|
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 ... |
116-694 |
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: 992.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 116 QPYEWISYKEVAERAEYVGSALLHRGFKPSPDQFVGIFAQNRPEWTIVELGCYTYSMVAVPLYDTLGAEAITYIINKADL 195
Cdd:cd05927 1 GPYEWISYKEVAERADNIGSALRSLGGKPAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 196 SVVFCDSpekaklllsnvekgetpvlrtivlmnpfdndlvergkkcGVELVSLKDIEEEGKANREKPKPPKPDDLAVVCF 275
Cdd:cd05927 81 SIVFCDA---------------------------------------GVKVYSLEEFEKLGKKNKVPPPPPKPEDLATICY 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 276 TSGTTGNPKGAMLSHKNIVSNSAGFMKVTEDLMFPSTQDVLISFLPLAHMFERVVECVVLCHGARIGFFQGDIRLLMDDL 355
Cdd:cd05927 122 TSGTTGNPKGVMLTHGNIVSNVAGVFKILEILNKINPTDVYISYLPLAHIFERVVEALFLYHGAKIGFYSGDIRLLLDDI 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 356 KVLQPTIFPVVPRLLNRMFDRIFG--QANTPVKRWMLDFASKRKEAELRSGIVRNDSFWDKIIFHKVQASLGGKVRLMVT 433
Cdd:cd05927 202 KALKPTVFPGVPRVLNRIYDKIFNkvQAKGPLKRKLFNFALNYKLAELRSGVVRASPFWDKLVFNKIKQALGGNVRLMLT 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 434 GAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCSLTIPGDWTAGHVGAPMPCNHVKLVDVEEMNYFA--SKGEGEVCIK 511
Cdd:cd05927 282 GSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAEVKLVDVPEMNYDAkdPNPRGEVCIR 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 512 GSNVFQGYLKDDEKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENVYTRSEPVVQVFVHGE 591
Cdd:cd05927 362 GPNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLSQGEYVAPEKIENIYARSPFVAQIFVYGD 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 592 SLQAFLVGIVVPDPDNVMNWAKKR-KFEGSYEELCKNKDFKNAVLEDLLKLGKEAGLKTFEQVKDIALHSEMFAIENGLL 670
Cdd:cd05927 442 SLKSFLVAIVVPDPDVLKEWAASKgGGTGSFEELCKNPEVKKAILEDLVRLGKENGLKGFEQVKAIHLEPEPFSVENGLL 521
|
570 580
....*....|....*....|....
gi 1270536209 671 TPTLKAKRPELRKYFKDEIDELYA 694
Cdd:cd05927 522 TPTFKLKRPQLKKYYKKQIDEMYK 545
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
86-694 |
0e+00 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 710.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 86 YDDVKTIYDIFQRGRRVSNNGPCLGHRKPNQ----PYEWISYKEVAERAEYVGSALLHRGFKPSpdQFVGIFAQNRPEWT 161
Cdd:PLN02736 40 HPEIGTLHDNFVYAVETFRDYKYLGTRIRVDgtvgEYKWMTYGEAGTARTAIGSGLVQHGIPKG--ACVGLYFINRPEWL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 162 IVELGCYTYSMVAVPLYDTLGAEAITYIINKADLSVVFCdSPEKAKLLLSNVekGETPVLRTIVLMNPFDNDLVERGKKC 241
Cdd:PLN02736 118 IVDHACSAYSYVSVPLYDTLGPDAVKFIVNHAEVAAIFC-VPQTLNTLLSCL--SEIPSVRLIVVVGGADEPLPSLPSGT 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 242 GVELVSLKDIEEEGKANREKPKPPKPDDLAVVCFTSGTTGNPKGAMLSHKNIVSNSAGFMKVTEdlMFPStqDVLISFLP 321
Cdd:PLN02736 195 GVEIVTYSKLLAQGRSSPQPFRPPKPEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTK--FYPS--DVHISYLP 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 322 LAHMFERVVECVVLCHGARIGFFQGDIRLLMDDLKVLQPTIFPVVPRLLNRMFDRIFG--QANTPVKRWMLDFASKRKEA 399
Cdd:PLN02736 271 LAHIYERVNQIVMLHYGVAVGFYQGDNLKLMDDLAALRPTIFCSVPRLYNRIYDGITNavKESGGLKERLFNAAYNAKKQ 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 400 ELRSGivRNDS-FWDKIIFHKVQASLGGKVRLMVTGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCSLTIPGDWTAG 478
Cdd:PLN02736 351 ALENG--KNPSpMWDRLVFNKIKAKLGGRVRFMSSGASPLSPDVMEFLRICFGGRVLEGYGMTETSCVISGMDEGDNLSG 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 479 HVGAPMPCNHVKLVDVEEMNYFASKG---EGEVCIKGSNVFQGYLKDDEKTAEALDKDGWLHTGDIGKWLPNGTLKIIDR 555
Cdd:PLN02736 429 HVGSPNPACEVKLVDVPEMNYTSEDQpypRGEICVRGPIIFKGYYKDEVQTREVIDEDGWLHTGDIGLWLPGGRLKIIDR 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 556 KKHIFKLAQGEYIAPEKIENVYTRSEPVVQVFVHGESLQAFLVGIVVPDPDNVMNWAKKRKFE-GSYEELCKNKDFKNAV 634
Cdd:PLN02736 509 KKNIFKLAQGEYIAPEKIENVYAKCKFVAQCFVYGDSLNSSLVAVVVVDPEVLKAWAASEGIKyEDLKQLCNDPRVRAAV 588
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 635 LEDLLKLGKEAGLKTFEQVKDIALHSEMFAIENGLLTPTLKAKRPELRKYFKDEIDELYA 694
Cdd:PLN02736 589 LADMDAVGREAQLRGFEFAKAVTLVPEPFTVENGLLTPTFKVKRPQAKAYFAKAISDMYA 648
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
86-695 |
0e+00 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 545.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 86 YDDVKTIYDIFQRGRRVSNNGPCLgHRKPNQPYEWISYKEVAERAEYVGSALLHRGFKPspDQFVGIFAQNRPEWTIVEL 165
Cdd:COG1022 7 VPPADTLPDLLRRRAARFPDRVAL-REKEDGIWQSLTWAEFAERVRALAAGLLALGVKP--GDRVAILSDNRPEWVIADL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 166 GCYTYSMVAVPLYDTLGAEAITYIINKADLSVVFCDSPEKAKLLLSnvEKGETPVLRTIVLMNPfdndlveRGKKCGVEL 245
Cdd:COG1022 84 AILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQEQLDKLLE--VRDELPSLRHIVVLDP-------RGLRDDPRL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 246 VSLKDIEEEGKANR------EKPKPPKPDDLAVVCFTSGTTGNPKGAMLSHKNIVSNSAGFMKVtedlMFPSTQDVLISF 319
Cdd:COG1022 155 LSLDELLALGREVAdpaeleARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLER----LPLGPGDRTLSF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 320 LPLAHMFERVVECVVLCHGARIGFfQGDIRLLMDDLKVLQPTIFPVVPRLLNRMFDRIFGQAN--TPVKRWMLDFA---S 394
Cdd:COG1022 231 LPLAHVFERTVSYYALAAGATVAF-AESPDTLAEDLREVKPTFMLAVPRVWEKVYAGIQAKAEeaGGLKRKLFRWAlavG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 395 KRKEAELRSGivRNDSFW--------DKIIFHKVQASLGGKVRLMVTGAAPVSPTVLTFLRAaLGCQFYEGYGQTECTAG 466
Cdd:COG1022 310 RRYARARLAG--KSPSLLlrlkhalaDKLVFSKLREALGGRLRFAVSGGAALGPELARFFRA-LGIPVLEGYGLTETSPV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 467 CSLTIPGDWTAGHVGAPMPCNHVKLVDveemnyfaskgEGEVCIKGSNVFQGYLKDDEKTAEALDKDGWLHTGDIGKWLP 546
Cdd:COG1022 387 ITVNRPGDNRIGTVGPPLPGVEVKIAE-----------DGEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELDE 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 547 NGTLKIIDRKKHIFKLAQGEYIAPEKIENVYTRSEPVVQVFVHGESlQAFLVGIVVPDPDNVMNWAKKR-KFEGSYEELC 625
Cdd:COG1022 456 DGFLRITGRKKDLIVTSGGKNVAPQPIENALKASPLIEQAVVVGDG-RPFLAALIVPDFEALGEWAEENgLPYTSYAELA 534
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 626 KNKDFKNAVLEDLLKLgkEAGLKTFEQVKDIALHSEMFAIENGLLTPTLKAKRPELRKYFKDEIDELYAN 695
Cdd:COG1022 535 QDPEVRALIQEEVDRA--NAGLSRAEQIKRFRLLPKEFTIENGELTPTLKLKRKVILEKYADLIEALYAG 602
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
116-681 |
7.97e-172 |
|
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: 499.04 E-value: 7.97e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 116 QPYEWISYKEVAERAEYVGSALLHRGFKPspDQFVGIFAQNRPEWTIVELGCYTYSMVAVPLYDTLGAEAITYIINKADL 195
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLIALGVEP--GDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 196 SVVFCDspekaklllsnvekgetpvlrtivlmnpfdndlvergkkcgvelvslkdieeegkanrekpkppKPDDLAVVCF 275
Cdd:cd05907 79 KALFVE----------------------------------------------------------------DPDDLATIIY 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 276 TSGTTGNPKGAMLSHKNIVSNSAGFMKVTEdlmfPSTQDVLISFLPLAHMFERV-VECVVLCHGARIGFFQgDIRLLMDD 354
Cdd:cd05907 95 TSGTTGRPKGVMLSHRNILSNALALAERLP----ATEGDRHLSFLPLAHVFERRaGLYVPLLAGARIYFAS-SAETLLDD 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 355 LKVLQPTIFPVVPRLLNRMFDRIFGQANTPVKRWMLDFASkrkeaelrsgivrndsfwdkiifhkvqaslGGKVRLMVTG 434
Cdd:cd05907 170 LSEVRPTVFLAVPRVWEKVYAAIKVKAVPGLKRKLFDLAV------------------------------GGRLRFAASG 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 435 AAPVSPTVLTFLRAaLGCQFYEGYGQTECTAGCSLTIPGDWTAGHVGAPMPCNHVKLVDveemnyfaskgEGEVCIKGSN 514
Cdd:cd05907 220 GAPLPAELLHFFRA-LGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVEVRIAD-----------DGEILVRGPN 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 515 VFQGYLKDDEKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENVYTRSEPVVQVFVHGESlQ 594
Cdd:cd05907 288 VMLGYYKNPEATAEALDADGWLHTGDLGEIDEDGFLHITGRKKDLIITSGGKNISPEPIENALKASPLISQAVVIGDG-R 366
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 595 AFLVGIVVPDPDNVMNWAKKR-KFEGSYEELCKNKDFKNAVLEDLLKLGkeAGLKTFEQVKDIALHSEMFAIENGLLTPT 673
Cdd:cd05907 367 PFLVALIVPDPEALEAWAEEHgIAYTDVAELAANPAVRAEIEAAVEAAN--ARLSRYEQIKKFLLLPEPFTIENGELTPT 444
|
....*...
gi 1270536209 674 LKAKRPEL 681
Cdd:cd05907 445 LKLKRPVI 452
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
88-695 |
3.16e-163 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 484.70 E-value: 3.16e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 88 DVKTIYDIFQRGRRVSNNGPCLGHRKPNQ----PYEWISYKEVAERAEYVGSALLHRGFKPSPDqfVGIFAQNRPEWTIV 163
Cdd:PLN02430 40 DITTAWDIFSKSVEKYPDNKMLGWRRIVDgkvgPYMWKTYKEVYEEVLQIGSALRASGAEPGSR--VGIYGSNCPQWIVA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 164 ELGCYTYSMVAVPLYDTLGAEAITYIINKADLSVVFCDSpEKAKLLLsNVEKGETPVLRTIVLMNPFDNDLVERGKKCGV 243
Cdd:PLN02430 118 MEACAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVFVQD-KKIKELL-EPDCKSAKRLKAIVSFTSVTEEESDKASQIGV 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 244 ELVSLKDIEEEGKANREKPKPPKPDDLAVVCFTSGTTGNPKGAMLSHKNIVSNSAG---FMKVTEDLMfpSTQDVLISFL 320
Cdd:PLN02430 196 KTYSWIDFLHMGKENPSETNPPKPLDICTIMYTSGTSGDPKGVVLTHEAVATFVRGvdlFMEQFEDKM--THDDVYLSFL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 321 PLAHMFERVVECVVLCHGARIGFFQGDIRLLMDDLKVLQPTIFPVVPRLLNRMFDRIFG--QANTPVKRWMLDFASKRKE 398
Cdd:PLN02430 274 PLAHILDRMIEEYFFRKGASVGYYHGDLNALRDDLMELKPTLLAGVPRVFERIHEGIQKalQELNPRRRLIFNALYKYKL 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 399 AELRSGIVRNDS--FWDKIIFHKVQASLGGKVRLMVTGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCSLTIPGDWT 476
Cdd:PLN02430 354 AWMNRGYSHKKAspMADFLAFRKVKAKLGGRLRLLISGGAPLSTEIEEFLRVTSCAFVVQGYGLTETLGPTTLGFPDEMC 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 477 A-GHVGAPMPCNHVKLVDVEEMNY--FASKGEGEVCIKGSNVFQGYLKDDEKTAEALdKDGWLHTGDIGKWLPNGTLKII 553
Cdd:PLN02430 434 MlGTVGAPAVYNELRLEEVPEMGYdpLGEPPRGEICVRGKCLFSGYYKNPELTEEVM-KDGWFHTGDIGEILPNGVLKII 512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 554 DRKKHIFKLAQGEYIAPEKIENVYTRSEPVVQVFVHGESLQAFLVGIVVPDPDNVMNWAKKRKFEGSYEELCKNKDFKNA 633
Cdd:PLN02430 513 DRKKNLIKLSQGEYVALEYLENVYGQNPIVEDIWVYGDSFKSMLVAVVVPNEENTNKWAKDNGFTGSFEELCSLPELKEH 592
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1270536209 634 VLEDLLKLGKEAGLKTFEQVKDIALHSEMFAIENGLLTPTLKAKRPELRKYFKDEIDELYAN 695
Cdd:PLN02430 593 ILSELKSTAEKNKLRGFEYIKGVILETKPFDVERDLVTATLKKRRNNLLKYYQVEIDEMYRK 654
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
117-678 |
8.09e-162 |
|
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: 475.55 E-value: 8.09e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 117 PYEWISYKEVAERAEYVGSALLHRGFKPspDQFVGIFAQNRPEWTIVELGCYTYSMVAVPLYDTLGAEAITYIINKADLS 196
Cdd:cd17639 2 EYKYMSYAEVWERVLNFGRGLVELGLKP--GDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 197 VVFCDspekaklllsnvekgetpvlrtivlmnpfdndlvergkkcgvelvslkdieeegkanrekpkpPKPDDLAVVCFT 276
Cdd:cd17639 80 AIFTD---------------------------------------------------------------GKPDDLACIMYT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 277 SGTTGNPKGAMLSHKNIVSNSAGFMKVTEDLMFPstQDVLISFLPLAHMFERVVECVVLCHGARIGFfqGDIRLLMD--- 353
Cdd:cd17639 97 SGSTGNPKGVMLTHGNLVAGIAGLGDRVPELLGP--DDRYLAYLPLAHIFELAAENVCLYRGGTIGY--GSPRTLTDksk 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 354 -----DLKVLQPTIFPVVPRLLNRMFDRIFGQANTP--VKRWMLDFASKRKEAELRSGIvrnDS-FWDKIIFHKVQASLG 425
Cdd:cd17639 173 rgckgDLTEFKPTLMVGVPAIWDTIRKGVLAKLNPMggLKRTLFWTAYQSKLKALKEGP---GTpLLDELVFKKVRAALG 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 426 GKVRLMVTGAAPVSPTVLTFLrAALGCQFYEGYGQTECTAGCSLTIPGDWTAGHVGAPMPCNHVKLVDVEEMNYFASKGE 505
Cdd:cd17639 250 GRLRYMLSGGAPLSADTQEFL-NIVLCPVIQGYGLTETCAGGTVQDPGDLETGRVGPPLPCCEIKLVDWEEGGYSTDKPP 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 506 --GEVCIKGSNVFQGYLKDDEKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENVYTRSEPV 583
Cdd:cd17639 329 prGEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQNGEYIALEKLESIYRSNPLV 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 584 VQVFVHGESLQAFLVGIVVPDPDNVMNWAKKRKF-EGSYEELCKNKDFKNAVLEDLLKLGKEAGLKTFEQVKDIALHSEM 662
Cdd:cd17639 409 NNICVYADPDKSYPVAIVVPNEKHLTKLAEKHGViNSEWEELCEDKKLQKAVLKSLAETARAAGLEKFEIPQGVVLLDEE 488
|
570
....*....|....*.
gi 1270536209 663 FAIENGLLTPTLKAKR 678
Cdd:cd17639 489 WTPENGLVTAAQKLKR 504
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
88-698 |
2.56e-160 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 477.41 E-value: 2.56e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 88 DVKTIYDIFQRGRRVSNNGPCLGHRKPNQ----PYEWISYKEVAERAEYVGSALLHRGFKPSpdQFVGIFAQNRPEWTIV 163
Cdd:PLN02861 41 DIDSPWQFFSDAVKKYPNNQMLGRRQVTDskvgPYVWLTYKEVYDAAIRIGSAIRSRGVNPG--DRCGIYGSNCPEWIIA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 164 ELGCYTYSMVAVPLYDTLGAEAITYIINKADLSVVFCDSpEKAKLLLSnVEKGETPVLRTIVLMNPFDNDLVERGKKCGV 243
Cdd:PLN02861 119 MEACNSQGITYVPLYDTLGANAVEFIINHAEVSIAFVQE-SKISSILS-CLPKCSSNLKTIVSFGDVSSEQKEEAEELGV 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 244 ELVSLKDIEEEGKANREKPKPPKpDDLAVVCFTSGTTGNPKGAMLSHKNIVsnsAGFMKvTEDLMF-----PSTQDVLIS 318
Cdd:PLN02861 197 SCFSWEEFSLMGSLDCELPPKQK-TDICTIMYTSGTTGEPKGVILTNRAII---AEVLS-TDHLLKvtdrvATEEDSYFS 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 319 FLPLAHMFERVVECVVLCHGARIGFFQGDIRLLMDDLKVLQPTIFPVVPRLlnrmFDRIFG------QANTPVKRWMLDF 392
Cdd:PLN02861 272 YLPLAHVYDQVIETYCISKGASIGFWQGDIRYLMEDVQALKPTIFCGVPRV----YDRIYTgimqkiSSGGMLRKKLFDF 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 393 ASKRKEAELRSGIVRNDS--FWDKIIFHKVQASLGGKVRLMVTGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCSLT 470
Cdd:PLN02861 348 AYNYKLGNLRKGLKQEEAspRLDRLVFDKIKEGLGGRVRLLLSGAAPLPRHVEEFLRVTSCSVLSQGYGLTESCGGCFTS 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 471 IPGDWT-AGHVGAPMPCNHVKLVDVEEMNY--FASKGEGEVCIKGSNVFQGYLKDDEKTAEALdKDGWLHTGDIGKWLPN 547
Cdd:PLN02861 428 IANVFSmVGTVGVPMTTIEARLESVPEMGYdaLSDVPRGEICLRGNTLFSGYHKRQDLTEEVL-IDGWFHTGDIGEWQPN 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 548 GTLKIIDRKKHIFKLAQGEYIAPEKIENVYTRSEPVVQVFVHGESLQAFLVGIVVPDPDNVMNWAKKRKFEGSYEELCKN 627
Cdd:PLN02861 507 GAMKIIDRKKNIFKLSQGEYVAVENLENTYSRCPLIASIWVYGNSFESFLVAVVVPDRQALEDWAANNNKTGDFKSLCKN 586
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1270536209 628 KDFKNAVLEDLLKLGKEAGLKTFEQVKDIALHSEMFAIENGLLTPTLKAKRPELRKYFKDEIDELYANNKV 698
Cdd:PLN02861 587 LKARKYILDELNSTGKKLQLRGFEMLKAIHLEPNPFDIERDLITPTFKLKRPQLLKYYKDCIDQLYSEAKG 657
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
87-697 |
1.99e-156 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 467.58 E-value: 1.99e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 87 DDVKTIYDIFQRGRRVSNNGPCLGHR-----KPNQpYEWISYKEVAERAEYVGSALLHRGFKPspDQFVGIFAQNRPEWT 161
Cdd:PLN02614 42 EGMDSCWDVFRMSVEKYPNNPMLGRReivdgKPGK-YVWQTYQEVYDIVIKLGNSLRSVGVKD--EAKCGIYGANSPEWI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 162 IVELGCYTYSMVAVPLYDTLGAEAITYIINKADLSVVFCDspEKAKLLLSNVEKGETPVLRTIVLMNPFDNDLVERGKKC 241
Cdd:PLN02614 119 ISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVE--EKKISELFKTCPNSTEYMKTVVSFGGVSREQKEEAETF 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 242 GVELVSLKDIEEEGKANREKPKPPKPDDLAVVCFTSGTTGNPKGAMLSHKNIVSNSAGFMK----VTEDLmfpSTQDVLI 317
Cdd:PLN02614 197 GLVIYAWDEFLKLGEGKQYDLPIKKKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRllksANAAL---TVKDVYL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 318 SFLPLAHMFERVVECVVLCHGARIGFFQGDIRLLMDDLKVLQPTIFPVVPRLLNRMFDRIFGQANTP--VKRWMLDFASK 395
Cdd:PLN02614 274 SYLPLAHIFDRVIEECFIQHGAAIGFWRGDVKLLIEDLGELKPTIFCAVPRVLDRVYSGLQKKLSDGgfLKKFVFDSAFS 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 396 RKEAELRSGI--VRNDSFWDKIIFHKVQASLGGKVRLMVTGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCSLTIPG 473
Cdd:PLN02614 354 YKFGNMKKGQshVEASPLCDKLVFNKVKQGLGGNVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTESCAGTFVSLPD 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 474 DW-TAGHVGAPMPCNHVKLVDVEEMNY--FASKGEGEVCIKGSNVFQGYLKDDEKTAEALdKDGWLHTGDIGKWLPNGTL 550
Cdd:PLN02614 434 ELdMLGTVGPPVPNVDIRLESVPEMEYdaLASTPRGEICIRGKTLFSGYYKREDLTKEVL-IDGWLHTGDVGEWQPNGSM 512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 551 KIIDRKKHIFKLAQGEYIAPEKIENVYTRSEPVVQVFVHGESLQAFLVGIVVPDPDNVMNWAKKRKFEGSYEELCKNKDF 630
Cdd:PLN02614 513 KIIDRKKNIFKLSQGEYVAVENIENIYGEVQAVDSVWVYGNSFESFLVAIANPNQQILERWAAENGVSGDYNALCQNEKA 592
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1270536209 631 KNAVLEDLLKLGKEAGLKTFEQVKDIALHSEMFAIENGLLTPTLKAKRPELRKYFKDEIDELYANNK 697
Cdd:PLN02614 593 KEFILGELVKMAKEKKMKGFEIIKAIHLDPVPFDMERDLLTPTFKKKRPQLLKYYQSVIDEMYKTTN 659
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
117-694 |
2.55e-138 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 421.83 E-value: 2.55e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 117 PYEWISYKEVAERAEYVGSALLHRGFKPspDQFVGIFAQNRPEWTIVELGCYTYSMVAVPLYDTLGAEAITYIINKADLS 196
Cdd:PLN02387 103 EYEWITYGQVFERVCNFASGLVALGHNK--EERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVT 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 197 VVFCDSPEKAKLLlSNVEKGETpVLRTIVLMNPFDNDLVERGKKCGVELVSLKDIEEEGKANREKPKPPKPDDLAVVCFT 276
Cdd:PLN02387 181 TVICDSKQLKKLI-DISSQLET-VKRVIYMDDEGVDSDSSLSGSSNWTVSSFSEVEKLGKENPVDPDLPSPNDIAVIMYT 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 277 SGTTGNPKGAMLSHKNIVSNSAGFMKVTEDLmfpSTQDVLISFLPLAHMFERVVECVVLCHGARIGFfqGDIRLLMD--- 353
Cdd:PLN02387 259 SGSTGLPKGVMMTHGNIVATVAGVMTVVPKL---GKNDVYLAYLPLAHILELAAESVMAAVGAAIGY--GSPLTLTDtsn 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 354 --------DLKVLQPTIFPVVPRLLNRMFDRIFGQANTP---VKRwMLDFASKRKEAELR------SGIVRndSFWDKII 416
Cdd:PLN02387 334 kikkgtkgDASALKPTLMTAVPAILDRVRDGVRKKVDAKgglAKK-LFDIAYKRRLAAIEgswfgaWGLEK--LLWDALV 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 417 FHKVQASLGGKVRLMVTGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCSLTIPGDWTAGHVGAPMPCNHVKLVDVEE 496
Cdd:PLN02387 411 FKKIRAVLGGRIRFMLSGGAPLSGDTQRFINICLGAPIGQGYGLTETCAGATFSEWDDTSVGRVGPPLPCCYVKLVSWEE 490
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 497 MNYFASKG---EGEVCIKGSNVFQGYLKDDEKTAEA--LDKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIA 569
Cdd:PLN02387 491 GGYLISDKpmpRGEIVIGGPSVTLGYFKNQEKTDEVykVDERGmrWFYTGDIGQFHPDGCLEIIDRKKDIVKLQHGEYVS 570
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 570 PEKIENVYTRSEPVVQVFVHGESLQAFLVGIVVPDPDNVMNWAKKRKFE-GSYEELCKNKDFKNAVLEDLLKLGKEAGLK 648
Cdd:PLN02387 571 LGKVEAALSVSPYVDNIMVHADPFHSYCVALVVPSQQALEKWAKKAGIDySNFAELCEKEEAVKEVQQSLSKAAKAARLE 650
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 1270536209 649 TFEQVKDIALHSEMFAIENGLLTPTLKAKRPELRKYFKDEIDELYA 694
Cdd:PLN02387 651 KFEIPAKIKLLPEPWTPESGLVTAALKLKREQIRKKFKDDLKKLYE 696
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
117-563 |
9.34e-131 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 392.83 E-value: 9.34e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 117 PYEWISYKEVAERAEYVGSALLHRGFKPspDQFVGIFAQNRPEWTIVELGCYTYSMVAVPLYDTLGAEAITYIINKADLS 196
Cdd:pfam00501 18 EGRRLTYRELDERANRLAAGLRALGVGK--GDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSGAK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 197 VVFCDSPEKAKLLLSNVEKGETPVLRTIVLMNPFDNDLVergkkcgvelvsLKDIEEEGKANREKPKPPKPDDLAVVCFT 276
Cdd:pfam00501 96 VLITDDALKLEELLEALGKLEVVKLVLVLDRDPVLKEEP------------LPEEAKPADVPPPPPPPPDPDDLAYIIYT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 277 SGTTGNPKGAMLSHKNIVSNSAGFMKVTEDLMFPSTQDVLISFLPLAHMFERVVEC-VVLCHGARIGFFQGDIRL----L 351
Cdd:pfam00501 164 SGTTGKPKGVMLTHRNLVANVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSLGLlGPLLAGATVVLPPGFPALdpaaL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 352 MDDLKVLQPTIFPVVPRLLNRMFDrifgqantpvkrwmldfaSKRKEAELRSGivrndsfwdkiifhkvqaslggkVRLM 431
Cdd:pfam00501 244 LELIERYKVTVLYGVPTLLNMLLE------------------AGAPKRALLSS-----------------------LRLV 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 432 VTGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCSLTIPGDW---TAGHVGAPMPCNHVKLVDVEEMNYFASKGEGEV 508
Cdd:pfam00501 283 LSGGAPLPPELARRFRELFGGALVNGYGLTETTGVVTTPLPLDEdlrSLGSVGRPLPGTEVKIVDDETGEPVPPGEPGEL 362
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1270536209 509 CIKGSNVFQGYLKDDEKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLA 563
Cdd:pfam00501 363 CVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
121-695 |
1.28e-112 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 355.05 E-value: 1.28e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 121 ISYKEVAERAEYVGSALLHRGFKPspDQFVGIFAQNRPEWTIVELGCYTYSMVAVPLYDTLGAEAITYIINKADLSVVFC 200
Cdd:PTZ00216 122 ITYAELWERIVNFGRGLAELGLTK--GSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAIVC 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 201 DSpEKAKLLLSNVEKGETPVLRTIVLmnpfdNDLVERGKKCGVELVSLKDIEEEGKANREKPKPPKP---DDLAVVCFTS 277
Cdd:PTZ00216 200 NG-KNVPNLLRLMKSGGMPNTTIIYL-----DSLPASVDTEGCRLVAWTDVVAKGHSAGSHHPLNIPennDDLALIMYTS 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 278 GTTGNPKGAMLSHKNIVsnsAGFM----KVTEDLMFPSTQDVLISFLPLAHMFERVVECVVLCHGARIGFfqGDIRLLMD 353
Cdd:PTZ00216 274 GTTGDPKGVMHTHGSLT---AGILaledRLNDLIGPPEEDETYCSYLPLAHIMEFGVTNIFLARGALIGF--GSPRTLTD 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 354 -------DLKVLQPTIFPVVPRLlnrmFDRIFG--QANTP----VKRWMLDFASKRKEAELRSGivRNDSFWDKIIFHKV 420
Cdd:PTZ00216 349 tfarphgDLTEFRPVFLIGVPRI----FDTIKKavEAKLPpvgsLKRRVFDHAYQSRLRALKEG--KDTPYWNEKVFSAP 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 421 QASLGGKVRLMVTGAAPVSPTVLTFLRAALGCqFYEGYGQTEcTAGC-SLTIPGDWTAGHVGAPMPCNHVKLVDVEEMNY 499
Cdd:PTZ00216 423 RAVLGGRVRAMLSGGGPLSAATQEFVNVVFGM-VIQGWGLTE-TVCCgGIQRTGDLEPNAVGQLLKGVEMKLLDTEEYKH 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 500 fASKGE--GEVCIKGSNVFQGYLKDDEKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENVY 577
Cdd:PTZ00216 501 -TDTPEprGEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVKALAKNCLGEYIALEALEALY 579
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 578 TRSEPV----VQVFVHgeSLQAFLVGIVVPDPDNVMNWAKKRKFEGSYEELCKNKDFKNAVLEDLLKLGKEAGLKTFEQV 653
Cdd:PTZ00216 580 GQNELVvpngVCVLVH--PARSYICALVLTDEAKAMAFAKEHGIEGEYPAILKDPEFQKKATESLQETARAAGRKSFEIV 657
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 1270536209 654 KDIALHSEMFAIENGLLTPTLKAKRPELRKYFKDEIDELYAN 695
Cdd:PTZ00216 658 RHVRVLSDEWTPENGVLTAAMKLKRRVIDERYADLIKELFAD 699
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
116-679 |
1.32e-91 |
|
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: 293.11 E-value: 1.32e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 116 QPYEWISYKEVAERAEYVGSALLHRGFKPspDQFVGIFAQNRPEWTIVELGCYTYSMVAVPLYDTLGAEAITYIINKADL 195
Cdd:cd17640 1 KPPKRITYKDLYQEILDFAAGLRSLGVKA--GEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 196 SVVFcdspekaklllsnvekgetpvlrtivlmnpFDNDlvergkkcgvelvslkdieeegkanrekpkppkPDDLAVVCF 275
Cdd:cd17640 79 VALV------------------------------VEND---------------------------------SDDLATIIY 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 276 TSGTTGNPKGAMLSHKNIVSNsagfMKVTEDLMFPSTQDVLISFLPLAHMFERVVECVVLCHGARIGFfqGDIRLLMDDL 355
Cdd:cd17640 96 TSGTTGNPKGVMLTHANLLHQ----IRSLSDIVPPQPGDRFLSILPIWHSYERSAEYFIFACGCSQAY--TSIRTLKDDL 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 356 KVLQPTIFPVVPRLlnrmfdrifgqantpvkrWmldfaskrkEAeLRSGI---VRNDSFWDKIIFHKvqASLGGKVRLMV 432
Cdd:cd17640 170 KRVKPHYIVSVPRL------------------W---------ES-LYSGIqkqVSKSSPIKQFLFLF--FLSGGIFKFGI 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 433 TGAAPVSPTVLTFLRaALGCQFYEGYGQTECTAGCSLTIPGDWTAGHVGAPMPCNHVKLVDVEEMNYFASKGEGEVCIKG 512
Cdd:cd17640 220 SGGGALPPHVDTFFE-AIGIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIVDPEGNVVLPPGEKGIVWVRG 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 513 SNVFQGYLKDDEKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENVYTRSEPVVQVFVHGES 592
Cdd:cd17640 299 PQVMKGYYKNPEATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSNGENVEPQPIEEALMRSPFIEQIMVVGQD 378
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 593 lQAFLVGIVVPDPDNVMNWAK--KRKFEGSYEELCKNKD----FKNAVLEdllKLGKEAGLKTFEQVKDIALHSEMFaIE 666
Cdd:cd17640 379 -QKRLGALIVPNFEELEKWAKesGVKLANDRSQLLASKKvlklYKNEIKD---EISNRPGFKSFEQIAPFALLEEPF-IE 453
|
570
....*....|...
gi 1270536209 667 NGLLTPTLKAKRP 679
Cdd:cd17640 454 NGEMTQTMKIKRN 466
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
118-685 |
6.67e-82 |
|
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: 268.95 E-value: 6.67e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 118 YEWISYKEVAERAEYVGSALLHRGFKPSPDqfVGIFAQNRPEWTIVELGCYTYSMVAVPLYDTLGAEAITYIINKADLSV 197
Cdd:cd05932 4 VVEFTWGEVADKARRLAAALRALGLEPGSK--IALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 198 VFCDSPEKAKLLLSNVekGETPVLRTIVLMNPFDNDLvergkkcgvelvSLKDIEEEGKANREKPkPPKPDDLAVVCFTS 277
Cdd:cd05932 82 LFVGKLDDWKAMAPGV--PEGLISISLPPPSAANCQY------------QWDDLIAQHPPLEERP-TRFPEQLATLIYTS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 278 GTTGNPKGAMLSHKNIVSNSAGfmkVTEDLMFpSTQDVLISFLPLAHMFERV-VECVVLCHGARIgFFQGDIRLLMDDLK 356
Cdd:cd05932 147 GTTGQPKGVMLTFGSFAWAAQA---GIEHIGT-EENDRMLSYLPLAHVTERVfVEGGSLYGGVLV-AFAESLDTFVEDVQ 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 357 VLQPTIFPVVPRLLNRMFDRIfgQANTPVKRwmLDFASKRkeaelrsgivrndSFWDKIIFHKVQASLG-GKVRLMVTGA 435
Cdd:cd05932 222 RARPTLFFSVPRLWTKFQQGV--QDKIPQQK--LNLLLKI-------------PVVNSLVKRKVLKGLGlDQCRLAGCGS 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 436 APVSPTVLTFLRAaLGCQFYEGYGQTECTAGCSLTIPGDWTAGHVGAPMPCNHVKLVDveemnyfaskgEGEVCIKGSNV 515
Cdd:cd05932 285 APVPPALLEWYRS-LGLNILEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRISE-----------DGEILVRSPAL 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 516 FQGYLKDDEKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENVYTRSEPVVQVFVHGESLQA 595
Cdd:cd05932 353 MMGYYKDPEATAEAFTADGFLRTGDKGELDADGNLTITGRVKDIFKTSKGKYVAPAPIENKLAEHDRVEMVCVIGSGLPA 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 596 fLVGIVVpdPDNVMNWAKKRKFEGSYEELCKnkdfknAVLEDLlklgkEAGLKTFEQVKDIALHSEMFAIENGLLTPTLK 675
Cdd:cd05932 433 -PLALVV--LSEEARLRADAFARAELEASLR------AHLARV-----NSTLDSHEQLAGIVVVKDPWSIDNGILTPTLK 498
|
570
....*....|
gi 1270536209 676 AKRPELRKYF 685
Cdd:cd05932 499 IKRNVLEKAY 508
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
113-693 |
5.05e-75 |
|
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: 253.05 E-value: 5.05e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 113 KPNQPYEWISYKEVAERAEYVGSALLHRGFkpspDQF--VGIFAQNRPEWTIVELGCYTYSMVAVPLYDTLGAEAITYII 190
Cdd:cd05933 1 KRGDKWHTLTYKEYYEACRQAAKAFLKLGL----ERFhgVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 191 NKADLSVVFCDSPEK-AKLLLSnveKGETPVLRTIV-LMNPFDNdlvergKKCGV----ELVSL-KDIEEEGKANREKPK 263
Cdd:cd05933 77 ETSEANILVVENQKQlQKILQI---QDKLPHLKAIIqYKEPLKE------KEPNLyswdEFMELgRSIPDEQLDAIISSQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 264 ppKPDDLAVVCFTSGTTGNPKGAMLSHKNIVSNSAGFMKVTEDLMFPSTQDVLISFLPLAHMFERVVEC-VVLCHGARIG 342
Cdd:cd05933 148 --KPNQCCTLIYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLRPATVGQESVVSYLPLSHIAAQILDIwLPIKVGGQVY 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 343 FFQGDIR--LLMDDLKVLQPTIFPVVPRLLNRMFDRI--FGQANTPVKRWMLDFAsKRKEAE-------LRSGIVRNDSF 411
Cdd:cd05933 226 FAQPDALkgTLVKTLREVRPTAFMGVPRVWEKIQEKMkaVGAKSGTLKRKIASWA-KGVGLEtnlklmgGESPSPLFYRL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 412 WDKIIFHKVQASLG-GKVRLMVTGAAPVSPTVLTFLrAALGCQFYEGYGQTECTAGCSLTIPGDWTAGHVGAPMPCNHVK 490
Cdd:cd05933 305 AKKLVFKKVRKALGlDRCQKFFTGAAPISRETLEFF-LSLNIPIMELYGMSETSGPHTISNPQAYRLLSCGKALPGCKTK 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 491 LVDVEemnyfaSKGEGEVCIKGSNVFQGYLKDDEKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAP 570
Cdd:cd05933 384 IHNPD------ADGIGEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITAGGENVPP 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 571 EKIENVYTRSEPVVQvfvhgeslQAFLVGivvpdpdnvmnwaKKRKF--------------------EGSYE--ELCKNK 628
Cdd:cd05933 458 VPIEDAVKKELPIIS--------NAMLIG-------------DKRKFlsmlltlkcevnpetgepldELTEEaiEFCRKL 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 629 DFKNAVLEDLLKLGKEAGLKTFEQ---------------VKDIALHSEMFAIENGLLTPTLKAKRPELRKYFKDEIDELY 693
Cdd:cd05933 517 GSQATRVSEIAGGKDPKVYEAIEEgikrvnkkaisnaqkIQKWVILEKDFSVPGGELGPTMKLKRPVVAKKYKDEIDKLY 596
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
121-615 |
2.33e-73 |
|
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: 244.33 E-value: 2.33e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 121 ISYKEVAERAEYVGSALLHRGFKPspDQFVGIFAQNRPEWTIVELGCYTYSMVAVPLYDTLGAEAITYIINKADLSVVFC 200
Cdd:COG0318 25 LTYAELDARARRLAAALRALGVGP--GDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEELAYILEDSGARALVT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 201 dspekaklllsnvekgetpvlrtivlmnpfdndlvergkkcgvelvslkdieeegkanrekpkppkpddlAVVCFTSGTT 280
Cdd:COG0318 103 ----------------------------------------------------------------------ALILYTSGTT 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 281 GNPKGAMLSHKNIVSNSAGFMkvteDLMFPSTQDVLISFLPLAHMFERVVECV-VLCHGARI----GFfqgDIRLLMDDL 355
Cdd:COG0318 113 GRPKGVMLTHRNLLANAAAIA----AALGLTPGDVVLVALPLFHVFGLTVGLLaPLLAGATLvllpRF---DPERVLELI 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 356 KVLQPTIFPVVPRLLNRMFDRifgqantpvkrwmldfaSKRKEAELRSgivrndsfwdkiifhkvqaslggkVRLMVTGA 435
Cdd:COG0318 186 ERERVTVLFGVPTMLARLLRH-----------------PEFARYDLSS------------------------LRLVVSGG 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 436 APVSPTVLTFLRAALGCQFYEGYGQTECTAGCSLTIPGDWTA--GHVGAPMPCNHVKLVDvEEMNYFASKGEGEVCIKGS 513
Cdd:COG0318 225 APLPPELLERFEERFGVRIVEGYGLTETSPVVTVNPEDPGERrpGSVGRPLPGVEVRIVD-EDGRELPPGEVGEIVVRGP 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 514 NVFQGYLKDDEKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENVYTRSEPVVQVFV----- 588
Cdd:COG0318 304 NVMKGYWNDPEATAEAF-RDGWLRTGDLGRLDEDGYLYIVGRKKDMIISG-GENVYPAEVEEVLAAHPGVAEAAVvgvpd 381
|
490 500 510
....*....|....*....|....*....|.
gi 1270536209 589 --HGESLQAFLV--GIVVPDPDNVMNWAKKR 615
Cdd:COG0318 382 ekWGERVVAFVVlrPGAELDAEELRAFLRER 412
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
118-671 |
4.53e-72 |
|
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: 244.67 E-value: 4.53e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 118 YEWISYKEVAERAEYVGSALlHRGFKPSPDQFVGIFAQNRPEWTIVELGCYTYSMVAVPLYDTLGAEAITYIINKADLSV 197
Cdd:cd17632 65 FETITYAELWERVGAVAAAH-DPEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRL 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 198 VfCDSPEKAKLLLSNVEKGETPVlRTIVlmnpFDN--------DLVER------GKKCGVELVSL-KDIEEEGKANREKP 262
Cdd:cd17632 144 L-AVSAEHLDLAVEAVLEGGTPP-RLVV----FDHrpevdahrAALESarerlaAVGIPVTTLTLiAVRGRDLPPAPLFR 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 263 KPPKPDDLAVVCFTSGTTGNPKGAMLSHKNIVSNSAGFMKVTEDLMFPStqdVLISFLPLAHMFERVVECVVLCHGArIG 342
Cdd:cd17632 218 PEPDDDPLALLIYTSGSTGTPKGAMYTERLVATFWLKVSSIQDIRPPAS---ITLNFMPMSHIAGRISLYGTLARGG-TA 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 343 FFQG--DIRLLMDDLKVLQPTIFPVVPRLLNRMFDRIfgQANtpVKRWMLDFA-----SKRKEAELRsgivrndsfwdki 415
Cdd:cd17632 294 YFAAasDMSTLFDDLALVRPTELFLVPRVCDMLFQRY--QAE--LDRRSVAGAdaetlAERVKAELR------------- 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 416 ifhkvQASLGGKVRLMVTGAAPVSPTVLTFLRAALGCQFYEGYGQTEctAGCSLTipgdwtAGHVGAPmPCNHVKLVDVE 495
Cdd:cd17632 357 -----ERVLGGRLLAAVCGSAPLSAEMKAFMESLLDLDLHDGYGSTE--AGAVIL------DGVIVRP-PVLDYKLVDVP 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 496 EMNYFASKG---EGEVCIKGSNVFQGYLKDDEKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEK 572
Cdd:cd17632 423 ELGYFRTDRphpRGELLVKTDTLFPGYYKRPEVTAEVFDEDGFYRTGDVMAELGPDRLVYVDRRNNVLKLSQGEFVTVAR 502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 573 IENVYTRSEPVVQVFVHGESLQAFLVGIVVPDPDNVMNWAKKRkfegsyeelcknkdFKNAVLEDLLKLGKEAGLKTFEQ 652
Cdd:cd17632 503 LEAVFAASPLVRQIFVYGNSERAYLLAVVVPTQDALAGEDTAR--------------LRAALAESLQRIAREAGLQSYEI 568
|
570
....*....|....*....
gi 1270536209 653 VKDIALHSEMFAIENGLLT 671
Cdd:cd17632 569 PRDFLIETEPFTIANGLLS 587
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
121-678 |
8.45e-71 |
|
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: 240.79 E-value: 8.45e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 121 ISYKEVAERAEYVGSALLHRGFKPSpdQFVGIFAQNRPEWTIVELGCYTYSMVAVPLYDTLGAEAITYIINKADLSVVFC 200
Cdd:cd17641 12 FTWADYADRVRAFALGLLALGVGRG--DVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 201 DSPEKAKLLLSNVEkgETPVLRTIVLMNPfdndlveRG--KKCGVELVSLKDIEEEGKA-NREKPK-------PPKPDDL 270
Cdd:cd17641 90 EDEEQVDKLLEIAD--RIPSVRYVIYCDP-------RGmrKYDDPRLISFEDVVALGRAlDRRDPGlyerevaAGKGEDV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 271 AVVCFTSGTTGNPKGAMLSHKNIVSNSAGFMKVteDLMFPStqDVLISFLPLAHMFERVVECVVLCHGARIGFFQGDIRL 350
Cdd:cd17641 161 AVLCTTSGTTGKPKLAMLSHGNFLGHCAAYLAA--DPLGPG--DEYVSVLPLPWIGEQMYSVGQALVCGFIVNFPEEPET 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 351 LMDDLKVLQPTIFPVVPRLLNRM--FDRIFGQANTPVKRWMLDF--------ASKRKEAELRSGIVRNDS-FWDKIIFHK 419
Cdd:cd17641 237 MMEDLREIGPTFVLLPPRVWEGIaaDVRARMMDATPFKRFMFELgmklglraLDRGKRGRPVSLWLRLASwLADALLFRP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 420 VQASLG-GKVRLMVTGAAPVSPTVLTFLRAaLGCQFYEGYGQTECTAGCSLTIPGDWTAGHVGAPMPCNHVKLVDVeemn 498
Cdd:cd17641 317 LRDRLGfSRLRSAATGGAALGPDTFRFFHA-IGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGTEVRIDEV---- 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 499 yfaskgeGEVCIKGSNVFQGYLKDDEKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENVYT 578
Cdd:cd17641 392 -------GEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTTSDGTRFSPQFIENKLK 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 579 RSEPVVQVFVHGESlQAFLVGIVVPDPDNVMNWAKKRKFE-GSYEELCKNKDFKNAVLEDLLKLGKEagLKTFEQV-KDI 656
Cdd:cd17641 465 FSPYIAEAVVLGAG-RPYLTAFICIDYAIVGKWAEQRGIAfTTYTDLASRPEVYELIRKEVEKVNAS--LPEAQRIrRFL 541
|
570 580
....*....|....*....|..
gi 1270536209 657 ALHSEMFAiENGLLTPTLKAKR 678
Cdd:cd17641 542 LLYKELDA-DDGELTRTRKVRR 562
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
121-678 |
5.45e-68 |
|
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: 230.41 E-value: 5.45e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 121 ISYKEVAERAEYVGSALLHRGFKPSPDqfVGIFAQNRPEWTIVELGCYTYSMVAVPLYDTLGAEAITYIINKADLSVVFC 200
Cdd:cd05914 8 LTYKDLADNIAKFALLLKINGVGTGDR--VALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 201 DspekaklllsnvekgetpvlrtivlmnpfdndlvergkkcgvelvslkdieeegkanrekpkppKPDDLAVVCFTSGTT 280
Cdd:cd05914 86 S----------------------------------------------------------------DEDDVALINYTSGTT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 281 GNPKGAMLSHKNIVSNSAGfmkVTEDLMFPSTqDVLISFLPLAHMFERVVECVV-LCHGARIGFFQGDIRLLMDDLKVLQ 359
Cdd:cd05914 102 GNSKGVMLTYRNIVSNVDG---VKEVVLLGKG-DKILSILPLHHIYPLTFTLLLpLLNGAHVVFLDKIPSAKIIALAFAQ 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 360 PTIFPVVPRLLNRMFDRIFGQANTPVKRWMLdFASKRKeaelrsgiVRNDSFWdKIIFHKVQASLGGKVRLMVTGAAPVS 439
Cdd:cd05914 178 VTPTLGVPVPLVIEKIFKMDIIPKLTLKKFK-FKLAKK--------INNRKIR-KLAFKKVHEAFGGNIKEFVIGGAKIN 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 440 PTVLTFLRAaLGCQFYEGYGQTECTAGCSLTIPGDWTAGHVGAPMPCNHVKLVDVEemnyfASKGEGEVCIKGSNVFQGY 519
Cdd:cd05914 248 PDVEEFLRT-IGFPYTIGYGMTETAPIISYSPPNRIRLGSAGKVIDGVEVRIDSPD-----PATGEGEIIVRGPNVMKGY 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 520 LKDDEKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENVYTRSEPVVQ--VFVHGESLQAfl 597
Cdd:cd05914 322 YKNPEATAEAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSSGKNIYPEEIEAKINNMPFVLEslVVVQEKKLVA-- 399
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 598 vgIVVPDPDnvmnwakkrkFEGSYEElcKNKDFKNAVLEDLL-KLGKEagLKTFEQVKDIALHSEMFAienglLTPTLKA 676
Cdd:cd05914 400 --LAYIDPD----------FLDVKAL--KQRNIIDAIKWEVRdKVNQK--VPNYKKISKVKIVKEEFE-----KTPKGKI 458
|
..
gi 1270536209 677 KR 678
Cdd:cd05914 459 KR 460
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
121-615 |
5.71e-65 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 223.63 E-value: 5.71e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 121 ISYKEVAERAEYVGSALLHRGFKPSpDQfVGIFAQNRPEWTIVELGCYTYSMVAVPLYDTLGAEAITYIINKADLSVVFC 200
Cdd:PRK07656 31 LTYAELNARVRRAAAALAALGIGKG-DR-VAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYILARGDAKALFV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 201 dspekAKLLLSNVEKGET--PVLRTIVLMNPfdndlvERGKKCGVELVSLKDIEEEGkANREKPKPPKPDDLAVVCFTSG 278
Cdd:PRK07656 109 -----LGLFLGVDYSATTrlPALEHVVICET------EEDDPHTEKMKTFTDFLAAG-DPAERAPEVDPDDVADILFTSG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 279 TTGNPKGAMLSHKNIVSNS---AGFMKVTEDlmfpstqDVLISFLPLAHMFERVVeCVVLC--HGARIgffqgDIRLLMD 353
Cdd:PRK07656 177 TTGRPKGAMLTHRQLLSNAadwAEYLGLTEG-------DRYLAANPFFHVFGYKA-GVNAPlmRGATI-----LPLPVFD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 354 DLKVLQ------PTIFPVVPRLLNRMFDrifgqantpvkrwmldfASKRKEAELRSgivrndsfwdkiifhkvqaslggk 427
Cdd:PRK07656 244 PDEVFRlieterITVLPGPPTMYNSLLQ-----------------HPDRSAEDLSS------------------------ 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 428 VRLMVTGAAPVSPTVLTFLRAALGCQ-FYEGYGQTECTAGCSLTIPGD---WTAGHVGAPMPcnHVKLVDVEEMNYFASK 503
Cdd:PRK07656 283 LRLAVTGAASMPVALLERFESELGVDiVLTGYGLSEASGVTTFNRLDDdrkTVAGTIGTAIA--GVENKIVNELGEEVPV 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 504 GE-GEVCIKGSNVFQGYLKDDEKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENVYTRSEP 582
Cdd:PRK07656 361 GEvGELLVRGPNVMKGYYDDPEATAAAIDADGWLHTGDLGRLDEEGYLYIVDRKKDMF-IVGGFNVYPAEVEEVLYEHPA 439
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1270536209 583 VVQVFV-------HGESLQAFLV---GIVVpDPDNVMNWAKKR 615
Cdd:PRK07656 440 VAEAAVigvpderLGEVGKAYVVlkpGAEL-TEEELIAYCREH 481
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
119-615 |
1.33e-63 |
|
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: 218.59 E-value: 1.33e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 119 EWISYKEVAERAEYVGSALLHRGFKPSpDQfVGIFAQNRPEWTIVELGCYTYSMVAVPLYDTLGAEAITYIINKADLSVV 198
Cdd:cd05936 23 RKLTYRELDALAEAFAAGLQNLGVQPG-DR-VALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPRELEHILNDSGAKAL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 199 FCDSPekaklLLSNVEKGETPvlrtivlmnpfdndlvergkkcgvelvslkdieeegkanrEKPKPPKPDDLAVVCFTSG 278
Cdd:cd05936 101 IVAVS-----FTDLLAAGAPL----------------------------------------GERVALTPEDVAVLQYTSG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 279 TTGNPKGAMLSHKNIVSNSAGFMKVTEDLMFPstQDVLISFLPLAHMFERVVECVV-LCHGARIGFFQG-DIRLLMDDLK 356
Cdd:cd05936 136 TTGVPKGAMLTHRNLVANALQIKAWLEDLLEG--DDVVLAALPLFHVFGLTVALLLpLALGATIVLIPRfRPIGVLKEIR 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 357 VLQPTIFPVVPRLLNRMFDrifgqantpvkrwmldfASKRKEAELRSgivrndsfwdkiifhkvqaslggkVRLMVTGAA 436
Cdd:cd05936 214 KHRVTIFPGVPTMYIALLN-----------------APEFKKRDFSS------------------------LRLCISGGA 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 437 PVSPTVLTFLRAALGCQFYEGYGQTEC---TAGCSLTIPGdwTAGHVGAPMPCNHVKLVDVEemNYFASKGE-GEVCIKG 512
Cdd:cd05936 253 PLPVEVAERFEELTGVPIVEGYGLTETspvVAVNPLDGPR--KPGSIGIPLPGTEVKIVDDD--GEELPPGEvGELWVRG 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 513 SNVFQGYLKDDEKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENVYTRSEPVVQVFV---- 588
Cdd:cd05936 329 PQVMKGYWNRPEETAEAF-VDGWLRTGDIGYMDEDGYFFIVDRKKDMI-IVGGFNVYPREVEEVLYEHPAVAEAAVvgvp 406
|
490 500 510
....*....|....*....|....*....|...
gi 1270536209 589 ---HGESLQAFLV---GiVVPDPDNVMNWAKKR 615
Cdd:cd05936 407 dpySGEAVKAFVVlkeG-ASLTEEEIIAFCREQ 438
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
269-606 |
4.50e-62 |
|
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341228 [Multi-domain] Cd Length: 336 Bit Score: 210.60 E-value: 4.50e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 269 DLAVVCFTSGTTGNPKGAMLSHKNIVSNSAGFmkvtEDLMFPSTQDVLISFLPLAHMFERVVECVVLCHGARI----GFF 344
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAAL----AASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVvllpKFD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 345 QGDIRLLMDDLKVlqpTIFPVVPRLLNRMFDRIfgqantpvkrwmldfasKRKEAELRSgivrndsfwdkiifhkvqasl 424
Cdd:cd04433 77 PEAALELIEREKV---TILLGVPTLLARLLKAP-----------------ESAGYDLSS--------------------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 425 ggkVRLMVTGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCSLTIPGDWT--AGHVGAPMPCNHVKLVDVEEmNYFAS 502
Cdd:cd04433 116 ---LRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTVATGPPDDDArkPGSVGRPVPGVEVRIVDPDG-GELPP 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 503 KGEGEVCIKGSNVFQGYLKDDEKTAEAlDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENVYTRSEP 582
Cdd:cd04433 192 GEIGELVVRGPSVMKGYWNNPEATAAV-DEDGWYRTGDLGRLDEDGYLYIVGRLKDMIK-SGGENVYPAEVEAVLLGHPG 269
|
330 340
....*....|....*....|....
gi 1270536209 583 VVQVFVHGeslqaflvgivVPDPD 606
Cdd:cd04433 270 VAEAAVVG-----------VPDPE 282
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
121-606 |
1.01e-61 |
|
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: 214.00 E-value: 1.01e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 121 ISYKEVAERAEYVGSALLHRGFKPspDQFVGIFAQNRPEWTIVELGCYTYSMVAVPLYDTLGAEAITYIINKADLSVVFC 200
Cdd:cd05911 11 LTYAQLRTLSRRLAAGLRKLGLKK--GDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 201 DSPEKAKLLlsNVEKGETPVLRtIVLMNPFDNDLVERGKkcgvelvSLKDIEEEGKANREKPKPPKPDDLAVVCFTSGTT 280
Cdd:cd05911 89 DPDGLEKVK--EAAKELGPKDK-IIVLDDKPDGVLSIED-------LLSPTLGEEDEDLPPPLKDGKDDTAAILYSSGTT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 281 GNPKGAMLSHKNIVSNSaGFMKVTEDLMFPStQDVLISFLPLAHMF--ERVVECvvLCHGA-RIGFFQGDIRLLMDDLKV 357
Cdd:cd05911 159 GLPKGVCLSHRNLIANL-SQVQTFLYGNDGS-NDVILGFLPLYHIYglFTTLAS--LLNGAtVIIMPKFDSELFLDLIEK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 358 LQPTIFPVVPRLLNRMfdrifgqANTPvkrwMLDFASkrkeaeLRSgivrndsfwdkiifhkvqaslggkVRLMVTGAAP 437
Cdd:cd05911 235 YKITFLYLVPPIAAAL-------AKSP----LLDKYD------LSS------------------------LRVILSGGAP 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 438 VSPTVLTFLRAALG-CQFYEGYGQTECTAGCSLTIPGDWTAGHVGAPMPCNHVKLVDVEEMNYFASKGEGEVCIKGSNVF 516
Cdd:cd05911 274 LSKELQELLAKRFPnATIKQGYGMTETGGILTVNPDGDDKPGSVGRLLPNVEAKIVDDDGKDSLGPNEPGEICVRGPQVM 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 517 QGYLKDDEKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENVYTRSEPVVQVFVhgeslqaf 596
Cdd:cd05911 354 KGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKKELIKY-KGFQVAPAELEAVLLEHPGVADAAV-------- 424
|
490
....*....|
gi 1270536209 597 lVGIvvPDPD 606
Cdd:cd05911 425 -IGI--PDEV 431
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
86-615 |
4.42e-61 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 213.12 E-value: 4.42e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 86 YDDVKTIYDIFQRGRRVSNNGPCL--GHRKpnqpyewISYKEVAERAEYVGSALLHRGFKPspDQFVGIFAQNRPEWTIV 163
Cdd:PRK06187 2 QDYPLTIGRILRHGARKHPDKEAVyfDGRR-------TTYAELDERVNRLANALRALGVKK--GDRVAVFDWNSHEYLEA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 164 ELGCytySM---VAVPLYDTLGAEAITYIINKADLSVVFCDSpEKAKLLLSNveKGETPVLRTIVLMNPFDNdlvergKK 240
Cdd:PRK06187 73 YFAV---PKigaVLHPINIRLKPEEIAYILNDAEDRVVLVDS-EFVPLLAAI--LPQLPTVRTVIVEGDGPA------AP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 241 CGVELVSLKDIEEEGKANREKPkPPKPDDLAVVCFTSGTTGNPKGAMLSHKNIVSNSAG---FMKVTEDlmfpstqDVLI 317
Cdd:PRK06187 141 LAPEVGEYEELLAAASDTFDFP-DIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAvcaWLKLSRD-------DVYL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 318 SFLPLAHMFERVVECVVLCHGARI---GFFqgDIRLLMDDLKVLQPTIFPVVPRLLNRMfdrifgqANTPVKRWMlDFAS 394
Cdd:PRK06187 213 VIVPMFHVHAWGLPYLALMAGAKQvipRRF--DPENLLDLIETERVTFFFAVPTIWQML-------LKAPRAYFV-DFSS 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 395 krkeaelrsgivrndsfwdkiifhkvqaslggkVRLMVTGAAPVSPTVLTFLRAALGCQFYEGYGQTECT-AGCSLT--- 470
Cdd:PRK06187 283 ---------------------------------LRLVIYGGAALPPALLREFKEKFGIDLVQGYGMTETSpVVSVLPped 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 471 -IPGDWT-AGHVGAPMPCNHVKLVDvEEMNYFASKGE--GEVCIKGSNVFQGYLKDDEKTAEALDkDGWLHTGDIGKWLP 546
Cdd:PRK06187 330 qLPGQWTkRRSAGRPLPGVEARIVD-DDGDELPPDGGevGEIIVRGPWLMQGYWNRPEATAETID-GGWLHTGDVGYIDE 407
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1270536209 547 NGTLKIIDRKKHIFKLAqGEYIAPEKIENVYTRSEPVVQVFV-------HGESLQAFLVG--IVVPDPDNVMNWAKKR 615
Cdd:PRK06187 408 DGYLYITDRIKDVIISG-GENIYPRELEDALYGHPAVAEVAVigvpdekWGERPVAVVVLkpGATLDAKELRAFLRGR 484
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
232-695 |
7.76e-48 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 180.30 E-value: 7.76e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 232 NDLVERGKKCGVELVSLKDIEEeGKANREKPKPPKPDDLAVVCFTSGTTGNPKGAMLSHKNI------VSNSAGFMKvte 305
Cdd:PTZ00342 269 KDLKEKAKKLGISIILFDDMTK-NKTTNYKIQNEDPDFITSIVYTSGTSGKPKGVMLSNKNLyntvvpLCKHSIFKK--- 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 306 dlMFPSTQdvlISFLPLAHMFERVVECVVLCHGARIGFFQGDIRLLMDDLKVLQPTIFPVVPRLLNRMFDRIFGQAN--T 383
Cdd:PTZ00342 345 --YNPKTH---LSYLPISHIYERVIAYLSFMLGGTINIWSKDINYFSKDIYNSKGNILAGVPKVFNRIYTNIMTEINnlP 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 384 PVKRWMLdfaskRKEAELRSGiVRNDSFWDKI--IFH---KVQASLGGKVRLMVTGAAPVSPTVLTFLRAALGCQFYEGY 458
Cdd:PTZ00342 420 PLKRFLV-----KKILSLRKS-NNNGGFSKFLegITHissKIKDKVNPNLEVILNGGGKLSPKIAEELSVLLNVNYYQGY 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 459 GQTECTAGCSLTIPGDWTAGHVGAPM-PCNHVKLVDVEEMNYFASKGEGEVCIKGSNVFQGYLKDDEKTAEALDKDGWLH 537
Cdd:PTZ00342 494 GLTETTGPIFVQHADDNNTESIGGPIsPNTKYKVRTWETYKATDTLPKGELLIKSDSIFSGYFLEKEQTKNAFTEDGYFK 573
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 538 TGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENVYTRSEPVVQVFVHG-ESLQAFLvGIVVPDP---------DN 607
Cdd:PTZ00342 574 TGDIVQINKNGSLTFLDRSKGLVKLSQGEYIETDMLNNLYSQISFINFCVVYGdDSMDGPL-AIISVDKyllfkclkdDN 652
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 608 VMNWA---KKRKFEGSYEELCKNKDFKNAVLEDLLKLGKEAGLKTFEQVKDIALHSEMFAIENgLLTPTLKAKRPELRK- 683
Cdd:PTZ00342 653 MLESTginEKNYLEKLTDETINNNIYVDYVKGKMLEVYKKTNLNRYNIINDIYLTSKVWDTNN-YLTPTFKVKRFYVFKd 731
|
490
....*....|....
gi 1270536209 684 --YFKDEIDELYAN 695
Cdd:PTZ00342 732 yaFFIDQVKKIYKN 745
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
121-607 |
2.36e-45 |
|
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: 167.79 E-value: 2.36e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 121 ISYKEVAERAEYVGSALLHRGFKPSpDQfVGIFAQNRPEWTIVELGCYTYSMVAVPLYDTLGAEAITYIINKADLSVVFc 200
Cdd:cd17631 21 LTYAELDERVNRLAHALRALGVAKG-DR-VAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAYILADSGAKVLF- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 201 dspekaklllsnvekgetpvlrtivlmnpfdndlvergkkcgvelvslkdieeegkanrekpkppkpDDLAVVCFTSGTT 280
Cdd:cd17631 98 -------------------------------------------------------------------DDLALLMYTSGTT 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 281 GNPKGAMLSHKNIVSNSagfMKVTEDLmFPSTQDVLISFLPLAHMFERVVECV-VLCHGARI----GFfqgDIRLLMDDL 355
Cdd:cd17631 111 GRPKGAMLTHRNLLWNA---VNALAAL-DLGPDDVLLVVAPLFHIGGLGVFTLpTLLRGGTVvilrKF---DPETVLDLI 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 356 KVLQPTIFPVVPRLLNRMFDRifGQANTPvkrwmlDFASkrkeaelrsgivrndsfwdkiifhkvqaslggkVRLMVTGA 435
Cdd:cd17631 184 ERHRVTSFFLVPTMIQALLQH--PRFATT------DLSS---------------------------------LRAVIYGG 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 436 APVSPTVLTFLRAAlGCQFYEGYGQTECTAGCSLTIPGDW--TAGHVGAPMPCNHVKLVDvEEMNYFASKGEGEVCIKGS 513
Cdd:cd17631 223 APMPERLLRALQAR-GVKFVQGYGMTETSPGVTFLSPEDHrrKLGSAGRPVFFVEVRIVD-PDGREVPPGEVGEIVVRGP 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 514 NVFQGYLKDDEKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENVYTRSEPVVQVFV----- 588
Cdd:cd17631 301 HVMAGYWNRPEATAAAF-RDGWFHTGDLGRLDEDGYLYIVDRKKDMII-SGGENVYPAEVEDVLYEHPAVAEVAVigvpd 378
|
490 500
....*....|....*....|.
gi 1270536209 589 --HGESLQAFlvgiVVPDPDN 607
Cdd:cd17631 379 ekWGEAVVAV----VVPRPGA 395
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
135-614 |
1.39e-41 |
|
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: 158.26 E-value: 1.39e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 135 SALLHRGFKPspDQFVGIFAQNRPEWTIVELGCYTYSMVAVPLYDTLGAEAITYIINKADLSVVFCDSP--EKAKLLLsn 212
Cdd:cd05909 21 ARKLAKMTKE--GENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLTSKQfiEKLKLHH-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 213 VEKGETPVlrTIVLMNPFDNDLvERGKKCGVELVSLkdIEEEGKANREKPKPPKPDDLAVVCFTSGTTGNPKGAMLSHKN 292
Cdd:cd05909 97 LFDVEYDA--RIVYLEDLRAKI-SKADKCKAFLAGK--FPPKWLLRIFGVAPVQPDDPAVILFTSGSEGLPKGVVLSHKN 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 293 IVSNSAGFMKVTEdlmfPSTQDVLISFLPLAHMFervvecvvlchgariGFFQGDIRLLMDDLKVLQ---PTIFPVVPRL 369
Cdd:cd05909 172 LLANVEQITAIFD----PNPEDVVFGALPFFHSF---------------GLTGCLWLPLLSGIKVVFhpnPLDYKKIPEL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 370 LNRMFDRIFGqaNTPVkrwMLDFASKRKEAELRSGIvrndsfwdkiifhkvqaslggkvRLMVTGAAPVSPTVLTFLRAA 449
Cdd:cd05909 233 IYDKKATILL--GTPT---FLRGYARAAHPEDFSSL-----------------------RLVVAGAEKLKDTLRQEFQEK 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 450 LGCQFYEGYGQTECTAGCSLTIPG-DWTAGHVGAPMPCNHVKLVDVEEMNYFASKGEGEVCIKGSNVFQGYLKDDEKTAE 528
Cdd:cd05909 285 FGIRILEGYGTTECSPVISVNTPQsPNKEGTVGRPLPGMEVKIVSVETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTSF 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 529 ALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIEN-VYTRSEPVVQVFV-------HGESLQAFLVGI 600
Cdd:cd05909 365 AF-GDGWYDTGDIGKIDGEGFLTITGRLSRFAKIA-GEMVSLEAIEDiLSEILPEDNEVAVvsvpdgrKGEKIVLLTTTT 442
|
490
....*....|....
gi 1270536209 601 vVPDPDNVMNWAKK 614
Cdd:cd05909 443 -DTDPSSLNDILKN 455
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
231-576 |
2.59e-41 |
|
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: 157.78 E-value: 2.59e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 231 DNDLVERGKKCGVELVSLKDIEEEGKANR---------EKPKPP-KPDDLAVVCFTSGTTGNPKGAMLSHKNIVSNSAGF 300
Cdd:cd05904 111 TAELAEKLASLALPVVLLDSAEFDSLSFSdllfeadeaEPPVVViKQDDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQF 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 301 MKVtEDLMFPStQDVLISFLPLAHMFERvveCVVLCHGARIG--------FfqgDIRLLMDDLKVLQPTIFPVVPrllnr 372
Cdd:cd05904 191 VAG-EGSNSDS-EDVFLCVLPMFHIYGL---SSFALGLLRLGatvvvmprF---DLEELLAAIERYKVTHLPVVP----- 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 373 mfdrifgqantPVkrwMLDFASKRKEA--ELRSgivrndsfwdkiifhkvqaslggkVRLMVTGAAPVSPTVLTFLRAAL 450
Cdd:cd05904 258 -----------PI---VLALVKSPIVDkyDLSS------------------------LRQIMSGAAPLGKELIEAFRAKF 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 451 -GCQFYEGYGQTECTAGCSLTIPGDWTAGHVGAP---MPCNHVKLVDVEEMNYFASKGEGEVCIKGSNVFQGYLKDDEKT 526
Cdd:cd05904 300 pNVDLGQGYGMTESTGVVAMCFAPEKDRAKYGSVgrlVPNVEAKIVDPETGESLPPNQTGELWIRGPSIMKGYLNNPEAT 379
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1270536209 527 AEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENV 576
Cdd:cd05904 380 AATIDKEGWLHTGDLCYIDEDGYLFIVDRLKELIKY-KGFQVAPAELEAL 428
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
90-615 |
3.98e-41 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 158.40 E-value: 3.98e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 90 KTIYDIFQRGRRVSNNGPCLGHRKPNQPYewiSYKEVAERAEYVGSALLHRGFKPSpdQFVGIFAQNRPEWTIVELGCYT 169
Cdd:PRK12583 18 QTIGDAFDATVARFPDREALVVRHQALRY---TWRQLADAVDRLARGLLALGVQPG--DRVGIWAPNCAEWLLTQFATAR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 170 YSMVAVPLYDTLGAEAITYIINKADLSVVFC-----DSPEKAKLL-----LSNVEKGET-----PVLRTIVLMNPFD--- 231
Cdd:PRK12583 93 IGAILVNINPAYRASELEYALGQSGVRWVICadafkTSDYHAMLQellpgLAEGQPGALacerlPELRGVVSLAPAPppg 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 232 ----NDLVERGkkcgvELVSLKDIEEEGKANRekpkppkPDDLAVVCFTSGTTGNPKGAMLSHKNIVSNsaGFMkVTEDL 307
Cdd:PRK12583 173 flawHELQARG-----ETVSREALAERQASLD-------RDDPINIQYTSGTTGFPKGATLSHHNILNN--GYF-VAESL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 308 MFPSTqDVLISFLPLAHMFERVVECVV-LCHGARIgFFQGDirlLMDDLKVLQP------TIFPVVPRllnrMFdriFGQ 380
Cdd:PRK12583 238 GLTEH-DRLCVPVPLYHCFGMVLANLGcMTVGACL-VYPNE---AFDPLATLQAveeercTALYGVPT----MF---IAE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 381 ANTPvKRWMLDFASkrkeaeLRSGIVrndsfwdkiifhkvqaslggkvrlmvtGAAPVSPTVLTFLRAALGC-QFYEGYG 459
Cdd:PRK12583 306 LDHP-QRGNFDLSS------LRTGIM---------------------------AGAPCPIEVMRRVMDEMHMaEVQIAYG 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 460 QTECTAGCSLTIPGD---WTAGHVGAPMPCNHVKLVDVEEMNyfASKGE-GEVCIKGSNVFQGYLKDDEKTAEALDKDGW 535
Cdd:PRK12583 352 MTETSPVSLQTTAADdleRRVETVGRTQPHLEVKVVDPDGAT--VPRGEiGELCTRGYSVMKGYWNNPEATAESIDEDGW 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 536 LHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENVYTRSEPVVQVFV-------HGESLQAFLV---GIVVpDP 605
Cdd:PRK12583 430 MHTGDLATMDEQGYVRIVGRSKDMI-IRGGENIYPREIEEFLFTHPAVADVQVfgvpdekYGEEIVAWVRlhpGHAA-SE 507
|
570
....*....|
gi 1270536209 606 DNVMNWAKKR 615
Cdd:PRK12583 508 EELREFCKAR 517
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
121-615 |
5.18e-40 |
|
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: 152.83 E-value: 5.18e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 121 ISYKEVAERAEYVGSALLHRGFKPSPDQfVGIFAQNRPEWTIVELGCYTYSMVAVPLYDTLGAEAITYIINKADLSVVFc 200
Cdd:cd05941 12 ITYADLVARAARLANRLLALGKDLRGDR-VAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDSEPSLVL- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 201 dspekaklllsnvekgetpvlrtivlmnpfdndlvergkkcgvelvslkdieeegkanrekpkppkpdDLAVVCFTSGTT 280
Cdd:cd05941 90 --------------------------------------------------------------------DPALILYTSGTT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 281 GNPKGAMLSHKNIVSNSAGFMKV---TEDlmfpstqDVLISFLPLAHMFERVVecVVLC---HGARI---GFF---QGDI 348
Cdd:cd05941 102 GRPKGVVLTHANLAANVRALVDAwrwTED-------DVLLHVLPLHHVHGLVN--ALLCplfAGASVeflPKFdpkEVAI 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 349 RLLMDDLkvlqpTIFPVVPRllnrMFDRIFGQANTPVKrwmlDFASKRKEAElrsgivrndsfwdkiifhkvqaslgGKV 428
Cdd:cd05941 173 SRLMPSI-----TVFMGVPT----IYTRLLQYYEAHFT----DPQFARAAAA-------------------------ERL 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 429 RLMVTGAAPVSPTVLTFLRAALGCQFYEGYGQTEctAGCSLTIP--GDWTAGHVGAPMPCNHVKLVDVEEMNYFASKGEG 506
Cdd:cd05941 215 RLMVSGSAALPVPTLEEWEAITGHTLLERYGMTE--IGMALSNPldGERRPGTVGMPLPGVQARIVDEETGEPLPRGEVG 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 507 EVCIKGSNVFQGYLKDDEKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKK-HIFKlAQGEYIAPEKIENVYTRSEPVVQ 585
Cdd:cd05941 293 EIQVRGPSVFKEYWNKPEATKEEFTDDGWFKTGDLGVVDEDGYYWILGRSSvDIIK-SGGYKVSALEIERVLLAHPGVSE 371
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1270536209 586 VFVHGESLQAF---LVGIVVP-------DPDNVMNWAKKR 615
Cdd:cd05941 372 CAVIGVPDPDWgerVVAVVVLragaaalSLEELKEWAKQR 411
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
114-628 |
8.21e-38 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 148.42 E-value: 8.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 114 PNQPYEWiSYKEVAERAEYVGSALLHRGFKPSpDQfVGIFAQNRPEWTIVELGCYTYSMVAV---PLYDTlgAEaITYII 190
Cdd:PRK08315 38 RDQGLRW-TYREFNEEVDALAKGLLALGIEKG-DR-VGIWAPNVPEWVLTQFATAKIGAILVtinPAYRL--SE-LEYAL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 191 NKADLSVVFC-----DS----------PEKAKLLLSNVEKGETPVLRTIVL--------MNPFDnDLVERGKkcGVELVS 247
Cdd:PRK08315 112 NQSGCKALIAadgfkDSdyvamlyelaPELATCEPGQLQSARLPELRRVIFlgdekhpgMLNFD-ELLALGR--AVDDAE 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 248 LKDIEEEgkanrekpkpPKPDDLAVVCFTSGTTGNPKGAMLSHKNIVSNsaGFMkVTEDLMFpSTQDVLISFLPLAHMFE 327
Cdd:PRK08315 189 LAARQAT----------LDPDDPINIQYTSGTTGFPKGATLTHRNILNN--GYF-IGEAMKL-TEEDRLCIPVPLYHCFG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 328 rvveCV-----VLCHGARI-----GFfqgdirllmDDLKVLQ-------------PTIFpvVPRLLNRMFDrifgqantp 384
Cdd:PRK08315 255 ----MVlgnlaCVTHGATMvypgeGF---------DPLATLAaveeerctalygvPTMF--IAELDHPDFA--------- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 385 vkrwMLDFASkrkeaeLRSGI-------VRndsfwdkiIFHKVQASLGgkvrlM--VTGAapvsptvltflraalgcqfy 455
Cdd:PRK08315 311 ----RFDLSS------LRTGImagspcpIE--------VMKRVIDKMH-----MseVTIA-------------------- 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 456 egYGQTECTAGCSLTIPGD------WTaghVGAPMPCNHVKLVDVEemnyfasKGE-------GEVCIKGSNVFQGYLKD 522
Cdd:PRK08315 348 --YGMTETSPVSTQTRTDDplekrvTT---VGRALPHLEVKIVDPE-------TGEtvprgeqGELCTRGYSVMKGYWND 415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 523 DEKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENVYTRSEPV--VQVF-V----HGESLQA 595
Cdd:PRK08315 416 PEKTAEAIDADGWMHTGDLAVMDEEGYVNIVGRIKDMI-IRGGENIYPREIEEFLYTHPKIqdVQVVgVpdekYGEEVCA 494
|
570 580 590
....*....|....*....|....*....|...
gi 1270536209 596 FlvgiVVPDPDNVMNWAKKRKFegsyeelCKNK 628
Cdd:PRK08315 495 W----IILRPGATLTEEDVRDF-------CRGK 516
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
267-615 |
1.13e-37 |
|
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: 143.96 E-value: 1.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 267 PDDLAVVCFTSGTTGNPKGAMLSHKNIVSNS---AGFMKVTEdlmfpstQDVLISFLPLAHMFERVVEcVVLC--HGARI 341
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNIVNNGyfiGERLGLTE-------QDRLCIPVPLFHCFGSVLG-VLACltHGATM 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 342 GFfqgdIRLLMDDLKVLQP------TIFPVVPRllnrMFDRIFGQANTPvkrwMLDFASkrkeaeLRSGIvrndsfwdki 415
Cdd:cd05917 73 VF----PSPSFDPLAVLEAiekekcTALHGVPT----MFIAELEHPDFD----KFDLSS------LRTGI---------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 416 ifhkvqaslggkvrlmvTGAAPVSPTVLTFLRAALGC-QFYEGYGQTECTAGCSLTIPGDWT---AGHVGAPMPCNHVKL 491
Cdd:cd05917 125 -----------------MAGAPCPPELMKRVIEVMNMkDVTIAYGMTETSPVSTQTRTDDSIekrVNTVGRIMPHTEAKI 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 492 VDvEEMNYFASKGE-GEVCIKGSNVFQGYLKDDEKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAP 570
Cdd:cd05917 188 VD-PEGGIVPPVGVpGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLAVMDEDGYCRIVGRIKDMI-IRGGENIYP 265
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1270536209 571 EKIENVYTRSEPVVQVFV-------HGESLQAFLVGIVVPDP--DNVMNWAKKR 615
Cdd:cd05917 266 REIEEFLHTHPKVSDVQVvgvpderYGEEVCAWIRLKEGAELteEDIKAYCKGK 319
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
119-615 |
4.81e-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: 145.15 E-value: 4.81e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 119 EWISYKEVAERAEYVGSALLHRGFKPSpDQfVGIFAQNRPEWTIVELGCYTYSMVAVPLYDTLGAEAITYIINKADLSVV 198
Cdd:cd05926 13 PALTYADLAELVDDLARQLAALGIKKG-DR-VAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 199 FCDSPEKAKLLLSNVEKG---ETPVLRTIVLMNPFDNDlvergkkcgvELVSLkdieEEGKANREKPKPPKPDDLAVVCF 275
Cdd:cd05926 91 LTPKGELGPASRAASKLGlaiLELALDVGVLIRAPSAE----------SLSNL----LADKKNAKSEGVPLPDDLALILH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 276 TSGTTGNPKGAMLSHKNIVS---NSAGFMKVTEDlmfpstqDVLISFLPLAHMFERVVECV-VLCHGARI----GFfqgD 347
Cdd:cd05926 157 TSGTTGRPKGVPLTHRNLAAsatNITNTYKLTPD-------DRTLVVMPLFHVHGLVASLLsTLAAGGSVvlppRF---S 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 348 IRLLMDDLKVLQPTIFPVVPRLLnrmfdrifgqantpvkRWMLDFASKRKEAELrsgivrndsfwdkiifhkvqaslgGK 427
Cdd:cd05926 227 ASTFWPDVRDYNATWYTAVPTIH----------------QILLNRPEPNPESPP------------------------PK 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 428 VRLMVTGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCSLT--IPGDWTAGHVGAPmpcNHVKLVDV-EEMNYFASKG 504
Cdd:cd05926 267 LRFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEAAHQMTSNplPPGPRKPGSVGKP---VGVEVRILdEDGEILPPGV 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 505 EGEVCIKGSNVFQGYLKDDEKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENVYTRSEPVV 584
Cdd:cd05926 344 VGEICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADGYLFLTGRIKELINRG-GEKISPLEVDGVLLSHPAVL 422
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1270536209 585 Q--VF-----VHGESLQAFlvgiVVP------DPDNVMNWAKKR 615
Cdd:cd05926 423 EavAFgvpdeKYGEEVAAA----VVLregasvTEEELRAFCRKH 462
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
111-598 |
1.04e-36 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 145.20 E-value: 1.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 111 HRKPNQPY-----EWISYKEVAERAEYVgSALLHRGFKPSPDQFVGIFAQNRPEWTIVELGCYTYSMVAV---PLY---- 178
Cdd:PRK08974 34 ARYADQPAfinmgEVMTFRKLEERSRAF-AAYLQNGLGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVnvnPLYtpre 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 179 ------DTlGAEAITYIINkadlsvvFCDSPEKAklllsnVEKgeTPVlRTIVLMNPfdNDLVERGKKCGVELV------ 246
Cdd:PRK08974 113 lehqlnDS-GAKAIVIVSN-------FAHTLEKV------VFK--TPV-KHVILTRM--GDQLSTAKGTLVNFVvkyikr 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 247 -----------SLKDIEEEGKaNREKPKPP-KPDDLAVVCFTSGTTGNPKGAMLSHKNIVSNSAGFMKVTEDLMFPSTQD 314
Cdd:PRK08974 174 lvpkyhlpdaiSFRSALHKGR-RMQYVKPElVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQAKAAYGPLLHPGKEL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 315 VLISfLPLAHMFERVVECVVLCH-GARigffqgdirllmdDLKVLQPTIFP-VVPRLLNRMFDRIFGqANTpvkrwmldf 392
Cdd:PRK08974 253 VVTA-LPLYHIFALTVNCLLFIElGGQ-------------NLLITNPRDIPgFVKELKKYPFTAITG-VNT--------- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 393 askrkeaeLRSGIVRNDSFwdkiifHKVQASlggKVRLMVTGAAPVSPTVLTFLRAALGCQFYEGYGQTECT---AGCSL 469
Cdd:PRK08974 309 --------LFNALLNNEEF------QELDFS---SLKLSVGGGMAVQQAVAERWVKLTGQYLLEGYGLTECSplvSVNPY 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 470 TIPGdwTAGHVGAPMPCNHVKLVDvEEMNYFASKGEGEVCIKGSNVFQGYLKDDEKTAEALdKDGWLHTGDIGKWLPNGT 549
Cdd:PRK08974 372 DLDY--YSGSIGLPVPSTEIKLVD-DDGNEVPPGEPGELWVKGPQVMLGYWQRPEATDEVI-KDGWLATGDIAVMDEEGF 447
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1270536209 550 LKIIDRKKHIFkLAQGEYIAPEKIENVYTRSEPVVQVF-------VHGESLQAFLV 598
Cdd:PRK08974 448 LRIVDRKKDMI-LVSGFNVYPNEIEDVVMLHPKVLEVAavgvpseVSGEAVKIFVV 502
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
246-615 |
1.09e-35 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 142.21 E-value: 1.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 246 VSLKDIEEEGKANREKPKPPKPDDLAVVCFTSGTTGNPKGAMLSHKNIVSNsagfMKVTEDLMFPSTQD---VLISFLPL 322
Cdd:PRK05677 185 VKFNDALAKGAGQPVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVAN----MLQCRALMGSNLNEgceILIAPLPL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 323 AHMFERVVECVVLchgarigffqgdirLLMDDLKVL--QPTIFPVVPRLLNRMFDRIFGQANTpvkrwmldfaskrkeae 400
Cdd:PRK05677 261 YHIYAFTFHCMAM--------------MLIGNHNILisNPRDLPAMVKELGKWKFSGFVGLNT----------------- 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 401 LRSGIVRNDSFwDKIIFHKVQASLGGKVRLMVTGAapvsptvlTFLRAALGCQFYEGYGQTECTAGCSLTIPGDWTAGHV 480
Cdd:PRK05677 310 LFVALCNNEAF-RKLDFSALKLTLSGGMALQLATA--------ERWKEVTGCAICEGYGMTETSPVVSVNPSQAIQVGTI 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 481 GAPMPCNHVKLVDvEEMNYFASKGEGEVCIKGSNVFQGYLKDDEKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIF 560
Cdd:PRK05677 381 GIPVPSTLCKVID-DDGNELPLGEVGELCVKGPQVMKGYWQRPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMI 459
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1270536209 561 kLAQGEYIAPEKIENVYTRSEPVVQVFV-------HGESLQAFlvgiVVPDP------DNVMNWAKKR 615
Cdd:PRK05677 460 -LVSGFNVYPNELEDVLAALPGVLQCAAigvpdekSGEAIKVF----VVVKPgetltkEQVMEHMRAN 522
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
121-615 |
1.95e-35 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 138.96 E-value: 1.95e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 121 ISYKEVAERAEYVGSALLHRGFKPsPDQfVGIFAQNRPEWTIVELGCYTYSMVAVPLYDTLGAEAITYIINKADLSVVFC 200
Cdd:cd05934 4 WTYAELLRESARIAAALAALGIRP-GDR-VALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 201 DspekaklllsnvekgetpvlrtivlmnpfdndlvergkkcgvelvslkdieeegkanrekpkppkpddLAVVCFTSGTT 280
Cdd:cd05934 82 D--------------------------------------------------------------------PASILYTSGTT 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 281 GNPKGAMLSHKNIVS---NSAGFMKVTEDlmfpstqDVLISFLPLAHMfervvecVVLCHGARIGFFQGdirllmddlkv 357
Cdd:cd05934 94 GPPKGVVITHANLTFagyYSARRFGLGED-------DVYLTVLPLFHI-------NAQAVSVLAALSVG----------- 148
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 358 lqpTIFPVVPRllnrmfdrifgqantpvkrwmldFASKRkeaelrsgivrndsFWDKI------IFHKVQASLG------ 425
Cdd:cd05934 149 ---ATLVLLPR-----------------------FSASR--------------FWSDVrrygatVTNYLGAMLSyllaqp 188
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 426 -------GKVRlmVTGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCSLTIPGDWTAGHVGAPMPCNHVKLVDveEMN 498
Cdd:cd05934 189 pspddraHRLR--AAYGAPNPPELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIVD--DDG 264
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 499 YFASKGE-GEVCIK---GSNVFQGYLKDDEKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIE 574
Cdd:cd05934 265 QELPAGEpGELVIRglrGWGFFKGYYNMPEATAEAM-RNGWFHTGDLGYRDADGFFYFVDRKKDMIR-RRGENISSAEVE 342
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1270536209 575 NVYTRSEPVVQVFVHG----ESLQAFLVGIVVP-----DPDNVMNWAKKR 615
Cdd:cd05934 343 RAILRHPAVREAAVVAvpdeVGEDEVKAVVVLRpgetlDPEELFAFCEGQ 392
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
269-615 |
5.06e-35 |
|
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: 135.71 E-value: 5.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 269 DLAVVCFTSGTTGNPKGAMLSHKNIVSNSAGF---MKVTEDlmfpstqDVLISFLPLAHMFERVVECVV-LCHGARI--- 341
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWadcADLTED-------DRYLIINPFFHTFGYKAGIVAcLLTGATVvpv 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 342 GFFqgDIRLLMDDLKVLQPTIFPVVPRLLNRMFDRifgqantpvkrwmldfaSKRKEAELRSgivrndsfwdkiifhkvq 421
Cdd:cd17638 74 AVF--DVDAILEAIERERITVLPGPPTLFQSLLDH-----------------PGRKKFDLSS------------------ 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 422 aslggkVRLMVTGAAPVSPTVLTFLRAALGCQ-FYEGYGQTECTAGcSLTIPGD---WTAGHVGAPMPCNHVKLVDveem 497
Cdd:cd17638 117 ------LRAAVTGAATVPVELVRRMRSELGFEtVLTAYGLTEAGVA-TMCRPGDdaeTVATTCGRACPGFEVRIAD---- 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 498 nyfaskgEGEVCIKGSNVFQGYLKDDEKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENVY 577
Cdd:cd17638 186 -------DGEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGELDERGYLRITDRLKDMY-IVGGFNVYPAEVEGAL 257
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1270536209 578 TRSEPVVQVFV-------HGESLQAFLVG--IVVPDPDNVMNWAKKR 615
Cdd:cd17638 258 AEHPGVAQVAVigvpderMGEVGKAFVVArpGVTLTEEDVIAWCRER 304
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
123-615 |
9.29e-35 |
|
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 162605 [Multi-domain] Cd Length: 436 Bit Score: 137.58 E-value: 9.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 123 YKEVAERAEYVGSALLHRGfkpspdQFVGIFAQNRPEWTIVELGCYTYSMVAVPLYDTLGAEAITYIINKADLSVVFCDS 202
Cdd:TIGR01923 6 DCEAAHLAKALKAQGIRSG------SRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 203 PEKAKLLLSnvekgetpvlrtivlmnpfdndlvergkkcgvelVSLKDIEEEGKANREKPKPPKPDDLAVVCFTSGTTGN 282
Cdd:TIGR01923 80 LLEEKDFQA----------------------------------DSLDRIEAAGRYETSLSASFNMDQIATLMFTSGTTGK 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 283 PKGAMLSHKNIvSNSAgfMKVTEDLMFPSTQDVLISfLPLAHMFERVVECVVLCHGARIGFFQGDIRLLmDDLKVLQPTI 362
Cdd:TIGR01923 126 PKAVPHTFRNH-YASA--VGSKENLGFTEDDNWLLS-LPLYHISGLSILFRWLIEGATLRIVDKFNQLL-EMIANERVTH 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 363 FPVVPRLLNRMFDRIFGQANtpvkrwmldfaskrkeaelrsgivrndsfwdkiifhkvqaslggkVRLMVTGAAPVSptv 442
Cdd:TIGR01923 201 ISLVPTQLNRLLDEGGHNEN---------------------------------------------LRKILLGGSAIP--- 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 443 LTFLRAAL--GCQFYEGYGQTE-CTAGCSLTIPGDWTAGHVGAPMPCNHVKL-VDVEEmnyfaskGEGEVCIKGSNVFQG 518
Cdd:TIGR01923 233 APLIEEAQqyGLPIYLSYGMTEtCSQVTTATPEMLHARPDVGRPLAGREIKIkVDNKE-------GHGEIMVKGANLMKG 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 519 YLKDDEKTaEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENVYTRSEPVVQVFV-------HGE 591
Cdd:TIGR01923 306 YLYQGELT-PAFEQQGWFNTGDIGELDGEGFLYVLGRRDDLI-ISGGENIYPEEIETVLYQHPGIQEAVVvpkpdaeWGQ 383
|
490 500
....*....|....*....|....
gi 1270536209 592 SLQAFLVGIVVPDPDNVMNWAKKR 615
Cdd:TIGR01923 384 VPVAYIVSESDISQAKLIAYLTEK 407
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
247-615 |
2.84e-33 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 135.13 E-value: 2.84e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 247 SLKDIEEEGKANREKPKPPKPDDLAVVCFTSGTTGNPKGAMLSHKNIVSNSA-GFMKVTEdlmFPSTQDVLISFLPLAHM 325
Cdd:PRK05605 198 TLVDAAIGGDGSDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAqGKAWVPG---LGDGPERVLAALPMFHA 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 326 F--ERVVECVVLCHGARIGFFQGDIRLLMDDLKVLQPTIFPVVPRLlnrmFDRIfgqantpvkrwmldfaskRKEAELRs 403
Cdd:PRK05605 275 YglTLCLTLAVSIGGELVLLPAPDIDLILDAMKKHPPTWLPGVPPL----YEKI------------------AEAAEER- 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 404 GIvrndsfwdkiifhkvqaSLGGkVRLMVTGAAPVSPTVLTFLRAALGCQFYEGYGQTECT---AGCSLTipGDWTAGHV 480
Cdd:PRK05605 332 GV-----------------DLSG-VRNAFSGAMALPVSTVELWEKLTGGLLVEGYGLTETSpiiVGNPMS--DDRRPGYV 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 481 GAPMPCNHVKLVDVEEMNYFASKGE-GEVCIKGSNVFQGYLKDDEKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHI 559
Cdd:PRK05605 392 GVPFPDTEVRIVDPEDPDETMPDGEeGELLVRGPQVFKGYWNRPEETAKSF-LDGWFRTGDVVVMEEDGFIRIVDRIKEL 470
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1270536209 560 FkLAQGEYIAPEKIENVYTRSEPVVQVFVHG-------ESLQAFLV---GIVVpDPDNVMNWAKKR 615
Cdd:PRK05605 471 I-ITGGFNVYPAEVEEVLREHPGVEDAAVVGlpredgsEEVVAAVVlepGAAL-DPEGLRAYCREH 534
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
113-574 |
4.23e-33 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 134.49 E-value: 4.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 113 KPNQPYEWiSYKEVAERAEYVGSALLHRGFKPSpdqfvGIFAQNRPEW---TIVELGCYTYSMVAVPLYDTLGAEAITYI 189
Cdd:PRK06087 43 VDNHGASY-TYSALDHAASRLANWLLAKGIEPG-----DRVAFQLPGWcefTIIYLACLKVGAVSVPLLPSWREAELVWV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 190 INKADLSVVFCDSPEKA----KLLLSNVEkgETPVLRTIVLMN---PFDNDLvergkkcgvelvSLKDIEEEGKAnREKP 262
Cdd:PRK06087 117 LNKCQAKMFFAPTLFKQtrpvDLILPLQN--QLPQLQQIVGVDklaPATSSL------------SLSQIIADYEP-LTTA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 263 KPPKPDDLAVVCFTSGTTGNPKGAMLSHKNIVSNSAGFMKVTEdlmfPSTQDVLISFLPLAHMfervvecvvlchgarIG 342
Cdd:PRK06087 182 ITTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLN----LTWQDVFMMPAPLGHA---------------TG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 343 FFQGDIR-LLMDDLKVLQPTIFPVVP-RLLNRmfDRI-FGQANTPVKRWMLDfASKRKEAELRSgivrndsfwdkiifhk 419
Cdd:PRK06087 243 FLHGVTApFLIGARSVLLDIFTPDAClALLEQ--QRCtCMLGATPFIYDLLN-LLEKQPADLSA---------------- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 420 vqaslggkVRLMVTGAAPVsPTVLTflRAAL--GCQFYEGYGQTECT--AGCSLTIPGDWTAGHVGAPMPCNHVKLVDvE 495
Cdd:PRK06087 304 --------LRFFLCGGTTI-PKKVA--RECQqrGIKLLSVYGSTESSphAVVNLDDPLSRFMHTDGYAAAGVEIKVVD-E 371
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1270536209 496 EMNYFASKGEGEVCIKGSNVFQGYLKDDEKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIE 574
Cdd:PRK06087 372 ARKTLPPGCEGEEASRGPNVFMGYLDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDII-VRGGENISSREVE 449
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
121-610 |
1.16e-32 |
|
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: 131.50 E-value: 1.16e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 121 ISYKEVAERAEYVGSALLHRGFKPspDQFVGIFAQNRPEWTIVELGCY----TYsmvaVPLYDTLGAEAITYIINKAdls 196
Cdd:cd05930 13 LTYAELDARANRLARYLRERGVGP--GDLVAVLLERSLEMVVAILAVLkagaAY----VPLDPSYPAERLAYILEDS--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 197 vvfcdspeKAKLLLSNvekgetpvlrtivlmnpfdndlvergkkcgvelvslkdieeegkanrekpkppkPDDLAVVCFT 276
Cdd:cd05930 84 --------GAKLVLTD------------------------------------------------------PDDLAYVIYT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 277 SGTTGNPKGAMLSHKNIVSnsagFMKVTEDLMFPSTQDVLISFLPLAH-MFerVVE-CVVLCHGARI----GFFQGDIRL 350
Cdd:cd05930 102 SGSTGKPKGVMVEHRGLVN----LLLWMQEAYPLTPGDRVLQFTSFSFdVS--VWEiFGALLAGATLvvlpEEVRKDPEA 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 351 LMDDLKVLQPTIFPVVPRLLNRMFDRIFGQANTPVKRWMLdfaskrkeaelrsgivrndsfwdkiifhkvqaslggkvrl 430
Cdd:cd05930 176 LADLLAEEGITVLHLTPSLLRLLLQELELAALPSLRLVLV---------------------------------------- 215
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 431 mvtGAAPVSPTVLT-FLRAALGCQFYEGYGQTECTAGCSL-TIPGDWTAGH---VGAPMPCNHVKLVDvEEMNYFASKGE 505
Cdd:cd05930 216 ---GGEALPPDLVRrWRELLPGARLVNLYGPTEATVDATYyRVPPDDEEDGrvpIGRPIPNTRVYVLD-ENLRPVPPGVP 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 506 GEVCIKGSNVFQGYLKDDEKTAEA-----LDKDGWLH-TGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENVYTR 579
Cdd:cd05930 292 GELYIGGAGLARGYLNRPELTAERfvpnpFGPGERMYrTGDLVRWLPDGNLEFLGRIDDQVKIR-GYRIELGEIEAALLA 370
|
490 500 510
....*....|....*....|....*....|....
gi 1270536209 580 SEPVVQVFV---HGESLQAFLVGIVVPDPDNVMN 610
Cdd:cd05930 371 HPGVREAAVvarEDGDGEKRLVAYVVPDEGGELD 404
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
122-605 |
1.29e-32 |
|
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: 132.37 E-value: 1.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 122 SYKEVAERAEYVGSALLHRGFKPspDQFVGIFAQNrpewTIVELGCYtysmVAVPLydtLGA-----------EAITYII 190
Cdd:cd12119 27 TYAEVAERARRLANALRRLGVKP--GDRVATLAWN----THRHLELY----YAVPG---MGAvlhtinprlfpEQIAYII 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 191 NKADLSVVFCDsPEKAKLLlsNVEKGETPVLRTIVLMnPFDNDLVERGkkcGVELVSLKDIEEEgkanrEKPKPPKPD-- 268
Cdd:cd12119 94 NHAEDRVVFVD-RDFLPLL--EAIAPRLPTVEHVVVM-TDDAAMPEPA---GVGVLAYEELLAA-----ESPEYDWPDfd 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 269 --DLAVVCFTSGTTGNPKGAMLSHKNIVSNSagFMKVTEDLMFPSTQDVlisFLPLAHMFervvecvvlcH--------- 337
Cdd:cd12119 162 enTAAAICYTSGTTGNPKGVVYSHRSLVLHA--MAALLTDGLGLSESDV---VLPVVPMF----------Hvnawglpya 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 338 ----GARI----GFFQGDIRL-LMDDLKVlqpTIFPVVPRLLNRMFDRifgqantpVKRWMLDFASKRKeaelrsgivrn 408
Cdd:cd12119 227 aamvGAKLvlpgPYLDPASLAeLIEREGV---TFAAGVPTVWQGLLDH--------LEANGRDLSSLRR----------- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 409 dsfwdkiifhkvqaslggkvrlMVTGAAPVSPTVLTFLRAaLGCQFYEGYGQTE-CTAGCSLTIPGDWTAGHV------- 480
Cdd:cd12119 285 ----------------------VVIGGSAVPRSLIEAFEE-RGVRVIHAWGMTEtSPLGTVARPPSEHSNLSEdeqlalr 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 481 ---GAPMPCNHVKLVDvEEMNYFASKGE--GEVCIKGSNVFQGYLKDDEkTAEALDKDGWLHTGDIGKWLPNGTLKIIDR 555
Cdd:cd12119 342 akqGRPVPGVELRIVD-DDGRELPWDGKavGELQVRGPWVTKSYYKNDE-ESEALTEDGWLRTGDVATIDEDGYLTITDR 419
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1270536209 556 KKHIFKLAqGEYIAPEKIENVYTRSEPVVQVFVhgeslqaflvgIVVPDP 605
Cdd:cd12119 420 SKDVIKSG-GEWISSVELENAIMAHPAVAEAAV-----------IGVPHP 457
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
122-588 |
1.90e-32 |
|
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: 130.08 E-value: 1.90e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 122 SYKEVAERAEYVGSALLHRGfKPSPDQFVGIFAqNRPEWTIVEL-------GCYtysmvaVPLYDTLGAEAITYIINKAD 194
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAG-GVGPGDRVAVLL-ERSAELVVAIlavlkagAAY------VPLDPAYPAERLAFILEDAG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 195 LSVVFCDSPekaklllsnvekgetpvlrtivlmnpFDNDLVERGKKCGVELVSLKDIEEEGKANREKPKPPKPDDLAVVC 274
Cdd:TIGR01733 73 ARLLLTDSA--------------------------LASRLAGLVLPVILLDPLELAALDDAPAPPPPDAPSGPDDLAYVI 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 275 FTSGTTGNPKGAMLSHKNIVSNSAGFMkvteDLMFPSTQDVLISFLPLAH------MFervvecVVLCHGAR-------- 340
Cdd:TIGR01733 127 YTSGSTGRPKGVVVTHRSLVNLLAWLA----RRYGLDPDDRVLQFASLSFdasveeIF------GALLAGATlvvppede 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 341 IGFFQGDIRLLMDDLKVlqpTIFPVVPRLLNRMFDRIFGQANTpvkrwmldfaskrkeaelrsgivrndsfwdkiifhkv 420
Cdd:TIGR01733 197 ERDDAALLAALIAEHPV---TVLNLTPSLLALLAAALPPALAS------------------------------------- 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 421 qaslggkVRLMVTGAAPVSPTVLTFLRAALG-CQFYEGYGQTECTAGCSLT-IPGDWTAGHV----GAPMPCNHVKLVDv 494
Cdd:TIGR01733 237 -------LRLVILGGEALTPALVDRWRARGPgARLINLYGPTETTVWSTATlVDPDDAPRESpvpiGRPLANTRLYVLD- 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 495 EEMNYFASKGEGEVCIKGSNVFQGYLKDDEKTAE--------ALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGE 566
Cdd:TIGR01733 309 DDLRPVPVGVVGELYIGGPGVARGYLNRPELTAErfvpdpfaGGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKI-RGY 387
|
490 500
....*....|....*....|..
gi 1270536209 567 YIAPEKIENVYTRSEPVVQVFV 588
Cdd:TIGR01733 388 RIELGEIEAALLRHPGVREAVV 409
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
255-605 |
1.95e-32 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 132.69 E-value: 1.95e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 255 GKANREKPKPPKPDDLAVVCFTSGTTGNPKGAMLSHKNIVSN---SAGFMKVTEDLMfpSTQDVLISFLPLAHMFERVVE 331
Cdd:PRK08751 195 GRKHSMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANmqqAHQWLAGTGKLE--EGCEVVITALPLYHIFALTAN 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 332 CVVLchgARIGFFQG------DIRLLMDDLKVLQPTIFPVVPRLLNrmfdrifGQANTPvkrwmldfaskrkeaelrsgi 405
Cdd:PRK08751 273 GLVF---MKIGGCNHlisnprDMPGFVKELKKTRFTAFTGVNTLFN-------GLLNTP--------------------- 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 406 vrndsFWDKIIFHKVQASLGGkvrlmvtGAApVSPTVLTFLRAALGCQFYEGYGQTECT-AGCSLTIPGDWTAGHVGAPM 484
Cdd:PRK08751 322 -----GFDQIDFSSLKMTLGG-------GMA-VQRSVAERWKQVTGLTLVEAYGLTETSpAACINPLTLKEYNGSIGLPI 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 485 PCNHVKLVDveEMNYFASKGE-GEVCIKGSNVFQGYLKDDEKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLA 563
Cdd:PRK08751 389 PSTDACIKD--DAGTVLAIGEiGELCIKGPQVMKGYWKRPEETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMI-LV 465
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1270536209 564 QGEYIAPEKIENVYTRSEPVVQVFVHG----ESLQAFLVGIVVPDP 605
Cdd:PRK08751 466 SGFNVYPNEIEDVIAMMPGVLEVAAVGvpdeKSGEIVKVVIVKKDP 511
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
121-606 |
3.02e-32 |
|
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: 131.50 E-value: 3.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 121 ISYKEVAERAEYVGSALLHRGFKPspDQFVGIFAQNRPEWTIVELGCYTYSMVAVPLYDTLGAEAITYIINKADLSVVFC 200
Cdd:cd17642 45 YSYAEYLEMSVRLAEALKKYGLKQ--NDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFC 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 201 DSPEKAKLLlsNVEKgETPVLRTIVLMnpfDNDLVERGKKCgveLVSLKDIEEEGKANREKPKPP---KPDDLAVVCFTS 277
Cdd:cd17642 123 SKKGLQKVL--NVQK-KLKIIKTIIIL---DSKEDYKGYQC---LYTFITQNLPPGFNEYDFKPPsfdRDEQVALIMNSS 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 278 GTTGNPKGAMLSHKNIVSN-SAGFMKVTEDLMFPSTqdVLISFLPLAHMFERVVECVVLCHGARIGF---FQGDIRL-LM 352
Cdd:cd17642 194 GSTGLPKGVQLTHKNIVARfSHARDPIFGNQIIPDT--AILTVIPFHHGFGMFTTLGYLICGFRVVLmykFEEELFLrSL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 353 DDLKV----LQPTIFPVVPRllnrmfdrifgqaNTPVKRWMLdfaSKRKEaelrsgivrndsfwdkiifhkvqaslggkv 428
Cdd:cd17642 272 QDYKVqsalLVPTLFAFFAK-------------STLVDKYDL---SNLHE------------------------------ 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 429 rlMVTGAAPVSPTVLTFLRAALGCQFY-EGYGQTECTAGCSLTIPGDWTAGHVGAPMPCNHVKLVDVEEMNYFASKGEGE 507
Cdd:cd17642 306 --IASGGAPLSKEVGEAVAKRFKLPGIrQGYGLTETTSAILITPEGDDKPGAVGKVVPFFYAKVVDLDTGKTLGPNERGE 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 508 VCIKGSNVFQGYLKDDEKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENVYTRSEPVVQVF 587
Cdd:cd17642 384 LCVKGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKY-KGYQVPPAELESILLQHPKIFDAG 462
|
490
....*....|....*....
gi 1270536209 588 VHGeslqaflvgivVPDPD 606
Cdd:cd17642 463 VAG-----------IPDED 470
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
246-606 |
5.36e-32 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 131.30 E-value: 5.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 246 VSLKDIEEEGKANREKPKPPKPDDLAVVCFTSGTTGNPKGAMLSHKNIVSN---SAGFMKVTEDLMFPSTQDVLISFLPL 322
Cdd:PRK07059 182 VRFNDALAEGARQTFKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANvlqMEAWLQPAFEKKPRPDQLNFVCALPL 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 323 AHMFERVVECVVlchGARIGffqG---------DIRLLMDDLKVLQPTIFPVVPRLLNRMFdrifgqaNTPvkrwmlDFa 393
Cdd:PRK07059 262 YHIFALTVCGLL---GMRTG---GrnilipnprDIPGFIKELKKYQVHIFPAVNTLYNALL-------NNP------DF- 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 394 skrkeaelrsgivrndsfwDKIIFHKVQASLGGkvrlmvtGAApVSPTVLTFLRAALGCQFYEGYG--QTECTAGCSLTI 471
Cdd:PRK07059 322 -------------------DKLDFSKLIVANGG-------GMA-VQRPVAERWLEMTGCPITEGYGlsETSPVATCNPVD 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 472 PGDWTaGHVGAPMPCNHVKLVDvEEMNYFASKGEGEVCIKGSNVFQGYLKDDEKTAEALDKDGWLHTGDIGKWLPNGTLK 551
Cdd:PRK07059 375 ATEFS-GTIGLPLPSTEVSIRD-DDGNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTK 452
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1270536209 552 IIDRKKHIFkLAQGEYIAPEKIENVYTRSEPVVQVFV------H-GESLQAFlvgIVVPDPD 606
Cdd:PRK07059 453 IVDRKKDMI-LVSGFNVYPNEIEEVVASHPGVLEVAAvgvpdeHsGEAVKLF---VVKKDPA 510
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
246-576 |
9.54e-32 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 130.71 E-value: 9.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 246 VSLKDIEEEGKANREKPKPPKPDDLAVVCFTSGTTGNPKGAMLSHKNIVSN----SAGFMKVTED--LMFPSTQDVLISF 319
Cdd:PRK12492 185 VPFKQALRQGRGLSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANmlqvRACLSQLGPDgqPLMKEGQEVMIAP 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 320 LPLAHMFERVVECVVLchgarigFFQGDIRLLMDDlkvlqptifpvvPRLLNRMFDRIfgqantpvKRWmlDFASKRKEA 399
Cdd:PRK12492 265 LPLYHIYAFTANCMCM-------MVSGNHNVLITN------------PRDIPGFIKEL--------GKW--RFSALLGLN 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 400 ELRSGIVRNDSFwDKIIFHKVQASLGGkvrlmvtGAAPVSPTVLTFlRAALGCQFYEGYGQTECTAGCSLTIPGDWTA-G 478
Cdd:PRK12492 316 TLFVALMDHPGF-KDLDFSALKLTNSG-------GTALVKATAERW-EQLTGCTIVEGYGLTETSPVASTNPYGELARlG 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 479 HVGAPMPCNHVKLVDvEEMNYFASKGEGEVCIKGSNVFQGYLKDDEKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKH 558
Cdd:PRK12492 387 TVGIPVPGTALKVID-DDGNELPLGERGELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRKKD 465
|
330
....*....|....*...
gi 1270536209 559 IFkLAQGEYIAPEKIENV 576
Cdd:PRK12492 466 LI-IVSGFNVYPNEIEDV 482
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
121-606 |
2.23e-31 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 128.45 E-value: 2.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 121 ISYKEVAERAEYVGSALLHRGFKPSpDQfVGIFAQNRPEWTIVELGCYTYSMVAVPLYDTLGAEAITYIINKADLSVVFC 200
Cdd:PRK07514 29 YTYGDLDAASARLANLLVALGVKPG-DR-VAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEPALVVC 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 201 DsPEKAKLLLSNVEKGETPVLRTIvlmnpfDND----LVERGKKCGVELVslkdieeegkanrekPKPPKPDDLAVVCFT 276
Cdd:PRK07514 107 D-PANFAWLSKIAAAAGAPHVETL------DADgtgsLLEAAAAAPDDFE---------------TVPRGADDLAAILYT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 277 SGTTGNPKGAMLSHKNIVSNSA------GFmkvTEDlmfpstqDVLISFLPLAH---MFerVVECVVLCHGARIGFFQG- 346
Cdd:PRK07514 165 SGTTGRSKGAMLSHGNLLSNALtlvdywRF---TPD-------DVLIHALPIFHthgLF--VATNVALLAGASMIFLPKf 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 347 DIRLLMDDLKvlQPTIFPVVP----RLL-NRMFDRifgqantpvkrwmldfaskrkEAelrsgiVRNdsfwdkiifhkvq 421
Cdd:PRK07514 233 DPDAVLALMP--RATVMMGVPtfytRLLqEPRLTR---------------------EA------AAH------------- 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 422 aslggkVRLMVTGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCSLTIPGDWTAGHVGAPMPCNHVKLVDVEEMNYFA 501
Cdd:PRK07514 271 ------MRLFISGSAPLLAETHREFQERTGHAILERYGMTETNMNTSNPYDGERRAGTVGFPLPGVSLRVTDPETGAELP 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 502 SKGEGEVCIKGSNVFQGYLKDDEKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIfkLAQGEY-IAPEKIENVYTRS 580
Cdd:PRK07514 345 PGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGFFITGDLGKIDERGYVHIVGRGKDL--IISGGYnVYPKEVEGEIDEL 422
|
490 500 510
....*....|....*....|....*....|...
gi 1270536209 581 EPVVQVFV----H---GESlqafLVGIVVPDPD 606
Cdd:PRK07514 423 PGVVESAVigvpHpdfGEG----VTAVVVPKPG 451
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
122-598 |
3.81e-31 |
|
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.
Pssm-ID: 341229 [Multi-domain] Cd Length: 437 Bit Score: 126.73 E-value: 3.81e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 122 SYKEVAERAEYVGSALLHRGFKPspDQFVGIFAQNRPEWTIVELGCYTYSMVAVPLYDTLGAEAITYIINKAdlsvvfcd 201
Cdd:cd05903 3 TYSELDTRADRLAAGLAALGVGP--GDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRA-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 202 speKAKLLLSNVEKGETpvlrtivlmnpfdndlvergkkcgvelvslkDIEEEgkanrekpkppkPDDLAVVCFTSGTTG 281
Cdd:cd05903 73 ---KAKVFVVPERFRQF-------------------------------DPAAM------------PDAVALLLFTSGTTG 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 282 NPKGAMLSHKNIVSNSAGFMkvtEDLMFPStQDVLISFLPLAHMFERVvecvvlcHGARIGFFQGDIRLLMDdlkVLQPT 361
Cdd:cd05903 107 EPKGVMHSHNTLSASIRQYA---ERLGLGP-GDVFLVASPMAHQTGFV-------YGFTLPLLLGAPVVLQD---IWDPD 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 362 ifpVVPRLLNRmfDRI-FGQANTPvkrwmldFASKRKEAELRSGIVRNDsfwdkiifhkvqaslggkVRLMVTGAAPVSP 440
Cdd:cd05903 173 ---KALALMRE--HGVtFMMGATP-------FLTDLLNAVEEAGEPLSR------------------LRTFVCGGATVPR 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 441 TVLTFLRAALGCQFYEGYGQTEC-TAGCSLTIPGDWTAGHV-GAPMPCNHVKLVDvEEMNYFASKGEGEVCIKGSNVFQG 518
Cdd:cd05903 223 SLARRAAELLGAKVCSAYGSTECpGAVTSITPAPEDRRLYTdGRPLPGVEIKVVD-DTGATLAPGVEGELLSRGPSVFLG 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 519 YLKDDEKTAEALDkDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENVYTRSEPVVQVFV-------HGE 591
Cdd:cd05903 302 YLDRPDLTADAAP-EGWFRTGDLARLDEDGYLRITGRSKDII-IRGGENIPVLEVEDLLLGHPGVIEAAVvalpderLGE 379
|
....*..
gi 1270536209 592 SLQAFLV 598
Cdd:cd05903 380 RACAVVV 386
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
121-576 |
4.44e-31 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 128.69 E-value: 4.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 121 ISYKEVAERAEYVGSALLHRGFKPspDQFVGIFAQNRPEWTIVELGCYTYSMVAVPLYDTLGAEAITYIINKADLSVVFC 200
Cdd:COG0365 40 LTYAELRREVNRFANALRALGVKK--GDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLIT 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 201 DS----PEKAKLLLSNVEK--GETPVLRTIVLMNPFDNDLVERGkkcgveLVSLKDIEEEGKANREkPKPPKPDDLAVVC 274
Cdd:COG0365 118 ADgglrGGKVIDLKEKVDEalEELPSLEHVIVVGRTGADVPMEG------DLDWDELLAAASAEFE-PEPTDADDPLFIL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 275 FTSGTTGNPKGAMLSHKNIVSNSAGFMK----VTE-DLMFpSTQDV-------LISFLPLAHmfervvECVVLCHGARIG 342
Cdd:COG0365 191 YTSGTTGKPKGVVHTHGGYLVHAATTAKyvldLKPgDVFW-CTADIgwatghsYIVYGPLLN------GATVVLYEGRPD 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 343 FFQGDiRL--LMDDLKVlqpTIFPVVPRLLnRMFdrifgqantpvKRWMLDFASKRKeaeLRSgivrndsfwdkiifhkv 420
Cdd:COG0365 264 FPDPG-RLweLIEKYGV---TVFFTAPTAI-RAL-----------MKAGDEPLKKYD---LSS----------------- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 421 qaslggkVRLMVTGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCSLTIPGDWT-AGHVGAPMPCNHVKLVDvEEMNY 499
Cdd:COG0365 308 -------LRLLGSAGEPLNPEVWEWWYEAVGVPIVDGWGQTETGGIFISNLPGLPVkPGSMGKPVPGYDVAVVD-EDGNP 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 500 FASKGEGEVCIKGSN--VFQGYLKDDEKTAEAL--DKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIEN 575
Cdd:COG0365 380 VPPGEEGELVIKGPWpgMFRGYWNDPERYRETYfgRFPGWYRTGDGARRDEDGYFWILGRSDDVINVS-GHRIGTAEIES 458
|
.
gi 1270536209 576 V 576
Cdd:COG0365 459 A 459
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
119-590 |
5.66e-31 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 127.28 E-value: 5.66e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 119 EWISYKEVAERAEYVGSALLHRgFKPSPDQFVGIFAQNRPEWTIVELGCYTYSMVAVPLYDTLGAEAITYIINKADLSVV 198
Cdd:PRK06839 26 EEMTYKQLHEYVSKVAAYLIYE-LNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTTVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 199 FCdSPEkaklllsnvekgetpvlrtivlmnpFDNDLVERGKKCGVE-LVSLKDIEEEGKANREKPKPPKPDDLAVVCFTS 277
Cdd:PRK06839 105 FV-EKT-------------------------FQNMALSMQKVSYVQrVISITSLKEIEDRKIDNFVEKNESASFIICYTS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 278 GTTGNPKGAMLSHKNIVSNSAGFMkVTEDLmfpSTQDVLISFLPLAHMfervvecvvlchgARIGFFQgdirllmddlkv 357
Cdd:PRK06839 159 GTTGKPKGAVLTQENMFWNALNNT-FAIDL---TMHDRSIVLLPLFHI-------------GGIGLFA------------ 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 358 lQPTIFP----VVPRLLN-----RMFDR-----IFGqanTPVKRWMLDFASKRKEAELRSgivrndsfwdkiifhkvqas 423
Cdd:PRK06839 210 -FPTLFAggviIVPRKFEptkalSMIEKhkvtvVMG---VPTIHQALINCSKFETTNLQS-------------------- 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 424 lggkVRLMVTGAAPVsPTVLTFLRAALGCQFYEGYGQTECTAGCSLTIPGDW--TAGHVGAPMPCNHVKLVDvEEMNYFA 501
Cdd:PRK06839 266 ----VRWFYNGGAPC-PEELMREFIDRGFLFGQGFGMTETSPTVFMLSEEDArrKVGSIGKPVLFCDYELID-ENKNKVE 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 502 SKGEGEVCIKGSNVFQGYLKDDEKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENVYTRSE 581
Cdd:PRK06839 340 VGEVGELLIRGPNVMKEYWNRPDATEETI-QDGWLCTGDLARVDEDGFVYIVGRKKEMI-ISGGENIYPLEVEQVINKLS 417
|
....*....
gi 1270536209 582 PVVQVFVHG 590
Cdd:PRK06839 418 DVYEVAVVG 426
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
95-574 |
8.18e-31 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 127.40 E-value: 8.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 95 IFQRGRRVSNNgPCLGHRKPNQPYewiSYKEVAERAEYVGSALLHRGFKPSpdQFVGIFAQNRPEWTIVELGCytySMva 174
Cdd:PLN02246 29 CFERLSEFSDR-PCLIDGATGRVY---TYADVELLSRRVAAGLHKLGIRQG--DVVMLLLPNCPEFVLAFLGA---SR-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 175 vplydtLGAEAITyiINKadlsvvFCDSPEKAK-LLLSNVekgetpvlRTIVLMNPFDNDLVERGKKCGVELVSLKDIEE 253
Cdd:PLN02246 98 ------RGAVTTT--ANP------FYTPAEIAKqAKASGA--------KLIITQSCYVDKLKGLAEDDGVTVVTIDDPPE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 254 ------EGKANREKPKPP---KPDDLAVVCFTSGTTGNPKGAMLSHKNIVSNSAgfMKVTED---LMFPStQDVLISFLP 321
Cdd:PLN02246 156 gclhfsELTQADENELPEveiSPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVA--QQVDGEnpnLYFHS-DDVILCVLP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 322 LAHMFErvVECVVLChGARIG--------FfqgDIRLLMDDLKVLQPTIFPVVPrllnrmfdrifgqantPVkrwMLDFA 393
Cdd:PLN02246 233 MFHIYS--LNSVLLC-GLRVGaailimpkF---EIGALLELIQRHKVTIAPFVP----------------PI---VLAIA 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 394 skrkeaelRSGIVRNDSFwdkiifhkvqASlggkVRLMVTGAAPVSPTVLTFLRAAL-GCQFYEGYGQTEctAGCSLTI- 471
Cdd:PLN02246 288 --------KSPVVEKYDL----------SS----IRMVLSGAAPLGKELEDAFRAKLpNAVLGQGYGMTE--AGPVLAMc 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 472 ------PGDWTAGHVGAPMPCNHVKLVDVEEMNYFASKGEGEVCIKGSNVFQGYLKDDEKTAEALDKDGWLHTGDIGKWL 545
Cdd:PLN02246 344 lafakePFPVKSGSCGTVVRNAELKIVDPETGASLPRNQPGEICIRGPQIMKGYLNDPEATANTIDKDGWLHTGDIGYID 423
|
490 500
....*....|....*....|....*....
gi 1270536209 546 PNGTLKIIDRKKHIFKLaQGEYIAPEKIE 574
Cdd:PLN02246 424 DDDELFIVDRLKELIKY-KGFQVAPAELE 451
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
121-576 |
2.61e-30 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 125.86 E-value: 2.61e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 121 ISYKEVAERAEYVGSALLHRGFKPSpdQFVGIFAQNRPEWTIVELGCytysMVAVPLYDTLGAEAITYIINKADlsvvfc 200
Cdd:PLN02330 56 VTYGEVVRDTRRFAKALRSLGLRKG--QVVVVVLPNVAEYGIVALGI----MAAGGVFSGANPTALESEIKKQA------ 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 201 dSPEKAKLLLSN---VEKGETPVLRTIVL--------MNPfdNDLVERGKKCGVELVSLKDIEEegkanrekpkppkpdD 269
Cdd:PLN02330 124 -EAAGAKLIVTNdtnYGKVKGLGLPVIVLgeekiegaVNW--KELLEAADRAGDTSDNEEILQT---------------D 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 270 LAVVCFTSGTTGNPKGAMLSHKNIVSN-SAGFMKVTEDLMfpsTQDVLISFLPLAHMFERVVECVVLCH--GARIGFFQG 346
Cdd:PLN02330 186 LCALPFSSGTTGISKGVMLTHRNLVANlCSSLFSVGPEMI---GQVVTLGLIPFFHIYGITGICCATLRnkGKVVVMSRF 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 347 DIRLLMDDLKVLQPTIFPVVPRLlnrmfdrIFGQANTPVKrwmldfaskrkeaelrsgivrndsfwDKIIFHKVqaslgg 426
Cdd:PLN02330 263 ELRTFLNALITQEVSFAPIVPPI-------ILNLVKNPIV--------------------------EEFDLSKL------ 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 427 KVRLMVTGAAPVSPTVLTFLRAAL-GCQFYEGYGQTECTagCSLTIPGDWTAGH-------VGAPMPCNHVKLVDVEEMN 498
Cdd:PLN02330 304 KLQAIMTAAAPLAPELLTAFEAKFpGVQVQEAYGLTEHS--CITLTHGDPEKGHgiakknsVGFILPNLEVKFIDPDTGR 381
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1270536209 499 YFASKGEGEVCIKGSNVFQGYLKDDEKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENV 576
Cdd:PLN02330 382 SLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIGYIDDDGDIFIVDRIKELIKY-KGFQVAPAELEAI 458
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
263-574 |
2.69e-30 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 128.12 E-value: 2.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 263 KPPKPDDLAVVCFTSGTTGNPKGAMLSHKNIVSNsagfMKVTEDLMFPSTQDVLISFLPLAHMFERVVE--------CVV 334
Cdd:PRK08633 777 PTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSN----IEQISDVFNLRNDDVILSSLPFFHSFGLTVTlwlpllegIKV 852
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 335 LCH-----GARIGffqgdirLLMDDLKVlqpTIFPVVPRLLnRMFDRifgqaNTPVKRwmLDFASkrkeaelrsgivrnd 409
Cdd:PRK08633 853 VYHpdptdALGIA-------KLVAKHRA---TILLGTPTFL-RLYLR-----NKKLHP--LMFAS--------------- 899
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 410 sfwdkiifhkvqaslggkVRLMVTGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCSLTIP-----GDWT-----AGH 479
Cdd:PRK08633 900 ------------------LRLVVAGAEKLKPEVADAFEEKFGIRILEGYGATETSPVASVNLPdvlaaDFKRqtgskEGS 961
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 480 VGAPMPCNHVKLVDVEEMNYFASKGEGEVCIKGSNVFQGYLKDDEKTAEAL---DKDGWLHTGDIGKWLPNGTLKIIDRK 556
Cdd:PRK08633 962 VGMPLPGVAVRIVDPETFEELPPGEDGLILIGGPQVMKGYLGDPEKTAEVIkdiDGIGWYVTGDKGHLDEDGFLTITDRY 1041
|
330
....*....|....*...
gi 1270536209 557 KHIFKLAqGEYIAPEKIE 574
Cdd:PRK08633 1042 SRFAKIG-GEMVPLGAVE 1058
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
117-557 |
6.44e-30 |
|
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: 124.70 E-value: 6.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 117 PYEWISYKEVAERAEYVGSALLHRGFKPsPDQFVGIFAQNRPewTIVEL-GCYTYSMVAVPLydtlgAEAITYiinkadl 195
Cdd:cd05906 36 SEEFQSYQDLLEDARRLAAGLRQLGLRP-GDSVILQFDDNED--FIPAFwACVLAGFVPAPL-----TVPPTY------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 196 svvfcDSPEKAKLLLSNVEK--GETPVLRTIVLMNPFDnDLVERGKKCGVELVSlkdIEEEGKANREKPKPPK-PDDLAV 272
Cdd:cd05906 101 -----DEPNARLRKLRHIWQllGSPVVLTDAELVAEFA-GLETLSGLPGIRVLS---IEELLDTAADHDLPQSrPDDLAL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 273 VCFTSGTTGNPKGAMLSHKNIVSNSAGfmKVTedlMFPST-QDVLISFLPLAHmfervVECVVLCHGArigffqgDIRLL 351
Cdd:cd05906 172 LMLTSGSTGFPKAVPLTHRNILARSAG--KIQ---HNGLTpQDVFLNWVPLDH-----VGGLVELHLR-------AVYLG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 352 MDDLKVLQPTIFPVVPRLLnRMFDRiFGQANTpvkrWMLDFA-SKRKEAELRsgivRNDSFWDkiifhkvqasLGGKVRL 430
Cdd:cd05906 235 CQQVHVPTEEILADPLRWL-DLIDR-YRVTIT----WAPNFAfALLNDLLEE----IEDGTWD----------LSSLRYL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 431 MVTGAAPVSPTVLTFLR--AALGCQ---FYEGYGQTECTAGC--SLTIP-GDWTAGH----VGAPMPCNHVKLVDVEEmn 498
Cdd:cd05906 295 VNAGEAVVAKTIRRLLRllEPYGLPpdaIRPAFGMTETCSGViySRSFPtYDHSQALefvsLGRPIPGVSMRIVDDEG-- 372
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1270536209 499 yfASKGEGEVC---IKGSNVFQGYLKDDEKTAEALDKDGWLHTGDIGkWLPNGTLKIIDRKK 557
Cdd:cd05906 373 --QLLPEGEVGrlqVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLG-FLDNGNLTITGRTK 431
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
121-604 |
7.76e-30 |
|
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: 122.80 E-value: 7.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 121 ISYKEVAERAEYVGSALLHRGFKPSpdQFVGIFAQNRPEW-----TIVELGCyTYsmvaVPLYDTLGAEAITYIINKADl 195
Cdd:cd17653 23 LTYGELDAASNALANRLLQLGVVPG--DVVPLLSDRSLEMlvailAILKAGA-AY----VPLDAKLPSARIQAILRTSG- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 196 svvfcdspekAKLLLSNvekgetpvlrtivlmnpfdndlvergkkcgvelvslkdieeegkanrekpkpPKPDDLAVVCF 275
Cdd:cd17653 95 ----------ATLLLTT----------------------------------------------------DSPDDLAYIIF 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 276 TSGTTGNPKGAMLSHKNI---VSNSAGFMKVTedlmfPSTQDVL---ISFLP-LAHMFervvecVVLCHGARIgFFQGDI 348
Cdd:cd17653 113 TSGSTGIPKGVMVPHRGVlnyVSQPPARLDVG-----PGSRVAQvlsIAFDAcIGEIF------STLCNGGTL-VLADPS 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 349 RLLMDDLKVLqpTIFPVVPRLLnrmfdrifgqantpvkrwmldfaskrkeaelrsGIVRNDSFwdkiifhkvqaslgGKV 428
Cdd:cd17653 181 DPFAHVARTV--DALMSTPSIL---------------------------------STLSPQDF--------------PNL 211
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 429 RLMVTGAAPVSPTVLTflRAALGCQFYEGYGQTECTAGCSLT--IPGDWTagHVGAPMPCNHVKLVDVEEMNyfASKGE- 505
Cdd:cd17653 212 KTIFLGGEAVPPSLLD--RWSPGRRLYNAYGPTECTISSTMTelLPGQPV--TIGKPIPNSTCYILDADLQP--VPEGVv 285
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 506 GEVCIKGSNVFQGYLKDDEKTAEAL----DKDGWLH--TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENVYTR 579
Cdd:cd17653 286 GEICISGVQVARGYLGNPALTASKFvpdpFWPGSRMyrTGDYGRWTEDGGLEFLGREDNQVKV-RGFRINLEEIEEVVLQ 364
|
490 500
....*....|....*....|....*...
gi 1270536209 580 SEPVVQ---VFVHGESLQAFlvgiVVPD 604
Cdd:cd17653 365 SQPEVTqaaAIVVNGRLVAF----VTPE 388
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
91-615 |
1.12e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 123.89 E-value: 1.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 91 TIYDIFQRGRRvsnngpclghRKPNQP------YEWiSYKEVAERAEYVGSALLHRGFKPSpDQfVGIFAQNRPEWTIVE 164
Cdd:PRK08316 12 TIGDILRRSAR----------RYPDKTalvfgdRSW-TYAELDAAVNRVAAALLDLGLKKG-DR-VAALGHNSDAYALLW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 165 LGCYTYSMVAVPLYDTLGAEAITYIINKADLSVVFCDSPekaklLLSNVEKG--ETPVLRTIVlmnpfdnDLVERGKKCG 242
Cdd:PRK08316 79 LACARAGAVHVPVNFMLTGEELAYILDHSGARAFLVDPA-----LAPTAEAAlaLLPVDTLIL-------SLVLGGREAP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 243 VELVSLKDIEEEGkANREKPKPPKPDDLAVVCFTSGTTGNPKGAMLSHKNIVSNSAGFMkVTEDLmfpSTQDVLISFLPL 322
Cdd:PRK08316 147 GGWLDFADWAEAG-SVAEPDVELADDDLAQILYTSGTESLPKGAMLTHRALIAEYVSCI-VAGDM---SADDIPLHALPL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 323 AHMFERVVecvvlchgarigffqgdirLLMDDLKVLQPTIFPVVPRLlNRMFDRIfgqantpvkrwmldfaskrkEAElr 402
Cdd:PRK08316 222 YHCAQLDV-------------------FLGPYLYVGATNVILDAPDP-ELILRTI--------------------EAE-- 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 403 sgivRNDSF------WDKIIFHKV--QASLGGkVRLMVTGAAPVSPTVLTFLRAAL-GCQFYEGYGQTECTAGCSLTIPG 473
Cdd:PRK08316 260 ----RITSFfapptvWISLLRHPDfdTRDLSS-LRKGYYGASIMPVEVLKELRERLpGLRFYNCYGQTEIAPLATVLGPE 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 474 DwTAGHVG-APMPCNHV--KLVDvEEMNYFASKGEGEVCIKGSNVFQGYLKDDEKTAEALdKDGWLHTGDIGKWLPNGTL 550
Cdd:PRK08316 335 E-HLRRPGsAGRPVLNVetRVVD-DDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAF-RGGWFHSGDLGVMDEEGYI 411
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1270536209 551 KIIDRKKHIFKLAqGEYIAPEKIENVYTRSEPVVQVFVHG-------ESLQAflvgIVVP------DPDNVMNWAKKR 615
Cdd:PRK08316 412 TVVDRKKDMIKTG-GENVASREVEEALYTHPAVAEVAVIGlpdpkwiEAVTA----VVVPkagatvTEDELIAHCRAR 484
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
173-615 |
8.60e-29 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 120.24 E-value: 8.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 173 VAVPLYDTLGAEAITYIINKADLSVVFCDSPEKAKLllsnvekgetpvlrTIVLMNPFDNDLVergkkcgvelvslkdIE 252
Cdd:cd05922 48 VFVPLNPTLKESVLRYLVADAGGRIVLADAGAADRL--------------RDALPASPDPGTV---------------LD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 253 EEGKANREKPK---PPKPDDLAVVCFTSGTTGNPKGAMLSHKNIVSNS---AGFMKVTEDlmfpstqDVLISFLPLAHMF 326
Cdd:cd05922 99 ADGIRAARASApahEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANArsiAEYLGITAD-------DRALTVLPLSYDY 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 327 ERVVECVVLCHGARIgFFQGDIRL---LMDDLKVLQPTIFPVVPRLLNrMFDRI-FGQANTPVKRWMldfaskrkeaelr 402
Cdd:cd05922 172 GLSVLNTHLLRGATL-VLTNDGVLddaFWEDLREHGATGLAGVPSTYA-MLTRLgFDPAKLPSLRYL------------- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 403 sgivrndsfwdkiifhkvqASLGGKVRlmvtgaapvsPTVLTFLRAAL-GCQFYEGYGQTECTAGCSlTIPGDWTA---G 478
Cdd:cd05922 237 -------------------TQAGGRLP----------QETIARLRELLpGAQVYVMYGQTEATRRMT-YLPPERILekpG 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 479 HVGAPMPCNHVKLVDVEEMNYfaSKGE-GEVCIKGSNVFQGYLKDDEKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKK 557
Cdd:cd05922 287 SIGLAIPGGEFEILDDDGTPT--PPGEpGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRD 364
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1270536209 558 HIFKLAqGEYIAPEKIENVyTRSEPVVQVFV-------HGESLQAFLVGIVVPDPDNVMNWAKKR 615
Cdd:cd05922 365 RMIKLF-GNRISPTEIEAA-ARSIGLIIEAAavglpdpLGEKLALFVTAPDKIDPKDVLRSLAER 427
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
107-696 |
1.00e-28 |
|
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: 121.38 E-value: 1.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 107 PCLGHRKPNQPYEWISYKEVAERAEYVGSALLHRGFkpSPDQFVGIFAQNRPEWTIVELGCYTYSMVAVPL---YDTLGA 183
Cdd:cd05921 12 TWLAEREGNGGWRRVTYAEALRQVRAIAQGLLDLGL--SAERPLLILSGNSIEHALMALAAMYAGVPAAPVspaYSLMSQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 184 E--AITYIINKADLSVVFCDSPEKAKLLLSNVEKGETPVlrtIVLMNPFDNDLVergkkcgVELVSLKDIEEEGKANREK 261
Cdd:cd05921 90 DlaKLKHLFELLKPGLVFAQDAAPFARALAAIFPLGTPL---VVSRNAVAGRGA-------ISFAELAATPPTAAVDAAF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 262 PKPpKPDDLAVVCFTSGTTGNPKGAMLSHKNIVSNSAGFMKVtedLMFPSTQD-VLISFLPLAHMFervvecvvlchGAR 340
Cdd:cd05921 160 AAV-GPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQT---YPFFGEEPpVLVDWLPWNHTF-----------GGN 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 341 IGF-----------------FQGDIRLLMDDLKVLQPTIFPVVPrllnrmfdrifgqantpvKRWMLDFASKRKEAELRS 403
Cdd:cd05921 225 HNFnlvlynggtlyiddgkpMPGGFEETLRNLREISPTVYFNVP------------------AGWEMLVAALEKDEALRR 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 404 givrndSFWDKiifhkvqaslggkVRLMVTGAAPVSPTVLTFLRAaLGCQ-------FYEGYGQTEcTAGCSLTIPGDWT 476
Cdd:cd05921 287 ------RFFKR-------------LKLMFYAGAGLSQDVWDRLQA-LAVAtvgeripMMAGLGATE-TAPTATFTHWPTE 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 477 -AGHVGAPMPCNHVKLVdveemnyfASKGEGEVCIKGSNVFQGYLKDDEKTAEALDKDGWLHTGDIGKWL----PNGTLK 551
Cdd:cd05921 346 rSGLIGLPAPGTELKLV--------PSGGKYEVRVKGPNVTPGYWRQPELTAQAFDEEGFYCLGDAAKLAdpddPAKGLV 417
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 552 IIDRKKHIFKLAQGEYIA--PEKIENVYTRSePVVQ-VFVHGESlQAFLVGIVVPDPDNVMnwAKKRKFEGSYEELCKNK 628
Cdd:cd05921 418 FDGRVAEDFKLASGTWVSvgPLRARAVAACA-PLVHdAVVAGED-RAEVGALVFPDLLACR--RLVGLQEASDAEVLRHA 493
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1270536209 629 DFKNAVLEDLLKLGKEAGlKTFEQVKDIALHSEMFAIENGLLTPTLKAKRPELRKYFKDEIDELYANN 696
Cdd:cd05921 494 KVRAAFRDRLAALNGEAT-GSSSRIARALLLDEPPSIDKGEITDKGYINQRAVLERRAALVERLYADT 560
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
146-557 |
1.66e-28 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 121.22 E-value: 1.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 146 PDQFVGIFAQNRPEWTIVELGCYTYSMVAvPLYDTLGAEAITYIINKADLSVVFCDSPEKAKLLLSNVEK--GETPVLRT 223
Cdd:PRK07529 82 PGDVVAFLLPNLPETHFALWGGEAAGIAN-PINPLLEPEQIAELLRAAGAKVLVTLGPFPGTDIWQKVAEvlAALPELRT 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 224 IVLMNPfdNDLVERGKKCGVELVSLK------DIEEE---GKANR-EKPKPPKPDDLAVVCFTSGTTGNPKGAMLSHKNI 293
Cdd:PRK07529 161 VVEVDL--ARYLPGPKRLAVPLIRRKaharilDFDAElarQPGDRlFSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNE 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 294 VSN---SAGFMKVTEDlmfpstqDVLISFLPLAHMFERVVEC---------VVLC--HGARigffqgDIRLLMDDLKVL- 358
Cdd:PRK07529 239 VANawlGALLLGLGPG-------DTVFCGLPLFHVNALLVTGlaplargahVVLAtpQGYR------GPGVIANFWKIVe 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 359 --QPTIFPVVPRLLNRMFDRifgqantPVKRWmlDFASkrkeaeLRSGIvrndsfwdkiifhkvqaslggkvrlmvTGAA 436
Cdd:PRK07529 306 ryRINFLSGVPTVYAALLQV-------PVDGH--DISS------LRYAL---------------------------CGAA 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 437 PVSPTVLTFLRAALGCQFYEGYGQTECTAGCSLTIP-GDWTAGHVGAPMPCNHVKLVDVEEM-NYF--ASKGE-GEVCIK 511
Cdd:PRK07529 344 PLPVEVFRRFEAATGVRIVEGYGLTEATCVSSVNPPdGERRIGSVGLRLPYQRVRVVILDDAgRYLrdCAVDEvGVLCIA 423
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1270536209 512 GSNVFQGYLkDDEKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKK 557
Cdd:PRK07529 424 GPNVFSGYL-EAAHNKGLWLEDGWLNTGDLGRIDADGYFWLTGRAK 468
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
112-606 |
2.21e-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: 2.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 112 RKPNQPY-----EWISYKEVAERAEYVGSALLHRGFKPspDQFVGIFAQNRPEWTIVELGCYTYSMVAVPLYDTLGAEAI 186
Cdd:cd17655 9 KTPDHTAvvfedQTLTYRELNERANQLARTLREKGVGP--DTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEERI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 187 TYIINKADLSVVFCDSPEKAKLLLSnvekgetpvlRTIVLMNPfdndlvergkkcgvelvslKDIEEEGKANREKPKppK 266
Cdd:cd17655 87 QYILEDSGADILLTQSHLQPPIAFI----------GLIDLLDE-------------------DTIYHEESENLEPVS--K 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 267 PDDLAVVCFTSGTTGNPKGAMLSHKNIVSNSAGFMKVtedlMFPSTQDVLISFLPLAhmFERVVECV--VLCHGARIGFF 344
Cdd:cd17655 136 SDDLAYVIYTSGSTGKPKGVMIEHRGVVNLVEWANKV----IYQGEHLRVALFASIS--FDASVTEIfaSLLSGNTLYIV 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 345 Q----GDIRLLMDDLKVLQPTIFPVVPRLLNrmfdrifgqantpvkrwMLDfaskrkeaelrsgivrndsfwdkiifhKV 420
Cdd:cd17655 210 RketvLDGQALTQYIRQNRITIIDLTPAHLK-----------------LLD---------------------------AA 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 421 QASLGGKVRLMVTGAAPVSPTVLTFL--RAALGCQFYEGYGQTECTAGCS--LTIPGDWTAGHV--GAPMPCNHVKLVDv 494
Cdd:cd17655 246 DDSEGLSLKHLIVGGEALSTELAKKIieLFGTNPTITNAYGPTETTVDASiyQYEPETDQQVSVpiGKPLGNTRIYILD- 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 495 EEMNYFASKGEGEVCIKGSNVFQGYLKDDEKTAEALDKDGWL------HTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYI 568
Cdd:cd17655 325 QYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVpgermyRTGDLARWLPDGNIEFLGRIDHQVKI-RGYRI 403
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1270536209 569 APEKIENVYTRSEPVVQ--VFVH-GESLQAFLVGIVVPDPD 606
Cdd:cd17655 404 ELGEIEARLLQHPDIKEavVIARkDEQGQNYLCAYIVSEKE 444
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
251-598 |
3.20e-28 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 119.75 E-value: 3.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 251 IEEEGKANREKPKPPKpDDLAVVCFTSGTTGNPKGAMLSHKNIVSNSagFMKVTEDLMFPSTQDVLISFLPLAHMF-ERV 329
Cdd:PRK06710 190 VEKEVNTGVEVPCDPE-NDLALLQYTGGTTGFPKGVMLTHKNLVSNT--LMGVQWLYNCKEGEEVVLGVLPFFHVYgMTA 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 330 VECVVLCHGARIGFF-QGDIRLLMDDLKVLQPTIFPVVPRLLNRMFdrifgqaNTPVkrwmldfaskRKEAELRSgivrn 408
Cdd:PRK06710 267 VMNLSIMQGYKMVLIpKFDMKMVFEAIKKHKVTLFPGAPTIYIALL-------NSPL----------LKEYDISS----- 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 409 dsfwdkiifhkvqaslggkVRLMVTGAAPVSPTVLTFLRAALGCQFYEGYGQTECT-AGCSLTIPGDWTAGHVGAPMPCN 487
Cdd:PRK06710 325 -------------------IRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSpVTHSNFLWEKRVPGSIGVPWPDT 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 488 HVKLVDVEEMNYFASKGEGEVCIKGSNVFQGYLKDDEKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEY 567
Cdd:PRK06710 386 EAMIMSLETGEALPPGEIGEIVVKGPQIMKGYWNKPEETAAVL-QDGWLHTGDVGYMDEDGFFYVKDRKKDMI-VASGFN 463
|
330 340 350
....*....|....*....|....*....|....*...
gi 1270536209 568 IAPEKIENVYTRSEPVVQVFV-------HGESLQAFLV 598
Cdd:PRK06710 464 VYPREVEEVLYEHEKVQEVVTigvpdpyRGETVKAFVV 501
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
121-608 |
5.88e-28 |
|
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: 118.38 E-value: 5.88e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 121 ISYKEVAERAEYVGSALLHRGfkPSPDQFVGIFAQNRPEWTIVELGCYTYSMVAVPLYDTLGAEAITYIINKADL-SVVF 199
Cdd:cd05923 29 LTYSELRARIEAVAARLHARG--LRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEMtAAVI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 200 CDSPEKAklllsnvekgetpvlrtivlmnPFDNDLVERGKKCGVElVSLKDIEEEGKAnrEKPKPPKPDDLAVVCFTSGT 279
Cdd:cd05923 107 AVDAQVM----------------------DAIFQSGVRVLALSDL-VGLGEPESAGPL--IEDPPREPEQPAFVFYTSGT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 280 TGNPKGAMLSHKNIVSNSAgFMKVTEDLMFPStQDVLISFLPLAHMfervvecvvlchgarIGFFQgdirLLMDDLkVLQ 359
Cdd:cd05923 162 TGLPKGAVIPQRAAESRVL-FMSTQAGLRHGR-HNVVLGLMPLYHV---------------IGFFA----VLVAAL-ALD 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 360 PTIFPVvprllnRMFDRIfgqantpvkrwmldFASKRKEAELRSGIVRNDSFWDKIIFHKVQASLGGK-VRLMVTGAAPV 438
Cdd:cd05923 220 GTYVVV------EEFDPA--------------DALKLIEQERVTSLFATPTHLDALAAAAEFAGLKLSsLRHVTFAGATM 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 439 SPTVLTFLRAALGCQFYEGYGQTEctAGCSLTIPgDWTAGHVGAPMPCNHVKLVDV-EEMNYFASKG-EGEVCIK--GSN 514
Cdd:cd05923 280 PDAVLERVNQHLPGEKVNIYGTTE--AMNSLYMR-DARTGTEMRPGFFSEVRIVRIgGSPDEALANGeEGELIVAaaADA 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 515 VFQGYLKDDEKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENVYTRSEPVVQVFV------ 588
Cdd:cd05923 357 AFTGYLNQPEATAKKL-QDGWYRTGDVGYVDPSGDVRILGRVDDMI-ISGGENIHPSEIERVLSRHPGVTEVVVigvade 434
|
490 500
....*....|....*....|.
gi 1270536209 589 -HGESLQAFlvgiVVPDPDNV 608
Cdd:cd05923 435 rWGQSVTAC----VVPREGTL 451
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
120-615 |
7.54e-28 |
|
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: 117.79 E-value: 7.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 120 WISYKEVAERAEYVGSALLHRGFkpSPDQFVGIFAQNRPEWTIVELGCYTYSMVAVPLYDTLGAEAITYIINKADLSVVF 199
Cdd:cd12118 29 RYTWRQTYDRCRRLASALAALGI--SRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVLF 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 200 CDSPekaklllsnvekgetpvlrtivlmnpFD-NDLVERGKKcgvelvslkdieeegkanREKPKPPKPD-DLAVVCFTS 277
Cdd:cd12118 107 VDRE--------------------------FEyEDLLAEGDP------------------DFEWIPPADEwDPIALNYTS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 278 GTTGNPKGAMLSHKNIVSNSAGfmKVTEDLMFPSTqdVLISFLPLAHmfervveCVVLCHGARIGFFQG--------DIR 349
Cdd:cd12118 143 GTTGRPKGVVYHHRGAYLNALA--NILEWEMKQHP--VYLWTLPMFH-------CNGWCFPWTVAAVGGtnvclrkvDAK 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 350 LLMDDLKVLQPTIFPVVPRLLNRMfdrifgqANTPvkrwmldfaskrkeaelrsgivrndsfwdkiifHKVQASLGGKVR 429
Cdd:cd12118 212 AIYDLIEKHKVTHFCGAPTVLNML-------ANAP---------------------------------PSDARPLPHRVH 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 430 LMVTGAAPvsPTVLTFLRAALGCQFYEGYGQTEcTAG----CSL-----TIPGDWTA--------GHVGApmpcNHVKLV 492
Cdd:cd12118 252 VMTAGAPP--PAAVLAKMEELGFDVTHVYGLTE-TYGpatvCAWkpewdELPTEERArlkarqgvRYVGL----EEVDVL 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 493 DVEEMNYFASKGE--GEVCIKGSNVFQGYLKDDEKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAP 570
Cdd:cd12118 325 DPETMKPVPRDGKtiGEIVFRGNIVMKGYLKNPEATAEAF-RGGWFHSGDLAVIHPDGYIEIKDRSKDII-ISGGENISS 402
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1270536209 571 EKIENVYTRSEPVVQVFVH-------GESLQAF--LVGIVVPDPDNVMNWAKKR 615
Cdd:cd12118 403 VEVEGVLYKHPAVLEAAVVarpdekwGEVPCAFveLKEGAKVTEEEIIAFCREH 456
|
|
| PTZ00297 |
PTZ00297 |
pantothenate kinase; Provisional |
89-693 |
7.85e-28 |
|
pantothenate kinase; Provisional
Pssm-ID: 140318 [Multi-domain] Cd Length: 1452 Bit Score: 120.34 E-value: 7.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 89 VKTIYDIFQRGRRVSNNGPCLGHRKPNQPYEWISYKEVAERAEYVGSALLHRGFKPSpdQFVGIFAQNRPEWTIVELGCY 168
Cdd:PTZ00297 426 VRSLGEMWERSVTRHSTFRCLGQTSESGESEWLTYGTVDARARELGSGLLALGVRPG--DVIGVDCEASRNIVILEVACA 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 169 TYSMVAVPLYDTlgAEAITYIINKADLSVVFCDSPEKAKLLLSNVEKgetpvLRTIVLMNPF-DNDLVERGKKCGVELVS 247
Cdd:PTZ00297 504 LYGFTTLPLVGK--GSTMRTLIDEHKIKVVFADRNSVAAILTCRSRK-----LETVVYTHSFyDEDDHAVARDLNITLIP 576
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 248 LKDIEEEGkanREKPKPPKP--DDLAVVCFTSGTTGNPKGAMLS-----HKNIVSNSAGFMKVTedlMFPSTQ--DVLIS 318
Cdd:PTZ00297 577 YEFVEQKG---RLCPVPLKEhvTTDTVFTYVVDNTTSASGDGLAvvrvtHADVLRDISTLVMTG---VLPSSFkkHLMVH 650
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 319 FLPLAHMFERVVECVVLCHGARIGffQGDIRLLMDDLKVLQPTIFPVVPRL-------LNRMFDRifgqaNTPVKRWMLD 391
Cdd:PTZ00297 651 FTPFAMLFNRVFVLGLFAHGSAVA--TVDAAHLQRAFVKFQPTILVAAPSLfstsrlqLSRANER-----YSAVYSWLFE 723
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 392 faskrKEAELRSGIV---RNDSFWDKIIFHK-VQASLGGKVRLMVTGAAPVSpTVLTFLRAALGCqfyegygQTECTAGC 467
Cdd:PTZ00297 724 -----RAFQLRSRLInihRRDSSLLRFIFFRaTQELLGGCVEKIVLCVSEES-TSFSLLEHISVC-------YVPCLREV 790
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 468 SLtIPGDWTAGHVGAPMPCNHVKLVDVEEMNyfASKGEGEVCIkgsnvfqgyLKDDEKTaealdkdgwlHTGDI-GKWLP 546
Cdd:PTZ00297 791 FF-LPSEGVFCVDGTPAPSLQVDLEPFDEPS--DGAGIGQLVL---------AKKGEPR----------RTLPIaAQWKR 848
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 547 NGTLKIIDRKKHIFKLAQGEYIAPEKIENVYTRSEPVVQVFVHGESLQAfLVGIVVPDPDNV-MNWAKKRKFE--GSYEE 623
Cdd:PTZ00297 849 DRTLRLLGPPLGILLPVAYEYVIAAELERIFSQSRYVNDIFLYADPSRP-IIAIVSPNRDTVeFEWRQSHCMGegGGPAR 927
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1270536209 624 LCKNKDF----KNAVLEDLLKLGKEAGLKTFEQVKDIALHSEMFAIENGLLTPTLKAKRPELRKYFKDEIDELY 693
Cdd:PTZ00297 928 QLGWTELvayaSSLLTADFACIAKENGLHPSNVPEYVHLHPHAFKDHSTFLTPYGKIRRDAVHSYFSSVIERFY 1001
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
262-576 |
1.42e-27 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 117.64 E-value: 1.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 262 PKPP-KPDDLAVVCFTSGTTGNPKGAMLSHKNIVSNSAGFMKVTEDLM-FPSTQDVLISFLPLAHMFERVVECV-VLCHG 338
Cdd:PLN02574 191 PKPViKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVRFEASQYeYPGSDNVYLAALPMFHIYGLSLFVVgLLSLG 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 339 ARI----GFFQGDIRLLMDDLKVlqpTIFPVVPRLLNRMFDRIFGQANTPVKrwmldfaskrkeaelrsgivrndsfwdk 414
Cdd:PLN02574 271 STIvvmrRFDASDMVKVIDRFKV---THFPVVPPILMALTKKAKGVCGEVLK---------------------------- 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 415 iifhkvqaslggKVRLMVTGAAPVS-PTVLTFLRAALGCQFYEGYGQTECTA----GCSLTIPGDWTAghVGAPMPCNHV 489
Cdd:PLN02574 320 ------------SLKQVSCGAAPLSgKFIQDFVQTLPHVDFIQGYGMTESTAvgtrGFNTEKLSKYSS--VGLLAPNMQA 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 490 KLVDVEEMNYFASKGEGEVCIKGSNVFQGYLKDDEKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIA 569
Cdd:PLN02574 386 KVVDWSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKY-KGFQIA 464
|
....*..
gi 1270536209 570 PEKIENV 576
Cdd:PLN02574 465 PADLEAV 471
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
122-605 |
4.34e-27 |
|
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: 114.74 E-value: 4.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 122 SYKEVAERAEYVGSALLHRGFKPSpdQFVGIFAQNRPEWTIVELGCYTYSMVAVPLYDTLGAEAITYIINKADLSVVFCD 201
Cdd:cd05972 2 SFRELKRESAKAANVLAKLGLRKG--DRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 202 SpekaklllsnvekgetpvlrtivlmnpfdndlvergkkcgvelvslkdieeegkanrekpkppkpDDLAVVCFTSGTTG 281
Cdd:cd05972 80 A-----------------------------------------------------------------EDPALIYFTSGTTG 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 282 NPKGAMLSHKNIVSN---SAGFMKVTEDLMFPSTQD------VLISFL-PLAHMFervveCVVLCHGARIgffqgDIRLL 351
Cdd:cd05972 95 LPKGVLHTHSYPLGHiptAAYWLGLRPDDIHWNIADpgwakgAWSSFFgPWLLGA-----TVFVYEGPRF-----DAERI 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 352 MDDLKVLQPTIFPVVPrllnrmfdrifgqanTPVKRWMldfaskrkeAELRSGIVRndsfwdkiifhkvqaslgGKVRLM 431
Cdd:cd05972 165 LELLERYGVTSFCGPP---------------TAYRMLI---------KQDLSSYKF------------------SHLRLV 202
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 432 VTGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCSLTIPGDWTAGHVGAPMPCNHVKLVDvEEMNYFASKGEGEVCIK 511
Cdd:cd05972 203 VSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDVAIID-DDGRELPPGEEGDIAIK 281
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 512 GSNV--FQGYLKDDEKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENVytrsepVVQvfvH 589
Cdd:cd05972 282 LPPPglFLGYVGDPEKTEASI-RGDYYLTGDRAYRDEDGYFWFVGRADDIIK-SSGYRIGPFEVESA------LLE---H 350
|
490
....*....|....*.
gi 1270536209 590 GESLQAFLVGivVPDP 605
Cdd:cd05972 351 PAVAEAAVVG--SPDP 364
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
266-607 |
6.09e-27 |
|
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: 114.95 E-value: 6.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 266 KPDDLAVVCFTSGTTGNPKGAMLSHKNIVSNSAGF---MKVTED---LMFPS-TQDVLI--SFLPLAHMFervveCVvlC 336
Cdd:cd05918 104 SPSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHgraLGLTSEsrvLQFASyTFDVSIleIFTTLAAGG-----CL--C 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 337 HGARigffqgdiRLLMDDLkvlqptifpvvPRLLNRMfdrifgQANTpvkrwmldfaskrkeAELRSGIVRndsfwdkII 416
Cdd:cd05918 177 IPSE--------EDRLNDL-----------AGFINRL------RVTW---------------AFLTPSVAR-------LL 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 417 FHKVQASLggkvRLMVTGAAPVSPTVLTflRAALGCQFYEGYGQTECTAGCSLTIPG-DWTAGHVGAPMPCN-HVklVDV 494
Cdd:cd05918 210 DPEDVPSL----RTLVLGGEALTQSDVD--TWADRVRLINAYGPAECTIAATVSPVVpSTDPRNIGRPLGATcWV--VDP 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 495 EEMNYFASKGE-GEVCIKGSNVFQGYLKDDEKTAEALDKD-GWLH------------TGDIGKWLPNGTLKIIDRKKHIF 560
Cdd:cd05918 282 DNHDRLVPIGAvGELLIEGPILARGYLNDPEKTAAAFIEDpAWLKqegsgrgrrlyrTGDLVRYNPDGSLEYVGRKDTQV 361
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1270536209 561 KLaQGEYIAPEKIENVYTRSEP-----VVQVFVH-GESLQAFLVGIVVPDPDN 607
Cdd:cd05918 362 KI-RGQRVELGEIEHHLRQSLPgakevVVEVVKPkDGSSSPQLVAFVVLDGSS 413
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
119-604 |
6.53e-27 |
|
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: 114.70 E-value: 6.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 119 EWISYKEVAERAEYVGSALLHRGFKPspDQFVGIFAQNRPEWTIVELGCYTYSMVAVPLYDTLGAEAITYIINKADLSVV 198
Cdd:cd12116 11 RSLSYAELDERANRLAARLRARGVGP--GDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 199 FCDSpekaklllsnvekgetpvlrtivlmnpfdnDLVERGKKCGveLVSLKDIEEEGKANREKPKPPKPDDLAVVCFTSG 278
Cdd:cd12116 89 LTDD------------------------------ALPDRLPAGL--PVLLLALAAAAAAPAAPRTPVSPDDLAYVIYTSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 279 TTGNPKGAMLSHKNIVSNSAGFMkvtEDLMFPSTQDVL--------IS----FLPLahmfervvecvvlCHGARIGFFQG 346
Cdd:cd12116 137 STGRPKGVVVSHRNLVNFLHSMR---ERLGLGPGDRLLavttyafdISllelLLPL-------------LAGARVVIAPR 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 347 DI----RLLMDDLKVLQPTIFpvvprllnrmfdrifgQAnTPVKrWMLDFASKRKEAElrsgivrndsfwdkiifhkvqa 422
Cdd:cd12116 201 ETqrdpEALARLIEAHSITVM----------------QA-TPAT-WRMLLDAGWQGRA---------------------- 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 423 slggKVRLMVTGAApvSPTVLTFLRAALGCQFYEGYGQTECT--AGCSLTIPGDwTAGHVGAPMPCNHVKLVDvEEMNYF 500
Cdd:cd12116 241 ----GLTALCGGEA--LPPDLAARLLSRVGSLWNLYGPTETTiwSTAARVTAAA-GPIPIGRPLANTQVYVLD-AALRPV 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 501 ASKGEGEVCIKGSNVFQGYLKDDEKTAEALDKDGWLH-------TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKI 573
Cdd:cd12116 313 PPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAGpgsrlyrTGDLVRRRADGRLEYLGRADGQVKI-RGHRIELGEI 391
|
490 500 510
....*....|....*....|....*....|...
gi 1270536209 574 ENVYTRSEPVVQ--VFVHGESLQAFLVGIVVPD 604
Cdd:cd12116 392 EAALAAHPGVAQaaVVVREDGGDRRLVAYVVLK 424
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
107-544 |
1.53e-26 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 114.98 E-value: 1.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 107 PCLGHR-------KPNQPY--------EW--ISYKEVAERAEYVGSALLHRGFkpSPDQFVGIFAQNRPEWTIVELGCYT 169
Cdd:PRK08180 39 RRLTDRlvhwaqeAPDRVFlaergadgGWrrLTYAEALERVRAIAQALLDRGL--SAERPLMILSGNSIEHALLALAAMY 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 170 YSMVAVPL---YDTLGA--EAITYIINKADLSVVFCDSPEKAKLLLSNVEKGETPVLrtivlmnpfdndlVERGKKCGVE 244
Cdd:PRK08180 117 AGVPYAPVspaYSLVSQdfGKLRHVLELLTPGLVFADDGAAFARALAAVVPADVEVV-------------AVRGAVPGRA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 245 LVSLKDIEE--EGKANREKPKPPKPDDLAVVCFTSGTTGNPKGAMLSHKNIVSNSAgfMKvtEDLM--FPSTQDVLISFL 320
Cdd:PRK08180 184 ATPFAALLAtpPTAAVDAAHAAVGPDTIAKFLFTSGSTGLPKAVINTHRMLCANQQ--ML--AQTFpfLAEEPPVLVDWL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 321 PLAHMFERVVEC-VVLCHGARI---------GFFQGDIRllmdDLKVLQPTIFPVVPRLlnrmfdrifgqantpvkrWML 390
Cdd:PRK08180 260 PWNHTFGGNHNLgIVLYNGGTLyiddgkptpGGFDETLR----NLREISPTVYFNVPKG------------------WEM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 391 DFASKRKEAELRsgivrnDSFWdkiifhkvqaslgGKVRLMVTGAAPVSPTVLTFL----RAALGCQ--FYEGYGQTEcT 464
Cdd:PRK08180 318 LVPALERDAALR------RRFF-------------SRLKLLFYAGAALSQDVWDRLdrvaEATCGERirMMTGLGMTE-T 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 465 AGCSL--TIPGDwTAGHVGAPMPCNHVKLVDVEemnyfaskGEGEVCIKGSNVFQGYLKDDEKTAEALDKDGWLHTGDIG 542
Cdd:PRK08180 378 APSATftTGPLS-RAGNIGLPAPGCEVKLVPVG--------GKLEVRVKGPNVTPGYWRAPELTAEAFDEEGYYRSGDAV 448
|
..
gi 1270536209 543 KW 544
Cdd:PRK08180 449 RF 450
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
121-607 |
4.00e-26 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 113.33 E-value: 4.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 121 ISYKEVAERAEYVGSALLHRGfkpspdqfVG------IFAQNRPEWTIVELGCYTYSMVAVPLYDTLGAEAITYIINKAD 194
Cdd:PRK07786 43 TTWRELDDRVAALAGALSRRG--------VGfgdrvlILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 195 LSVVFCDSPekakllLSNVEKG---ETPVLRTIVLMNPFDNDLVergkkcgvelVSLKD-IEEEGKanrekPKPPK--PD 268
Cdd:PRK07786 115 AHVVVTEAA------LAPVATAvrdIVPLLSTVVVAGGSSDDSV----------LGYEDlLAEAGP-----AHAPVdiPN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 269 DL-AVVCFTSGTTGNPKGAMLSHKNIVSNSAGFMKVTEdlmFPSTQDVLISFLPLAHMfervvecvvlchgARIGFFQgd 347
Cdd:PRK07786 174 DSpALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNG---ADINSDVGFVGVPLFHI-------------AGIGSML-- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 348 IRLLMDDLKVLQPTifpvvprllnRMFDrifgqantPVKrwMLDFAskrkEAELRSGIVRNDSFWDKIIFHKVQASLGGK 427
Cdd:PRK07786 236 PGLLLGAPTVIYPL----------GAFD--------PGQ--LLDVL----EAEKVTGIFLVPAQWQAVCAEQQARPRDLA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 428 VRLMVTGAAPVSPTVLTFLRAAL-GCQFYEGYGQTECT-AGCSLTipGD---WTAGHVGAPMPCNHVKLVDvEEMNYFAS 502
Cdd:PRK07786 292 LRVLSWGAAPASDTLLRQMAATFpEAQILAAFGQTEMSpVTCMLL--GEdaiRKLGSVGKVIPTVAARVVD-ENMNDVPV 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 503 KGEGEVCIKGSNVFQGYLKDDEKTAEALDkDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENVYTRSEP 582
Cdd:PRK07786 369 GEVGEIVYRAPTLMSGYWNNPEATAEAFA-GGWFHSGDLVRQDEEGYVWVVDRKKDMI-ISGGENIYCAEVENVLASHPD 446
|
490 500
....*....|....*....|....*...
gi 1270536209 583 VVQVFVHGESLQAF---LVGIVVPDPDN 607
Cdd:PRK07786 447 IVEVAVIGRADEKWgevPVAVAAVRNDD 474
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
119-606 |
7.00e-26 |
|
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: 114.18 E-value: 7.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 119 EWISYKEVAERAEYVGSALLHRGFKPspDQFVGIFAQNRPEWTIVELG------CYtysmvaVPLYDTLGAEAITYIINK 192
Cdd:COG1020 500 QSLTYAELNARANRLAHHLRALGVGP--GDLVGVCLERSLEMVVALLAvlkagaAY------VPLDPAYPAERLAYMLED 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 193 ADLSVVFCDSpekaklllsnvekgetpvlrtivlmnpfdnDLVERGKKCGVELVSLkDIEEEGKANREKPKPP-KPDDLA 271
Cdd:COG1020 572 AGARLVLTQS------------------------------ALAARLPELGVPVLAL-DALALAAEPATNPPVPvTPDDLA 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 272 VVCFTSGTTGNPKGAMLSHKNIVSNSAGFmkvTEDLMFpSTQDVLISFLPLAH------MFervvecVVLCHGARIGFFQ 345
Cdd:COG1020 621 YVIYTSGSTGRPKGVMVEHRALVNLLAWM---QRRYGL-GPGDRVLQFASLSFdasvweIF------GALLSGATLVLAP 690
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 346 GDIRLLMDDLKVL----QPTIFPVVPRLLNRMFDRIFGQantpvkrwmldfaskrkeaeLRSgivrndsfwdkiifhkvq 421
Cdd:COG1020 691 PEARRDPAALAELlarhRVTVLNLTPSLLRALLDAAPEA--------------------LPS------------------ 732
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 422 aslggkVRLMVTGAAPVSPTVLTFLRAAL-GCQFYEGYGQTECTAGCSLTI--PGDWTAGHV--GAPMPCNHVKLVDvee 496
Cdd:COG1020 733 ------LRLVLVGGEALPPELVRRWRARLpGARLVNLYGPTETTVDSTYYEvtPPDADGGSVpiGRPIANTRVYVLD--- 803
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 497 mnyfaSKGE-------GEVCIKGSNVFQGYLKDDEKTAEA-----LDKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKL 562
Cdd:COG1020 804 -----AHLQpvpvgvpGELYIGGAGLARGYLNRPELTAERfvadpFGFPGarLYRTGDLARWLPDGNLEFLGRADDQVKI 878
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1270536209 563 aQGEYIAPEKIENVYTRSEPVVQ--VFVHGESLQA-FLVGIVVPDPD 606
Cdd:COG1020 879 -RGFRIELGEIEAALLQHPGVREavVVAREDAPGDkRLVAYVVPEAG 924
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
121-606 |
7.74e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 112.00 E-value: 7.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 121 ISYKEVAERAEYVGSALLHRGFKPSPDqfVGIFAQNRPEWTIVELGCYTYSMVAVPLYdTLGAEA-ITYIINKADLSVVF 199
Cdd:PRK06188 38 LTYGQLADRISRYIQAFEALGLGTGDA--VALLSLNRPEVLMAIGAAQLAGLRRTALH-PLGSLDdHAYVLEDAGISTLI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 200 CDS---PEKAKLLLSNVekgetPVLRTIVLMNPFDNdlvergkkcGVELVSLKDIEEegkanrekPKPPK----PDDLAV 272
Cdd:PRK06188 115 VDPapfVERALALLARV-----PSLKHVLTLGPVPD---------GVDLLAAAAKFG--------PAPLVaaalPPDIAG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 273 VCFTSGTTGNPKGAMLSHKNIVSNSAGFMKvteDLMFPSTqdvlISFL---PLAH----MFERVVE---CVVLCHGARIG 342
Cdd:PRK06188 173 LAYTGGTTGKPKGVMGTHRSIATMAQIQLA---EWEWPAD----PRFLmctPLSHaggaFFLPTLLrggTVIVLAKFDPA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 343 FFqgdIRLLMDDlkvlQPTIFPVVPRLLNRMFDrifgqANTPVKRwmlDFASkrkeaelrsgivrndsfwdkiifhkvqa 422
Cdd:PRK06188 246 EV---LRAIEEQ----RITATFLVPTMIYALLD-----HPDLRTR---DLSS---------------------------- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 423 slggkVRLMVTGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCSLTIPGDWTAGHV------GAPMPCNHVKLVDvEE 496
Cdd:PRK06188 283 -----LETVYYGASPMSPVRLAEAIERFGPIFAQYYGQTEAPMVITYLRKRDHDPDDPkrltscGRPTPGLRVALLD-ED 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 497 MNYFASkGE-GEVCIKGSNVFQGYLKDDEKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIEN 575
Cdd:PRK06188 357 GREVAQ-GEvGEICVRGPLVMDGYWNRPEETAEAF-RDGWLHTGDVAREDEDGFYYIVDRKKDMI-VTGGFNVFPREVED 433
|
490 500 510
....*....|....*....|....*....|....*...
gi 1270536209 576 VYTRSEPVVQVFV-------HGESLQAflvgIVVPDPD 606
Cdd:PRK06188 434 VLAEHPAVAQVAVigvpdekWGEAVTA----VVVLRPG 467
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
90-605 |
1.16e-25 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 111.68 E-value: 1.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 90 KTIYDIFQRGRRVSNNGPCL-----GHRKPNQpyewISYKEVAERAEYVGSALLHRGFKPspDQFVGIFAQNRPEWTIVE 164
Cdd:PRK13295 24 RTINDDLDACVASCPDKTAVtavrlGTGAPRR----FTYRELAALVDRVAVGLARLGVGR--GDVVSCQLPNWWEFTVLY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 165 LGCYTYSMVAVPLYDTLGAEAITYIINKADLSVVFC-------DSPEKAKLLlsnveKGETPVLRTIVLMNPFDNDLVER 237
Cdd:PRK13295 98 LACSRIGAVLNPLMPIFRERELSFMLKHAESKVLVVpktfrgfDHAAMARRL-----RPELPALRHVVVVGGDGADSFEA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 238 gkkcgveLVSLKDIEEEGKANREKPKP-PKPDDLAVVCFTSGTTGNPKGAMLSHKNIVSNS---AGFMKVTEDlmfpstq 313
Cdd:PRK13295 173 -------LLITPAWEQEPDAPAILARLrPGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIvpyAERLGLGAD------- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 314 DVLISFLPLAHMfervvecvvlchgarIGFFQGDIRLLMDDLK-VLQPTIFPVvprllnRMFDRI------FGQANTPvk 386
Cdd:PRK13295 239 DVILMASPMAHQ---------------TGFMYGLMMPVMLGATaVLQDIWDPA------RAAELIrtegvtFTMASTP-- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 387 rWMLDFASKRKEAElrsgivrndsfwdkiifhKVQASLggkvRLMVTGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAg 466
Cdd:PRK13295 296 -FLTDLTRAVKESG------------------RPVSSL----RTFLCAGAPIPGALVERARAALGAKIVSAWGMTENGA- 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 467 CSLTIPGD---WTAGHVGAPMPCNHVKLVDVEEMNYFASKgEGEVCIKGSNVFQGYLKDDEKTAEalDKDGWLHTGDIGK 543
Cdd:PRK13295 352 VTLTKLDDpdeRASTTDGCPLPGVEVRVVDADGAPLPAGQ-IGRLQVRGCSNFGGYLKRPQLNGT--DADGWFDTGDLAR 428
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1270536209 544 WLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENVYTRSEPVVQVFVHG---ESLQAFLVGIVVPDP 605
Cdd:PRK13295 429 IDADGYIRISGRSKDVI-IRGGENIPVVEIEALLYRHPAIAQVAIVAypdERLGERACAFVVPRP 492
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
121-615 |
2.11e-25 |
|
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.
Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 109.49 E-value: 2.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 121 ISYKEVAERAEYVGSALLHRGFKPSpdQFVGIFAQNRPEWTIVELGCYTYSMVAVPLYDTLGAEAITYIINkadlsvvfc 200
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKG--DRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILN--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 201 DSPEKAKLLLSNVekgetpvlrtivlmnpfdndlvergkkcgvelvslkdieeegkanrekpkppkpDDLAVVCFTSGTT 280
Cdd:cd05935 71 DSGAKVAVVGSEL------------------------------------------------------DDLALIPYTSGTT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 281 GNPKGAMLSHKNIVSNSAGFMKVTEdlmfPSTQDVLISFLPLAHM--FERVVECVVLCHGARIGFFQGDIRLLMDDLKVL 358
Cdd:cd05935 97 GLPKGCMHTHFSAAANALQSAVWTG----LTPSDVILACLPLFHVtgFVGSLNTAVYVGGTYVLMARWDRETALELIEKY 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 359 QPTIFPVVPRLLNRMFdrifgqaNTPvkrwmldfaskrkeaelrsgivrndsfwdkiifhKVQASLGGKVRLMVTGAAPV 438
Cdd:cd05935 173 KVTFWTNIPTMLVDLL-------ATP----------------------------------EFKTRDLSSLKVLTGGGAPM 211
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 439 SPTVLTFLRAALGCQFYEGYGQTECTAGCSLTIPGDWTAGHVGAPMPCNHVKLVDVEEMNYFASKGEGEVCIKGSNVFQG 518
Cdd:cd05935 212 PPAVAEKLLKLTGLRFVEGYGLTETMSQTHTNPPLRPKLQCLGIP*FGVDARVIDIETGRELPPNEVGEIVVRGPQIFKG 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 519 YLKDDEKTAEALDKDG---WLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENVYTRSEPVVQVFV------- 588
Cdd:cd05935 292 YWNRPEETEESFIEIKgrrFFRTGDLGYMDEEGYFFFVDRVKRMINVS-GFKVWPAEVEAKLYKHPAI*EVCVisvpder 370
|
490 500 510
....*....|....*....|....*....|...
gi 1270536209 589 HGESLQAFLVgiVVP------DPDNVMNWAKKR 615
Cdd:cd05935 371 VGEEVKAFIV--LRPeyrgkvTEEDIIEWAREQ 401
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
262-606 |
2.64e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 109.69 E-value: 2.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 262 PKPPkPDDLAVVCFTSGTTGNPKGAMLSHKNIVSNSAGFMKV---TEDlmfpstqDVLISFLPLAHMfervvecvvlcHG 338
Cdd:PRK07787 123 PEPD-PDAPALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAwqwTAD-------DVLVHGLPLFHV-----------HG 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 339 ARIGffqgdirllmddlkVLQPTifpvvprllnrmfdRIFGQANTPVKrwmldFASKRKEAELRSG--------IVrnds 410
Cdd:PRK07787 184 LVLG--------------VLGPL--------------RIGNRFVHTGR-----PTPEAYAQALSEGgtlyfgvpTV---- 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 411 fWDKIIFHKVQASLGGKVRLMVTGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCSLTIPGDWTAGHVGAPMPCNHVK 490
Cdd:PRK07787 227 -WSRIAADPEAARALRGARLLVSGSAALPVPVFDRLAALTGHRPVERYGMTETLITLSTRADGERRPGWVGLPLAGVETR 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 491 LVDvEEMNYFASKGE--GEVCIKGSNVFQGYLKDDEKTAEALDKDGWLHTGDIGKWLPNGTLKIIDR------KKHIFKL 562
Cdd:PRK07787 306 LVD-EDGGPVPHDGEtvGELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDPDGMHRIVGRestdliKSGGYRI 384
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1270536209 563 AQGEyiapekIENVYTRSEPVVQVFVHGEslqaflvgivvPDPD 606
Cdd:PRK07787 385 GAGE------IETALLGHPGVREAAVVGV-----------PDDD 411
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
119-605 |
3.89e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 109.51 E-value: 3.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 119 EWiSYKEVAERAEYVGSALLHRGFKPSpdQFVGIFAQNRPEWTIVELGCYTYSMVAVPLYDTLGAEAITYIINKADLSVV 198
Cdd:PRK09088 22 RW-TYAELDALVGRLAAVLRRRGCVDG--ERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 199 FCDSPEKAklllsnvekgetpvLRTIVlmnpfdndlvergkkcgvelVSLKDIEEEGKANREKPKPP-KPDDLAVVCFTS 277
Cdd:PRK09088 99 LGDDAVAA--------------GRTDV--------------------EDLAAFIASADALEPADTPSiPPERVSLILFTS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 278 GTTGNPKGAMLSHKNIVSNSAGFMKVTEdlmfpstQDVLISFLPLAHMFERV--VECV--VLCHGARIGFFQGdirllmd 353
Cdd:PRK09088 145 GTSGQPKGVMLSERNLQQTAHNFGVLGR-------VDAHSSFLCDAPMFHIIglITSVrpVLAVGGSILVSNG------- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 354 dlkvLQPTifpvvpRLLNRMFDRIFGQANTPVKRWMLDfaskrkeaelrsgIVRNDSFWDkiifhkvqASLGGKVRLMVT 433
Cdd:PRK09088 211 ----FEPK------RTLGRLGDPALGITHYFCVPQMAQ-------------AFRAQPGFD--------AAALRHLTALFT 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 434 GAAP-VSPTVLTFLraALGCQFYEGYGQTEctAGCSLTIPGDWT-----AGHVGAPMPCNHVKLVDVEEMNYFAskGE-G 506
Cdd:PRK09088 260 GGAPhAAEDILGWL--DDGIPMVDGFGMSE--AGTVFGMSVDCDvirakAGAAGIPTPTVQTRVVDDQGNDCPA--GVpG 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 507 EVCIKGSNVFQGYLKDDEKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENVYTRsepvvqv 586
Cdd:PRK09088 334 ELLLRGPNLSPGYWRRPQATARAFTGDGWFRTGDIARRDADGFFWVVDRKKDMF-ISGGENVYPAEIEAVLAD------- 405
|
490
....*....|....*....
gi 1270536209 587 fvHGESLQAFLVGivVPDP 605
Cdd:PRK09088 406 --HPGIRECAVVG--MADA 420
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
265-591 |
6.04e-25 |
|
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: 107.82 E-value: 6.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 265 PKPDDLAVVCFTSGTTGNPKGAMLSHKNIVSNSAGFMkvtEDLMFpSTQDVLISFLPLAH------MFERVVE-CVVLCH 337
Cdd:cd05912 74 VKLDDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSA---LNLGL-TEDDNWLCALPLFHisglsiLMRSVIYgMTVYLV 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 338 GArigFFQGDIRLLMDDLKVlqpTIFPVVPRLLNRMFDrIFGQANTPVKRWMLdfaskrkeaelrsgivrndsfwdkiif 417
Cdd:cd05912 150 DK---FDAEQVLHLINSGKV---TIISVVPTMLQRLLE-ILGEGYPNNLRCIL--------------------------- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 418 hkvqasLGGkvrlmvtgaAPVSPTVLTFLRAaLGCQFYEGYGQTEcTAGCSLTIPGDWTA---GHVGAPMPCNHVKLVDV 494
Cdd:cd05912 196 ------LGG---------GPAPKPLLEQCKE-KGIPVYQSYGMTE-TCSQIVTLSPEDALnkiGSAGKPLFPVELKIEDD 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 495 EEmnyfASKGEGEVCIKGSNVFQGYLKDDEKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIE 574
Cdd:cd05912 259 GQ----PPYEVGEILLKGPNVTKGYLNRPDATEESF-ENGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIE 332
|
330
....*....|....*..
gi 1270536209 575 NVYTRSEPVVQVFVHGE 591
Cdd:cd05912 333 EVLLSHPAIKEAGVVGI 349
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
119-585 |
1.06e-24 |
|
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: 108.87 E-value: 1.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 119 EWISYKEVAERAEYVGSALLHRGfkpSPDQFVGIFAQNRPEWTIVELGCYTYSMVAVPLYDTLGAEA---ITYIINKADL 195
Cdd:cd05931 23 ETLTYAELDRRARAIAARLQAVG---KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPPTPGRHaerLAAILADAGP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 196 SVVFCDSPEKAKL--LLSNVEKGETPVLRTIvlmnpfdnDLVErgkkcgvelvslkdieeEGKANREKPKPPKPDDLAVV 273
Cdd:cd05931 100 RVVLTTAAALAAVraFAASRPAAGTPRLLVV--------DLLP-----------------DTSAADWPPPSPDPDDIAYL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 274 CFTSGTTGNPKGAMLSHKNIVSNSAGFMKvtedLMFPSTQDVLISFLPLAH-MfervvecvvlchgariGFFQGdirllm 352
Cdd:cd05931 155 QYTSGSTGTPKGVVVTHRNLLANVRQIRR----AYGLDPGDVVVSWLPLYHdM----------------GLIGG------ 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 353 ddlkVLQPTI--FPVV----------PRLLNRMFDRiFGQANTPVKRWMLDFASKRKEAELRSGIvrnDsfwdkiifhkv 420
Cdd:cd05931 209 ----LLTPLYsgGPSVlmspaaflrrPLRWLRLISR-YRATISAAPNFAYDLCVRRVRDEDLEGL---D----------- 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 421 qasLgGKVRLMVTGAAPVSPTVLT-FLRAALGCQF-----YEGYGQTECTAGCSLTIPG----------DWTAGHV---- 480
Cdd:cd05931 270 ---L-SSWRVALNGAEPVRPATLRrFAEAFAPFGFrpeafRPSYGLAEATLFVSGGPPGtgpvvlrvdrDALAGRAvava 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 481 ------------GAPMPCNHVKLVDVEEMNYFASKGEGEVCIKGSNVFQGYLKDDEKTAE------ALDKDGWLHTGDIG 542
Cdd:cd05931 346 addpaarelvscGRPLPDQEVRIVDPETGRELPDGEVGEIWVRGPSVASGYWGRPEATAEtfgalaATDEGGWLRTGDLG 425
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1270536209 543 kWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENVYTRSEPVVQ 585
Cdd:cd05931 426 -FLHDGELYITGRLKDLIIVR-GRNHYPQDIEATAEEAHPALR 466
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
121-598 |
1.30e-24 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 107.74 E-value: 1.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 121 ISYKEVAERAEYVGSALLHRGFKPspDQFVGIFAQNRPEWTIVELGCYTYSMVAVPLYDTLGAEAITYIINKADLSVVFC 200
Cdd:PRK03640 28 VTFMELHEAVVSVAGKLAALGVKK--GDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKCLIT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 201 DSPEKAKLllsnveKGETPVlrtivlmnpfdndlvergkkcgvelvslkDIEEEGKANREKPKPPKP---DDLAVVCFTS 277
Cdd:PRK03640 106 DDDFEAKL------IPGISV-----------------------------KFAELMNGPKEEAEIQEEfdlDEVATIMYTS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 278 GTTGNPKGAMLSHKN----IVSnSAGFMKVTEDlmfpstqDVLISFLPLAH------MFERVVecvvlcHGARI----GF 343
Cdd:PRK03640 151 GTTGKPKGVIQTYGNhwwsAVG-SALNLGLTED-------DCWLAAVPIFHisglsiLMRSVI------YGMRVvlveKF 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 344 FQGDI-RLLMDDlKVlqpTIFPVVPRLLNRMFDRIfGQANTPvkrwmldfaskrkeaelrsgivrnDSFwdkiifhkvqa 422
Cdd:PRK03640 217 DAEKInKLLQTG-GV---TIISVVSTMLQRLLERL-GEGTYP------------------------SSF----------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 423 slggkvRLMVTGAAPVSPTVLTFLRAAlGCQFYEGYGQTEcTAGCSLTIPGDWTA---GHVGAPM-PCNhVKLVDveEMN 498
Cdd:PRK03640 257 ------RCMLLGGGPAPKPLLEQCKEK-GIPVYQSYGMTE-TASQIVTLSPEDALtklGSAGKPLfPCE-LKIEK--DGV 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 499 YFASKGEGEVCIKGSNVFQGYLKDDEKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENVYT 578
Cdd:PRK03640 326 VVPPFEEGEIVVKGPNVTKGYLNREDATRETF-QDGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIEEVLL 403
|
490 500
....*....|....*....|....*..
gi 1270536209 579 RSEPVVQVFVHGESLQ-------AFLV 598
Cdd:PRK03640 404 SHPGVAEAGVVGVPDDkwgqvpvAFVV 430
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
121-605 |
2.36e-24 |
|
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341267 [Multi-domain] Cd Length: 449 Bit Score: 106.56 E-value: 2.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 121 ISYKEVAERAEYVGSALLHRGfkPSPDQFVGIFAQNRPEWTIVELGCYTYSMVAVPLYDTLGAEAITYIINKADLSVVFC 200
Cdd:cd05945 17 LTYRELKERADALAAALASLG--LDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIREILDAAKPALLIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 201 DspekaklllsnvekgetpvlrtivlmnpfdndlvergkkcgvelvslkdieeegkanrekpkppkPDDLAVVCFTSGTT 280
Cdd:cd05945 95 D-----------------------------------------------------------------GDDNAYIIFTSGST 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 281 GNPKGAMLSHKNIVSNSA---GFMKVTEDLMFPSTQDvlISF-LPLAHMFervvecVVLCHGArigffqgdirllmddlk 356
Cdd:cd05945 110 GRPKGVQISHDNLVSFTNwmlSDFPLGPGDVFLNQAP--FSFdLSVMDLY------PALASGA----------------- 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 357 vlqpTIFPVvPRLLNRMFDRIF-GQANTPVKRWmldfaskrkeaelrsgiVRNDSFWDKIIFHK--VQASLGGKVRLMVT 433
Cdd:cd05945 165 ----TLVPV-PRDATADPKQLFrFLAEHGITVW-----------------VSTPSFAAMCLLSPtfTPESLPSLRHFLFC 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 434 GAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCSLT-IPGDWTAGH----VGAPMPCNHVKLVDvEEMNYFASKGEGEV 508
Cdd:cd05945 223 GEVLPHKTARALQQRFPDARIYNTYGPTEATVAVTYIeVTPEVLDGYdrlpIGYAKPGAKLVILD-EDGRPVPPGEKGEL 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 509 CIKGSNVFQGYLKDDEKTAEALDKD---GWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENVYTRSEPVVQ 585
Cdd:cd05945 302 VISGPSVSKGYLNNPEKTAAAFFPDegqRAYRTGDLVRLEADGLLFYRGRLDFQVKL-NGYRIELEEIEAALRQVPGVKE 380
|
490 500
....*....|....*....|....
gi 1270536209 586 VFV----HGESLQAfLVGIVVPDP 605
Cdd:cd05945 381 AVVvpkyKGEKVTE-LIAFVVPKP 403
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
269-618 |
3.29e-24 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 103.95 E-value: 3.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 269 DLAVVCFTSGTTGNPKGAMLSHKNIVSNSAGfmkvTEDLMFPSTQDVLISFLPLAHM--FERVVECVVLchGARIGFFQG 346
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAG----LHSRLGFGGGDSWLLSLPLYHVggLAILVRSLLA--GAELVLLER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 347 DiRLLMDDLKVLQPTIFPVVPRLLNRMFDRifGQANTPVKRwmldfaskrkeaelrsgivrndsfwdkiifhkvqaslgg 426
Cdd:cd17630 75 N-QALAEDLAPPGVTHVSLVPTQLQRLLDS--GQGPAALKS--------------------------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 427 kVRLMVTGAAPVsPTVLTFLRAALGCQFYEGYGQTECTAGCSLTIPGDWTAGHVGAPMPCNHVKLVDveemnyfaskgEG 506
Cdd:cd17630 113 -LRAVLLGGAPI-PPELLERAADRGIPLYTTYGMTETASQVATKRPDGFGRGGVGVLLPGRELRIVE-----------DG 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 507 EVCIKGSNVFQGYLKDDEKtaEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENVYTRSEPVVQV 586
Cdd:cd17630 180 EIWVGGASLAMGYLRGQLV--PEFNEDGWFTTKDLGELHADGRLTVLGRADNMI-ISGGENIQPEEIEAALAAHPAVRDA 256
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1270536209 587 FV-------HGESLQAFLVGIVVPDPDNVMNWAKKR--KFE 618
Cdd:cd17630 257 FVvgvpdeeLGQRPVAVIVGRGPADPAELRAWLKDKlaRFK 297
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
119-598 |
8.08e-24 |
|
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: 104.82 E-value: 8.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 119 EWISYKEVAERAEYVGSALLHRGFKPSpdQFVGIFAQNRPEWTIVELGCYTYSMVAVPLYDTLGAEAITYIINKADLSVV 198
Cdd:cd05971 5 EKVTFKELKTASNRFANVLKEIGLEKG--DRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 199 FCDSPekaklllsnvekgetpvlrtivlmnpfdndlvergkkcgvelvslkdieeegkanrekpkppkpDDLAVVCFTSG 278
Cdd:cd05971 83 VTDGS----------------------------------------------------------------DDPALIIYTSG 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 279 TTGNPKGAMLSHKNIVSNSAGFMKVTEdlMFPSTQDVLisFLPlahmfervvecvvlchgARIGFFQGdirlLMDdlkVL 358
Cdd:cd05971 99 TTGPPKGALHAHRVLLGHLPGVQFPFN--LFPRDGDLY--WTP-----------------ADWAWIGG----LLD---VL 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 359 QPTIFPVVPRLLNRM--FDRifGQANTPVKRWMLDFASKRKEAeLRsgIVRndsfwdkiiFHKVQASLGG-KVRLMVTGA 435
Cdd:cd05971 151 LPSLYFGVPVLAHRMtkFDP--KAALDLMSRYGVTTAFLPPTA-LK--MMR---------QQGEQLKHAQvKLRAIATGG 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 436 APVSPTVLTFLRAALGCQFYEGYGQTEC---TAGCSLTIPGDwtAGHVGAPMPCNHVKLVDvEEMNYFASKGEGEVCIK- 511
Cdd:cd05971 217 ESLGEELLGWAREQFGVEVNEFYGQTECnlvIGNCSALFPIK--PGSMGKPIPGHRVAIVD-DNGTPLPPGEVGEIAVEl 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 512 -GSNVFQGYLKDDEKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENVYTRSEPVVQVFV-- 588
Cdd:cd05971 294 pDPVAFLGYWNNPSATEKKM-AGDWLLTGDLGRKDSDGYFWYVGRDDDVITSS-GYRIGPAEIEECLLKHPAVLMAAVvg 371
|
490
....*....|....*
gi 1270536209 589 -----HGESLQAFLV 598
Cdd:cd05971 372 ipdpiRGEIVKAFVV 386
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
121-615 |
8.55e-24 |
|
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: 105.36 E-value: 8.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 121 ISYKEVAERAEYVGSALLHRGFKPspDQFVGIFAQNRPEWTIVELG------CYtysmvaVPLYDTLGAEAITYIINKAD 194
Cdd:cd12117 23 LTYAELNERANRLARRLRAAGVGP--GDVVGVLAERSPELVVALLAvlkagaAY------VPLDPELPAERLAFMLADAG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 195 lsvvfcdspekAKLLLSnvekgetpvlrtivlmnpfDNDLVERGKKCGVELVSLKDIEEEGKANrekPKPP-KPDDLAVV 273
Cdd:cd12117 95 -----------AKVLLT-------------------DRSLAGRAGGLEVAVVIDEALDAGPAGN---PAVPvSPDDLAYV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 274 CFTSGTTGNPKGAMLSHKNIVS--NSAGFMKVTEdlmfpstQDVLISFLPL---AHMFERVvecVVLCHGARIgffqgdi 348
Cdd:cd12117 142 MYTSGSTGRPKGVAVTHRGVVRlvKNTNYVTLGP-------DDRVLQTSPLafdASTFEIW---GALLNGARL------- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 349 rllmddlkVLQPTIFPVVPRLLNRMFDRifGQANTpvkRWMldfaskrkEAELRSGIVRNDSfwdkiifhkvqASLGGkV 428
Cdd:cd12117 205 --------VLAPKGTLLDPDALGALIAE--EGVTV---LWL--------TAALFNQLADEDP-----------ECFAG-L 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 429 RLMVTGAAPVSPT-VLTFLRAALGCQFYEGYGQTECT--AGCSLTIPGDWTAGHV--GAPMPCNHVKLVDveEMNYFASK 503
Cdd:cd12117 252 RELLTGGEVVSPPhVRRVLAACPGLRLVNGYGPTENTtfTTSHVVTELDEVAGSIpiGRPIANTRVYVLD--EDGRPVPP 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 504 GE-GEVCIKGSNVFQGYLKDDEKTAEALDKDGWL------HTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENV 576
Cdd:cd12117 330 GVpGELYVGGDGLALGYLNRPALTAERFVADPFGpgerlyRTGDLARWLPDGRLEFLGRIDDQVKI-RGFRIELGEIEAA 408
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1270536209 577 YTRSEPVVQVFV------HGE-SLQAFLVGIVVPDPDNVMNWAKKR 615
Cdd:cd12117 409 LRAHPGVREAVVvvredaGGDkRLVAYVVAEGALDAAELRAFLRER 454
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
111-613 |
9.88e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 105.81 E-value: 9.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 111 HRKPNQPYEW-----ISYKEVAERAEYVgSALLHRGFKPSPDQFVGIFAQNRPEWTIVELGCYTYSMVAVPLYDTLGAEA 185
Cdd:PRK08314 21 RRYPDKTAIVfygraISYRELLEEAERL-AGYLQQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 186 ITYIINKADLSVVFCDSPekaklLLSNVEK--GETPVLRTIV-----LMNPFDNDLVERGKKCGVELVSLKDIE----EE 254
Cdd:PRK08314 100 LAHYVTDSGARVAIVGSE-----LAPKVAPavGNLRLRHVIVaqysdYLPAEPEIAVPAWLRAEPPLQALAPGGvvawKE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 255 GKANREKPKP--PKPDDLAVVCFTSGTTGNPKGAMLSHKNIVSNSAGFMkvtedLMFPSTQD-VLISFLPLAHmferVVE 331
Cdd:PRK08314 175 ALAAGLAPPPhtAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSV-----LWSNSTPEsVVLAVLPLFH----VTG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 332 CVVLCHGArigFFQGDIRLLMddlkvlqptifP-----VVPRLLNRMfdRIFGQANTPVKrwMLDF-ASKR-KEAELRSg 404
Cdd:PRK08314 246 MVHSMNAP---IYAGATVVLM-----------PrwdreAAARLIERY--RVTHWTNIPTM--VVDFlASPGlAERDLSS- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 405 ivrndsfwdkiifhkvQASLGGkvrlmvtGAAPVSPTVLTFLRAALGCQFYEGYGQTEcTAGCSLTIPGDWTA-GHVGAP 483
Cdd:PRK08314 307 ----------------LRYIGG-------GGAAMPEAVAERLKELTGLDYVEGYGLTE-TMAQTHSNPPDRPKlQCLGIP 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 484 MPCNHVKLVDVEEMNYFASKGEGEVCIKGSNVFQGYLKDDEKTAEA---LDKDGWLHTGDIGKWLPNGTLKIIDRKKHIF 560
Cdd:PRK08314 363 TFGVDARVIDPETLEELPPGEVGEIVVHGPQVFKGYWNRPEATAEAfieIDGKRFFRTGDLGRMDEEGYFFITDRLKRMI 442
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1270536209 561 KlAQGEYIAPEKIENVYTRSEPVVQVFV-------HGESLQAFlvgiVVPDP--------DNVMNWAK 613
Cdd:PRK08314 443 N-ASGFKVWPAEVENLLYKHPAIQEACViatpdprRGETVKAV----VVLRPeargktteEEIIAWAR 505
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
133-575 |
3.92e-23 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 105.43 E-value: 3.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 133 VGSALLHRGFKP--SPDQFVGIFAQNRPEWTIVELGCYTYSMVAVPLYDTLGAEAITYIINKADLSVVFCDSP--EKAKL 208
Cdd:PRK06814 666 TGAFVLGRKLKKntPPGENVGVMLPNANGAAVTFFALQSAGRVPAMINFSAGIANILSACKAAQVKTVLTSRAfiEKARL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 209 --LLSNVEKGetpvLRTIVLmnpfdNDLVERgkkcgvelVSLKDiEEEGKANREKPKPP----KPDDLAVVCFTSGTTGN 282
Cdd:PRK06814 746 gpLIEALEFG----IRIIYL-----EDVRAQ--------IGLAD-KIKGLLAGRFPLVYfcnrDPDDPAVILFTSGSEGT 807
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 283 PKGAMLSHKNIVSNSAgfmKVTEDLMFpSTQDVLISFLPLAHMFervvecvvlchgariGFFQGDIRLLMDDLKVL---Q 359
Cdd:PRK06814 808 PKGVVLSHRNLLANRA---QVAARIDF-SPEDKVFNALPVFHSF---------------GLTGGLVLPLLSGVKVFlypS 868
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 360 PTIFPVVPRLLnrmFDR----IFGQ-------ANT--PvkrwmLDFASkrkeaelrsgivrndsfwdkiifhkvqaslgg 426
Cdd:PRK06814 869 PLHYRIIPELI---YDTnatiLFGTdtflngyARYahP-----YDFRS-------------------------------- 908
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 427 kVRLMVTGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCSLTIPGDWTAGHVGAPMPCNHVKLVDVEEMNyfasKGeG 506
Cdd:PRK06814 909 -LRYVFAGAEKVKEETRQTWMEKFGIRILEGYGVTETAPVIALNTPMHNKAGTVGRLLPGIEYRLEPVPGID----EG-G 982
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1270536209 507 EVCIKGSNVFQGYLKDDEKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIEN 575
Cdd:PRK06814 983 RLFVRGPNVMLGYLRAENPGVLEPPADGWYDTGDIVTIDEEGFITIKGRAKRFAKIA-GEMISLAAVEE 1050
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
269-605 |
6.77e-23 |
|
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: 100.42 E-value: 6.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 269 DLAVVCFTSGTTGNPKGAMLSHKNIVSNS---AGFMKVTEDlmfpstqDVLISFLPLAHMFERVVECVVLCHGAR---IG 342
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIAANlqlIHAMGLTEA-------DVYLNMLPLFHIAGLNLALATFHAGGAnvvME 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 343 FFQGDIRL-LMDDLKVlqpTIFPVVPRLLNRMFDRIfgqantpvkrwmldfasKRKEAELRSgiVRNdsfwdkiifhkvq 421
Cdd:cd17637 74 KFDPAEALeLIEEEKV---TLMGSFPPILSNLLDAA-----------------EKSGVDLSS--LRH------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 422 aslggkvrlmVTGAApvSPTVLTFLRAALGCQFYEGYGQTEcTAGCSLTIPGDWTAGHVGAPMPCNHVKLVDveEMNYFA 501
Cdd:cd17637 119 ----------VLGLD--APETIQRFEETTGATFWSLYGQTE-TSGLVTLSPYRERPGSAGRPGPLVRVRIVD--DNDRPV 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 502 SKGE-GEVCIKGSNVFQGYLKDDEKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRK--KHIFKlAQGEYIAPEKIENVYT 578
Cdd:cd17637 184 PAGEtGEIVVRGPLVFQGYWNLPELTAYTF-RNGWHHTGDLGRFDEDGYLWYAGRKpeKELIK-PGGENVYPAEVEKVIL 261
|
330 340
....*....|....*....|....*..
gi 1270536209 579 RSEPVVQVFVHGeslqaflvgivVPDP 605
Cdd:cd17637 262 EHPAIAEVCVIG-----------VPDP 277
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
107-671 |
9.19e-23 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 103.20 E-value: 9.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 107 PCLGHRKPNQ-PYEWISYKEVAERAEYVGSALLHRGFkpSPDQFVGIFAQNRPEWTIVELGCYTYSMVAVPL---YDTLG 182
Cdd:PRK12582 66 PWLAQREPGHgQWRKVTYGEAKRAVDALAQALLDLGL--DPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVspaYSLMS 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 183 AE--AITYIINKADLSVVFCDSPEKAKLLLSNVEKGETPVlrtIVLMNPFDndlvergkkcGVELVSLKDI-----EEEG 255
Cdd:PRK12582 144 HDhaKLKHLFDLVKPRVVFAQSGAPFARALAALDLLDVTV---VHVTGPGE----------GIASIAFADLaatppTAAV 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 256 KANREKPKPpkpDDLAVVCFTSGTTGNPKGAMLSHKNIVSNSAGFMKVTEDLMFPSTQDVLiSFLPLAHMFervvecvvl 335
Cdd:PRK12582 211 AAAIAAITP---DTVAKYLFTSGSTGMPKAVINTQRMMCANIAMQEQLRPREPDPPPPVSL-DWMPWNHTM--------- 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 336 chGARIGFfQGDIR----LLMDDLKVLqPTIFPVVPRLLNRMFDRIFGqaNTPVKRWMLDFASKRKEAELRSgivrndsf 411
Cdd:PRK12582 278 --GGNANF-NGLLWgggtLYIDDGKPL-PGMFEETIRNLREISPTVYG--NVPAGYAMLAEAMEKDDALRRS-------- 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 412 wdkiiFHKvqaslggKVRLMVTGAAPVSPTVLTFLRA----ALGCQ--FYEGYGQTEcTAGCSLTIpgDWTA---GHVGA 482
Cdd:PRK12582 344 -----FFK-------NLRLMAYGGATLSDDLYERMQAlavrTTGHRipFYTGYGATE-TAPTTTGT--HWDTervGLIGL 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 483 PMPCNHVKLVDVEEmNYfaskgegEVCIKGSNVFQGYLKDDEKTAEALDKDGWLHTGDIGKWL----PNGTLKIIDRKKH 558
Cdd:PRK12582 409 PLPGVELKLAPVGD-KY-------EVRVKGPNVTPGYHKDPELTAAAFDEEGFYRLGDAARFVdpddPEKGLIFDGRVAE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 559 IFKLAQGEYIAPEKIE-NVYTRSEPVVQ-VFVHGESlQAFLVGIVVPDPDNVMNWAKKRkfEGSYEELCKNKDFKNAVLE 636
Cdd:PRK12582 481 DFKLSTGTWVSVGTLRpDAVAACSPVIHdAVVAGQD-RAFIGLLAWPNPAACRQLAGDP--DAAPEDVVKHPAVLAILRE 557
|
570 580 590
....*....|....*....|....*....|....*
gi 1270536209 637 DLLKLGKEAGLKTfEQVKDIALHSEMFAIENGLLT 671
Cdd:PRK12582 558 GLSAHNAEAGGSS-SRIARALLMTEPPSIDAGEIT 591
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
119-584 |
1.95e-22 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 101.76 E-value: 1.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 119 EWISYKEVAERAEYVGSALLHRGFKPSpDQfVGIFAQNRPEWTIVELGCYTYSMVAVPLYDTLGAEAITYIINKADLSVV 198
Cdd:PRK06155 45 TRWTYAEAARAAAAAAHALAAAGVKRG-DR-VALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 199 FCDSPEKAklLLSNVEKGETPvLRTIVLMNPFDNDLVERGKKCgVELVSLkdieeegkANREKPKPPKPDDLAVVCFTSG 278
Cdd:PRK06155 123 VVEAALLA--ALEAADPGDLP-LPAVWLLDAPASVSVPAGWST-APLPPL--------DAPAPAAAVQPGDTAAILYTSG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 279 TTGNPKGAMLSHKNIV---SNSAGFMKVTEDlmfpstqDVLISFLPLAH-----MFERvvecvVLCHGARI--------- 341
Cdd:PRK06155 191 TTGPSKGVCCPHAQFYwwgRNSAEDLEIGAD-------DVLYTTLPLFHtnalnAFFQ-----ALLAGATYvleprfsas 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 342 GFFqgdirllmDDLKVLQPTIFpvvpRLLNRMFDRIFGQANTPVKRwmldfaskrkeaelrsgivrndsfwdkiiFHKVQ 421
Cdd:PRK06155 259 GFW--------PAVRRHGATVT----YLLGAMVSILLSQPARESDR-----------------------------AHRVR 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 422 ASLGGKvrlmvtgaapVSPTVLTFLRAALGCQFYEGYGQTECTAGCSLTIPGDwTAGHVGAPMPCNHVKLVDvEEMNYFA 501
Cdd:PRK06155 298 VALGPG----------VPAALHAAFRERFGVDLLDGYGSTETNFVIAVTHGSQ-RPGSMGRLAPGFEARVVD-EHDQELP 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 502 SKGEGEVCIKGSNVF---QGYLKDDEKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENVyT 578
Cdd:PRK06155 366 DGEPGELLLRADEPFafaTGYFGMPEKTVEAW-RNLWFHTGDRVVRDADGWFRFVDRIKDAIR-RRGENISSFEVEQV-L 442
|
....*.
gi 1270536209 579 RSEPVV 584
Cdd:PRK06155 443 LSHPAV 448
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
121-605 |
3.96e-22 |
|
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: 100.52 E-value: 3.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 121 ISYKEVAERAEYVGSALLHRGFKPspDQFVGIFAQNRPEWTIVELGCYTYSMVAVPLYDTLGAEAITYIINKADLSVVFC 200
Cdd:cd05959 30 LTYAELEAEARRVAGALRALGVKR--EERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 201 dSPEKAKLLLSNVEKGEtPVLRTIVLMNPfdndlvERGKKCGVELVSLKDIEEEGkanrEKPKPPKPDDLAVVCFTSGTT 280
Cdd:cd05959 108 -SGELAPVLAAALTKSE-HTLVVLIVSGG------AGPEAGALLLAELVAAEAEQ----LKPAATHADDPAFWLYSSGST 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 281 GNPKGAMLSHKNI--VSNSAG--FMKVTEDlmfpstqDVLISFLPLAHMFErvvecvvLCHGARIGFFQGDIRLLM---- 352
Cdd:cd05959 176 GRPKGVVHLHADIywTAELYArnVLGIRED-------DVCFSAAKLFFAYG-------LGNSLTFPLSVGATTVLMperp 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 353 ------DDLKVLQPTIFPVVPRLLNRMFdrifgQANTPVKRwmlDFASkrkeaelrsgivrndsfwdkiifhkvqaslgg 426
Cdd:cd05959 242 tpaavfKRIRRYRPTVFFGVPTLYAAML-----AAPNLPSR---DLSS-------------------------------- 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 427 kVRLMVTGAAPVSPTVLTFLRAALGCQFYEGYGQTEctagcSLTI-----PGDWTAGHVGAPMPCNHVKLVDvEEMNYFA 501
Cdd:cd05959 282 -LRLCVSAGEALPAEVGERWKARFGLDILDGIGSTE-----MLHIflsnrPGRVRYGTTGKPVPGYEVELRD-EDGGDVA 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 502 SKGEGEVCIKGSNVFQGYLKDDEKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENVYTRSE 581
Cdd:cd05959 355 DGEPGELYVRGPSSATMYWNNRDKTRDTF-QGEWTRTGDKYVRDDDGFYTYAGRADDMLK-VSGIWVSPFEVESALVQHP 432
|
490 500
....*....|....*....|....*..
gi 1270536209 582 PVVQVFVHGESLQAFL---VGIVVPDP 605
Cdd:cd05959 433 AVLEAAVVGVEDEDGLtkpKAFVVLRP 459
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
119-590 |
2.18e-21 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 98.70 E-value: 2.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 119 EWISYKEVAERAEYVGSALlHRGFKPSPDQFVGIFAQNRPEWTIVELGcyTYSMVAV--PLYDTLGAEAITYIINKADLS 196
Cdd:PRK05620 37 EQTTFAAIGARAAALAHAL-HDELGITGDQRVGSMMYNCAEHLEVLFA--VACMGAVfnPLNKQLMNDQIVHIINHAEDE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 197 VVFCDsPEKAKLLLSNVEkgETPVLRTIVLMNPFDNDLVERGKKCGVELVSLKDIEEEGKANREKPKPPKpDDLAVVCFT 276
Cdd:PRK05620 114 VIVAD-PRLAEQLGEILK--ECPCVRAVVFIGPSDADSAAAHMPEGIKVYSYEALLDGRSTVYDWPELDE-TTAAAICYS 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 277 SGTTGNPKGAMLSHKNIVSNSAGFMkvTEDlMFPSTQDVliSFL---PLAHmfervvecvVLCHGARIGFFQGDIRLLMD 353
Cdd:PRK05620 190 TGTTGAPKGVVYSHRSLYLQSLSLR--TTD-SLAVTHGE--SFLccvPIYH---------VLSWGVPLAAFMSGTPLVFP 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 354 DLKVLQPTIFPVVPRLLNRmfdrifgQANTPVKRWMldfaskrkeaELRSGIVRNdsfwdkiifHKVQASLggkvRLMVT 433
Cdd:PRK05620 256 GPDLSAPTLAKIIATAMPR-------VAHGVPTLWI----------QLMVHYLKN---------PPERMSL----QEIYV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 434 GAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCSLTIPGDWTAGHVGA---------PMPCNHvKLVDVEEMNYFASKG 504
Cdd:PRK05620 306 GGSAVPPILIKAWEERYGVDVVHVWGMTETSPVGTVARPPSGVSGEARWayrvsqgrfPASLEY-RIVNDGQVMESTDRN 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 505 EGEVCIKGSNVFQGYLKDD----------------EKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYI 568
Cdd:PRK05620 385 EGEIQVRGNWVTASYYHSPteegggaastfrgedvEDANDRFTADGWLRTGDVGSVTRDGFLTIHDRARDVIR-SGGEWI 463
|
490 500
....*....|....*....|..
gi 1270536209 569 APEKIENVYTRSEPVVQVFVHG 590
Cdd:PRK05620 464 YSAQLENYIMAAPEVVECAVIG 485
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
222-583 |
3.70e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 97.76 E-value: 3.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 222 RTIVLMNPFDnDLVERGKKCGVELVSLKDIEEEGKAnreKPKPPKPDDLAVVCFTSGTTGNPKGAMLSHKNIVSNSAGFM 301
Cdd:PRK07768 110 KAVVVGEPFL-AAAPVLEEKGIRVLTVADLLAADPI---DPVETGEDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMF 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 302 KVTEdlmFPSTQDVLISFLPLAH-MfervvecvvlchgARIGFFQGDIRLLMDDLKVlQPTIFPVVPRLLNRMFDRIFGq 380
Cdd:PRK07768 186 VAAE---FDVETDVMVSWLPLFHdM-------------GMVGFLTVPMYFGAELVKV-TPMDFLRDPLLWAELISKYRG- 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 381 ANTPVKRWMLDFASKRkeaeLRSgivrndsfwdkiifhkvQASLG----GKVRLMVTGAAPVSP-TVLTFLRA------- 448
Cdd:PRK07768 248 TMTAAPNFAYALLARR----LRR-----------------QAKPGafdlSSLRFALNGAEPIDPaDVEDLLDAgarfglr 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 449 --ALGCqfyeGYGQTECTAGCSLTIPGD--------------------WTAGHV------GAPMPCNHVKLVDvEEMNYF 500
Cdd:PRK07768 307 peAILP----AYGMAEATLAVSFSPCGAglvvdevdadllaalrravpATKGNTrrlatlGPPLPGLEVRVVD-EDGQVL 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 501 ASKGEGEVCIKGSNVFQGYLKDDeKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENVYTRS 580
Cdd:PRK07768 382 PPRGVGVIELRGESVTPGYLTMD-GFIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMA-GRNIYPTDIERAAARV 459
|
...
gi 1270536209 581 EPV 583
Cdd:PRK07768 460 EGV 462
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
121-605 |
4.60e-21 |
|
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: 97.57 E-value: 4.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 121 ISYKEVAERAEYVGSALLHRGFKPSpdQFVGIFAQNRPEWTIVELGCYTYSMVAVPLYDTLGAEAITYIINKADLSVVFC 200
Cdd:cd05970 48 FTFAELADYSDKTANFFKAMGIGKG--DTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 201 DSpekAKLLLSNVEKG--ETPVLRTIVLMNPFDNDLVERGKKcGVELVSlKDIEEegkanREKPKPPKPDDLAVVCFTSG 278
Cdd:cd05970 126 IA---EDNIPEEIEKAapECPSKPKLVWVGDPVPEGWIDFRK-LIKNAS-PDFER-----PTANSYPCGEDILLVYFSSG 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 279 TTGNPKgaMLSHKNIvsnsagfmkvtedlmfpstqdvlisfLPLAH----MFERVVEcvvlchgarigffQGDIRLLMDD 354
Cdd:cd05970 196 TTGMPK--MVEHDFT--------------------------YPLGHivtaKYWQNVR-------------EGGLHLTVAD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 355 LKVLQPtifpvvprllnrMFDRIFGQ--ANTPV-----KRW----MLDFASKRKEAELRSG------IVRND-SFWDKii 416
Cdd:cd05970 235 TGWGKA------------VWGKIYGQwiAGAAVfvydyDKFdpkaLLEKLSKYGVTTFCAPptiyrfLIREDlSRYDL-- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 417 fhkvqaslgGKVRLMVTGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAgCSLTIPG-DWTAGHVGAPMPCNHVKLVDVE 495
Cdd:cd05970 301 ---------SSLRYCTTAGEALNPEVFNTFKEKTGIKLMEGFGQTETTL-TIATFPWmEPKPGSMGKPAPGYEIDLIDRE 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 496 EMNYFASKgEGEVCIKGSN-----VFQGYLKDDEKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAP 570
Cdd:cd05970 371 GRSCEAGE-EGEIVIRTSKgkpvgLFGGYYKDAEKTAEVW-HDGYYHTGDAAWMDEDGYLWFVGRTDDLIK-SSGYRIGP 447
|
490 500 510
....*....|....*....|....*....|....*
gi 1270536209 571 EKIENVYTRSEPVVQVFVHGeslqaflvgivVPDP 605
Cdd:cd05970 448 FEVESALIQHPAVLECAVTG-----------VPDP 471
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
121-608 |
7.02e-21 |
|
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: 96.58 E-value: 7.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 121 ISYKEVAERAEYVGSALLHRGFKPspDQFVGIFAQNRPEWTIVELGCYTYSMVAVPLYDTLGAEAITYIINKADLSVVFC 200
Cdd:cd17646 24 LTYRELDERANRLAHLLRARGVGP--EDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAYMLADAGPAVVLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 201 DSpekaklllsnvekgetpvlrtivlmnpfdnDLVERGKKCGVELVSLKDIEEEGKANREKPkPPKPDDLAVVCFTSGTT 280
Cdd:cd17646 102 TA------------------------------DLAARLPAGGDVALLGDEALAAPPATPPLV-PPRPDNLAYVIYTSGST 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 281 GNPKGAMLSHKNIVsNSAGFMK------VTEDLMF--PSTQDVLIS--FLPLAHMfervvECVVLC-HGAR--IGFFQGd 347
Cdd:cd17646 151 GRPKGVMVTHAGIV-NRLLWMQdeyplgPGDRVLQktPLSFDVSVWelFWPLVAG-----ARLVVArPGGHrdPAYLAA- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 348 irlLMDDLKVlqpTIFPVVPRLLnrmfdRIFGQantpvkrwmldfaskrkEAELRSGivrndsfwdkiifhkvqASLggk 427
Cdd:cd17646 224 ---LIREHGV---TTCHFVPSML-----RVFLA-----------------EPAAGSC-----------------ASL--- 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 428 vRLMVTGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCSL-TIPGDWTAGHV--GAPMPCNHVKLVDvEEMNYFASKG 504
Cdd:cd17646 256 -RRVFCSGEALPPELAARFLALPGAELHNLYGPTEAAIDVTHwPVRGPAETPSVpiGRPVPNTRLYVLD-DALRPVPVGV 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 505 EGEVCIKGSNVFQGYLKDDEKTAEALDKDGWLH------TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENVYT 578
Cdd:cd17646 334 PGELYLGGVQLARGYLGRPALTAERFVPDPFGPgsrmyrTGDLARWRPDGALEFLGRSDDQVKI-RGFRVEPGEIEAALA 412
|
490 500 510
....*....|....*....|....*....|...
gi 1270536209 579 RSEPVVQVFV---HGESLQAFLVGIVVPDPDNV 608
Cdd:cd17646 413 AHPAVTHAVVvarAAPAGAARLVGYVVPAAGAA 445
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
267-605 |
1.19e-20 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 94.08 E-value: 1.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 267 PDDLAVVCFTSGTTGNPKGAMLSHKNIVSNS---AGFMKVTEDlmfpstqDVLISFLPLAHMFERVVECVVLchgarigF 343
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNAwmlALNSLFDPD-------DVLLCGLPLFHVNGSVVTLLTP-------L 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 344 FQGDIRLLMDDLKVLQPTIFPVVPRLlnrmfdrifgqantpVKRWMLDFASKRKEAelrsgivrndsfWDKIIFHKVQAS 423
Cdd:cd05944 67 ASGAHVVLAGPAGYRNPGLFDNFWKL---------------VERYRITSLSTVPTV------------YAALLQVPVNAD 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 424 LGgKVRLMVTGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCSLTIP-GDWTAGHVGAPMPCNHVKLVDVE-EMNYF- 500
Cdd:cd05944 120 IS-SLRFAMSGAAPLPVELRARFEDATGLPVVEGYGLTEATCLVAVNPPdGPKRPGSVGLRLPYARVRIKVLDgVGRLLr 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 501 -ASKGE-GEVCIKGSNVFQGYLkDDEKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENVYT 578
Cdd:cd05944 199 dCAPDEvGEICVAGPGVFGGYL-YTEGNKNAFVADGWLNTGDLGRLDADGYLFITGRAKDLI-IRGGHNIDPALIEEALL 276
|
330 340
....*....|....*....|....*..
gi 1270536209 579 RsEPVVqvfvhgeslqAFLVGIVVPDP 605
Cdd:cd05944 277 R-HPAV----------AFAGAVGQPDA 292
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
267-617 |
6.30e-20 |
|
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: 93.30 E-value: 6.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 267 PDDLAVVCFTSGTTGNPKGAMLSHKNIVSNSAGFMKVTEDLMFPST--QDVLISFLPLAHMFERVvecvvLCHGarigff 344
Cdd:cd17650 92 PEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWRREYELDSFPVRllQMASFSFDVFAGDFARS-----LLNG------ 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 345 qGDIRLLMDDLKVLQPTIFpvvpRLLNRmfDRIFGQANTP-VKRWMLDFASKRKE--AELRSGIVRNDSFWDKIiFHKVQ 421
Cdd:cd17650 161 -GTLVICPDEVKLDPAALY----DLILK--SRITLMESTPaLIRPVMAYVYRNGLdlSAMRLLIVGSDGCKAQD-FKTLA 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 422 ASLGGKVRLM----VTgaapvsptvltflRAALGCQFYEGYGQTECTAGcslTIPgdwtaghVGAPMPCNHVKLVDvEEM 497
Cdd:cd17650 233 ARFGQGMRIInsygVT-------------EATIDSTYYEEGRDPLGDSA---NVP-------IGRPLPNTAMYVLD-ERL 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 498 NYFASKGEGEVCIKGSNVFQGYLKDDEKTAEALDKDGW------LHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPE 571
Cdd:cd17650 289 QPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFapgermYRTGDLARWRADGNVELLGRVDHQVKI-RGFRIELG 367
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1270536209 572 KIENVYTRSEPVVQVFV---HGESLQAFLVGIVVpdPDNVMNWAKKRKF 617
Cdd:cd17650 368 EIESQLARHPAIDEAVVavrEDKGGEARLCAYVV--AAATLNTAELRAF 414
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
121-576 |
8.86e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 93.41 E-value: 8.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 121 ISYKEVAERAEYVGSALLHRGFKPspDQFVGIFAQNRPEWTIVELGCYTYSMVAVPL-YDTLGAEaITYIINKADLSVVF 199
Cdd:PRK07798 29 LTYAELEERANRLAHYLIAQGLGP--GDHVGIYARNRIEYVEAMLGAFKARAVPVNVnYRYVEDE-LRYLLDDSDAVALV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 200 CDS---PEKAKLLlsnvekGETPVLRTIVLM-NPFDNDLVERGkkcgvelVSLKDIEEEGKANREkPKPPKPDDLAVVCf 275
Cdd:PRK07798 106 YERefaPRVAEVL------PRLPKLRTLVVVeDGSGNDLLPGA-------VDYEDALAAGSPERD-FGERSPDDLYLLY- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 276 TSGTTGNPKGAMLSHKNIVSNSAG---FMKVTedlmfPSTQDVLISFLPLAHMFERVVECVVLCHGAR-----IGFFQGd 347
Cdd:PRK07798 171 TGGTTGMPKGVMWRQEDIFRVLLGgrdFATGE-----PIEDEEELAKRAAAGPGMRRFPAPPLMHGAGqwaafAALFSG- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 348 irllmddlkvlQPTIFPVVPRL-------------LNRMFdrIFGQAntpVKRWMLDFASKRKEAELRSgivrndsfwdk 414
Cdd:PRK07798 245 -----------QTVVLLPDVRFdadevwrtierekVNVIT--IVGDA---MARPLLDALEARGPYDLSS----------- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 415 iifhkvqaslggkVRLMVTGAAPVSPTVLTFLRAAL-GCQFYEGYGQTECTAGCSLTIPGDwtAGHVGAP--MPCNHVKL 491
Cdd:PRK07798 298 -------------LFAIASGGALFSPSVKEALLELLpNVVLTDSIGSSETGFGGSGTVAKG--AVHTGGPrfTIGPRTVV 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 492 VDveEMNYFASKGEGEVCI--KGSNVFQGYLKDDEKTAEAL-DKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGE 566
Cdd:PRK07798 363 LD--EDGNPVEPGSGEIGWiaRRGHIPLGYYKDPEKTAETFpTIDGvrYAIPGDRARVEADGTITLLGRGSVCINTG-GE 439
|
490
....*....|
gi 1270536209 567 YIAPEKIENV 576
Cdd:PRK07798 440 KVFPEEVEEA 449
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
121-606 |
1.60e-19 |
|
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: 92.41 E-value: 1.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 121 ISYKEVAERAEYVGSALLHRGFKPspDQFVGIFAQNRPEWTIVELGCYTYSMVAVPLYDTLGAEAITYIINKADLSVVfc 200
Cdd:cd17651 21 LTYAELDRRANRLAHRLRARGVGP--GDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFMLADAGPVLV-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 201 dspekaklLLSNVEKGETPVLRtivlmnpfdndlvergkkcgVELVSLKDIEEEGKANREKPKPPKPDDLAVVCFTSGTT 280
Cdd:cd17651 97 --------LTHPALAGELAVEL--------------------VAVTLLDQPGAAAGADAEPDPALDADDLAYVIYTSGST 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 281 GNPKGAMLSHK---NIVSNSAGFMKVTEDLmfPSTQDVLISFlplAHMFERVVEcvVLCHGARIGFFQGDIRllMDDLKV 357
Cdd:cd17651 149 GRPKGVVMPHRslaNLVAWQARASSLGPGA--RTLQFAGLGF---DVSVQEIFS--TLCAGATLVLPPEEVR--TDPPAL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 358 LqptifpvvpRLLNRM-FDRIFgqANTPVKRWMLdfaskrkEAELRSGIVrndsfwdkiifhkvqaslGGKVRLMVTG-- 434
Cdd:cd17651 220 A---------AWLDEQrISRVF--LPTVALRALA-------EHGRPLGVR------------------LAALRYLLTGge 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 435 AAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCSLTIPGD---WTA-GHVGAPMPCNHVKLVDvEEMNYFASKGEGEVCI 510
Cdd:cd17651 264 QLVLTEDLREFCAGLPGLRLHNHYGPTETHVVTALSLPGDpaaWPApPPIGRPIDNTRVYVLD-AALRPVPPGVPGELYI 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 511 KGSNVFQGYLKDDEKTAEALDKDGWL------HTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENVYTRSEPVV 584
Cdd:cd17651 343 GGAGLARGYLNRPELTAERFVPDPFVpgarmyRTGDLARWLPDGELEFLGRADDQVKI-RGFRIELGEIEAALARHPGVR 421
|
490 500
....*....|....*....|....*
gi 1270536209 585 Q--VFVHGE-SLQAFLVGIVVPDPD 606
Cdd:cd17651 422 EavVLAREDrPGEKRLVAYVVGDPE 446
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
121-615 |
2.96e-19 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 91.87 E-value: 2.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 121 ISYKEVAERAEYVGSALLHRGFKPSpdQFVGIFAQNRPEWTIVELGCYTYSMVAVPLYDTLGAEAITYIINKADLSVVFC 200
Cdd:PRK05852 44 ISYRDLARLVDDLAGQLTRSGLLPG--DRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLI 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 201 DSpekakLLLSNVEKGETPVLRTIVLMNPfdndlvERGKKCGVELVSLkDIEEEGKANREKPKPPKPDDlAVVCFTSGTT 280
Cdd:PRK05852 122 DA-----DGPHDRAEPTTRWWPLTVNVGG------DSGPSGGTLSVHL-DAATEPTPATSTPEGLRPDD-AMIMFTGGTT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 281 GNPKGAMLSHKNIVSNSAGFMKVTEdlmfPSTQDVLISFLPLAHMFERVVECV-VLCHGARI-----GFFQGdiRLLMDD 354
Cdd:PRK05852 189 GLPKMVPWTHANIASSVRAIITGYR----LSPRDATVAVMPLYHGHGLIAALLaTLASGGAVllparGRFSA--HTFWDD 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 355 LKVLQPTIFPVVPRLLNRMFDRifgqANTPvkrwmldfASKRKEAELRsgIVRNDSfwdkiifhkvqaslggkvrlmvtg 434
Cdd:PRK05852 263 IKAVGATWYTAVPTIHQILLER----AATE--------PSGRKPAALR--FIRSCS------------------------ 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 435 aAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCSLT-IPGdwtAGHVGAP-MPCNHVKLVDVEEMNYFASKGE------- 505
Cdd:PRK05852 305 -APLTAETAQALQTEFAAPVVCAFGMTEATHQVTTTqIEG---IGQTENPvVSTGLVGRSTGAQIRIVGSDGLplpagav 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 506 GEVCIKGSNVFQGYLKDDEKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENVYTRSEPVVQ 585
Cdd:PRK05852 381 GEVWLRGTTVVRGYLGDPTITAANF-TDGWLRTGDLGSLSAAGDLSIRGRIKELINRG-GEKISPERVEGVLASHPNVME 458
|
490 500 510
....*....|....*....|....*....|....*....
gi 1270536209 586 VFV-------HGESLQAFLV--GIVVPDPDNVMNWAKKR 615
Cdd:PRK05852 459 AAVfgvpdqlYGEAVAAVIVprESAPPTAEELVQFCRER 497
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
121-606 |
4.21e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 91.26 E-value: 4.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 121 ISYKEVAERAEYVGSALLHRGFKPSpDQfVGIFAQNRPEWTIVELGCYTYSMVAVPLYDTLGAEAITYIINKADLSVVFC 200
Cdd:PRK06178 59 ITYAELDELSDRFAALLRQRGVGAG-DR-VAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 201 -DSpekaklLLSNVEK--GETPvLRTIVL-----MNPFDNDLVERgkkcgvELVSLKDIEEEG-----KANREKPKP--- 264
Cdd:PRK06178 137 lDQ------LAPVVEQvrAETS-LRHVIVtsladVLPAEPTLPLP------DSLRAPRLAAAGaidllPALRACTAPvpl 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 265 --PKPDDLAVVCFTSGTTGNPKGAMLSHKNIVSNSAGFMKVTEDLmfpSTQDVLISFLPlahMFervvecvvlchgarig 342
Cdd:PRK06178 204 ppPALDALAALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAVAVVG---GEDSVFLSFLP---EF---------------- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 343 FFQGDirllmdDLKVLQPTIF--PVVprLLNRMFDRIFGQAntpVKRW-------MLDFA------SKRKEAELRS-GIV 406
Cdd:PRK06178 262 WIAGE------NFGLLFPLFSgaTLV--LLARWDAVAFMAA---VERYrvtrtvmLVDNAvelmdhPRFAEYDLSSlRQV 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 407 RNDSFWDKIifhkvqaslggkvrlmvtgaapvSPTVLTFLRAALGCQFYEG-YGQTEcTAGCSlTIpgdwTAG------- 478
Cdd:PRK06178 331 RVVSFVKKL-----------------------NPDYRQRWRALTGSVLAEAaWGMTE-THTCD-TF----TAGfqdddfd 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 479 ------HVGAPMPCNHVKLVDVEEMNYFASKGEGEVCIKGSNVFQGYLKDDEKTAEALdKDGWLHTGDIGKWLPNGTLKI 552
Cdd:PRK06178 382 llsqpvFVGLPVPGTEFKICDFETGELLPLGAEGEIVVRTPSLLKGYWNKPEATAEAL-RDGWLHTGDIGKIDEQGFLHY 460
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1270536209 553 IDRKKHIFKLaQGEYIAPEKIENVYTRsepvvqvfvHGESLQAFLVGivVPDPD 606
Cdd:PRK06178 461 LGRRKEMLKV-NGMSVFPSEVEALLGQ---------HPAVLGSAVVG--RPDPD 502
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
115-583 |
5.69e-19 |
|
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: 90.63 E-value: 5.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 115 NQPYEWISYKEVAERAEYVGSALLHRGFKPSpdQFVGIFAQNRPEWTIVELGCYTYSMVAVPlydtlgaeaityiinkad 194
Cdd:cd05908 10 DKKEKFVSYRHLREEALGYLGALQELGIKPG--QEVVFQITHNNKFLYLFWACLLGGMIAVP------------------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 195 lsvVFCDSPEKAKLLLSNVEKgetpvlrtiVLMNPFDndlvergkkcgvelvslkdIEEEGKANRekpkppKPDDLAVVC 274
Cdd:cd05908 70 ---VSIGSNEEHKLKLNKVWN---------TLKNPYL-------------------ITEEEVLCE------LADELAFIQ 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 275 FTSGTTGNPKGAMLSHKNIVSNSAGFMKVTEdlmfPSTQDVLISFLPLAHMFErvvecVVLCHGARIgfFQGDIRLLMdd 354
Cdd:cd05908 113 FSSGSTGDPKGVMLTHENLVHNMFAILNSTE----WKTKDRILSWMPLTHDMG-----LIAFHLAPL--IAGMNQYLM-- 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 355 lkvlqPT-IFPVVPRLlnrmfdrifgqantpvkrWMldfaskRKEAELRSGIVRNDSFWDKIIFHKVQASLG-----GKV 428
Cdd:cd05908 180 -----PTrLFIRRPIL------------------WL------KKASEHKATIVSSPNFGYKYFLKTLKPEKAndwdlSSI 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 429 RLMVTGAAPVSPTVLTFLRAALGC------QFYEGYGQTECTAGCSL----------------------------TIPGD 474
Cdd:cd05908 231 RMILNGAEPIDYELCHEFLDHMSKyglkrnAILPVYGLAEASVGASLpkaqspfktitlgrrhvthgepepevdkKDSEC 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 475 WTAGHVGAPMPCNHVKLVDvEEMNYFASKGEGEVCIKGSNVFQGYLKDDEKTAEALDKDGWLHTGDIGkWLPNGTLKIID 554
Cdd:cd05908 311 LTFVEVGKPIDETDIRICD-EDNKILPDGYIGHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLG-FIRNGRLVITG 388
|
490 500
....*....|....*....|....*....
gi 1270536209 555 RKKHIFkLAQGEYIAPEKIENVYTRSEPV 583
Cdd:cd05908 389 REKDII-FVNGQNVYPHDIERIAEELEGV 416
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
264-582 |
9.71e-19 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 90.92 E-value: 9.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 264 PPKPDDLAVVCFTSGTTGNPKGAMLSHKNIVSNSAGfMKVTEDLmfpSTQDVLISFLPLAHMFERVVECVV-LCHGARIG 342
Cdd:PRK08043 361 KQQPEDAALILFTSGSEGHPKGVVHSHKSLLANVEQ-IKTIADF---TPNDRFMSALPLFHSFGLTVGLFTpLLTGAEVF 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 343 FFQgdirllmddlkvlQPTIFPVVPRLLnrmFDR----IFGQANtpvkrWMLDFASkrkeaelrsgivrndsFWDKIIFH 418
Cdd:PRK08043 437 LYP-------------SPLHYRIVPELV---YDRnctvLFGTST-----FLGNYAR----------------FANPYDFA 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 419 KVqaslggkvRLMVTGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCSLTIPGDWTAGHVGAPMPCNHVKLVDVEEMn 498
Cdd:PRK08043 480 RL--------RYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSVPGI- 550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 499 yfaSKGeGEVCIKGSNVFQGYLKDDE---------KTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIA 569
Cdd:PRK08043 551 ---EQG-GRLQLKGPNIMNGYLRVEKpgvlevptaENARGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIA-GEMVS 625
|
330
....*....|...
gi 1270536209 570 PEKIENVYTRSEP 582
Cdd:PRK08043 626 LEMVEQLALGVSP 638
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
156-605 |
1.44e-18 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 89.36 E-value: 1.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 156 NRPEWTIVELGCYTYSMVAVPLYDTLGAEAITYIINKADLSVVFCdSPEKAKLLLSNVEKGETPvLRTIVLMNPFDndlv 235
Cdd:PRK08008 71 NCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLVT-SAQFYPMYRQIQQEDATP-LRHICLTRVAL---- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 236 erGKKCGVelVSLKDIEEEGKANREKPKPPKPDDLAVVCFTSGTTGNPKGAMLSHKNIVSnsAGFM-----KVTEDlmfp 310
Cdd:PRK08008 145 --PADDGV--SSFTQLKAQQPATLCYAPPLSTDDTAEILFTSGTTSRPKGVVITHYNLRF--AGYYsawqcALRDD---- 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 311 stqDVLISFLPLAHmfervVECvvLCHGARIGFFQGdirllmddlkvlqptifpvvprllnrmfdrifgqaNTPVkrwML 390
Cdd:PRK08008 215 ---DVYLTVMPAFH-----IDC--QCTAAMAAFSAG-----------------------------------ATFV---LL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 391 DFASKRKeaelrsgivrndsFWDKIifHKVQASLGGKVRLMVTG--AAPVSPT--------VLTFLRAA----------L 450
Cdd:PRK08008 247 EKYSARA-------------FWGQV--CKYRATITECIPMMIRTlmVQPPSANdrqhclreVMFYLNLSdqekdafeerF 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 451 GCQFYEGYGQTECTAGCSLTIPGD---WTAghVGAPMPCNHVKLVDveEMNYFASKGE-GEVCIKG---SNVFQGYLKDD 523
Cdd:PRK08008 312 GVRLLTSYGMTETIVGIIGDRPGDkrrWPS--IGRPGFCYEAEIRD--DHNRPLPAGEiGEICIKGvpgKTIFKEYYLDP 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 524 EKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENVYTrSEPVVQvfvhgeslQAFLVGivVP 603
Cdd:PRK08008 388 KATAKVLEADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRG-GENVSCVELENIIA-THPKIQ--------DIVVVG--IK 455
|
..
gi 1270536209 604 DP 605
Cdd:PRK08008 456 DS 457
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
269-576 |
3.84e-18 |
|
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: 86.55 E-value: 3.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 269 DLAVVCFTSGTTGNPKGAMLSHKNIVSNSAGFMKVTEDLmfpSTQDVLISFLPLAHMFERVVECVVLCHGARIGFFQGDI 348
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNW---VVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGENT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 349 RL--LMDDLKVLQPTIFPVVPRLLNRMfdrifgqantpvkrwMLDFASKRKEAElrsgivrndsfwdkiifhkvqaslgg 426
Cdd:cd17635 79 TYksLFKILTTNAVTTTCLVPTLLSKL---------------VSELKSANATVP-------------------------- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 427 KVRLMVTGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCSLTIPGDWT-AGHVGAPMPCNHVKLVDVEEMNyFASKGE 505
Cdd:cd17635 118 SLRLIGYGGSRAIAADVRFIEATGLTNTAQVYGLSETGTALCLPTDDDSIeINAVGRPYPGVDVYLAATDGIA-GPSASF 196
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1270536209 506 GEVCIKGSNVFQGYLKDDEKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENV 576
Cdd:cd17635 197 GTIWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLGERREDGFLFITGRSSESINCG-GVKIAPDEVERI 265
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
121-599 |
5.78e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 89.25 E-value: 5.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 121 ISYKEVAERAEYVGSALLHRGFkpSPDQFVGIFAQNRPEWTIVELGCYTYSMVAVPLYDTLGAEAITYIINKADLSVVFC 200
Cdd:PRK12316 2029 LSYAELDSRANRLAHRLRARGV--GPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLT 2106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 201 DSPEKAKLLLSnvekGETPVLrtivlmnPFDNDLvergkkcgvelvSLKDIEEEGKANREKPkppkpDDLAVVCFTSGTT 280
Cdd:PRK12316 2107 QRHLLERLPLP----AGVARL-------PLDRDA------------EWADYPDTAPAVQLAG-----ENLAYVIYTSGST 2158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 281 GNPKGAMLSHKNIVSnsagFMKVTEDLMFPSTQDVLISFLPLAhmFERVVE--CVVLCHGArigffqgdiRLLMDDLKVL 358
Cdd:PRK12316 2159 GLPKGVAVSHGALVA----HCQAAGERYELSPADCELQFMSFS--FDGAHEqwFHPLLNGA---------RVLIRDDELW 2223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 359 QPtifpvvprllNRMFDRIFGQANTpvkrwMLDFASkrkeaelrsgivrndSFWDKIIFHKVQASLGGKVRLMVTGAAPV 438
Cdd:PRK12316 2224 DP----------EQLYDEMERHGVT-----ILDFPP---------------VYLQQLAEHAERDGRPPAVRVYCFGGEAV 2273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 439 SPTVLTFLRAALGCQF-YEGYGQTECTagcslTIPGDWTAGH----------VGAPMPCNHVKLVDvEEMNYFASKGEGE 507
Cdd:PRK12316 2274 PAASLRLAWEALRPVYlFNGYGPTEAV-----VTPLLWKCRPqdpcgaayvpIGRALGNRRAYILD-ADLNLLAPGMAGE 2347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 508 VCIKGSNVFQGYLKDDEKTAEALDKDGWLH-------TGDIGKWLPNGTLKIIDRKKHI-----FKLAQGEyIAPEKIEN 575
Cdd:PRK12316 2348 LYLGGEGLARGYLNRPGLTAERFVPDPFSAsgerlyrTGDLARYRADGVVEYLGRIDHQvkirgFRIELGE-IEARLQAH 2426
|
490 500
....*....|....*....|....*
gi 1270536209 576 VYTRSEPVV-QVFVHGESLQAFLVG 599
Cdd:PRK12316 2427 PAVREAVVVaQDGASGKQLVAYVVP 2451
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
197-598 |
7.59e-18 |
|
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: 86.75 E-value: 7.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 197 VVFC--DSPEKAKLLLSNVEKGETPVLRTiVLMNPFDNDLVERGKKCGVELVSlkdieeegkanrekpkppkPDDLAVVC 274
Cdd:cd05919 38 VLLLmlDSPELVQLFLGCLARGAIAVVIN-PLLHPDDYAYIARDCEARLVVTS-------------------ADDIAYLL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 275 FTSGTTGNPKGAMLSHKNIVSNSAGFMKvteDLMFPSTQDVLISflpLAHMFErvveCVVLCHGARIGFFQGDIRLLMDD 354
Cdd:cd05919 98 YSSGTTGPPKGVMHAHRDPLLFADAMAR---EALGLTPGDRVFS---SAKMFF----GYGLGNSLWFPLAVGASAVLNPG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 355 ----------LKVLQPTIFPVVPRLLNRMfdrifgqantpvkrwmldfaskrkeaeLRSGIVRNDSFWDkiifhkvqasl 424
Cdd:cd05919 168 wptaervlatLARFRPTVLYGVPTFYANL---------------------------LDSCAGSPDALRS----------- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 425 ggkVRLMVTGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCSLTIPGDWTAGHVGAPMPCNHVKLVDvEEMNYFASKG 504
Cdd:cd05919 210 ---LRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVGHIFLSNRPGAWRLGSTGRPVPGYEIRLVD-EEGHTIPPGE 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 505 EGEVCIKGSNVFQGYLKDDEKTaEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENVYTRSEPVV 584
Cdd:cd05919 286 EGDLLVRGPSAAVGYWNNPEKS-RATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVG-GQWVSPVEVESLIIQHPAVA 363
|
410 420
....*....|....*....|.
gi 1270536209 585 QVFV------HGES-LQAFLV 598
Cdd:cd05919 364 EAAVvavpesTGLSrLTAFVV 384
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
267-576 |
1.12e-17 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 86.79 E-value: 1.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 267 PDDLAVVCFTSGTTGNPKGAMLSHKNIVSNSagfmKVTEDLMFPSTQDVLISFLPLAHMFervvecvvlchgariGFFQG 346
Cdd:PRK06334 182 PEDVAVILFTSGTEKLPKGVPLTHANLLANQ----RACLKFFSPKEDDVMMSFLPPFHAY---------------GFNSC 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 347 DIRLLMDDLkvlqPTIF---PVVPRLLNRMFDR----IFGqaNTPVkrwMLDF---ASKRKEA---ELRSGIVRNDSFWD 413
Cdd:PRK06334 243 TLFPLLSGV----PVVFaynPLYPKKIVEMIDEakvtFLG--STPV---FFDYilkTAKKQESclpSLRFVVIGGDAFKD 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 414 KiifhkvqaslggkvrlMVTGAAPVSPTVltflraalgcQFYEGYGQTECTAgcSLTIPGDWTAGH---VGAPMPCNHVK 490
Cdd:PRK06334 314 S----------------LYQEALKTFPHI----------QLRQGYGTTECSP--VITINTVNSPKHescVGMPIRGMDVL 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 491 LVDvEEMNYFASKGE-GEVCIKGSNVFQGYLKDDEKTA-EALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYI 568
Cdd:PRK06334 366 IVS-EETKVPVSSGEtGLVLTRGTSLFSGYLGEDFGQGfVELGGETWYVTGDLGYVDRHGELFLKGRLSRFVKIG-AEMV 443
|
....*...
gi 1270536209 569 APEKIENV 576
Cdd:PRK06334 444 SLEALESI 451
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
150-598 |
1.35e-17 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 86.61 E-value: 1.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 150 VGIFAQNRPEWTIVELGCYTYSMVAVPLYDTLGAEAITYIINKADLSVVFCDSPEK--AKLLLSNVEKGETPVLRTIVLM 227
Cdd:PLN03102 67 VSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFVDRSFEplAREVLHLLSSEDSNLNLPVIFI 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 228 NpfDNDLVERgkkcgvelVSLKDIEEEGKANREKPKPP---------KPDDLAVVCFTSGTTGNPKGAMLSHKNIVSNSA 298
Cdd:PLN03102 147 H--EIDFPKR--------PSSEELDYECLIQRGEPTPSlvarmfriqDEHDPISLNYTSGTTADPKGVVISHRGAYLSTL 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 299 GFMKVTEDLMFPstqdVLISFLPLAHmfervvecvvlCHGARIGF---FQGDIRLLMDdlKVLQPTIFPvvprllNRMFD 375
Cdd:PLN03102 217 SAIIGWEMGTCP----VYLWTLPMFH-----------CNGWTFTWgtaARGGTSVCMR--HVTAPEIYK------NIEMH 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 376 RIFGQANTP-VKRWMLDfaSKRKEAELRSGIVRndsfwdkiifhkvqaslggkvrlMVTGAAPvSPTVLTFLRAALGCQF 454
Cdd:PLN03102 274 NVTHMCCVPtVFNILLK--GNSLDLSPRSGPVH-----------------------VLTGGSP-PPAALVKKVQRLGFQV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 455 YEGYGQTECTAG---CSLTipGDWT------AGHVGAPMPCNHVKLVDVEEMNYFA-------SKGEGEVCIKGSNVFQG 518
Cdd:PLN03102 328 MHAYGLTEATGPvlfCEWQ--DEWNrlpenqQMELKARQGVSILGLADVDVKNKETqesvprdGKTMGEIVIKGSSIMKG 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 519 YLKDDEKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENVYTRSEPVVQVFV----H---GE 591
Cdd:PLN03102 406 YLKNPKATSEAF-KHGWLNTGDVGVIHPDGHVEIKDRSKDII-ISGGENISSVEVENVLYKYPKVLETAVvampHptwGE 483
|
....*..
gi 1270536209 592 SLQAFLV 598
Cdd:PLN03102 484 TPCAFVV 490
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
112-590 |
2.58e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 85.32 E-value: 2.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 112 RKPNQPY-----EWISYKEVAERAEYVGSALLHRGFkpSPDQFVGIFAQNRPEWTIVELGCYTYSMVAVPLYDTLGAEAI 186
Cdd:PRK06145 14 RTPDRAAlvyrdQEISYAEFHQRILQAAGMLHARGI--GQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 187 TYIINKADlsvvfcdspekAKLLLSNVEKGETPVLRTivlmnpfdndlvergKKCGVELVSLKDIEEEGKANREKPK--P 264
Cdd:PRK06145 92 AYILGDAG-----------AKLLLVDEEFDAIVALET---------------PKIVIDAAAQADSRRLAQGGLEIPPqaA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 265 PKPDDLAVVCFTSGTTGNPKGAMLSHKNIVSNSAGFMKVtedlMFPSTQDVLISFLPLAHmferVVEC-----VVLCHGa 339
Cdd:PRK06145 146 VAPTDLVRLMYTSGTTDRPKGVMHSYGNLHWKSIDHVIA----LGLTASERLLVVGPLYH----VGAFdlpgiAVLWVG- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 340 rigffqGDIRLLMDdlkvLQP-TIFPVVPRllnrmfDRIFGQANTPVKRWMLDFASKRKEAELrsgivrnDSF-Wdkiif 417
Cdd:PRK06145 217 ------GTLRIHRE----FDPeAVLAAIER------HRLTCAWMAPVMLSRVLTVPDRDRFDL-------DSLaW----- 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 418 hkvqaSLGGkvrlmvtGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCSLTIPGDWTA--GHVGAPMPcnHVKL-VDV 494
Cdd:PRK06145 269 -----CIGG-------GEKTPESRIRDFTRVFTRARYIDAYGLTETCSGDTLMEAGREIEkiGSTGRALA--HVEIrIAD 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 495 EEMNYFASKGEGEVCIKGSNVFQGYLKDDEKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIE 574
Cdd:PRK06145 335 GAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAF-YGDWFRSGDVGYLDEEGFLYLTDRKKDMI-ISGGENIASSEVE 412
|
490
....*....|....*.
gi 1270536209 575 NVYTRSEPVVQVFVHG 590
Cdd:PRK06145 413 RVIYELPEVAEAAVIG 428
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
267-604 |
2.86e-17 |
|
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: 85.05 E-value: 2.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 267 PDDLAVVCFTSGTTGNPKGAMLSHKNIVSnsagFMKVTEDLMFPSTQDVLISFLPLAHMFErVVECV-VLCHGARIGFFQ 345
Cdd:cd17643 92 PDDLAYVIYTSGSTGRPKGVVVSHANVLA----LFAATQRWFGFNEDDVWTLFHSYAFDFS-VWEIWgALLHGGRLVVVP 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 346 GDIRLLMDDLkvlqptifpvvPRLLNRMFDRIFGQANTPVKRWMldfaskrkEAELRsgivrndsfwdkiiFHKVQASLg 425
Cdd:cd17643 167 YEVARSPEDF-----------ARLLRDEGVTVLNQTPSAFYQLV--------EAADR--------------DGRDPLAL- 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 426 gkvRLMVTGAAPVSPTVLTFLRAALGC---QFYEGYGQTECTAGCSLTI--PGDW---TAGHVGAPMPCNHVKLVDvEEM 497
Cdd:cd17643 213 ---RYVIFGGEALEAAMLRPWAGRFGLdrpQLVNMYGITETTVHVTFRPldAADLpaaAASPIGRPLPGLRVYVLD-ADG 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 498 NYFASKGEGEVCIKGSNVFQGYLKDDEKTAE-------ALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAP 570
Cdd:cd17643 289 RPVPPGVVGELYVSGAGVARGYLGRPELTAErfvanpfGGPGSRMYRTGDLARRLPDGELEYLGRADEQVKI-RGFRIEL 367
|
330 340 350
....*....|....*....|....*....|....*..
gi 1270536209 571 EKIENVYTRSEPVVQVFV---HGESLQAFLVGIVVPD 604
Cdd:cd17643 368 GEIEAALATHPSVRDAAVivrEDEPGDTRLVAYVVAD 404
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
266-617 |
3.69e-17 |
|
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: 84.79 E-value: 3.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 266 KPDDLAVVCFTSGTTGNPKGAMLSHKNIVSNSAGFMKVtedlMFPSTQDVLISFLPLAhmFERVVE--CVVLCHGARIgf 343
Cdd:cd17644 104 QPENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKE----YGITSSDRVLQFASIA--FDVAAEeiYVTLLSGATL-- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 344 fqgdirllmddlkVLQPtifpvvprllNRMFDRIfgqantpvkrwmLDFASKRKEAELRsgiVRN--DSFWDKIIFHKVQ 421
Cdd:cd17644 176 -------------VLRP----------EEMRSSL------------EDFVQYIQQWQLT---VLSlpPAYWHLLVLELLL 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 422 ASLGG--KVRLMVTGAAPVSPTVLTFLRAALG--CQFYEGYGQTECTAGCSLTIPGDWTAGH-----VGAPMPCNHVKLV 492
Cdd:cd17644 218 STIDLpsSLRLVIVGGEAVQPELVRQWQKNVGnfIQLINVYGPTEATIAATVCRLTQLTERNitsvpIGRPIANTQVYIL 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 493 DvEEMNYFASKGEGEVCIKGSNVFQGYLKDDEKTAEALDKDGWLH--------TGDIGKWLPNGTLKIIDRKKHIFKLaQ 564
Cdd:cd17644 298 D-ENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNSseserlykTGDLARYLPDGNIEYLGRIDNQVKI-R 375
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1270536209 565 GEYIAPEKIENVYTRSEPVVQVFV---HGESLQAFLVGIVVPDPDNVMNWAKKRKF 617
Cdd:cd17644 376 GFRIELGEIEAVLSQHNDVKTAVVivrEDQPGNKRLVAYIVPHYEESPSTVELRQF 431
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
120-606 |
4.94e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 84.61 E-value: 4.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 120 WISYKEVAERAEYVGSALLHRGFKPSpDQfVGIFAQNRPEwtivelgcytysMV----AVP--------LYDTLGAEAIT 187
Cdd:PRK08162 43 RRTWAETYARCRRLASALARRGIGRG-DT-VAVLLPNIPA------------MVeahfGVPmagavlntLNTRLDAASIA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 188 YIINKADLSVVFCDsPEKAKLLLSNVEkgETPVLRTIVLmnpfDNDLVERGkkcGVELVSLKDIEE---EGKANREKPKP 264
Cdd:PRK08162 109 FMLRHGEAKVLIVD-TEFAEVAREALA--LLPGPKPLVI----DVDDPEYP---GGRFIGALDYEAflaSGDPDFAWTLP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 265 PKPDDLAVVCFTSGTTGNPKGAMLSHK----NIVSNsagfmkVTEDLMFPstQDVLISFLPLAHmfervveCVVLCH--- 337
Cdd:PRK08162 179 ADEWDAIALNYTSGTTGNPKGVVYHHRgaylNALSN------ILAWGMPK--HPVYLWTLPMFH-------CNGWCFpwt 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 338 -GARIG----FFQGDIRLLMDDLKVLQPTIF---PVVPRLLnrmfdrifgqANTPvkrwmldfaskrkeAELRSGIVrnd 409
Cdd:PRK08162 244 vAARAGtnvcLRKVDPKLIFDLIREHGVTHYcgaPIVLSAL----------INAP--------------AEWRAGID--- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 410 sfwdkiifHKVQAslggkvrlMVTGAAPvSPTVLTFLRAAlGCQFYEGYGQTEcTAG----CSL-----TIPGDWTA--- 477
Cdd:PRK08162 297 --------HPVHA--------MVAGAAP-PAAVIAKMEEI-GFDLTHVYGLTE-TYGpatvCAWqpewdALPLDERAqlk 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 478 GHVGAPMPC-NHVKLVDVEEMNYFASKGE--GEVCIKGSNVFQGYLKDDEKTAEALdKDGWLHTGDIGKWLPNGTLKIID 554
Cdd:PRK08162 358 ARQGVRYPLqEGVTVLDPDTMQPVPADGEtiGEIMFRGNIVMKGYLKNPKATEEAF-AGGWFHTGDLAVLHPDGYIKIKD 436
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1270536209 555 RKKHIFkLAQGEYIAPEKIENVYTRsEPVVqvfvhgeslqafLVGIVVPDPD 606
Cdd:PRK08162 437 RSKDII-ISGGENISSIEVEDVLYR-HPAV------------LVAAVVAKPD 474
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
121-609 |
1.84e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 82.81 E-value: 1.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 121 ISYKEVAERAEYVGSALLHRgFKPSPDQFVGIFAQNRPEWTIVELGCYTYSMVAVPLYDTLGAEAITYIINKADLSVVFC 200
Cdd:PRK07867 29 TSWREHIRGSAARAAALRAR-LDPTRPPHVGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIAHADCQLVLT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 201 DSPEKAKLllsnveKGETPVLRTIVLMNPFDNDlvergkkcgvELVSLKDIEEEgkanrekPKPPKPDDLAVVCFTSGTT 280
Cdd:PRK07867 108 ESAHAELL------DGLDPGVRVINVDSPAWAD----------ELAAHRDAEPP-------FRVADPDDLFMLIFTSGTS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 281 GNPKGAMLSHKNIVSnsAGFMKVTedlMFP-STQDVLISFLPLAHMFERVVE-CVVLCHGARI---------GFfqgdir 349
Cdd:PRK07867 165 GDPKAVRCTHRKVAS--AGVMLAQ---RFGlGPDDVCYVSMPLFHSNAVMAGwAVALAAGASIalrrkfsasGF------ 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 350 llMDDLKVLQPTIFPVVPRLLNrmfdrifgqantpvkrWMLDFASKRKEAE--LRsgivrndsfwdkiifhkvqaslggk 427
Cdd:PRK07867 234 --LPDVRRYGATYANYVGKPLS----------------YVLATPERPDDADnpLR------------------------- 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 428 vrlMVTGAAPVSPTVLTFlRAALGCQFYEGYGQTEctAGCSLTIPGDWTAGHVGAPMPcnHVKLVDVE------------ 495
Cdd:PRK07867 271 ---IVYGNEGAPGDIARF-ARRFGCVVVDGFGSTE--GGVAITRTPDTPPGALGPLPP--GVAIVDPDtgtecppaedad 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 496 --EMNYFASKGEgEVCIKGSNVFQGYLKDDEKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKI 573
Cdd:PRK07867 343 grLLNADEAIGE-LVNTAGPGGFEGYYNDPEADAERM-RGGVYWSGDLAYRDADGYAYFAGRLGDWMRV-DGENLGTAPI 419
|
490 500 510
....*....|....*....|....*....|....*....
gi 1270536209 574 ENVYTRSEPVVQVFVHGeslqaflvgivVPDP---DNVM 609
Cdd:PRK07867 420 ERILLRYPDATEVAVYA-----------VPDPvvgDQVM 447
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
267-683 |
1.94e-16 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 82.92 E-value: 1.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 267 PDDLAVVCFTSGTTGNPKGAMLSHKNIVSNS---AGFMKVTEDlmfpstqDVLISFLPLAHM--FERVVECVVL--CHGA 339
Cdd:PLN02860 171 PDDAVLICFTSGTTGRPKGVTISHSALIVQSlakIAIVGYGED-------DVYLHTAPLCHIggLSSALAMLMVgaCHVL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 340 RIGFfqgDIRLLMDDLKVLQPTIFPVVPRLlnrmfdrifgqantpvkrwMLDFASKRKEAELRSGivrndsfwdkiiFHK 419
Cdd:PLN02860 244 LPKF---DAKAALQAIKQHNVTSMITVPAM-------------------MADLISLTRKSMTWKV------------FPS 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 420 VQASLGGKVRLmvtGAAPVSPTVLTFLRAALgcqfYEGYGQTEctAGCSLTI--------------------PGDWTAGH 479
Cdd:PLN02860 290 VRKILNGGGSL---SSRLLPDAKKLFPNAKL----FSAYGMTE--ACSSLTFmtlhdptlespkqtlqtvnqTKSSSVHQ 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 480 -----VGAPMPcnHVKLvdveEMNYFASKGEGEVCIKGSNVFQGYLKDDEKTAEALDKDGWLHTGDIGKWLPNGTLKIID 554
Cdd:PLN02860 361 pqgvcVGKPAP--HVEL----KIGLDESSRVGRILTRGPHVMLGYWGQNSETASVLSNDGWLDTGDIGWIDKAGNLWLIG 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 555 RKKHIFKlAQGEYIAPEKIENVYTRSEPVVQVFVHG---ESLQAFLVGIV-VPDpdnvmNWakkrKFEGSYEELCKnkdf 630
Cdd:PLN02860 435 RSNDRIK-TGGENVYPEEVEAVLSQHPGVASVVVVGvpdSRLTEMVVACVrLRD-----GW----IWSDNEKENAK---- 500
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1270536209 631 KNAVL--EDLLKLGKEAGLKTFEQVKDIALHSEMFAienglLTPTLKAKRPELRK 683
Cdd:PLN02860 501 KNLTLssETLRHHCREKNLSRFKIPKLFVQWRKPFP-----LTTTGKIRRDEVRR 550
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
121-606 |
2.67e-16 |
|
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: 81.98 E-value: 2.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 121 ISYKEVAERAEYVGSALLHRGFKPspDQFVGIFAQNRPEWTIVELGCYTYSMVAVPLYDTLGAEAITYIINKADLSVVFC 200
Cdd:cd12115 25 LTYAELNRRANRLAARLRAAGVGP--ESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLRFILEDAQARLVLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 201 DspekaklllsnvekgetpvlrtivlmnpfdndlvergkkcgvelvslkdieeegkanrekpkppkPDDLAVVCFTSGTT 280
Cdd:cd12115 103 D-----------------------------------------------------------------PDDLAYVIYTSGST 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 281 GNPKGAMLSHKNIVS--NSAGFMKVTEDL--MFPSTQdvlISF-LPLAHMFervvecVVLCHGARIGFFQGDIRLLmDDL 355
Cdd:cd12115 118 GRPKGVAIEHRNAAAflQWAAAAFSAEELagVLASTS---ICFdLSVFELF------GPLATGGKVVLADNVLALP-DLP 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 356 KVLQPTIFPVVPRLLnrmfdrifgqantpvkrwmldfaskrkeAELrsgiVRNDSfwdkiifhkvqasLGGKVRLMVTGA 435
Cdd:cd12115 188 AAAEVTLINTVPSAA----------------------------AEL----LRHDA-------------LPASVRVVNLAG 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 436 APVSPTVLTFLRAAL-GCQFYEGYGQTECTA---GCSLTiPGDWTAGHVGAPMPCNHVKLVDvEEMNYFASKGEGEVCIK 511
Cdd:cd12115 223 EPLPRDLVQRLYARLqVERVVNLYGPSEDTTystVAPVP-PGASGEVSIGRPLANTQAYVLD-RALQPVPLGVPGELYIG 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 512 GSNVFQGYLKDDEKTAEALDKDGWL------HTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENVYTRSEPVVQ 585
Cdd:cd12115 301 GAGVARGYLGRPGLTAERFLPDPFGpgarlyRTGDLVRWRPDGLLEFLGRADNQVKV-RGFRIELGEIEAALRSIPGVRE 379
|
490 500
....*....|....*....|....
gi 1270536209 586 --VFVHGESL-QAFLVGIVVPDPD 606
Cdd:cd12115 380 avVVAIGDAAgERRLVAYIVAEPG 403
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
121-606 |
4.45e-16 |
|
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: 81.73 E-value: 4.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 121 ISYKEVAERAEYVGSALLHRGFKP-------SPdqfvgifaqNRPEWTIVELGCYtySMVAVPLYdTL----GAEaITYI 189
Cdd:COG1021 51 LSYAELDRRADRLAAGLLALGLRPgdrvvvqLP---------NVAEFVIVFFALF--RAGAIPVF-ALpahrRAE-ISHF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 190 INKADLS-VVFCDSPEKAKL--LLSNVeKGETPVLRTIVLMNPFDndlvergkkcgvELVSLKDIEEEGkanREKPKP-P 265
Cdd:COG1021 118 AEQSEAVaYIIPDRHRGFDYraLAREL-QAEVPSLRHVLVVGDAG------------EFTSLDALLAAP---ADLSEPrP 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 266 KPDDLAVVCFTSGTTGNPKGAMLSHKNIVSN---SAGFMKVTEDlmfpstqDVLISFLPLAHMFERVVECV--VLCHGAR 340
Cdd:COG1021 182 DPDDVAFFQLSGGTTGLPKLIPRTHDDYLYSvraSAEICGLDAD-------TVYLAALPAAHNFPLSSPGVlgVLYAGGT 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 341 IgffqgdirllmddlkVLQP-----TIFP-----------VVPRLLNRMfdrifgqantpvkrwmLDFASKRKeAELRSg 404
Cdd:COG1021 255 V---------------VLAPdpspdTAFPlierervtvtaLVPPLALLW----------------LDAAERSR-YDLSS- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 405 ivrndsfwdkiifhkvqaslggkVRLMVTGAAPVSPTVLTFLRAALGCQFYEGYGQTE----CTagcSLTIPGDWTAGHV 480
Cdd:COG1021 302 -----------------------LRVLQVGGAKLSPELARRVRPALGCTLQQVFGMAEglvnYT---RLDDPEEVILTTQ 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 481 GAPM-PCNHVKLVDvEEMNYFASKGEGEVCIKGSNVFQGYLKDDEKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKK-H 558
Cdd:COG1021 356 GRPIsPDDEVRIVD-EDGNPVPPGEVGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKdQ 434
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1270536209 559 IFKlaQGEYIAPEKIENvytrsepvvQVFVHGESLQAFLVGivVPDPD 606
Cdd:COG1021 435 INR--GGEKIAAEEVEN---------LLLAHPAVHDAAVVA--MPDEY 469
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
110-598 |
6.88e-16 |
|
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: 80.97 E-value: 6.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 110 GHRKPNQPYEWI---------SYKEVAERAEYVGSAL-----LHRGfkpspDQFVGIFAQnRPEWTIVELGCYTYSMVAV 175
Cdd:cd05928 22 GKRPPNPALWWVngkgdevkwSFRELGSLSRKAANVLsgacgLQRG-----DRVAVILPR-VPEWWLVNVACIRTGLVFI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 176 PLYDTLGAEAITY--IINKADlSVVFCDSpekaklLLSNVEK--GETPVLRTIVLMNPFDNDlverGKKCGVELvsLKDI 251
Cdd:cd05928 96 PGTIQLTAKDILYrlQASKAK-CIVTSDE------LAPEVDSvaSECPSLKTKLLVSEKSRD----GWLNFKEL--LNEA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 252 EEEGKANREKPKPPkpddlAVVCFTSGTTGNPKGAMLSHKN----IVSNSAGFMKVTEDLMFPSTQDVLISFLPLAHMFE 327
Cdd:cd05928 163 STEHHCVETGSQEP-----MAIYFTSGTTGSPKMAEHSHSSlglgLKVNGRYWLDLTASDIMWNTSDTGWIKSAWSSLFE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 328 RVVE--CVVLCHGARIgffqgDIRLLMDDLKVLQPTIFPVVPRLLnRMFdrifgqantpvkrwmldfaskrkeaelrsgi 405
Cdd:cd05928 238 PWIQgaCVFVHHLPRF-----DPLVILKTLSSYPITTFCGAPTVY-RML------------------------------- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 406 VRNDsfwdkIIFHKVQAslggkVRLMVTGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCSLTIPGDWTAGHVGAPMP 485
Cdd:cd05928 281 VQQD-----LSSYKFPS-----LQHCVTGGEPLNPEVLEKWKAQTGLDIYEGYGQTETGLICANFKGMKIKPGSMGKASP 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 486 CNHVKLVDvEEMNYFASKGEGEVCIKGSNV-----FQGYLKDDEKTAEALDKDGWLhTGDIGKWLPNGTLKIIDRKKHIF 560
Cdd:cd05928 351 PYDVQIID-DNGNVLPPGTEGDIGIRVKPIrpfglFSGYVDNPEKTAATIRGDFYL-TGDRGIMDEDGYFWFMGRADDVI 428
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1270536209 561 kLAQGEYIAPEKIENVYTRSEPVVQVFV-------HGESLQAFLV 598
Cdd:cd05928 429 -NSSGYRIGPFEVESALIEHPAVVESAVvsspdpiRGEVVKAFVV 472
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
121-615 |
7.56e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 80.94 E-value: 7.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 121 ISYKEVAERAEYVGSALLHRGFKPSpdQFVGIFAQNRPEWTIVELGCYTYSMVAVPLYDTLGAEAITYIINK--ADLSVV 198
Cdd:PRK06164 36 LSRAELRALVDRLAAWLAAQGVRRG--DRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRgrARWLVV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 199 fcdSPEKAKL----LLSNVEKGETPVLRTIVLMNPFDNDLVERGKKCGVELVSLKDIEEEGKAnrekPKPPKPDDLAVVC 274
Cdd:PRK06164 114 ---WPGFKGIdfaaILAAVPPDALPPLRAIAVVDDAADATPAPAPGARVQLFALPDPAPPAAA----GERAADPDAGALL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 275 FT-SGTTGNPK------GAMLSHKNIVSNSAGFmkvtedlmfpSTQDVLISFLPLahmfervveCVVLCHGARIGFFQGD 347
Cdd:PRK06164 187 FTtSGTTSGPKlvlhrqATLLRHARAIARAYGY----------DPGAVLLAALPF---------CGVFGFSTLLGALAGG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 348 IRLLMDDLkvlqptiF--PVVPRLL-----------NRMFDRIFGQAntPVKRwmlDFASKRkeaelRSGIVrndSFwdk 414
Cdd:PRK06164 248 APLVCEPV-------FdaARTARALrrhrvthtfgnDEMLRRILDTA--GERA---DFPSAR-----LFGFA---SF--- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 415 iifhkvqaslggkvrlmvtgaAPVSPTVLTFLRAAlGCQFYEGYGQTECTAGCSL-TIPGDWTAGHV--GAPM-PCNHVK 490
Cdd:PRK06164 305 ---------------------APALGELAALARAR-GVPLTGLYGSSEVQALVALqPATDPVSVRIEggGRPAsPEARVR 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 491 LVDVEEMNYFASKGEGEVCIKGSNVFQGYLKDDEKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAP 570
Cdd:PRK06164 363 ARDPQDGALLPDGESGEIEIRAPSLMRGYLDNPDATARALTDDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLG-GFLVNP 441
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1270536209 571 EKIENVYTRSEPVVQVFVHGESLQ------AFLVGI--VVPDPDNVMNWAKKR 615
Cdd:PRK06164 442 AEIEHALEALPGVAAAQVVGATRDgktvpvAFVIPTdgASPDEAGLMAACREA 494
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
121-604 |
1.51e-15 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 81.36 E-value: 1.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 121 ISYKEVAERAEYVGSALLHRGFkpSPDQFVGIFAQNRPEWTIVELGCYTYSMVAVPLYDTLGAEAITYIINKADLSVVFC 200
Cdd:PRK12467 538 LSYAELNRQANRLAHVLIAAGV--GPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLT 615
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 201 DSPEKAKLLLsnvekgetPV-LRTIVLMNPFDndlvergkkcgvelvslkdiEEEGKANREKPKPPKPDDLAVVCFTSGT 279
Cdd:PRK12467 616 QSHLLAQLPV--------PAgLRSLCLDEPAD--------------------LLCGYSGHNPEVALDPDNLAYVIYTSGS 667
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 280 TGNPKGAMLSHKNIvSNSAGFMKVTEDLmfpSTQDVLISFLPLAHMFERVVECVVLCHGARIgffqgdirLLMDDLKVLQ 359
Cdd:PRK12467 668 TGQPKGVAISHGAL-ANYVCVIAERLQL---AADDSMLMVSTFAFDLGVTELFGALASGATL--------HLLPPDCARD 735
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 360 PTIFpvvprllnrmFDRIFGQANTpvkrwMLDFASkrkeaelrsgivrndSFWDKIIFHKVQASLGGKVRLMVTGAA-PV 438
Cdd:PRK12467 736 AEAF----------AALMADQGVT-----VLKIVP---------------SHLQALLQASRVALPRPQRALVCGGEAlQV 785
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 439 SPTVLTFlRAALGCQFYEGYGQTECTAG-----CSLTiPGDWTAGHVGAPMPCNHVKLVDvEEMNYFASKGEGEVCIKGS 513
Cdd:PRK12467 786 DLLARVR-ALGPGARLINHYGPTETTVGvstyeLSDE-ERDFGNVPIGQPLANLGLYILD-HYLNPVPVGVVGELYIGGA 862
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 514 NVFQGYLKDDEKTAEALDKD------GWLH-TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENVYTRSEPVVQV 586
Cdd:PRK12467 863 GLARGYHRRPALTAERFVPDpfgadgGRLYrTGDLARYRADGVIEYLGRMDHQVKI-RGFRIELGEIEARLLAQPGVREA 941
|
490 500
....*....|....*....|....
gi 1270536209 587 FV------HGESLQAFLVGIVVPD 604
Cdd:PRK12467 942 VVlaqpgdAGLQLVAYLVPAAVAD 965
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
121-606 |
1.93e-15 |
|
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: 79.62 E-value: 1.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 121 ISYKEVAERAEYVGSALLHRGFKPspDQFVGIFAQNRPEWTIVELGCYTYSMVAVPLYDTLGAEAITYIINKADLSVVFC 200
Cdd:cd12114 13 LTYGELAERARRVAGALKAAGVRP--GDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLVLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 201 DSPekaklllsnVEKGETPVLRTIVLmnpfDNDLVERGKkcgvelvslkdieeegkanREKPKPPKPDDLAVVCFTSGTT 280
Cdd:cd12114 91 DGP---------DAQLDVAVFDVLIL----DLDALAAPA-------------------PPPPVDVAPDDLAYVIFTSGST 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 281 GNPKGAMLSHKNiVSNSAGFM----KVTEDlmfpstqDVLISFLPLAH------MFErvvecvVLCHGARIGFFQGDIR- 349
Cdd:cd12114 139 GTPKGVMISHRA-ALNTILDInrrfAVGPD-------DRVLALSSLSFdlsvydIFG------ALSAGATLVLPDEARRr 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 350 ---LLMDDLKVLQPTIFPVVPRLLNRMFDriFGQANTPVKRwmldfaskrkeaELRSGIVRNDsfWdkiifhkVQASLGG 426
Cdd:cd12114 205 dpaHWAELIERHGVTLWNSVPALLEMLLD--VLEAAQALLP------------SLRLVLLSGD--W-------IPLDLPA 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 427 KVRLMVTGAAPVSptvltflraaLGcqfyegyGQTEcTAGCSL-----TIPGDWTAGHVGAPMPCNHVKLVD-------- 493
Cdd:cd12114 262 RLRALAPDARLIS----------LG-------GATE-ASIWSIyhpidEVPPDWRSIPYGRPLANQRYRVLDprgrdcpd 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 494 -VEemnyfaskgeGEVCIKGSNVFQGYLKDDEKTAEAL--DKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYI 568
Cdd:cd12114 324 wVP----------GELWIGGRGVALGYLGDPELTAARFvtHPDGerLYRTGDLGRYRPDGTLEFLGRRDGQVKV-RGYRI 392
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1270536209 569 APEKIENVYTRSEPVVQ--VFVHGESLQAFLVGIVVPDPD 606
Cdd:cd12114 393 ELGEIEAALQAHPGVARavVVVLGDPGGKRLAAFVVPDND 432
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
269-606 |
4.39e-15 |
|
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.
Pssm-ID: 341244 [Multi-domain] Cd Length: 482 Bit Score: 78.52 E-value: 4.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 269 DLAVVCFTSGTTGNPKGAMLSHKNIVSNsagfMKVTEDLMFPSTQDVLISFLPLAHMFerVVECV----VLCHGARIGFF 344
Cdd:cd05920 140 EVALFLLSGGTTGTPKLIPRTHNDYAYN----VRASAEVCGLDQDTVYLAVLPAAHNF--PLACPgvlgTLLAGGRVVLA 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 345 Q----GDIRLLMDDLKVlqpTIFPVVPRLlnrmfdrifgqantpVKRWmLDFASKRKeAELRSgivrndsfwdkiifhkv 420
Cdd:cd05920 214 PdpspDAAFPLIEREGV---TVTALVPAL---------------VSLW-LDAAASRR-ADLSS----------------- 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 421 qaslggkVRLMVTGAAPVSPTVLTFLRAALGCQFYEGYGQTE----CTAgcsLTIPGDWTAGHVGAPM-PCNHVKLVDvE 495
Cdd:cd05920 257 -------LRLLQVGGARLSPALARRVPPVLGCTLQQVFGMAEgllnYTR---LDDPDEVIIHTQGRPMsPDDEIRVVD-E 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 496 EMNYFASKGEGEVCIKGSNVFQGYLKDDEKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIEN 575
Cdd:cd05920 326 EGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRG-GEKIAAEEVEN 404
|
330 340 350
....*....|....*....|....*....|.
gi 1270536209 576 vytrsepvvQVFVHGESLQAFLVGivVPDPD 606
Cdd:cd05920 405 ---------LLLRHPAVHDAAVVA--MPDEL 424
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
121-592 |
5.74e-15 |
|
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ligase, 4-hydroxybenzoate-CoA ligase, 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases.
Pssm-ID: 274059 [Multi-domain] Cd Length: 505 Bit Score: 77.96 E-value: 5.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 121 ISYKEVAERAEYVGSALLHRGFKPspDQFVGIFAQNRPEWTIVELGCYTYSMVAVPLYDTLGAEAITYIINKADLSVVFC 200
Cdd:TIGR02262 31 LSYGELEAQVRRLAAALRRLGVKR--EERVLLLMLDGVDFPIAFLGAIRAGIVPVALNTLLTADDYAYMLEDSRARVVFV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 201 DSpekAKLLLSNVEKGETPVLRTIVLmnpfdndlVERGKKCGVELVSLKDIEEEGkanrEKPKPPKPDDLAVVCFTSGTT 280
Cdd:TIGR02262 109 SG---ALLPVIKAALGKSPHLEHRVV--------VGRPEAGEVQLAELLATESEQ----FKPAATQADDPAFWLYSSGST 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 281 GNPKGAMLSHKNIVSNSAGFMKVT-----EDLMFPSTQDVLISFLPLAHMFERVVECVVLCHGARigffqGDIRLLMDDL 355
Cdd:TIGR02262 174 GMPKGVVHTHSNPYWTAELYARNTlgireDDVCFSAAKLFFAYGLGNALTFPMSVGATTVLMGER-----PTPDAVFDRL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 356 KVLQPTIFPVVPRLLNRMFdrifgqaNTPvkrwmldfaSKRKEAELRsgivrndsfwdkiifhkvqaslggkVRLMVTGA 435
Cdd:TIGR02262 249 RRHQPTIFYGVPTLYAAML-------ADP---------NLPSEDQVR-------------------------LRLCTSAG 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 436 APVSPTVLTFLRAALGCQFYEGYGQTECTAGCSLTIPGDWTAGHVGAPMPCNHVKLVDveEMNYFASKGE-GEVCIKGSN 514
Cdd:TIGR02262 288 EALPAEVGQRWQARFGVDIVDGIGSTEMLHIFLSNLPGDVRYGTSGKPVPGYRLRLVG--DGGQDVADGEpGELLISGPS 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 515 VFQGYLKDDEKTAEALdKDGWLHTGDigKWLPN--GTLKIIDRKKHIFKLAqGEYIAPEKIENVYTRSEPVVQVFVHGES 592
Cdd:TIGR02262 366 SATMYWNNRAKSRDTF-QGEWTRSGD--KYVRNddGSYTYAGRTDDMLKVS-GIYVSPFEIESALIQHPAVLEAAVVGVA 441
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
267-588 |
8.54e-15 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 77.22 E-value: 8.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 267 PDDLAVVCFTSGTTGNPKGAMLSHKNIVSNSAGFMkvteDLM-FPSTQDVLISfLPLAHmfervvecvvlchgarigffq 345
Cdd:PRK09029 134 PQRLATMTLTSGSTGLPKAAVHTAQAHLASAEGVL----SLMpFTAQDSWLLS-LPLFH--------------------- 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 346 gdirllmddlkvlqptifpvvprllnrmfdrIFGQAntPVKRWMLdfaskrKEAELrsgIVRND-SFWDKIifHKV-QAS 423
Cdd:PRK09029 188 -------------------------------VSGQG--IVWRWLY------AGATL---VVRDKqPLEQAL--AGCtHAS 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 424 LggkV-----RLMVTGAAPVS-----------PTVLTFLRAALGCQFYEGYGQTEctAGCSLTI-PGDWTAGhVGAPMPC 486
Cdd:PRK09029 224 L---VptqlwRLLDNRSEPLSlkavllggaaiPVELTEQAEQQGIRCWCGYGLTE--MASTVCAkRADGLAG-VGSPLPG 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 487 NHVKLVDveemnyfaskgeGEVCIKGSNVFQGYLKDDEKTAeALDKDGWLHTGDIGKWLpNGTLKIIDRKKHIFkLAQGE 566
Cdd:PRK09029 298 REVKLVD------------GEIWLRGASLALGYWRQGQLVP-LVNDEGWFATRDRGEWQ-NGELTILGRLDNLF-FSGGE 362
|
330 340
....*....|....*....|..
gi 1270536209 567 YIAPEKIENVYTRSEPVVQVFV 588
Cdd:PRK09029 363 GIQPEEIERVINQHPLVQQVFV 384
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
121-598 |
2.04e-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: 341277 [Multi-domain] Cd Length: 437 Bit Score: 76.02 E-value: 2.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 121 ISYKEVAERAEYVGSALLHRGFKPSpDQFVGIFAQNrPEWTIVELGCYTYSMVAVPLYDTLGAEAITYIINKADLSVVFC 200
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPG-DVVAGLLPRT-PELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 201 DSPEKAKLllsnvekgetpvlrtivlmnpfdndlvergkkcgvelvslkdieeegkanrekpkppkPDDLAVVCFTSGTT 280
Cdd:cd05973 79 DAANRHKL----------------------------------------------------------DSDPFVMMFTSGTT 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 281 GNPKGAMLSHKNIVSNSAgFMK----VTEDLMFPSTQD---------VLISFLPLAHMfervvecVVLCHGariGFFQGD 347
Cdd:cd05973 101 GLPKGVPVPLRALAAFGA-YLRdavdLRPEDSFWNAADpgwayglyyAITGPLALGHP-------TILLEG---GFSVES 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 348 IRLLMDDLKVLQPTIFPVVPRLLnrmfdrifgqantpvkrwMLDFASkrkeaelrsgivrndsfwdkiifhkVQASLGGK 427
Cdd:cd05973 170 TWRVIERLGVTNLAGSPTAYRLL------------------MAAGAE-------------------------VPARPKGR 206
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 428 VRLMVTGAAPVSPTVLTFLRAALGCQFYEGYGQTEctagCSLTIPGDWTAGHV------GAPMPCNHVKLVDvEEMNYFA 501
Cdd:cd05973 207 LRRVSSAGEPLTPEVIRWFDAALGVPIHDHYGQTE----LGMVLANHHALEHPvhagsaGRAMPGWRVAVLD-DDGDELG 281
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 502 SKGEGEVCIKGSNV----FQGYLKDDEKTAEAldkdGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENVY 577
Cdd:cd05973 282 PGEPGRLAIDIANSplmwFRGYQLPDTPAIDG----GYYLTGDTVEFDPDGSFSFIGRADDVITMS-GYRIGPFDVESAL 356
|
490 500
....*....|....*....|....*...
gi 1270536209 578 TRSEPVVQVFV-------HGESLQAFLV 598
Cdd:cd05973 357 IEHPAVAEAAVigvpdpeRTEVVKAFVV 384
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
422-608 |
2.12e-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: 2.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 422 ASLGGKVRLMVTGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCSLTIPGDWTAGHVGAPMPCNHVKLVDVEEmnyfA 501
Cdd:cd05974 196 ASFDVKLREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVGNSPGQPVKAGSMGRPLPGYRVALLDPDG----A 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 502 SKGEGEVCIKGSN-----VFQGYLKDDEKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENV 576
Cdd:cd05974 272 PATEGEVALDLGDtrpvgLMKGYAGDPDKTAHAM-RGGYYRTGDIAMRDEDGYLTYVGRADDVFK-SSDYRISPFELESV 349
|
170 180 190
....*....|....*....|....*....|..
gi 1270536209 577 YTRSEPVVQvfvhgeslqaflvGIVVPDPDNV 608
Cdd:cd05974 350 LIEHPAVAE-------------AAVVPSPDPV 368
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
246-583 |
2.47e-14 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 76.34 E-value: 2.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 246 VSLKDIEEEGKANREKPKPPKPD-DLAVVCFTSGTTGNPKGAMLSHKNIVSNSAGfmkVTEDLMFPSTQDVLISFLPLAH 324
Cdd:PRK05851 129 VTVHDLATAAHTNRSASLTPPDSgGPAVLQGTAGSTGTPRTAILSPGAVLSNLRG---LNARVGLDAATDVGCSWLPLYH 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 325 -MfervvecvvlchgarigffqGDIRLLMDDLK----VLQPT-IFPVVPrllnrmfdriFgqantpvkRWmLDFASkrke 398
Cdd:PRK05851 206 dM--------------------GLAFLLTAALAgaplWLAPTtAFSASP----------F--------RW-LSWLS---- 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 399 aELRSGIVRNDSFWDKII---FHKVQASLGGKVRLMVTGAAPVSPTVLT-FLRAALGCQFYEG-----YGQTECTagCSL 469
Cdd:PRK05851 243 -DSRATLTAAPNFAYNLIgkyARRVSDVDLGALRVALNGGEPVDCDGFErFATAMAPFGFDAGaaapsYGLAEST--CAV 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 470 TIP---------------GDWTAGH--VGAPMPCNHVKLVDVEEMNYFASKGEGEVCIKGSNVFQGYLKDDektaeALDK 532
Cdd:PRK05851 320 TVPvpgiglrvdevttddGSGARRHavLGNPIPGMEVRISPGDGAAGVAGREIGEIEIRGASMMSGYLGQA-----PIDP 394
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1270536209 533 DGWLHTGDIGkWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENVYTRSEPV 583
Cdd:PRK05851 395 DDWFPTGDLG-YLVDGGLVVCGRAKELITVA-GRNIFPTEIERVAAQVRGV 443
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
122-606 |
2.79e-14 |
|
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: 75.75 E-value: 2.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 122 SYKEVAERAEYVGSALLHRGFKPspDQFVGIFAQNRPEWTIVELGCYTYSMVAVPLYDTLGAEAITYIINKADlsvvfcd 201
Cdd:cd17652 14 TYAELNARANRLARLLAARGVGP--ERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYMLADAR------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 202 spekAKLLLSnvekgetpvlrtivlmnpfdndlvergkkcgvelvslkdieeegkanrekpkppKPDDLAVVCFTSGTTG 281
Cdd:cd17652 85 ----PALLLT------------------------------------------------------TPDNLAYVIYTSGSTG 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 282 NPKGAMLSHKNIVSNSAG---FMKVTED---LMFPSTQ-DVLISFLplahmfervveCVVLCHGARigffqgdirLLMDD 354
Cdd:cd17652 107 RPKGVVVTHRGLANLAAAqiaAFDVGPGsrvLQFASPSfDASVWEL-----------LMALLAGAT---------LVLAP 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 355 LKVLQPTifPVVPRLLNRmfDRIFGQANTPVKRWMLDfaskrkeaelrsgivrndsfwdkiifhkvQASLGGKVRLMVTG 434
Cdd:cd17652 167 AEELLPG--EPLADLLRE--HRITHVTLPPAALAALP-----------------------------PDDLPDLRTLVVAG 213
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 435 AAPVSPTVLtflRAALGCQFYEGYGQTECTAGCSLTIP-GDWTAGHVGAPMPCNHVKLVDvEEMNYFASKGEGEVCIKGS 513
Cdd:cd17652 214 EACPAELVD---RWAPGRRMINAYGPTETTVCATMAGPlPGGGVPPIGRPVPGTRVYVLD-ARLRPVPPGVPGELYIAGA 289
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 514 NVFQGYLKDDEKTAEALDKD------GWLH-TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENVYTRSEPVVQ- 585
Cdd:cd17652 290 GLARGYLNRPGLTAERFVADpfgapgSRMYrTGDLARWRADGQLEFLGRADDQVKI-RGFRIELGEVEAALTEHPGVAEa 368
|
490 500
....*....|....*....|...
gi 1270536209 586 -VFVHGESL-QAFLVGIVVPDPD 606
Cdd:cd17652 369 vVVVRDDRPgDKRLVAYVVPAPG 391
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
122-576 |
3.96e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 75.51 E-value: 3.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 122 SYKEVAERAEYVGSALLHRGFKPSpdQFVGIFAQNRPEWTIVELGCYTYSMVAVPLYDTLGAEAITYIINKADLSVVFCD 201
Cdd:PRK07008 41 TYRDCERRAKQLAQALAALGVEPG--DRVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRLFPEQIAYIVNHAEDRYVLFD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 202 SPekaklLLSNVEK--GETPVLRTIVLMNpfDNDLVERGKkcgVELVSLKDIEEEGKANREKPKPPKpDDLAVVCFTSGT 279
Cdd:PRK07008 119 LT-----FLPLVDAlaPQCPNVKGWVAMT--DAAHLPAGS---TPLLCYETLVGAQDGDYDWPRFDE-NQASSLCYTSGT 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 280 TGNPKGAMLSHKNIVSNSagFMKVTEDLMFPSTQDVLISFLPLAHMFERVVECVVLCHGARIgffqgdirllmddlkvlq 359
Cdd:PRK07008 188 TGNPKGALYSHRSTVLHA--YGAALPDAMGLSARDAVLPVVPMFHVNAWGLPYSAPLTGAKL------------------ 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 360 ptIFPvvprllnrmfdrifGQAntpvkrwmLDFASKRK--EAELRSGIVRNDSFWDKIIFHKVQASLG-GKVRLMVTGAA 436
Cdd:PRK07008 248 --VLP--------------GPD--------LDGKSLYEliEAERVTFSAGVPTVWLGLLNHMREAGLRfSTLRRTVIGGS 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 437 PVSPTVLTFLRAALGCQFYEGYGQTECT---AGCSLT-----IPGD------WTAGHV--GAPMpcnhvKLVDVE--EMN 498
Cdd:PRK07008 304 ACPPAMIRTFEDEYGVEVIHAWGMTEMSplgTLCKLKwkhsqLPLDeqrkllEKQGRViyGVDM-----KIVGDDgrELP 378
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1270536209 499 YfASKGEGEVCIKGSNVFQGYLKDDektAEALDkDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENV 576
Cdd:PRK07008 379 W-DGKAFGDLQVRGPWVIDRYFRGD---ASPLV-DGWFPTGDVATIDADGFMQITDRSKDVIK-SGGEWISSIDIENV 450
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
118-628 |
6.58e-14 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 74.88 E-value: 6.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 118 YEWisyKEVAERAEYVGSALLHRGFkpSPDQFVGIFAQNRPEWTIVELGCYTYSMVAVPLYDTLGAEAITYIINKADLSV 197
Cdd:PLN02479 46 YTW---AQTYQRCRRLASALAKRSI--GPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 198 VFCD------SPEKAKLLLSNVEKGETPVLRTIVLMNPFDNDLVERGKKCGVelvslkdIEEEGKANREKP----KPPKP 267
Cdd:PLN02479 121 VMVDqefftlAEEALKILAEKKKSSFKPPLLIVIGDPTCDPKSLQYALGKGA-------IEYEKFLETGDPefawKPPAD 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 268 D-DLAVVCFTSGTTGNPKGAMLSHKnivsnSAGFMKVTEDLMFPSTQD-VLISFLPLAHmfervveC---------VVLC 336
Cdd:PLN02479 194 EwQSIALGYTSGTTASPKGVVLHHR-----GAYLMALSNALIWGMNEGaVYLWTLPMFH-------CngwcftwtlAALC 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 337 hGARIGFFQGDIRLLMDDLKVLQPTIFPVVPRLLNRMFdrifgqaNTPVKRWMLdfaskrkeaelrsgivrndsfwdkii 416
Cdd:PLN02479 262 -GTNICLRQVTAKAIYSAIANYGVTHFCAAPVVLNTIV-------NAPKSETIL-------------------------- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 417 fhkvqaSLGGKVRLMVTGAAPvSPTVLtFLRAALGCQFYEGYGQTEcTAGCSL---------TIPGDwTAGHVGAPMPCN 487
Cdd:PLN02479 308 ------PLPRVVHVMTAGAAP-PPSVL-FAMSEKGFRVTHTYGLSE-TYGPSTvcawkpewdSLPPE-EQARLNARQGVR 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 488 HVKL-----VDVEEMNYFASKGE--GEVCIKGSNVFQGYLKDDEKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIF 560
Cdd:PLN02479 378 YIGLegldvVDTKTMKPVPADGKtmGEIVMRGNMVMKGYLKNPKANEEAF-ANGWFHSGDLGVKHPDGYIEIKDRSKDII 456
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1270536209 561 kLAQGEYIAPEKIENVYTRSEPVVQVFV-------HGESLQAFlvgiVVPDPDnvMNWAKKRKFEGSYEELCKNK 628
Cdd:PLN02479 457 -ISGGENISSLEVENVVYTHPAVLEASVvarpderWGESPCAF----VTLKPG--VDKSDEAALAEDIMKFCRER 524
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
121-608 |
1.34e-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: 73.59 E-value: 1.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 121 ISYKEVAERAEYVGSALLHRGfKPSPDQFVGIFAqNRPEWTIVE-LGCYTYSMVAVPLYDTLGAEAITYIINkadlsvvf 199
Cdd:cd17648 13 LTYRELNERANRLAHYLLSVA-EIRPDDLVGLVL-DKSELMIIAiLAVWKAGAAYVPIDPSYPDERIQFILE-------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 200 cDSpeKAKLLLSNvekgetpvlrtivlmnpfdndlvergkkcgvelvslkdieeegkanrekpkppkPDDLAVVCFTSGT 279
Cdd:cd17648 83 -DT--GARVVITN------------------------------------------------------STDLAYAIYTSGT 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 280 TGNPKGAMLSHKNIVSNSAGFMKvtedLMFPSTQD--VLISFLplAHMFERVVECVVLchgARIGffqGDIRLLMDDLKV 357
Cdd:cd17648 106 TGKPKGVLVEHGSVVNLRTSLSE----RYFGRDNGdeAVLFFS--NYVFDFFVEQMTL---ALLN---GQKLVVPPDEMR 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 358 LQPTIFPvvpRLLNRmfDRIFGQANTPVKRWMLDFASKrkeAELRsgivrndsfwdkiifhkvqaslggkvRLMVTGAAp 437
Cdd:cd17648 174 FDPDRFY---AYINR--EKVTYLSGTPSVLQQYDLARL---PHLK--------------------------RVDAAGEE- 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 438 VSPTVLTFLRAALGCQFYEGYGQTEC--TAGCSLTIPGDWTAGHVGAPMPCNHVKLVDvEEMNYFASKGEGEVCIKGSNV 515
Cdd:cd17648 219 FTAPVFEKLRSRFAGLIINAYGPTETtvTNHKRFFPGDQRFDKSLGRPVRNTKCYVLN-DAMKRVPVGAVGELYLGGDGV 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 516 FQGYLKDDEKTAE-------------ALDKDGWLH-TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENVYTRSE 581
Cdd:cd17648 298 ARGYLNRPELTAErflpnpfqteqerARGRNARLYkTGDLVRWLPSGELEYLGRNDFQVKI-RGQRIEPGEVEAALASYP 376
|
490 500 510
....*....|....*....|....*....|....*
gi 1270536209 582 PVVQVFV--------HGESLQAFLVGIVVPDPDNV 608
Cdd:cd17648 377 GVRECAVvakedasqAQSRIQKYLVGYYLPEPGHV 411
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
121-615 |
2.38e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 73.04 E-value: 2.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 121 ISYKEVAERAEYVGSALLHRGFKPspDQFVGIFAQNRpEWTIVELGCYTYSMVAVPLYDT-LGAEAITYIINKADLSVVF 199
Cdd:PRK07788 75 LTYAELDEQSNALARGLLALGVRA--GDGVAVLARNH-RGFVLALYAAGKVGARIILLNTgFSGPQLAEVAAREGVKALV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 200 CDSpEKAKLLlSNVEKgETPVLRTIVlmnpfdnDLVERGKKCGVELVSLKDIEEEGKANReKPKPPKPDdlAVVCFTSGT 279
Cdd:PRK07788 152 YDD-EFTDLL-SALPP-DLGRLRAWG-------GNPDDDEPSGSTDETLDDLIAGSSTAP-LPKPPKPG--GIVILTSGT 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 280 TGNPKGAMLSHKNIVSNSAGFMkvteDLM-FPSTQDVLISflplAHMFervvecvvlcHG-----ARIGFFQG------- 346
Cdd:PRK07788 219 TGTPKGAPRPEPSPLAPLAGLL----SRVpFRAGETTLLP----APMF----------HAtgwahLTLAMALGstvvlrr 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 347 --DIRLLMDDLKVLQPTIFPVVPRLLNRMFDRIfgqANTPVKRwmlDFASKRkeaelrsgivrndsfwdkIIFhkvqasl 424
Cdd:PRK07788 281 rfDPEATLEDIAKHKATALVVVPVMLSRILDLG---PEVLAKY---DTSSLK------------------IIF------- 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 425 ggkvrlmVTGAApVSPTVLTFLRAALGCQFYEGYGQTECtAGCSLTIPGDWTA--GHVGAPMPCNHVKLVDvEEMNYFAS 502
Cdd:PRK07788 330 -------VSGSA-LSPELATRALEAFGPVLYNLYGSTEV-AFATIATPEDLAEapGTVGRPPKGVTVKILD-ENGNEVPR 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 503 KGEGEVCIKGSNVFQGYLKDDEKTAealdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENVYTRSEP 582
Cdd:PRK07788 400 GVVGRIFVGNGFPFEGYTDGRDKQI----IDGLLSSGDVGYFDEDGLLFVDGRDDDMI-VSGGENVFPAEVEDLLAGHPD 474
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1270536209 583 VVQVFV-------HGESLQAFlvgiVVP------DPDNVMNWAKKR 615
Cdd:PRK07788 475 VVEAAVigvddeeFGQRLRAF----VVKapgaalDEDAIKDYVRDN 516
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
121-585 |
3.64e-13 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 73.66 E-value: 3.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 121 ISYKEVAERAEYVGSALLHRGfkpSP-DQFVGIFAQNrPEWTIVELGCYTYSMVAVPLYdtlgaeaityiinkadlsvvf 199
Cdd:PRK05691 41 LSYRDLDLRARTIAAALQARA---SFgDRAVLLFPSG-PDYVAAFFGCLYAGVIAVPAY--------------------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 200 cdSPEKAK-----LLLSNVEKGETPVLRTIVLMNPFDNDLVERGKKCGVELVSLKDIEEEGKANREKPKPPkPDDLAVVC 274
Cdd:PRK05691 96 --PPESARrhhqeRLLSIIADAEPRLLLTVADLRDSLLQMEELAAANAPELLCVDTLDPALAEAWQEPALQ-PDDIAFLQ 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 275 FTSGTTGNPKGAMLSHKNIVSNSA----GF-MKVTEDlmfpstqDVLISFLPLAHmfervvecvvlchgaRIGFFQGdir 349
Cdd:PRK05691 173 YTSGSTALPKGVQVSHGNLVANEQlirhGFgIDLNPD-------DVIVSWLPLYH---------------DMGLIGG--- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 350 llmddlkVLQPtIFPVVPRLLnrMFDRIFgqANTPVkRWMldfaskrkEA--ELRSGIVRNDSFWDKIIFHKV-QASLGG 426
Cdd:PRK05691 228 -------LLQP-IFSGVPCVL--MSPAYF--LERPL-RWL--------EAisEYGGTISGGPDFAYRLCSERVsESALER 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 427 ----KVRLMVTGAAPVSPTVL-TFLRAALGC-----QFYEGYGQTECT---AGC-------SLTIPGDWTAGHV------ 480
Cdd:PRK05691 287 ldlsRWRVAYSGSEPIRQDSLeRFAEKFAACgfdpdSFFASYGLAEATlfvSGGrrgqgipALELDAEALARNRaepgtg 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 481 ------GAPMPCNHVKLVDVEEMNYFASKGEGEVCIKGSNVFQGYLKDDEKTAEA-LDKDG--WLHTGDIGkWLPNGTLK 551
Cdd:PRK05691 367 svlmscGRSQPGHAVLIVDPQSLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTfVEHDGrtWLRTGDLG-FLRDGELF 445
|
490 500 510
....*....|....*....|....*....|....
gi 1270536209 552 IIDRKKHIFkLAQGEYIAPEKIENVYTRSEPVVQ 585
Cdd:PRK05691 446 VTGRLKDML-IVRGHNLYPQDIEKTVEREVEVVR 478
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
107-605 |
5.82e-13 |
|
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: 71.36 E-value: 5.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 107 PCLghRKPNQpyEWiSYKEVAERAEYVGSALLHRGFkPSPDQFVGIFAQNRPEWTIVELGCYTYSMVAVPLYDTLGAEAI 186
Cdd:cd05958 2 TCL--RSPER--EW-TYRDLLALANRIANVLVGELG-IVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKEL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 187 TYIINKADLSVVFCDSPEKAKlllsnvekgetpvlrtivlmnpfdndlvergkkcgvelvslkdieeegkanrekpkppk 266
Cdd:cd05958 76 AYILDKARITVALCAHALTAS----------------------------------------------------------- 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 267 pDDLAVVCFTSGTTGNPKGAMLSHKNIVSNSAGFmkvTEDLMFPSTQDVLISFLPLAHMFERVVECVVLCH-GARIGFFQ 345
Cdd:cd05958 97 -DDICILAFTSGTTGAPKATMHFHRDPLASADRY---AVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGvGASGVLLE 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 346 GDI-RLLMDDLKVLQPTIFPVVPRLLNRMFdrifgqantpvkrwmldfASKRKEAELRSGivrndsfwdkiifhkvqasl 424
Cdd:cd05958 173 EATpDLLLSAIARYKPTVLFTAPTAYRAML------------------AHPDAAGPDLSS-------------------- 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 425 ggkVRLMVTGAAPVSPTVLTFLRAALGCQFYEGYGQTEctagcSLTI-----PGDWTAGHVGAPMPCNHVKLVDvEEMNY 499
Cdd:cd05958 215 ---LRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTE-----MFHIfisarPGDARPGATGKPVPGYEAKVVD-DEGNP 285
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 500 FASKGEGEVCIKGSNvfqGYLKDDEKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENVYTR 579
Cdd:cd05958 286 VPDGTIGRLAVRGPT---GCRYLADKRQRTYVQGGWNITGDTYSRDPDGYFRHQGRSDDMIVSG-GYNIAPPEVEDVLLQ 361
|
490 500
....*....|....*....|....*....
gi 1270536209 580 SEPVVQVFVHGESLQAFLV---GIVVPDP 605
Cdd:cd05958 362 HPAVAECAVVGHPDESRGVvvkAFVVLRP 390
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
267-603 |
1.07e-12 |
|
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: 70.86 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 267 PDDLAVVCFTSGTTGNPKGAMLSHKNIVSNSAGFMKVTEdlMFPStqDVLISFLPLAhmFERVVECVV--LCHGARIgff 344
Cdd:cd17649 93 PRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAERYG--LTPG--DRELQFASFN--FDGAHEQLLppLICGACV--- 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 345 qgdirlLMDDLKVLQPtifpvvPRLLNRMFDRifGQANtpvkrwMLDFASkrkeaelrsgivrndSFWDKIIFHKVQASL 424
Cdd:cd17649 164 ------VLRPDELWAS------ADELAEMVRE--LGVT------VLDLPP---------------AYLQQLAEEADRTGD 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 425 G--GKVRLMVTGAAPVSPTvltFLRAALGCQ--FYEGYGQTECTAgCSLTIPGDWTAGHVGAPMPC-----NHVKLVDVE 495
Cdd:cd17649 209 GrpPSLRLYIFGGEALSPE---LLRRWLKAPvrLFNAYGPTEATV-TPLVWKCEAGAARAGASMPIgrplgGRSAYILDA 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 496 EMNYFASKGEGEVCIKGSNVFQGYLKDDEKTAEAL--DKDG-----WLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYI 568
Cdd:cd17649 285 DLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFvpDPFGapgsrLYRTGDLARWRDDGVIEYLGRVDHQVKI-RGFRI 363
|
330 340 350
....*....|....*....|....*....|....*..
gi 1270536209 569 APEKIENVYTRSEPVVQVFVHGES--LQAFLVGIVVP 603
Cdd:cd17649 364 ELGEIEAALLEHPGVREAAVVALDgaGGKQLVAYVVL 400
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
457-605 |
1.77e-12 |
|
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: 69.25 E-value: 1.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 457 GYGQTECTAGCSLTIPGDWTAGHVGAPMPCNHVKLVDvEEMNYFASkGE-GEVCIKGSNVFQGYLKDDEKTAEALdKDGW 535
Cdd:cd17636 142 GYGQTEVMGLATFAALGGGAIGGAGRPSPLVQVRILD-EDGREVPD-GEvGEIVARGPTVMAGYWNRPEVNARRT-RGGW 218
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1270536209 536 LHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENVyTRSEP-VVQVFVhgeslqaflvgIVVPDP 605
Cdd:cd17636 219 HHTNDLGRREPDGSLSFVGPKTRMIKSG-AENIYPAEVERC-LRQHPaVADAAV-----------IGVPDP 276
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
119-590 |
2.78e-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: 2.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 119 EWISYKEVAERAEYVGSALLHRGFKPSpdQFVGIFAQNRPEWTIVELGCYTYSMVAVPLYDTLGAEAITYIINKADlsvv 198
Cdd:cd05940 2 EALTYAELDAMANRYARWLKSLGLKPG--DVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSS---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 199 fcdspekAKLLLSnvekgetpvlrtivlmnpfdndlvergkkcgvelvslkdieeegkanrekpkppkpdDLAVVCFTSG 278
Cdd:cd05940 76 -------AKHLVV---------------------------------------------------------DAALYIYTSG 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 279 TTGNPKGAMLSHKNIVSNSAGFMKVTedLMFPstQDVLISFLPLAHMFERVVE-CVVLCHGARIGF---FQGdiRLLMDD 354
Cdd:cd05940 92 TTGLPKAAIISHRRAWRGGAFFAGSG--GALP--SDVLYTCLPLYHSTALIVGwSACLASGATLVIrkkFSA--SNFWDD 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 355 LKVLQPTIFPVVPRLLnrmfdrifgqantpvkRWMLdfASKRKEAELRsgivrndsfwdkiifHKVQASLGGKVRlmvtg 434
Cdd:cd05940 166 IRKYQATIFQYIGELC----------------RYLL--NQPPKPTERK---------------HKVRMIFGNGLR----- 207
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 435 aapvsPTVLTFLRAALGC-QFYEGYGQTECTAGcSLTIPG-DWTAGHVGA----PMPCNHVKlVDVEEMNYF-------- 500
Cdd:cd05940 208 -----PDIWEEFKERFGVpRIAEFYAATEGNSG-FINFFGkPGAIGRNPSllrkVAPLALVK-YDLESGEPIrdaegrci 280
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 501 -ASKGE-GE-VC-IKGSNVFQGYLKDDEKTAEAL-----DKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPE 571
Cdd:cd05940 281 kVPRGEpGLlISrINPLEPFDGYTDPAATEKKILrdvfkKGDAWFNTGDLMRLDGEGFWYFVDRLGDTFRW-KGENVSTT 359
|
490
....*....|....*....
gi 1270536209 572 KIENVYTRSEPVVQVFVHG 590
Cdd:cd05940 360 EVAAVLGAFPGVEEANVYG 378
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
265-603 |
9.99e-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: 67.49 E-value: 9.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 265 PKPDDLAVVCFTSGTTGNPKGAMLSHKNIvsnsAGFMKVTEDLMFPSTQDVLISFLPLAHMFervvecvvlchGARIGff 344
Cdd:cd05910 82 PKADEPAAILFTSGSTGTPKGVVYRHGTF----AAQIDALRQLYGIRPGEVDLATFPLFALF-----------GPALG-- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 345 qgdirllmddLKVLQPTIFPVVPRLLNRMFdrIFGqantPVKRWMLD--FASKrkeaelrsgivrndSFWDKIIFHKVQA 422
Cdd:cd05910 145 ----------LTSVIPDMDPTRPARADPQK--LVG----AIRQYGVSivFGSP--------------ALLERVARYCAQH 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 423 SLG-GKVRLMVTGAAPVSPTVLTFLRAAL--GCQFYEGYGQTECTAGCS------LTIPGDWTAGH----VGAPMPCNHV 489
Cdd:cd05910 195 GITlPSLRRVLSAGAPVPIALAARLRKMLsdEAEILTPYGATEALPVSSigsrelLATTTAATSGGagtcVGRPIPGVRV 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 490 KLVDVEEMNYFASKGE--------GEVCIKGSNVFQGYLKDDEKTAEALDKDG----WLHTGDIGKWLPNGTLKIIDRKK 557
Cdd:cd05910 275 RIIEIDDEPIAEWDDTlelprgeiGEITVTGPTVTPTYVNRPVATALAKIDDNsegfWHRMGDLGYLDDEGRLWFCGRKA 354
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1270536209 558 HIFKLAQGEYiapekienvYTrsEPVVQVF-VHGESLQAFLVGIVVP 603
Cdd:cd05910 355 HRVITTGGTL---------YT--EPVERVFnTHPGVRRSALVGVGKP 390
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
119-604 |
2.07e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 67.67 E-value: 2.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 119 EWISYKEVAERAEYVGSALLHRGFkpSPDQFVGIFAQNRPEWTIVELGCYTYSMVAVPLYDTLGAEAITYIINkadlsvv 198
Cdd:PRK12316 4575 EKLTYAELNRRANRLAHALIARGV--GPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMME------- 4645
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 199 fcDSpeKAKLLLSnvekgETPVLRTIVLMNPFDNDLVERgkkcgvelvslkDIEEEGKANREKPKPPKPDDLAVVCFTSG 278
Cdd:PRK12316 4646 --DS--GAALLLT-----QSHLLQRLPIPDGLASLALDR------------DEDWEGFPAHDPAVRLHPDNLAYVIYTSG 4704
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 279 TTGNPKGAMLSHKNIVSnsagFMKVTEDLMFPSTQDVLISFLPLAhmFERVVECV--VLCHGARIgffqgdirllmddlk 356
Cdd:PRK12316 4705 STGRPKGVAVSHGSLVN----HLHATGERYELTPDDRVLQFMSFS--FDGSHEGLyhPLINGASV--------------- 4763
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 357 VLQPTIFPVVPRLLNRMFDRifgqantpvKRWMLDFASkrkeaelrsgivrndSFWDKIIFHKVQASLGGKVRLMVTGAA 436
Cdd:PRK12316 4764 VIRDDSLWDPERLYAEIHEH---------RVTVLVFPP---------------VYLQQLAEHAERDGEPPSLRVYCFGGE 4819
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 437 PVSPTVLT-FLRAALGCQFYEGYGQTECTAGCSL-TIPGDWTAG----HVGAPMPCNHVKLVDVEeMNYFASKGEGEVCI 510
Cdd:PRK12316 4820 AVAQASYDlAWRALKPVYLFNGYGPTETTVTVLLwKARDGDACGaaymPIGTPLGNRSGYVLDGQ-LNPLPVGVAGELYL 4898
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 511 KGSNVFQGYLKDDEKTAE-----ALDKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIEnVYTRSEPV 583
Cdd:PRK12316 4899 GGEGVARGYLERPALTAErfvpdPFGAPGgrLYRTGDLARYRADGVIDYLGRVDHQVKI-RGFRIELGEIE-ARLREHPA 4976
|
490 500
....*....|....*....|....
gi 1270536209 584 VQ--VFVHGE-SLQAFLVGIVVPD 604
Cdd:PRK12316 4977 VReaVVIAQEgAVGKQLVGYVVPQ 5000
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
111-606 |
3.64e-11 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 66.25 E-value: 3.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 111 HRKPNQPY-------EWISYKEVAERAEYVGSALLHRGFKPSpDQfVGIFAQNRPEWTIVELGCYTYSMVAVPLYDTLGA 183
Cdd:PRK13391 8 QTTPDKPAvimastgEVVTYRELDERSNRLAHLFRSLGLKRG-DH-VAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 184 EAITYIINKADLSVVFCDSpekAKLLLSNVEKGETPVLRTIVLMNPFDndlvergkkcgvELVSLKDIEEegkANREKPK 263
Cdd:PRK13391 86 AEAAYIVDDSGARALITSA---AKLDVARALLKQCPGVRHRLVLDGDG------------ELEGFVGYAE---AVAGLPA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 264 PPKPDDL--AVVCFTSGTTGNPKG--AMLSHKNivsnsagfmkvtedlmfPSTQdvlisfLPLAHMFERVV----ECVVL 335
Cdd:PRK13391 148 TPIADESlgTDMLYSSGTTGRPKGikRPLPEQP-----------------PDTP------LPLTAFLQRLWgfrsDMVYL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 336 C-----HGARIGFFQGDIRL-----LMDD------LKVLQP---TIFPVVPRllnrMFDRifgqantpvkrwMLDF-ASK 395
Cdd:PRK13391 205 SpaplyHSAPQRAVMLVIRLggtviVMEHfdaeqyLALIEEygvTHTQLVPT----MFSR------------MLKLpEEV 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 396 RKEAELRSgivrndsfwdkiifhkvqaslggkVRLMVTGAAPVSPTVLTFLRAALGCQFYEGYGQTEcTAGCSLTIPGDW 475
Cdd:PRK13391 269 RDKYDLSS------------------------LEVAIHAAAPCPPQVKEQMIDWWGPIIHEYYAATE-GLGFTACDSEEW 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 476 TA--GHVGAPMPCN-HVKLVDVEEMnyfaSKGE-GEVCIKGSNVFQgYLKDDEKTAEALDKDG-WLHTGDIGKWLPNGTL 550
Cdd:PRK13391 324 LAhpGTVGRAMFGDlHILDDDGAEL----PPGEpGTIWFEGGRPFE-YLNDPAKTAEARHPDGtWSTVGDIGYVDEDGYL 398
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1270536209 551 KIIDRKKHIFkLAQGEYIAPEKIENVYTRSEPVVQVFVHGeslqaflvgivVPDPD 606
Cdd:PRK13391 399 YLTDRAAFMI-ISGGVNIYPQEAENLLITHPKVADAAVFG-----------VPNED 442
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
268-605 |
4.14e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 65.83 E-value: 4.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 268 DDLAVVCFTSGTTGNPKGAMLSHKN---IVSNSAGfmkvteDLMfPST--QDVLISFLPLAHMfervVECVVLCHGARig 342
Cdd:PRK07470 163 DDPCWFFFTSGTTGRPKAAVLTHGQmafVITNHLA------DLM-PGTteQDASLVVAPLSHG----AGIHQLCQVAR-- 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 343 ffqGDIRLLMDDLKVLQPTIFPVVPRL-LNRMFdrifgQANTPVKRWMLDFASKRKEaelrsgivrndsfwdkiifhkvQ 421
Cdd:PRK07470 230 ---GAATVLLPSERFDPAEVWALVERHrVTNLF-----TVPTILKMLVEHPAVDRYD----------------------H 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 422 ASLggkvRLMVTGAAPVSPTVLTFLRAALGCQFYEGYGQTECTaGC------SLTIPGDWTAGHVGapmPCNH------V 489
Cdd:PRK07470 280 SSL----RYVIYAGAPMYRADQKRALAKLGKVLVQYFGLGEVT-GNitvlppALHDAEDGPDARIG---TCGFertgmeV 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 490 KLVDvEEMNYFASKGEGEVCIKGSNVFQGYLKDDEKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIA 569
Cdd:PRK07470 352 QIQD-DEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAF-RDGWFRTGDLGHLDARGFLYITGRASDMY-ISGGSNVY 428
|
330 340 350
....*....|....*....|....*....|....*.
gi 1270536209 570 PEKIENvytrsepvvQVFVHGESLQAFLVGivVPDP 605
Cdd:PRK07470 429 PREIEE---------KLLTHPAVSEVAVLG--VPDP 453
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
262-606 |
5.70e-11 |
|
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: 65.48 E-value: 5.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 262 PKPPKPDDLA--VVCFTSGTTGNPKGamlshknIVSNSAGFMKVTEDLMFPStqdvlisfLPLAHMFERVVECVV-LCHG 338
Cdd:cd05929 117 PETPIEDEAAgwKMLYSGGTTGRPKG-------IKRGLPGGPPDNDTLMAAA--------LGFGPGADSVYLSPApLYHA 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 339 ARIGFFQGDIRL-----LM---DDLKVLQP------TIFPVVPRLLNRMfdrifgqANTP-VKRWMLDFASKrkeaelrs 403
Cdd:cd05929 182 APFRWSMTALFMggtlvLMekfDPEEFLRLieryrvTFAQFVPTMFVRL-------LKLPeAVRNAYDLSSL-------- 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 404 givrndsfwdKIIFHkvqaslggkvrlmvtGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCslTIPG-DWTA--GHV 480
Cdd:cd05929 247 ----------KRVIH---------------AAAPCPPWVKEQWIDWGGPIIWEYYGGTEGQGLT--IINGeEWLThpGSV 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 481 GAPMPcNHVKLVDvEEMNYFASKGEGEVCIKGSNVFQgYLKDDEKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIF 560
Cdd:cd05929 300 GRAVL-GKVHILD-EDGNEVPPGEIGEVYFANGPGFE-YTNDPEKTAAARNEGGWSTLGDVGYLDEDGYLYLTDRRSDMI 376
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1270536209 561 kLAQGEYIAPEKIENVYTRsepvvqvfvHGESLQAFLVGivVPDPD 606
Cdd:cd05929 377 -ISGGVNIYPQEIENALIA---------HPKVLDAAVVG--VPDEE 410
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
121-588 |
7.54e-11 |
|
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: 64.80 E-value: 7.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 121 ISYKEVAERAEYVGSALLHRGFKPspDQFVGIFAQNRPEWTIVELGCYTYSMVAVPLYDTLGAEAITYIINkadlsvvfc 200
Cdd:cd17656 14 LTYRELNERSNQLARFLREKGVKK--DSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIML--------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 201 DSpeKAKLLLSNVEKGETPVLRTIVLMnpFDNDLVERGKKCGVELVSlkdieeegkanrekpkppKPDDLAVVCFTSGTT 280
Cdd:cd17656 83 DS--GVRVVLTQRHLKSKLSFNKSTIL--LEDPSISQEDTSNIDYIN------------------NSDDLLYIIYTSGTT 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 281 GNPKGAMLSHKNIVSnsagFMKVTEDLMFPSTQDVLISFLPLAhmFERVVECVV--LCHGARIGFFQGDIRLLMDDLkvl 358
Cdd:cd17656 141 GKPKGVQLEHKNMVN----LLHFEREKTNINFSDKVLQFATCS--FDVCYQEIFstLLSGGTLYIIREETKRDVEQL--- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 359 qptifpvvprllnrmFDRIfgqANTPVKRWMLDFASKRKEAELRSGIVRNDSFWDKIIFHKVQaslggkvrLMVTgaapv 438
Cdd:cd17656 212 ---------------FDLV---KRHNIEVVFLPVAFLKFIFSEREFINRFPTCVKHIITAGEQ--------LVIT----- 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 439 SPTVLTFLRAalGCQFYEGYGQTECTAGCSLTI-PGDWTAGH--VGAPMPCNHVKLVDvEEMNYFASKGEGEVCIKGSNV 515
Cdd:cd17656 261 NEFKEMLHEH--NVHLHNHYGPSETHVVTTYTInPEAEIPELppIGKPISNTWIYILD-QEQQLQPQGIVGELYISGASV 337
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1270536209 516 FQGYLKDDEKTAEALDKDGW------LHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENVYTRSEPVVQVFV 588
Cdd:cd17656 338 ARGYLNRQELTAEKFFPDPFdpnermYRTGDLARYLPDGNIEFLGRADHQVKI-RGYRIELGEIEAQLLNHPGVSEAVV 415
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
112-604 |
8.20e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 65.75 E-value: 8.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 112 RKPNQPY-----EWISYKEVAERAEYVGSALLHRGFkpSPDQFVGIFAQNRPEWTIVELGCYTYSMVAVPLYDTLGAEAI 186
Cdd:PRK12316 3069 RTPDAVAlafgeQRLSYAELNRRANRLAHRLIERGV--GPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERL 3146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 187 TYIINKAdlsvvfcdspeKAKLLLSNvekgetPVLRtIVLMNPFDNDLVERGkkcgvelvslkdieEEGKANREKPKPPK 266
Cdd:PRK12316 3147 AYMLEDS-----------GAQLLLSQ------SHLR-LPLAQGVQVLDLDRG--------------DENYAEANPAIRTM 3194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 267 PDDLAVVCFTSGTTGNPKGAMLSHKNIVSNSAGfmkvTEDLMFPSTQDVLISFLPLAHMFERVVECVVLCHGARIgffqg 346
Cdd:PRK12316 3195 PENLAYVIYTSGSTGKPKGVGIRHSALSNHLCW----MQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARV----- 3265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 347 dirllmddlkVLQPTIFPVVPRLLNRMFDRifGQANTPVKRWmldfaskrkeaelrsgivrndSFWDKiIFHKVQASLGG 426
Cdd:PRK12316 3266 ----------VLAGPEDWRDPALLVELINS--EGVDVLHAYP---------------------SMLQA-FLEEEDAHRCT 3311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 427 KVRLMVTGAAPVSPTVLTflRAALGCQFYEGYGQTECTAGCSLTIPGDWTAGH--VGAPMPCNHVKLVDVeEMNYFASKG 504
Cdd:PRK12316 3312 SLKRIVCGGEALPADLQQ--QVFAGLPLYNLYGPTEATITVTHWQCVEEGKDAvpIGRPIANRACYILDG-SLEPVPVGA 3388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 505 EGEVCIKGSNVFQGYLKDDEKTAEALDKDGW------LHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENVYT 578
Cdd:PRK12316 3389 LGELYLGGEGLARGYHNRPGLTAERFVPDPFvpgerlYRTGDLARYRADGVIEYIGRVDHQVKI-RGFRIELGEIEARLL 3467
|
490 500
....*....|....*....|....*.
gi 1270536209 579 RSEPVVQVFVHGESLQAfLVGIVVPD 604
Cdd:PRK12316 3468 EHPWVREAVVLAVDGRQ-LVAYVVPE 3492
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
123-574 |
9.91e-11 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 65.03 E-value: 9.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 123 YKEVAERAEYVGSALLHRGFKPSpDQfVGIFAQNRPEWTIVELGCYTYSMVAVPLY--DTLGAEAItYIinkADLSVVFC 200
Cdd:PRK09192 52 YQTLRARAEAGARRLLALGLKPG-DR-VALIAETDGDFVEAFFACQYAGLVPVPLPlpMGFGGRES-YI---AQLRGMLA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 201 DSpeKAKLLLSNVEkgetpvlrtivlMNPFDNDLVERGKkcGVELVSLKDIEEEGKANREKPkPPKPDDLAVVCFTSGTT 280
Cdd:PRK09192 126 SA--QPAAIITPDE------------LLPWVNEATHGNP--LLHVLSHAWFKALPEADVALP-RPTPDDIAYLQYSSGST 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 281 GNPKGAMLSHKNIVSNSAGfmkVTEDLMFPSTQDVLISFLPLAH-MfervvecvvlchgARIGFFqgdirllmddlkvLQ 359
Cdd:PRK09192 189 RFPRGVIITHRALMANLRA---ISHDGLKVRPGDRCVSWLPFYHdM-------------GLVGFL-------------LT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 360 PTIFPV-VPRLLNRMFdrifgqANTPVKrWmLDFASKRkeaelRSGIVRNDSFWDKIIFHKVQ-ASLGG----KVRLMVT 433
Cdd:PRK09192 240 PVATQLsVDYLPTRDF------ARRPLQ-W-LDLISRN-----RGTISYSPPFGYELCARRVNsKDLAEldlsCWRVAGI 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 434 GAAPVSPTVL-----TFlrAALGCQ---FYEGYGQTECTAGCSLTIPGDwtaghvGApmpcnHVKLVDVEEMNY------ 499
Cdd:PRK09192 307 GADMIRPDVLhqfaeAF--APAGFDdkaFMPSYGLAEATLAVSFSPLGS------GI-----VVEEVDRDRLEYqgkava 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 500 ----------FASKGE----------------------GEVCIKGSNVFQGYLKDDEkTAEALDKDGWLHTGDIGkWLPN 547
Cdd:PRK09192 374 pgaetrrvrtFVNCGKalpgheieirneagmplpervvGHICVRGPSLMSGYFRDEE-SQDVLAADGWLDTGDLG-YLLD 451
|
490 500
....*....|....*....|....*..
gi 1270536209 548 GTLKIIDRKKHIFkLAQGEYIAPEKIE 574
Cdd:PRK09192 452 GYLYITGRAKDLI-IINGRNIWPQDIE 477
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
267-614 |
1.58e-10 |
|
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: 63.73 E-value: 1.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 267 PDDLAVVCFTSGTTGNPKGAMLSHKNIVS----NSAGFMKVTED--LMFPStqdvlISFLPLA-HMFERvvecvvLCHGA 339
Cdd:cd17645 103 PDDLAYVIYTSGSTGLPKGVMIEHHNLVNlcewHRPYFGVTPADksLVYAS-----FSFDASAwEIFPH------LTAGA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 340 RIGFFQGDIRLLMDDLkvlqptifpvvprllnrmfDRIFGQANTPVKRWMLDFASKRKEAElrsgivrNDSFwdkiifhk 419
Cdd:cd17645 172 ALHVVPSERRLDLDAL-------------------NDYFNQEGITISFLPTGAAEQFMQLD-------NQSL-------- 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 420 vqaslggkvRLMVTGAAPVSPTVLTflraalGCQFYEGYGQTECTAgCSLTIPGDWTAGHVGAPMPCNHVKLVDVEEMNY 499
Cdd:cd17645 218 ---------RVLLTGGDKLKKIERK------GYKLVNNYGPTENTV-VATSFEIDKPYANIPIGKPIDNTRVYILDEALQ 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 500 FASKG-EGEVCIKGSNVFQGYLKDDEKTAEALDKDGWL------HTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEK 572
Cdd:cd17645 282 LQPIGvAGELCIAGEGLARGYLNRPELTAEKFIVHPFVpgermyRTGDLAKFLPDGNIEFLGRLDQQVKI-RGYRIEPGE 360
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1270536209 573 IENV---YTRSEPVVQVFVHGESLQAFLVGIVVP----DPDNVMNWAKK 614
Cdd:cd17645 361 IEPFlmnHPLIELAAVLAKEDADGRKYLVAYVTApeeiPHEELREWLKN 409
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
118-603 |
2.00e-10 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 63.76 E-value: 2.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 118 YEWISYKEVAERAEYVGSALLHRGFK----------PSPDQFVGIFAqnrpewtIVELGcytysmvAVP-LYDT-LGAEA 185
Cdd:PRK09274 39 YDELSFAELDARSDAIAHGLNAAGIGrgmravlmvtPSLEFFALTFA-------LFKAG-------AVPvLVDPgMGIKN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 186 ITYIINKADLSVvFCDSPEK--AKLLLSNVEKGetpvLRTIVLmnpfdndlVERGKKCGVelVSLKDIEEEGKANREKPK 263
Cdd:PRK09274 105 LKQCLAEAQPDA-FIGIPKAhlARRLFGWGKPS----VRRLVT--------VGGRLLWGG--TTLATLLRDGAAAPFPMA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 264 PPKPDDLAVVCFTSGTTGNPKGAMLSHKnivsnsagfmkvtedlmfpstqdvlisflplahMFERVVECVvlchGARIGF 343
Cdd:PRK09274 170 DLAPDDMAAILFTSGSTGTPKGVVYTHG---------------------------------MFEAQIEAL----REDYGI 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 344 FQGDIrllmdDLkvlqPTiFPVVPrllnrmfdrIFGQA--NTPVKRWMlDFA--SKRKEAELRSGIVR--------NDSF 411
Cdd:PRK09274 213 EPGEI-----DL----PT-FPLFA---------LFGPAlgMTSVIPDM-DPTrpATVDPAKLFAAIERygvtnlfgSPAL 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 412 WDKIIFHKVQ--ASLGGkVRLMVTGAAPVSPTVLTFLRAAL--GCQFYEGYGQTECTAGCS------LTIPGDWT---AG 478
Cdd:PRK09274 273 LERLGRYGEAngIKLPS-LRRVISAGAPVPIAVIERFRAMLppDAEILTPYGATEALPISSiesreiLFATRAATdngAG 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 479 H-VGAPMPCNHVKLVDV--------EEMNYFASKGEGEVCIKGSNVFQGYLKDDEKTAEA--LDKDG--WLHTGDIGkWL 545
Cdd:PRK09274 352 IcVGRPVDGVEVRIIAIsdapipewDDALRLATGEIGEIVVAGPMVTRSYYNRPEATRLAkiPDGQGdvWHRMGDLG-YL 430
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 546 -PNGTLKIIDRKKHIFKLAQGEYiapekienvYTrsEPVVQVF-VHGESLQAFLVGIVVP 603
Cdd:PRK09274 431 dAQGRLWFCGRKAHRVETAGGTL---------YT--IPCERIFnTHPGVKRSALVGVGVP 479
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
122-576 |
2.09e-10 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 63.62 E-value: 2.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 122 SYKEVAERAEYVGSALLHRGFKPSpDQfVGIFAQNRPEWTIVELGCYTYSMVAVPLYDTLGAEAITYIINKADLSVVFCD 201
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRDGIKLG-DR-VATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVITD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 202 spekaKLLLSNVEK--GETPVLRTIVLMNpfDNDLVERGKKCGveLVSLKDIEEEGKANReKPKPPKPDDLAVVCFTSGT 279
Cdd:PRK06018 119 -----LTFVPILEKiaDKLPSVERYVVLT--DAAHMPQTTLKN--AVAYEEWIAEADGDF-AWKTFDENTAAGMCYTSGT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 280 TGNPKGAMLSHKNIVSNSagFMKVTEDLMFPSTQDVLISFLPLAH------------MFERVVecvvlCHGARIGffQGD 347
Cdd:PRK06018 189 TGDPKGVLYSHRSNVLHA--LMANNGDALGTSAADTMLPVVPLFHanswgiafsapsMGTKLV-----MPGAKLD--GAS 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 348 IRLLMDDLKVlqpTIFPVVPRLlnrmfdrifgqantpvkrWMLDFASKRKEaelrsgivrndsfwDKIIFHKVQASLGGk 427
Cdd:PRK06018 260 VYELLDTEKV---TFTAGVPTV------------------WLMLLQYMEKE--------------GLKLPHLKMVVCGG- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 428 vrlmvtGAAPVSptvltFLRA--ALGCQFYEGYGQTECTAGCSL--------TIPGDWTAGHV---GAPMPCNHVKLVDv 494
Cdd:PRK06018 304 ------SAMPRS-----MIKAfeDMGVEVRHAWGMTEMSPLGTLaalkppfsKLPGDARLDVLqkqGYPPFGVEMKITD- 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 495 EEMNYFASKGE--GEVCIKGSNVFQGYLKDDektAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEK 572
Cdd:PRK06018 372 DAGKELPWDGKtfGRLKVRGPAVAAAYYRVD---GEILDDDGFFDTGDVATIDAYGYMRITDRSKDVIK-SGGEWISSID 447
|
....
gi 1270536209 573 IENV 576
Cdd:PRK06018 448 LENL 451
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
121-604 |
3.72e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 63.64 E-value: 3.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 121 ISYKEVAERAEYVGSALLHRGFKPspDQFVGIFAQNRPEWTIVELGCYTYSMVAVPLYDTLGAEAITYIINKADLSVVFC 200
Cdd:PRK12467 1600 LTYGELNRRANRLAHRLIALGVGP--EVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLT 1677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 201 DSPEKAKLLLSNvekgetpvlrtivlmnpfdndlvergkkcGVELVSLkDIEEEGKANREKPKP---PKPDDLAVVCFTS 277
Cdd:PRK12467 1678 QSHLQARLPLPD-----------------------------GLRSLVL-DQEDDWLEGYSDSNPavnLAPQNLAYVIYTS 1727
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 278 GTTGNPKGAMLSHKNIVsNSAGFMKVTEDLmfpSTQDVLISFLPLAhmFERVVECVV--LCHGARIgffqgdirllmddl 355
Cdd:PRK12467 1728 GSTGRPKGAGNRHGALV-NRLCATQEAYQL---SAADVVLQFTSFA--FDVSVWELFwpLINGARL-------------- 1787
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 356 kVLQPtifPVVPRLLNRMFDRIFGQANTpvkrwMLDFASkrkeaelrsgivrndSFWDKIIFHKVQASLGGKVRLMVTGA 435
Cdd:PRK12467 1788 -VIAP---PGAHRDPEQLIQLIERQQVT-----TLHFVP---------------SMLQQLLQMDEQVEHPLSLRRVVCGG 1843
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 436 APVSPTVLTFLRAALG-CQFYEGYGQTECTAG-----CSLTIPGDWTAGHVGAPMPCNHVKLVDvEEMNYFASKGEGEVC 509
Cdd:PRK12467 1844 EALEVEALRPWLERLPdTGLFNLYGPTETAVDvthwtCRRKDLEGRDSVPIGQPIANLSTYILD-ASLNPVPIGVAGELY 1922
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 510 IKGSNVFQGYLKDDEKTAEAL------DKDGWLH-TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIEnVYTRSEP 582
Cdd:PRK12467 1923 LGGVGLARGYLNRPALTAERFvadpfgTVGSRLYrTGDLARYRADGVIEYLGRIDHQVKI-RGFRIELGEIE-ARLREQG 2000
|
490 500
....*....|....*....|....*
gi 1270536209 583 VVQ---VFVHGESLQAFLVGIVVPD 604
Cdd:PRK12467 2001 GVReavVIAQDGANGKQLVAYVVPT 2025
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
122-628 |
6.66e-10 |
|
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: 62.06 E-value: 6.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 122 SYKEVAERAEYVGSALLHRGFkpSPDQFVGIFAQNRPEWTIVELGCYTYSMVAVPLYDTLGAEAITYIINKADLSVVFCD 201
Cdd:cd05915 26 TYAEVYQRARRLMGGLRALGV--GVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLLFD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 202 S-----PEKAKLLLSNVEKgetpvlrtivlmNPFDNDLVERgkkcgvelvsLKDIEEEGKANREKPKPPKPDDLAVVCFT 276
Cdd:cd05915 104 PnllplVEAIRGELKTVQH------------FVVMDEKAPE----------GYLAYEEALGEEADPVRVPERAACGMAYT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 277 SGTTGNPKGAMLSHKNIVSNSAGFMKVTEdlMFPSTQDVLISFLPLAHmfervveCVVLCHGARIGFFQGDIRLLMDdlk 356
Cdd:cd05915 162 TGTTGLPKGVVYSHRALVLHSLAASLVDG--TALSEKDVVLPVVPMFH-------VNAWCLPYAATLVGAKQVLPGP--- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 357 VLQPTIfpvvprllnrMFDRIfgqantpVKRWMLDFASKRKEAELRSGIvrNDSfwdkiifhkVQASLGGKVRLMVTGAA 436
Cdd:cd05915 230 RLDPAS----------LVELF-------DGEGVTFTAGVPTVWLALADY--LES---------TGHRLKTLRRLVVGGSA 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 437 PvsPTVLTFLRA--------ALGCQFYEGYGqTECTAGCSLTIPGDWTAGHVGAPMPCNH-VKLVDVEEMNYFASKGEGE 507
Cdd:cd05915 282 A--PRSLIARFErmgvevrqGYGLTETSPVV-VQNFVKSHLESLSEEEKLTLKAKTGLPIpLVRLRVADEEGRPVPKDGK 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 508 ----VCIKGSNVFQGYLKDDEKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENVytrsepv 583
Cdd:cd05915 359 algeVQLKGPWITGGYYGNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSG-GEWISSVDLENA------- 430
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1270536209 584 vqVFVHGESLQAFLVGivVPDP---DNVMNWAKKRKFEGSYEEL---CKNK 628
Cdd:cd05915 431 --LMGHPKVKEAAVVA--IPHPkwqERPLAVVVPRGEKPTPEELnehLLKA 477
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
113-622 |
6.75e-10 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 61.83 E-value: 6.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 113 KPNQP-YEW----ISYKEVAERAEYVGSALLHRGF-KPSPdqfVGIFAQNRPEWTIVELGC----YTYsmvaVPLYDTLG 182
Cdd:PRK04813 15 QPDFPaYDYlgekLTYGQLKEDSDALAAFIDSLKLpDKSP---IIVFGHMSPEMLATFLGAvkagHAY----IPVDVSSP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 183 AEAITYIINKADLSVVFCDSPEkaklllsNVEKGETPVLRtivlmnpfdndlvergkkcgveLVSLKDIEEEGKAnREKP 262
Cdd:PRK04813 88 AERIEMIIEVAKPSLIIATEEL-------PLEILGIPVIT----------------------LDELKDIFATGNP-YDFD 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 263 KPPKPDDLAVVCFTSGTTGNPKGAMLSHKNIVSnSAGFMkvTEDLMFPSTQDVLI----SFlplahmfervvecvvlchg 338
Cdd:PRK04813 138 HAVKGDDNYYIIFTSGTTGKPKGVQISHDNLVS-FTNWM--LEDFALPEGPQFLNqapySF------------------- 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 339 arigffqgdirllmdDLKV--LQP------TIFPVV------PRLLNRMFdrifgqANTPVKRW----------MLD--F 392
Cdd:PRK04813 196 ---------------DLSVmdLYPtlasggTLVALPkdmtanFKQLFETL------PQLPINVWvstpsfadmcLLDpsF 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 393 ASKrKEAELRSGIvrndsFWDKIIFHKVQASLggKVRlmvtgaapvsptvltFLRAalgcQFYEGYGQTECT-AGCSLTI 471
Cdd:PRK04813 255 NEE-HLPNLTHFL-----FCGEELPHKTAKKL--LER---------------FPSA----TIYNTYGPTEATvAVTSIEI 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 472 PGDWTAGHvgAPMPCNHVK-----LVDVEEMNYFASKGEGEVCIKGSNVFQGYLKDDEKTAEAL-DKDGW--LHTGDIGK 543
Cdd:PRK04813 308 TDEMLDQY--KRLPIGYAKpdsplLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFfTFDGQpaYHTGDAGY 385
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 544 wLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENVYTRSEPV---VQVFVHGESLQAFLVGIVVPdpdnvmnwaKKRKFEGS 620
Cdd:PRK04813 386 -LEDGLLFYQGRIDFQIKLN-GYRIELEEIEQNLRQSSYVesaVVVPYNKDHKVQYLIAYVVP---------KEEDFERE 454
|
..
gi 1270536209 621 YE 622
Cdd:PRK04813 455 FE 456
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
121-606 |
3.91e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 59.53 E-value: 3.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 121 ISYKEVAERAEYVGSALLHRGFKPspDQFVGIFAQNRPEWTIVELGCYTYSMVAVPLYDTLGAEAITYIINKADLSVVFC 200
Cdd:PRK08276 12 VTYGELEARSNRLAHGLRALGLRE--GDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVLIV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 201 DspekAKLLlsnvekgetPVLRTIVLMNPFDND--LVERGKKCGVElvslkDIEEEGKANREKPKPPKP--DDLAvvcFT 276
Cdd:PRK08276 90 S----AALA---------DTAAELAAELPAGVPllLVVAGPVPGFR-----SYEEALAAQPDTPIADETagADML---YS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 277 SGTTGNPKGAM--LSHKNIVSNSAGFMKVtedlmfpstqdvlisflpLAHMFERVVECVVLC-----HGARIGFFQGDIR 349
Cdd:PRK08276 149 SGTTGRPKGIKrpLPGLDPDEAPGMMLAL------------------LGFGMYGGPDSVYLSpaplyHTAPLRFGMSALA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 350 L-----LM---DDLKVLQ-------------PTifpvvprllnrMFDRifgqantpvkrwMLdfasKRKEAelrsgiVRN 408
Cdd:PRK08276 211 LggtvvVMekfDAEEALAlieryrvthsqlvPT-----------MFVR------------ML----KLPEE------VRA 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 409 --DSfwdkiifhkvqASLggkvRLMVTGAAPVSPTVLtflRAAL---GCQFYEGYGQTEctaGCSLTI--PGDWTA--GH 479
Cdd:PRK08276 258 ryDV-----------SSL----RVAIHAAAPCPVEVK---RAMIdwwGPIIHEYYASSE---GGGVTVitSEDWLAhpGS 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 480 VGAPMPCNhVKLVDvEEMNYFASKGEGEVCIK-GSNVFQgYLKDDEKTAEALDKDGWLHTGDIGkWL-PNGTLKIIDRKK 557
Cdd:PRK08276 317 VGKAVLGE-VRILD-EDGNELPPGEIGTVYFEmDGYPFE-YHNDPEKTAAARNPHGWVTVGDVG-YLdEDGYLYLTDRKS 392
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1270536209 558 HIFkLAQGEYIAPEKIENVYTRSEPVVQVFVHGeslqaflvgivVPDPD 606
Cdd:PRK08276 393 DMI-ISGGVNIYPQEIENLLVTHPKVADVAVFG-----------VPDEE 429
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
119-291 |
5.31e-09 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 59.14 E-value: 5.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 119 EWISYKEVAERAEYVGSALLHRGFKPSPDQFvgIFAQNRPEWTIVELGCYTYSMVAVPLYDTLGAEAITYIINKADLSVV 198
Cdd:PRK04319 72 EKYTYKELKELSNKFANVLKELGVEKGDRVF--IFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 199 FCdSPEkaklLLSNVEKGETPVLRTIVLMNpfdnDLVERGKKCgvelVSLKDIEEEGKANREKPkPPKPDDLAVVCFTSG 278
Cdd:PRK04319 150 IT-TPA----LLERKPADDLPSLKHVLLVG----EDVEEGPGT----LDFNALMEQASDEFDIE-WTDREDGAILHYTSG 215
|
170
....*....|...
gi 1270536209 279 TTGNPKGAMLSHK 291
Cdd:PRK04319 216 STGKPKGVLHVHN 228
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
101-609 |
6.04e-09 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 58.88 E-value: 6.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 101 RVSNNGPCLGHRkpNQPYEWISY-KEVAERAEYVGSalLHRGFKPSpdqFVGIFAQNRPEWTIVELGCYTYSMVAVPLYD 179
Cdd:PRK13388 12 RAGDDTIAVRYG--DRTWTWREVlAEAAARAAALIA--LADPDRPL---HVGVLLGNTPEMLFWLAAAALGGYVLVGLNT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 180 TLGAEAITYIINKADLSVVFCDSPEKAklLLSNVEKGETPVLRTivlMNPFDNDLVERgkkcgvelvslkdieeegkANR 259
Cdd:PRK13388 85 TRRGAALAADIRRADCQLLVTDAEHRP--LLDGLDLPGVRVLDV---DTPAYAELVAA-------------------AGA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 260 EKP-KPPKPDDLAVVCFTSGTTGNPKGAMLSHKNIV----SNSAGFMKVTEDLMFPStqdvlisfLPLAHMfERVVE--C 332
Cdd:PRK13388 141 LTPhREVDAMDPFMLIFTSGTTGAPKAVRCSHGRLAfagrALTERFGLTRDDVCYVS--------MPLFHS-NAVMAgwA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 333 VVLCHGARI---------GFfqgdirllMDDLKVLQPTIFPVVPRLL-------NRMFDrifgqANTPVKRWMLDFASKR 396
Cdd:PRK13388 212 PAVASGAAValpakfsasGF--------LDDVRRYGATYFNYVGKPLayilatpERPDD-----ADNPLRVAFGNEASPR 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 397 KEAElrsgivrndsfwdkiifhkvqaslggkvrlmvtgaapvsptvltFLRAaLGCQFYEGYGQTEctAGCSLTIPGDWT 476
Cdd:PRK13388 279 DIAE--------------------------------------------FSRR-FGCQVEDGYGSSE--GAVIVVREPGTP 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 477 AGHVGAPMPcnHVKLVDVEEMN-----YFASKGE--------GE-VCIKGSNVFQGYLKDDEKTAEALdKDGWLHTGDIG 542
Cdd:PRK13388 312 PGSIGRGAP--GVAIYNPETLTecavaRFDAHGAllnadeaiGElVNTAGAGFFEGYYNNPEATAERM-RHGMYWSGDLA 388
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 543 KWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENVYTRSEPVVQVFVHGeslqaflvgivVPDP---DNVM 609
Cdd:PRK13388 389 YRDADGWIYFAGRTADWMRV-DGENLSAAPIERILLRHPAINRVAVYA-----------VPDErvgDQVM 446
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
429-609 |
7.85e-09 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 58.85 E-value: 7.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 429 RLMVTGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCSLTIPGDWTAGHV-GAPM-PCNHVKLVDvEEMNYFASKGEG 506
Cdd:PRK10946 303 KLLQVGGARLSETLARRIPAELGCQLQQVFGMAEGLVNYTRLDDSDERIFTTqGRPMsPDDEVWVAD-ADGNPLPQGEVG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 507 EVCIKGSNVFQGYLKDDEKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHifklaQ----GEYIAPEKIENVYTRsep 582
Cdd:PRK10946 382 RLMTRGPYTFRGYYKSPQHNASAFDANGFYCSGDLVSIDPDGYITVVGREKD-----QinrgGEKIAAEEIENLLLR--- 453
|
170 180
....*....|....*....|....*..
gi 1270536209 583 vvqvfvHGESLQAFLVGIvvpdPDNVM 609
Cdd:PRK10946 454 ------HPAVIHAALVSM----EDELM 470
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
119-606 |
8.59e-09 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 58.48 E-value: 8.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 119 EWISYKEVAERAEYVGSALLHRGFKPSpdQFVGIFAQNRPEWTIVelgcyTYSMVAVPLYDTlgaeAITYIINKADLSVV 198
Cdd:PRK13390 23 EQVSYRQLDDDSAALARVLYDAGLRTG--DVVALLSDNSPEALVV-----LWAALRSGLYIT----AINHHLTAPEADYI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 199 FCDSPEkaklllsnvekgetpvlRTIVLMNPFDNDLVERGKKCGVELVSLKDIE-----EEGKANREKPKPPKPDDlAVV 273
Cdd:PRK13390 92 VGDSGA-----------------RVLVASAALDGLAAKVGADLPLRLSFGGEIDgfgsfEAALAGAGPRLTEQPCG-AVM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 274 CFTSGTTGNPKGAM--LSHKN-------IVSNSAGFMKVTEdlmfpstQDVLISFLPLAH--------MFERVVECVVLC 336
Cdd:PRK13390 154 LYSSGTTGFPKGIQpdLPGRDvdapgdpIVAIARAFYDISE-------SDIYYSSAPIYHaaplrwcsMVHALGGTVVLA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 337 HgarigffQGDIRLLMDDLKVLQPTIFPVVPRLLNRMFdrifgqantpvkrwmldfaskRKEAELRSgivRNDSfwdkii 416
Cdd:PRK13390 227 K-------RFDAQATLGHVERYRITVTQMVPTMFVRLL---------------------KLDADVRT---RYDV------ 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 417 fhkvqaslgGKVRLMVTGAAPVSPTVLTFLRAALGCQFYEGYGQTEcTAGCSLTIPGDWTA--GHVGAPMpCNHVKLVDv 494
Cdd:PRK13390 270 ---------SSLRAVIHAAAPCPVDVKHAMIDWLGPIVYEYYSSTE-AHGMTFIDSPDWLAhpGSVGRSV-LGDLHICD- 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 495 EEMNYFASKGEGEVCIKGSNVFQGYLKDDEKTAEALDKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEK 572
Cdd:PRK13390 338 DDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAAAQHPAHpfWTTVGDLGSVDEDGYLYLADRKSFMI-ISGGVNIYPQE 416
|
490 500 510
....*....|....*....|....*....|....
gi 1270536209 573 IENVYTRSEPVVQVFVHGeslqaflvgivVPDPD 606
Cdd:PRK13390 417 TENALTMHPAVHDVAVIG-----------VPDPE 439
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
275-592 |
1.04e-08 |
|
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: 57.42 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 275 FTSGTTGNPKGAMLSHKNIvsnsAGFMKVTEDLMFPSTQDVLISFLPLAH-MFERVVECVVLCHGARIGFFQGDIRLLMD 353
Cdd:cd17633 7 FTSGTTGLPKAYYRSERSW----IESFVCNEDLFNISGEDAILAPGPLSHsLFLYGAISALYLGGTFIGQRKFNPKSWIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 354 DLKVLQPTIFPVVPRLLnrmfdrifgqantpvkrwmldfaskrkEAELRSGivRNDSfwdkiifhkvqaslggKVRLMVT 433
Cdd:cd17633 83 KINQYNATVIYLVPTML---------------------------QALARTL--EPES----------------KIKSIFS 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 434 GAAPVSPTVLTFLRAAL-GCQFYEGYGQTECTAGCSLTIPGDWTAGHVGAPMPCnhvklVDVEEMNYfASKGEGEVCIKG 512
Cdd:cd17633 118 SGQKLFESTKKKLKNIFpKANLIEFYGTSELSFITYNFNQESRPPNSVGRPFPN-----VEIEIRNA-DGGEIGKIFVKS 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 513 SNVFQGYLKddektAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENVYTRSEPVVQVFVHGES 592
Cdd:cd17633 192 EMVFSGYVR-----GGFSNPDGWMSVGDIGYVDEEGYLYLVGRESDMI-IIGGINIFPTEIESVLKAIPGIEEAIVVGIP 265
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
121-604 |
1.56e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 58.25 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 121 ISYKEVAERAEYVGSALLHRGFkpSPDQFVGIfAQNRPEWTIVEL-------GCYtysmvaVPLYDTLGAEAITYIINKA 193
Cdd:PRK12467 3121 LSYAELNRRANRLAHRLIAIGV--GPDVLVGV-AVERSVEMIVALlavlkagGAY------VPLDPEYPRERLAYMIEDS 3191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 194 DLsvvfcdspekaKLLLSNVEkgetpvlrtivlmnpfdndLVER-GKKCGVELVSLKDIEEEGKANREKPKPPKPDDLAV 272
Cdd:PRK12467 3192 GV-----------KLLLTQAH-------------------LLEQlPAPAGDTALTLDRLDLNGYSENNPSTRVMGENLAY 3241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 273 VCFTSGTTGNPKGAMLSHKNIVSNsagfMKVTEDLMFPSTQDVLISFLPLAhmFERVVECV--VLCHGARIGFFQGDIRl 350
Cdd:PRK12467 3242 VIYTSGSTGKPKGVGVRHGALANH----LCWIAEAYELDANDRVLLFMSFS--FDGAQERFlwTLICGGCLVVRDNDLW- 3314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 351 lmddlkvlqptifpvvprllnrmfdrifgqanTPVKRWMLDFASKRKEAELRSGIVRndsfwDKIIFHKVQAslGGKVRL 430
Cdd:PRK12467 3315 --------------------------------DPEELWQAIHAHRISIACFPPAYLQ-----QFAEDAGGAD--CASLDI 3355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 431 MVTGAAPVSPTVLTFLRAALG-CQFYEGYGQTECTAGCSL-TIPGDWTAGHVGAPM--PCNHVKLVDVE-EMNYFASKGE 505
Cdd:PRK12467 3356 YVFGGEAVPPAAFEQVKRKLKpRGLTNGYGPTEAVVTVTLwKCGGDAVCEAPYAPIgrPVAGRSIYVLDgQLNPVPVGVA 3435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 506 GEVCIKGSNVFQGYLKDDEKTAEALDKD------GWLH-TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENVYT 578
Cdd:PRK12467 3436 GELYIGGVGLARGYHQRPSLTAERFVADpfsgsgGRLYrTGDLARYRADGVIEYLGRIDHQVKI-RGFRIELGEIEARLL 3514
|
490 500
....*....|....*....|....*...
gi 1270536209 579 RSEPVVQVFVHGESLQA--FLVGIVVPD 604
Cdd:PRK12467 3515 QHPSVREAVVLARDGAGgkQLVAYVVPA 3542
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
429-617 |
2.00e-08 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 57.40 E-value: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 429 RLMVTGAAPVSPTVLTFLRAALGCQFYEGYGQTEcTAGCSLTIPGDWTA--GHVGAPMPCNHVKLVDvEEMNYFASKGEG 506
Cdd:PRK12406 274 RHVIHAAAPCPADVKRAMIEWWGPVIYEYYGSTE-SGAVTFATSEDALShpGTVGKAAPGAELRFVD-EDGRPLPQGEIG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 507 EVC--IKGSNVFQgYLKDDEKTAEaLDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENVYTRSEPVV 584
Cdd:PRK12406 352 EIYsrIAGNPDFT-YHNKPEKRAE-IDRGGFITSGDVGYLDADGYLFLCDRKRDMV-ISGGVNIYPAEIEAVLHAVPGVH 428
|
170 180 190
....*....|....*....|....*....|....*.
gi 1270536209 585 QVFVHG---ESLQAFLVGIVVPDPDNVMNWAKKRKF 617
Cdd:PRK12406 429 DCAVFGipdAEFGEALMAVVEPQPGATLDEADIRAQ 464
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
121-310 |
7.81e-08 |
|
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: 55.57 E-value: 7.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 121 ISYKEVAERAEYVGSALLHRGFKPSpDQfVGIFAQNRPEWTIVELGCYTYSMVAVPLYDTLGAEAITYIINKADlsvvfc 200
Cdd:cd05968 92 LTYGELLYEVKRLANGLRALGVGKG-DR-VGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAE------ 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 201 dspekAKLLLSN---VEKGE----TPVLRTIVLMNP-FDNDLVERGKKCGVELVSLKDI--EEEGKANREKPKPPKPDDL 270
Cdd:cd05968 164 -----AKALITAdgfTRRGRevnlKEEADKACAQCPtVEKVVVVRHLGNDFTPAKGRDLsyDEEKETAGDGAERTESEDP 238
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1270536209 271 AVVCFTSGTTGNPKGAMLSHknivsnsAGF-MKVTEDLMFP 310
Cdd:cd05968 239 LMIIYTSGTTGKPKGTVHVH-------AGFpLKAAQDMYFQ 272
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
121-341 |
1.19e-07 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 54.88 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 121 ISYKEVAERAEYVGSALLHRGFKPSpdQFVGIFAQNRPE----WT-IVELGcytysmVAVPLYDT-LGAEAITYIINKAD 194
Cdd:PRK08279 63 ISYAELNARANRYAHWAAARGVGKG--DVVALLMENRPEylaaWLgLAKLG------AVVALLNTqQRGAVLAHSLNLVD 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 195 LSVVFCDsPEkaklLLSNVEKGETPVLRTIVLMNPFDNDLVERGkkcgvELVSLKD-IEEEGKANREKPKPPKPDDLAVV 273
Cdd:PRK08279 135 AKHLIVG-EE----LVEAFEEARADLARPPRLWVAGGDTLDDPE-----GYEDLAAaAAGAPTTNPASRSGVTAKDTAFY 204
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1270536209 274 CFTSGTTGNPKGAMLSHKNIVSNSAGF---MKVTEDlmfpstqDVLISFLPLAH-MFERVVECVVLCHGARI 341
Cdd:PRK08279 205 IYTSGTTGLPKAAVMSHMRWLKAMGGFgglLRLTPD-------DVLYCCLPLYHnTGGTVAWSSVLAAGATL 269
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
121-294 |
1.39e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 55.35 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 121 ISYKEVAERAEYVGSALLHRGFkpSPDQFVGIFAQNRPEWTIVELGCYTYSMVAVPLYDTLGAEAITYIINkadlsvvfc 200
Cdd:PRK12316 537 LDYAELNRRANRLAHALIERGV--GPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLE--------- 605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 201 DSpeKAKLLLSnvekgETPVLRTIvlmnPFDNdlvergkkcGVELVSLKDIEEEGKANREKPkpPK----PDDLAVVCFT 276
Cdd:PRK12316 606 DS--GVQLLLS-----QSHLGRKL----PLAA---------GVQVLDLDRPAAWLEGYSEEN--PGtelnPENLAYVIYT 663
|
170
....*....|....*...
gi 1270536209 277 SGTTGNPKGAMLSHKNIV 294
Cdd:PRK12316 664 SGSTGKPKGAGNRHRALS 681
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
268-576 |
6.91e-07 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 52.32 E-value: 6.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 268 DDLAVVCFTSGTTGNPKGAMLSHKNivsnsagFMKVTEDLMFPSTQ-------DVLISFLPLAHM--FERVVECvvLCHG 338
Cdd:PRK05857 169 EDPLAMIFTSGTTGEPKAVLLANRT-------FFAVPDILQKEGLNwvtwvvgETTYSPLPATHIggLWWILTC--LMHG 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 339 ARI---GFFQGDIRLLMDDLKVLQPTIfpvVPRLLNRMFdrifgqantpvkrwmldfaskrkeAELRSGIVRNDSfwdki 415
Cdd:PRK05857 240 GLCvtgGENTTSLLEILTTNAVATTCL---VPTLLSKLV------------------------SELKSANATVPS----- 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 416 ifhkvqaslggkVRLMVTGAAPVSPTVLTFLRAA--LGCQFYeGYGQTECTAGCSLTIPGDWT---AGHVGAPMPCNHVK 490
Cdd:PRK05857 288 ------------LRLVGYGGSRAIAADVRFIEATgvRTAQVY-GLSETGCTALCLPTDDGSIVkieAGAVGRPYPGVDVY 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 491 LVDVEEMNYFASKGE-----GEVCIKGSNVFQGYLKDDEKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQG 565
Cdd:PRK05857 355 LAATDGIGPTAPGAGpsasfGTLWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLLERREDGFFYIKGRSSEMI-ICGG 432
|
330
....*....|.
gi 1270536209 566 EYIAPEKIENV 576
Cdd:PRK05857 433 VNIAPDEVDRI 443
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
119-605 |
1.09e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 51.70 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 119 EWISYKEVAERAEYVGSALlhrGFKPSPDQFVGIFAQNRPEWTIVELGCYTYSMVAVPL-----YDTLgAEAITyiINKA 193
Cdd:PRK07638 25 RVLTYKDWFESVCKVANWL---NEKESKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLdikwkQDEL-KERLA--ISNA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 194 DLsvVFCDspekaKLLLSNVEKGETPVLrtivlmnpfDNDLVERgkkcgvelvslkDIEEEgkANREKPKPPKPDDLAVV 273
Cdd:PRK07638 99 DM--IVTE-----RYKLNDLPDEEGRVI---------EIDEWKR------------MIEKY--LPTYAPIENVQNAPFYM 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 274 CFTSGTTGNPKGAMLSHknivsnsagfmkvtedlmfpstQDVLISFLPLAHMFERVVECVVLCHGARIG--FFQGDIR-L 350
Cdd:PRK07638 149 GFTSGSTGKPKAFLRAQ----------------------QSWLHSFDCNVHDFHMKREDSVLIAGTLVHslFLYGAIStL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 351 LMDDLKVLQPTIFPvvprllNRMFDRIFGQANT-----PVkrwMLdfaskrkEAELRSGIVRNDSfwDKIIfhkvqaSLG 425
Cdd:PRK07638 207 YVGQTVHLMRKFIP------NQVLDKLETENISvmytvPT---ML-------ESLYKENRVIENK--MKII------SSG 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 426 GKvrlmvTGAAPVSPTVLTFLRAalgcQFYEGYGQTECTAGCSLTiPGDWTAGHVGAPMPCNHVKLVDVEEMNYFASKGE 505
Cdd:PRK07638 263 AK-----WEAEAKEKIKNIFPYA----KLYEFYGASELSFVTALV-DEESERRPNSVGRPFHNVQVRICNEAGEEVQKGE 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 506 -GEVCIKGSNVFQGYlKDDEKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENVYTRsepvv 584
Cdd:PRK07638 333 iGTVYVKSPQFFMGY-IIGGVLARELNADGWMTVRDVGYEDEEGFIYIVGREKNMI-LFGGINIFPEEIESVLHE----- 405
|
490 500
....*....|....*....|.
gi 1270536209 585 qvfvHGESLQAFLVGivVPDP 605
Cdd:PRK07638 406 ----HPAVDEIVVIG--VPDS 420
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
265-605 |
1.16e-06 |
|
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: 51.23 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 265 PKPDDLAVVCfTSGTTGNPKGAMLSHKNIVS---NSAGFMKVtEDLMFPSTQDV-----LISFLPLAHmfervvecvvLC 336
Cdd:cd05924 1 RSADDLYILY-TGGTTGMPKGVMWRQEDIFRmlmGGADFGTG-EFTPSEDAHKAaaaaaGTVMFPAPP----------LM 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 337 HGAR-----IGFFQGDiRLLMDDLKVLQPTIFPVVPR-LLNRMFdrIFGQAntpVKRWMLDfaskrkeaELRSGIVRNDS 410
Cdd:cd05924 69 HGTGswtafGGLLGGQ-TVVLPDDRFDPEEVWRTIEKhKVTSMT--IVGDA---MARPLID--------ALRDAGPYDLS 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 411 fwdkiifhkvqaSLggkvRLMVTGAAPVSPTVLT-FLRAALGCQFYEGYGQTECTAGCSLTIPGdwtAGHVGAPMPCNHV 489
Cdd:cd05924 135 ------------SL----FAISSGGALLSPEVKQgLLELVPNITLVDAFGSSETGFTGSGHSAG---SGPETGPFTRANP 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 490 KLVDVEEMNYFASKGEGEVCIKGSN--VFQGYLKDDEKTAEAL-DKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLAq 564
Cdd:cd05924 196 DTVVLDDDGRVVPPGSGGVGWIARRghIPLGYYGDEAKTAETFpEVDGvrYAVPGDRATVEADGTVTLLGRGSVCINTG- 274
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1270536209 565 GEYIAPEKIENVyTRSEPVVqvfvhgesLQAFLVGivVPDP 605
Cdd:cd05924 275 GEKVFPEEVEEA-LKSHPAV--------YDVLVVG--RPDE 304
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
264-606 |
1.73e-06 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 51.58 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 264 PPKPDDLAVVCFTSGTTGNPKGAMLSHKNIVsNSAGFMK-----VTEDLMF---PSTQDVLI--SFLPLahmfervvecv 333
Cdd:PRK10252 594 LSQPHHTAYIIFTSGSTGRPKGVMVGQTAIV-NRLLWMQnhyplTADDVVLqktPCSFDVSVweFFWPF----------- 661
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 334 vLChGARIGFFQGD-------IRLLMDDLKVlqpTIFPVVPRLLNrmfdrIFGQANTPVkrwmldfASKRKEAELRsgiv 406
Cdd:PRK10252 662 -IA-GAKLVMAEPEahrdplaMQQFFAEYGV---TTTHFVPSMLA-----AFVASLTPE-------GARQSCASLR---- 720
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 407 rndsfwdkiifhkvqaslggkvRLMVTGAApvsptvltfLRAALgCQFYEG---------YGQTECTAGCSLTiP--GDW 475
Cdd:PRK10252 721 ----------------------QVFCSGEA---------LPADL-CREWQQltgaplhnlYGPTEAAVDVSWY-PafGEE 767
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 476 TAGHVGAPMPC-----NHVKLVDVEEMNYFASKGEGEVCIKGSNVFQGYLKDDEKTAEALDKDGWL------HTGDIGKW 544
Cdd:PRK10252 768 LAAVRGSSVPIgypvwNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFApgermyRTGDVARW 847
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1270536209 545 LPNGTLKIIDRKKHIFKLaQGEYIAPEKIENVYTRSEPVVQVFVH-----------GESLQafLVGIVVPDPD 606
Cdd:PRK10252 848 LDDGAVEYLGRSDDQLKI-RGQRIELGEIDRAMQALPDVEQAVTHacvinqaaatgGDARQ--LVGYLVSQSG 917
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
270-603 |
2.86e-06 |
|
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: 50.16 E-value: 2.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 270 LAVVCFTSGTTGNPKGAMLSHKNIVSNSAGFMKVtedlmFPSTQDVLISFLPLAHMFERVVECVV-LCHGARIgffqgdi 348
Cdd:cd17654 120 LAYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSL-----FNITSEDILFLTSPLTFDPSVVEIFLsLSSGATL------- 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 349 rllmddlkVLQPTIFPVVPRLLNRMFDRIFG----QANTPVKRwmlDFASKRKEAELRSGIvrndsfwdkiifhkvqASL 424
Cdd:cd17654 188 --------LIVPTSVKVLPSKLADILFKRHRitvlQATPTLFR---RFGSQSIKSTVLSAT----------------SSL 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 425 ggkvRLMVTGAAP-VSPTVLTFLRAA-LGCQFYEGYGQTECTAGCSLTIPGDWTAG-HVGAPMPCNHVKLVDVEemnyfA 501
Cdd:cd17654 241 ----RVLALGGEPfPSLVILSSWRGKgNRTRIFNIYGITEVSCWALAYKVPEEDSPvQLGSPLLGTVIEVRDQN-----G 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 502 SKGEGEVCIKGSNVfQGYLKDDEKTAEALdkdgWLHTGDIGKwLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENVYTRSE 581
Cdd:cd17654 312 SEGTGQVFLGGLNR-VCILDDEVTVPKGT----MRATGDFVT-VKDGELFFLGRKDSQIKRR-GKRINLDLIQQVIESCL 384
|
330 340
....*....|....*....|..
gi 1270536209 582 PVVQVFVHGESLQAFLVGIVVP 603
Cdd:cd17654 385 GVESCAVTLSDQQRLIAFIVGE 406
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
122-598 |
5.12e-06 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 50.17 E-value: 5.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 122 SYKEVAERAEYVGSALLHRGFkpSPDQFVGIFAQNRPEWTIVELGCYTYSMVAVPLYDTLGAEAITYIINKADLSVVFCD 201
Cdd:PRK05691 3747 SYAELNRAANRLGHALRAAGV--GVDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGLPAQRLQRIIELSRTPVLVCS 3824
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 202 SP--EKAKLLLSNVEKGETPvlrtivlmnpfdndlvergkkcgvELVSLKDIEEEGKANREKPKPPKPDDLAVVCFTSGT 279
Cdd:PRK05691 3825 AAcrEQARALLDELGCANRP------------------------RLLVWEEVQAGEVASHNPGIYSGPDNLAYVIYTSGS 3880
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 280 TGNPKGAMLSHKNIVSNSAG---FMKVTEDLMFPST--QDVLIS---FLPlAHMFervvecvvlchGARIGFFQGDI--- 348
Cdd:PRK05691 3881 TGLPKGVMVEQRGMLNNQLSkvpYLALSEADVIAQTasQSFDISvwqFLA-APLF-----------GARVEIVPNAIahd 3948
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 349 -RLLMDDLKVLQPTIFPVVPRLLNRMF--DRIFGQAntpvKRWML--------DFASKRKEAELRSGIVRndsfwdkiif 417
Cdd:PRK05691 3949 pQGLLAHVQAQGITVLESVPSLIQGMLaeDRQALDG----LRWMLptgeamppELARQWLQRYPQIGLVN---------- 4014
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 418 hkvqaslggkvrlmVTGAAPVSPTVlTFLRAALgcqfyegygqtECTAGCSLTIpgdwtaghvGAPMPCNHVKLVDvEEM 497
Cdd:PRK05691 4015 --------------AYGPAECSDDV-AFFRVDL-----------ASTRGSYLPI---------GSPTDNNRLYLLD-EAL 4058
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 498 NYFASKGEGEVCIKGSNVFQGYLKDDEKTAEALDKDGW-------LHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAP 570
Cdd:PRK05691 4059 ELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPHPFgapgerlYRTGDLARRRSDGVLEYVGRIDHQVKI-RGYRIEL 4137
|
490 500 510
....*....|....*....|....*....|....
gi 1270536209 571 EKIENVYTRSEPV------VQVFVHGESLQAFLV 598
Cdd:PRK05691 4138 GEIEARLHEQAEVreaavaVQEGVNGKHLVGYLV 4171
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
261-295 |
2.20e-05 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 47.35 E-value: 2.20e-05
10 20 30
....*....|....*....|....*....|....*
gi 1270536209 261 KPKPPKPDDLAVVCFTSGTTGNPKGAMLSHKNIVS 295
Cdd:PRK07824 28 RVGEPIDDDVALVVATSGTTGTPKGAMLTAAALTA 62
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
268-599 |
2.41e-05 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 47.86 E-value: 2.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 268 DDLAVVCFTSGTTGNPKGAMLSHKNIVSNSAgFMKVTEDLmfpSTQDVLISFLPLAhmFE-RVVECVV-LCHGARIGFF- 344
Cdd:PRK05691 1273 DNLAYVIYTSGSTGQPKGVGNTHAALAERLQ-WMQATYAL---DDSDVLMQKAPIS--FDvSVWECFWpLITGCRLVLAg 1346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 345 ---QGDIRLLMDDLKVLQPTIFPVVPRLLNRMFDRIFGQANTPVKRwmLDFASKRKEAELRSgivrndsfwdkiifhKVQ 421
Cdd:PRK05691 1347 pgeHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLAAACTSLRR--LFSGGEALPAELRN---------------RVL 1409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 422 ASLggkvrlmvtgaapvsPTVltflraalgcQFYEGYGQTE---------CTAGCSLTIPgdwtaghVGAPMPCNHVKLV 492
Cdd:PRK05691 1410 QRL---------------PQV----------QLHNRYGPTEtainvthwqCQAEDGERSP-------IGRPLGNVLCRVL 1457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 493 DvEEMNYFASKGEGEVCIKGSNVFQGYLKDDEKTAE-----ALDKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLaQG 565
Cdd:PRK05691 1458 D-AELNLLPPGVAGELCIGGAGLARGYLGRPALTAErfvpdPLGEDGarLYRTGDRARWNADGALEYLGRLDQQVKL-RG 1535
|
330 340 350
....*....|....*....|....*....|....*.
gi 1270536209 566 EYIAPEKIENVYTRSEPVVQ--VFVHGESLQAFLVG 599
Cdd:PRK05691 1536 FRVEPEEIQARLLAQPGVAQaaVLVREGAAGAQLVG 1571
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
264-325 |
2.83e-05 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 47.29 E-value: 2.83e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1270536209 264 PPKPDDLAVVCFTSGTTGNPKGAMLSHKNIVSNSA--GFMKVTEDlmfpstqDVLISFLPLAHM 325
Cdd:cd05938 140 HVTIKSPALYIYTSGTTGLPKAARISHLRVLQCSGflSLCGVTAD-------DVIYITLPLYHS 196
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
262-324 |
1.30e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 45.32 E-value: 1.30e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1270536209 262 PKPPKPDDLAVVCFTSGTTGNPKGAMLSHKNIVSN----SAGFMKVTEDlmFPSTQDVLISFLPLAH 324
Cdd:PRK05850 154 ARPRDLPSTAYLQYTSGSTRTPAGVMVSHRNVIANfeqlMSDYFGDTGG--VPPPDTTVVSWLPFYH 218
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
121-605 |
2.32e-04 |
|
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: 44.49 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 121 ISYKEVAERAEYVGSALLHRGFKPSpdQFVGIFAQNRPEWTIVELGCYTYSMVAVPLYDTLGAEAI-TYIINKADLSVVF 199
Cdd:cd17634 85 ISYRELHREVCRFAGTLLDLGVKKG--DRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVaGRIIDSSSRLLIT 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 200 CDS---PEKAKLLLSNVEKG----ETPVLRTIVLmnpfDNDLVERGKKCGVELVSLKDIEEEgkANREKPKPPKPDDLAV 272
Cdd:cd17634 163 ADGgvrAGRSVPLKKNVDDAlnpnVTSVEHVIVL----KRTGSDIDWQEGRDLWWRDLIAKA--SPEHQPEAMNAEDPLF 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 273 VCFTSGTTGNPKGAMLSHKNIVSNSAGFMKVTEDLmfpSTQDVLISFLPLAHMFER--VVECVVLChGARIGFFQGdirl 350
Cdd:cd17634 237 ILYTSGTTGKPKGVLHTTGGYLVYAATTMKYVFDY---GPGDIYWCTADVGWVTGHsyLLYGPLAC-GATTLLYEG---- 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 351 lmddlKVLQPTifpvvPRLLNRMFDR----IFGQANTPVKRWMldfaskrkeAELRSGIVRNDsfwdkiifhkvQASLgg 426
Cdd:cd17634 309 -----VPNWPT-----PARMWQVVDKhgvnILYTAPTAIRALM---------AAGDDAIEGTD-----------RSSL-- 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 427 kvRLMVTGAAPVSPTVLTFLRAALG---CQFYEGYGQTECTAGCSLTIPG--DWTAGHVGAPMPCNHVKLVDvEEMNYFA 501
Cdd:cd17634 357 --RILGSVGEPINPEAYEWYWKKIGkekCPVVDTWWQTETGGFMITPLPGaiELKAGSATRPVFGVQPAVVD-NEGHPQP 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 502 SKGEGEVCIKGS--NVFQGYLKDDEKTAEALDK--DGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENVY 577
Cdd:cd17634 434 GGTEGNLVITDPwpGQTRTLFGDHERFEQTYFStfKGMYFSGDGARRDEDGYYWITGRSDDVINVA-GHRLGTAEIESVL 512
|
490 500
....*....|....*....|....*...
gi 1270536209 578 TrSEPVVQvfvhgeslQAFLVGIvvPDP 605
Cdd:cd17634 513 V-AHPKVA--------EAAVVGI--PHA 529
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
122-324 |
2.42e-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: 44.34 E-value: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 122 SYKEVAERAEYVGSALLHRGFKpSPDqFVGIFAQNRPEWTIVELGCYTYSMVAVPLYDTLGAEAITYIINKAdlsvvfcd 201
Cdd:cd05939 5 TFRELNEYSNKVANFFQAQGYR-SGD-VVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVS-------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270536209 202 speKAKLLLSNvekgetpvlrtivLMNPFdndlvergkkcgvelvsLKDIEEEgkanrekpkPPKPDDL---AVVCF--T 276
Cdd:cd05939 75 ---KAKALIFN-------------LLDPL-----------------LTQSSTE---------PPSQDDVnfrDKLFYiyT 112
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1270536209 277 SGTTGNPKGAMLSHKNIVSNSAGFMKVTEdlMFPStqDVLISFLPLAH 324
Cdd:cd05939 113 SGTTGLPKAAVIVHSRYYRIAAGAYYAFG--MRPE--DVVYDCLPLYH 156
|
|
| |
