|
Name |
Accession |
Description |
Interval |
E-value |
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
95-685 |
0e+00 |
|
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: 809.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 95 SHYHYNSFDQLTDIMHEIGRGLVKIGLKPNDddKLHLYAATSHKWMKMFLGAQSQGIPVVTAYDTLGEKGLIHSLVQTGS 174
Cdd:cd17639 1 GEYKYMSYAEVWERVLNFGRGLVELGLKPGD--KVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETEC 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 175 KAIFTDNSllpslikpvqaaqdvkyiihfdsissedrrqsgkiyqsahdainrikevrpdiktfsfddilklgkescnei 254
Cdd:cd17639 79 SAIFTDGK------------------------------------------------------------------------ 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 255 dvhppgKDDLCCIMYTSGSTGEPKGVVLKHSNVVAGVGGASLNVLKFVGNTDRVICFLPLAHIFELVFELLSFYWGACIG 334
Cdd:cd17639 87 ------PDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRVPELLGPDDRYLAYLPLAHIFELAAENVCLYRGGTIG 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 335 YATVKTLTSSSVRNCQGDLQEFKPTIMVGVAAVWETVRKGILNQIDNLPFLTKKIFWTAYNTKLNMQRlHIPGGGALGNL 414
Cdd:cd17639 161 YGSPRTLTDKSKRGCKGDLTEFKPTLMVGVPAIWDTIRKGVLAKLNPMGGLKRTLFWTAYQSKLKALK-EGPGTPLLDEL 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 415 VFKKIRTATGGQLRYLLNGGSPISRDAQEFITNLICPMLIGYGLTETCASTTILDPANFELGVAGDLTGCVTVKLVDVEE 494
Cdd:cd17639 240 VFKKVRAALGGRLRYMLSGGAPLSADTQEFLNIVLCPVIQGYGLTETCAGGTVQDPGDLETGRVGPPLPCCEIKLVDWEE 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 495 LGY--FAKNNQGEVWITGANVTPEYYKNEEETSQALTSDGWFKTGDIGEWEANGHLKIIDRKKNLVKTMNGEYIALEKLE 572
Cdd:cd17639 320 GGYstDKPPPRGEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQNGEYIALEKLE 399
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 573 SVYRSNEYVANICVYADQSKTKPVGIIVPNHAPLTKLAKKLGimeqkDSSINIENYLEDAKLIKAVYSDLLKTGKDQGLV 652
Cdd:cd17639 400 SIYRSNPLVNNICVYADPDKSYPVAIVVPNEKHLTKLAEKHG-----VINSEWEELCEDKKLQKAVLKSLAETARAAGLE 474
|
570 580 590
....*....|....*....|....*....|...
gi 398366229 653 GIELLAGIVFFDGEWTPQNGFVTSAQKLKRKDI 685
Cdd:cd17639 475 KFEIPQGVVLLDEEWTPENGLVTAAQKLKRKEI 507
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
97-698 |
1.47e-154 |
|
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: 458.60 E-value: 1.47e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 97 YHYNSFDQLTDIMHEIGRGLVKIGLKPNDDDKLHLYAATSHKWMKMFLGAQSQGIPVVTAYDTLGEKGLIHSLVQTGSKA 176
Cdd:cd05927 3 YEWISYKEVAERADNIGSALRSLGGKPAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 177 IFTDnsllpslikpvqaaqdvkyiihfdsissedrrqsgkiyqsahdainrikevrPDIKTFSFDDILKLGKEscNEIDV 256
Cdd:cd05927 83 VFCD----------------------------------------------------AGVKVYSLEEFEKLGKK--NKVPP 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 257 HPPGKDDLCCIMYTSGSTGEPKGVVLKHSNVVAGVGGA--SLNVLKFVGNTDRVICFLPLAHIFELVFELLSFYWGACIG 334
Cdd:cd05927 109 PPPKPEDLATICYTSGTTGNPKGVMLTHGNIVSNVAGVfkILEILNKINPTDVYISYLPLAHIFERVVEALFLYHGAKIG 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 335 YatvktlTSSSVRNCQGDLQEFKPTIMVGVAAVWETVRKGILNQIDNLPFLTKKIFWTAYNTKLN-MQRLHIPGGGALGN 413
Cdd:cd05927 189 F------YSGDIRLLLDDIKALKPTVFPGVPRVLNRIYDKIFNKVQAKGPLKRKLFNFALNYKLAeLRSGVVRASPFWDK 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 414 LVFKKIRTATGGQLRYLLNGGSPISRDAQEFI-TNLICPMLIGYGLTETCASTTILDPANFELGVAGDLTGCVTVKLVDV 492
Cdd:cd05927 263 LVFNKIKQALGGNVRLMLTGSAPLSPEVLEFLrVALGCPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAEVKLVDV 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 493 EELGYFAK--NNQGEVWITGANVTPEYYKNEEETSQALTSDGWFKTGDIGEWEANGHLKIIDRKKNLVKTMNGEYIALEK 570
Cdd:cd05927 343 PEMNYDAKdpNPRGEVCIRGPNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLSQGEYVAPEK 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 571 LESVYRSNEYVANICVYADQSKTKPVGIIVPNHAPLTKLAKklgimEQKDSSINIENYLEDAKLIKAVYSDLLKTGKDQG 650
Cdd:cd05927 423 IENIYARSPFVAQIFVYGDSLKSFLVAIVVPDPDVLKEWAA-----SKGGGTGSFEELCKNPEVKKAILEDLVRLGKENG 497
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 398366229 651 LVGIELLAGIVFFDGEWTPQNGFVTSAQKLKRKDILNAVKDKVDAVYS 698
Cdd:cd05927 498 LKGFEQVKAIHLEPEPFSVENGLLTPTFKLKRPQLKKYYKKQIDEMYK 545
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
21-698 |
8.27e-137 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 417.98 E-value: 8.27e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 21 RRNYqcREKPLVRPPNTKCSTVYEFVLECFQKNKNSNAMGWRdvKEIHEESKSvmkKVDGKetSVEKkwmyYELSHYHYN 100
Cdd:PLN02387 41 IRNA--RFPELVETPWEGATTLAALFEQSCKKYSDKRLLGTR--KLISREFET---SSDGR--KFEK----LHLGEYEWI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 101 SFDQLTDIMHEIGRGLVKIGlkPNDDDKLHLYAATSHKWMKMFLGAQSQGIPVVTAYDTLGEKGLIHSLVQTGSKAIFTD 180
Cdd:PLN02387 108 TYGQVFERVCNFASGLVALG--HNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICD 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 181 NSLLPSLIKPVQAAQDVKYIIHFDSISSEDRrqsgkiyQSAHDAINrikevrpdIKTFSFDDILKLGKEscNEIDVHPPG 260
Cdd:PLN02387 186 SKQLKKLIDISSQLETVKRVIYMDDEGVDSD-------SSLSGSSN--------WTVSSFSEVEKLGKE--NPVDPDLPS 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 261 KDDLCCIMYTSGSTGEPKGVVLKHSNVVAGVGGASLNVLKfVGNTDRVICFLPLAHIFELVFELLSFYWGACIGYATVKT 340
Cdd:PLN02387 249 PNDIAVIMYTSGSTGLPKGVMMTHGNIVATVAGVMTVVPK-LGKNDVYLAYLPLAHILELAAESVMAAVGAAIGYGSPLT 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 341 LTSSS---VRNCQGDLQEFKPTIMVGVAAVWETVRKGILNQIDNLPFLTKKIFWTAYNTKLNMqrlhIPGG--GALG--- 412
Cdd:PLN02387 328 LTDTSnkiKKGTKGDASALKPTLMTAVPAILDRVRDGVRKKVDAKGGLAKKLFDIAYKRRLAA----IEGSwfGAWGlek 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 413 ----NLVFKKIRTATGGQLRYLLNGGSPISRDAQEFITnlIC---PMLIGYGLTETCASTTILDPANFELGVAGDLTGCV 485
Cdd:PLN02387 404 llwdALVFKKIRAVLGGRIRFMLSGGAPLSGDTQRFIN--IClgaPIGQGYGLTETCAGATFSEWDDTSVGRVGPPLPCC 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 486 TVKLVDVEELGYFAKNN---QGEVWITGANVTPEYYKNEEETSQALTSDG----WFKTGDIGEWEANGHLKIIDRKKNLV 558
Cdd:PLN02387 482 YVKLVSWEEGGYLISDKpmpRGEIVIGGPSVTLGYFKNQEKTDEVYKVDErgmrWFYTGDIGQFHPDGCLEIIDRKKDIV 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 559 KTMNGEYIALEKLESVYRSNEYVANICVYADQSKTKPVGIIVPNHAPLTKLAKKLGIMEQkdssiNIENYLEDAKLIKAV 638
Cdd:PLN02387 562 KLQHGEYVSLGKVEAALSVSPYVDNIMVHADPFHSYCVALVVPSQQALEKWAKKAGIDYS-----NFAELCEKEEAVKEV 636
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 639 YSDLLKTGKDQGLVGIELLAGIVFFDGEWTPQNGFVTSAQKLKRKDILNAVKDKVDAVYS 698
Cdd:PLN02387 637 QQSLSKAAKAARLEKFEIPAKIKLLPEPWTPESGLVTAALKLKREQIRKKFKDDLKKLYE 696
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
101-700 |
1.38e-123 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 380.60 E-value: 1.38e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 101 SFDQLTDIMHEIGRGLVKIGLKPNDddKLHLYAATSHKWMKMFLGAQSQGIPVVTAYDTLGEKGLIHSLVQTGSKAIFTD 180
Cdd:COG1022 42 TWAEFAERVRALAAGLLALGVKPGD--RVAILSDNRPEWVIADLAILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 181 NSLLPSLIKPVQA-AQDVKYIIHFDSissedrrqsgkiyqsahdainriKEVRPDIKTFSFDDILKLGKESCNEIDV--- 256
Cdd:COG1022 120 DQEQLDKLLEVRDeLPSLRHIVVLDP-----------------------RGLRDDPRLLSLDELLALGREVADPAELear 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 257 -HPPGKDDLCCIMYTSGSTGEPKGVVLKHSNVVAGVggasLNVLKF--VGNTDRVICFLPLAHIFELVFELLSFYWGACI 333
Cdd:COG1022 177 rAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNA----RALLERlpLGPGDRTLSFLPLAHVFERTVSYYALAAGATV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 334 GYAtvktltsSSVRNCQGDLQEFKPTIMVGVAAVWETVRKGILNQIDNLPFLTKKIF----WTAYNTKLNMQRLHIPGGG 409
Cdd:COG1022 253 AFA-------ESPDTLAEDLREVKPTFMLAVPRVWEKVYAGIQAKAEEAGGLKRKLFrwalAVGRRYARARLAGKSPSLL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 410 -----ALGN-LVFKKIRTATGGQLRYLLNGGSPISRDAQEFITNLICPMLIGYGLTETCASTTILDPANFELGVAGDLTG 483
Cdd:COG1022 326 lrlkhALADkLVFSKLREALGGRLRFAVSGGAALGPELARFFRALGIPVLEGYGLTETSPVITVNRPGDNRIGTVGPPLP 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 484 CVTVKLVDveelgyfaknnQGEVWITGANVTPEYYKNEEETSQALTSDGWFKTGDIGEWEANGHLKIIDRKKNLVKTMNG 563
Cdd:COG1022 406 GVEVKIAE-----------DGEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELDEDGFLRITGRKKDLIVTSGG 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 564 EYIALEKLESVYRSNEYVANICVYADQSKTkPVGIIVPNHAPLTKLAKKLGImeqkdSSINIENYLEDAKLIKAVYSDLL 643
Cdd:COG1022 475 KNVAPQPIENALKASPLIEQAVVVGDGRPF-LAALIVPDFEALGEWAEENGL-----PYTSYAELAQDPEVRALIQEEVD 548
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 398366229 644 KTGKdqGLVGIELLAGIVFFDGEWTPQNGFVTSAQKLKRKDILNAVKDKVDAVYSSS 700
Cdd:COG1022 549 RANA--GLSRAEQIKRFRLLPKEFTIENGELTPTLKLKRKVILEKYADLIEALYAGA 603
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
41-685 |
2.22e-122 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 380.86 E-value: 2.22e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 41 TVYEFVLECFQKNKNSNAMGWRDVKEIheeSKSVMKKVDGKEtsveKKWMYYELSHYHYNSFDQLTDIMHEIGRGLVKIG 120
Cdd:PTZ00216 70 NFLQRLERICKERGDRRALAYRPVERV---EKEVVKDADGKE----RTMEVTHFNETRYITYAELWERIVNFGRGLAELG 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 121 LKPNDddKLHLYAATSHKWMKMFLGAQSQGIPVVTAYDTLGEKGLIHSLVQTGSKAIFTDNSLLPSLIKPVQ--AAQDVK 198
Cdd:PTZ00216 143 LTKGS--NVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAIVCNGKNVPNLLRLMKsgGMPNTT 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 199 yIIHFDSISSEDRRQSGKIYqsahdainrikevrpdiktfSFDDILKLGKESCNEIDVHPPG-KDDLCCIMYTSGSTGEP 277
Cdd:PTZ00216 221 -IIYLDSLPASVDTEGCRLV--------------------AWTDVVAKGHSAGSHHPLNIPEnNDDLALIMYTSGTTGDP 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 278 KGVVLKHSNVVAGVGGASLNVLKFVG--NTDRVIC-FLPLAHIFELVFELLSFYWGACIGYATVKTLTSSSVRNCqGDLQ 354
Cdd:PTZ00216 280 KGVMHTHGSLTAGILALEDRLNDLIGppEEDETYCsYLPLAHIMEFGVTNIFLARGALIGFGSPRTLTDTFARPH-GDLT 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 355 EFKPTIMVGVAAVWETVRKGILNQIDNLPFLTKKIFWTAYNTKLNmqrlhipgggALGN---------LVFKKIRTATGG 425
Cdd:PTZ00216 359 EFRPVFLIGVPRIFDTIKKAVEAKLPPVGSLKRRVFDHAYQSRLR----------ALKEgkdtpywneKVFSAPRAVLGG 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 426 QLRYLLNGGSPISRDAQEFITNLICPMLIGYGLTETCASTTILDPANFELGVAGDLTGCVTVKLVDVEELGYFAKNN-QG 504
Cdd:PTZ00216 429 RVRAMLSGGGPLSAATQEFVNVVFGMVIQGWGLTETVCCGGIQRTGDLEPNAVGQLLKGVEMKLLDTEEYKHTDTPEpRG 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 505 EVWITGANVTPEYYKNEEETSQALTSDGWFKTGDIGEWEANGHLKIIDRKKNLVKTMNGEYIALEKLESVYRSNEYVAN- 583
Cdd:PTZ00216 509 EILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVKALAKNCLGEYIALEALEALYGQNELVVPn 588
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 584 -ICVYADQSKTKPVGIIVPNHAPLTKLAKKLGImEQKDSSInienyLEDAKLIKAVYSDLLKTGKDQGLVGIELLAGIVF 662
Cdd:PTZ00216 589 gVCVLVHPARSYICALVLTDEAKAMAFAKEHGI-EGEYPAI-----LKDPEFQKKATESLQETARAAGRKSFEIVRHVRV 662
|
650 660
....*....|....*....|...
gi 398366229 663 FDGEWTPQNGFVTSAQKLKRKDI 685
Cdd:PTZ00216 663 LSDEWTPENGVLTAAMKLKRRVI 685
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
34-697 |
1.36e-103 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 330.62 E-value: 1.36e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 34 PPNTKCSTVYEFVLECFQKNKNSNAMGWRDVkeiheesksvmkkVDGKetsvekkwmyyeLSHYHYNSFDQLTDIMHEIG 113
Cdd:PLN02430 36 PIDSDITTAWDIFSKSVEKYPDNKMLGWRRI-------------VDGK------------VGPYMWKTYKEVYEEVLQIG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 114 RGLVKIGLKPNDddKLHLYAATSHKWMKMFLGAQSQGIPVVTAYDTLGEKGLIHSLVQTGSKAIFTDNSLLPSLIKP-VQ 192
Cdd:PLN02430 91 SALRASGAEPGS--RVGIYGSNCPQWIVAMEACAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVFVQDKKIKELLEPdCK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 193 AAQDVKYIIHFDSISSEDRRQSGKIyqsahdainrikevrpDIKTFSFDDILKLGKEscNEIDVHPPGKDDLCCIMYTSG 272
Cdd:PLN02430 169 SAKRLKAIVSFTSVTEEESDKASQI----------------GVKTYSWIDFLHMGKE--NPSETNPPKPLDICTIMYTSG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 273 STGEPKGVVLKHSNVVAGVGGASLNVLKF---VGNTDRVICFLPLAHIFELVFELLSFYWGACIGYatvktlTSSSVRNC 349
Cdd:PLN02430 231 TSGDPKGVVLTHEAVATFVRGVDLFMEQFedkMTHDDVYLSFLPLAHILDRMIEEYFFRKGASVGY------YHGDLNAL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 350 QGDLQEFKPTIMVGVAAVWETVRKGILNQIDNLPFLTKKIFWTAYNTKL-NMQR--LHIPGGGALGNLVFKKIRTATGGQ 426
Cdd:PLN02430 305 RDDLMELKPTLLAGVPRVFERIHEGIQKALQELNPRRRLIFNALYKYKLaWMNRgySHKKASPMADFLAFRKVKAKLGGR 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 427 LRYLLNGGSPISRDAQEFITNLICPMLI-GYGLTETCASTTILDPANFE-LGVAGDLTGCVTVKLVDVEELGY--FAKNN 502
Cdd:PLN02430 385 LRLLISGGAPLSTEIEEFLRVTSCAFVVqGYGLTETLGPTTLGFPDEMCmLGTVGAPAVYNELRLEEVPEMGYdpLGEPP 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 503 QGEVWITGANVTPEYYKNEEETSQALtSDGWFKTGDIGEWEANGHLKIIDRKKNLVKTMNGEYIALEKLESVYRSNEYVA 582
Cdd:PLN02430 465 RGEICVRGKCLFSGYYKNPELTEEVM-KDGWFHTGDIGEILPNGVLKIIDRKKNLIKLSQGEYVALEYLENVYGQNPIVE 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 583 NICVYADQSKTKPVGIIVPNHAPLTKLAKKLGIMEqkdssiNIENYLEDAKLIKAVYSDLLKTGKDQGLVGIELLAGIVF 662
Cdd:PLN02430 544 DIWVYGDSFKSMLVAVVVPNEENTNKWAKDNGFTG------SFEELCSLPELKEHILSELKSTAEKNKLRGFEYIKGVIL 617
|
650 660 670
....*....|....*....|....*....|....*....
gi 398366229 663 ----FDGEwtpqNGFVTSAQKLKRKDILNAVKDKVDAVY 697
Cdd:PLN02430 618 etkpFDVE----RDLVTATLKKRRNNLLKYYQVEIDEMY 652
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
1-698 |
9.04e-100 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 320.64 E-value: 9.04e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 1 MVAQYTVPVGK---AANEHETAP--RRNYQCREKPLVRPpnTKCSTVYEFVLECFQKNKNSNAMGWRDVkeiheesksvm 75
Cdd:PLN02861 1 MAETYTVKVEEsrpATGGKPSAGpvYRSIYAKDGLLDLP--ADIDSPWQFFSDAVKKYPNNQMLGRRQV----------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 76 kkVDGKetSVEKKWMYYELSHyhynsfdqltDIMHEIGRGLVKIGLKPNDddKLHLYAATSHKWMKMFLGAQSQGIPVVT 155
Cdd:PLN02861 68 --TDSK--VGPYVWLTYKEVY----------DAAIRIGSAIRSRGVNPGD--RCGIYGSNCPEWIIAMEACNSQGITYVP 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 156 AYDTLGEKGLIHSLVQTGSKAIFTDNSLLPSLIKPV-QAAQDVKYIIHFDSISSEDRRQSGKIYQSAhdainrikevrpd 234
Cdd:PLN02861 132 LYDTLGANAVEFIINHAEVSIAFVQESKISSILSCLpKCSSNLKTIVSFGDVSSEQKEEAEELGVSC------------- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 235 iktFSFDDILKLGKESCNeidVHPPGKDDLCCIMYTSGSTGEPKGVVLKHSNVVAGVggasLNVLKFVGNTDRVI----- 309
Cdd:PLN02861 199 ---FSWEEFSLMGSLDCE---LPPKQKTDICTIMYTSGTTGEPKGVILTNRAIIAEV----LSTDHLLKVTDRVAteeds 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 310 --CFLPLAHIFELVFELLSFYWGACIGYatvktlTSSSVRNCQGDLQEFKPTIMVGVAAVWETVRKGILNQIDNLPFLTK 387
Cdd:PLN02861 269 yfSYLPLAHVYDQVIETYCISKGASIGF------WQGDIRYLMEDVQALKPTIFCGVPRVYDRIYTGIMQKISSGGMLRK 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 388 KIFWTAYNTKLNMQRLHIPGGGA---LGNLVFKKIRTATGGQLRYLLNGGSPISRDAQEFITNLICPMLI-GYGLTETCA 463
Cdd:PLN02861 343 KLFDFAYNYKLGNLRKGLKQEEAsprLDRLVFDKIKEGLGGRVRLLLSGAAPLPRHVEEFLRVTSCSVLSqGYGLTESCG 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 464 S--TTILDPANFeLGVAGDLTGCVTVKLVDVEELGYFAKNN--QGEVWITGANVTPEYYKNEEETSQALtSDGWFKTGDI 539
Cdd:PLN02861 423 GcfTSIANVFSM-VGTVGVPMTTIEARLESVPEMGYDALSDvpRGEICLRGNTLFSGYHKRQDLTEEVL-IDGWFHTGDI 500
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 540 GEWEANGHLKIIDRKKNLVKTMNGEYIALEKLESVYRSNEYVANICVYADQSKTKPVGIIVPNHAPLTKLAKklgimeQK 619
Cdd:PLN02861 501 GEWQPNGAMKIIDRKKNIFKLSQGEYVAVENLENTYSRCPLIASIWVYGNSFESFLVAVVVPDRQALEDWAA------NN 574
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398366229 620 DSSINIENYLEDAKLIKAVYSDLLKTGKDQGLVGIELLAGIVFFDGEWTPQNGFVTSAQKLKRKDILNAVKDKVDAVYS 698
Cdd:PLN02861 575 NKTGDFKSLCKNLKARKYILDELNSTGKKLQLRGFEMLKAIHLEPNPFDIERDLITPTFKLKRPQLLKYYKDCIDQLYS 653
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
61-682 |
1.66e-94 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 306.26 E-value: 1.66e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 61 WRDVKEIHEESKSVMKKVDGKETSVEKKWMYYelshyhynsfDQLTDIMHEIGRGLVKIGLKPNDddKLHLYAATSHKWM 140
Cdd:PLN02736 50 FVYAVETFRDYKYLGTRIRVDGTVGEYKWMTY----------GEAGTARTAIGSGLVQHGIPKGA--CVGLYFINRPEWL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 141 KMFLGAQSQGIPVVTAYDTLGEKGLI----HSLVQtgskAIFTDNSLLPSLIKPVQAAQDVKYII---HFDSISSEDRRQ 213
Cdd:PLN02736 118 IVDHACSAYSYVSVPLYDTLGPDAVKfivnHAEVA----AIFCVPQTLNTLLSCLSEIPSVRLIVvvgGADEPLPSLPSG 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 214 SGkiyqsahdainrikevrpdIKTFSFDDILKLGKESCNEIdvHPPGKDDLCCIMYTSGSTGEPKGVVLKHSNVVAGVGG 293
Cdd:PLN02736 194 TG-------------------VEIVTYSKLLAQGRSSPQPF--RPPKPEDVATICYTSGTTGTPKGVVLTHGNLIANVAG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 294 ASLNVLKFVGntDRVICFLPLAHIFELVFELLSFYWGACIGYatvktlTSSSVRNCQGDLQEFKPTIMVGVAAVWETVRK 373
Cdd:PLN02736 253 SSLSTKFYPS--DVHISYLPLAHIYERVNQIVMLHYGVAVGF------YQGDNLKLMDDLAALRPTIFCSVPRLYNRIYD 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 374 GILNQIDNLPFLTKKIFWTAYNTKLNMQRLHIPGGGALGNLVFKKIRTATGGQLRYLLNGGSPISRDAQEFITnlIC--- 450
Cdd:PLN02736 325 GITNAVKESGGLKERLFNAAYNAKKQALENGKNPSPMWDRLVFNKIKAKLGGRVRFMSSGASPLSPDVMEFLR--ICfgg 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 451 PMLIGYGLTETCASTTILDPANFELGVAGDLTGCVTVKLVDVEELGYFAKNN---QGEVWITGANVTPEYYKNEEETSQA 527
Cdd:PLN02736 403 RVLEGYGMTETSCVISGMDEGDNLSGHVGSPNPACEVKLVDVPEMNYTSEDQpypRGEICVRGPIIFKGYYKDEVQTREV 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 528 LTSDGWFKTGDIGEWEANGHLKIIDRKKNLVKTMNGEYIALEKLESVYRSNEYVANICVYADQSKTKPVGIIVPNHAPLT 607
Cdd:PLN02736 483 IDEDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLAQGEYIAPEKIENVYAKCKFVAQCFVYGDSLNSSLVAVVVVDPEVLK 562
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398366229 608 KLAKKLGIMEQkdssiNIENYLEDAKLIKAVYSDLLKTGKDQGLVGIELLAGIVFFDGEWTPQNGFVTSAQKLKR 682
Cdd:PLN02736 563 AWAASEGIKYE-----DLKQLCNDPRVRAAVLADMDAVGREAQLRGFEFAKAVTLVPEPFTVENGLLTPTFKVKR 632
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
101-685 |
6.06e-93 |
|
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: 296.04 E-value: 6.06e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 101 SFDQLTDIMHEIGRGLVKIGLKPndDDKLHLYAATSHKWMKMFLGAQSQGIPVVTAYDTLGEKGLIHSLVQTGSKAIFTD 180
Cdd:cd05907 7 TWAEFAEEVRALAKGLIALGVEP--GDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 181 Nsllpslikpvqaaqdvkyiihfdsissedrrqsgkiyqsahdainrikevrpdiktfsfddilklgkescneidvhppg 260
Cdd:cd05907 85 D------------------------------------------------------------------------------- 85
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 261 KDDLCCIMYTSGSTGEPKGVVLKHSNVVAGVGGASLNVLKfvGNTDRVICFLPLAHIFELVF-ELLSFYWGACIGYAtvk 339
Cdd:cd05907 86 PDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPA--TEGDRHLSFLPLAHVFERRAgLYVPLLAGARIYFA--- 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 340 tltsSSVRNCQGDLQEFKPTIMVGVAAVWETVRKGIlnQIDNLPFLTKKIFwtayntklnmqrlhipgggalgnlvfkki 419
Cdd:cd05907 161 ----SSAETLLDDLSEVRPTVFLAVPRVWEKVYAAI--KVKAVPGLKRKLF----------------------------- 205
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 420 RTATGGQLRYLLNGGSPISRDAQEFITNLICPMLIGYGLTETCASTTILDPANFELGVAGDLTGCVTVKLVDveelgyfa 499
Cdd:cd05907 206 DLAVGGRLRFAASGGAPLPAELLHFFRALGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVEVRIAD-------- 277
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 500 knnQGEVWITGANVTPEYYKNEEETSQALTSDGWFKTGDIGEWEANGHLKIIDRKKNLVKTMNGEYIALEKLESVYRSNE 579
Cdd:cd05907 278 ---DGEILVRGPNVMLGYYKNPEATAEALDADGWLHTGDLGEIDEDGFLHITGRKKDLIITSGGKNISPEPIENALKASP 354
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 580 YVANICVYADQsKTKPVGIIVPNHAPLTKLAKKLGIMEqkdssINIENYLEDAKLIKAVYSDLLKTGkdQGLVGIELLAG 659
Cdd:cd05907 355 LISQAVVIGDG-RPFLVALIVPDPEALEAWAEEHGIAY-----TDVAELAANPAVRAEIEAAVEAAN--ARLSRYEQIKK 426
|
570 580
....*....|....*....|....*.
gi 398366229 660 IVFFDGEWTPQNGFVTSAQKLKRKDI 685
Cdd:cd05907 427 FLLLPEPFTIENGELTPTLKLKRPVI 452
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
97-699 |
3.82e-88 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 290.00 E-value: 3.82e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 97 YHYNSFDQLTDIMHEIGRGLVKIGLKpnDDDKLHLYAATSHKWMKMFLGAQSQGIPVVTAYDTLGEKGLIHSLVQTGSKA 176
Cdd:PLN02614 77 YVWQTYQEVYDIVIKLGNSLRSVGVK--DEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSI 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 177 IFTDNSLLPSLIKPV-QAAQDVKYIIHFDSISSEDRRQSGKIyqsahdainrikevrpDIKTFSFDDILKLGKESCNEID 255
Cdd:PLN02614 155 VFVEEKKISELFKTCpNSTEYMKTVVSFGGVSREQKEEAETF----------------GLVIYAWDEFLKLGEGKQYDLP 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 256 VHPPgkDDLCCIMYTSGSTGEPKGVVLKHSNVVAGVGGaslnVLKFVGNT-------DRVICFLPLAHIFELVFELLSFY 328
Cdd:PLN02614 219 IKKK--SDICTIMYTSGTTGDPKGVMISNESIVTLIAG----VIRLLKSAnaaltvkDVYLSYLPLAHIFDRVIEECFIQ 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 329 WGACIGY--ATVKTLTSssvrncqgDLQEFKPTIMVGVAAVWETVRKGILNQIDNLPFLTKKIFWTAYNTKL-NMQR--L 403
Cdd:PLN02614 293 HGAAIGFwrGDVKLLIE--------DLGELKPTIFCAVPRVLDRVYSGLQKKLSDGGFLKKFVFDSAFSYKFgNMKKgqS 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 404 HIPGGGALGNLVFKKIRTATGGQLRYLLNGGSPISRDAQEFITNL-ICPMLIGYGLTETCASTTILDPANFE-LGVAGDL 481
Cdd:PLN02614 365 HVEASPLCDKLVFNKVKQGLGGNVRIILSGAAPLASHVESFLRVVaCCHVLQGYGLTESCAGTFVSLPDELDmLGTVGPP 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 482 TGCVTVKLVDVEELGY--FAKNNQGEVWITGANVTPEYYKNEEETSQALTsDGWFKTGDIGEWEANGHLKIIDRKKNLVK 559
Cdd:PLN02614 445 VPNVDIRLESVPEMEYdaLASTPRGEICIRGKTLFSGYYKREDLTKEVLI-DGWLHTGDVGEWQPNGSMKIIDRKKNIFK 523
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 560 TMNGEYIALEKLESVYRSNEYVANICVYADQSKTKPVGIIVPNHAPLTKLAKKLGIMEQKDSsinienYLEDAKLIKAVY 639
Cdd:PLN02614 524 LSQGEYVAVENIENIYGEVQAVDSVWVYGNSFESFLVAIANPNQQILERWAAENGVSGDYNA------LCQNEKAKEFIL 597
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398366229 640 SDLLKTGKDQGLVGIELLAGI----VFFDGEwtpqNGFVTSAQKLKRKDILNAVKDKVDAVYSS 699
Cdd:PLN02614 598 GELVKMAKEKKMKGFEIIKAIhldpVPFDME----RDLLTPTFKKKRPQLLKYYQSVIDEMYKT 657
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
101-560 |
4.61e-83 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 268.80 E-value: 4.61e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 101 SFDQLTDIMHEIGRGLVKIGLKPndDDKLHLYAATSHKWMKMFLGAQSQGIPVVTAYDTLGEKGLIHSLVQTGSKAIFTD 180
Cdd:pfam00501 23 TYRELDERANRLAAGLRALGVGK--GDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSGAKVLITD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 181 NSLLPSLIKPVQAAQDV---KYIIHFDSISSEDRRQSGKIYQSAHdainrikevrpdiktfsfddilklgkescnEIDVH 257
Cdd:pfam00501 101 DALKLEELLEALGKLEVvklVLVLDRDPVLKEEPLPEEAKPADVP------------------------------PPPPP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 258 PPGKDDLCCIMYTSGSTGEPKGVVLKHSNVVAGV-GGASLNVLKF-VGNTDRVICFLPLAHIFELVFELL-SFYWGACIG 334
Cdd:pfam00501 151 PPDPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVlSIKRVRPRGFgLGPDDRVLSTLPLFHDFGLSLGLLgPLLAGATVV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 335 YATVKTLTSssVRNCQGDLQEFKPTIMVGVAAVWETVRkgilnqidNLPFLTKKIFWTayntklnmqrlhipgggalgnl 414
Cdd:pfam00501 231 LPPGFPALD--PAALLELIERYKVTVLYGVPTLLNMLL--------EAGAPKRALLSS---------------------- 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 415 vfkkirtatggqLRYLLNGGSPISRDAQEFITN-LICPMLIGYGLTETCASTTI---LDPANFELGVAGDLTGCVTVKLV 490
Cdd:pfam00501 279 ------------LRLVLSGGAPLPPELARRFRElFGGALVNGYGLTETTGVVTTplpLDEDLRSLGSVGRPLPGTEVKIV 346
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 491 DVEELGYFAKNNQGEVWITGANVTPEYYKNEEETSQALTSDGWFKTGDIGEWEANGHLKIIDRKKNLVKT 560
Cdd:pfam00501 347 DDETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKL 416
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
262-682 |
2.41e-65 |
|
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: 223.39 E-value: 2.41e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 262 DDLCCIMYTSGSTGEPKGVVLKHSNVVAGVGGASLNVLKFVGntDRVICFLPLAHIFELVFELLSFYWGACIGYATVKTL 341
Cdd:cd17640 88 DDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQPG--DRFLSILPIWHSYERSAEYFIFACGCSQAYTSIRTL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 342 TSssvrncqgDLQEFKPTIMVGVAAVWETVRKGILNQIDNLPFLTKKIFWTAyntklnmqrlhipgggalgnlvfkkirt 421
Cdd:cd17640 166 KD--------DLKRVKPHYIVSVPRLWESLYSGIQKQVSKSSPIKQFLFLFF---------------------------- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 422 ATGGQLRYLLNGGSPISRDAQEFITNLICPMLIGYGLTETCASTTILDPANFELGVAGDLTGCVTVKLVDVEELGYFAKN 501
Cdd:cd17640 210 LSGGIFKFGISGGGALPPHVDTFFEAIGIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIVDPEGNVVLPPG 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 502 NQGEVWITGANVTPEYYKNEEETSQALTSDGWFKTGDIGEWEANGHLKIIDRKKNLVKTMNGEYIALEKLESVYRSNEYV 581
Cdd:cd17640 290 EKGIVWVRGPQVMKGYYKNPEATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSNGENVEPQPIEEALMRSPFI 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 582 ANICVYA-DQsktKPVG-IIVPNHAPLTKLAKKLGIMEQKDssinIENYLEDAKLIKAvYSDLLKT--GKDQGLVGIELL 657
Cdd:cd17640 370 EQIMVVGqDQ---KRLGaLIVPNFEELEKWAKESGVKLAND----RSQLLASKKVLKL-YKNEIKDeiSNRPGFKSFEQI 441
|
410 420
....*....|....*....|....*
gi 398366229 658 AGIVFFDGEWTPqNGFVTSAQKLKR 682
Cdd:cd17640 442 APFALLEEPFIE-NGEMTQTMKIKR 465
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
261-647 |
1.20e-60 |
|
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: 210.76 E-value: 1.20e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 261 KDDLCCIMYTSGSTGEPKGVVLKHSNVVAGVggASLNVLKFVGNTDRVICFLPLAHIFELVFE-LLSFYWGACIGYATvk 339
Cdd:cd05914 88 EDDVALINYTSGTTGNSKGVMLTYRNIVSNV--DGVKEVVLLGKGDKILSILPLHHIYPLTFTlLLPLLNGAHVVFLD-- 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 340 TLTSSSVRNcqgdLQEFKPTIMVGVAAVWETVRKGILnqiDNLPFLTKKIFWTAYNTKLNMQRLHipgggalgNLVFKKI 419
Cdd:cd05914 164 KIPSAKIIA----LAFAQVTPTLGVPVPLVIEKIFKM---DIIPKLTLKKFKFKLAKKINNRKIR--------KLAFKKV 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 420 RTATGGQLRYLLNGGSPISRDAQEFITNLICPMLIGYGLTETCASTTILDPANFELGVAGDLTGCVTVKLVDVEelgyfA 499
Cdd:cd05914 229 HEAFGGNIKEFVIGGAKINPDVEEFLRTIGFPYTIGYGMTETAPIISYSPPNRIRLGSAGKVIDGVEVRIDSPD-----P 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 500 KNNQGEVWITGANVTPEYYKNEEETSQALTSDGWFKTGDIGEWEANGHLKIIDRKKNLVKTMNGEYIALEKLESVYRSNE 579
Cdd:cd05914 304 ATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSSGKNIYPEEIEAKINNMP 383
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398366229 580 YVANICVYADQSKTKPVGIIVPNHAPLTKL---AKKLGIMEQKDSSINIE--NYLEDAKlIKAVYSDLLKTGK 647
Cdd:cd05914 384 FVLESLVVVQEKKLVALAYIDPDFLDVKALkqrNIIDAIKWEVRDKVNQKvpNYKKISK-VKIVKEEFEKTPK 455
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
240-692 |
4.87e-55 |
|
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: 196.54 E-value: 4.87e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 240 FDDILKLGKEscnEIDVHPPGKDDLCCIMYTSGSTGEPKGVVLKHSNVvAGVGGASLNVLKFVGNtDRVICFLPLAHIFE 319
Cdd:cd05932 118 WDDLIAQHPP---LEERPTRFPEQLATLIYTSGTTGQPKGVMLTFGSF-AWAAQAGIEHIGTEEN-DRMLSYLPLAHVTE 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 320 LVF-ELLSFYWGACIGYAtvktltsSSVRNCQGDLQEFKPTIMVGVAAVWETVRKGIlnqIDNLPfltkkifwtayNTKL 398
Cdd:cd05932 193 RVFvEGGSLYGGVLVAFA-------ESLDTFVEDVQRARPTLFFSVPRLWTKFQQGV---QDKIP-----------QQKL 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 399 NMQrLHIPgggALGNLVFKKIRTATG-GQLRYLLNGGSPISRDAQEFITNLICPMLIGYGLTETCASTTILDPANFELGV 477
Cdd:cd05932 252 NLL-LKIP---VVNSLVKRKVLKGLGlDQCRLAGCGSAPVPPALLEWYRSLGLNILEAYGMTENFAYSHLNYPGRDKIGT 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 478 AGDLTGCVTVKLVDveelgyfaknnQGEVWITGANVTPEYYKNEEETSQALTSDGWFKTGDIGEWEANGHLKIIDRKKNL 557
Cdd:cd05932 328 VGNAGPGVEVRISE-----------DGEILVRSPALMMGYYKDPEATAEAFTADGFLRTGDKGELDADGNLTITGRVKDI 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 558 VKTMNGEYIALEKLESVYRSNEYVANICVYAdQSKTKPVGIIVPNHAPltKLAKKLGIMEQKDSSINienyledaKLIKA 637
Cdd:cd05932 397 FKTSKGKYVAPAPIENKLAEHDRVEMVCVIG-SGLPAPLALVVLSEEA--RLRADAFARAELEASLR--------AHLAR 465
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 398366229 638 VYSDLLKTgkdqglvgiELLAGIVFFDGEWTPQNGFVTSAQKLKRkdilNAVKDK 692
Cdd:cd05932 466 VNSTLDSH---------EQLAGIVVVKDPWSIDNGILTPTLKIKR----NVLEKA 507
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
101-586 |
2.56e-52 |
|
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: 188.58 E-value: 2.56e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 101 SFDQLTDIMHEIGRGLVKIGLKPndDDKLHLYAATSHKWMKMFLGAQSQGIPVVTAYDTLGEKGLIHSLVQTGSKAIFTD 180
Cdd:cd05911 12 TYAQLRTLSRRLAAGLRKLGLKK--GDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 181 NSLLPSLIKPVQAAQDVKYIIHFDSisSEDRRQSGKIYQSAHDAINRIKEVRPDIKtfsfddilklgkescneidvhppG 260
Cdd:cd05911 90 PDGLEKVKEAAKELGPKDKIIVLDD--KPDGVLSIEDLLSPTLGEEDEDLPPPLKD-----------------------G 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 261 KDDLCCIMYTSGSTGEPKGVVLKHSNVVAGVGGASLNVLKFVGNTDRVICFLPLAHIFELVFELLSFYWGACIgYATVKT 340
Cdd:cd05911 145 KDDTAAILYSSGTTGLPKGVCLSHRNLIANLSQVQTFLYGNDGSNDVILGFLPLYHIYGLFTTLASLLNGATV-IIMPKF 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 341 LTSSSVRNCQgdlqEFKPTIMVGVAAvwetvrkgILNQIDNLPFLTKkifwtaYNtklnmqrlhipgggaLGNLvfkkir 420
Cdd:cd05911 224 DSELFLDLIE----KYKITFLYLVPP--------IAAALAKSPLLDK------YD---------------LSSL------ 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 421 tatggqlRYLLNGGSPISRDAQEFITNLI--CPMLIGYGLTETCASTTILDPANFELGVAGDLTGCVTVKLVDV---EEL 495
Cdd:cd05911 265 -------RVILSGGAPLSKELQELLAKRFpnATIKQGYGMTETGGILTVNPDGDDKPGSVGRLLPNVEAKIVDDdgkDSL 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 496 GYfakNNQGEVWITGANVTPEYYKNEEETSQALTSDGWFKTGDIGEWEANGHLKIIDRKKNLVKtMNGEYIALEKLESVY 575
Cdd:cd05911 338 GP---NEPGEICVRGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKKELIK-YKGFQVAPAELEAVL 413
|
490
....*....|.
gi 398366229 576 RSNEYVANICV 586
Cdd:cd05911 414 LEHPGVADAAV 424
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
177-567 |
2.46e-49 |
|
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: 182.56 E-value: 2.46e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 177 IFTDNSllpslikpVQAAQDVKYIIHFDSISSEDRRQSGKIYQSAH-----DAI----NRIKEVRPDIktFSFDDILKLG 247
Cdd:cd05933 63 IYTTNS--------PEACQYVAETSEANILVVENQKQLQKILQIQDklphlKAIiqykEPLKEKEPNL--YSWDEFMELG 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 248 KESCNE-----IDVHPPGKddLCCIMYTSGSTGEPKGVVLKHSNVVAGVGGASlNVLKFVGNTDR---VICFLPLAHIFE 319
Cdd:cd05933 133 RSIPDEqldaiISSQKPNQ--CCTLIYTSGTTGMPKGVMLSHDNITWTAKAAS-QHMDLRPATVGqesVVSYLPLSHIAA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 320 LVFEL-LSFYWGACIGYATVKTLTSSSVRNcqgdLQEFKPTIMVGVAAVWETVRKGILNQIDNLPFLTKKIFWTA----- 393
Cdd:cd05933 210 QILDIwLPIKVGGQVYFAQPDALKGTLVKT----LREVRPTAFMGVPRVWEKIQEKMKAVGAKSGTLKRKIASWAkgvgl 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 394 -YNTKLNMQRLHIPGGGALGN-LVFKKIRTATG-GQLRYLLNGGSPISRDAQEFITNLICPMLIGYGLTETCASTTILDP 470
Cdd:cd05933 286 eTNLKLMGGESPSPLFYRLAKkLVFKKVRKALGlDRCQKFFTGAAPISRETLEFFLSLNIPIMELYGMSETSGPHTISNP 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 471 ANFELGVAGD-LTGCvTVKLVDVEelgyfaKNNQGEVWITGANVTPEYYKNEEETSQALTSDGWFKTGDIGEWEANGHLK 549
Cdd:cd05933 366 QAYRLLSCGKaLPGC-KTKIHNPD------ADGIGEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLY 438
|
410
....*....|....*...
gi 398366229 550 IIDRKKNLVKTMNGEYIA 567
Cdd:cd05933 439 ITGRIKELIITAGGENVP 456
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
263-588 |
8.81e-46 |
|
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: 166.31 E-value: 8.81e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 263 DLCCIMYTSGSTGEPKGVVLKHSNVVAGVggASLNVLKFVGNTDRVICFLPLAHIFELVFELLSFYWGACI----GYATV 338
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAA--AALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVvllpKFDPE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 339 KTLTsssvrncqgDLQEFKPTIMVGVAAVWETVRKGILNQIDNLPfltkkifwtayntklnmqrlhipgggalgnlvfkk 418
Cdd:cd04433 79 AALE---------LIEREKVTILLGVPTLLARLLKAPESAGYDLS----------------------------------- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 419 irtatggQLRYLLNGGSPISRDAQEFITNLI-CPMLIGYGLTETCASTTILDPANFE--LGVAGDLTGCVTVKLVDVEEl 495
Cdd:cd04433 115 -------SLRALVSGGAPLPPELLERFEEAPgIKLVNGYGLTETGGTVATGPPDDDArkPGSVGRPVPGVEVRIVDPDG- 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 496 GYFAKNNQGEVWITGANVTPEYYKNEEETsQALTSDGWFKTGDIGEWEANGHLKIIDRKKNLVKTmNGEYIALEKLESVY 575
Cdd:cd04433 187 GELPPGEIGELVVRGPSVMKGYWNNPEAT-AAVDEDGWYRTGDLGRLDEDGYLYIVGRLKDMIKS-GGENVYPAEVEAVL 264
|
330
....*....|...
gi 398366229 576 RSNEYVANICVYA 588
Cdd:cd04433 265 LGHPGVAEAAVVG 277
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
265-588 |
1.08e-45 |
|
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: 169.22 E-value: 1.08e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 265 CCIMYTSGSTGEPKGVVLKHSNVVAGVGGASLNVlkFVGNTDRVICFLPLAHIFELVFELL-SFYWGAcigyaTVKTLTS 343
Cdd:COG0318 103 ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAAL--GLTPGDVVLVALPLFHVFGLTVGLLaPLLAGA-----TLVLLPR 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 344 SSVRNCQGDLQEFKPTIMVGVAAVWetvrkgilNQIDNLPFLTKKIFwtayntklnmqrlhipgggalgnlvfkkirtat 423
Cdd:COG0318 176 FDPERVLELIERERVTVLFGVPTML--------ARLLRHPEFARYDL--------------------------------- 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 424 gGQLRYLLNGGSPISRD-AQEFITNLICPMLIGYGLTETCASTTI--LDPANFELGVAGDLTGCVTVKLVDVE--ELgyf 498
Cdd:COG0318 215 -SSLRLVVSGGAPLPPElLERFEERFGVRIVEGYGLTETSPVVTVnpEDPGERRPGSVGRPLPGVEVRIVDEDgrEL--- 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 499 AKNNQGEVWITGANVTPEYYKNEEETSQALtSDGWFKTGDIGEWEANGHLKIIDRKKNLVKTmNGEYIALEKLESVYRSN 578
Cdd:COG0318 291 PPGEVGEIVVRGPNVMKGYWNDPEATAEAF-RDGWLRTGDLGRLDEDGYLYIVGRKKDMIIS-GGENVYPAEVEEVLAAH 368
|
330
....*....|
gi 398366229 579 EYVANICVYA 588
Cdd:COG0318 369 PGVAEAAVVG 378
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
235-644 |
1.65e-40 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 158.73 E-value: 1.65e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 235 IKTFSFDDILKlGKESCNEIDVHPPgkDDLCCIMYTSGSTGEPKGVVLKHSNVVAGVGGASLNVLKFVGNTDRVICFLPL 314
Cdd:PTZ00342 280 ISIILFDDMTK-NKTTNYKIQNEDP--DFITSIVYTSGTSGKPKGVMLSNKNLYNTVVPLCKHSIFKKYNPKTHLSYLPI 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 315 AHIFELVFELLSFYWGACIgyatvkTLTSSSVRNCQGDLQEFKPTIMVGVAAVWETVRKGILNQIDNLPFLTKKIFwtay 394
Cdd:PTZ00342 357 SHIYERVIAYLSFMLGGTI------NIWSKDINYFSKDIYNSKGNILAGVPKVFNRIYTNIMTEINNLPPLKRFLV---- 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 395 NTKLNMQR--LHIPGGGALGNL--VFKKIRTATGGQLRYLLNGGSPISRD-AQEFITNLICPMLIGYGLTETCASTTILD 469
Cdd:PTZ00342 427 KKILSLRKsnNNGGFSKFLEGIthISSKIKDKVNPNLEVILNGGGKLSPKiAEELSVLLNVNYYQGYGLTETTGPIFVQH 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 470 PA--NFElGVAGDLTGCVTVKLVDVEElgYFAKNN--QGEVWITGANVTPEYYKNEEETSQALTSDGWFKTGDIGEWEAN 545
Cdd:PTZ00342 507 ADdnNTE-SIGGPISPNTKYKVRTWET--YKATDTlpKGELLIKSDSIFSGYFLEKEQTKNAFTEDGYFKTGDIVQINKN 583
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 546 GHLKIIDRKKNLVKTMNGEYIALEKLESVYRSNEYVANICVYADQSKTKPVGIIVPNHAPLTKLAKKLGIMEqkDSSINI 625
Cdd:PTZ00342 584 GSLTFLDRSKGLVKLSQGEYIETDMLNNLYSQISFINFCVVYGDDSMDGPLAIISVDKYLLFKCLKDDNMLE--STGINE 661
|
410 420
....*....|....*....|..
gi 398366229 626 ENYLE---DAKLIKAVYSDLLK 644
Cdd:PTZ00342 662 KNYLEkltDETINNNIYVDYVK 683
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
101-558 |
2.05e-38 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 149.67 E-value: 2.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 101 SFDQLTDIMHEIGRGLVKIGLKPNDddKLHLYAATSHKWMKMFLGAQSQG---IPVVTAYdTLGEKGLIhsLVQTGSKAI 177
Cdd:PRK07656 32 TYAELNARVRRAAAALAALGIGKGD--RVAIWAPNSPHWVIAALGALKAGavvVPLNTRY-TADEAAYI--LARGDAKAL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 178 FTDNSLLPSLIKPVQAAQDVKYIIHFDSISSEDrrqsgkiyqsahdainrikevrPDIKTFSFDDILKLGKESCNEIDVH 257
Cdd:PRK07656 107 FVLGLFLGVDYSATTRLPALEHVVICETEEDDP----------------------HTEKMKTFTDFLAAGDPAERAPEVD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 258 PpgkDDLCCIMYTSGSTGEPKGVVLKHSN------VVAGVGGASLNvlkfvgntDRVICFLPLAHIFELVFELLsfywgA 331
Cdd:PRK07656 165 P---DDVADILFTSGTTGRPKGAMLTHRQllsnaaDWAEYLGLTEG--------DRYLAANPFFHVFGYKAGVN-----A 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 332 CI--GyATVKTLTSSSVRNCQGDLQEFKPTIMVGVaavwetvrkgilnqidnlPfltkkifwTAYNTKLNmqrlhIPGGG 409
Cdd:PRK07656 229 PLmrG-ATILPLPVFDPDEVFRLIETERITVLPGP------------------P--------TMYNSLLQ-----HPDRS 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 410 ALGnlvFKKIRTA-TGG-----QLryllnggspISRDAQEFITNLIcpmLIGYGLTETCASTTIL---DPANFELGVAGd 480
Cdd:PRK07656 277 AED---LSSLRLAvTGAasmpvAL---------LERFESELGVDIV---LTGYGLSEASGVTTFNrldDDRKTVAGTIG- 340
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398366229 481 lTGCVTVKLVDVEELGYFAKNNQ-GEVWITGANVTPEYYKNEEETSQALTSDGWFKTGDIGEWEANGHLKIIDRKKNLV 558
Cdd:PRK07656 341 -TAIAGVENKIVNELGEEVPVGEvGELLVRGPNVMKGYYDDPEATAAAIDADGWLHTGDLGRLDEEGYLYIVDRKKDMF 418
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
235-558 |
6.51e-38 |
|
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: 147.32 E-value: 6.51e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 235 IKTFSFDDILKLGKescNEIDVHPPGKDDLCCIMYTSGSTGEPKGVVLKHSNVVAGV--GGASLNVLKfvGNTDRVICFL 312
Cdd:cd05936 101 IVAVSFTDLLAAGA---PLGERVALTPEDVAVLQYTSGTTGVPKGAMLTHRNLVANAlqIKAWLEDLL--EGDDVVLAAL 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 313 PLAHIFELVFELLSFYwgaCIGyATVKTLTSSSVRNCQGDLQEFKPTIMVGVAAVWEtvrkGILNQIDnlpfltkkifwt 392
Cdd:cd05936 176 PLFHVFGLTVALLLPL---ALG-ATIVLIPRFRPIGVLKEIRKHRVTIFPGVPTMYI----ALLNAPE------------ 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 393 ayntklnmqrlhipgggalgnlvFKKIRTATggqLRYLLNGGSPISRDAQEF---ITNliCPMLIGYGLTETCASTTiLD 469
Cdd:cd05936 236 -----------------------FKKRDFSS---LRLCISGGAPLPVEVAERfeeLTG--VPIVEGYGLTETSPVVA-VN 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 470 PANFE--LGVAG-DLTGcVTVKLVDVEelGYFAKNNQ-GEVWITGANVTPEYYKNEEETSQALTsDGWFKTGDIGEWEAN 545
Cdd:cd05936 287 PLDGPrkPGSIGiPLPG-TEVKIVDDD--GEELPPGEvGELWVRGPQVMKGYWNRPEETAEAFV-DGWLRTGDIGYMDED 362
|
330
....*....|...
gi 398366229 546 GHLKIIDRKKNLV 558
Cdd:cd05936 363 GYFFIVDRKKDMI 375
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
262-574 |
4.86e-35 |
|
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: 138.13 E-value: 4.86e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 262 DDLCCIMYTSGSTGEPKGVVLKHSNVVAGVggASLNVLKFVGNTDRVICFLPLAHIFEL-VFELLSFYWGACIGYatvkt 340
Cdd:cd17631 98 DDLALLMYTSGTTGRPKGAMLTHRNLLWNA--VNALAALDLGPDDVLLVVAPLFHIGGLgVFTLPTLLRGGTVVI----- 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 341 ltsssvrncqgdLQEFKPTimvgvaAVWETVRKGILNQIDNLPfltkkifwTAYNTKLNMQRlhipgggalgnlvFKKIR 420
Cdd:cd17631 171 ------------LRKFDPE------TVLDLIERHRVTSFFLVP--------TMIQALLQHPR-------------FATTD 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 421 TATggqLRYLLNGGSPISRDAQEFITNLICPMLIGYGLTETCASTTILDPANFE--LGVAGDLTGCVTVKLVDvEELGYF 498
Cdd:cd17631 212 LSS---LRAVIYGGAPMPERLLRALQARGVKFVQGYGMTETSPGVTFLSPEDHRrkLGSAGRPVFFVEVRIVD-PDGREV 287
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398366229 499 AKNNQGEVWITGANVTPEYYKNEEETSQALtSDGWFKTGDIGEWEANGHLKIIDRKKNLVKTmNGEYIALEKLESV 574
Cdd:cd17631 288 PPGEVGEIVVRGPHVMAGYWNRPEATAAAF-RDGWFHTGDLGRLDEDGYLYIVDRKKDMIIS-GGENVYPAEVEDV 361
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
249-574 |
5.28e-35 |
|
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: 139.29 E-value: 5.28e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 249 ESCNEIDVHPPGKDDLCCIMYTSGSTGEPKGVVLKHSNVVAGVGGASLNVLKFVGNTDRVICFLPLAHIFELVFELLSfy 328
Cdd:cd05904 145 ADEAEPPVVVIKQDDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEGSNSDSEDVFLCVLPMFHIYGLSSFALG-- 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 329 wGACIGyATVKTLTSSSVRNCQGDLQEFKPTIMVGVAAVwetvrkgILNqidnlpfLTKKifwtayntklnmqrlhipgg 408
Cdd:cd05904 223 -LLRLG-ATVVVMPRFDLEELLAAIERYKVTHLPVVPPI-------VLA-------LVKS-------------------- 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 409 GALGNLVFKKirtatggqLRYLLNGGSPISRDAQE-FITNLICPMLI-GYGLTETCA-STTILDPANF--ELGVAGDLTG 483
Cdd:cd05904 267 PIVDKYDLSS--------LRQIMSGAAPLGKELIEaFRAKFPNVDLGqGYGMTESTGvVAMCFAPEKDraKYGSVGRLVP 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 484 CVTVKLVDVEELGYFAKNNQGEVWITGANVTPEYYKNEEETSQALTSDGWFKTGDIGEWEANGHLKIIDRKKNLVKtMNG 563
Cdd:cd05904 339 NVEAKIVDPETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKEGWLHTGDLCYIDEDGYLFIVDRLKELIK-YKG 417
|
330
....*....|.
gi 398366229 564 EYIALEKLESV 574
Cdd:cd05904 418 FQVAPAELEAL 428
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
253-675 |
1.77e-33 |
|
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: 136.05 E-value: 1.77e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 253 EIDVHPPGKDDLCCIMYTSGSTGEPKGVVLKHSNVVAgvggASLNVLKFVGNTDR---VICFLPLAHIFELvfelLSFYW 329
Cdd:cd17632 214 PLFRPEPDDDPLALLIYTSGSTGTPKGAMYTERLVAT----FWLKVSSIQDIRPPasiTLNFMPMSHIAGR----ISLYG 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 330 GACIGyATVKTLTSSSVRNCQGDLQEFKPTIMVGVAAVWETVRKGILNQIDnlpfltkkifwtayntklnmqRLHIPGG- 408
Cdd:cd17632 286 TLARG-GTAYFAAASDMSTLFDDLALVRPTELFLVPRVCDMLFQRYQAELD---------------------RRSVAGAd 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 409 -GALGNLVFKKIRTAT-GGQLRYLLNGGSPISRDAQEFITNLI-CPMLIGYGLTEtcASTTILDPANFELGVagdltgcV 485
Cdd:cd17632 344 aETLAERVKAELRERVlGGRLLAAVCGSAPLSAEMKAFMESLLdLDLHDGYGSTE--AGAVILDGVIVRPPV-------L 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 486 TVKLVDVEELGYFAKNN---QGEVWITGANVTPEYYKNEEETSQALTSDGWFKTGDIGEWEANGHLKIIDRKKNLVKTMN 562
Cdd:cd17632 415 DYKLVDVPELGYFRTDRphpRGELLVKTDTLFPGYYKRPEVTAEVFDEDGFYRTGDVMAELGPDRLVYVDRRNNVLKLSQ 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 563 GEYIALEKLESVYRSNEYVANICVYADQSKTKPVGIIVPNHAPLTKlakklgimeqkdssinienyLEDAKLIKAVYSDL 642
Cdd:cd17632 495 GEFVTVARLEAVFAASPLVRQIFVYGNSERAYLLAVVVPTQDALAG--------------------EDTARLRAALAESL 554
|
410 420 430
....*....|....*....|....*....|...
gi 398366229 643 LKTGKDQGLVGIELLAGIVFFDGEWTPQNGFVT 675
Cdd:cd17632 555 QRIAREAGLQSYEIPRDFLIETEPFTIANGLLS 587
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
101-582 |
3.13e-33 |
|
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: 133.98 E-value: 3.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 101 SFDQLTDIMHEIGRGLVKIGLKPNDddKLHLYAATSHKWMKMFLGAQSQG---IPVVTAYdTLGEKGLIHSlvQTGSKAI 177
Cdd:cd05926 16 TYADLAELVDDLARQLAALGIKKGD--RVAIALPNGLEFVVAFLAAARAGavvAPLNPAY-KKAEFEFYLA--DLGSKLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 178 FTDN----SLLPSLIKPVQAAQDVkyiiHFDSISSEDRRQSGKIyqSAHDAINRIKEVRPdiktfsfddilklgkescne 253
Cdd:cd05926 91 LTPKgelgPASRAASKLGLAILEL----ALDVGVLIRAPSAESL--SNLLADKKNAKSEG-------------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 254 idvhPPGKDDLCCIMYTSGSTGEPKGVVLKHSNVVAGVGGASlNVLKfVGNTDRVICFLPLAHIFELVFELLS-FYWGAC 332
Cdd:cd05926 145 ----VPLPDDLALILHTSGTTGRPKGVPLTHRNLAASATNIT-NTYK-LTPDDRTLVVMPLFHVHGLVASLLStLAAGGS 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 333 IGYATvktltSSSVRNCQGDLQEFKPTimvgvaavWETVRKGILnqidnlpfltkKIFWTAYNTKlnmqrlhipGGGALG 412
Cdd:cd05926 219 VVLPP-----RFSASTFWPDVRDYNAT--------WYTAVPTIH-----------QILLNRPEPN---------PESPPP 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 413 NLVFkkIRTAtggqlryllngGSPISRD-AQEFITNLICPMLIGYGLTETC--ASTTILDPANFELGVAGDLTGcvtVKL 489
Cdd:cd05926 266 KLRF--IRSC-----------SASLPPAvLEALEATFGAPVLEAYGMTEAAhqMTSNPLPPGPRKPGSVGKPVG---VEV 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 490 VDVEELGYFAKNNQ-GEVWITGANVTPEYYKNEEETSQALTSDGWFKTGDIGEWEANGHLKIIDRKKNLVktmN--GEYI 566
Cdd:cd05926 330 RILDEDGEILPPGVvGEICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADGYLFLTGRIKELI---NrgGEKI 406
|
490
....*....|....*.
gi 398366229 567 ALEKLESVYRSNEYVA 582
Cdd:cd05926 407 SPLEVDGVLLSHPAVL 422
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
115-589 |
1.35e-32 |
|
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: 133.32 E-value: 1.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 115 GLVKIGLKPNDddKLHLYAATSHKWMKMFLGAQSQG-IPVVTAYDTLGEKgLIHSLVQTGSKAIFT-DNSLLPSLIKPVQ 192
Cdd:cd17641 27 GLLALGVGRGD--VVAILGDNRPEWVWAELAAQAIGaLSLGIYQDSMAEE-VAYLLNYTGARVVIAeDEEQVDKLLEIAD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 193 AAQDVKYIIHFDsissedrrQSGkiyQSAHDainrikevrpDIKTFSFDDILKLGKEscneIDVHPPGK----------D 262
Cdd:cd17641 104 RIPSVRYVIYCD--------PRG---MRKYD----------DPRLISFEDVVALGRA----LDRRDPGLyerevaagkgE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 263 DLCCIMYTSGSTGEPKGVVLKHSNVvAGVGGASLNVlKFVGNTDRVICFLPLAHIFELVfellsfywgacigYATVKTLT 342
Cdd:cd17641 159 DVAVLCTTSGTTGKPKLAMLSHGNF-LGHCAAYLAA-DPLGPGDEYVSVLPLPWIGEQM-------------YSVGQALV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 343 SSSVRNC-------QGDLQEFKPTIMVGVAAVWEtvrkGILNQI-----DNLPFltKKIFWTAY----NTKLNMQRLHIP 406
Cdd:cd17641 224 CGFIVNFpeepetmMEDLREIGPTFVLLPPRVWE----GIAADVrarmmDATPF--KRFMFELGmklgLRALDRGKRGRP 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 407 GGGALGN-------LVFKKIRTATG-GQLRYLLNGGSPISRDAQEFITNLICPMLIGYGLTETCASTTIldpanfelGVA 478
Cdd:cd17641 298 VSLWLRLaswladaLLFRPLRDRLGfSRLRSAATGGAALGPDTFRFFHAIGVPLKQLYGQTELAGAYTV--------HRD 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 479 GDL-TGCVTVKLVDVEelgyFAKNNQGEVWITGANVTPEYYKNEEETSQALTSDGWFKTGDIGEWEANGHLKIIDRKKNL 557
Cdd:cd17641 370 GDVdPDTVGVPFPGTE----VRIDEVGEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDV 445
|
490 500 510
....*....|....*....|....*....|..
gi 398366229 558 VKTMNGEYIALEKLESVYRSNEYVANICVYAD 589
Cdd:cd17641 446 GTTSDGTRFSPQFIENKLKFSPYIAEAVVLGA 477
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
255-601 |
5.37e-29 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 121.83 E-value: 5.37e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 255 DVHPPGKDDLCCIMYTSGSTGEPKGVVLKHSNVVAGvggaSLNVLKF--VGNTDRVICFLPLAHIFELVFELLSFYWGAC 332
Cdd:PRK06187 160 DFPDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLH----SLAVCAWlkLSRDDVYLVIVPMFHVHAWGLPYLALMAGAK 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 333 IGYA------TVKTLTsssvrncqgdLQEfKPTIMVGVAAVWEtvrkGILNQIDnlpfltkkifwtAYNTKLNmqrlhip 406
Cdd:PRK06187 236 QVIPrrfdpeNLLDLI----------ETE-RVTFFFAVPTIWQ----MLLKAPR------------AYFVDFS------- 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 407 gggalgnlvfkkirtatggQLRYLLNGGSPISRD-AQEFITNLICPMLIGYGLTETCASTTIL-----DPANFEL----G 476
Cdd:PRK06187 282 -------------------SLRLVIYGGAALPPAlLREFKEKFGIDLVQGYGMTETSPVVSVLppedqLPGQWTKrrsaG 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 477 VAgdLTGcVTVKLVDVE--ELGYFAKNnQGEVWITGANVTPEYYKNEEETSQALTsDGWFKTGDIGEWEANGHLKIIDRK 554
Cdd:PRK06187 343 RP--LPG-VEARIVDDDgdELPPDGGE-VGEIIVRGPWLMQGYWNRPEATAETID-GGWLHTGDVGYIDEDGYLYITDRI 417
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 398366229 555 KNLVKTmNGEYIALEKLESVYRSNEYVANICVYA---DQSKTKPVGIIVP 601
Cdd:PRK06187 418 KDVIIS-GGENIYPRELEDALYGHPAVAEVAVIGvpdEKWGERPVAVVVL 466
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
112-581 |
1.31e-28 |
|
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: 120.71 E-value: 1.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 112 IGRGLVKIGLKPNdddklHLYAATSHKWMKMFL---GAQSQGIPVVTAYDTLGEKGLIHSLVQTGSKAIFTDNSLLPSLI 188
Cdd:cd17642 57 LAEALKKYGLKQN-----DRIAVCSENSLQFFLpviAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCSKKGLQKVL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 189 KPVQAAQDVKYIIHFDSISSEDRRQSGKIYQSAHDAINRIKEvrpDIKTFSFDDilklgkescneidvhppgKDDLCCIM 268
Cdd:cd17642 132 NVQKKLKIIKTIIILDSKEDYKGYQCLYTFITQNLPPGFNEY---DFKPPSFDR------------------DEQVALIM 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 269 YTSGSTGEPKGVVLKHSNVVAGVGGASLNVlkfVGN----TDRVICFLPLAHIFELvFELLSFywgACIGYATV------ 338
Cdd:cd17642 191 NSSGSTGLPKGVQLTHKNIVARFSHARDPI---FGNqiipDTAILTVIPFHHGFGM-FTTLGY---LICGFRVVlmykfe 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 339 -KTLTSSsvrncqgdLQEFK-------PTIMVgvaavwetvrkgilnqidnlpFLTKKIFWTAYNtklnmqrlhipggga 410
Cdd:cd17642 264 eELFLRS--------LQDYKvqsallvPTLFA---------------------FFAKSTLVDKYD--------------- 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 411 LGNLVfkkirtatggqlrYLLNGGSPISRDAQEFITNLICPMLI--GYGLTETCASTTILDPANFELGVAGDLTGCVTVK 488
Cdd:cd17642 300 LSNLH-------------EIASGGAPLSKEVGEAVAKRFKLPGIrqGYGLTETTSAILITPEGDDKPGAVGKVVPFFYAK 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 489 LVDVEELGYFAKNNQGEVWITGANVTPEYYKNEEETSQALTSDGWFKTGDIGEWEANGHLKIIDRKKNLVKtMNGEYIAL 568
Cdd:cd17642 367 VVDLDTGKTLGPNERGELCVKGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSLIK-YKGYQVPP 445
|
490
....*....|...
gi 398366229 569 EKLESVYRSNEYV 581
Cdd:cd17642 446 AELESILLQHPKI 458
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
259-586 |
2.14e-28 |
|
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.
Pssm-ID: 341238 [Multi-domain] Cd Length: 411 Bit Score: 118.22 E-value: 2.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 259 PGKDDLCCIMYTSGSTGEPKGVVLKHSNVVAGVGGASLNvLKFVGNtDRVICFLPLAHIFELVFELLSFYWGAcigyaTV 338
Cdd:cd05912 74 VKLDDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALN-LGLTED-DNWLCALPLFHISGLSILMRSVIYGM-----TV 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 339 KTLTSSSVRNCQGDLQEFKPTIMVGVAAvwetvrkgILNQIdnlpfltkkifwtayntklnMQRLHIPgggalgnlvfkk 418
Cdd:cd05912 147 YLVDKFDAEQVLHLINSGKVTIISVVPT--------MLQRL--------------------LEILGEG------------ 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 419 irtaTGGQLRYLLNGGSPISRDAQEFITNLICPMLIGYGLTETCASTTILDPANFE--LGVAGDLTGCVTVKLVDVEElg 496
Cdd:cd05912 187 ----YPNNLRCILLGGGPAPKPLLEQCKEKGIPVYQSYGMTETCSQIVTLSPEDALnkIGSAGKPLFPVELKIEDDGQ-- 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 497 yfAKNNQGEVWITGANVTPEYYKNEEeTSQALTSDGWFKTGDIGEWEANGHLKIIDRKKNLVKTmNGEYIALEKLESVYR 576
Cdd:cd05912 261 --PPYEVGEILLKGPNVTKGYLNRPD-ATEESFENGWFKTGDIGYLDEEGFLYVLDRRSDLIIS-GGENIYPAEIEEVLL 336
|
330
....*....|
gi 398366229 577 SNEYVANICV 586
Cdd:cd05912 337 SHPAIKEAGV 346
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
165-586 |
9.80e-28 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 117.37 E-value: 9.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 165 LIHSLVQTGSKAIFTDNSLLPSLIKPVQAAQDVKYIIHFDSISSEDRRQSGKIYQsahDAINRIKEVRPDIKTFSFDDIL 244
Cdd:PRK03640 68 VIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKCLITDDDFEAKLIPGISVKFA---ELMNGPKEEAEIQEEFDLDEVA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 245 KlgkescneidvhppgkddlccIMYTSGSTGEPKGVVLKHSNVVAGVGGASLNVlkfvGNT--DRVICFLPLAHIFELVF 322
Cdd:PRK03640 145 T---------------------IMYTSGTTGKPKGVIQTYGNHWWSAVGSALNL----GLTedDCWLAAVPIFHISGLSI 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 323 ELLSFYWGAcigyaTVKTLTSSSVRNCQGDLQEFKPTIMVGVAAVwetvrkgilnqidnlpfltkkifwtayntklnMQR 402
Cdd:PRK03640 200 LMRSVIYGM-----RVVLVEKFDAEKINKLLQTGGVTIISVVSTM--------------------------------LQR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 403 L--HIPGGGALGNLvfkkirtatggqlRYLLNGGSPISRDAQEfitnlIC-----PMLIGYGLTETCASTTILDP--ANF 473
Cdd:PRK03640 243 LleRLGEGTYPSSF-------------RCMLLGGGPAPKPLLE-----QCkekgiPVYQSYGMTETASQIVTLSPedALT 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 474 ELGVAGDLTGCVTVKLVDveELGYFAKNNQGEVWITGANVTPEYYKNEEETSQALtSDGWFKTGDIGEWEANGHLKIIDR 553
Cdd:PRK03640 305 KLGSAGKPLFPCELKIEK--DGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETF-QDGWFKTGDIGYLDEEGFLYVLDR 381
|
410 420 430
....*....|....*....|....*....|...
gi 398366229 554 KKNLVKTmNGEYIALEKLESVYRSNEYVANICV 586
Cdd:PRK03640 382 RSDLIIS-GGENIYPAEIEEVLLSHPGVAEAGV 413
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
262-587 |
1.23e-27 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 114.68 E-value: 1.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 262 DDLCCIMYTSGSTGEPKGVVLKHSNVVagvggaslNVLKFVGNT------DRVICFLPLAHIFELVFELLsfywgACIGY 335
Cdd:cd05917 2 DDVINIQFTSGTTGSPKGATLTHHNIV--------NNGYFIGERlglteqDRLCIPVPLFHCFGSVLGVL-----ACLTH 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 336 ATVKTLTSSS--VRNCQGDLQEFKPTIMVGVAavweTVRKGILNQIDnlpfltkkifwtayntklnmqrlhipgggaLGN 413
Cdd:cd05917 69 GATMVFPSPSfdPLAVLEAIEKEKCTALHGVP----TMFIAELEHPD------------------------------FDK 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 414 LVFKKIRTAtggqlrylLNGGSPISRDAQEFITNL--ICPMLIGYGLTET---CASTTILDPANFELGVAGDLTGCVTVK 488
Cdd:cd05917 115 FDLSSLRTG--------IMAGAPCPPELMKRVIEVmnMKDVTIAYGMTETspvSTQTRTDDSIEKRVNTVGRIMPHTEAK 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 489 LVDVEELGYFAKNNQGEVWITGANVTPEYYKNEEETSQALTSDGWFKTGDIGEWEANGHLKIIDRKKNLVkTMNGEYIAL 568
Cdd:cd05917 187 IVDPEGGIVPPVGVPGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLAVMDEDGYCRIVGRIKDMI-IRGGENIYP 265
|
330
....*....|....*....
gi 398366229 569 EKLESVYRSNEYVANICVY 587
Cdd:cd05917 266 REIEEFLHTHPKVSDVQVV 284
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
234-637 |
1.41e-27 |
|
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: 116.39 E-value: 1.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 234 DIKTFSFDDILKLGKESCNEIDVHPPGK-DDLCCIMYTSGSTGEPKGVVLKHSNVVAGVGGaSLNVLKFvGNTDRVICFL 312
Cdd:TIGR01923 82 EEKDFQADSLDRIEAAGRYETSLSASFNmDQIATLMFTSGTTGKPKAVPHTFRNHYASAVG-SKENLGF-TEDDNWLLSL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 313 PLAHIfelvfELLSFYWGACIGYATVKtltsssvrncqgdlqefkptIMVGVAAVWETVRKGILNQIDNLPFLTKKIfwt 392
Cdd:TIGR01923 160 PLYHI-----SGLSILFRWLIEGATLR--------------------IVDKFNQLLEMIANERVTHISLVPTQLNRL--- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 393 ayntklnMQRLHipgggalgnlvfkkirtaTGGQLRYLLNGGSPISrdaQEFITNLIC---PMLIGYGLTETCASTTILD 469
Cdd:TIGR01923 212 -------LDEGG------------------HNENLRKILLGGSAIP---APLIEEAQQyglPIYLSYGMTETCSQVTTAT 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 470 PANF-ELGVAGDLTGCVTVKL-VDveelgyfAKNNQGEVWITGANVTPEYYKNEEETsQALTSDGWFKTGDIGEWEANGH 547
Cdd:TIGR01923 264 PEMLhARPDVGRPLAGREIKIkVD-------NKEGHGEIMVKGANLMKGYLYQGELT-PAFEQQGWFNTGDIGELDGEGF 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 548 LKIIDRKKNLVKTmNGEYIALEKLESVYRSNEYVAN-ICVYADQSK--TKPVGIIV----PNHAPLT-----KLAK-KLG 614
Cdd:TIGR01923 336 LYVLGRRDDLIIS-GGENIYPEEIETVLYQHPGIQEaVVVPKPDAEwgQVPVAYIVsesdISQAKLIaylteKLAKyKVP 414
|
410 420
....*....|....*....|...
gi 398366229 615 IMEQKdssINIENYLEDAKLIKA 637
Cdd:TIGR01923 415 IAFEK---LDELPYNASGKILRN 434
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
263-602 |
1.48e-26 |
|
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: 110.88 E-value: 1.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 263 DLCCIMYTSGSTGEPKGVVLKHSNVVAGVGGaSLNVLKFVGNtDRVICFLPLAHIfelvfellsfywgacIGYATVktlt 342
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAG-LHSRLGFGGG-DSWLLSLPLYHV---------------GGLAIL---- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 343 sssVRNcqgdlqefkptimvgVAAVWETVrkgilnqidnlpFLTKKifWTAYNTKLNMQRLHI---PGggALGNLVFKKI 419
Cdd:cd17630 60 ---VRS---------------LLAGAELV------------LLERN--QALAEDLAPPGVTHVslvPT--QLQRLLDSGQ 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 420 RTATGGQLRYLLNGGSPISRDAQEFITNLICPMLIGYGLTETCASTTILDPANFELGVAGDLTGCVTVKLVDveelgyfa 499
Cdd:cd17630 106 GPAALKSLRAVLLGGAPIPPELLERAADRGIPLYTTYGMTETASQVATKRPDGFGRGGVGVLLPGRELRIVE-------- 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 500 knnQGEVWITGANVTPEYYKNEEEtsQALTSDGWFKTGDIGEWEANGHLKIIDRKKNLVKTmNGEYIALEKLESVYRSNE 579
Cdd:cd17630 178 ---DGEIWVGGASLAMGYLRGQLV--PEFNEDGWFTTKDLGELHADGRLTVLGRADNMIIS-GGENIQPEEIEAALAAHP 251
|
330 340
....*....|....*....|....*.
gi 398366229 580 YVANICVYADQSKT---KPVGIIVPN 602
Cdd:cd17630 252 AVRDAFVVGVPDEElgqRPVAVIVGR 277
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
227-586 |
3.60e-25 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 108.51 E-value: 3.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 227 RIKEVRPDIKTFSFDDILKLGKESCNEIDVHPPGKDDLCCIMYTSGSTGEPKGVVLKHSNVVAGVggASLNVLKFVGNTD 306
Cdd:TIGR01733 85 RLAGLVLPVILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLL--AWLARRYGLDPDD 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 307 RVICFLPLAhiFEL-VFELlsfyWGACIGYATVKTLTSSSVRNCQGDLQ----EFKPTIMVGVAAVWETVRKGILNQIDN 381
Cdd:TIGR01733 163 RVLQFASLS--FDAsVEEI----FGALLAGATLVVPPEDEERDDAALLAaliaEHPVTVLNLTPSLLALLAAALPPALAS 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 382 LpfltkkifwtayntklnmqRLHIPGGGALGNLVFKKIRTATGGqlRYLLNggspisrdaqefitnlicpmliGYGLTET 461
Cdd:TIGR01733 237 L-------------------RLVILGGEALTPALVDRWRARGPG--ARLIN----------------------LYGPTET 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 462 CASTTILDPANFELGVAGDLT-----GCVTVKLVDvEELGYFAKNNQGEVWITGANVTPEYYKNEEETSQALTSDG---- 532
Cdd:TIGR01733 274 TVWSTATLVDPDDAPRESPVPigrplANTRLYVLD-DDLRPVPVGVVGELYIGGPGVARGYLNRPELTAERFVPDPfagg 352
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 398366229 533 ----WFKTGDIGEWEANGHLKIIDRKKNLVKtMNGEYIALEKLESVYRSNEYVANICV 586
Cdd:TIGR01733 353 dgarLYRTGDLVRYLPDGNLEFLGRIDDQVK-IRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
188-600 |
4.19e-25 |
|
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: 109.07 E-value: 4.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 188 IKPVQAAQDVKYIIHFdsissedrrQSGKIYQSAHDAINRIKEVRPDiktfSFDDILKLGKESC----NEIDVHPPGKDD 263
Cdd:cd05922 52 LNPTLKESVLRYLVAD---------AGGRIVLADAGAADRLRDALPA----SPDPGTVLDADGIraarASAPAHEVSHED 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 264 LCCIMYTSGSTGEPKGVVLKHSNVVAgvGGASLN-VLKFVGNtDRVICFLPLAHIFELVFELLSFYWGAcigyATVKTLT 342
Cdd:cd05922 119 LALLLYTSGSTGSPKLVRLSHQNLLA--NARSIAeYLGITAD-DRALTVLPLSYDYGLSVLNTHLLRGA----TLVLTND 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 343 SSSVRNCQGDLQEFKPTIMVGVAAVWETVRKgilnqidnlpfltkkifwtayntklnmqrlhipgggalgnLVFKKIRTA 422
Cdd:cd05922 192 GVLDDAFWEDLREHGATGLAGVPSTYAMLTR----------------------------------------LGFDPAKLP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 423 TggqLRYLLNGGspiSRDAQEFITNLiCPMLIG------YGLTETCASTTILDP--ANFELGVAG-DLTGCvtvKLVDVE 493
Cdd:cd05922 232 S---LRYLTQAG---GRLPQETIARL-RELLPGaqvyvmYGQTEATRRMTYLPPerILEKPGSIGlAIPGG---EFEILD 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 494 ELGYFAKNNQ-GEVWITGANVTPEYYKNEEETSQALTSDGWFKTGDIGEWEANGHLKIIDRKKNLVKTMnGEYIALEKLE 572
Cdd:cd05922 302 DDGTPTPPGEpGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLF-GNRISPTEIE 380
|
410 420
....*....|....*....|....*....
gi 398366229 573 SVYRS-NEYVANICVYADQSKTKPVGIIV 600
Cdd:cd05922 381 AAARSiGLIIEAAAVGLPDPLGEKLALFV 409
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
263-602 |
4.33e-24 |
|
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: 105.83 E-value: 4.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 263 DLCCIMYTSGSTGEPKGVVLKHSNVVAGVGgASLNVLKFVgNTDRVICFLPLAHIFELVFELL-SFYWGAcigyaTVKTL 341
Cdd:cd05941 90 DPALILYTSGTTGRPKGVVLTHANLAANVR-ALVDAWRWT-EDDVLLHVLPLHHVHGLVNALLcPLFAGA-----SVEFL 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 342 TSSSVRNCQGDLQEFKPTIMVGVAAVW----ETVRKGILNQIDNLPFLTKKIfwtayntklnmqRLHIPGGGALGNLVFK 417
Cdd:cd05941 163 PKFDPKEVAISRLMPSITVFMGVPTIYtrllQYYEAHFTDPQFARAAAAERL------------RLMVSGSAALPVPTLE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 418 KIRTATGGQLryllnggspISRdaqefitnlicpmligYGLTETCASTTilDPANFE--LGVAGDLTGCVTVKLVDVEEL 495
Cdd:cd05941 231 EWEAITGHTL---------LER----------------YGMTEIGMALS--NPLDGErrPGTVGMPLPGVQARIVDEETG 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 496 GYFAKNNQGEVWITGANVTPEYYKNEEETSQALTSDGWFKTGDIGEWEANGHLKIIDRKKNLVKTMNGEYI-ALEkLESV 574
Cdd:cd05941 284 EPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGWFKTGDLGVVDEDGYYWILGRSSVDIIKSGGYKVsALE-IERV 362
|
330 340 350
....*....|....*....|....*....|.
gi 398366229 575 YRSNEYVANICVYADQSKT---KPVGIIVPN 602
Cdd:cd05941 363 LLAHPGVSECAVIGVPDPDwgeRVVAVVVLR 393
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
95-619 |
4.41e-24 |
|
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: 106.98 E-value: 4.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 95 SHYHYNSFDQLTDIMHEIGRGLVKIGLKPNDddKLHLYAATSHKWMKMFLGAQSQG-IPVVT----AYDTL--GEKGLIH 167
Cdd:cd05906 35 GSEEFQSYQDLLEDARRLAAGLRQLGLRPGD--SVILQFDDNEDFIPAFWACVLAGfVPAPLtvppTYDEPnaRLRKLRH 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 168 SLVQTGSKAIFTDNSLLPSlIKPVQAAQDVKYIihfDSISSEDRRQSGKIYqsahdainrikevrpdiktfsfddilklg 247
Cdd:cd05906 113 IWQLLGSPVVLTDAELVAE-FAGLETLSGLPGI---RVLSIEELLDTAADH----------------------------- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 248 kescneiDVHPPGKDDLCCIMYTSGSTGEPKGVVLKHSNVVAGVGGAslNVLKFVGNTDRVICFLPLAHIFELVF-ELLS 326
Cdd:cd05906 160 -------DLPQSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGK--IQHNGLTPQDVFLNWVPLDHVGGLVElHLRA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 327 FYWGAcigyATVKTLTSSSVRNcqgdlqefkPTimvgvaaVWetvrkgiLNQIDnlpflTKKIFWT-AYNTKLNMqrlhi 405
Cdd:cd05906 231 VYLGC----QQVHVPTEEILAD---------PL-------RW-------LDLID-----RYRVTITwAPNFAFAL----- 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 406 pgggaLGNLVfKKIRTATG--GQLRYLLNGGSPISRDAQEFITNLICP-------MLIGYGLTETCASTTI-LDPANFEL 475
Cdd:cd05906 274 -----LNDLL-EEIEDGTWdlSSLRYLVNAGEAVVAKTIRRLLRLLEPyglppdaIRPAFGMTETCSGVIYsRSFPTYDH 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 476 GVAGDLTGC------VTVKLVDvEELGYFAKNNQGEVWITGANVTPEYYKNEEETSQALTSDGWFKTGDIGeWEANGHLK 549
Cdd:cd05906 348 SQALEFVSLgrpipgVSMRIVD-DEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLG-FLDNGNLT 425
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398366229 550 IIDRKKNLVkTMNGEYI-------ALEKLESVYRSneYVANICVYADQSKTKPVGII-VPNHAPLTKLAKKLGIMEQK 619
Cdd:cd05906 426 ITGRTKDTI-IVNGVNYysheieaAVEEVPGVEPS--FTAAFAVRDPGAETEELAIFfVPEYDLQDALSETLRAIRSV 500
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
224-558 |
7.82e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 106.39 E-value: 7.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 224 AINRIKEVRPDI---KTFSFDDILKLGK-ESCNEIDVHPpgkDDLCCIMYTSGSTGEPKGVVLKHSNVVAGVggasLNVL 299
Cdd:PRK05677 168 VVKHVKKMVPAYhlpQAVKFNDALAKGAgQPVTEANPQA---DDVAVLQYTGGTTGVAKGAMLTHRNLVANM----LQCR 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 300 KFVGNT-----DRVICFLPLAHIFELVFELLSFYwgaCIGYATVKTltsSSVRNCQG---DLQEFKPTIMVGVaavwETV 371
Cdd:PRK05677 241 ALMGSNlnegcEILIAPLPLYHIYAFTFHCMAMM---LIGNHNILI---SNPRDLPAmvkELGKWKFSGFVGL----NTL 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 372 RKGILNQID--NLPFLTKKifwtayntklnmqrLHIPGGGALGNLVFKKIRTATGgqlryllnggspisrdaqefitnli 449
Cdd:PRK05677 311 FVALCNNEAfrKLDFSALK--------------LTLSGGMALQLATAERWKEVTG------------------------- 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 450 CPMLIGYGLTETCASTTILDPANFELGVAGDLTGCVTVKLVDvEELGYFAKNNQGEVWITGANVTPEYYKNEEETSQALT 529
Cdd:PRK05677 352 CAICEGYGMTETSPVVSVNPSQAIQVGTIGIPVPSTLCKVID-DDGNELPLGEVGELCVKGPQVMKGYWQRPEATDEILD 430
|
330 340
....*....|....*....|....*....
gi 398366229 530 SDGWFKTGDIGEWEANGHLKIIDRKKNLV 558
Cdd:PRK05677 431 SDGWLKTGDIALIQEDGYMRIVDRKKDMI 459
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
257-588 |
1.68e-23 |
|
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: 104.00 E-value: 1.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 257 HPPGKDDLCCIMYTSGSTGEPKGVVLKHSNVVAGVGGASLNVLkfVGNTDRVICFLPLAHIfelvfellsfywgacIGYa 336
Cdd:cd05903 88 PAAMPDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLG--LGPGDVFLVASPMAHQ---------------TGF- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 337 tvktltsssvrncqgdLQEFKPTIMVGVAAVwetvrkgiLNQIdnlpfltkkifWTAYNTKLNMQRLHIPGGGALGNLVF 416
Cdd:cd05903 150 ----------------VYGFTLPLLLGAPVV--------LQDI-----------WDPDKALALMREHGVTFMMGATPFLT 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 417 KKIRTATGG-----QLRYLLNGGSPI----SRDAQEFITNLICPMligYGLTETCASTTILDPANFELGVAGDltGC--- 484
Cdd:cd05903 195 DLLNAVEEAgeplsRLRTFVCGGATVprslARRAAELLGAKVCSA---YGSTECPGAVTSITPAPEDRRLYTD--GRplp 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 485 -VTVKLVDvEELGYFAKNNQGEVWITGANVTPEYYKNEEETSQALtSDGWFKTGDIGEWEANGHLKIIDRKKNLVkTMNG 563
Cdd:cd05903 270 gVEIKVVD-DTGATLAPGVEGELLSRGPSVFLGYLDRPDLTADAA-PEGWFRTGDLARLDEDGYLRITGRSKDII-IRGG 346
|
330 340
....*....|....*....|....*
gi 398366229 564 EYIALEKLESVYRSNEYVANICVYA 588
Cdd:cd05903 347 ENIPVLEVEDLLLGHPGVIEAAVVA 371
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
144-558 |
2.58e-23 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 104.57 E-value: 2.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 144 LGAQSQGIPVVTAYDTLGEKGLIHSLVQTGSKAIFT-DNslLPSLIKPVQAAQDVKYIIHFDSISSEDRRQSGKIyqsaH 222
Cdd:PRK08751 94 FGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLVViDN--FGTTVQQVIADTPVKQVITTGLGDMLGFPKAALV----N 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 223 DAINRIKEVRPDIK---TFSFDDILKLG-KESCNEIDVHPpgkDDLCCIMYTSGSTGEPKGVVLKHSNVVAGVGGASlnv 298
Cdd:PRK08751 168 FVVKYVKKLVPEYRingAIRFREALALGrKHSMPTLQIEP---DDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAH--- 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 299 lKFVGNTDR-------VICFLPLAHIFELVFELLSFY-WGACigyatvKTLTSSSvRNCQGDLQEFKPTIMVGVAAVwET 370
Cdd:PRK08751 242 -QWLAGTGKleegcevVITALPLYHIFALTANGLVFMkIGGC------NHLISNP-RDMPGFVKELKKTRFTAFTGV-NT 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 371 VRKGILNQidnlpfltkkifwtayntklnmqrlhiPGggalgnlvFKKIRTATggqLRYLLNGGSPISRDAQEF---ITN 447
Cdd:PRK08751 313 LFNGLLNT---------------------------PG--------FDQIDFSS---LKMTLGGGMAVQRSVAERwkqVTG 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 448 LicPMLIGYGLTET----CASTTILDPANFELGVAGDLT-GCVTVKLVDVEELGYFaknnqGEVWITGANVTPEYYKNEE 522
Cdd:PRK08751 355 L--TLVEAYGLTETspaaCINPLTLKEYNGSIGLPIPSTdACIKDDAGTVLAIGEI-----GELCIKGPQVMKGYWKRPE 427
|
410 420 430
....*....|....*....|....*....|....*.
gi 398366229 523 ETSQALTSDGWFKTGDIGEWEANGHLKIIDRKKNLV 558
Cdd:PRK08751 428 ETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMI 463
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
263-588 |
5.40e-23 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 102.37 E-value: 5.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 263 DLCCIMYTSGSTGEPKGVVLKHSNVV-AGVGGASLNVLkfvGNTDRVICFLPLAHIFELVFELLsfywGACIGYATVKTL 341
Cdd:cd05934 82 DPASILYTSGTTGPPKGVVITHANLTfAGYYSARRFGL---GEDDVYLTVLPLFHINAQAVSVL----AALSVGATLVLL 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 342 TSSSVRNCQGDLQEFKPTIMvgvaavwetvrkgilNQIdnlpfltkkifwtayntklnmqrlhipggGALGNLVFKKIRT 421
Cdd:cd05934 155 PRFSASRFWSDVRRYGATVT---------------NYL-----------------------------GAMLSYLLAQPPS 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 422 ATGGQLRYLLNGGSPI-SRDAQEFITNLICPMLIGYGLTETCASTTILDPANFELGVAGDLTGCVTVKLVDVE--ELgyf 498
Cdd:cd05934 191 PDDRAHRLRAAYGAPNpPELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIVDDDgqEL--- 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 499 AKNNQGEVWITGAN---VTPEYYKNEEETSQALtSDGWFKTGDIGEWEANGHLKIIDRKKNLVKtMNGEYIALEKLESVY 575
Cdd:cd05934 268 PAGEPGELVIRGLRgwgFFKGYYNMPEATAEAM-RNGWFHTGDLGYRDADGFFYFVDRKKDMIR-RRGENISSAEVERAI 345
|
330
....*....|...
gi 398366229 576 RSNEYVANICVYA 588
Cdd:cd05934 346 LRHPAVREAAVVA 358
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
231-586 |
6.84e-23 |
|
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: 102.17 E-value: 6.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 231 VRPDIKTFSFDDILKlgkESCNEIDVHPPGKDDLCCIMYTSGSTGEPKGVVLKHSNVVAGVggASLNVLKFVGNTDRVIC 310
Cdd:cd05935 56 INPMLKERELEYILN---DSGAKVAVVGSELDDLALIPYTSGTTGLPKGCMHTHFSAAANA--LQSAVWTGLTPSDVILA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 311 FLPLAHIfelvfellsfywgacigyatvktltsssvrncqgdlQEFKPTIMVGVAAVWETVRKGILNQiDNLPFLTKK-- 388
Cdd:cd05935 131 CLPLFHV------------------------------------TGFVGSLNTAVYVGGTYVLMARWDR-ETALELIEKyk 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 389 -IFWTAYNTKLNmQRLHIPgggalgnlvfkKIRTATGGQLRYLLNGGSPISRDAQEFITNLI-CPMLIGYGLTETCASTT 466
Cdd:cd05935 174 vTFWTNIPTMLV-DLLATP-----------EFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTgLRFVEGYGLTETMSQTH 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 467 ILDPANFELGVAGDLTGCVTVKLVDVEELGYFAKNNQGEVWITGANVTPEYYKNEEETSQALTSDG---WFKTGDIGEWE 543
Cdd:cd05935 242 TNPPLRPKLQCLGIP*FGVDARVIDIETGRELPPNEVGEIVVRGPQIFKGYWNRPEETEESFIEIKgrrFFRTGDLGYMD 321
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 398366229 544 ANGHLKIIDRKKNLVKtMNGEYIALEKLESVYRSNEYVANICV 586
Cdd:cd05935 322 EEGYFFFVDRVKRMIN-VSGFKVWPAEVEAKLYKHPAI*EVCV 363
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
239-558 |
7.31e-23 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 103.18 E-value: 7.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 239 SFDDILKLGKEScneiDVHPP--GKDDLCCIMYTSGSTGEPKGVVLKHSNVVAGVGGASLNVLKFVGNTDRV-----ICF 311
Cdd:PRK07059 183 RFNDALAEGARQ----TFKPVklGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQMEAWLQPAFEKKPRPdqlnfVCA 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 312 LPLAHIFEL-VFELLSFYWGACigyatvkTLTSSSVRNCQGDLQEFKPTimvgvaavwetvrkgilnQIDNLPFLTkkif 390
Cdd:PRK07059 259 LPLYHIFALtVCGLLGMRTGGR-------NILIPNPRDIPGFIKELKKY------------------QVHIFPAVN---- 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 391 wTAYNTKLNMqrlhiPGggaLGNLVFKKIRTATGGqlryllngGSPISRD-AQEFITNLICPMLIGYGLTETCASTTIlD 469
Cdd:PRK07059 310 -TLYNALLNN-----PD---FDKLDFSKLIVANGG--------GMAVQRPvAERWLEMTGCPITEGYGLSETSPVATC-N 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 470 PANfelgvAGDLTGCVTVKLVDVE-----ELGYFAKNNQ-GEVWITGANVTPEYYKNEEETSQALTSDGWFKTGDIGEWE 543
Cdd:PRK07059 372 PVD-----ATEFSGTIGLPLPSTEvsirdDDGNDLPLGEpGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMD 446
|
330
....*....|....*
gi 398366229 544 ANGHLKIIDRKKNLV 558
Cdd:PRK07059 447 ERGYTKIVDRKKDMI 461
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
256-573 |
8.60e-23 |
|
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: 102.41 E-value: 8.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 256 VHPPGKDDLCCIMYTSGSTGEPKGVVLKHSNVVAGVGgASLNVLKFVGNtDRVICFLPLAHIF----ELVFELLS----F 327
Cdd:cd05909 141 VAPVQPDDPAVILFTSGSEGLPKGVVLSHKNLLANVE-QITAIFDPNPE-DVVFGALPFFHSFgltgCLWLPLLSgikvV 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 328 YWGACIGYATVKTLtsssvrncqgdLQEFKPTIMVGVaavwETVRKGILNqidnlpfltkkiFWTAYNTKlnmqrlhipg 407
Cdd:cd05909 219 FHPNPLDYKKIPEL-----------IYDKKATILLGT----PTFLRGYAR------------AAHPEDFS---------- 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 408 ggalgnlvfkkirtatggQLRYLLNGGSPISRD-AQEFITNLICPMLIGYGLTETCA--STTILDPANFELGVAGDLTGc 484
Cdd:cd05909 262 ------------------SLRLVVAGAEKLKDTlRQEFQEKFGIRILEGYGTTECSPviSVNTPQSPNKEGTVGRPLPG- 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 485 VTVKLVDVEELGYFAKNNQGEVWITGANVTpEYYKNEEETSQALTSDGWFKTGDIGEWEANGHLKIIDRKKNLVKtMNGE 564
Cdd:cd05909 323 MEVKIVSVETHEEVPIGEGGLLLVRGPNVM-LGYLNEPELTSFAFGDGWYDTGDIGKIDGEGFLTITGRLSRFAK-IAGE 400
|
....*....
gi 398366229 565 YIALEKLES 573
Cdd:cd05909 401 MVSLEAIED 409
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
101-587 |
1.00e-21 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 99.46 E-value: 1.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 101 SFDQLTDIMHEIGRGLVKIGLKPNDddKLHLYAATSHKWMKMFLGAQSQGIPVVTAYDTLGEKGLIHSLVQTGSKAIFTd 180
Cdd:PRK12583 47 TWRQLADAVDRLARGLLALGVQPGD--RVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVIC- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 181 nsllpslikpVQAAQDVKYIIHFDSISSEdrRQSGKIYQSAHDAINRIKEV-----RPDIKTFSFDDILKLGK----ESC 251
Cdd:PRK12583 124 ----------ADAFKTSDYHAMLQELLPG--LAEGQPGALACERLPELRGVvslapAPPPGFLAWHELQARGEtvsrEAL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 252 NEIDVHPPgKDDLCCIMYTSGSTGEPKGVVLKHSNVV--AGVGGASLNVlkfvGNTDRVICFLPLAHIFELVF-ELLSFY 328
Cdd:PRK12583 192 AERQASLD-RDDPINIQYTSGTTGFPKGATLSHHNILnnGYFVAESLGL----TEHDRLCVPVPLYHCFGMVLaNLGCMT 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 329 WGACIGYATvktltsssvrncqgdlQEFKPTimvgvaAVWETVRKGILNQIDNLPfltkkifwTAYNTKLNMQRLhipgg 408
Cdd:PRK12583 267 VGACLVYPN----------------EAFDPL------ATLQAVEEERCTALYGVP--------TMFIAELDHPQR----- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 409 galGNLVFKKIRTAtggqlrylLNGGSPISRDA-QEFITNLICP-MLIGYGLTETCA---STTILDPANFELGVAGDLTG 483
Cdd:PRK12583 312 ---GNFDLSSLRTG--------IMAGAPCPIEVmRRVMDEMHMAeVQIAYGMTETSPvslQTTAADDLERRVETVGRTQP 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 484 CVTVKLVDVEElGYFAKNNQGEVWITGANVTPEYYKNEEETSQALTSDGWFKTGDIGEWEANGHLKIIDRKKNLVkTMNG 563
Cdd:PRK12583 381 HLEVKVVDPDG-ATVPRGEIGELCTRGYSVMKGYWNNPEATAESIDEDGWMHTGDLATMDEQGYVRIVGRSKDMI-IRGG 458
|
490 500
....*....|....*....|....
gi 398366229 564 EYIALEKLESVYRSNEYVANICVY 587
Cdd:PRK12583 459 ENIYPREIEEFLFTHPAVADVQVF 482
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
175-574 |
3.26e-21 |
|
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: 97.70 E-value: 3.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 175 KAIFTDNSLLPsLIKPVQAAQD-VKYIIHFDSISSEDRRQSGKIYqsAHDAInrIKEVRPDIKTFSFDDilklgkescne 253
Cdd:cd12119 99 RVVFVDRDFLP-LLEAIAPRLPtVEHVVVMTDDAAMPEPAGVGVL--AYEEL--LAAESPEYDWPDFDE----------- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 254 idvhppgkDDLCCIMYTSGSTGEPKGVVLKH-SNVVAGVGGASLNVLKfVGNTDRVICFLPLAHIFElvfellsfyWGac 332
Cdd:cd12119 163 --------NTAAAICYTSGTTGNPKGVVYSHrSLVLHAMAALLTDGLG-LSESDVVLPVVPMFHVNA---------WG-- 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 333 IGYATvkTLTSSSV----RNCQGD-----LQEFKPTIMVGVAAVWEtvrkGILNQIDNLPfltkkifwtayntklnmqrl 403
Cdd:cd12119 223 LPYAA--AMVGAKLvlpgPYLDPAslaelIEREGVTFAAGVPTVWQ----GLLDHLEANG-------------------- 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 404 hipgggalgnlvfkkirtATGGQLRYLLNGGSPISRDAQEFITNLICPMLIGYGLTETCASTTILDPANFELGVAGD--- 480
Cdd:cd12119 277 ------------------RDLSSLRRVVIGGSAVPRSLIEAFEERGVRVIHAWGMTETSPLGTVARPPSEHSNLSEDeql 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 481 ----LTG----CVTVKLVDVEelGYFAK---NNQGEVWITGANVTPEYYKNEEEtSQALTSDGWFKTGDIGEWEANGHLK 549
Cdd:cd12119 339 alraKQGrpvpGVELRIVDDD--GRELPwdgKAVGELQVRGPWVTKSYYKNDEE-SEALTEDGWLRTGDVATIDEDGYLT 415
|
410 420
....*....|....*....|....*
gi 398366229 550 IIDRKKNLVKTmNGEYIALEKLESV 574
Cdd:cd12119 416 ITDRSKDVIKS-GGEWISSVELENA 439
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
267-557 |
3.47e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 97.57 E-value: 3.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 267 IMYTSGSTGEPKGVVLKHSNVVAgvggASLN--VLKFVGNTDRVICFLPLAHIfelvfellsfywgacIGYATvktltss 344
Cdd:PRK09088 140 ILFTSGTSGQPKGVMLSERNLQQ----TAHNfgVLGRVDAHSSFLCDAPMFHI---------------IGLIT------- 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 345 SVRncqgdlqefkPTIMVG----VAAVWETVRKgiLNQIDNLPFLTkkifwTAYNTKLNMQRL--HIPG--GGALGNLvf 416
Cdd:PRK09088 194 SVR----------PVLAVGgsilVSNGFEPKRT--LGRLGDPALGI-----THYFCVPQMAQAfrAQPGfdAAALRHL-- 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 417 kkirTAtggqlryLLNGGSP-ISRDAQEFITNLIcPMLIGYGLTEtcASTTILDPANFE-----LGVAGDLTGCVTVKLV 490
Cdd:PRK09088 255 ----TA-------LFTGGAPhAAEDILGWLDDGI-PMVDGFGMSE--AGTVFGMSVDCDvirakAGAAGIPTPTVQTRVV 320
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398366229 491 DVEELGYFAkNNQGEVWITGANVTPEYYKNEEETSQALTSDGWFKTGDIGEWEANGHLKIIDRKKNL 557
Cdd:PRK09088 321 DDQGNDCPA-GVPGELLLRGPNLSPGYWRRPQATARAFTGDGWFRTGDIARRDADGFFWVVDRKKDM 386
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
262-612 |
4.32e-21 |
|
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: 96.93 E-value: 4.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 262 DDLCCIMYTSGSTGEPKGVVLKHSNVVAGVGGAslNVLKFVGNTDRVICFLPLAhiFEL-VFELlsfyWGACIGYATVKT 340
Cdd:cd05945 97 DDNAYIIFTSGSTGRPKGVQISHDNLVSFTNWM--LSDFPLGPGDVFLNQAPFS--FDLsVMDL----YPALASGATLVP 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 341 LTSSSVRNCQgDLQEFKP----TIMVGVAAVWETVRK-GILNQiDNLPFLTKKIFwtayntklnmqrlhipGGGALgnlv 415
Cdd:cd05945 169 VPRDATADPK-QLFRFLAehgiTVWVSTPSFAAMCLLsPTFTP-ESLPSLRHFLF----------------CGEVL---- 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 416 fkkirtaTGGQLRYLLnggspiSRDAQEFITNLicpmligYGLTETCASTTILDPANFELGVAGDLT-G----CVTVKLV 490
Cdd:cd05945 227 -------PHKTARALQ------QRFPDARIYNT-------YGPTEATVAVTYIEVTPEVLDGYDRLPiGyakpGAKLVIL 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 491 DvEELGYFAKNNQGEVWITGANVTPEYYKNEEETSQALTSD---GWFKTGDIGEWEANGHLKIIDRKKNLVKtMNGEYIA 567
Cdd:cd05945 287 D-EDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDegqRAYRTGDLVRLEADGLLFYRGRLDFQVK-LNGYRIE 364
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 398366229 568 LEKLESVYRSNEYVANICV---YADQSKTKPVGIIVPNH---APLTKLAKK 612
Cdd:cd05945 365 LEEIEAALRQVPGVKEAVVvpkYKGEKVTELIAFVVPKPgaeAGLTKAIKA 415
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
257-560 |
1.02e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 96.61 E-value: 1.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 257 HP-PGKDDLCCIMYTSGSTGEPKGVVLKHSNVVAGV--GGASLNVLKfvGNTDRVICFLPLAHIFELVFEL-LSFYWGAc 332
Cdd:PRK05605 213 HPrPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAaqGKAWVPGLG--DGPERVLAALPMFHAYGLTLCLtLAVSIGG- 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 333 igyaTVKTLTSSSVRNCQGDLQEFKPTIMVGVAAVWETVRKGIlnqidnlpfltkkifwTAYNTKLNMQRLHIPGGGALG 412
Cdd:PRK05605 290 ----ELVLLPAPDIDLILDAMKKHPPTWLPGVPPLYEKIAEAA----------------EERGVDLSGVRNAFSGAMALP 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 413 NLVFKKIRTATGGqlryllnggspisrdaqefitnlicpMLI-GYGLTETcaSTTIL-DPANFE-----LGVAGDLTgcv 485
Cdd:PRK05605 350 VSTVELWEKLTGG--------------------------LLVeGYGLTET--SPIIVgNPMSDDrrpgyVGVPFPDT--- 398
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398366229 486 TVKLVDVEELGY-FAKNNQGEVWITGANVTPEYYKNEEETSQALTsDGWFKTGDIGEWEANGHLKIIDRKKNLVKT 560
Cdd:PRK05605 399 EVRIVDPEDPDEtMPDGEEGELLVRGPQVFKGYWNRPEETAKSFL-DGWFRTGDVVVMEEDGFIRIVDRIKELIIT 473
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
261-558 |
1.41e-20 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 95.89 E-value: 1.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 261 KDDLCCIMYTSGSTGEPKGVVLKHSNVVAGVGGASLNVLKFVGNTDR-VICFLPLAHIFEL-VFELLSFYWGACigyatv 338
Cdd:PRK08974 205 PEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQAKAAYGPLLHPGKElVVTALPLYHIFALtVNCLLFIELGGQ------ 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 339 kTLTSSSVRNCQG---DLQEFKPTIMVGVAavwetvrkgilnqidnlpfltkkifwTAYNTKLNMQRLHipgggalgNLV 415
Cdd:PRK08974 279 -NLLITNPRDIPGfvkELKKYPFTAITGVN--------------------------TLFNALLNNEEFQ--------ELD 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 416 FKKIRTATGGqlryllngGSPISRDAQEFITNLI-CPMLIGYGLTEtCASTTILDPANFEL--GVAGDLTGCVTVKLVDv 492
Cdd:PRK08974 324 FSSLKLSVGG--------GMAVQQAVAERWVKLTgQYLLEGYGLTE-CSPLVSVNPYDLDYysGSIGLPVPSTEIKLVD- 393
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398366229 493 EELGYFAKNNQGEVWITGANVTPEYYKNEEETSQALtSDGWFKTGDIGEWEANGHLKIIDRKKNLV 558
Cdd:PRK08974 394 DDGNEVPPGEPGELWVKGPQVMLGYWQRPEATDEVI-KDGWLATGDIAVMDEEGFLRIVDRKKDMI 458
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
224-558 |
6.06e-20 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 94.25 E-value: 6.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 224 AINRIKEVRPDIKTFSFDDILKlgKESCNE-IDVHPPGKDDLCCIMYTSGSTGEPKGVVLKHSNVVAGvgGASLNVLKFV 302
Cdd:PRK07529 176 LAVPLIRRKAHARILDFDAELA--RQPGDRlFSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVAN--AWLGALLLGL 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 303 GNTDRVICFLPLAHIFELVFELLS-FYWGAcigyaTVKTLTSSSVRNcQGDLQEFkptimvgvaavWETVRKGILNQIDN 381
Cdd:PRK07529 252 GPGDTVFCGLPLFHVNALLVTGLApLARGA-----HVVLATPQGYRG-PGVIANF-----------WKIVERYRINFLSG 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 382 LPfltkkifwTAYNTKLNmqrlhIPGGGAlgNLvfkkirtatgGQLRYLLNGGSPISRD-AQEFITNLICPMLIGYGLTE 460
Cdd:PRK07529 315 VP--------TVYAALLQ-----VPVDGH--DI----------SSLRYALCGAAPLPVEvFRRFEAATGVRIVEGYGLTE 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 461 -TCASTtiLDPANFE--LGVAG-DLTGCvTVKLVDVEELGYF----AKNNQGEVWITGANVTPEYYkNEEETSQALTSDG 532
Cdd:PRK07529 370 aTCVSS--VNPPDGErrIGSVGlRLPYQ-RVRVVILDDAGRYlrdcAVDEVGVLCIAGPNVFSGYL-EAAHNKGLWLEDG 445
|
330 340
....*....|....*....|....*.
gi 398366229 533 WFKTGDIGEWEANGHLKIIDRKKNLV 558
Cdd:PRK07529 446 WLNTGDLGRIDADGYFWLTGRAKDLI 471
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
145-583 |
1.16e-19 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 93.35 E-value: 1.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 145 GAQSQGIPVVTAYDTLGEKGLIHSLVQTGSKAIFTDNsLLPSLIKPVQAAQDVKYIIHFdsissedrrQSGKIYQSA--- 221
Cdd:PRK12492 94 GALRAGLIVVNTNPLYTAREMRHQFKDSGARALVYLN-MFGKLVQEVLPDTGIEYLIEA---------KMGDLLPAAkgw 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 222 --HDAINRIKEVRPDI---KTFSFDDILKLGKEScnEIDVHPPGKDDLCCIMYTSGSTGEPKGVVLKHSNVVA------- 289
Cdd:PRK12492 164 lvNTVVDKVKKMVPAYhlpQAVPFKQALRQGRGL--SLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVAnmlqvra 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 290 -----GVGGASLnvlkFVGNTDRVICFLPLAHIFELVFELLsfywgaCIGYATVKTLTSSSVRNCQG---DLQEFKPTIM 361
Cdd:PRK12492 242 clsqlGPDGQPL----MKEGQEVMIAPLPLYHIYAFTANCM------CMMVSGNHNVLITNPRDIPGfikELGKWRFSAL 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 362 VGVaavwETVRKGILN--QIDNLPFLTKKIfwtaYNTklnmqrlhipGGGALGNLVFKKIRTATGgqlryllnggspisr 439
Cdd:PRK12492 312 LGL----NTLFVALMDhpGFKDLDFSALKL----TNS----------GGTALVKATAERWEQLTG--------------- 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 440 daqefitnliCPMLIGYGLTET--CASTtilDP--ANFELGVAGDLTGCVTVKLVDvEELGYFAKNNQGEVWITGANVTP 515
Cdd:PRK12492 359 ----------CTIVEGYGLTETspVAST---NPygELARLGTVGIPVPGTALKVID-DDGNELPLGERGELCIKGPQVMK 424
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398366229 516 EYYKNEEETSQALTSDGWFKTGDIGEWEANGHLKIIDRKKNLVkTMNGEYIALEKLESVYRSNEYVAN 583
Cdd:PRK12492 425 GYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLI-IVSGFNVYPNEIEDVVMAHPKVAN 491
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
244-602 |
1.26e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 92.64 E-value: 1.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 244 LKLGKESCNEidVHPPGKDDLCCIMYTSGSTGEPKGVVLKHSNV-------VAGVGgaslnvlkfVGNTDRVICFLPLAH 316
Cdd:PRK06145 133 LAQGGLEIPP--QAAVAPTDLVRLMYTSGTTDRPKGVMHSYGNLhwksidhVIALG---------LTASERLLVVGPLYH 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 317 IFELVFELLSFYWGAciGYATVktltsssvrncqgdLQEFKPTimvgvaAVWETVRKGILNQIDNLPFLTKKIFWTAYNT 396
Cdd:PRK06145 202 VGAFDLPGIAVLWVG--GTLRI--------------HREFDPE------AVLAAIERHRLTCAWMAPVMLSRVLTVPDRD 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 397 KLNMqrlhipgggalgnlvfkkirtatgGQLRYLLNGG--SPISR--DAQEFITNliCPMLIGYGLTETCASTTILDpAN 472
Cdd:PRK06145 260 RFDL------------------------DSLAWCIGGGekTPESRirDFTRVFTR--ARYIDAYGLTETCSGDTLME-AG 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 473 FEL---GVAGDLTGCVTVKLVDvEELGYFAKNNQGEVWITGANVTPEYYKNEEETSQALTsDGWFKTGDIGEWEANGHLK 549
Cdd:PRK06145 313 REIekiGSTGRALAHVEIRIAD-GAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFY-GDWFRSGDVGYLDEEGFLY 390
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 398366229 550 IIDRKKNLVKTmNGEYIALEKLESV-YRSNEY--VANICVYADQSKTKPVGIIVPN 602
Cdd:PRK06145 391 LTDRKKDMIIS-GGENIASSEVERViYELPEVaeAAVIGVHDDRWGERITAVVVLN 445
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
254-590 |
2.40e-19 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 91.85 E-value: 2.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 254 IDVHPPGKDDLCCIMYTSGSTGEPKGVVLKHSNVVAGvggaSLNVLKFVGNT--DRVICFLPLAHIFEL-VFELLSFYWG 330
Cdd:PRK06839 141 DNFVEKNESASFIICYTSGTTGKPKGAVLTQENMFWN----ALNNTFAIDLTmhDRSIVLLPLFHIGGIgLFAFPTLFAG 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 331 ACIGYATvKTLTSSSVRNcqgdLQEFKPTIMVGVAAVWETVRKGILNQIDNLpfltkkifwtayntklnmqrlhipggga 410
Cdd:PRK06839 217 GVIIVPR-KFEPTKALSM----IEKHKVTVVMGVPTIHQALINCSKFETTNL---------------------------- 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 411 lgnlvfkkirtatgGQLRYLLNGGSPISRD-AQEFITNLIcPMLIGYGLTETCASTTIL--DPANFELGVAGDLTGCVTV 487
Cdd:PRK06839 264 --------------QSVRWFYNGGAPCPEElMREFIDRGF-LFGQGFGMTETSPTVFMLseEDARRKVGSIGKPVLFCDY 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 488 KLVDvEELGYFAKNNQGEVWITGANVTPEYYKNEEETSQALtSDGWFKTGDIGEWEANGHLKIIDRKKNLVKTmNGEYIA 567
Cdd:PRK06839 329 ELID-ENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETI-QDGWLCTGDLARVDEDGFVYIVGRKKEMIIS-GGENIY 405
|
330 340
....*....|....*....|...
gi 398366229 568 LEKLESVYRSNEYVANICVYADQ 590
Cdd:PRK06839 406 PLEVEQVINKLSDVYEVAVVGRQ 428
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
256-600 |
4.65e-19 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 91.44 E-value: 4.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 256 VHPP-GKDDLCCIMYTSGSTGEPKGVVLKHSNVVAGVG-----GASLnvLKFVGNTDRVICFLPLAHIFEL---VFELLS 326
Cdd:PLN02574 191 PKPViKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVElfvrfEASQ--YEYPGSDNVYLAALPMFHIYGLslfVVGLLS 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 327 fywgacigyatvktLTSSSVRncqgdLQEFKPTIMVGVAAVWETVRKGILNQIdnLPFLTKKifwtaynTKlnmqrlhIP 406
Cdd:PLN02574 269 --------------LGSTIVV-----MRRFDASDMVKVIDRFKVTHFPVVPPI--LMALTKK-------AK-------GV 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 407 GGGALGNLvfKKIRTatggqlryllnGGSPISRDA-QEFITNLICPMLI-GYGLTETCA-STTILDPANFE-LGVAGDLT 482
Cdd:PLN02574 314 CGEVLKSL--KQVSC-----------GAAPLSGKFiQDFVQTLPHVDFIqGYGMTESTAvGTRGFNTEKLSkYSSVGLLA 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 483 GCVTVKLVDVEELGYFAKNNQGEVWITGANVTPEYYKNEEETSQALTSDGWFKTGDIGEWEANGHLKIIDRKKNLVKtMN 562
Cdd:PLN02574 381 PNMQAKVVDWSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIK-YK 459
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 398366229 563 GEYIALEKLESVYRSNEYVANICVYADQSKTK---PVGIIV 600
Cdd:PLN02574 460 GFQIAPADLEAVLISHPEIIDAAVTAVPDKECgeiPVAFVV 500
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
262-582 |
5.57e-19 |
|
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: 90.28 E-value: 5.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 262 DDLCCIMYTSGSTGEPKGVVLKHSNVVAGVggASLNVLKFVGNTDRVICFLPL---AHIFELVFELLSfywGACIgyatv 338
Cdd:cd05930 93 DDLAYVIYTSGSTGKPKGVMVEHRGLVNLL--LWMQEAYPLTPGDRVLQFTSFsfdVSVWEIFGALLA---GATL----- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 339 kTLTSSSVRNCQGDLQEF----KPTIMVGVAAVWETVrkgilnqidnlpfltkkifwtayntklnmqrLHIPGGGALGNl 414
Cdd:cd05930 163 -VVLPEEVRKDPEALADLlaeeGITVLHLTPSLLRLL-------------------------------LQELELAALPS- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 415 vfkkirtatggqLRYLLNGGSPISRDAQEFITNLICPMLI--GYGLTET--CASTTILDPANFELGVA--GDLTGCVTVK 488
Cdd:cd05930 210 ------------LRLVLVGGEALPPDLVRRWRELLPGARLvnLYGPTEAtvDATYYRVPPDDEEDGRVpiGRPIPNTRVY 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 489 LVDveelgyfaKNNQ-------GEVWITGANVTPEYYKNEEETSQALTSDGWF------KTGDIGEWEANGHLKIIDRKK 555
Cdd:cd05930 278 VLD--------ENLRpvppgvpGELYIGGAGLARGYLNRPELTAERFVPNPFGpgermyRTGDLVRWLPDGNLEFLGRID 349
|
330 340
....*....|....*....|....*..
gi 398366229 556 NLVKtMNGEYIALEKLESVYRSNEYVA 582
Cdd:cd05930 350 DQVK-IRGYRIELGEIEAALLAHPGVR 375
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
262-593 |
9.99e-19 |
|
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: 89.67 E-value: 9.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 262 DDLCCIMYTSGSTGEPKGVVLKHSNVVAGVGGASLnVLKFvGNTDRVICFLPLAHIFElVFELlsfyWGACIGYATVKTL 341
Cdd:cd17643 93 DDLAYVIYTSGSTGRPKGVVVSHANVLALFAATQR-WFGF-NEDDVWTLFHSYAFDFS-VWEI----WGALLHGGRLVVV 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 342 TSSSVRncqgdlqefKPtimvgvAAVWETVRKG---ILNQidnlpflTKKIFwtayntKLNMQRLHIPGGGALGnlvfkk 418
Cdd:cd17643 166 PYEVAR---------SP------EDFARLLRDEgvtVLNQ-------TPSAF------YQLVEAADRDGRDPLA------ 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 419 irtatggqLRYLLNGGSPISRD-----AQEFitNLICPMLI-GYGLTETCASTT--ILDPANFElGVAGDLTGC----VT 486
Cdd:cd17643 212 --------LRYVIFGGEALEAAmlrpwAGRF--GLDRPQLVnMYGITETTVHVTfrPLDAADLP-AAAASPIGRplpgLR 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 487 VKLVDvEELGYFAKNNQGEVWITGANVTPEYYKNEEETSQALTSDGW-------FKTGDIGEWEANGHLKIIDRKKNLVK 559
Cdd:cd17643 281 VYVLD-ADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFggpgsrmYRTGDLARRLPDGELEYLGRADEQVK 359
|
330 340 350
....*....|....*....|....*....|....
gi 398366229 560 tMNGEYIALEKLESVYRSNEYVANICVYADQSKT 593
Cdd:cd17643 360 -IRGFRIELGEIEAALATHPSVRDAAVIVREDEP 392
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
239-586 |
1.22e-18 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 90.04 E-value: 1.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 239 SFDDILKLGKESCNEIDVHPPGKDDLCCIMYTSGSTGEPKGVVLKHSNVVAGVGGASLNV-LKFVGNTdRVICFLPLAHI 317
Cdd:PLN02330 161 NWKELLEAADRAGDTSDNEEILQTDLCALPFSSGTTGISKGVMLTHRNLVANLCSSLFSVgPEMIGQV-VTLGLIPFFHI 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 318 FELVfellsfywGACigYATVKTLTSSSVRNcQGDLQEFKPTIMVGVAAVWETVRKGILNQIDNlPFLTKkifwtayntk 397
Cdd:PLN02330 240 YGIT--------GIC--CATLRNKGKVVVMS-RFELRTFLNALITQEVSFAPIVPPIILNLVKN-PIVEE---------- 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 398 LNMQRLhipgggalgnlvfkkirtatggQLRYLLNGGSPISRDAQEFITNLICPMLI--GYGLTE-TCASTTILDPANFE 474
Cdd:PLN02330 298 FDLSKL----------------------KLQAIMTAAAPLAPELLTAFEAKFPGVQVqeAYGLTEhSCITLTHGDPEKGH 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 475 lGVA-----GDLTGCVTVKLVDVEELGYFAKNNQGEVWITGANVTPEYYKNEEETSQALTSDGWFKTGDIGEWEANGHLK 549
Cdd:PLN02330 356 -GIAkknsvGFILPNLEVKFIDPDTGRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIGYIDDDGDIF 434
|
330 340 350
....*....|....*....|....*....|....*..
gi 398366229 550 IIDRKKNLVKtMNGEYIALEKLESVYRSNEYVANICV 586
Cdd:PLN02330 435 IVDRIKELIK-YKGFQVAPAELEAILLTHPSVEDAAV 470
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
258-558 |
1.65e-18 |
|
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: 89.61 E-value: 1.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 258 PPGKDDLCCIMYTSGSTGEPKGVVLKHSNVVAGVGGASLNVlkFVGNTDRVICFLPLAHIFELVFELLSFYWGaciGYAT 337
Cdd:cd05931 145 SPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAY--GLDPGDVVVSWLPLYHDMGLIGGLLTPLYS---GGPS 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 338 VKTLTSSSVRNCQGDLQ---EFKPTIMVGvaavwetvrkgilnqidnlP-FltkkifwtAYNtklnmqrlhipgggalgn 413
Cdd:cd05931 220 VLMSPAAFLRRPLRWLRlisRYRATISAA-------------------PnF--------AYD------------------ 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 414 LVFKKIRTATGGQL-----RYLLNGGSPISRDA-QEFIT---------NLICPmliGYGLTE-TCASTTI---------- 467
Cdd:cd05931 255 LCVRRVRDEDLEGLdlsswRVALNGAEPVRPATlRRFAEafapfgfrpEAFRP---SYGLAEaTLFVSGGppgtgpvvlr 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 468 LDPANFELGVAG---------DLTGC------VTVKLVDVEELGYFAKNNQGEVWITGANVTPEYYKNEEET------SQ 526
Cdd:cd05931 332 VDRDALAGRAVAvaaddpaarELVSCgrplpdQEVRIVDPETGRELPDGEVGEIWVRGPSVASGYWGRPEATaetfgaLA 411
|
330 340 350
....*....|....*....|....*....|..
gi 398366229 527 ALTSDGWFKTGDIGeWEANGHLKIIDRKKNLV 558
Cdd:cd05931 412 ATDEGGWLRTGDLG-FLHDGELYITGRLKDLI 442
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
257-572 |
1.59e-17 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 87.29 E-value: 1.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 257 HPPGKDDLCCIMYTSGSTGEPKGVVLKHSNVVAGVGGASlNVLKfVGNTDRVICFLPLAHIFELVFELlsfyWG-ACIGY 335
Cdd:PRK08633 777 PTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQIS-DVFN-LRNDDVILSSLPFFHSFGLTVTL----WLpLLEGI 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 336 ATVktltsssvrnCQGDlqefkPTIMVGVAAVWETVRKGILnqidnlpfLTKKIFWTAYntkLNMQRLHipgggalgNLV 415
Cdd:PRK08633 851 KVV----------YHPD-----PTDALGIAKLVAKHRATIL--------LGTPTFLRLY---LRNKKLH--------PLM 896
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 416 FKKIRTATGG--QLRyllnggspiSRDAQEFITNLICPMLIGYGLTETCASTTILDPaNFELGVAGDLTGC--------- 484
Cdd:PRK08633 897 FASLRLVVAGaeKLK---------PEVADAFEEKFGIRILEGYGATETSPVASVNLP-DVLAADFKRQTGSkegsvgmpl 966
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 485 --VTVKLVDVEELGYFAKNNQGEVWITGANVTPEYYKNEEETSQALT---SDGWFKTGDIGEWEANGHLKIIDRKKNLVK 559
Cdd:PRK08633 967 pgVAVRIVDPETFEELPPGEDGLILIGGPQVMKGYLGDPEKTAEVIKdidGIGWYVTGDKGHLDEDGFLTITDRYSRFAK 1046
|
330
....*....|...
gi 398366229 560 tMNGEYIALEKLE 572
Cdd:PRK08633 1047 -IGGEMVPLGAVE 1058
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
238-600 |
2.02e-17 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 86.19 E-value: 2.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 238 FSFDDILKLGKESCNEIDVHPpgkDDLCCIMYTSGSTGEPKGVVLKHSNVVAGVG----GASLNvLKFVGNtDRVICFLP 313
Cdd:PLN02246 158 LHFSELTQADENELPEVEISP---DDVVALPYSSGTTGLPKGVMLTHKGLVTSVAqqvdGENPN-LYFHSD-DVILCVLP 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 314 LAHIFELVFELL-SFYWGACI----GYATVKTLtsSSVRNCQGDLQEFKPTIMVGVAavwetvrkgilnqidnlpfltKK 388
Cdd:PLN02246 233 MFHIYSLNSVLLcGLRVGAAIlimpKFEIGALL--ELIQRHKVTIAPFVPPIVLAIA---------------------KS 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 389 IFWTAYNtkLNMQRLHIPGGGALGnlvfKKIRTATGGQLryllnggsPISRDAQefitnlicpmliGYGLTEtcaSTTIL 468
Cdd:PLN02246 290 PVVEKYD--LSSIRMVLSGAAPLG----KELEDAFRAKL--------PNAVLGQ------------GYGMTE---AGPVL 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 469 --------DPANFELGVAGDLTGCVTVKLVDVEELGYFAKNNQGEVWITGANVTPEYYKNEEETSQALTSDGWFKTGDIG 540
Cdd:PLN02246 341 amclafakEPFPVKSGSCGTVVRNAELKIVDPETGASLPRNQPGEICIRGPQIMKGYLNDPEATANTIDKDGWLHTGDIG 420
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398366229 541 EWEANGHLKIIDRKKNLVKtMNGEYIALEKLESVYRSNEYVANICVYA---DQSKTKPVGIIV 600
Cdd:PLN02246 421 YIDDDDELFIVDRLKELIK-YKGFQVAPAELEALLISHPSIADAAVVPmkdEVAGEVPVAFVV 482
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
96-608 |
3.22e-17 |
|
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.
Pssm-ID: 211788 [Multi-domain] Cd Length: 517 Bit Score: 85.22 E-value: 3.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 96 HYHYNSFDQLTDIMHEIGRGLVKIGLKPNDddKLHLYAATSHKWMKMFLGAQSQGIPVVTAYDTLGEKGLIHSLVQTGSK 175
Cdd:TIGR03098 22 HDRTLTYAALSERVLALASGLRGLGLARGE--RVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQVAHILADCNVR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 176 AIFTDNSLLPSLIKPVQAAQDVKYIIHFDSissedrrqsgkiyqSAHDainriKEVRPDIKTFSFDDILKLGkescNEID 255
Cdd:TIGR03098 100 LLVTSSERLDLLHPALPGCHDLRTLIIVGD--------------PAHA-----SEGHPGEEPASWPKLLALG----DADP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 256 VHPPGKDDLCCIMYTSGSTGEPKGVVLKHSNVVAGvggaSLNVLKFVGNT--DRVICFLPLAhiFELVFELL--SFYWGA 331
Cdd:TIGR03098 157 PHPVIDSDMAAILYTSGSTGRPKGVVLSHRNLVAG----AQSVATYLENRpdDRLLAVLPLS--FDYGFNQLttAFYVGA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 332 CI---GYATVKTLTSSSVRNcqgdlqefKPTIMVGVAAVWetvrkgilnqidnlpfltkkifwtayntkLNMQRLHIPgg 408
Cdd:TIGR03098 231 TVvlhDYLLPRDVLKALEKH--------GITGLAAVPPLW-----------------------------AQLAQLDWP-- 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 409 galgnlvfkkirTATGGQLRYLLNGGSPISRDA----QEFITNL-ICPMligYGLTETCASTTiLDPAnfELGVAGDLTG 483
Cdd:TIGR03098 272 ------------ESAAPSLRYLTNSGGAMPRATlsrlRSFLPNArLFLM---YGLTEAFRSTY-LPPE--EVDRRPDSIG 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 484 --CVTVKLVDVEELG-YFAKNNQGEVWITGANVTPEYYKNEEETSQALTSDGWFK-----------TGDIGEWEANGHLK 549
Cdd:TIGR03098 334 kaIPNAEVLVLREDGsECAPGEEGELVHRGALVAMGYWNDPEKTAERFRPLPPFPgelhlpelavwSGDTVRRDEEGFLY 413
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398366229 550 IIDRKKNLVKTmNGEYIALEKLESVYRSNEYVANICVYADQSKTKPVGIIV----PNHAPLTK 608
Cdd:TIGR03098 414 FVGRRDEMIKT-SGYRVSPTEVEEVAYATGLVAEAVAFGVPDPTLGQAIVLvvtpPGGEELDR 475
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
261-604 |
4.69e-17 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 84.94 E-value: 4.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 261 KDDLCCIMYTSGSTGEPKGVVLKHSNVVAGVggASLNVLKFVGNTDRVICFLPLAHIFELVFELLSFYWGAciGYATVKT 340
Cdd:PRK05852 175 RPDDAMIMFTGGTTGLPKMVPWTHANIASSV--RAIITGYRLSPRDATVAVMPLYHGHGLIAALLATLASG--GAVLLPA 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 341 LTSSSVRNCQGDlqefkptiMVGVAAVWETVRKGIlNQIdnlpfltkkifwtayntklnmqrlhipgggalgnlVFKKIR 420
Cdd:PRK05852 251 RGRFSAHTFWDD--------IKAVGATWYTAVPTI-HQI-----------------------------------LLERAA 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 421 TATGGQ----LRYLLNGGSPISRD-AQEFITNLICPMLIGYGLTET---CASTTIL------DPAnFELGVAGDLTGcVT 486
Cdd:PRK05852 287 TEPSGRkpaaLRFIRSCSAPLTAEtAQALQTEFAAPVVCAFGMTEAthqVTTTQIEgigqteNPV-VSTGLVGRSTG-AQ 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 487 VKLV--DVEELGyfaKNNQGEVWITGANVTPEYYKNEEETSQALTsDGWFKTGDIGEWEANGHLKIIDRKKNLVKTmNGE 564
Cdd:PRK05852 365 IRIVgsDGLPLP---AGAVGEVWLRGTTVVRGYLGDPTITAANFT-DGWLRTGDLGSLSAAGDLSIRGRIKELINR-GGE 439
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 398366229 565 YIALEKLESVYRSNEYVANICVYA--DQSKTKPVG-IIVPNHA 604
Cdd:PRK05852 440 KISPERVEGVLASHPNVMEAAVFGvpDQLYGEAVAaVIVPRES 482
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
263-574 |
1.10e-16 |
|
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: 81.92 E-value: 1.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 263 DLCCIMYTSGSTGEPKGVVLKHSNVVAGVGGASLNVLKFVgNTDRVICFLPLAHIFELVFELLS-FYWGACIGYATVKTL 341
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWV-VGDVTYLPLPATHIGGLWWILTClIHGGLCVTGGENTTY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 342 TSssvrnCQGDLQEFKPTIMVGVAAVWETvrkgILNQIDNLpfltkkifwtayntklnmqrlhipgggalgnlvfkkirT 421
Cdd:cd17635 81 KS-----LFKILTTNAVTTTCLVPTLLSK----LVSELKSA--------------------------------------N 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 422 ATGGQLRYLLNGGS-PISRDAQEFITNLICPMLIGYGLTETCASTTI-LDPANFELGVAGDLTGCVTVKLVDVEELGYFA 499
Cdd:cd17635 114 ATVPSLRLIGYGGSrAIAADVRFIEATGLTNTAQVYGLSETGTALCLpTDDDSIEINAVGRPYPGVDVYLAATDGIAGPS 193
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398366229 500 KNNqGEVWITGANVTPEYYKNEEETSQALTsDGWFKTGDIGEWEANGHLKIIDRKKNLVkTMNGEYIALEKLESV 574
Cdd:cd17635 194 ASF-GTIWIKSPANMLGYWNNPERTAEVLI-DGWVNTGDLGERREDGFLFITGRSSESI-NCGGVKIAPDEVERI 265
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
267-560 |
2.45e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 82.35 E-value: 2.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 267 IMYTSGSTGEPKGVVLKHSNVVAGVGGASlNVLKFVGNtDRVICFLPLAHIFELVFELLsfywGAC-IGYATVKTLTSSS 345
Cdd:PRK07787 133 IVYTSGTTGPPKGVVLSRRAIAADLDALA-EAWQWTAD-DVLVHGLPLFHVHGLVLGVL----GPLrIGNRFVHTGRPTP 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 346 VRNCQGdlQEFKPTIMVGVAAVWetvrkgilNQIDNLPFLTKKifwtayntkLNMQRLHIPGGGALGNLVFKKIRTATGG 425
Cdd:PRK07787 207 EAYAQA--LSEGGTLYFGVPTVW--------SRIAADPEAARA---------LRGARLLVSGSAALPVPVFDRLAALTGH 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 426 QlryllnggsPISRdaqefitnlicpmligYGLTETCASTTILDPANFELGVAG-DLTGcVTVKLVDvEELGYFAKNNQ- 503
Cdd:PRK07787 268 R---------PVER----------------YGMTETLITLSTRADGERRPGWVGlPLAG-VETRLVD-EDGGPVPHDGEt 320
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 398366229 504 -GEVWITGANVTPEYYKNEEETSQALTSDGWFKTGDIGEWEANGHLKIIDRKK-NLVKT 560
Cdd:PRK07787 321 vGELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDPDGMHRIVGREStDLIKS 379
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
217-586 |
2.66e-16 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 82.42 E-value: 2.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 217 IYQSAHDAINRIKEVRPDIKTFS----FDDILklGKESCnEIDVHPP-GKDDLCCIMYTSGSTGEPKGVVLKHSNVV-AG 290
Cdd:PRK08008 126 IQQEDATPLRHICLTRVALPADDgvssFTQLK--AQQPA-TLCYAPPlSTDDTAEILFTSGTTSRPKGVVITHYNLRfAG 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 291 VGGASLNVLKfvgNTDRVICFLPLAHI-FELVFELLSFYWGAcigyaTVKTLTSSSVRNCQGDLQEFKPTI--------- 360
Cdd:PRK08008 203 YYSAWQCALR---DDDVYLTVMPAFHIdCQCTAAMAAFSAGA-----TFVLLEKYSARAFWGQVCKYRATItecipmmir 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 361 --MVGVAAVWEtvrkgilnqidnlpfltkkifwtayntklnmqRLHipgggALGNLVFkkirtatggqlrYLlnggsPIS 438
Cdd:PRK08008 275 tlMVQPPSAND--------------------------------RQH-----CLREVMF------------YL-----NLS 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 439 -RDAQEFITNLICPMLIGYGLTETCasttildpanfeLGVAGDLTG-------------CVTVKLVDvEELGYFAKNNQG 504
Cdd:PRK08008 301 dQEKDAFEERFGVRLLTSYGMTETI------------VGIIGDRPGdkrrwpsigrpgfCYEAEIRD-DHNRPLPAGEIG 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 505 EVWITGA---NVTPEYYKNEEETSQALTSDGWFKTGDIGEWEANGHLKIIDRKKNLVKTmNGEYIALEKLESVYRSNEYV 581
Cdd:PRK08008 368 EICIKGVpgkTIFKEYYLDPKATAKVLEADGWLHTGDTGYVDEEGFFYFVDRRCNMIKR-GGENVSCVELENIIATHPKI 446
|
....*
gi 398366229 582 ANICV 586
Cdd:PRK08008 447 QDIVV 451
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
262-558 |
3.03e-16 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 80.99 E-value: 3.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 262 DDLCCIMYTSGSTGEPKGVVLKHSNVVAGvgGASLNVLKFVGNTDRVICFLPLAHIFELVFELLS-FYWGACIGYATVKT 340
Cdd:cd05944 2 DDVAAYFHTGGTTGTPKLAQHTHSNEVYN--AWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTpLASGAHVVLAGPAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 341 LTSSSV-RNCQGDLQEFKPTIMVGVAAVWETVrkgilnqidnlpfltkkifwtayntklnMQRlhiPGGGALGNLvfkki 419
Cdd:cd05944 80 YRNPGLfDNFWKLVERYRITSLSTVPTVYAAL----------------------------LQV---PVNADISSL----- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 420 rtatggqlRYLLNGGSPIS---RDAQEFITNLicPMLIGYGLTE-TCASTTILDPANFELGVAGDLTGCVTVKLVDVEEL 495
Cdd:cd05944 124 --------RFAMSGAAPLPvelRARFEDATGL--PVVEGYGLTEaTCLVAVNPPDGPKRPGSVGLRLPYARVRIKVLDGV 193
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398366229 496 GYF----AKNNQGEVWITGANVTPEYYkNEEETSQALTSDGWFKTGDIGEWEANGHLKIIDRKKNLV 558
Cdd:cd05944 194 GRLlrdcAPDEVGEICVAGPGVFGGYL-YTEGNKNAFVADGWLNTGDLGRLDADGYLFITGRAKDLI 259
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
261-558 |
4.19e-16 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 81.77 E-value: 4.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 261 KDDLCCIMYTSGSTGEPKGVVLKHSNVVAGVGgASLNVLKfVGNTDRVICFLPLAHIFELV-FELLSFYWGACigyatvk 339
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMF-AILNSTE-WKTKDRILSWMPLTHDMGLIaFHLAPLIAGMN------- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 340 tltsssvrncqgdlQEFKPTIMvgvaavwetvrkgilnqidnlpFLTKKIFWTAYNTKLNMQRLHIPGGGAlgNLVFKKI 419
Cdd:cd05908 176 --------------QYLMPTRL----------------------FIRRPILWLKKASEHKATIVSSPNFGY--KYFLKTL 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 420 RTATGGQ-----LRYLLNGGSPISRDAQEFITNLICP-------MLIGYGLTETCASTTI--LDPANFELGVAGD-LTGC 484
Cdd:cd05908 218 KPEKANDwdlssIRMILNGAEPIDYELCHEFLDHMSKyglkrnaILPVYGLAEASVGASLpkAQSPFKTITLGRRhVTHG 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 485 VTVKLVDVE--------ELGYFAKNNQ----------------GEVWITGANVTPEYYKNEEETSQALTSDGWFKTGDIG 540
Cdd:cd05908 298 EPEPEVDKKdsecltfvEVGKPIDETDiricdednkilpdgyiGHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLG 377
|
330
....*....|....*...
gi 398366229 541 eWEANGHLKIIDRKKNLV 558
Cdd:cd05908 378 -FIRNGRLVITGREKDII 394
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
256-613 |
6.82e-16 |
|
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: 80.43 E-value: 6.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 256 VHPPGKDDLCCIMYTSGSTGEPKGVVLKHSNVVAGVGGASLNVlkFVGNTDRVicflplAHIFELVFEllsfywgACIG- 334
Cdd:cd17653 99 LTTDSPDDLAYIIFTSGSTGIPKGVMVPHRGVLNYVSQPPARL--DVGPGSRV------AQVLSIAFD-------ACIGe 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 335 -YATVktltsssvrnCQGDLqefkpTIMVGVAAVWETVRKgilnQIDNLPfLTKKIFWTayntkLNMQRLhiPgggalgn 413
Cdd:cd17653 164 iFSTL----------CNGGT-----LVLADPSDPFAHVAR----TVDALM-STPSILST-----LSPQDF--P------- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 414 lvfkkirtatggQLRYLLNGGSPISRdaqefitNLICP------MLIGYGLTET--CASTTILDPANF-ELGVAGDLTGC 484
Cdd:cd17653 210 ------------NLKTIFLGGEAVPP-------SLLDRwspgrrLYNAYGPTECtiSSTMTELLPGQPvTIGKPIPNSTC 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 485 VtvkLVDvEELGYFAKNNQGEVWITGANVTPEYYKNEEETSQALTSDGW------FKTGDIGEWEANGHLKIIDRKKNLV 558
Cdd:cd17653 271 Y---ILD-ADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFwpgsrmYRTGDYGRWTEDGGLEFLGREDNQV 346
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 398366229 559 KtMNGEYIALEKLES-VYRSNEYVANicVYADQSKTKPVGIIVPNHAPLTKLAKKL 613
Cdd:cd17653 347 K-VRGFRINLEEIEEvVLQSQPEVTQ--AAAIVVNGRLVAFVTPETVDVDGLRSEL 399
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
118-558 |
8.39e-16 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 80.77 E-value: 8.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 118 KIGLKPNDddKLHLYAATSHKWMKMFLGAQSQGIPVVTAYDTLGEKGLIHSLVQTGSKAIFTDNSLLPSlIKPVQAAQDV 197
Cdd:PRK08314 55 ECGVRKGD--RVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGARVAIVGSELAPK-VAPAVGNLRL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 198 KYII--HFdsissedrrqSGKIYQSAHDAINRIKEVRPDIKTFSFDDILKLgKESCNEIDVHPP---GKDDLCCIMYTSG 272
Cdd:PRK08314 132 RHVIvaQY----------SDYLPAEPEIAVPAWLRAEPPLQALAPGGVVAW-KEALAAGLAPPPhtaGPDDLAVLPYTSG 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 273 STGEPKGVVLKHSNVVAGVGGASLnvlkFVGNT--DRVICFLPLAHIFELVFELLS-FYWGAcigyaTVKTLTSSSvRNC 349
Cdd:PRK08314 201 TTGVPKGCMHTHRTVMANAVGSVL----WSNSTpeSVVLAVLPLFHVTGMVHSMNApIYAGA-----TVVLMPRWD-REA 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 350 QGDLQE-FKPTimvgvaavwetvrkgilnqidnlpfltkkiFWTAYNTKL-------NMQR------LHIPGGGA-LGNL 414
Cdd:PRK08314 271 AARLIErYRVT------------------------------HWTNIPTMVvdflaspGLAErdlsslRYIGGGGAaMPEA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 415 VFKKIRTATGgqLRYLlnggspisrdaqEfitnlicpmliGYGLTETCASTTILDPANFELGVAGDLTGCVTVKLVDVEE 494
Cdd:PRK08314 321 VAERLKELTG--LDYV------------E-----------GYGLTETMAQTHSNPPDRPKLQCLGIPTFGVDARVIDPET 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398366229 495 LGYFAKNNQGEVWITGANVTPEYYKNEEETSQA-LTSDG--WFKTGDIGEWEANGHLKIIDRKKNLV 558
Cdd:PRK08314 376 LEELPPGEVGEIVVHGPQVFKGYWNRPEATAEAfIEIDGkrFFRTGDLGRMDEEGYFFITDRLKRMI 442
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
263-557 |
1.10e-15 |
|
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: 78.70 E-value: 1.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 263 DLCCIMYTSGSTGEPKGVVLKHSNVVaGVGGASLNVLKfVGNTDRVICFLPLAHIFElvfellsfYWGACIgyatVKTLT 342
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTL-RAAAAWADCAD-LTEDDRYLIINPFFHTFG--------YKAGIV----ACLLT 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 343 SSSVrncqgdlqefKPTIMVGVAAVWETVRKgilNQIDNLP-----FLTKKIFWTAYNTKLNMQRLHIPGGGALGNLVFK 417
Cdd:cd17638 67 GATV----------VPVAVFDVDAILEAIER---ERITVLPgpptlFQSLLDHPGRKKFDLSSLRAAVTGAATVPVELVR 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 418 KIRTATGgqlryllnggspisrdaqefitnlICPMLIGYGLTEtCASTTILDPANFELGVA---GDLTGCVTVKLVDvee 494
Cdd:cd17638 134 RMRSELG------------------------FETVLTAYGLTE-AGVATMCRPGDDAETVAttcGRACPGFEVRIAD--- 185
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398366229 495 lgyfaknnQGEVWITGANVTPEYYKNEEETSQALTSDGWFKTGDIGEWEANGHLKIIDRKKNL 557
Cdd:cd17638 186 --------DGEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGELDERGYLRITDRLKDM 240
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
253-614 |
3.99e-15 |
|
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: 78.52 E-value: 3.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 253 EIDVHPPGK-DDLCCIMYTSGSTGEPKGVVLKHSNVVAGVggASLNVLKFVGNTDRVICFLPLAhiFEL-VFELlsfywg 330
Cdd:cd17655 127 SENLEPVSKsDDLAYVIYTSGSTGKPKGVMIEHRGVVNLV--EWANKVIYQGEHLRVALFASIS--FDAsVTEI------ 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 331 acigYATVktLTSSS---VRncqgdlqefKPTIMVGVAAVwETVRKGILNQIDNLPFLTKKIFWTAYNTKLNMQRLhIPG 407
Cdd:cd17655 197 ----FASL--LSGNTlyiVR---------KETVLDGQALT-QYIRQNRITIIDLTPAHLKLLDAADDSEGLSLKHL-IVG 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 408 GGALGNLVFKKIRTATGGQLRyllnggspisrdaqefITNLicpmligYGLTET--CASTTILDPANFE-----LGVAgd 480
Cdd:cd17655 260 GEALSTELAKKIIELFGTNPT----------------ITNA-------YGPTETtvDASIYQYEPETDQqvsvpIGKP-- 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 481 lTGCVTVKLVDvEELGYFAKNNQGEVWITGANVTPEYYKNEEETSQALTSDGW------FKTGDIGEWEANGHLKIIDRK 554
Cdd:cd17655 315 -LGNTRIYILD-QYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFvpgermYRTGDLARWLPDGNIEFLGRI 392
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398366229 555 KNLVKtMNGEYIALEKLESVYRSNEYVANICVYA--DQSKTKPV-GIIVPN-HAPLTKLAKKLG 614
Cdd:cd17655 393 DHQVK-IRGYRIELGEIEARLLQHPDIKEAVVIArkDEQGQNYLcAYIVSEkELPVAQLREFLA 455
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
101-576 |
4.34e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 78.44 E-value: 4.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 101 SFDQLTDIMHEIGRGLVKIGLKPNDddKLHLYAATSHKWMKMFLGAQSQGIPVVTAYDTLGEKGLIHSLVQTGSKAIFTD 180
Cdd:PRK08316 38 TYAELDAAVNRVAAALLDLGLKKGD--RVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAFLVD 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 181 NSLLPSLIKPVQAAQDVKYIIhfdsissedrrqSGKIYQSAHDAINRikevrpdiktfSFDDILKLGKEScnEIDVHPPG 260
Cdd:PRK08316 116 PALAPTAEAALALLPVDTLIL------------SLVLGGREAPGGWL-----------DFADWAEAGSVA--EPDVELAD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 261 kDDLCCIMYTSGSTGEPKGVVLKH--------SNVVAGVGGASlnvlkfvgntDRVICFLPLAHIFEL-VFELLSFYWGA 331
Cdd:PRK08316 171 -DDLAQILYTSGTESLPKGAMLTHraliaeyvSCIVAGDMSAD----------DIPLHALPLYHCAQLdVFLGPYLYVGA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 332 cigyaTVKTLTSSSVRNCQGDLQEFKPTIMVGVAAVWetvrKGILNQID----NLPFLTKkifwtAYntklnmqrlhipg 407
Cdd:PRK08316 240 -----TNVILDAPDPELILRTIEAERITSFFAPPTVW----ISLLRHPDfdtrDLSSLRK-----GY------------- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 408 ggalgnlvfkkirtatggqlrYllnGGS----PISRDAQEFITNLI---CpmligYGLTETCASTTILDPANFE--LGVA 478
Cdd:PRK08316 293 ---------------------Y---GASimpvEVLKELRERLPGLRfynC-----YGQTEIAPLATVLGPEEHLrrPGSA 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 479 GDLTGCVTVKLVDvEELGYFAKNNQGEVWITGANVTPEYYKNEEETSQALtSDGWFKTGDIGEWEANGHLKIIDRKKNLV 558
Cdd:PRK08316 344 GRPVLNVETRVVD-DDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAF-RGGWFHSGDLGVMDEEGYITVVDRKKDMI 421
|
490
....*....|....*....
gi 398366229 559 KTmNGEYIA-LEKLESVYR 576
Cdd:PRK08316 422 KT-GGENVAsREVEEALYT 439
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
257-588 |
5.26e-15 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 78.56 E-value: 5.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 257 HPPGKDDLCCIMYTSGSTGEPKGVVLKHSNVVAGVGgASLNVLKfVGNTDRVICFLPLAHifelvfeLLSFYWGACIgya 336
Cdd:PRK13295 192 LRPGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIV-PYAERLG-LGADDVILMASPMAH-------QTGFMYGLMM--- 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 337 tvktltsssvrncqgdlqefkpTIMVGVAAV----WETVRKGILNQidnlpflTKKIFWTAYNTklnmqrlhiPGGGALG 412
Cdd:PRK13295 260 ----------------------PVMLGATAVlqdiWDPARAAELIR-------TEGVTFTMAST---------PFLTDLT 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 413 NLVfkKIRTATGGQLRYLLNGGSPISR----DAQEFITNLICPmliGYGLTETCASTTILDPANFELGVAGDltGC---- 484
Cdd:PRK13295 302 RAV--KESGRPVSSLRTFLCAGAPIPGalveRARAALGAKIVS---AWGMTENGAVTLTKLDDPDERASTTD--GCplpg 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 485 VTVKLVDvEELGYFAKNNQGEVWITGANVTPEYYKNEEETSQAltSDGWFKTGDIGEWEANGHLKIIDRKKNLVkTMNGE 564
Cdd:PRK13295 375 VEVRVVD-ADGAPLPAGQIGRLQVRGCSNFGGYLKRPQLNGTD--ADGWFDTGDLARIDADGYIRISGRSKDVI-IRGGE 450
|
330 340
....*....|....*....|....
gi 398366229 565 YIALEKLESVYRSNEYVANICVYA 588
Cdd:PRK13295 451 NIPVVEIEALLYRHPAIAQVAIVA 474
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
262-558 |
6.70e-15 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 78.25 E-value: 6.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 262 DDLCCIMYTSGSTGEPKGVVLKHSNVVAgvggASLNVLKFVGNTDRVICFL--PLAHIfelvfelLSFYWGAC----IGY 335
Cdd:PRK06087 187 DELAAVLFTSGTEGLPKGVMLTHNNILA----SERAYCARLNLTWQDVFMMpaPLGHA-------TGFLHGVTapflIGA 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 336 ATVKtltsssvrncqgdLQEFKPTimvgvAAVWETVRKGILNQIDNLPFLtkkifwtaYN--TKLNMQRLHIPgggalgn 413
Cdd:PRK06087 256 RSVL-------------LDIFTPD-----ACLALLEQQRCTCMLGATPFI--------YDllNLLEKQPADLS------- 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 414 lvfkkirtatggQLRYLLNGGSPI----SRDAQEFITNLicpmLIGYGLTETCASTTILDPANFELGVAGD---LTGcVT 486
Cdd:PRK06087 303 ------------ALRFFLCGGTTIpkkvARECQQRGIKL----LSVYGSTESSPHAVVNLDDPLSRFMHTDgyaAAG-VE 365
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398366229 487 VKLVDvEELGYFAKNNQGEVWITGANVTPEYYKNEEETSQALTSDGWFKTGDIGEWEANGHLKIIDRKKNLV 558
Cdd:PRK06087 366 IKVVD-EARKTLPPGCEGEEASRGPNVFMGYLDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDII 436
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
101-602 |
6.87e-15 |
|
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: 77.79 E-value: 6.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 101 SFDQLTDIMHEIGRGLVKIGLKPndDDKLHLYAATSHKWMKMFLGAQSQGI-PVVTAYDTLGEKgLIHSLVQTGSKAIFT 179
Cdd:cd05959 31 TYAELEAEARRVAGALRALGVKR--EERVLLIMLDTVDFPTAFLGAIRAGIvPVPVNTLLTPDD-YAYYLEDSRARVVVV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 180 DNSLLPSLIKPVQAAQDVKYIIhfdsISSEDRRqsgkiyqsahdainrikevrPDIKTFSFDDILKLGKESCNEIDVHPp 259
Cdd:cd05959 108 SGELAPVLAAALTKSEHTLVVL----IVSGGAG--------------------PEAGALLLAELVAAEAEQLKPAATHA- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 260 gkDDLCCIMYTSGSTGEPKGVVLKHSNVVAGVGGASLNVLKFVGNtDRVICFLPLAHIFELVFELLSFYW--GACIGYAT 337
Cdd:cd05959 163 --DDPAFWLYSSGSTGRPKGVVHLHADIYWTAELYARNVLGIRED-DVCFSAAKLFFAYGLGNSLTFPLSvgATTVLMPE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 338 VKTLTSSSVRncqgdLQEFKPTIMVGVAavwetvrkgilnqidnlpfltkkifwTAYNTKLNMQRLhipgggalgnlvfk 417
Cdd:cd05959 240 RPTPAAVFKR-----IRRYRPTVFFGVP--------------------------TLYAAMLAAPNL-------------- 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 418 kirTATGG-QLRYLLNGGSPISRDA-QEFITNLICPMLIGYGLTET----CASTtildPANFELGVAGDLTGCVTVKLVD 491
Cdd:cd05959 275 ---PSRDLsSLRLCVSAGEALPAEVgERWKARFGLDILDGIGSTEMlhifLSNR----PGRVRYGTTGKPVPGYEVELRD 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 492 vEELGYFAKNNQGEVWITGANVTPEYYKNEEETsqALTSDG-WFKTGDIGEWEANGHLKIIDRKKNLVKtMNGEYIALEK 570
Cdd:cd05959 348 -EDGGDVADGEPGELYVRGPSSATMYWNNRDKT--RDTFQGeWTRTGDKYVRDDDGFYTYAGRADDMLK-VSGIWVSPFE 423
|
490 500 510
....*....|....*....|....*....|....*
gi 398366229 571 LESVYRSNEYVANICVYA---DQSKTKPVGIIVPN 602
Cdd:cd05959 424 VESALVQHPAVLEAAVVGvedEDGLTKPKAFVVLR 458
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
237-558 |
7.57e-15 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 77.93 E-value: 7.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 237 TFSFDDILKLGK----ESCNEI--DVHPpgkDDLCCIMYTSGSTGEPKGVVLKHSNVvagvggasLNVLKFVGNT----- 305
Cdd:PRK08315 171 MLNFDELLALGRavddAELAARqaTLDP---DDPINIQYTSGTTGFPKGATLTHRNI--------LNNGYFIGEAmklte 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 306 -DRVICFLPLAHIFELVF-ELLSFYWGACI-----GYATVKTLTSssvrncqgdLQEFKPTIMVGVAavweTVRKGILNQ 378
Cdd:PRK08315 240 eDRLCIPVPLYHCFGMVLgNLACVTHGATMvypgeGFDPLATLAA---------VEEERCTALYGVP----TMFIAELDH 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 379 IDnlpfltkkiFwtaynTKLNMQRLhipgggalgnlvfkkiRTatggqlryllnG---GSPisrdaqefitnliCP---- 451
Cdd:PRK08315 307 PD---------F-----ARFDLSSL----------------RT-----------GimaGSP-------------CPievm 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 452 -----------MLIGYGLTETcaS-----TTILDPanFELGVA--GDLTGCVTVKLVDVEELGYFAKNNQGEVWITGANV 513
Cdd:PRK08315 333 krvidkmhmseVTIAYGMTET--SpvstqTRTDDP--LEKRVTtvGRALPHLEVKIVDPETGETVPRGEQGELCTRGYSV 408
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 398366229 514 TPEYYKNEEETSQALTSDGWFKTGDIGEWEANGHLKIIDRKKNLV 558
Cdd:PRK08315 409 MKGYWNDPEKTAEAIDADGWMHTGDLAVMDEEGYVNIVGRIKDMI 453
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
262-574 |
7.59e-15 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 77.92 E-value: 7.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 262 DDLCCIMYTSGSTGEPKGVVLKHSNVVAgvggASLNVLKFVG-NTDRVicFL---PLAHIFELVFELLSFYWGACigYAT 337
Cdd:PLN02860 172 DDAVLICFTSGTTGRPKGVTISHSALIV----QSLAKIAIVGyGEDDV--YLhtaPLCHIGGLSSALAMLMVGAC--HVL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 338 VKTLTSSSVRNCqgdLQEFKPTIMVGVAAVwetvrkgilnQIDNLPFLTKKIFWTayntklnmqrlhipgggalgnlVFK 417
Cdd:PLN02860 244 LPKFDAKAALQA---IKQHNVTSMITVPAM----------MADLISLTRKSMTWK----------------------VFP 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 418 KIRTatggqlryLLNGGSPISRDAQEFITNLI--CPMLIGYGLTETCASTTIL---DPANFELGVAGDLTG--------- 483
Cdd:PLN02860 289 SVRK--------ILNGGGSLSSRLLPDAKKLFpnAKLFSAYGMTEACSSLTFMtlhDPTLESPKQTLQTVNqtksssvhq 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 484 ----CVTVKLVDVE-ELGYFAKNNQGEVWITGANVTPEYYKNEEETSQALTSDGWFKTGDIGEWEANGHLKIIDRKKNLV 558
Cdd:PLN02860 361 pqgvCVGKPAPHVElKIGLDESSRVGRILTRGPHVMLGYWGQNSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRI 440
|
330
....*....|....*.
gi 398366229 559 KTmNGEYIALEKLESV 574
Cdd:PLN02860 441 KT-GGENVYPEEVEAV 455
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
253-558 |
1.99e-14 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 76.45 E-value: 1.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 253 EIDVHPPGKDDLCCIMYTSGSTGEPKGVVLKHSNVVAGvgGASLNVLKFVGNTDRVICFLPLAHIFELvfellsFYwgac 332
Cdd:PRK07514 147 DFETVPRGADDLAAILYTSGTTGRSKGAMLSHGNLLSN--ALTLVDYWRFTPDDVLIHALPIFHTHGL------FV---- 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 333 igyATVKTLTSssvrncqGD----LQEFKP----------TIMVGVAAVWetVRkgILNQidnlPFLTKKIfwTAyntkl 398
Cdd:PRK07514 215 ---ATNVALLA-------GAsmifLPKFDPdavlalmpraTVMMGVPTFY--TR--LLQE----PRLTREA--AA----- 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 399 NMqRLHIPGGGALGNLVFKKIRTATGGqlryllnggspisrdaqefitnlicPMLIGYGLTETCASTTilDPANFELgVA 478
Cdd:PRK07514 270 HM-RLFISGSAPLLAETHREFQERTGH-------------------------AILERYGMTETNMNTS--NPYDGER-RA 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 479 GD----LTGcVTVKLVDVEELGYFAKNNQGEVWITGANVTPEYYKNEEETSQALTSDGWFKTGDIGEWEANGHLKIIDRK 554
Cdd:PRK07514 321 GTvgfpLPG-VSLRVTDPETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGFFITGDLGKIDERGYVHIVGRG 399
|
....
gi 398366229 555 KNLV 558
Cdd:PRK07514 400 KDLI 403
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
263-586 |
3.78e-14 |
|
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341292 [Multi-domain] Cd Length: 333 Bit Score: 74.23 E-value: 3.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 263 DLCCIMYTSGSTGEPKGVVLKHSNVVAGvgGASLNVLKFVGNTDRVICFLPLAHIFELVFELLSFYWGAcigyATV---K 339
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIAA--NLQLIHAMGLTEADVYLNMLPLFHIAGLNLALATFHAGG----ANVvmeK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 340 TLTSSSVRncqgDLQEFKPTIMVGVAavwetvrkgilnqidnlPFLTkkifwtayntklNMQRLHIPGGGALGNLvfkki 419
Cdd:cd17637 75 FDPAEALE----LIEEEKVTLMGSFP-----------------PILS------------NLLDAAEKSGVDLSSL----- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 420 RTATGgqlrylLNGGSPISRdaqeFITnlICPM--LIGYGLTETCASTTiLDPANFELGVAGDLTGCVTVKLVDveELGY 497
Cdd:cd17637 117 RHVLG------LDAPETIQR----FEE--TTGAtfWSLYGQTETSGLVT-LSPYRERPGSAGRPGPLVRVRIVD--DNDR 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 498 FAKNNQ-GEVWITGANVTPEYYKNEEETSQAlTSDGWFKTGDIGEWEANGHLKIIDRK--KNLVKTmNGEYIALEKLESV 574
Cdd:cd17637 182 PVPAGEtGEIVVRGPLVFQGYWNLPELTAYT-FRNGWHHTGDLGRFDEDGYLWYAGRKpeKELIKP-GGENVYPAEVEKV 259
|
330
....*....|..
gi 398366229 575 YRSNEYVANICV 586
Cdd:cd17637 260 ILEHPAIAEVCV 271
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
262-613 |
6.43e-14 |
|
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: 74.42 E-value: 6.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 262 DDLCCIMYTSGSTGEPKGVVLKHSNVVAGVGGASLNVLKFVGNtDRVICflpLAHIFeLVFEL---LSFYW---GACI-- 333
Cdd:cd05919 91 DDIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMAREALGLTPG-DRVFS---SAKMF-FGYGLgnsLWFPLavgASAVln 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 334 -GYATVKTLTSSSVRncqgdlqeFKPTIMVGVAAVWETVRkgilnqidnlpfltkkifwtayntklnmqrlhipgggALG 412
Cdd:cd05919 166 pGWPTAERVLATLAR--------FRPTVLYGVPTFYANLL-------------------------------------DSC 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 413 NLVFKKIRTatggqLRYLLNGGSPISRD-AQEFITNLICPMLIGYGLTETCASTTILDPANFELGVAGDLTGCVTVKLVD 491
Cdd:cd05919 201 AGSPDALRS-----LRLCVSAGEALPRGlGERWMEHFGGPILDGIGATEVGHIFLSNRPGAWRLGSTGRPVPGYEIRLVD 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 492 veELGYFAK-NNQGEVWITGANVTPEYYKNEEETSQALtSDGWFKTGDIGEWEANGHLKIIDRKKNLVKtMNGEYIALEK 570
Cdd:cd05919 276 --EEGHTIPpGEEGDLLVRGPSAAVGYWNNPEKSRATF-NGGWYRTGDKFCRDADGWYTHAGRADDMLK-VGGQWVSPVE 351
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 398366229 571 LESVYRSNEYVANICVYA---DQSKTKPVGIIVPN--HAPLTKLAKKL 613
Cdd:cd05919 352 VESLIIQHPAVAEAAVVAvpeSTGLSRLTAFVVLKspAAPQESLARDI 399
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
256-577 |
2.01e-13 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 73.39 E-value: 2.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 256 VHPPGKDDLCCIMYTSGSTGEPKGVVLKHSNVVAGVGgaslnVLKFV-----GNTDrvicfLPlahifelVFELLSFYwG 330
Cdd:PRK09274 168 MADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIE-----ALREDygiepGEID-----LP-------TFPLFALF-G 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 331 ACIGYATVktltsssvrncqgdLQEFKPT--IMVGVAAVWETVRKgilNQIDNL---PFLTKKIfwTAYNTKLNMQrlhI 405
Cdd:PRK09274 230 PALGMTSV--------------IPDMDPTrpATVDPAKLFAAIER---YGVTNLfgsPALLERL--GRYGEANGIK---L 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 406 PGggalgnlvfkkirtatggqLRYLLNGGSPISRDAQEFITNLICP---MLIGYGLTE-----TCASTTILDPANF--EL 475
Cdd:PRK09274 288 PS-------------------LRRVISAGAPVPIAVIERFRAMLPPdaeILTPYGATEalpisSIESREILFATRAatDN 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 476 GvAGDLTG----CVTVKLV-----------DVEELgyfAKNNQGEVWITGANVTPEYYKNEEETSQALTSDG----WFKT 536
Cdd:PRK09274 349 G-AGICVGrpvdGVEVRIIaisdapipewdDALRL---ATGEIGEIVVAGPMVTRSYYNRPEATRLAKIPDGqgdvWHRM 424
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 398366229 537 GDIGEWEANGHLKIIDRKKNLVKTMNGEY--IALEK----LESVYRS 577
Cdd:PRK09274 425 GDLGYLDAQGRLWFCGRKAHRVETAGGTLytIPCERifntHPGVKRS 471
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
257-586 |
2.13e-13 |
|
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: 73.00 E-value: 2.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 257 HPPGKDDLCCIMYTSGSTGEPKGVVLKHSNVVAGVGGASlnvlkFVGNT--DRVICFLPLAhiFE-LVFELlsfyWGACI 333
Cdd:cd12117 131 VPVSPDDLAYVMYTSGSTGRPKGVAVTHRGVVRLVKNTN-----YVTLGpdDRVLQTSPLA--FDaSTFEI----WGALL 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 334 GYATVKTLTSSSVRncqgDLQEFKptimvgvaavwETVRKgilNQIDNLpFLTKKIFwtayntklnmqrlhipgggalgN 413
Cdd:cd12117 200 NGARLVLAPKGTLL----DPDALG-----------ALIAE---EGVTVL-WLTAALF----------------------N 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 414 LVFKKIRTATGGqLRYLLNGGSPIS----RDAqefitNLICP---MLIGYGLTETCASTT---ILDPANFELGVA-GDLT 482
Cdd:cd12117 239 QLADEDPECFAG-LRELLTGGEVVSpphvRRV-----LAACPglrLVNGYGPTENTTFTTshvVTELDEVAGSIPiGRPI 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 483 GCVTVKLVDveelgyfaKNNQ-------GEVWITGANVTPEYYKNEEETSQALTSDGW------FKTGDIGEWEANGHLK 549
Cdd:cd12117 313 ANTRVYVLD--------EDGRpvppgvpGELYVGGDGLALGYLNRPALTAERFVADPFgpgerlYRTGDLARWLPDGRLE 384
|
330 340 350
....*....|....*....|....*....|....*..
gi 398366229 550 IIDRKKNLVKtMNGEYIALEKLESVYRSNEYVANICV 586
Cdd:cd12117 385 FLGRIDDQVK-IRGFRIELGEIEAALRAHPGVREAVV 420
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
262-613 |
3.17e-13 |
|
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: 72.47 E-value: 3.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 262 DDLCCIMYTSGSTGEPKGVVLKHSNVVAGVGGASLNVlkFVGNTDRVICFLPLAhiFELVFELL--SFYWGACIGYATVK 339
Cdd:cd17644 106 ENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEY--GITSSDRVLQFASIA--FDVAAEEIyvTLLSGATLVLRPEE 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 340 TLTSS-SVRNCqgdLQEFKPTIMVGVAAVW-ETVRKGILNQIDNLPFLtkkifwtayntklnmqRLHIPGGGALGNLVFK 417
Cdd:cd17644 182 MRSSLeDFVQY---IQQWQLTVLSLPPAYWhLLVLELLLSTIDLPSSL----------------RLVIVGGEAVQPELVR 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 418 KIRTATGGQLRyLLNGGSP-----------ISRDAQEFITNLicpmLIGYGLTETcaSTTILDPanfelgvagdltgcvT 486
Cdd:cd17644 243 QWQKNVGNFIQ-LINVYGPteatiaatvcrLTQLTERNITSV----PIGRPIANT--QVYILDE---------------N 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 487 VKLVDVEelgyfaknNQGEVWITGANVTPEYYKNEEETSQALTSDGW--------FKTGDIGEWEANGHLKIIDRKKNLV 558
Cdd:cd17644 301 LQPVPVG--------VPGELHIGGVGLARGYLNRPELTAEKFISHPFnsseserlYKTGDLARYLPDGNIEYLGRIDNQV 372
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 398366229 559 KtMNGEYIALEKLESVYRSNEYVANICVYA--DQSKTKP-VGIIVPnHAPLTKLAKKL 613
Cdd:cd17644 373 K-IRGFRIELGEIEAVLSQHNDVKTAVVIVreDQPGNKRlVAYIVP-HYEESPSTVEL 428
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
101-586 |
3.48e-13 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 72.76 E-value: 3.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 101 SFDQLTDIMHEIGRGLVKIGLKPNDddKLHLYAATSHKWMKMFLGAQSQGIPVVTAYDTLGEKGLIHSLVQTGSKAIFTD 180
Cdd:PRK06710 51 TFSVFHDKVKRFANYLQKLGVEKGD--RVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 181 NSLLPSlIKPVQAAQDVKYIIhfdsissedrrqsgkiyqsahdaINRIKEVRPDIKTFSFDDILK--------------- 245
Cdd:PRK06710 129 DLVFPR-VTNVQSATKIEHVI-----------------------VTRIADFLPFPKNLLYPFVQKkqsnlvvkvseseti 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 246 -----LGKESCNEIDVHPPGKDDLCCIMYTSGSTGEPKGVVLKHSNVVAGVGGASLNVLKFVGNTDRVICFLPLAHIFel 320
Cdd:PRK06710 185 hlwnsVEKEVNTGVEVPCDPENDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYNCKEGEEVVLGVLPFFHVY-- 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 321 vfellsfywgaciGYATVKTLTSssvrncqgdLQEFKPTIM--VGVAAVWETVRKGILNQIDNLPfltkkifwTAYNTKL 398
Cdd:PRK06710 263 -------------GMTAVMNLSI---------MQGYKMVLIpkFDMKMVFEAIKKHKVTLFPGAP--------TIYIALL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 399 NMQRLhipgggalgnlvfKKIRTATggqLRYLLNGGSPISRDAQEFITNLICPMLI-GYGLTETCASTTildpANF---- 473
Cdd:PRK06710 313 NSPLL-------------KEYDISS---IRACISGSAPLPVEVQEKFETVTGGKLVeGYGLTESSPVTH----SNFlwek 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 474 ----ELGVAGDLTGCVTVKLVDVEELgyfAKNNQGEVWITGANVTPEYYKNEEETSqALTSDGWFKTGDIGEWEANGHLK 549
Cdd:PRK06710 373 rvpgSIGVPWPDTEAMIMSLETGEAL---PPGEIGEIVVKGPQIMKGYWNKPEETA-AVLQDGWLHTGDVGYMDEDGFFY 448
|
490 500 510
....*....|....*....|....*....|....*..
gi 398366229 550 IIDRKKNLVkTMNGEYIALEKLESVYRSNEYVANICV 586
Cdd:PRK06710 449 VKDRKKDMI-VASGFNVYPREVEEVLYEHEKVQEVVT 484
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
260-542 |
6.23e-13 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 71.83 E-value: 6.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 260 GKDDLCCIMYTSGSTGEPKGVVLKHSNVVAgVGGASLNVLKFVGNTDRVI-CFLPLAHIFELVFEL-LSFYWGACI---- 333
Cdd:PRK08180 207 GPDTIAKFLFTSGSTGLPKAVINTHRMLCA-NQQMLAQTFPFLAEEPPVLvDWLPWNHTFGGNHNLgIVLYNGGTLyidd 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 334 GYATVKtLTSSSVRNcqgdLQEFKPTIMVGVAAVWETVrkgilnqidnLPFLTKKifwtayntklnmqrlhipggGALGN 413
Cdd:PRK08180 286 GKPTPG-GFDETLRN----LREISPTVYFNVPKGWEML----------VPALERD--------------------AALRR 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 414 LVFKKirtatggqLRYLLNGGSPISRD--------AQEFITNLIcPMLIGYGLTETCASTTIldpANFELGVAGD----L 481
Cdd:PRK08180 331 RFFSR--------LKLLFYAGAALSQDvwdrldrvAEATCGERI-RMMTGLGMTETAPSATF---TTGPLSRAGNiglpA 398
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398366229 482 TGCvTVKLVDVEelGYFaknnqgEVWITGANVTPEYYKNEEETSQALTSDGWFKTGDIGEW 542
Cdd:PRK08180 399 PGC-EVKLVPVG--GKL------EVRVKGPNVTPGYWRAPELTAEAFDEEGYYRSGDAVRF 450
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
238-574 |
1.23e-12 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.
Pssm-ID: 341283 [Multi-domain] Cd Length: 486 Bit Score: 70.79 E-value: 1.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 238 FSFDDILKLGKEScneIDVHPP-GKDDLCCIMYTSGSTGEPKGVVLKHSnvvagvgGASLNVLKFV-----GNTDRVICF 311
Cdd:cd12118 111 FEYEDLLAEGDPD---FEWIPPaDEWDPIALNYTSGTTGRPKGVVYHHR-------GAYLNALANIlewemKQHPVYLWT 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 312 LPLAHifelvfellsfywgaCIGYATVKTLTSSSVRN-CqgdLQEFKPTimvgvaAVWETVRKGILNQIDNLPfltkkif 390
Cdd:cd12118 181 LPMFH---------------CNGWCFPWTVAAVGGTNvC---LRKVDAK------AIYDLIEKHKVTHFCGAP------- 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 391 wTAYNTKLNMQ---RLHIPGggalgnlvfkKIRTATGGqlryllnggSPISRDAQEFITNLICPMLIGYGLTETCASTTI 467
Cdd:cd12118 230 -TVLNMLANAPpsdARPLPH----------RVHVMTAG---------APPPAAVLAKMEELGFDVTHVYGLTETYGPATV 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 468 ---------LDPA-----NFELGVAGDLTGCVTVklVDVEELGYFAKNNQ--GEVWITGANVTPEYYKNEEETSQALtSD 531
Cdd:cd12118 290 cawkpewdeLPTEerarlKARQGVRYVGLEEVDV--LDPETMKPVPRDGKtiGEIVFRGNIVMKGYLKNPEATAEAF-RG 366
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 398366229 532 GWFKTGDIGEWEANGHLKIIDRKKNLVKTmNGEYIALEKLESV 574
Cdd:cd12118 367 GWFHSGDLAVIHPDGYIEIKDRSKDIIIS-GGENISSVEVEGV 408
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
101-553 |
1.64e-12 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 70.53 E-value: 1.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 101 SFDQLTDIMHEIGRGLVKIGLKPndDDKLHLYaatshkwMKM-------FLGAQSQGIPVVTAYDTLGEKGLIHSLVQTG 173
Cdd:COG0365 41 TYAELRREVNRFANALRALGVKK--GDRVAIY-------LPNipeaviaMLACARIGAVHSPVFPGFGAEALADRIEDAE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 174 SKAIFTDNSLL----PSLIKP-----VQAAQDVKYIIHFDSISSEDRRQsgkiyqsahdainrikevrpdiKTFSFDDIL 244
Cdd:COG0365 112 AKVLITADGGLrggkVIDLKEkvdeaLEELPSLEHVIVVGRTGADVPME----------------------GDLDWDELL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 245 KLGKESCNEIDVHPpgkDDLCCIMYTSGSTGEPKGVVLKHSNVVAGVGGASLNVLKfVGNTDRVICFLPLA----HIFEL 320
Cdd:COG0365 170 AAASAEFEPEPTDA---DDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVLD-LKPGDVFWCTADIGwatgHSYIV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 321 VFELLSfywGACI-------GYATVKTLTSssvrncqgDLQEFKPTIMVGVAAVWETVRKgilnqidnlpfltkkifwta 393
Cdd:COG0365 246 YGPLLN---GATVvlyegrpDFPDPGRLWE--------LIEKYGVTVFFTAPTAIRALMK-------------------- 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 394 yntklnmqrlhipgggaLGNLVFKKIRTATggqLRYLLNGGSPISRDAQEFITNLI-CPMLIGYGLTETC---ASTTILD 469
Cdd:COG0365 295 -----------------AGDEPLKKYDLSS---LRLLGSAGEPLNPEVWEWWYEAVgVPIVDGWGQTETGgifISNLPGL 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 470 PAnfelgVAGDLTGCV---TVKLVDveELGYFAKNNQ-GEVWITGAN--VTPEYYKNEEETSQAL--TSDGWFKTGDIGE 541
Cdd:COG0365 355 PV-----KPGSMGKPVpgyDVAVVD--EDGNPVPPGEeGELVIKGPWpgMFRGYWNDPERYRETYfgRFPGWYRTGDGAR 427
|
490
....*....|..
gi 398366229 542 WEANGHLKIIDR 553
Cdd:COG0365 428 RDEDGYFWILGR 439
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
262-577 |
1.74e-12 |
|
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: 70.26 E-value: 1.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 262 DDLCCIMYTSGSTGEPKGVVLKHSNVVAGVGgaSLNVLKFVGNTDRVICFLPLA---HIFELVFELLSfywGACIGyatv 338
Cdd:cd05918 106 SDAAYVIFTSGSTGKPKGVVIEHRALSTSAL--AHGRALGLTSESRVLQFASYTfdvSILEIFTTLAA---GGCLC---- 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 339 ktLTSSSVR--NCQGDLQEFKPTIMVGVAAVwetvrkgiLNQID--NLPFLtkkifwtayntklnmQRLhIPGGGALGNL 414
Cdd:cd05918 177 --IPSEEDRlnDLAGFINRLRVTWAFLTPSV--------ARLLDpeDVPSL---------------RTL-VLGGEALTQS 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 415 VfkkirTATGGQLRYLLNGGSP----ISRDAQEfITNLICPMLIGYGLtetCASTTILDPANFELGVAgdlTGCVtvklv 490
Cdd:cd05918 231 D-----VDTWADRVRLINAYGPaectIAATVSP-VVPSTDPRNIGRPL---GATCWVVDPDNHDRLVP---IGAV----- 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 491 dveelgyfaknnqGEVWITGANVTPEYYKNEEETSQALTSD-GW------------FKTGDIGEWEANGHLKIIDRKKNL 557
Cdd:cd05918 294 -------------GELLIEGPILARGYLNDPEKTAAAFIEDpAWlkqegsgrgrrlYRTGDLVRYNPDGSLEYVGRKDTQ 360
|
330 340
....*....|....*....|
gi 398366229 558 VKtMNGEYIALEKLESVYRS 577
Cdd:cd05918 361 VK-IRGQRVELGEIEHHLRQ 379
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
262-553 |
1.75e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 70.46 E-value: 1.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 262 DDLCCIMYTSGSTGEPKGVVLKHSNVVAGVGGASLNVLKFVGNTDRVICFLPLAHifelvfellsfywGACI-------- 333
Cdd:PRK07470 163 DDPCWFFFTSGTTGRPKAAVLTHGQMAFVITNHLADLMPGTTEQDASLVVAPLSH-------------GAGIhqlcqvar 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 334 GYATVktLTSSsvrncqgdlQEFKPtimvgvAAVWETVRKgilNQIDNLpFLTKKIfwtayntkLNMQRLHipgggalgn 413
Cdd:PRK07470 230 GAATV--LLPS---------ERFDP------AEVWALVER---HRVTNL-FTVPTI--------LKMLVEH--------- 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 414 lvfKKIRTATGGQLRYLLNGGSPISRDAQEFITNLICPMLIGY-GLTETCASTTILDPA--------NFELGVAG-DLTG 483
Cdd:PRK07470 272 ---PAVDRYDHSSLRYVIYAGAPMYRADQKRALAKLGKVLVQYfGLGEVTGNITVLPPAlhdaedgpDARIGTCGfERTG 348
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398366229 484 cVTVKLVDVE--ELGYFAKnnqGEVWITGANVTPEYYKNEEETSQALtSDGWFKTGDIGEWEANGHLKIIDR 553
Cdd:PRK07470 349 -MEVQIQDDEgrELPPGET---GEICVIGPAVFAGYYNNPEANAKAF-RDGWFRTGDLGHLDARGFLYITGR 415
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
258-605 |
1.96e-12 |
|
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: 70.01 E-value: 1.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 258 PPGKDDLCCIMYTSGSTGEPKGVVLKHSNVVAGVggASLNVLKFVGNTDRVICFLPLA---HIFELVFELLSfywGACIG 334
Cdd:cd12116 122 PVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFL--HSMRERLGLGPGDRLLAVTTYAfdiSLLELLLPLLA---GARVV 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 335 YAtvKTLTSSSVRNCQGDLQEFKPTIMVGVAAVWetvrkgilnqidnlpfltkKIFWTAyntklnmqrlhipGGGALGNL 414
Cdd:cd12116 197 IA--PRETQRDPEALARLIEAHSITVMQATPATW-------------------RMLLDA-------------GWQGRAGL 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 415 VfkkirtatggqlryLLNGGSPISRD-AQEFI------TNLicpmligYGLTETC--ASTTILDPANFELGVAGDLTGcV 485
Cdd:cd12116 243 T--------------ALCGGEALPPDlAARLLsrvgslWNL-------YGPTETTiwSTAARVTAAAGPIPIGRPLAN-T 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 486 TVKLVDvEELGYFAKNNQGEVWITGANVTPEYYKNEEETSQALTSDG-------WFKTGDIGEWEANGHLKIIDRKKNLV 558
Cdd:cd12116 301 QVYVLD-AALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPfagpgsrLYRTGDLVRRRADGRLEYLGRADGQV 379
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 398366229 559 KtMNGEYIALEKLESVYRSNEYVANICV--YADQSKTKPVGIIVPNHAP 605
Cdd:cd12116 380 K-IRGHRIELGEIEAALAAHPGVAQAAVvvREDGGDRRLVAYVVLKAGA 427
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
262-613 |
4.74e-12 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 68.65 E-value: 4.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 262 DDLCCIMYTSGSTGEPKGVVLKHSNVVAGVGG-----------------ASLNVLKFVGNTDRVICFLPLAHIF--ELVF 322
Cdd:cd17650 93 EDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAwrreyeldsfpvrllqmASFSFDVFAGDFARSLLNGGTLVICpdEVKL 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 323 ELLSFYwgacigyatvKTLTSSSVrncqgDLQEFKPTIMVGVAAvwETVRKGIlnqidNLPFLtkkifwtayntklnmqR 402
Cdd:cd17650 173 DPAALY----------DLILKSRI-----TLMESTPALIRPVMA--YVYRNGL-----DLSAM----------------R 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 403 LHIPGGGALGNLVFKKIRTATGGQLRyllnggspisrdaqefITNlicpmliGYGLTETCASTTIldpanFELGVAGDLT 482
Cdd:cd17650 215 LLIVGSDGCKAQDFKTLAARFGQGMR----------------IIN-------SYGVTEATIDSTY-----YEEGRDPLGD 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 483 GC----------VTVKLVDvEELGYFAKNNQGEVWITGANVTPEYYKNEEETSQALTSDGW------FKTGDIGEWEANG 546
Cdd:cd17650 267 SAnvpigrplpnTAMYVLD-ERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFapgermYRTGDLARWRADG 345
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398366229 547 HLKIIDRKKNLVKtMNGEYIALEKLESVYRSNEYVANICVYADQSKTKP---VGIIVPNHAPLTK-----LAKKL 613
Cdd:cd17650 346 NVELLGRVDHQVK-IRGFRIELGEIESQLARHPAIDEAVVAVREDKGGEarlCAYVVAAATLNTAelrafLAKEL 419
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
241-602 |
8.01e-12 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 68.27 E-value: 8.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 241 DDILKLGKESCNEIDVHPP---GKDDLCCIMYTSGSTGEPKGVVLKHSNVVagvgGASLNVLKFVG---NTDRVICFLPL 314
Cdd:PRK07786 150 DSVLGYEDLLAEAGPAHAPvdiPNDSPALIMYTSGTTGRPKGAVLTHANLT----GQAMTCLRTNGadiNSDVGFVGVPL 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 315 AHIFELVfellSFYWGACIGYATVKTltsssvrncqgDLQEFKPTIMVGVaavWETVR-KGIlnqidnlpFLTKkIFWTA 393
Cdd:PRK07786 226 FHIAGIG----SMLPGLLLGAPTVIY-----------PLGAFDPGQLLDV---LEAEKvTGI--------FLVP-AQWQA 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 394 YntkLNMQRlhiPGGGALgnlvfkkirtatggQLRYLLNGGSPIS-----RDAQEFITNLIcpmLIGYGLTETCASTTIL 468
Cdd:PRK07786 279 V---CAEQQ---ARPRDL--------------ALRVLSWGAAPASdtllrQMAATFPEAQI---LAAFGQTEMSPVTCML 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 469 D--PANFELGVAGDLTGCVTVKLVDvEELGYFAKNNQGEVWITGANVTPEYYKNEEETSQALTSdGWFKTGDIGEWEANG 546
Cdd:PRK07786 336 LgeDAIRKLGSVGKVIPTVAARVVD-ENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAG-GWFHSGDLVRQDEEG 413
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 398366229 547 HLKIIDRKKNLVKTmNGEYIALEKLESVYRSNEYVANICVY--ADQSKTK-PVGIIVPN 602
Cdd:PRK07786 414 YVWVVDRKKDMIIS-GGENIYCAEVENVLASHPDIVEVAVIgrADEKWGEvPVAVAAVR 471
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
253-559 |
3.83e-11 |
|
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: 66.80 E-value: 3.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 253 EIDVHPpgkDDLCCIMYTSGSTGEPKGVVLKHSNVVagvggaslNVLKF------VGNTDRVICFLPLAhiFEL-VFELl 325
Cdd:COG1020 611 PVPVTP---DDLAYVIYTSGSTGRPKGVMVEHRALV--------NLLAWmqrrygLGPGDRVLQFASLS--FDAsVWEI- 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 326 sfyWGA-CIGyATVKTLTSSSVRNCQG---DLQEFKPTIMVGVAAVWETVrkgilnqIDNLPfltkkifwtayntklnmq 401
Cdd:COG1020 677 ---FGAlLSG-ATLVLAPPEARRDPAAlaeLLARHRVTVLNLTPSLLRAL-------LDAAP------------------ 727
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 402 rlhipgggalgnlvfkkirtATGGQLRYLLNGGSPISRD-AQEFITNLICPMLI-GYGLTET--CASTTILDPANFELG- 476
Cdd:COG1020 728 --------------------EALPSLRLVLVGGEALPPElVRRWRARLPGARLVnLYGPTETtvDSTYYEVTPPDADGGs 787
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 477 ------VAGdltgcVTVKLVDveelgyfaKNNQ-------GEVWITGANVTPEYYKNEEETSQA-----LTSDG--WFKT 536
Cdd:COG1020 788 vpigrpIAN-----TRVYVLD--------AHLQpvpvgvpGELYIGGAGLARGYLNRPELTAERfvadpFGFPGarLYRT 854
|
330 340
....*....|....*....|...
gi 398366229 537 GDIGEWEANGHLKIIDRKKNLVK 559
Cdd:COG1020 855 GDLARWLPDGNLEFLGRADDQVK 877
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
262-573 |
4.34e-11 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 66.53 E-value: 4.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 262 DDLCCIMYTSGSTGEPKGVVLKHSNVVAGVGGASlNVLKFvGNTDRVICFLPLAHIFEL----VFELLS----FYWGACI 333
Cdd:PRK06814 793 DDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVA-ARIDF-SPEDKVFNALPVFHSFGLtgglVLPLLSgvkvFLYPSPL 870
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 334 GYATVKTLTSSSvrncqgdlqefKPTIMVGVaavwETvrkgilnqidnlpFLTkkifwtayntklnmqrlhipgGGAlgn 413
Cdd:PRK06814 871 HYRIIPELIYDT-----------NATILFGT----DT-------------FLN---------------------GYA--- 898
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 414 lvfkkiRTATG---GQLRYLLNGGSPIsRDA--QEFITNLICPMLIGYGLTETCASTTILDPANFELGVAGDLTGCVTVK 488
Cdd:PRK06814 899 ------RYAHPydfRSLRYVFAGAEKV-KEEtrQTWMEKFGIRILEGYGVTETAPVIALNTPMHNKAGTVGRLLPGIEYR 971
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 489 LVDVEELgyfakNNQGEVWITGANVTPEYYKNEEETSQALTSDGWFKTGDIGEWEANGHLKIIDRKKNLVKtMNGEYIAL 568
Cdd:PRK06814 972 LEPVPGI-----DEGGRLFVRGPNVMLGYLRAENPGVLEPPADGWYDTGDIVTIDEEGFITIKGRAKRFAK-IAGEMISL 1045
|
....*
gi 398366229 569 EKLES 573
Cdd:PRK06814 1046 AAVEE 1050
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
101-538 |
7.31e-11 |
|
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: 65.15 E-value: 7.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 101 SFDQLTDIMHEIGRGLVKIGLKPndDDKLHLYAATSHKWMKMFLGAQSQGIP---VVTAYDTLGekglihslvqtgskai 177
Cdd:cd05921 27 TYAEALRQVRAIAQGLLDLGLSA--ERPLLILSGNSIEHALMALAAMYAGVPaapVSPAYSLMS---------------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 178 fTDNSLLPSLIKPVQAAqdVKYIihfdsissedrrQSGKIYQSAHDAINR-------IKEVRPDIKTFSFDDILKL--GK 248
Cdd:cd05921 89 -QDLAKLKHLFELLKPG--LVFA------------QDAAPFARALAAIFPlgtplvvSRNAVAGRGAISFAELAATppTA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 249 ESCNEIDVHPPgkDDLCCIMYTSGSTGEPKGVVLKHSNVvAGVGGASLNVLKFVGNTDRVIC-FLPLAHIF--ELVFELL 325
Cdd:cd05921 154 AVDAAFAAVGP--DTVAKFLFTSGSTGLPKAVINTQRML-CANQAMLEQTYPFFGEEPPVLVdWLPWNHTFggNHNFNLV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 326 -----SFYWGAciGYATvKTLTSSSVRNcqgdLQEFKPTIMVGVAAVWETvrkgILNQIDNLPFLTKKIFwtayntklnm 400
Cdd:cd05921 231 lynggTLYIDD--GKPM-PGGFEETLRN----LREISPTVYFNVPAGWEM----LVAALEKDEALRRRFF---------- 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 401 qrlhipgggalgnlvfkkirtatgGQLRYLLNGGSPISRDAQEFITNLI-------CPMLIGYGLTETCASTTILDPANF 473
Cdd:cd05921 290 ------------------------KRLKLMFYAGAGLSQDVWDRLQALAvatvgerIPMMAGLGATETAPTATFTHWPTE 345
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398366229 474 ELGVAGDLTGCVTVKLVDVeelgyfakNNQGEVWITGANVTPEYYKNEEETSQALTSDGWFKTGD 538
Cdd:cd05921 346 RSGLIGLPAPGTELKLVPS--------GGKYEVRVKGPNVTPGYWRQPELTAQAFDEEGFYCLGD 402
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
183-607 |
2.39e-10 |
|
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: 63.30 E-value: 2.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 183 LLPSLIKPVQAAQDVKYIIHFDSISSEDRRQSGKIYQSAHDAINRIKEVRPDIKTfsfddilklgKESCNE---IDVHPP 259
Cdd:cd05923 78 AVPALINPRLKAAELAELIERGEMTAAVIAVDAQVMDAIFQSGVRVLALSDLVGL----------GEPESAgplIEDPPR 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 260 GKDDLCCIMYTSGSTGEPKGVVLKHSNVVAGVGGASLNVLKFVGNTDRVICFLPLAHIFElVFELLSfywGACIGYATVK 339
Cdd:cd05923 148 EPEQPAFVFYTSGTTGLPKGAVIPQRAAESRVLFMSTQAGLRHGRHNVVLGLMPLYHVIG-FFAVLV---AALALDGTYV 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 340 TLTSSSVRNCQGDLQEFKPTIMVGVAAVWETVRKGILNQIDNLPFLTKKIFwtayntklnmqrlhipGGGALGNLVFKKI 419
Cdd:cd05923 224 VVEEFDPADALKLIEQERVTSLFATPTHLDALAAAAEFAGLKLSSLRHVTF----------------AGATMPDAVLERV 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 420 RTATGGQlryllnggspisrdaqefITNLicpmligYGLTETCASTTILDPANFELGVAG--------DLTGCVTVKLVD 491
Cdd:cd05923 288 NQHLPGE------------------KVNI-------YGTTEAMNSLYMRDARTGTEMRPGffsevrivRIGGSPDEALAN 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 492 VEElgyfaknnqGEVWIT-GANVTPEYYKNEEETSQALTSDGWFKTGDIGEWEANGHLKIIDRKKNLVKTmNGEYIALEK 570
Cdd:cd05923 343 GEE---------GELIVAaAADAAFTGYLNQPEATAKKLQDGWYRTGDVGYVDPSGDVRILGRVDDMIIS-GGENIHPSE 412
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 398366229 571 LESVYRSNEYVANICV--YADQSKTKPV-GIIVPNHAPLT 607
Cdd:cd05923 413 IERVLSRHPGVTEVVVigVADERWGQSVtACVVPREGTLS 452
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
241-589 |
3.24e-10 |
|
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: 63.13 E-value: 3.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 241 DDILKLGKESCNEIDVhPPGKDDLCCIMYTSGSTGEPKGVVLKHSNVVAGVggASLNVLKFVGNTDRVICFLPLAhiFEL 320
Cdd:cd17651 116 LDQPGAAAGADAEPDP-ALDADDLAYVIYTSGSTGRPKGVVMPHRSLANLV--AWQARASSLGPGARTLQFAGLG--FDV 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 321 VFELLsfyWGACIGYATVkTLTSSSVRNcqgDLQEFkptimvgvAAVWETVRkgiLNQIDnLPFLtkkifwtayntklnM 400
Cdd:cd17651 191 SVQEI---FSTLCAGATL-VLPPEEVRT---DPPAL--------AAWLDEQR---ISRVF-LPTV--------------A 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 401 QRLHIPGGGALGnlvfkkirtATGGQLRYLLNGGSPISRDA--QEFITNLICPMLI-GYGLTETCASTTILDPANF---- 473
Cdd:cd17651 238 LRALAEHGRPLG---------VRLAALRYLLTGGEQLVLTEdlREFCAGLPGLRLHnHYGPTETHVVTALSLPGDPaawp 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 474 ELGVAGDLTGCVTVKLVDvEELGYFAKNNQGEVWITGANVTPEYYKNEEETSQALTSDGW------FKTGDIGEWEANGH 547
Cdd:cd17651 309 APPPIGRPIDNTRVYVLD-AALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFvpgarmYRTGDLARWLPDGE 387
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 398366229 548 LKIIDRKKNLVKtMNGEYIALEKLESVYRSNEYVANICVYAD 589
Cdd:cd17651 388 LEFLGRADDQVK-IRGFRIELGEIEAALARHPGVREAVVLAR 428
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
175-619 |
3.50e-10 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 62.85 E-value: 3.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 175 KAIFTDNSLLPSLIKPVQAAQDVK-YIIHFDSISSEDRRQSGKIyqsAHDAInrIKEVRPDIKTFSFDDilklgkescne 253
Cdd:PRK06018 113 RVVITDLTFVPILEKIADKLPSVErYVVLTDAAHMPQTTLKNAV---AYEEW--IAEADGDFAWKTFDE----------- 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 254 idvhppgkDDLCCIMYTSGSTGEPKGVVLKH-SNVVAGVGGASLNVLKfVGNTDRVICFLPLAHifelvfellSFYWGac 332
Cdd:PRK06018 177 --------NTAAGMCYTSGTTGDPKGVLYSHrSNVLHALMANNGDALG-TSAADTMLPVVPLFH---------ANSWG-- 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 333 IGYATVKTLTSSSVRNCQGD-------LQEFKPTIMVGVAAVWETVrkgilnqidnLPFLTKkifwtayntklnmQRLHI 405
Cdd:PRK06018 237 IAFSAPSMGTKLVMPGAKLDgasvyelLDTEKVTFTAGVPTVWLML----------LQYMEK-------------EGLKL 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 406 PgggalgnlvfkkirtatggQLRYLLNGGSPISRDAQEFITNLICPMLIGYGLTETCASTTI--LDPANFELGVAGDLTG 483
Cdd:PRK06018 294 P-------------------HLKMVVCGGSAMPRSMIKAFEDMGVEVRHAWGMTEMSPLGTLaaLKPPFSKLPGDARLDV 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 484 ---------CVTVKLVDVE--ELGYFAKNNqGEVWITGANVTPEYYKNEEETsqaLTSDGWFKTGDIGEWEANGHLKIID 552
Cdd:PRK06018 355 lqkqgyppfGVEMKITDDAgkELPWDGKTF-GRLKVRGPAVAAAYYRVDGEI---LDDDGFFDTGDVATIDAYGYMRITD 430
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 553 RKKNLVKTmNGEYIALEKLESVYRSNEYVAN---ICVYADQSKTKPVGIIVPNHAPLTKLAKKLGIMEQK 619
Cdd:PRK06018 431 RSKDVIKS-GGEWISSIDLENLAVGHPKVAEaavIGVYHPKWDERPLLIVQLKPGETATREEILKYMDGK 499
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
259-601 |
4.61e-10 |
|
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: 62.48 E-value: 4.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 259 PGKDDLCCIMYTSGSTGEPKGVVLKHSNVVAGVggASLNVLKFVGNTDRVI-CFLPlahifelvFELLsfywGACIGYAT 337
Cdd:cd05910 82 PKADEPAAILFTSGSTGTPKGVVYRHGTFAAQI--DALRQLYGIRPGEVDLaTFPL--------FALF----GPALGLTS 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 338 V------KTLTSSSVRNCQGDLQEFKPTIMVGVAAVWETV-RKGILNQIdNLPFLTKKIfwtayntklnmqrlhipGGGA 410
Cdd:cd05910 148 VipdmdpTRPARADPQKLVGAIRQYGVSIVFGSPALLERVaRYCAQHGI-TLPSLRRVL-----------------SAGA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 411 lgnlvfkKIRTATGGQLRYLLNGGSPIsrdaqefitnlicpmLIGYGLTETCASTTILDPANFEL------GVAGDLTGC 484
Cdd:cd05910 210 -------PVPIALAARLRKMLSDEAEI---------------LTPYGATEALPVSSIGSRELLATttaatsGGAGTCVGR 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 485 ----VTVKLVDVEELGYFAKNNQ--------GEVWITGANVTPEYYKNEEETSQALTSDG----WFKTGDIGEWEANGHL 548
Cdd:cd05910 268 pipgVRVRIIEIDDEPIAEWDDTlelprgeiGEITVTGPTVTPTYVNRPVATALAKIDDNsegfWHRMGDLGYLDDEGRL 347
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 398366229 549 KIIDRKKNLVKTMNGEYIAlEKLESVYRSNEYVAnicvyadqsKTKPVGIIVP 601
Cdd:cd05910 348 WFCGRKAHRVITTGGTLYT-EPVERVFNTHPGVR---------RSALVGVGKP 390
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
111-572 |
1.23e-09 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 61.17 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 111 EIGRGLVKIGLKPNDddKLHLYAATSHKWMKMFLGAQSQG-----IPVVTAYdtlgekglihslvqtGSKAIFTDNslLP 185
Cdd:PRK09192 61 AGARRLLALGLKPGD--RVALIAETDGDFVEAFFACQYAGlvpvpLPLPMGF---------------GGRESYIAQ--LR 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 186 SLIKPVQAAqdvkYIIHFDSISsedrrqsgkiyqsahDAINRIKEVRPDIKTFSFDDiLKLGKEScnEIDVHPPGKDDLC 265
Cdd:PRK09192 122 GMLASAQPA----AIITPDELL---------------PWVNEATHGNPLLHVLSHAW-FKALPEA--DVALPRPTPDDIA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 266 CIMYTSGSTGEPKGVVLKHSNVVAGVGGASLNVLKfVGNTDRVICFLPLAHIFELVFELLSfywgacigyatvkTLTSS- 344
Cdd:PRK09192 180 YLQYSSGSTRFPRGVIITHRALMANLRAISHDGLK-VRPGDRCVSWLPFYHDMGLVGFLLT-------------PVATQl 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 345 SVrncqgDL---QEF--KPTimvgvaaVWetvrkgiLNQID--------NLPF---LTKKIFWTAYNTKLNMQRLHIPGG 408
Cdd:PRK09192 246 SV-----DYlptRDFarRPL-------QW-------LDLISrnrgtisySPPFgyeLCARRVNSKDLAELDLSCWRVAGI 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 409 GAlgnlvfKKIRTatgGQLRYLLNGGSPISRDAQEFitnlicpmLIGYGLTETCASTTILDPAnfelgvagdlTGcVTVK 488
Cdd:PRK09192 307 GA------DMIRP---DVLHQFAEAFAPAGFDDKAF--------MPSYGLAEATLAVSFSPLG----------SG-IVVE 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 489 LVDVEELGY----------------FAKNNQ----------------------GEVWITGANVTPEYYkNEEETSQALTS 530
Cdd:PRK09192 359 EVDRDRLEYqgkavapgaetrrvrtFVNCGKalpgheieirneagmplpervvGHICVRGPSLMSGYF-RDEESQDVLAA 437
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 398366229 531 DGWFKTGDIGeWEANGHLKIIDRKKNLVkTMNGEYIALEKLE 572
Cdd:PRK09192 438 DGWLDTGDLG-YLLDGYLYITGRAKDLI-IINGRNIWPQDIE 477
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
427-613 |
1.58e-09 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 60.95 E-value: 1.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 427 LRYLLNGGSPISrdaqefitnlicPMLIG-------------YGLTETCASTTILDPANfelGVAGD-----------LT 482
Cdd:PRK05620 300 LQEIYVGGSAVP------------PILIKaweerygvdvvhvWGMTETSPVGTVARPPS---GVSGEarwayrvsqgrFP 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 483 GCVTVKLVDVEELGYFAKNNQGEVWITGANVTPEYYKNE----------------EETSQALTSDGWFKTGDIGEWEANG 546
Cdd:PRK05620 365 ASLEYRIVNDGQVMESTDRNEGEIQVRGNWVTASYYHSPteegggaastfrgedvEDANDRFTADGWLRTGDVGSVTRDG 444
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398366229 547 HLKIIDRKKNLVKTmNGEYIALEKLESVYRSNEYV---ANICVYADQSKTKPVGIIV------PNHAPLTKLAKKL 613
Cdd:PRK05620 445 FLTIHDRARDVIRS-GGEWIYSAQLENYIMAAPEVvecAVIGYPDDKWGERPLAVTVlapgiePTRETAERLRDQL 519
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
230-613 |
1.95e-09 |
|
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: 60.18 E-value: 1.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 230 EVRPDIKTFSFDDILKLGKESCNEIDVHPPGKDDLCCIMYTSGSTGEPKGVVLKHSNVVAGVGGASLNVLKfVGNTDRVI 309
Cdd:cd05958 65 ATMPLLRPKELAYILDKARITVALCAHALTASDDICILAFTSGTTGAPKATMHFHRDPLASADRYAVNVLR-LREDDRFV 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 310 CFLPLAHIFELVFELLsFYWGacIGYATVkTLTSSSVRNCQGDLQEFKPTIMVGVAavweTVRKGILNQIDnlpfltkki 389
Cdd:cd05958 144 GSPPLAFTFGLGGVLL-FPFG--VGASGV-LLEEATPDLLLSAIARYKPTVLFTAP----TAYRAMLAHPD--------- 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 390 fwtAYNTKLNMQRLHIPGGGALGNLVFKKIRTATGgqlryllnggspisrdaqefitnliCPMLIGYGLTETCASTTILD 469
Cdd:cd05958 207 ---AAGPDLSSLRKCVSAGEALPAALHRAWKEATG-------------------------IPIIDGIGSTEMFHIFISAR 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 470 PANFELGVAGDLTGCVTVKLVDveELGYFAKNNQ-GEVWITGANVtpeYYKNEEETSQALTSDGWFKTGDIGEWEANGHL 548
Cdd:cd05958 259 PGDARPGATGKPVPGYEAKVVD--DEGNPVPDGTiGRLAVRGPTG---CRYLADKRQRTYVQGGWNITGDTYSRDPDGYF 333
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 549 KIIDRKKNLVKTmNGEYIALEKLESVYRSNEYVANICVYA--DQSK-TKPVGIIV--PNHAPLTKLAKKL 613
Cdd:cd05958 334 RHQGRSDDMIVS-GGYNIAPPEVEDVLLQHPAVAECAVVGhpDESRgVVVKAFVVlrPGVIPGPVLAREL 402
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
165-563 |
2.28e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 60.44 E-value: 2.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 165 LIHSLVQTGSKAIFTDNSLLPsLIKPVQAAQDVKYIIHfdsissedrrqsgkiyQSAHDainrikeVRPDIKT----FSF 240
Cdd:PRK06178 122 LSYELNDAGAEVLLALDQLAP-VVEQVRAETSLRHVIV----------------TSLAD-------VLPAEPTlplpDSL 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 241 D----------DILKLGKESCNEIDVHPPGKDDLCCIMYTSGSTGEPKGVVLKHSNVV---AGVGGASLnvlkfVGNTDR 307
Cdd:PRK06178 178 RaprlaaagaiDLLPALRACTAPVPLPPPALDALAALNYTGGTTGMPKGCEHTQRDMVytaAAAYAVAV-----VGGEDS 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 308 V-ICFLPLAHI----FELVFELLSfywgaciGyATVKTLTSSSVRNCQGDLQEFKPTIMVGVaavwetvrkgilnqIDNL 382
Cdd:PRK06178 253 VfLSFLPEFWIagenFGLLFPLFS-------G-ATLVLLARWDAVAFMAAVERYRVTRTVML--------------VDNA 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 383 PFLTKKIFWTAYNtklnMQRLHIPGGGALgnlvFKKIRTATGGQLRYLLngGSPISRDAqefitnlicpmligYGLTETC 462
Cdd:PRK06178 311 VELMDHPRFAEYD----LSSLRQVRVVSF----VKKLNPDYRQRWRALT--GSVLAEAA--------------WGMTETH 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 463 ASTTIL------------DPANFELGVAGdltgcVTVKLVDVEELGYFAKNNQGEVWITGANVTPEYYKNEEETSQALtS 530
Cdd:PRK06178 367 TCDTFTagfqdddfdllsQPVFVGLPVPG-----TEFKICDFETGELLPLGAEGEIVVRTPSLLKGYWNKPEATAEAL-R 440
|
410 420 430
....*....|....*....|....*....|...
gi 398366229 531 DGWFKTGDIGEWEANGHLKIIDRKKNLVKTmNG 563
Cdd:PRK06178 441 DGWLHTGDIGKIDEQGFLHYLGRRKEMLKV-NG 472
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
253-558 |
2.62e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 60.39 E-value: 2.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 253 EIDVHPPGKDDLCCIMYTSGSTGEPKGVVLKHSNVVAGVgGASLNVLKFVGNTDRVICFLPLAHIFELVfellsfywgac 332
Cdd:PRK07768 143 PIDPVETGEDDLALMQLTSGSTGSPKAVQITHGNLYANA-EAMFVAAEFDVETDVMVSWLPLFHDMGMV----------- 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 333 iGYATVKTLtsssvrnCQGDLQEFKPTIMVGVAAVWETV---RKGILNQIDNLpfltkkifwtAYNtkLNMQRLHipggg 409
Cdd:PRK07768 211 -GFLTVPMY-------FGAELVKVTPMDFLRDPLLWAELiskYRGTMTAAPNF----------AYA--LLARRLR----- 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 410 algnlvfkkiRTATGGQ-----LRYLLNGGSPISRDAQEFITNLICP-------MLIGYGLTETCASTTILDP------- 470
Cdd:PRK07768 266 ----------RQAKPGAfdlssLRFALNGAEPIDPADVEDLLDAGARfglrpeaILPAYGMAEATLAVSFSPCgaglvvd 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 471 -------ANFELGVAGD-------------LTGCvTVKLVDvEELGYFAKNNQGEVWITGANVTPeYYKNEEETSQALTS 530
Cdd:PRK07768 336 evdadllAALRRAVPATkgntrrlatlgppLPGL-EVRVVD-EDGQVLPPRGVGVIELRGESVTP-GYLTMDGFIPAQDA 412
|
330 340
....*....|....*....|....*...
gi 398366229 531 DGWFKTGDIGEWEANGHLKIIDRKKNLV 558
Cdd:PRK07768 413 DGWLDTGDLGYLTEEGEVVVCGRVKDVI 440
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
455-586 |
3.11e-09 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 59.89 E-value: 3.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 455 GYGLTETcASTTILDPANFELGVAGDLTGcVTVKLVDveelgyfaknnqGEVWITGANVTPEYYKNEEETSqaLT-SDGW 533
Cdd:PRK09029 270 GYGLTEM-ASTVCAKRADGLAGVGSPLPG-REVKLVD------------GEIWLRGASLALGYWRQGQLVP--LVnDEGW 333
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 398366229 534 FKTGDIGEWEaNGHLKIIDRKKNLVKTmNGEYIALEKLESVYRSNEYVANICV 586
Cdd:PRK09029 334 FATRDRGEWQ-NGELTILGRLDNLFFS-GGEGIQPEEIERVINQHPLVQQVFV 384
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
260-601 |
4.07e-09 |
|
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: 59.30 E-value: 4.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 260 GKDDLCCIMYTSGSTGEPKGVVLKHSNVVAGVgGASLNVLKfVGNTDRVICFLPL---AHIFELVFELLSfywGACIgya 336
Cdd:cd17649 92 HPRQLAYVIYTSGSTGTPKGVAVSHGPLAAHC-QATAERYG-LTPGDRELQFASFnfdGAHEQLLPPLIC---GACV--- 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 337 tvktltssSVRncqgDLQEFKPTimvgvAAVWETVRKGILNQIDnLPfltkkifwTAYNTKLNMQRLHIPGGGAlgnlvf 416
Cdd:cd17649 164 --------VLR----PDELWASA-----DELAEMVRELGVTVLD-LP--------PAYLQQLAEEADRTGDGRP------ 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 417 kkirtatgGQLRYLLNGGSPISRDAQEFITNLICPMLIGYGLTETCASTTILD-PANFELGVA----GDLTGCVTVKLVD 491
Cdd:cd17649 212 --------PSLRLYIFGGEALSPELLRRWLKAPVRLFNAYGPTEATVTPLVWKcEAGAARAGAsmpiGRPLGGRSAYILD 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 492 vEELGYFAKNNQGEVWITGANVTPEYYKNEEETSQALTSDG-------WFKTGDIGEWEANGHLKIIDRKKNLVKtMNGE 564
Cdd:cd17649 284 -ADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPfgapgsrLYRTGDLARWRDDGVIEYLGRVDHQVK-IRGF 361
|
330 340 350
....*....|....*....|....*....|....*....
gi 398366229 565 YIALEKLESVYRSNEYVANICVYA--DQSKTKPVGIIVP 601
Cdd:cd17649 362 RIELGEIEAALLEHPGVREAAVVAldGAGGKQLVAYVVL 400
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
262-586 |
5.07e-09 |
|
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: 59.25 E-value: 5.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 262 DDLCCIMYTSGSTGEPKGVVLKHSNVVAGVGGASLN--------VLkfvGNTDrvICFlPLAhIFELvFELLSFywGACI 333
Cdd:cd12115 105 DDLAYVIYTSGSTGRPKGVAIEHRNAAAFLQWAAAAfsaeelagVL---ASTS--ICF-DLS-VFEL-FGPLAT--GGKV 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 334 GYA-TVKTLTSSSVRnCQGDLQEFKPTIMvgvAAvwetvrkgiLNQIDNLPfltkkifwtaynTKLNMQRLhipGGGALG 412
Cdd:cd12115 175 VLAdNVLALPDLPAA-AEVTLINTVPSAA---AE---------LLRHDALP------------ASVRVVNL---AGEPLP 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 413 NLVFKKIRTATGGQLRYLLNG---------GSPISRDAQEFITnlicpmlIGYGLTETCASttILDpANFE---LGVAGD 480
Cdd:cd12115 227 RDLVQRLYARLQVERVVNLYGpsedttystVAPVPPGASGEVS-------IGRPLANTQAY--VLD-RALQpvpLGVPGE 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 481 LtgcvtvklvdveelgyfaknnqgevWITGANVTPEYYKNEEETSQALTSDGW------FKTGDIGEWEANGHLKIIDRK 554
Cdd:cd12115 297 L-------------------------YIGGAGVARGYLGRPGLTAERFLPDPFgpgarlYRTGDLVRWRPDGLLEFLGRA 351
|
330 340 350
....*....|....*....|....*....|..
gi 398366229 555 KNLVKtMNGEYIALEKLESVYRSNEYVANICV 586
Cdd:cd12115 352 DNQVK-VRGFRIELGEIEAALRSIPGVREAVV 382
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
262-594 |
7.74e-09 |
|
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: 58.64 E-value: 7.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 262 DDLCCIMYTSGSTGEPKGVVLKHSNVVagvggaslNVLKFvgntdrvicflplahifELVFELLSFYwgacigyATVKTL 341
Cdd:cd17656 128 DDLLYIIYTSGTTGKPKGVQLEHKNMV--------NLLHF-----------------EREKTNINFS-------DKVLQF 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 342 TSSSVRNCqgdLQEFKPTIMVGvaAVWETVRKGILNQIDNLPFLTKK------IFWTAYNTKLNMQRLHIPgggALGNLV 415
Cdd:cd17656 176 ATCSFDVC---YQEIFSTLLSG--GTLYIIREETKRDVEQLFDLVKRhnievvFLPVAFLKFIFSEREFIN---RFPTCV 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 416 fKKIRTAtGGQLRyllnggspISRDAQEFITNLICPMLIGYGLTET-CASTTILDPANF--ELGVAGDLTGCVTVKLVDv 492
Cdd:cd17656 248 -KHIITA-GEQLV--------ITNEFKEMLHEHNVHLHNHYGPSEThVVTTYTINPEAEipELPPIGKPISNTWIYILD- 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 493 EELGYFAKNNQGEVWITGANVTPEYYKNEEETSQALTSDGW------FKTGDIGEWEANGHLKIIDRKKNLVKtMNGEYI 566
Cdd:cd17656 317 QEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFdpnermYRTGDLARYLPDGNIEFLGRADHQVK-IRGYRI 395
|
330 340 350
....*....|....*....|....*....|
gi 398366229 567 ALEKLESVYRSNEYV--ANICVYADQSKTK 594
Cdd:cd17656 396 ELGEIEAQLLNHPGVseAVVLDKADDKGEK 425
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
427-560 |
9.39e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 58.46 E-value: 9.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 427 LRYLLNGGSPIS----RDAQEFITNLICPMligYGLTETCASTTILDPANFELGVAGDLTGC------VTVKLVDvEELG 496
Cdd:PRK06188 283 LETVYYGASPMSpvrlAEAIERFGPIFAQY---YGQTEAPMVITYLRKRDHDPDDPKRLTSCgrptpgLRVALLD-EDGR 358
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398366229 497 YFAKNNQGEVWITGANVTPEYYKNEEETSQALtSDGWFKTGDIGEWEANGHLKIIDRKKNLVKT 560
Cdd:PRK06188 359 EVAQGEVGEICVRGPLVMDGYWNRPEETAEAF-RDGWLHTGDVAREDEDGFYYIVDRKKDMIVT 421
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
144-572 |
1.06e-08 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 58.57 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 144 LGAQSQG-IPVVTAYdTLGEKGLIHSLVQTGSKAIFTDNSLL--------PSLIKPVQAA--QDVKyiihfDSISSEDrr 212
Cdd:PRK08043 273 FGASLRRrIPAMMNY-TAGVKGLTSAITAAEIKTIFTSRQFLdkgklwhlPEQLTQVRWVylEDLK-----DDVTTAD-- 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 213 qsgKIYQSAHDAINRIKEVrpdiktfsfddilklgkescneidvhPPGKDDLCCIMYTSGSTGEPKGVVLKHSNVVAGVG 292
Cdd:PRK08043 345 ---KLWIFAHLLMPRLAQV--------------------------KQQPEDAALILFTSGSEGHPKGVVHSHKSLLANVE 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 293 GASlNVLKFVGNtDRVICFLPLAHIFELVFELLS--------FYWGACIGYATVKTLTSSsvRNCqgdlqefkpTIMVGV 364
Cdd:PRK08043 396 QIK-TIADFTPN-DRFMSALPLFHSFGLTVGLFTplltgaevFLYPSPLHYRIVPELVYD--RNC---------TVLFGT 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 365 AAvwetvrkgilnqidnlpFLTkkifwtayntklNMQRLHIPGGGAlgnlvfkkirtatggQLRYLLNGGSPIS-RDAQE 443
Cdd:PRK08043 463 ST-----------------FLG------------NYARFANPYDFA---------------RLRYVVAGAEKLQeSTKQL 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 444 FITNLICPMLIGYGLTETCASTTILDPANFELGVAGDLTGCVTVKLVDVEELgyfakNNQGEVWITGANVTPEYYKNEE- 522
Cdd:PRK08043 499 WQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSVPGI-----EQGGRLQLKGPNIMNGYLRVEKp 573
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 398366229 523 --------ETSQALTSDGWFKTGDIGEWEANGHLKIIDRKKNLVKtMNGEYIALEKLE 572
Cdd:PRK08043 574 gvlevptaENARGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAK-IAGEMVSLEMVE 630
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
267-540 |
1.18e-08 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 58.13 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 267 IMYTSGSTGEPKGVVLKHSnVVAGVGGASLNVLKFVGNTD--RVICFLPLAHIF--ELVFEllsfywGACIGYAT----- 337
Cdd:PRK12582 225 YLFTSGSTGMPKAVINTQR-MMCANIAMQEQLRPREPDPPppVSLDWMPWNHTMggNANFN------GLLWGGGTlyidd 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 338 ---VKTLTSSSVRNcqgdLQEFKPTIMVGVAAvwetvrkgilnqidnlpfltkkifwtAYNtklnMQRLHIPGGGALGNL 414
Cdd:PRK12582 298 gkpLPGMFEETIRN----LREISPTVYGNVPA--------------------------GYA----MLAEAMEKDDALRRS 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 415 VFKKirtatggqLRYLLNGGSPISRDAQEFITNLIC-------PMLIGYGLTETCASTTILDPANFELGVAG-DLTGcVT 486
Cdd:PRK12582 344 FFKN--------LRLMAYGGATLSDDLYERMQALAVrttghriPFYTGYGATETAPTTTGTHWDTERVGLIGlPLPG-VE 414
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 398366229 487 VKLVDVEElgyfaknnQGEVWITGANVTPEYYKNEEETSQALTSDGWFKTGDIG 540
Cdd:PRK12582 415 LKLAPVGD--------KYEVRVKGPNVTPGYHKDPELTAAAFDEEGFYRLGDAA 460
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
503-576 |
1.73e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 57.65 E-value: 1.73e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398366229 503 QGEVWITGANVTPEYYKNEEETSQALtSDGWFKTGDIGEWEANGHLKIIDRKKNLVKTmNGEYIALEKLESV-YR 576
Cdd:PRK08162 388 IGEIMFRGNIVMKGYLKNPKATEEAF-AGGWFHTGDLAVLHPDGYIKIKDRSKDIIIS-GGENISSIEVEDVlYR 460
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
425-613 |
1.74e-08 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 57.31 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 425 GQLRYLLNGGSPISRDAQEFITNLICPMLIGYGLTETCASTTILDPANFELGvaGDLTGCV----TVKLVDveelgyfak 500
Cdd:PRK07445 230 AQFRTILLGGAPAWPSLLEQARQLQLRLAPTYGMTETASQIATLKPDDFLAG--NNSSGQVlphaQITIPA--------- 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 501 NNQGEVWITGANVTPEYYKneeetsQALTSDGWFKTGDIGEWEANGHLKIIDRKKNLVKTmNGEYIALEKLESVYRSNEY 580
Cdd:PRK07445 299 NQTGNITIQAQSLALGYYP------QILDSQGIFETDDLGYLDAQGYLHILGRNSQKIIT-GGENVYPAEVEAAILATGL 371
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 398366229 581 VANICVY--ADQSKTKPV-GIIVPNHAPL------TKLAKKL 613
Cdd:PRK07445 372 VQDVCVLglPDPHWGEVVtAIYVPKDPSIsleelkTAIKDQL 413
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
259-591 |
1.98e-08 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 57.46 E-value: 1.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 259 PGkdDLCCIMYTSGSTGEPKGVVLKHS-------NVVAGVGgaslnvlkfVGNTDRVICFLPLAHIfelvfellsfywga 331
Cdd:PRK06155 179 PG--DTAAILYTSGTTGPSKGVCCPHAqfywwgrNSAEDLE---------IGADDVLYTTLPLFHT-------------- 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 332 cigyatvktltsssvrncqGDLQEFKPTIMVGVAAVWEtvrkgilnqidnlPFLTKKIFWTAyntklnMQRLHIPGG--- 408
Cdd:PRK06155 234 -------------------NALNAFFQALLAGATYVLE-------------PRFSASGFWPA------VRRHGATVTyll 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 409 GALGNLVFKKIRTAT--GGQLRYLLNGGSPiSRDAQEFITNLICPMLIGYGLTET---CASTT----------------- 466
Cdd:PRK06155 276 GAMVSILLSQPARESdrAHRVRVALGPGVP-AALHAAFRERFGVDLLDGYGSTETnfvIAVTHgsqrpgsmgrlapgfea 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 467 -ILDPANFEL--GVAGDLtgcvtvkLVDVEELGYFAknnqgevwiTGanvtpeYYKNEEETSQALtSDGWFKTGDIGEWE 543
Cdd:PRK06155 355 rVVDEHDQELpdGEPGEL-------LLRADEPFAFA---------TG------YFGMPEKTVEAW-RNLWFHTGDRVVRD 411
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 398366229 544 ANGHLKIIDRKKNLVKtMNGEYIALEKLESVYRSNEYVANICVYADQS 591
Cdd:PRK06155 412 ADGWFRFVDRIKDAIR-RRGENISSFEVEQVLLSHPAVAAAAVFPVPS 458
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
269-588 |
2.85e-08 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 56.95 E-value: 2.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 269 YTSGSTGEPKGVVLKHSnvvagvgGASLNVLKFVGNTDRVIC-----FLPLAHIfelvfELLSFYWGAcigyaTVKTLTS 343
Cdd:PLN03102 193 YTSGTTADPKGVVISHR-------GAYLSTLSAIIGWEMGTCpvylwTLPMFHC-----NGWTFTWGT-----AARGGTS 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 344 SSVRNcqgdlqefkptimVGVAAVWETVRKGILNQIDNLPfltkkifwTAYNTKLNMQRLHI-PGGGALgnlvfkkirta 422
Cdd:PLN03102 256 VCMRH-------------VTAPEIYKNIEMHNVTHMCCVP--------TVFNILLKGNSLDLsPRSGPV----------- 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 423 tggqlrYLLNGGSPISRDAQEFITNLICPMLIGYGLTETCASTTILD--------PANFEL------GVAGDLTGCVTVK 488
Cdd:PLN03102 304 ------HVLTGGSPPPAALVKKVQRLGFQVMHAYGLTEATGPVLFCEwqdewnrlPENQQMelkarqGVSILGLADVDVK 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 489 LVDVEELGYFAKNNQGEVWITGANVTPEYYKNEEETSQALtSDGWFKTGDIGEWEANGHLKIIDRKKNLVKTmNGEYIAL 568
Cdd:PLN03102 378 NKETQESVPRDGKTMGEIVIKGSSIMKGYLKNPKATSEAF-KHGWLNTGDVGVIHPDGHVEIKDRSKDIIIS-GGENISS 455
|
330 340
....*....|....*....|
gi 398366229 569 EKLESVYRSNEYVANICVYA 588
Cdd:PLN03102 456 VEVENVLYKYPKVLETAVVA 475
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
101-601 |
2.99e-08 |
|
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: 56.77 E-value: 2.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 101 SFDQLTDIMHEIGRGLVKIGLKPndDDKLHLYAATSHKWMKMFLGAQSQGIPVVTAYDTLGEKGLIHSLVQTGSKAIFTD 180
Cdd:TIGR02262 32 SYGELEAQVRRLAAALRRLGVKR--EERVLLLMLDGVDFPIAFLGAIRAGIVPVALNTLLTADDYAYMLEDSRARVVFVS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 181 NSLLPsLIKPvqAAQDVKYIIHfdsissedrrqsgkiyqsahdainRIKEVRPDIKTFSFDDILKLGKESCNEIDVHPpg 260
Cdd:TIGR02262 110 GALLP-VIKA--ALGKSPHLEH------------------------RVVVGRPEAGEVQLAELLATESEQFKPAATQA-- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 261 kDDLCCIMYTSGSTGEPKGVVLKHSNVVAgvgGASLNVLKFVGNTDRVICFlPLAHIFelvfellsFYWGACIGYATVKT 340
Cdd:TIGR02262 161 -DDPAFWLYSSGSTGMPKGVVHTHSNPYW---TAELYARNTLGIREDDVCF-SAAKLF--------FAYGLGNALTFPMS 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 341 LTSSSVRNCQgdlqefKPTimvgVAAVWETVRKgilnqidnlpfLTKKIFW---TAYNTKLNMQRLhipgggalgnlvfk 417
Cdd:TIGR02262 228 VGATTVLMGE------RPT----PDAVFDRLRR-----------HQPTIFYgvpTLYAAMLADPNL-------------- 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 418 kiRTATGGQLRYLLNGGSPISRD-AQEFITNLICPMLIGYGLTETCASTTILDPANFELGVAGDLTGCVTVKLVDvEELG 496
Cdd:TIGR02262 273 --PSEDQVRLRLCTSAGEALPAEvGQRWQARFGVDIVDGIGSTEMLHIFLSNLPGDVRYGTSGKPVPGYRLRLVG-DGGQ 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 497 YFAKNNQGEVWITGANVTPEYYKNEEETSQALTSdGWFKTGDIGEWEANGHLKIIDRKKNLVKtMNGEYIALEKLESVYR 576
Cdd:TIGR02262 350 DVADGEPGELLISGPSSATMYWNNRAKSRDTFQG-EWTRSGDKYVRNDDGSYTYAGRTDDMLK-VSGIYVSPFEIESALI 427
|
490 500
....*....|....*....|....*...
gi 398366229 577 SNEYV--ANICVYADQSK-TKPVGIIVP 601
Cdd:TIGR02262 428 QHPAVleAAVVGVADEDGlIKPKAFVVL 455
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
486-601 |
9.72e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 55.13 E-value: 9.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 486 TVKLVDVEELGYFAKNNQGEVWITGANVTPEYYKNEEETSQALTSDGWFKTGDIGEWEANGHLKIIDRKKNLVKtMNGEY 565
Cdd:PRK06164 360 RVRARDPQDGALLPDGESGEIEIRAPSLMRGYLDNPDATARALTDDGYFRTGDLGYTRGDGQFVYQTRMGDSLR-LGGFL 438
|
90 100 110
....*....|....*....|....*....|....*...
gi 398366229 566 IALEKLESVYRSNEYVANICVYADQS--KTKPVGIIVP 601
Cdd:PRK06164 439 VNPAEIEHALEALPGVAAAQVVGATRdgKTVPVAFVIP 476
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
258-590 |
1.38e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 54.74 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 258 PPGKDDLCCIMYTSGSTGEPKGVVLKHSNVVAgvggaslNVLKFV----GNT-DRVICFLPLAHIFELVFELLSFYWGAC 332
Cdd:PRK07769 176 EANEDTIAYLQYTSGSTRIPAGVQITHLNLPT-------NVLQVIdaleGQEgDRGVSWLPFFHDMGLITVLLPALLGHY 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 333 IgyatvktltsssvrncqgdlqefkpTIMVGVAAVWETVRkgILNQIDNLPFLTKKIFWTAYNTKLNMQRLH-IPGGGA- 410
Cdd:PRK07769 249 I-------------------------TFMSPAAFVRRPGR--WIRELARKPGGTGGTFSAAPNFAFEHAAARgLPKDGEp 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 411 ---LGNLvfkkirtatggqlRYLLNGGSPISRDAQEFITNLICPmligYGLTETC-------------ASTTILD----- 469
Cdd:PRK07769 302 pldLSNV-------------KGLLNGSEPVSPASMRKFNEAFAP----YGLPPTAikpsygmaeatlfVSTTPMDeeptv 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 470 ----------------PANFELGVAGDLTGCVTVK----LVDVEELGYFAKNNQGEVWITGANVTPEYYKNEEETSQA-- 527
Cdd:PRK07769 365 iyvdrdelnagrfvevPADAPNAVAQVSAGKVGVSewavIVDPETASELPDGQIGEIWLHGNNIGTGYWGKPEETAATfq 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 528 --LTS-------------DGWFKTGDIGEWeANGHLKIIDRKKNLVkTMNG--------EYIALEKLESVyRSNeYVANI 584
Cdd:PRK07769 445 niLKSrlseshaegapddALWVRTGDYGVY-FDGELYITGRVKDLV-IIDGrnhypqdlEYTAQEATKAL-RTG-YVAAF 520
|
....*.
gi 398366229 585 CVYADQ 590
Cdd:PRK07769 521 SVPANQ 526
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
264-582 |
1.48e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 54.71 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 264 LCcimYTSGSTGEPKGVVLKHSNVVAGVGGASLNVLKFVGNTDRVICFLPLAHIFElvfellsfyWG-----ACIGYATV 338
Cdd:PRK07008 181 LC---YTSGTTGNPKGALYSHRSTVLHAYGAALPDAMGLSARDAVLPVVPMFHVNA---------WGlpysaPLTGAKLV 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 339 ---KTLTSSSVRNCqgdLQEFKPTIMVGVAAVWEtvrkGILNqidnlpfltkkifwtayntklnmqrlHIPGGGalgnLV 415
Cdd:PRK07008 249 lpgPDLDGKSLYEL---IEAERVTFSAGVPTVWL----GLLN--------------------------HMREAG----LR 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 416 FKKI-RTATGGQlryllngGSPISRdAQEFITNLICPMLIGYGLTETCASTTILDPANFELGVAGD------------LT 482
Cdd:PRK07008 292 FSTLrRTVIGGS-------ACPPAM-IRTFEDEYGVEVIHAWGMTEMSPLGTLCKLKWKHSQLPLDeqrkllekqgrvIY 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 483 GcVTVKLVDVE--ELGYFAKNnQGEVWITGANVTPEYYKNEEETsqalTSDGWFKTGDIGEWEANGHLKIIDRKKNLVKT 560
Cdd:PRK07008 364 G-VDMKIVGDDgrELPWDGKA-FGDLQVRGPWVIDRYFRGDASP----LVDGWFPTGDVATIDADGFMQITDRSKDVIKS 437
|
330 340
....*....|....*....|..
gi 398366229 561 mNGEYIALEKLESVYRSNEYVA 582
Cdd:PRK07008 438 -GGEWISSIDIENVAVAHPAVA 458
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
262-557 |
2.10e-07 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 54.79 E-value: 2.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 262 DDLCCIMYTSGSTGEPKGVVLKHSNVVA-------GVGgaslnvlKFVGNTDRVICFLPLAHIFELVFELL-SFYWGA-C 332
Cdd:PRK05691 166 DDIAFLQYTSGSTALPKGVQVSHGNLVAneqlirhGFG-------IDLNPDDVIVSWLPLYHDMGLIGGLLqPIFSGVpC 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 333 IGYATVKTLTsSSVRNCQGdLQEFKPTIMVGvaavwetvrkgilnqidnlPFLtkkifwtAYntKLNMQRLhipGGGALG 412
Cdd:PRK05691 239 VLMSPAYFLE-RPLRWLEA-ISEYGGTISGG-------------------PDF-------AY--RLCSERV---SESALE 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 413 NLVFKKIRTAtggqlrylLNGGSPISRD-----AQEFITNLICP--MLIGYGLTETCASTT-----------ILDPANF- 473
Cdd:PRK05691 286 RLDLSRWRVA--------YSGSEPIRQDslerfAEKFAACGFDPdsFFASYGLAEATLFVSggrrgqgipalELDAEALa 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 474 ----ELGVAGDLTGCVT------VKLVDVEELGYFAKNNQGEVWITGANVTPEYYKNEEETSQALTS-DG--WFKTGDI- 539
Cdd:PRK05691 358 rnraEPGTGSVLMSCGRsqpghaVLIVDPQSLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTFVEhDGrtWLRTGDLg 437
|
330 340
....*....|....*....|....
gi 398366229 540 ----GEWEANGHLK--IIDRKKNL 557
Cdd:PRK05691 438 flrdGELFVTGRLKdmLIVRGHNL 461
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
517-572 |
4.02e-07 |
|
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: 53.23 E-value: 4.02e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 398366229 517 YYKNEEETSQALTSDGWFKTGDIGEWEANGHLKIIDRKKNLVktmN--GEYIALEKLE 572
Cdd:COG1021 394 YYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKDQI---NrgGEKIAAEEVE 448
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
262-606 |
1.04e-06 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 52.65 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 262 DDLCCIMYTSGSTGEPKGVVLKHSNVVAGVggASLNVLKFVGNTDRVICFLPLAhiFELVFEllSFYWGACIGYATVktL 341
Cdd:PRK12316 4694 DNLAYVIYTSGSTGRPKGVAVSHGSLVNHL--HATGERYELTPDDRVLQFMSFS--FDGSHE--GLYHPLINGASVV--I 4765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 342 TSSSVRNCQGDLQEF---KPTIMVGVAAVWETVRKGILNQiDNLPFLTKKIFwtayntklnmqrlhipGGGALG----NL 414
Cdd:PRK12316 4766 RDDSLWDPERLYAEIhehRVTVLVFPPVYLQQLAEHAERD-GEPPSLRVYCF----------------GGEAVAqasyDL 4828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 415 VFKKIRTAtggqlrYLLNggspisrdaqefitnlicpmliGYGLTETCASTTILDPANFELGVA-----GDLTGCVTVKL 489
Cdd:PRK12316 4829 AWRALKPV------YLFN----------------------GYGPTETTVTVLLWKARDGDACGAaympiGTPLGNRSGYV 4880
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 490 VDVeELGYFAKNNQGEVWITGANVTPEYYKNEEETSQALTSDGW-------FKTGDIGEWEANGHLKIIDRKKNLVKtMN 562
Cdd:PRK12316 4881 LDG-QLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgapggrlYRTGDLARYRADGVIDYLGRVDHQVK-IR 4958
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 398366229 563 GEYIALEKLESVYRSNEYVANICVYADQSKTKP--VGIIVPNHAPL 606
Cdd:PRK12316 4959 GFRIELGEIEARLREHPAVREAVVIAQEGAVGKqlVGYVVPQDPAL 5004
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
263-574 |
1.08e-06 |
|
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: 51.63 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 263 DLCCIMYTSGSTGEPKGVVLKHSNVVAGVggASLNVLKFV-GNTDRVICFLPlAHIFELVFELLsfywgaCIGYATVKTL 341
Cdd:cd17648 95 DLAYAIYTSGTTGKPKGVLVEHGSVVNLR--TSLSERYFGrDNGDEAVLFFS-NYVFDFFVEQM------TLALLNGQKL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 342 T--SSSVRNCQGDLQEF----KPTIMVGVAAVwetvrkgiLNQIDnlpfltkkifwtaYNTKLNMQRLhIPGGGALGNLV 415
Cdd:cd17648 166 VvpPDEMRFDPDRFYAYinreKVTYLSGTPSV--------LQQYD-------------LARLPHLKRV-DAAGEEFTAPV 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 416 FKKIRTATGGQlryllnggspisrdaqefITNlicpmliGYGLTETcASTTILDPanFELGVAGDLTGCVTVKLVDVEEL 495
Cdd:cd17648 224 FEKLRSRFAGL------------------IIN-------AYGPTET-TVTNHKRF--FPGDQRFDKSLGRPVRNTKCYVL 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 496 GYFAK----NNQGEVWITGANVTPEYYKNEEETSQALTSDGW--------------FKTGDIGEWEANGHLKIIDRKKNL 557
Cdd:cd17648 276 NDAMKrvpvGAVGELYLGGDGVARGYLNRPELTAERFLPNPFqteqerargrnarlYKTGDLVRWLPSGELEYLGRNDFQ 355
|
330
....*....|....*..
gi 398366229 558 VKtMNGEYIALEKLESV 574
Cdd:cd17648 356 VK-IRGQRIEPGEVEAA 371
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
489-612 |
1.10e-06 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 51.82 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 489 LVDVEELGYFAKNNQGEVWITGANVTPEYYKNEEETSQAL-TSDGW--FKTGDIGEWEaNGHLKIIDRKKNLVKtMNGEY 565
Cdd:PRK04813 330 LIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFfTFDGQpaYHTGDAGYLE-DGLLFYQGRIDFQIK-LNGYR 407
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 398366229 566 IALEKLESVYRSNEYVANICV--YADQSK-TKPVGIIVPNH------APLTKLAKK 612
Cdd:PRK04813 408 IELEEIEQNLRQSSYVESAVVvpYNKDHKvQYLIAYVVPKEedfereFELTKAIKK 463
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
258-327 |
2.39e-06 |
|
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: 50.73 E-value: 2.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 258 PPGKDDLCCIMYTSGSTGEPKGVVLKHSnvvagvggASLNVL-----KF-VGNTDRVICFLPLAhiFEL----VFELLSF 327
Cdd:cd12114 122 DVAPDDLAYVIFTSGSTGTPKGVMISHR--------AALNTIldinrRFaVGPDDRVLALSSLS--FDLsvydIFGALSA 191
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
242-588 |
3.09e-06 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 50.93 E-value: 3.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 242 DILKLGKESCNEIDVHPP---GKDDLCCIMYTSGSTGEPKGVVLKHSNVVAGVGGASlNVLKFVGNtDRVICFLPLAhiF 318
Cdd:PRK12467 633 CLDEPADLLCGYSGHNPEvalDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIA-ERLQLAAD-DSMLMVSTFA--F 708
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 319 ELVFELLsfYWGACIGyATVKTLTSSSVRncqgDLQEFkptimvgvAAVWETVRKGILNQIdnlPFLTKKIFWTAYNTKL 398
Cdd:PRK12467 709 DLGVTEL--FGALASG-ATLHLLPPDCAR----DAEAF--------AALMADQGVTVLKIV---PSHLQALLQASRVALP 770
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 399 NMQRLHIPGGGALGNLVFKKIRtATGGQLRYLlnggspisrdaqefitNLicpmligYGLTETCASTTI-------LDPA 471
Cdd:PRK12467 771 RPQRALVCGGEALQVDLLARVR-ALGPGARLI----------------NH-------YGPTETTVGVSTyelsdeeRDFG 826
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 472 NFELGVAgdLTGcVTVKLVDvEELGYFAKNNQGEVWITGANVTPEYYKNEEETSQALTSDGW-------FKTGDIGEWEA 544
Cdd:PRK12467 827 NVPIGQP--LAN-LGLYILD-HYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDPFgadggrlYRTGDLARYRA 902
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 398366229 545 NGHLKIIDRKKNLVKtMNGEYIALEKLESVYRSNEYVANICVYA 588
Cdd:PRK12467 903 DGVIEYLGRMDHQVK-IRGFRIELGEIEARLLAQPGVREAVVLA 945
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
504-593 |
3.95e-06 |
|
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: 49.96 E-value: 3.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 504 GEVWITGANVTPEYYKNEEETSQALTSDG----WFKTGDIGEWEANGHLKIIDRKKNLVKtMNGEYIALEKLESVYRSNE 579
Cdd:cd12114 327 GELWIGGRGVALGYLGDPELTAARFVTHPdgerLYRTGDLGRYRPDGTLEFLGRRDGQVK-VRGYRIELGEIEAALQAHP 405
|
90
....*....|....
gi 398366229 580 YVANICVYADQSKT 593
Cdd:cd12114 406 GVARAVVVVLGDPG 419
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
249-613 |
4.38e-06 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 50.54 E-value: 4.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 249 ESCNEIDVHPpgkDDLCCIMYTSGSTGEPKGVVLKHSNVVAGVggASLNVLKFVGNTDRVICFLPLAhiFELVFEllSFY 328
Cdd:PRK12467 3227 ENNPSTRVMG---ENLAYVIYTSGSTGKPKGVGVRHGALANHL--CWIAEAYELDANDRVLLFMSFS--FDGAQE--RFL 3297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 329 WGACIGYATVktltsssVRNcqGDLQEfkPTimvgvaavwETVRKGILNQIDNLPFLtkkifwTAYntklnMQRLHIPGG 408
Cdd:PRK12467 3298 WTLICGGCLV-------VRD--NDLWD--PE---------ELWQAIHAHRISIACFP------PAY-----LQQFAEDAG 3346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 409 GalgnlvfkkirtATGGQLRYLLNGGSPISRDAQEFITNLICPMLI--GYGLTETCASTTILD---PANFELGVA--GDL 481
Cdd:PRK12467 3347 G------------ADCASLDIYVFGGEAVPPAAFEQVKRKLKPRGLtnGYGPTEAVVTVTLWKcggDAVCEAPYApiGRP 3414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 482 TGCVTVKLVDvEELGYFAKNNQGEVWITGANVTPEYYKNEEETSQALTSDGW-------FKTGDIGEWEANGHLKIIDRK 554
Cdd:PRK12467 3415 VAGRSIYVLD-GQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVADPFsgsggrlYRTGDLARYRADGVIEYLGRI 3493
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398366229 555 KNLVKtMNGEYIALEKLESVYRSNEYVANICVYA--DQSKTKPVGIIVPnHAPLTKLAKKL 613
Cdd:PRK12467 3494 DHQVK-IRGFRIELGEIEARLLQHPSVREAVVLArdGAGGKQLVAYVVP-ADPQGDWRETL 3552
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
262-332 |
5.08e-06 |
|
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: 49.56 E-value: 5.08e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398366229 262 DDLCCIMYTSGSTGEPKGVVLKHSNV--VAGVGGASLNvlkfVGNTDRVICFLPL---AHIFELVFELLSfywGAC 332
Cdd:cd17652 93 DNLAYVIYTSGSTGRPKGVVVTHRGLanLAAAQIAAFD----VGPGSRVLQFASPsfdASVWELLMALLA---GAT 161
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
455-586 |
7.66e-06 |
|
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: 48.45 E-value: 7.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 455 GYGLTETCASTTILDPANFELGVAGDLTGCVTVKLVDVE--ELgyfAKNNQGEVWITGANVTPEYYkNEEETSQALTSDG 532
Cdd:cd17636 142 GYGQTEVMGLATFAALGGGAIGGAGRPSPLVQVRILDEDgrEV---PDGEVGEIVARGPTVMAGYW-NRPEVNARRTRGG 217
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 398366229 533 WFKTGDIGEWEANGHLKIIDRKKNLVKTMnGEYIALEKLESVYRSNEYVANICV 586
Cdd:cd17636 218 WHHTNDLGRREPDGSLSFVGPKTRMIKSG-AENIYPAEVERCLRQHPAVADAAV 270
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
253-601 |
8.03e-06 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 49.57 E-value: 8.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 253 EIDVHPpgkDDLCCIMYTSGSTGEPKGVVLKHSNVVAGVGGASLNVLkfVGNTDRVICFLPLAhiFELVFELLsfYWGAC 332
Cdd:PRK12316 2140 AVQLAG---ENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYE--LSPADCELQFMSFS--FDGAHEQW--FHPLL 2210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 333 IGYATVktLTSSSVRNCQ---GDLQEFKPTIMVGVAAVWETVRKGIlnQIDNLPfltkkifwtayntkLNMQRLHIpGGG 409
Cdd:PRK12316 2211 NGARVL--IRDDELWDPEqlyDEMERHGVTILDFPPVYLQQLAEHA--ERDGRP--------------PAVRVYCF-GGE 2271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 410 ALGNLVFKKIRTATGGQlrYLLNggspisrdaqefitnlicpmliGYGLTETCASTTI-----LDPANFELGVAGDLTGC 484
Cdd:PRK12316 2272 AVPAASLRLAWEALRPV--YLFN----------------------GYGPTEAVVTPLLwkcrpQDPCGAAYVPIGRALGN 2327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 485 VTVKLVDvEELGYFAKNNQGEVWITGANVTPEYYKNEEETSQALTSDGW-------FKTGDIGEWEANGHLKIIDRKKNL 557
Cdd:PRK12316 2328 RRAYILD-ADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFsasgerlYRTGDLARYRADGVVEYLGRIDHQ 2406
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 398366229 558 VKtMNGEYIALEKLESVYRSNEYVANICVYADQSKTKP--VGIIVP 601
Cdd:PRK12316 2407 VK-IRGFRIELGEIEARLQAHPAVREAVVVAQDGASGKqlVAYVVP 2451
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
262-603 |
1.05e-05 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 48.58 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 262 DDLCCIMYTSGSTGEPKGVVLkhSNVVAGVGGASLNVLKFVGNTDRVICFLPL----AHIFELVFELLSfywGACIGYAT 337
Cdd:cd05937 87 DDPAILIYTSGTTGLPKAAAI--SWRRTLVTSNLLSHDLNLKNGDRTYTCMPLyhgtAAFLGACNCLMS---GGTLALSR 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 338 vktltSSSVRNCQGDLQEFKPTIMVGVAavwETVRkgilnQIDNLPfltkkifwtayntKLNMQRLHipgggalgnlvfk 417
Cdd:cd05937 162 -----KFSASQFWKDVRDSGATIIQYVG---ELCR-----YLLSTP-------------PSPYDRDH------------- 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 418 KIRTATGgqlryllNGGSP-ISRDAQE-FITNLICPMligYGLTETCASTTILDPANFELGVAGD--------LTGCVTV 487
Cdd:cd05937 203 KVRVAWG-------NGLRPdIWERFRErFNVPEIGEF---YAATEGVFALTNHNVGDFGAGAIGHhglirrwkFENQVVL 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 488 KLVDVE--------ELGyFAK----NNQGEVW--ITGANVT--PEYYKNEEETSQALTS------DGWFKTGDIGEWEAN 545
Cdd:cd05937 273 VKMDPEtddpirdpKTG-FCVrapvGEPGEMLgrVPFKNREafQGYLHNEDATESKLVRdvfrkgDIYFRTGDLLRQDAD 351
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 398366229 546 GHLKIIDRkknLVKTMNGeyialeKLESVyRSNEYVANICVYADQSKTKPVGIIVPNH 603
Cdd:cd05937 352 GRWYFLDR---LGDTFRW------KSENV-STTEVADVLGAHPDIAEANVYGVKVPGH 399
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
263-603 |
1.14e-05 |
|
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: 48.50 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 263 DLCCIMYTSGSTGEPKGVVLKHSNVVAGVGGASLnvLKFVGNTDRVICFLPLAHIFELVFEllsfyWGACI-GYATVKTL 341
Cdd:cd05940 82 DAALYIYTSGTTGLPKAAIISHRRAWRGGAFFAG--SGGALPSDVLYTCLPLYHSTALIVG-----WSACLaSGATLVIR 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 342 TSSSVRNCQGDLQEFKPTIMVGVAavwETVRKgILNQidnlpfltkkifwtaynTKLNMQRLHipgggalgnlvfkKIRT 421
Cdd:cd05940 155 KKFSASNFWDDIRKYQATIFQYIG---ELCRY-LLNQ-----------------PPKPTERKH-------------KVRM 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 422 ATGGQLRyllnggSPISRDAQE-FITNLICPMligYGLTETCASTTILDPANFELGVAGDLTGCV-TVKLV--DVE---- 493
Cdd:cd05940 201 IFGNGLR------PDIWEEFKErFGVPRIAEF---YAATEGNSGFINFFGKPGAIGRNPSLLRKVaPLALVkyDLEsgep 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 494 ---ELGYFAKNNQGEVWITGANVTPE-----YYKNEEETSQALTS-----DGWFKTGDIGEWEANGHLKIIDRkknLVKT 560
Cdd:cd05940 272 irdAEGRCIKVPRGEPGLLISRINPLepfdgYTDPAATEKKILRDvfkkgDAWFNTGDLMRLDGEGFWYFVDR---LGDT 348
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 398366229 561 M--NGEYIALEKLESVYRSNEYVANICVYadqsktkpvGIIVPNH 603
Cdd:cd05940 349 FrwKGENVSTTEVAAVLGAFPGVEEANVY---------GVQVPGT 384
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
517-573 |
1.60e-05 |
|
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: 48.09 E-value: 1.60e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 398366229 517 YYKNEEETSQALTSDGWFKTGDIGEWEANGHLKIIDRKKNLVkTMNGEYIALEKLES 573
Cdd:cd05920 349 YYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQI-NRGGEKIAAEEVEN 404
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
258-333 |
2.66e-05 |
|
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: 47.27 E-value: 2.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 258 PPGKDDLCCIMYTSGSTGEPKGVVLKHSNVVagvggaslNVLKF------VGNTDRVICFLPLAhiFEL-VFELLsfyW- 329
Cdd:cd17646 134 PPRPDNLAYVIYTSGSTGRPKGVMVTHAGIV--------NRLLWmqdeypLGPGDRVLQKTPLS--FDVsVWELF---Wp 200
|
....*..
gi 398366229 330 ---GACI 333
Cdd:cd17646 201 lvaGARL 207
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
259-606 |
3.77e-05 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 47.46 E-value: 3.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 259 PGKDDLCCIMYTSGSTGEPKGVVLKHSNVVagvggaslNVLKFVGN------TDRVICFLPLAHIFElVFEllsFYWGAC 332
Cdd:PRK12467 1715 LAPQNLAYVIYTSGSTGRPKGAGNRHGALV--------NRLCATQEayqlsaADVVLQFTSFAFDVS-VWE---LFWPLI 1782
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 333 IGYATVKTLTSSSVrncqgDLQEFKPTImvgvaavwETVRKGILNQIDNlpfltkkifwtayntklnmqrlhipgggALG 412
Cdd:PRK12467 1783 NGARLVIAPPGAHR-----DPEQLIQLI--------ERQQVTTLHFVPS----------------------------MLQ 1821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 413 NLVFKKIRTATGGQLRYLLNGGSPISRDAQEFITNLICPMLI--GYGLTETCASTTildpanFELGVAGDLTGCVTVKL- 489
Cdd:PRK12467 1822 QLLQMDEQVEHPLSLRRVVCGGEALEVEALRPWLERLPDTGLfnLYGPTETAVDVT------HWTCRRKDLEGRDSVPIg 1895
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 490 VDVEELGYFAKNNQ---------GEVWITGANVTPEYYKNEEETSQALTSDGW-------FKTGDIGEWEANGHLKIIDR 553
Cdd:PRK12467 1896 QPIANLSTYILDASlnpvpigvaGELYLGGVGLARGYLNRPALTAERFVADPFgtvgsrlYRTGDLARYRADGVIEYLGR 1975
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 398366229 554 KKNLVKtMNGEYIALEKLESVYRSNEYVANICVYADQ--SKTKPVGIIVPNHAPL 606
Cdd:PRK12467 1976 IDHQVK-IRGFRIELGEIEARLREQGGVREAVVIAQDgaNGKQLVAYVVPTDPGL 2029
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
260-613 |
9.82e-05 |
|
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: 45.50 E-value: 9.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 260 GKDDLCCIMYTSGSTGEPKGVVLKHSNVVAGVGGASLnVLKFVGNTDRVIcFLPL--AHIFELVFELL-SFYWGacigya 336
Cdd:cd05971 86 GSDDPALIIYTSGTTGPPKGALHAHRVLLGHLPGVQF-PFNLFPRDGDLY-WTPAdwAWIGGLLDVLLpSLYFG------ 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 337 tVKTLTSSSvrncqgdlQEFKPTIMVGVAAVWeTVRKGilnqidnlpFLTKkifwtaynTKLNMQRLHipgggalgnlvf 416
Cdd:cd05971 158 -VPVLAHRM--------TKFDPKAALDLMSRY-GVTTA---------FLPP--------TALKMMRQQ------------ 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 417 KKIRTATGGQLRYLLNGGSPISR------------DAQEFITNLICPMLIGyglteTCASTTILDPANFELGVAGDltgc 484
Cdd:cd05971 199 GEQLKHAQVKLRAIATGGESLGEellgwareqfgvEVNEFYGQTECNLVIG-----NCSALFPIKPGSMGKPIPGH---- 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 485 vTVKLVDV--EELgyfAKNNQGEVWIT--GANVTPEYYKNEEETSQALTSDgWFKTGDIGEWEANGHLKIIDRKKNLVKT 560
Cdd:cd05971 270 -RVAIVDDngTPL---PPGEVGEIAVElpDPVAFLGYWNNPSATEKKMAGD-WLLTGDLGRKDSDGYFWYVGRDDDVITS 344
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 398366229 561 mNGEYIALEKLESVYRSNEYVANICVYA--DQSKTKPVGIIV---PNHAPLTKLAKKL 613
Cdd:cd05971 345 -SGYRIGPAEIEECLLKHPAVLMAAVVGipDPIRGEIVKAFVvlnPGETPSDALAREI 401
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
262-614 |
1.11e-04 |
|
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.
Pssm-ID: 341300 [Multi-domain] Cd Length: 440 Bit Score: 45.24 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 262 DDLCCIMYTSGSTGEPKGVVLKHSNVVAgvggaslnvlkfvgntdrvicflplahifelvfelLSFYWGACIGY-ATVKT 340
Cdd:cd17645 104 DDLAYVIYTSGSTGLPKGVMIEHHNLVN-----------------------------------LCEWHRPYFGVtPADKS 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 341 LTSSSVrNCQGDLQEFKPTIMVGvaAVWETVRKGILNQIDNLP--FLTKKIFWTAYNTKLNMQRLhipgggALGNlvfkk 418
Cdd:cd17645 149 LVYASF-SFDASAWEIFPHLTAG--AALHVVPSERRLDLDALNdyFNQEGITISFLPTGAAEQFM------QLDN----- 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 419 irtatgGQLRYLLNGGSPISRDAQEFITnlicpMLIGYGLTETCASTTI--LDP--ANFELGVAGDLTgcvTVKLVDvEE 494
Cdd:cd17645 215 ------QSLRVLLTGGDKLKKIERKGYK-----LVNNYGPTENTVVATSfeIDKpyANIPIGKPIDNT---RVYILD-EA 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 495 LGYFAKNNQGEVWITGANVTPEYYKNEEETSQALTSDGW------FKTGDIGEWEANGHLKIIDRKKNLVKtMNGEYIAL 568
Cdd:cd17645 280 LQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFvpgermYRTGDLAKFLPDGNIEFLGRLDQQVK-IRGYRIEP 358
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 398366229 569 EKLESVYRSNEYVANICVYA----DQSKTKPVGIIVPNHAPLTKLAKKLG 614
Cdd:cd17645 359 GEIEPFLMNHPLIELAAVLAkedaDGRKYLVAYVTAPEEIPHEELREWLK 408
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
427-647 |
1.50e-04 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 45.12 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 427 LRYLLNGGSPISRDAQEFITN-LICPMLIGYGLTET-CASTTILDPANFELGVAGDLTgcVTVKLV----DVEELGyfaK 500
Cdd:PTZ00237 382 LKEIWCGGEVIEESIPEYIENkLKIKSSRGYGQTEIgITYLYCYGHINIPYNATGVPS--IFIKPSilseDGKELN---V 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 501 NNQGEVWIT---GANVTPEYYKNEEETSQALTS-DGWFKTGDIGEWEANGHLKIIDRKKNLVKtMNGEYIALEKLESVYR 576
Cdd:PTZ00237 457 NEIGEVAFKlpmPPSFATTFYKNDEKFKQLFSKfPGYYNSGDLGFKDENGYYTIVSRSDDQIK-ISGNKVQLNTIETSIL 535
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 577 SNEYVANIC---VYADQSKTKPVGIIVPN------HAPLTKLAKKLGIMEQKDssinIENYLEDAKLIKAVYSDLLKTGK 647
Cdd:PTZ00237 536 KHPLVLECCsigIYDPDCYNVPIGLLVLKqdqsnqSIDLNKLKNEINNIITQD----IESLAVLRKIIIVNQLPKTKTGK 611
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
427-558 |
1.78e-04 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 44.69 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 427 LRYLLNGGSPISRDAQEFITNLICPMLIG-YGLTETCASTTildpANFE-----LGVAGDLTGCVTVKLVDvEELGYFAK 500
Cdd:PRK12406 273 LRHVIHAAAPCPADVKRAMIEWWGPVIYEyYGSTESGAVTF----ATSEdalshPGTVGKAAPGAELRFVD-EDGRPLPQ 347
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 398366229 501 NNQGEVWITGANVTPEYYKNEEETSQALTSDGWFKTGDIGEWEANGHLKIIDRKKNLV 558
Cdd:PRK12406 348 GEIGEIYSRIAGNPDFTYHNKPEKRAEIDRGGFITSGDVGYLDADGYLFLCDRKRDMV 405
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
262-316 |
2.12e-04 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 44.48 E-value: 2.12e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 398366229 262 DDLCCIMYTSGSTGEPKGVVLKHSNVVAGVG--GASLNvlkfVGNTDRVICFLPLAH 316
Cdd:PRK08279 199 KDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGgfGGLLR----LTPDDVLYCCLPLYH 251
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
504-574 |
2.53e-04 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 44.06 E-value: 2.53e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398366229 504 GEVWITGANVTPEYYKNEEETSQALtSDGWFKTGDIGEWEANGHLKIIDRKKNLVKTmNGEYIALEKLESV 574
Cdd:PLN02479 403 GEIVMRGNMVMKGYLKNPKANEEAF-ANGWFHSGDLGVKHPDGYIEIKDRSKDIIIS-GGENISSLEVENV 471
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
253-289 |
4.12e-04 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 44.18 E-value: 4.12e-04
10 20 30
....*....|....*....|....*....|....*..
gi 398366229 253 EIDVHPpgkDDLCCIMYTSGSTGEPKGVVLKHSNVVA 289
Cdd:PRK12316 649 GTELNP---ENLAYVIYTSGSTGKPKGAGNRHRALSN 682
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
486-558 |
5.49e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 43.01 E-value: 5.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 486 TVKLVDVEELGYFAKNNQGEVWITGANVTPEYYKNEEETSQ----------ALTSDG-WFKTGDIGeWEANGHLKIIDRK 554
Cdd:PRK05850 380 TVRIVDPDTCIECPAGTVGEIWVHGDNVAAGYWQKPEETERtfgatlvdpsPGTPEGpWLRTGDLG-FISEGELFIVGRI 458
|
....
gi 398366229 555 KNLV 558
Cdd:PRK05850 459 KDLL 462
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
504-554 |
5.79e-04 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 42.97 E-value: 5.79e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 398366229 504 GEVWITGANVTPEYYKNEEETSQALTSDGWFKTGDIGEWEANGHLKIIDRK 554
Cdd:PRK08276 341 GTVYFEMDGYPFEYHNDPEKTAAARNPHGWVTVGDVGYLDEDGYLYLTDRK 391
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
258-288 |
8.58e-04 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 42.72 E-value: 8.58e-04
10 20 30
....*....|....*....|....*....|.
gi 398366229 258 PPGKDDLCCIMYTSGSTGEPKGVVLKHSNVV 288
Cdd:PRK10252 594 LSQPHHTAYIIFTSGSTGRPKGVMVGQTAIV 624
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
427-574 |
1.13e-03 |
|
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: 42.10 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 427 LRYLLNGGSPISRDAQE-FITNLICPMLIGYGLTETCASTTILDPANFELGVAGDLTGCVTVKLVDVE----ELGyfakn 501
Cdd:cd05970 303 LRYCTTAGEALNPEVFNtFKEKTGIKLMEGFGQTETTLTIATFPWMEPKPGSMGKPAPGYEIDLIDREgrscEAG----- 377
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398366229 502 NQGEVWITGANVTP-----EYYKNEEETSQALtSDGWFKTGDIGEWEANGHLKIIDRKKNLVKTmNGEYIALEKLESV 574
Cdd:cd05970 378 EEGEIVIRTSKGKPvglfgGYYKDAEKTAEVW-HDGYYHTGDAAWMDEDGYLWFVGRTDDLIKS-SGYRIGPFEVESA 453
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
217-281 |
1.22e-03 |
|
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.
Pssm-ID: 341271 [Multi-domain] Cd Length: 617 Bit Score: 41.92 E-value: 1.22e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398366229 217 IYQSAHDAINRIKEVRPDIKT--------FSFDDILKlgkeSCNEIDVHPPGKDDLCCIMYTSGSTGEPKGVV 281
Cdd:cd05967 181 LELSGHKPHHVLVLNRPQVPAdltkpgrdLDWSELLA----KAEPVDCVPVAATDPLYILYTSGTTGKPKGVV 249
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
432-588 |
1.31e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 41.98 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 432 NGGSPisRDAQEFITNLICPMLIGYGLTETCASTT-ILDPANFELGVAGDltgcvTVKLVDVE--------ELGYFAKNN 502
Cdd:PRK07867 275 NEGAP--GDIARFARRFGCVVVDGFGSTEGGVAITrTPDTPPGALGPLPP-----GVAIVDPDtgtecppaEDADGRLLN 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 503 Q----GE-VWITGANVTPEYYKNEEETSQALtSDGWFKTGDIGEWEANGHLKIIDRKKNLVKtMNGEYIALEKLESVYRS 577
Cdd:PRK07867 348 AdeaiGElVNTAGPGGFEGYYNDPEADAERM-RGGVYWSGDLAYRDADGYAYFAGRLGDWMR-VDGENLGTAPIERILLR 425
|
170
....*....|.
gi 398366229 578 NEYVANICVYA 588
Cdd:PRK07867 426 YPDATEVAVYA 436
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
240-593 |
1.56e-03 |
|
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: 41.65 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 240 FDDILKLGKESCNEIdvHPPGKDDLCCIMYTSGSTGEPKGVVLKHSnvvagvgGASLNVLKfVGNTDRV--------ICF 311
Cdd:cd05915 133 GYLAYEEALGEEADP--VRVPERAACGMAYTTGTTGLPKGVVYSHR-------ALVLHSLA-ASLVDGTalsekdvvLPV 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 312 LPLAHifelvfellsfywgaCIGYATVKTLTS-----SSVRNCQGDLQEFKPTIMVGVAAVWETvrKGILNQIDNLPFLT 386
Cdd:cd05915 203 VPMFH---------------VNAWCLPYAATLvgakqVLPGPRLDPASLVELFDGEGVTFTAGV--PTVWLALADYLEST 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 387 KKIF-WTayntklnmqrLHIPGGGA--------LGNLVFKKIRTATGGQLRYLLNGGSPISRDAQEFITNLICPMLIGYG 457
Cdd:cd05915 266 GHRLkTL----------RRLVVGGSaaprsliaRFERMGVEVRQGYGLTETSPVVVQNFVKSHLESLSEEEKLTLKAKTG 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 458 LTETCASTTILDPANFELGVAGDltgcvTVKLVDVEelgyfaknnqgevwitGANVTPEYYKNEEETSQALTSDGWFKTG 537
Cdd:cd05915 336 LPIPLVRLRVADEEGRPVPKDGK-----ALGEVQLK----------------GPWITGGYYGNEEATRSALTPDGFFRTG 394
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 398366229 538 DIGEWEANGHLKIIDRKKNLVkTMNGEYIALEKLESVYRSNEYVANICVYADQSKT 593
Cdd:cd05915 395 DIAVWDEEGYVEIKDRLKDLI-KSGGEWISSVDLENALMGHPKVKEAAVVAIPHPK 449
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
252-316 |
2.79e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 40.82 E-value: 2.79e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398366229 252 NEIDVHPPGKDDLCCIMYTSGSTGEPKGVVLKHSNVVagVGGASLNVLKFVGNTDRVICFLPLAH 316
Cdd:PRK07867 142 AEPPFRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVA--SAGVMLAQRFGLGPDDVCYVSMPLFH 204
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
112-300 |
3.43e-03 |
|
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.
Pssm-ID: 341265 [Multi-domain] Cd Length: 629 Bit Score: 40.72 E-value: 3.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 112 IGRGLVKIGLKPNDDDKLHLYAATSHkwmkmfLGAqsqgIPVVTAYDTlGEKGLIHSLVQTGSKAIFTDNS--------- 182
Cdd:cd05943 120 VKPGDRVAGYLPNIPEAVVAMLATAS------IGA----IWSSCSPDF-GVPGVLDRFGQIEPKVLFAVDAytyngkrhd 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 183 LLPSLIKPVQAAQDVKYIIHFDSISSEdrrqsgkiyqSAHDAinrikevRPDIKTFSFDDILklGKESCNEIDVHPPGKD 262
Cdd:cd05943 189 VREKVAELVKGLPSLLAVVVVPYTVAA----------GQPDL-------SKIAKALTLEDFL--ATGAAGELEFEPLPFD 249
|
170 180 190
....*....|....*....|....*....|....*...
gi 398366229 263 DLCCIMYTSGSTGEPKGVVlkHsnvvaGVGGASLNVLK 300
Cdd:cd05943 250 HPLYILYSSGTTGLPKCIV--H-----GAGGTLLQHLK 280
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
230-289 |
4.07e-03 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 40.26 E-value: 4.07e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 230 EVRPDIKTFSFDdilKLGKESCNEIDVHPPGKDDLCCIMYTSGSTGEPKGVVLKHSNVVA 289
Cdd:PRK04319 176 DVEEGPGTLDFN---ALMEQASDEFDIEWTDREDGAILHYTSGSTGKPKGVLHVHNAMLQ 232
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
267-285 |
4.53e-03 |
|
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.
Pssm-ID: 341270 [Multi-domain] Cd Length: 608 Bit Score: 40.24 E-value: 4.53e-03
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
267-285 |
5.15e-03 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 40.12 E-value: 5.15e-03
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
217-296 |
6.25e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 39.87 E-value: 6.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366229 217 IYQSAHDAinRIKEVRPD---IKTF----------------SFDDILKLGKEscnEIDVHPPGKDDLCcIMYTSGSTGEP 277
Cdd:PRK07798 105 VYEREFAP--RVAEVLPRlpkLRTLvvvedgsgndllpgavDYEDALAAGSP---ERDFGERSPDDLY-LLYTGGTTGMP 178
|
90 100
....*....|....*....|
gi 398366229 278 KGVVLKHSNV-VAGVGGASL 296
Cdd:PRK07798 179 KGVMWRQEDIfRVLLGGRDF 198
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
252-285 |
9.58e-03 |
|
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called acetyl-CoA synthetase and acetyl-activating enzyme. It catalyzes the reaction ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA and belongs to the family of AMP-binding enzymes described by pfam00501.
Pssm-ID: 274022 [Multi-domain] Cd Length: 626 Bit Score: 39.15 E-value: 9.58e-03
10 20 30
....*....|....*....|....*....|....*..
gi 398366229 252 NEIDVHPP---GKDDLCCIMYTSGSTGEPKGVVlkHS 285
Cdd:TIGR02188 224 KASAYCEPepmDSEDPLFILYTSGSTGKPKGVL--HT 258
|
|
| |
