLGGkvrLMITGAAPVSATVLTFLRaalgcqFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYIklv 493
Cdd:cd17648 224 ----FEKLRSRFAG---LIINAYGPTETTVTNHKR------FFPGDQRFDKSLGRPVRNTKCYVLNDAMKRVPVGAV--- 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 494 dvedmnyqaakgeGEVCVKGANVFKGYLKDPARTAE-------------ALDKDGWLH-TGDIGKWLPNGTLKIIDRKKH 559
Cdd:cd17648 288 -------------GELYLGGDGVARGYLNRPELTAErflpnpfqteqerARGRNARLYkTGDLVRWLPSGELEYLGRNDF 354
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 564389119 560 IFKLaQGEYIAPEKIENIYLRSEAVAQVFV--------HGESLQAFLIAIVVPDVEILP 610
Cdd:cd17648 355 QVKI-RGQRIEPGEVEAALASYPGVRECAVvakedasqAQSRIQKYLVGYYLPEPGHVP 412
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
423-604 |
1.08e-12 |
|
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: 70.87 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 423 SSLggkvRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLSlPGDWTA--GHVGAPMPCNyIKLVDvEDMNY 500
Cdd:cd05929 244 SSL----KRVIHAAAPCPPWVKEQWIDWGGPIIWEYYGGTEGQGLTIIN-GEEWLThpGSVGRAVLGK-VHILD-EDGNE 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 501 QAAKGEGEVCVKGANVFKgYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLR 580
Cdd:cd05929 317 VPPGEIGEVYFANGPGFE-YTNDPEKTAAARNEGGWSTLGDVGYLDEDGYLYLTDRRSDMI-ISGGVNIYPQEIENALIA 394
|
170 180
....*....|....*....|....*..
gi 564389119 581 SEAVAQVFVHG---ESLQAFLIAIVVP 604
Cdd:cd05929 395 HPKVLDAAVVGvpdEELGQRVHAVVQP 421
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
246-576 |
1.30e-12 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 70.70 E-value: 1.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 246 IIGLKALEDLGRVNRTKPKPP---EPEDLAIICFTSGTTGNPKGAMVTHQNimndcsgF---IKATESAF-IASPEDVLI 318
Cdd:PRK09274 148 LWGGTTLATLLRDGAAAPFPMadlAPDDMAAILFTSGSTGTPKGVVYTHGM-------FeaqIEALREDYgIEPGEIDLP 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 319 SFlPLAHMFE------TVVECvmlchgakigffqgdirllMDDLKVLQptifpVVPRllnRMFDRIFGQANTSVkrwlld 392
Cdd:PRK09274 221 TF-PLFALFGpalgmtSVIPD-------------------MDPTRPAT-----VDPA---KLFAAIERYGVTNL------ 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 393 FASKrkeaelrsgivrnnSLWDKLIFHKIQS--SLGGkVRLMITGAAPVSATVLTFLRAAL--GCQFYEGYGQTEC---- 464
Cdd:PRK09274 267 FGSP--------------ALLERLGRYGEANgiKLPS-LRRVISAGAPVPIAVIERFRAMLppDAEILTPYGATEAlpis 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 465 --TAGCCLSLPGDWT---AGH-VGAPMPCNYIKLVDVEDmNYQA--------AKGE-GEVCVKGANVFKGYLKDPARTAE 529
Cdd:PRK09274 332 siESREILFATRAATdngAGIcVGRPVDGVEVRIIAISD-APIPewddalrlATGEiGEIVVAGPMVTRSYYNRPEATRL 410
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 564389119 530 A--LDKDG--WLHTGDIGkWL-PNGTLKIIDRKKHIFKLAQGEY--IAPEKIEN 576
Cdd:PRK09274 411 AkiPDGQGdvWHRMGDLG-YLdAQGRLWFCGRKAHRVETAGGTLytIPCERIFN 463
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
185-591 |
2.47e-12 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 69.78 E-value: 2.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 185 DAITYIVNKAELSVIFADK---PekaklLLEGVENKLtPCLKIIVImdsydndLVERGQKCGVEIIGLKALEDL--GRVN 259
Cdd:PRK06018 101 EQIAWIINHAEDRVVITDLtfvP-----ILEKIADKL-PSVERYVV-------LTDAAHMPQTTLKNAVAYEEWiaEADG 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 260 RTKPKPPEPEDLAIICFTSGTTGNPKGAMVTHQ-NIMNdcsGFIKATESAFIASPEDVLISFLPLAH-------MFETVV 331
Cdd:PRK06018 168 DFAWKTFDENTAAGMCYTSGTTGDPKGVLYSHRsNVLH---ALMANNGDALGTSAADTMLPVVPLFHanswgiaFSAPSM 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 332 ECVMLCHGAKIGffQGDIRLLMDDLKVlqpTIFPVVPRLlnrmfdrifgqantsvkrWLLDFASKRKEAElrsgivrnns 411
Cdd:PRK06018 245 GTKLVMPGAKLD--GASVYELLDTEKV---TFTAGVPTV------------------WLMLLQYMEKEGL---------- 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 412 lwdKLIFHKiqsslggkvRLMITGAAPVSATVLTFLRaaLGCQFYEGYGQTECTAGCCLS--------LPGDWTAGHV-- 481
Cdd:PRK06018 292 ---KLPHLK---------MVVCGGSAMPRSMIKAFED--MGVEVRHAWGMTEMSPLGTLAalkppfskLPGDARLDVLqk 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 482 -GAPMPCNYIKLVDvEDMNYQAAKGE--GEVCVKGANVFKGYLKDparTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKK 558
Cdd:PRK06018 358 qGYPPFGVEMKITD-DAGKELPWDGKtfGRLKVRGPAVAAAYYRV---DGEILDDDGFFDTGDVATIDAYGYMRITDRSK 433
|
410 420 430
....*....|....*....|....*....|...
gi 564389119 559 HIFKlAQGEYIAPEKIENIYLRSEAVAQVFVHG 591
Cdd:PRK06018 434 DVIK-SGGEWISSIDLENLAVGHPKVAEAAVIG 465
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
270-591 |
2.93e-12 |
|
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: 69.30 E-value: 2.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 270 DLAIICFTSGTTGNPKGAMVTHQNIMNDCSGFikatESAFIASPEDVLISFLPLAHMFE-TVVECVMLCHGAKIGF---F 345
Cdd:cd05940 82 DAALYIYTSGTTGLPKAAIISHRRAWRGGAFF----AGSGGALPSDVLYTCLPLYHSTAlIVGWSACLASGATLVIrkkF 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 346 QGdiRLLMDDLKVLQPTIFPVVPRLLnrmfdrifgqantsvkRWLLdfASKRKEAELRsgivrnnslwdklifHKIQSSL 425
Cdd:cd05940 158 SA--SNFWDDIRKYQATIFQYIGELC----------------RYLL--NQPPKPTERK---------------HKVRMIF 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 426 GGKVRLMITGaapvsatvlTFL-RAALGcQFYEGYGQTECTAGcCLSLPG-DWTAGHVGAPMPCNY-IKLV--DVEDMN- 499
Cdd:cd05940 203 GNGLRPDIWE---------EFKeRFGVP-RIAEFYAATEGNSG-FINFFGkPGAIGRNPSLLRKVApLALVkyDLESGEp 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 500 --------YQAAKGEGEVCVKGAN---VFKGYLkDPARTAEAL------DKDGWLHTGDIGKWLPNGTLKIIDRKKHIFK 562
Cdd:cd05940 272 irdaegrcIKVPRGEPGLLISRINplePFDGYT-DPAATEKKIlrdvfkKGDAWFNTGDLMRLDGEGFWYFVDRLGDTFR 350
|
330 340
....*....|....*....|....*....
gi 564389119 563 LaQGEYIAPEKIENIYLRSEAVAQVFVHG 591
Cdd:cd05940 351 W-KGENVSTTEVAAVLGAFPGVEEANVYG 378
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
267-608 |
3.27e-12 |
|
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: 69.43 E-value: 3.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 267 EPEDLAIICFTSGTTGNPKGAMVTHQNIMNdcsgfikatesafiaspedvlisflPLAHMFEtvvecvmlchgaKIGFFQ 346
Cdd:cd17656 126 NSDDLLYIIYTSGTTGKPKGVQLEHKNMVN-------------------------LLHFERE------------KTNINF 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 347 GDirllmddlKVLQPTIFPvvprlLNRMFDRIFGQANTSVKRWLLDFASKRKEAELRSGIVRNN--------SLWdKLIF 418
Cdd:cd17656 169 SD--------KVLQFATCS-----FDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNievvflpvAFL-KFIF 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 419 HKIQ--SSLGGKVRLMITGAAP--VSATVLTFLRAAlGCQFYEGYG--QTECTAGCCLSLPGDWTA-GHVGAPMPCNYIK 491
Cdd:cd17656 235 SEREfiNRFPTCVKHIITAGEQlvITNEFKEMLHEH-NVHLHNHYGpsETHVVTTYTINPEAEIPElPPIGKPISNTWIY 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 492 LVDvEDMNYQAAKGEGEVCVKGANVFKGYLKDPARTAEALDKDGW------LHTGDIGKWLPNGTLKIIDRKKHIFKLaQ 565
Cdd:cd17656 314 ILD-QEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFdpnermYRTGDLARYLPDGNIEFLGRADHQVKI-R 391
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 564389119 566 GEYIAPEKIENIYLRSEAVAQ--VFVHGESL-QAFLIAIVVPDVEI 608
Cdd:cd17656 392 GYRIELGEIEAQLLNHPGVSEavVLDKADDKgEKYLCAYFVMEQEL 437
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
269-611 |
3.72e-12 |
|
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: 69.04 E-value: 3.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 269 EDLAIICFTSGTTGNPKGAMVTHQNIMNDCSGFikaTESAFIASPEDVLISFLPLAHMFET-VVECVMLCHGAKIGFFQG 347
Cdd:cd05958 97 DDICILAFTSGTTGAPKATMHFHRDPLASADRY---AVNVLRLREDDRFVGSPPLAFTFGLgGVLLFPFGVGASGVLLEE 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 348 DI-RLLMDDLKVLQPTIFPVVPRLLNRMFdrifgqantsvkrwlldfASKRKEAELRSGivrnnslwdklifhkiqsslg 426
Cdd:cd05958 174 ATpDLLLSAIARYKPTVLFTAPTAYRAML------------------AHPDAAGPDLSS--------------------- 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 427 gkVRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYIKLVDveDMNYQAAKGE 506
Cdd:cd05958 215 --LRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEMFHIFISARPGDARPGATGKPVPGYEAKVVD--DEGNPVPDGT 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 507 -GEVCVKGANVFKgYLKDPARTAEAldKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYLRSEAVA 585
Cdd:cd05958 291 iGRLAVRGPTGCR-YLADKRQRTYV--QGGWNITGDTYSRDPDGYFRHQGRSDDMIVSG-GYNIAPPEVEDVLLQHPAVA 366
|
330 340
....*....|....*....|....*....
gi 564389119 586 QVFVHGESLQAFLI---AIVVPDVEILPS 611
Cdd:cd05958 367 ECAVVGHPDESRGVvvkAFVVLRPGVIPG 395
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
266-586 |
5.46e-12 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 68.64 E-value: 5.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 266 PEPEDLAIICFTSGTTGNPKGAMVTHQNImndcSGFIKATESAFIASPEDVLISFLPLAHMFetvvecvmlchGAKIGff 345
Cdd:cd05910 82 PKADEPAAILFTSGSTGTPKGVVYRHGTF----AAQIDALRQLYGIRPGEVDLATFPLFALF-----------GPALG-- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 346 qgdirllmddLKVLQPTIFPVVPrllnrmfdrifGQANtsvKRWLLDFASKRKEaelrSGIVRNNSLWDKLIFHKIQSSL 425
Cdd:cd05910 145 ----------LTSVIPDMDPTRP-----------ARAD---PQKLVGAIRQYGV----SIVFGSPALLERVARYCAQHGI 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 426 G-GKVRLMITGAAPVSATVLTFLRAAL--GCQFYEGYGQTECTAGCC------LSLPGDWTAGH----VGAPMPCNYIKL 492
Cdd:cd05910 197 TlPSLRRVLSAGAPVPIALAARLRKMLsdEAEILTPYGATEALPVSSigsrelLATTTAATSGGagtcVGRPIPGVRVRI 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 493 VDVEDMNYQAAKGE--------GEVCVKGANVFKGYLKDPARTAEALDKDG----WLHTGDIGKWLPNGTLKIIDRKKHI 560
Cdd:cd05910 277 IEIDDEPIAEWDDTlelprgeiGEITVTGPTVTPTYVNRPVATALAKIDDNsegfWHRMGDLGYLDDEGRLWFCGRKAHR 356
|
330 340
....*....|....*....|....*.
gi 564389119 561 FKLAQGEYIApEKIENIYLRSEAVAQ 586
Cdd:cd05910 357 VITTGGTLYT-EPVERVFNTHPGVRR 381
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
433-599 |
7.69e-12 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 68.26 E-value: 7.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 433 ITGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYIKLVDvEDMNYQAAKGEGEVCV- 511
Cdd:cd05928 297 VTGGEPLNPEVLEKWKAQTGLDIYEGYGQTETGLICANFKGMKIKPGSMGKASPPYDVQIID-DNGNVLPPGTEGDIGIr 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 512 ----KGANVFKGYLKDPARTAEALDKDGWLhTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAVAQV 587
Cdd:cd05928 376 vkpiRPFGLFSGYVDNPEKTAATIRGDFYL-TGDRGIMDEDGYFWFMGRADDVI-NSSGYRIGPFEVESALIEHPAVVES 453
|
170
....*....|....*....
gi 564389119 588 FV-------HGESLQAFLI 599
Cdd:cd05928 454 AVvsspdpiRGEVVKAFVV 472
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
151-607 |
9.66e-12 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 68.01 E-value: 9.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 151 IGIFSQNRPEWVTIEQGCFTYSMVVVPLYDTLGTDAITYIVNKAELSVIF--ADKPEKAKLLLEGVENKLTPCLkiivim 228
Cdd:PRK08276 39 VAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVLIvsAALADTAAELAAELPAGVPLLL------ 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 229 dsydndlVERGQKCGVEiiglkALEDLGRVNRTKPKPPEPE--DLAiicFTSGTTGNPKGAM--VTHQNIMNDCSGFIKA 304
Cdd:PRK08276 113 -------VVAGPVPGFR-----SYEEALAAQPDTPIADETAgaDML---YSSGTTGRPKGIKrpLPGLDPDEAPGMMLAL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 305 TESAFIASPEDVLISFLPLAHmfetvvecvmlchGAKIGFFQGDIRL-----LM---DDLKVLQ-------------PTI 363
Cdd:PRK08276 178 LGFGMYGGPDSVYLSPAPLYH-------------TAPLRFGMSALALggtvvVMekfDAEEALAlieryrvthsqlvPTM 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 364 FPvvpRLLnrmfdrifgqantsvkrwlldfasKRKEAelrsgiVRNNslWDklifhkiQSSLggkvRLMITGAAPVSATV 443
Cdd:PRK08276 245 FV---RML------------------------KLPEE------VRAR--YD-------VSSL----RVAIHAAAPCPVEV 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 444 LtflRAAL---GCQFYEGYGQTEcTAGCCLSLPGDWTA--GHVGAPMPCNyIKLVDvEDMNYQAAKGEGEVCVK-GANVF 517
Cdd:PRK08276 279 K---RAMIdwwGPIIHEYYASSE-GGGVTVITSEDWLAhpGSVGKAVLGE-VRILD-EDGNELPPGEIGTVYFEmDGYPF 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 518 KgYLKDPARTAEALDKDGWLHTGDIGkWL-PNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAVAQVFVHGeslqa 596
Cdd:PRK08276 353 E-YHNDPEKTAAARNPHGWVTVGDVG-YLdEDGYLYLTDRKSDMI-ISGGVNIYPQEIENLLVTHPKVADVAVFG----- 424
|
490
....*....|.
gi 564389119 597 fliaivVPDVE 607
Cdd:PRK08276 425 ------VPDEE 429
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
430-605 |
2.53e-11 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 66.55 E-value: 2.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 430 RLMITGAAPVSATVLTFLRAALGCQFYEGYGQTE----------------CTAGCCLSlPGD--WTAGHVGAPMPcnyik 491
Cdd:PRK10946 303 KLLQVGGARLSETLARRIPAELGCQLQQVFGMAEglvnytrlddsderifTTQGRPMS-PDDevWVADADGNPLP----- 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 492 lvdvedmnyqaaKGE-GEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHifklaQ----G 566
Cdd:PRK10946 377 ------------QGEvGRLMTRGPYTFRGYYKSPQHNASAFDANGFYCSGDLVSIDPDGYITVVGREKD-----QinrgG 439
|
170 180 190
....*....|....*....|....*....|....*....
gi 564389119 567 EYIAPEKIENIYLRSEAVaqvfvhgesLQAFLIAIvvPD 605
Cdd:PRK10946 440 EKIAAEEIENLLLRHPAV---------IHAALVSM--ED 467
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
122-591 |
2.59e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 66.45 E-value: 2.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 122 ISYKQVAEMAECIGSALIQKGFKPCSEqfIGIFSQNRPEWVTIEQGCFTYSMVVVPLYDTLGTDAITYIVNKAELSVIFA 201
Cdd:PRK07798 29 LTYAELEERANRLAHYLIAQGLGPGDH--VGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLLDDSDAVALVY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 202 DK---PEKAKLLLEgvenklTPCLK-IIVIMDSYDNDLvERGqkcGVEiiglkaLEDLGRVNRTKPKPPE--PEDLAIIC 275
Cdd:PRK07798 107 ERefaPRVAEVLPR------LPKLRtLVVVEDGSGNDL-LPG---AVD------YEDALAAGSPERDFGErsPDDLYLLY 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 276 fTSGTTGNPKGAMVTHQNIMNDCSGFIKATESAFIASPEDVL--------ISFLPLAHMfetvvecvMlcHGAK-----I 342
Cdd:PRK07798 171 -TGGTTGMPKGVMWRQEDIFRVLLGGRDFATGEPIEDEEELAkraaagpgMRRFPAPPL--------M--HGAGqwaafA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 343 GFFQGdirllmddlkvlQPTIFPVVPRL-------------LNRMFdrIFGQAntsVKRWLLDFASKRKEAELrsgivrn 409
Cdd:PRK07798 240 ALFSG------------QTVVLLPDVRFdadevwrtierekVNVIT--IVGDA---MARPLLDALEARGPYDL------- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 410 nslwdklifhkiqSSLggkvRLMITGAAPVSATVLTFLRAAL-GCQFYEGYGQTEctAGCCLSLPGDWTAGHVGAP--MP 486
Cdd:PRK07798 296 -------------SSL----FAIASGGALFSPSVKEALLELLpNVVLTDSIGSSE--TGFGGSGTVAKGAVHTGGPrfTI 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 487 CNYIKLVDVEDMNYQAAKGEGEVCVKGANVFKGYLKDPARTAEAL-DKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKL 563
Cdd:PRK07798 357 GPRTVVLDEDGNPVEPGSGEIGWIARRGHIPLGYYKDPEKTAETFpTIDGvrYAIPGDRARVEADGTITLLGRGSVCINT 436
|
490 500
....*....|....*....|....*...
gi 564389119 564 AqGEYIAPEKIENIYLRSEAVAQVFVHG 591
Cdd:PRK07798 437 G-GEKVFPEEVEEALKAHPDVADALVVG 463
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
185-585 |
3.66e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 66.27 E-value: 3.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 185 DAITYIVNKAELSVIFAD---KPekaklLLEGVENKLtPCLKIIVIMDSYDndlvergqKCGVEIIGLKALEDL-GRVNR 260
Cdd:PRK07008 101 EQIAYIVNHAEDRYVLFDltfLP-----LVDALAPQC-PNVKGWVAMTDAA--------HLPAGSTPLLCYETLvGAQDG 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 261 TKPKPPEPEDLAI-ICFTSGTTGNPKGAMVTHQNIMndCSGFIKATESAFIASPEDVLisfLPLAHMFEtvVECVMLCH- 338
Cdd:PRK07008 167 DYDWPRFDENQASsLCYTSGTTGNPKGALYSHRSTV--LHAYGAALPDAMGLSARDAV---LPVVPMFH--VNAWGLPYs 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 339 ----GAKIgFFQG------DIRLLMDDLKVLQPTIFPVV-PRLLNRMfdrifgqantsvkrwlldfaskrKEAELRSGIV 407
Cdd:PRK07008 240 apltGAKL-VLPGpdldgkSLYELIEAERVTFSAGVPTVwLGLLNHM-----------------------REAGLRFSTL 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 408 RnnslwdklifhkiqsslggkvRLMITGAAPVSATVLTFlRAALGCQFYEGYGQTE-------CT-AGCCLSLPGD---- 475
Cdd:PRK07008 296 R---------------------RTVIGGSACPPAMIRTF-EDEYGVEVIHAWGMTEmsplgtlCKlKWKHSQLPLDeqrk 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 476 --WTAGHV--GAPMpcnyiKLVDvEDMNYQAAKGE--GEVCVKGANVFKGYLKdpaRTAEALDkDGWLHTGDIGKWLPNG 549
Cdd:PRK07008 354 llEKQGRViyGVDM-----KIVG-DDGRELPWDGKafGDLQVRGPWVIDRYFR---GDASPLV-DGWFPTGDVATIDADG 423
|
410 420 430
....*....|....*....|....*....|....*.
gi 564389119 550 TLKIIDRKKHIFKlAQGEYIAPEKIENIYLRSEAVA 585
Cdd:PRK07008 424 FMQITDRSKDVIK-SGGEWISSIDIENVAVAHPAVA 458
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
251-599 |
1.50e-10 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 64.02 E-value: 1.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 251 ALEDL---GRVNRTKPKPPEP-EDLAIICFTSGTTGNPKGAMVTHQNIMNDCSGFIKATEsafIASPEDVLISFLPLAH- 325
Cdd:PRK05851 130 TVHDLataAHTNRSASLTPPDsGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVG---LDAATDVGCSWLPLYHd 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 326 MFETVVECVMLChGAKIGffqgdirllmddlkvLQPTifpvvprllnrmfdrifGQANTSVKRWLlDFASkrkeaELRSG 405
Cdd:PRK05851 207 MGLAFLLTAALA-GAPLW---------------LAPT-----------------TAFSASPFRWL-SWLS-----DSRAT 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 406 IVRNNSLWDKLI---FHKIQSSLGGKVRLMITGAAPVSATVLT-FLRAALGCQFYEG-----YGQTECTAGCCLSLPG-- 474
Cdd:PRK05851 248 LTAAPNFAYNLIgkyARRVSDVDLGALRVALNGGEPVDCDGFErFATAMAPFGFDAGaaapsYGLAESTCAVTVPVPGig 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 475 ---------DWTAGH----VGAPMPCNYIKLVDVEDMNYQAAKGEGEVCVKGANVFKGYLKDPArtaeaLDKDGWLHTGD 541
Cdd:PRK05851 328 lrvdevttdDGSGARrhavLGNPIPGMEVRISPGDGAAGVAGREIGEIEIRGASMMSGYLGQAP-----IDPDDWFPTGD 402
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564389119 542 IGkWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIY-----LRSEAVAQVFVHGESLQAFLI 599
Cdd:PRK05851 403 LG-YLVDGGLVVCGRAKELITVA-GRNIFPTEIERVAaqvrgVREGAVVAVGTGEGSARPGLV 463
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
122-599 |
1.58e-10 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 63.69 E-value: 1.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 122 ISYKQVAEMAECIGSALIQKGFKPcSEQFIGIFSQNrPEWVTIEQGCFTYSMVVVPLYDTLGTDAITYIVNKAELSVIFA 201
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGP-GDVVAGLLPRT-PELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 202 DKPEKAKLllegvenkltpclkiivimdsydndlvergqkcgveiiglkaledlgrvnrtkpkppePEDLAIICFTSGTT 281
Cdd:cd05973 79 DAANRHKL----------------------------------------------------------DSDPFVMMFTSGTT 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 282 GNPKGAMVTHQNIMndcsGFIKATESAFIASPEDVlisFLPLAH------MFETVVECVMLCHGAKI---GFFQGDIRLL 352
Cdd:cd05973 101 GLPKGVPVPLRALA----AFGAYLRDAVDLRPEDS---FWNAADpgwaygLYYAITGPLALGHPTILlegGFSVESTWRV 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 353 MDDLKVLQPTIFPVVPRLLnrmfdrifgqantsvkrwlldfASKRKEAELRsgivrnnslwdklifhkiqssLGGKVRLM 432
Cdd:cd05973 174 IERLGVTNLAGSPTAYRLL----------------------MAAGAEVPAR---------------------PKGRLRRV 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 433 ITGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCC--LSLPGDWTAGHVGAPMPCNYIKLVDveDMNYQAAKGE-GEV 509
Cdd:cd05973 211 SSAGEPLTPEVIRWFDAALGVPIHDHYGQTELGMVLAnhHALEHPVHAGSAGRAMPGWRVAVLD--DDGDELGPGEpGRL 288
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 510 CVKGANV----FKGYLKDPARTAEAldkdGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYLRSEAVA 585
Cdd:cd05973 289 AIDIANSplmwFRGYQLPDTPAIDG----GYYLTGDTVEFDPDGSFSFIGRADDVITMS-GYRIGPFDVESALIEHPAVA 363
|
490 500
....*....|....*....|.
gi 564389119 586 QVFV-------HGESLQAFLI 599
Cdd:cd05973 364 EAAVigvpdpeRTEVVKAFVV 384
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
423-591 |
2.92e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 63.17 E-value: 2.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 423 SSLggkvRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTEcTAGCCLSLPGDWTA--GHVGAPMpcnYIKLVDVEDMNY 500
Cdd:PRK13391 275 SSL----EVAIHAAAPCPPQVKEQMIDWWGPIIHEYYAATE-GLGFTACDSEEWLAhpGTVGRAM---FGDLHILDDDGA 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 501 QAAKGE-GEVCVKGANVFKgYLKDPARTAEALDKDG-WLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIY 578
Cdd:PRK13391 347 ELPPGEpGTIWFEGGRPFE-YLNDPAKTAEARHPDGtWSTVGDIGYVDEDGYLYLTDRAAFMI-ISGGVNIYPQEAENLL 424
|
170
....*....|...
gi 564389119 579 LRSEAVAQVFVHG 591
Cdd:PRK13391 425 ITHPKVADAAVFG 437
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
122-342 |
9.20e-10 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 61.81 E-value: 9.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 122 ISYKQVAEMAECIGSALIQKGFKPcsEQFIGIFSQNRPEWVTIEQGcFTYSMVVVPLYDT-LGTDAITYIVNKAELSVIF 200
Cdd:PRK08279 63 ISYAELNARANRYAHWAAARGVGK--GDVVALLMENRPEYLAAWLG-LAKLGAVVALLNTqQRGAVLAHSLNLVDAKHLI 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 201 ADkPEKAKLLlEGVENKLTPCLKIIVImdsydndlverGQKCGVEIIGLKALEDLGRvNRTKPKPPE-----PEDLAIIC 275
Cdd:PRK08279 140 VG-EELVEAF-EEARADLARPPRLWVA-----------GGDTLDDPEGYEDLAAAAA-GAPTTNPASrsgvtAKDTAFYI 205
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564389119 276 FTSGTTGNPKGAMVTHQNIMNDCSGFIKATEsafiASPEDVLISFLPLAH-MFETVVECVMLCHGAKI 342
Cdd:PRK08279 206 YTSGTTGLPKAAVMSHMRWLKAMGGFGGLLR----LTPDDVLYCCLPLYHnTGGTVAWSSVLAAGATL 269
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
260-587 |
1.06e-09 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 61.56 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 260 RTKPKPPEPEDLAIIcFTSGTTGNPKGAMVTHQN-------IMNDCSGFIKATESAFIASPedvlisfLPLAHM--FETV 330
Cdd:PRK05857 161 AGNADQGSEDPLAMI-FTSGTTGEPKAVLLANRTffavpdiLQKEGLNWVTWVVGETTYSP-------LPATHIggLWWI 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 331 VECVMlcHGAKI---GFFQGDIRLLMDDLKVLQPTIfpvVPRLLNRMFdrifgqantsvkrwlldfaskrkeAELRSGIV 407
Cdd:PRK05857 233 LTCLM--HGGLCvtgGENTTSLLEILTTNAVATTCL---VPTLLSKLV------------------------SELKSANA 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 408 RNNSLwdklifhkiqsslggkvRLMITGAAPVSATVLTFLRAA--LGCQFYeGYGQTECTAGCclsLPGD------WTAG 479
Cdd:PRK05857 284 TVPSL-----------------RLVGYGGSRAIAADVRFIEATgvRTAQVY-GLSETGCTALC---LPTDdgsivkIEAG 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 480 HVGAPMPCNYIKLVDVEDMNYQAAKGE-----GEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKII 554
Cdd:PRK05857 343 AVGRPYPGVDVYLAATDGIGPTAPGAGpsasfGTLWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLLERREDGFFYIK 421
|
330 340 350
....*....|....*....|....*....|...
gi 564389119 555 DRKKHIFkLAQGEYIAPEKIENIylrSEAVAQV 587
Cdd:PRK05857 422 GRSSEMI-ICGGVNIAPDEVDRI---AEGVSGV 450
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
268-607 |
3.88e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 60.56 E-value: 3.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 268 PEDLAIICFTSGTTGNPKGAMVTHQNIMNDCsgfiKATESAFIASPEDVLISFLPLAhmFETVVECVM--LCHGAKIGFF 345
Cdd:PRK12467 3236 GENLAYVIYTSGSTGKPKGVGVRHGALANHL----CWIAEAYELDANDRVLLFMSFS--FDGAQERFLwtLICGGCLVVR 3309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 346 QGDIR---LLMDDLKVLQPTIFPVVPRLLNRMFDRIFGQANTSVKRWLldfaskrkeaelrsgivrnnslwdklifhkiq 422
Cdd:PRK12467 3310 DNDLWdpeELWQAIHAHRISIACFPPAYLQQFAEDAGGADCASLDIYV-------------------------------- 3357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 423 ssLGGKvrlmitgAAPVSATVLTFlRAALGCQFYEGYGQTECTAGCCL-SLPGDWTAGHVGAPM--PCNYIKLVdVEDMN 499
Cdd:PRK12467 3358 --FGGE-------AVPPAAFEQVK-RKLKPRGLTNGYGPTEAVVTVTLwKCGGDAVCEAPYAPIgrPVAGRSIY-VLDGQ 3426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 500 YQ-AAKGE-GEVCVKGANVFKGYLKDPARTAEALDKD------GWLH-TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIA 570
Cdd:PRK12467 3427 LNpVPVGVaGELYIGGVGLARGYHQRPSLTAERFVADpfsgsgGRLYrTGDLARYRADGVIEYLGRIDHQVKI-RGFRIE 3505
|
330 340 350
....*....|....*....|....*....|....*....
gi 564389119 571 PEKIENIYLRSEAVAQVFVHGESLQA--FLIAIVVPDVE 607
Cdd:PRK12467 3506 LGEIEARLLQHPSVREAVVLARDGAGgkQLVAYVVPADP 3544
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
267-575 |
3.99e-09 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 60.57 E-value: 3.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 267 EPEDLAIICFTSGTTGNPKGAMVTHQNIMNDCS----GFikatesAFIASPEDVLISFLPLAHmfetvvecvmlchgaKI 342
Cdd:PRK05691 164 QPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQlirhGF------GIDLNPDDVIVSWLPLYH---------------DM 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 343 GFFQGdirllmddlkVLQPtIFPVVPRLLnrMFDRIFgqaNTSVKRWLL-------------DFA----SKR-KEAELRS 404
Cdd:PRK05691 223 GLIGG----------LLQP-IFSGVPCVL--MSPAYF---LERPLRWLEaiseyggtisggpDFAyrlcSERvSESALER 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 405 givRNNSLWdklifhkiqsslggkvRLMITGAAPVSATVL-TFLRAALGC-----QFYEGYGQTECT---AGC------- 468
Cdd:PRK05691 287 ---LDLSRW----------------RVAYSGSEPIRQDSLeRFAEKFAACgfdpdSFFASYGLAEATlfvSGGrrgqgip 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 469 CLSLPGDWTAGHVGAP------MPCNY------IKLVDVEDMNYQAAKGEGEVCVKGANVFKGYLKDPARTAEA-LDKDG 535
Cdd:PRK05691 348 ALELDAEALARNRAEPgtgsvlMSCGRsqpghaVLIVDPQSLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTfVEHDG 427
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 564389119 536 --WLHTGDIGkWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIE 575
Cdd:PRK05691 428 rtWLRTGDLG-FLRDGELFVTGRLKDML-IVRGHNLYPQDIE 467
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
274-605 |
4.39e-09 |
|
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: 58.57 E-value: 4.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 274 ICFTSGTTGNPKGAMVTHQNIMndcsGFIKATESAFIASPEDVLISFLPLAH-MFETVVECVMLCHGAKIGFFQGDIRLL 352
Cdd:cd17633 5 IGFTSGTTGLPKAYYRSERSWI----ESFVCNEDLFNISGEDAILAPGPLSHsLFLYGAISALYLGGTFIGQRKFNPKSW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 353 MDDLKVLQPTIFPVVPRLLnrmfdrifgqantsvkrwlldfaskrkEAELRSGIvrnnslwdklIFHKIQSSLGGkvrlm 432
Cdd:cd17633 81 IRKINQYNATVIYLVPTML---------------------------QALARTLE----------PESKIKSIFSS----- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 433 itGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCnyiklVDVEDMNyQAAKGEGEVCVK 512
Cdd:cd17633 119 --GQKLFESTKKKLKNIFPKANLIEFYGTSELSFITYNFNQESRPPNSVGRPFPN-----VEIEIRN-ADGGEIGKIFVK 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 513 GANVFKGYLKdpartAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAVAQVFVHGE 592
Cdd:cd17633 191 SEMVFSGYVR-----GGFSNPDGWMSVGDIGYVDEEGYLYLVGRESDMI-IIGGINIFPTEIESVLKAIPGIEEAIVVGI 264
|
330
....*....|....*.
gi 564389119 593 SLQAF---LIAIVVPD 605
Cdd:cd17633 265 PDARFgeiAVALYSGD 280
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
243-607 |
5.01e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 59.97 E-value: 5.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 243 GVEIIGLKA-LEDLGRVNrtKPKPPEPEDLAIICFTSGTTGNPKGAMVTHQNImndcSGFIKATESAFIASPEDVLISFL 321
Cdd:PRK12316 3171 GVQVLDLDRgDENYAEAN--PAIRTMPENLAYVIYTSGSTGKPKGVGIRHSAL----SNHLCWMQQAYGLGVGDRVLQFT 3244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 322 PLAHMFETVVECVMLCHGAKIgffqgdirllmddlkVLQPTIFPVVPRLLNRMFDRIFGQANTSVKRWLLDFASKRKEAE 401
Cdd:PRK12316 3245 TFSFDVFVEELFWPLMSGARV---------------VLAGPEDWRDPALLVELINSEGVDVLHAYPSMLQAFLEEEDAHR 3309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 402 LRSgivrnnslwdklifhkiqsslggkVRLMITGAAPVSATVLTflRAALGCQFYEGYGQTECTAGCCLSLPGDWTAGH- 480
Cdd:PRK12316 3310 CTS------------------------LKRIVCGGEALPADLQQ--QVFAGLPLYNLYGPTEATITVTHWQCVEEGKDAv 3363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 481 -VGAPMPCNYIKLVDVeDMNYQAAKGEGEVCVKGANVFKGYLKDPARTAEALDKDGW------LHTGDIGKWLPNGTLKI 553
Cdd:PRK12316 3364 pIGRPIANRACYILDG-SLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPFvpgerlYRTGDLARYRADGVIEY 3442
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 564389119 554 IDRKKHIFKLaQGEYIAPEKIENIYLRSEAVAQVFVHGESLQAfLIAIVVPDVE 607
Cdd:PRK12316 3443 IGRVDHQVKI-RGFRIELGEIEARLLEHPWVREAVVLAVDGRQ-LVAYVVPEDE 3494
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
102-605 |
7.84e-09 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 58.88 E-value: 7.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 102 QVSNDGPCLGSRkpNQPYEWisyKQVAEMAECIGSALIQKGfKPCSEQFIGIFSQNRPEWVTIEQGCFTYSMVVVPLYDT 181
Cdd:PRK13388 12 RAGDDTIAVRYG--DRTWTW---REVLAEAAARAAALIALA-DPDRPLHVGVLLGNTPEMLFWLAAAALGGYVLVGLNTT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 182 LGTDAITYIVNKAELSVIFADKPEKAklLLEGVEnkltpcLKIIVIMDSYDNDLVERgqkcgveiiglkaledLGRVNRT 261
Cdd:PRK13388 86 RRGAALAADIRRADCQLLVTDAEHRP--LLDGLD------LPGVRVLDVDTPAYAEL----------------VAAAGAL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 262 KP-KPPEPEDLAIICFTSGTTGNPKGAMVTHQNImndcsGFIKATESA-FIASPEDVLISFLPLAHMfetvvECVM---- 335
Cdd:PRK13388 142 TPhREVDAMDPFMLIFTSGTTGAPKAVRCSHGRL-----AFAGRALTErFGLTRDDVCYVSMPLFHS-----NAVMagwa 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 336 --LCHGAKI---------GFfqgdirllMDDLKVLQPTIFPVVPRLLNrmfdrifgqantsvkrWLLDFASKRKEAE--L 402
Cdd:PRK13388 212 paVASGAAValpakfsasGF--------LDDVRRYGATYFNYVGKPLA----------------YILATPERPDDADnpL 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 403 RSGivrnnslwdklifhkiqssLGgkvrlmiTGAAPVSATvlTFLRAaLGCQFYEGYGQTEctAGCCLSLPGDWTAGHVG 482
Cdd:PRK13388 268 RVA-------------------FG-------NEASPRDIA--EFSRR-FGCQVEDGYGSSE--GAVIVVREPGTPPGSIG 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 483 APMPCnyIKLVDVEDM---------------NYQAAKGEgEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLP 547
Cdd:PRK13388 317 RGAPG--VAIYNPETLtecavarfdahgallNADEAIGE-LVNTAGAGFFEGYYNNPEATAERM-RHGMYWSGDLAYRDA 392
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 564389119 548 NGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSEAVAQVFVHGeslqafliaivVPD 605
Cdd:PRK13388 393 DGWIYFAGRTADWMRV-DGENLSAAPIERILLRHPAINRVAVYA-----------VPD 438
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
484-639 |
7.90e-09 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 58.75 E-value: 7.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 484 PMPCNYIK-----LVDVEDMNYQAAKGEGEVCVKGANVFKGYLKDPARTAEAL-DKDGW--LHTGDIGKwLPNGTLKIID 555
Cdd:PRK04813 317 RLPIGYAKpdsplLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFfTFDGQpaYHTGDAGY-LEDGLLFYQG 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 556 RKKHIFKLAqGEYIAPEKIENiYLR-----SEAVAQVFVHGESLQAfLIAIVVPDveilpswaqkrgfQGSFEelcRNKD 630
Cdd:PRK04813 396 RIDFQIKLN-GYRIELEEIEQ-NLRqssyvESAVVVPYNKDHKVQY-LIAYVVPK-------------EEDFE---REFE 456
|
....*....
gi 564389119 631 INKAILEDM 639
Cdd:PRK04813 457 LTKAIKKEL 465
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
252-607 |
9.44e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 58.40 E-value: 9.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 252 LEDLGRVNRTKPKPPEPEDLAIICFTSGTTGNPKGAMVTHQNIMNDCSGFI-----KATESAFIASPedvlisflplahM 326
Cdd:PRK07788 190 LDDLIAGSSTAPLPKPPKPGGIVILTSGTTGTPKGAPRPEPSPLAPLAGLLsrvpfRAGETTLLPAP------------M 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 327 FetvvecvmlcHG-----AKIGFFQG---------DIRLLMDDLKVLQPTIFPVVPRLLNRMFDrifgqantsvkrwLLD 392
Cdd:PRK07788 258 F----------HAtgwahLTLAMALGstvvlrrrfDPEATLEDIAKHKATALVVVPVMLSRILD-------------LGP 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 393 FASKRKEAelrsgivrnnslwdklifhkiqSSLggkvRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECtAGCCLSL 472
Cdd:PRK07788 315 EVLAKYDT----------------------SSL----KIIFVSGSALSPELATRALEAFGPVLYNLYGSTEV-AFATIAT 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 473 PGDWTA--GHVGAPMPCNYIKLVDvEDMNyQAAKGE-GEVCVKGANVFKGYL--KDPARtaealdKDGWLHTGDIGKWLP 547
Cdd:PRK07788 368 PEDLAEapGTVGRPPKGVTVKILD-ENGN-EVPRGVvGRIFVGNGFPFEGYTdgRDKQI------IDGLLSSGDVGYFDE 439
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 548 NGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAVAQVFVHGeslqafliaivVPDVE 607
Cdd:PRK07788 440 DGLLFVDGRDDDMI-VSGGENVFPAEVEDLLAGHPDVVEAAVIG-----------VDDEE 487
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
269-600 |
1.65e-08 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 58.26 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 269 EDLAIICFTSGTTGNPKGAMVTHQNIMNDCSgFIKATesaFIASPEDVLISFLPLAhmFE-TVVECVM-LCHGAKIGFF- 345
Cdd:PRK05691 1273 DNLAYVIYTSGSTGQPKGVGNTHAALAERLQ-WMQAT---YALDDSDVLMQKAPIS--FDvSVWECFWpLITGCRLVLAg 1346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 346 ---QGDIRLLMDDLKVLQPTIFPVVPRLLNRMFDRIFGQANTSVkrwlldfaskrkeaelrsgivrnnslwdklifhkiq 422
Cdd:PRK05691 1347 pgeHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLAAACTSL------------------------------------ 1390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 423 sslggkvRLMITGAAPVSATVLTFLRAAL-GCQFYEGYGQTE----CTAGCCLSLPGDWTAghVGAPMPCNYIKLVDVEd 497
Cdd:PRK05691 1391 -------RRLFSGGEALPAELRNRVLQRLpQVQLHNRYGPTEtainVTHWQCQAEDGERSP--IGRPLGNVLCRVLDAE- 1460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 498 MNYQAAKGEGEVCVKGANVFKGYLKDPARTAE-----ALDKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIA 570
Cdd:PRK05691 1461 LNLLPPGVAGELCIGGAGLARGYLGRPALTAErfvpdPLGEDGarLYRTGDRARWNADGALEYLGRLDQQVKL-RGFRVE 1539
|
330 340 350
....*....|....*....|....*....|..
gi 564389119 571 PEKIENIYLRSEAVAQ--VFVHGESLQAFLIA 600
Cdd:PRK05691 1540 PEEIQARLLAQPGVAQaaVLVREGAAGAQLVG 1571
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
120-608 |
3.16e-08 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 56.56 E-value: 3.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 120 EWISYKQVAEMAECIGSALIQKGFKPcsEQFIGIFSQNRPE-----WVTIEQGcftysmvvvpLYDTlgtdAITYIVNKA 194
Cdd:PRK13390 23 EQVSYRQLDDDSAALARVLYDAGLRT--GDVVALLSDNSPEalvvlWAALRSG----------LYIT----AINHHLTAP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 195 ELSVIFADKPEK---AKLLLEGVENKLTPCLKIIVIMdsydndlvergqkcGVEIIGLKALEdlGRVNRTKPKPPEPEDL 271
Cdd:PRK13390 87 EADYIVGDSGARvlvASAALDGLAAKVGADLPLRLSF--------------GGEIDGFGSFE--AALAGAGPRLTEQPCG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 272 AIICFTSGTTGNPKGAMVTHQNIMNDCSG--FIKATESAFIASPEDVLISFLPLAHMfETVVECVMLcH---GAKIGFFQ 346
Cdd:PRK13390 151 AVMLYSSGTTGFPKGIQPDLPGRDVDAPGdpIVAIARAFYDISESDIYYSSAPIYHA-APLRWCSMV-HalgGTVVLAKR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 347 GDIRLLMDDLKVLQPTIFPVVPRLLNRMFdrifgqantsvkrwlldfaskRKEAELRSgivrnnsLWDklifhkiQSSLg 426
Cdd:PRK13390 229 FDAQATLGHVERYRITVTQMVPTMFVRLL---------------------KLDADVRT-------RYD-------VSSL- 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 427 gkvRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTEcTAGCCLSLPGDWTA--GHVGAPMpCNYIKLVDvEDMNYQAAK 504
Cdd:PRK13390 273 ---RAVIHAAAPCPVDVKHAMIDWLGPIVYEYYSSTE-AHGMTFIDSPDWLAhpGSVGRSV-LGDLHICD-DDGNELPAG 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 505 GEGEVCVKGANVFKGYLKDPARTAEALDKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSE 582
Cdd:PRK13390 347 RIGTVYFERDRLPFRYLNDPEKTAAAQHPAHpfWTTVGDLGSVDEDGYLYLADRKSFMI-ISGGVNIYPQETENALTMHP 425
|
490 500
....*....|....*....|....*.
gi 564389119 583 AVAQVFVHGeslqafliaivVPDVEI 608
Cdd:PRK13390 426 AVHDVAVIG-----------VPDPEM 440
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
423-605 |
3.19e-08 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 56.63 E-value: 3.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 423 SSLggkvRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTE------CTAGCCLSLPGDwtaghVGAPMPCNYIKLVDvE 496
Cdd:PRK12406 271 SSL----RHVIHAAAPCPADVKRAMIEWWGPVIYEYYGSTEsgavtfATSEDALSHPGT-----VGKAAPGAELRFVD-E 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 497 DMNY--QAAKGEGEVCVKGANVFKgYLKDPARTAEaLDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKI 574
Cdd:PRK12406 341 DGRPlpQGEIGEIYSRIAGNPDFT-YHNKPEKRAE-IDRGGFITSGDVGYLDADGYLFLCDRKRDMV-ISGGVNIYPAEI 417
|
170 180 190
....*....|....*....|....*....|....
gi 564389119 575 ENIYLRSEAVAQVFVHG---ESLQAFLIAIVVPD 605
Cdd:PRK12406 418 EAVLHAVPGVHDCAVFGipdAEFGEALMAVVEPQ 451
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
482-575 |
4.82e-08 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 56.17 E-value: 4.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 482 GAPMPCNYIKLVDvEDMNYQAAKGEGEVCVKGANVFKGYLKDPArTAEALDKDGWLHTGDIGkWLPNGTLKIIDRKKHIF 561
Cdd:PRK09192 388 GKALPGHEIEIRN-EAGMPLPERVVGHICVRGPSLMSGYFRDEE-SQDVLAADGWLDTGDLG-YLLDGYLYITGRAKDLI 464
|
90
....*....|....
gi 564389119 562 kLAQGEYIAPEKIE 575
Cdd:PRK09192 465 -IINGRNIWPQDIE 477
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
268-616 |
5.12e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 56.89 E-value: 5.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 268 PEDLAIICFTSGTTGNPKGAMVTHQNIMN------------DCSGFIKATESAFIASpedVLISFLPLAHmfetvvecvm 335
Cdd:PRK12316 654 PENLAYVIYTSGSTGKPKGAGNRHRALSNrlcwmqqayglgVGDTVLQKTPFSFDVS---VWEFFWPLMS---------- 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 336 lchGAkigffqgdiRLLmddlkvlqptifpVVPRLLNRMFDRIFGQANTSVKRwLLDFASKRKEAELRSGivrnnslwdk 415
Cdd:PRK12316 721 ---GA---------RLV-------------VAAPGDHRDPAKLVELINREGVD-TLHFVPSMLQAFLQDE---------- 764
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 416 lifhKIQSSLggKVRLMITGAAPVSATVLTFLRAAL-GCQFYEGYGQTECTAGCCLSLPGDWTAGHV--GAPMPCNYIKL 492
Cdd:PRK12316 765 ----DVASCT--SLRRIVCSGEALPADAQEQVFAKLpQAGLYNLYGPTEAAIDVTHWTCVEEGGDSVpiGRPIANLACYI 838
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 493 VDVeDMNYQAAKGEGEVCVKGANVFKGYLKDPARTAEAL------DKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQG 566
Cdd:PRK12316 839 LDA-NLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFvpspfvAGERMYRTGDLARYRADGVIEYAGRIDHQVKL-RG 916
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 564389119 567 EYIAPEKIENIYLRSEAVAQVFVHGESLQAfLIAIVVPD------VEILPSWAQKR 616
Cdd:PRK12316 917 LRIELGEIEARLLEHPWVREAAVLAVDGKQ-LVGYVVLEseggdwREALKAHLAAS 971
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
276-591 |
1.20e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 54.79 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 276 FTSGTTGNPKGAMVTHQNIMN--DCsgfikaTESAFIASPED-VLISflplahmfETVVECVMLcHGAKIGFFQGDIRLL 352
Cdd:PRK07638 150 FTSGSTGKPKAFLRAQQSWLHsfDC------NVHDFHMKREDsVLIA--------GTLVHSLFL-YGAISTLYVGQTVHL 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 353 MddlkvlqPTIFPvvprllNRMFDRIfGQANTSVkrwlLDFASKRKEAELRSGIVRNNSLwdklifhKIQSSlGGKvrlm 432
Cdd:PRK07638 215 M-------RKFIP------NQVLDKL-ETENISV----MYTVPTMLESLYKENRVIENKM-------KIISS-GAK---- 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 433 iTGAAPVSATVLTFLRAalgcQFYEGYGQTECTAGCCLSlPGDWTAGHVGAPMPCNYIKLVDVEDMNYQAAKGE-GEVCV 511
Cdd:PRK07638 265 -WEAEAKEKIKNIFPYA----KLYEFYGASELSFVTALV-DEESERRPNSVGRPFHNVQVRICNEAGEEVQKGEiGTVYV 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 512 KGANVFKGYLKDpARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAVAQVFVHG 591
Cdd:PRK07638 339 KSPQFFMGYIIG-GVLARELNADGWMTVRDVGYEDEEGFIYIVGREKNMI-LFGGINIFPEEIESVLHEHPAVDEIVVIG 416
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
266-557 |
1.26e-07 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 54.79 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 266 PEPEDLAIICFTSGTTGNPKGAMVTHQNIMNdcsgFIKATESAFIASPEDVLIsFLPLAHMFETVVECVM-LCHGAKIgf 344
Cdd:cd17654 115 RTDECLAYVIHTSGTTGTPKIVAVPHKCILP----NIQHFRSLFNITSEDILF-LTSPLTFDPSVVEIFLsLSSGATL-- 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 345 fqgdirllmddlkVLQPTIFPVVPRLLNRMFDRIFG----QANTSVKRwllDFASKRKEAELRSGIvrnnslwdklifhk 420
Cdd:cd17654 188 -------------LIVPTSVKVLPSKLADILFKRHRitvlQATPTLFR---RFGSQSIKSTVLSAT-------------- 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 421 iqSSLggKVrLMITGAAPVSATVLTFLRAA-LGCQFYEGYGQTECtagCCLSL----PGDWTAGHVGAPMPCNYIKLVDV 495
Cdd:cd17654 238 --SSL--RV-LALGGEPFPSLVILSSWRGKgNRTRIFNIYGITEV---SCWALaykvPEEDSPVQLGSPLLGTVIEVRDQ 309
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564389119 496 EdmnyqAAKGEGEVCVKGANVfKGYLKDPARTAEALdkdgWLHTGDIGKwLPNGTLKIIDRK 557
Cdd:cd17654 310 N-----GSEGTGQVFLGGLNR-VCILDDEVTVPKGT----MRATGDFVT-VKDGELFFLGRK 360
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
268-600 |
3.40e-07 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 54.02 E-value: 3.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 268 PEDLAIICFTSGTTGNPKGAMVTHQNIMNDCSG---FIKATESAFIA--SPEDVLIS---FLPlAHMFETVVECV--MLC 337
Cdd:PRK05691 3868 PDNLAYVIYTSGSTGLPKGVMVEQRGMLNNQLSkvpYLALSEADVIAqtASQSFDISvwqFLA-APLFGARVEIVpnAIA 3946
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 338 HgakigffqgDIRLLMDDLKVLQPTIFPVVPRLLNRMF--DRifgQANTSVkRWLL--------DFASKRKEAELRSGIV 407
Cdd:PRK05691 3947 H---------DPQGLLAHVQAQGITVLESVPSLIQGMLaeDR---QALDGL-RWMLptgeamppELARQWLQRYPQIGLV 4013
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 408 rnNSLwdklifhkiqsslggkvrlmitGAAPVSATVlTFLRAALgcqfyegygqtECTAGCCLSlpgdwtaghVGAPMPC 487
Cdd:PRK05691 4014 --NAY----------------------GPAECSDDV-AFFRVDL-----------ASTRGSYLP---------IGSPTDN 4048
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 488 NYIKLVDvEDMNYQAAKGEGEVCVKGANVFKGYLKDPARTAEALDKDGW-------LHTGDIGKWLPNGTLKIIDRKKHI 560
Cdd:PRK05691 4049 NRLYLLD-EALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPHPFgapgerlYRTGDLARRRSDGVLEYVGRIDHQ 4127
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 564389119 561 -----FKLAQGEyIAPEKIENIYLRSEAVA-QVFVHGESLQAFLIA 600
Cdd:PRK05691 4128 vkirgYRIELGE-IEARLHEQAEVREAAVAvQEGVNGKHLVGYLVP 4172
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
266-615 |
9.46e-07 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 51.61 E-value: 9.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 266 PEPEDLAIICfTSGTTGNPKGAMVTHQNImndcsgFIKATESAFIASPEDVLISFLPLAHMFETVVECVMLC---HGAK- 341
Cdd:cd05924 1 RSADDLYILY-TGGTTGMPKGVMWRQEDI------FRMLMGGADFGTGEFTPSEDAHKAAAAAAGTVMFPAPplmHGTGs 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 342 ----IGFFQGDiRLLMDDLKVLQPTIFPVVPR-LLNRMFdrIFGQAntsVKRWLLDfaskrkeaELRSGivRNNSLwdkl 416
Cdd:cd05924 74 wtafGGLLGGQ-TVVLPDDRFDPEEVWRTIEKhKVTSMT--IVGDA---MARPLID--------ALRDA--GPYDL---- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 417 ifhkiqSSLggkvRLMITGAAPVSATVLT-FLRAALGCQFYEGYGQTECTA-GCCLSLPGDWTAGHVGAPMPcnyiKLVD 494
Cdd:cd05924 134 ------SSL----FAISSGGALLSPEVKQgLLELVPNITLVDAFGSSETGFtGSGHSAGSGPETGPFTRANP----DTVV 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 495 VEDMNYQAAKGEGEVCV--KGANVFKGYLKDPARTAEAL-DKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYI 569
Cdd:cd05924 200 LDDDGRVVPPGSGGVGWiaRRGHIPLGYYGDEAKTAETFpEVDGvrYAVPGDRATVEADGTVTLLGRGSVCINTG-GEKV 278
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 564389119 570 APEKIENIYLRSEAVAQVFVHGeslqafliaivVPDveilPSWAQK 615
Cdd:cd05924 279 FPEEVEEALKSHPAVYDVLVVG-----------RPD----ERWGQE 309
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
265-296 |
1.34e-06 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 51.97 E-value: 1.34e-06
10 20 30
....*....|....*....|....*....|..
gi 564389119 265 PPEPEDLAIICFTSGTTGNPKGAMVTHQNIMN 296
Cdd:PRK10252 594 LSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVN 625
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
246-605 |
1.62e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 51.48 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 246 IIGLKALeDLGRVNRTKPKPPEPEDLAIICFTSGTTGNPKGAMVTHQNIMNDC----SGFIKATESafIASPEDVLISFL 321
Cdd:PRK05850 138 VIEVDLL-DLDSPRGSDARPRDLPSTAYLQYTSGSTRTPAGVMVSHRNVIANFeqlmSDYFGDTGG--VPPPDTTVVSWL 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 322 PLAH-MFETVVECV-MLChgakigffqGDIRLLMDDLKVLQPtifpvvP----RLLNRmfdriFGQANTSVKRWLLDFAS 395
Cdd:PRK05850 215 PFYHdMGLVLGVCApILG---------GCPAVLTSPVAFLQR------ParwmQLLAS-----NPHAFSAAPNFAFELAV 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 396 KRKEAELRSGIvrnnslwdklifhkiqsSLGGkVRLMITGAAPV-SATVLTFLR--AALGcqFYE-----GYGQTECTAG 467
Cdd:PRK05850 275 RKTSDDDMAGL-----------------DLGG-VLGIISGSERVhPATLKRFADrfAPFN--LREtairpSYGLAEATVY 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 468 CCLSLPGD-----------WTAGHVgapMPC---------NY-------IKLVDVEDMNYQAAKGEGEVCVKGANVFKGY 520
Cdd:PRK05850 335 VATREPGQppesvrfdyekLSAGHA---KRCetgggtplvSYgsprsptVRIVDPDTCIECPAGTVGEIWVHGDNVAAGY 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 521 LKDPART-----AEALDK-----DG-WLHTGDIGkWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIeniylrsEAVAQVFV 589
Cdd:PRK05850 412 WQKPEETertfgATLVDPspgtpEGpWLRTGDLG-FISEGELFIVGRIKDLL-IVDGRNHYPDDI-------EATIQEIT 482
|
410
....*....|....*.
gi 564389119 590 HGEslqafLIAIVVPD 605
Cdd:PRK05850 483 GGR-----VAAISVPD 493
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
265-326 |
4.52e-06 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 49.98 E-value: 4.52e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564389119 265 PPEPEDLAIICFTSGTTGNPKGAMVTHQNIMNdCSGFIkateSAFIASPEDVLISFLPLAHM 326
Cdd:cd05938 140 HVTIKSPALYIYTSGTTGLPKAARISHLRVLQ-CSGFL----SLCGVTADDVIYITLPLYHS 196
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
120-291 |
8.84e-06 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 49.12 E-value: 8.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 120 EWISYKQVAEMAECIGSALIQKGFKPCSEQFIgiFSQNRPEWVTIEQGCFTYSMVVVPLYDTLGTDAITYIVNKAELSVI 199
Cdd:PRK04319 72 EKYTYKELKELSNKFANVLKELGVEKGDRVFI--FMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 200 FADKpekaKLLLEGVENKLtPCLKIIVIMDsydnDLVERGQKCgveiIGLKAL-----EDLgrvnrtKPKPPEPEDLAII 274
Cdd:PRK04319 150 ITTP----ALLERKPADDL-PSLKHVLLVG----EDVEEGPGT----LDFNALmeqasDEF------DIEWTDREDGAIL 210
|
170 180
....*....|....*....|...
gi 564389119 275 CFTSGTTGNPKG------AMVTH 291
Cdd:PRK04319 211 HYTSGSTGKPKGvlhvhnAMLQH 233
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
256-598 |
9.78e-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: 48.58 E-value: 9.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 256 GRVNRTKPKPPEPEDLAIICFTSGTTGNPKGAMVTHQnimndcSGFIKATE----SAFIASPEDVLISFLPLAHmfetvv 331
Cdd:cd05915 140 ALGEEADPVRVPERAACGMAYTTGTTGLPKGVVYSHR------ALVLHSLAaslvDGTALSEKDVVLPVVPMFH------ 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 332 eCVMLCHGAKIGFFQGDI---------RLLMDDLKVLQPTIFPVVPRLLNrmfdrIFGQANTSVKRwlldfaskrkeael 402
Cdd:cd05915 208 -VNAWCLPYAATLVGAKQvlpgprldpASLVELFDGEGVTFTAGVPTVWL-----ALADYLESTGH-------------- 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 403 rsgivrnnslwdklifhkiqsSLGGKVRLMITGAAPvsATVLTFLRAALGCQFYEGYGQTEC--TAGCCLSLPgDWT--- 477
Cdd:cd05915 268 ---------------------RLKTLRRLVVGGSAA--PRSLIARFERMGVEVRQGYGLTETspVVVQNFVKS-HLEsls 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 478 ---AGHVGAPMPCN-YIKLVDVEDMNYQAAKGEGE----VCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNG 549
Cdd:cd05915 324 eeeKLTLKAKTGLPiPLVRLRVADEEGRPVPKDGKalgeVQLKGPWITGGYYGNEEATRSALTPDGFFRTGDIAVWDEEG 403
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 564389119 550 TLKIIDRKKHIFKLAqGEYIAPEKIENIYLRSEAVAQVFV-------HGESLQAFL 598
Cdd:cd05915 404 YVEIKDRLKDLIKSG-GEWISSVDLENALMGHPKVKEAAVvaiphpkWQERPLAVV 458
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
122-347 |
1.02e-05 |
|
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: 48.64 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 122 ISYKQVAEMAECIGSALIQKGFKPCSEqfIGIFSQNRPEWVTIEQGCFTYSMVVVPLYDTLGTDAITYIVNKAELSVIF- 200
Cdd:cd05968 92 LTYGELLYEVKRLANGLRALGVGKGDR--VGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALIt 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 201 ADkpekaKLLLEGVENKLTPCL-KIIVIMDSYDNDLVERGQKCGVeiigLKALEDLGRVNRTKPKPP------EPEDLAI 273
Cdd:cd05968 170 AD-----GFTRRGREVNLKEEAdKACAQCPTVEKVVVVRHLGNDF----TPAKGRDLSYDEEKETAGdgaertESEDPLM 240
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564389119 274 ICFTSGTTGNPKGAMVTHqnimndcSGF-IKATESA---FIASPEDVLISFLPLAHMFETVVECVMLCHGAKIGFFQG 347
Cdd:cd05968 241 IIYTSGTTGKPKGTVHVH-------AGFpLKAAQDMyfqFDLKPGDLLTWFTDLGWMMGPWLIFGGLILGATMVLYDG 311
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
452-602 |
1.08e-05 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 48.87 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 452 GCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYIKLVdVEDMNYQAAKGEGEVCVKGANVFKGYLKDPArtaEAL 531
Cdd:PRK06060 286 GIPILDGIGSTEVGQTFVSNRVDEWRLGTLGRVLPPYEIRVV-APDGTTAGPGVEGDLWVRGPAIAKGYWNRPD---SPV 361
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564389119 532 DKDGWLHTGDIGKWLPNGTLKIIDRKKHIfKLAQGEYIAPEKIENIYLRSEAVAQVFVHG-------ESLQAFLIAIV 602
Cdd:PRK06060 362 ANEGWLDTRDRVCIDSDGWVTYRCRADDT-EVIGGVNVDPREVERLIIEDEAVAEAAVVAvrestgaSTLQAFLVATS 438
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
268-589 |
5.19e-05 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 47.09 E-value: 5.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 268 PEDLAIICFTSGTTGNPKGAMVTHQNIMNDCSGFIKAtesaFIASPEDvlisflplahmfetvveCVMlcHGAKIGFFQG 347
Cdd:PRK05691 2332 PQHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIER----FGMRADD-----------------CEL--HFYSINFDAA 2388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 348 DIRLLmddlkvlqptifpvVPRLLN-RMFDRIFGQantsvkrWlldfaskrkEAELRSGIVRNNSLwDKLIFHKIQSS-- 424
Cdd:PRK05691 2389 SERLL--------------VPLLCGaRVVLRAQGQ-------W---------GAEEICQLIREQQV-SILGFTPSYGSql 2437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 425 ---LGGK-----VRLMITGAAPVSATVLTFLRAALGCQ-FYEGYGQTE-------CTAGccLSLPGDWTAGHVGAPMPCN 488
Cdd:PRK05691 2438 aqwLAGQgeqlpVRMCITGGEALTGEHLQRIRQAFAPQlFFNAYGPTEtvvmplaCLAP--EQLEEGAASVPIGRVVGAR 2515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 489 YIKLVDvEDMNYQAAKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLH-------TGDIGKWLPNGTLKIIDRKKHIF 561
Cdd:PRK05691 2516 VAYILD-ADLALVPQGATGELYVGGAGLAQGYHDRPGLTAERFVADPFAAdggrlyrTGDLVRLRADGLVEYVGRIDHQV 2594
|
330 340
....*....|....*....|....*...
gi 564389119 562 KLaQGEYIAPEKIENIYLRSEAVAQVFV 589
Cdd:PRK05691 2595 KI-RGFRIELGEIESRLLEHPAVREAVV 2621
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
260-591 |
6.47e-05 |
|
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: 46.03 E-value: 6.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 260 RTKPKPPEPEDLAIICFTSGTTGNPKGAMVTHqnimndcSGF-IKATES---AFIASPEDVLISFLPLAHMF--ETVVEC 333
Cdd:cd17634 223 EHQPEAMNAEDPLFILYTSGTTGKPKGVLHTT-------GGYlVYAATTmkyVFDYGPGDIYWCTADVGWVTghSYLLYG 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 334 VMLChGAKIGFFQGdirllmddlKVLQPTifpvvPRLLNRMFDR----IFGQANTSVKrwlldfaSKRKEAelrsgivrn 409
Cdd:cd17634 296 PLAC-GATTLLYEG---------VPNWPT-----PARMWQVVDKhgvnILYTAPTAIR-------ALMAAG--------- 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 410 nslwDKLIFHKIQSSLggkvRLMITGAAPVSATVLTFLRAALG---CQFYEGYGQTECTAGCCLSLPG--DWTAGHVGAP 484
Cdd:cd17634 345 ----DDAIEGTDRSSL----RILGSVGEPINPEAYEWYWKKIGkekCPVVDTWWQTETGGFMITPLPGaiELKAGSATRP 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 485 MPCNYIKLVDVEDmNYQAAKGEGEVCVKGA--NVFKGYLKDPARTAEALDK--DGWLHTGDIGKWLPNGTLKIIDRKKHI 560
Cdd:cd17634 417 VFGVQPAVVDNEG-HPQPGGTEGNLVITDPwpGQTRTLFGDHERFEQTYFStfKGMYFSGDGARRDEDGYYWITGRSDDV 495
|
330 340 350
....*....|....*....|....*....|.
gi 564389119 561 FKLAqGEYIAPEKIENIYLRSEAVAQVFVHG 591
Cdd:cd17634 496 INVA-GHRLGTAEIESVLVAHPKVAEAAVVG 525
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
264-618 |
1.12e-04 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 45.04 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 264 KPPEP--EDLAIICFTSGTTGNPKGAMVTHQNIMNDCSgfikATEsAFIASPEDVLISfLPLAHmfetvvecvmlchgak 341
Cdd:PRK07824 28 RVGEPidDDVALVVATSGTTGTPKGAMLTAAALTASAD----ATH-DRLGGPGQWLLA-LPAHH---------------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 342 IGFFQGDIRLLmddLKVLQPTIFPVvprllNRMFDrifgqantsvkrwLLDFAskRKEAELRSGiVRNNSLWD-KLIfhK 420
Cdd:PRK07824 86 IAGLQVLVRSV---IAGSEPVELDV-----SAGFD-------------PTALP--RAVAELGGG-RRYTSLVPmQLA--K 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 421 IQSSLGGKVRL-----MITGAAPVSATVLTflRA-ALGCQFYEGYGQTEcTAGCCLslpgdwtagHVGAPMPCNYIKLVD 494
Cdd:PRK07824 140 ALDDPAATAALaeldaVLVGGGPAPAPVLD--AAaAAGINVVRTYGMSE-TSGGCV---------YDGVPLDGVRVRVED 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 495 vedmnyqaakgeGEVCVKGANVFKGY--LKDPARTAEaldkDGWLHTGDIGKwLPNGTLKIIDRKKHIFKLAqGEYIAPE 572
Cdd:PRK07824 208 ------------GRIALGGPTLAKGYrnPVDPDPFAE----PGWFRTDDLGA-LDDGVLTVLGRADDAISTG-GLTVLPQ 269
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 564389119 573 KIENIYLRSEAVAQVFVHG---ESLQAFLIAIVVPDVEILPSWAQKRGF 618
Cdd:PRK07824 270 VVEAALATHPAVADCAVFGlpdDRLGQRVVAAVVGDGGPAPTLEALRAH 318
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
123-613 |
5.05e-04 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 43.18 E-value: 5.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 123 SYKQVAEMAECIGSALIQKGFKpcSEQFIGIFSQNRPEWVTIEQGCFTYSmVVVPLYDT-LGTDAITYIVNKAelsvifa 201
Cdd:cd05939 5 TFRELNEYSNKVANFFQAQGYR--SGDVVALFMENRLEFVALWLGLAKIG-VETALINSnLRLESLLHCITVS------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 202 dkpeKAKLLlegVENKLTPCLKiivimdsydndlvergqkcgveiiglkaledlgrvnRTKPKPPEPEDL---AIICF-- 276
Cdd:cd05939 75 ----KAKAL---IFNLLDPLLT------------------------------------QSSTEPPSQDDVnfrDKLFYiy 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 277 TSGTTGNPKGAMVTHQNIMNDCSGFIKatesAFIASPEDVLISFLPLAHMFETVVeCV--MLCHGAKIgffqgDIRL--- 351
Cdd:cd05939 112 TSGTTGLPKAAVIVHSRYYRIAAGAYY----AFGMRPEDVVYDCLPLYHSAGGIM-GVgqALLHGSTV-----VIRKkfs 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 352 ---LMDDLKVLQPTIfpvvprllnrmfdrifGQANTSVKRWLLdfASKRKEAELRsgivrnnslwdklifHKIQSSLGGK 428
Cdd:cd05939 182 asnFWDDCVKYNCTI----------------VQYIGEICRYLL--AQPPSEEEQK---------------HNVRLAVGNG 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 429 VRLMITgaapvSATVLTFLRAALGcqfyEGYGQTECTAgcclSLpGDWTaGHVGApmpCNY----------IKLVDVEDM 498
Cdd:cd05939 229 LRPQIW-----EQFVRRFGIPQIG----EFYGATEGNS----SL-VNID-NHVGA---CGFnsrilpsvypIRLIKVDED 290
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389119 499 NYQAAKGEGEVCVK------GANV-----------FKGYLKDPArTAEALDKDGWLH------TGDIGKWLPNGTLKIID 555
Cdd:cd05939 291 TGELIRDSDGLCIPcqpgepGLLVgkiiqndplrrFDGYVNEGA-TNKKIARDVFKKgdsaflSGDVLVMDELGYLYFKD 369
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564389119 556 RKKHIFKLaQGEYIAPEKIENIYLRSEAVAQVFVHGESL-----QAFLIAIVVP----DVEI--------LPSWA 613
Cdd:cd05939 370 RTGDTFRW-KGENVSTTEVEGILSNVLGLEDVVVYGVEVpgvegRAGMAAIVDPerkvDLDRfsavlaksLPPYA 443
|
|
| |
