|
Name |
Accession |
Description |
Interval |
E-value |
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
121-696 |
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: 826.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 121 GNYKWINYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASY 200
Cdd:cd17639 1 GEYKYMSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECSA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 201 LITSvellesklkaalvdincvkhiiyvdnktinraeypegleihsmqsveelgakpenlsvppsrPTPSDMAIVMYTSG 280
Cdd:cd17639 81 IFTD--------------------------------------------------------------GKPDDLACIMYTSG 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 281 STGRPKGVMMHHSNLIAGMTGQCERIPG-LGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSSPLTLSDqssKIKKGS 359
Cdd:cd17639 99 STGNPKGVMLTHGNLVAGIAGLGDRVPElLGPDDRYLAYLPLAHIFELAAENVCLYRGGTIGYGSPRTLTD---KSKRGC 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 360 KGDCTVLKPTLMAAVPEIMDRIYKNVMSKVQEMNYVQKTLFKIGYDYKLEQIKKGYDAPLCNLILFKKVKALLGGNVRMM 439
Cdd:cd17639 176 KGDLTEFKPTLMVGVPAIWDTIRKGVLAKLNPMGGLKRTLFWTAYQSKLKALKEGPGTPLLDELVFKKVRAALGGRLRYM 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 440 LSGGAPLSPQTHRFMNVcFCCPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDWQEGGYtVHDKPNPRGEI 519
Cdd:cd17639 256 LSGGAPLSADTQEFLNI-VLCPVIQGYGLTETCAGGTVQDPGDLETGRVGPPLPCCEIKLVDWEEGGY-STDKPPPRGEI 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 520 VIGGQNISMGYFKNEEKTAEDYcvdeNGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGEYVSLGKVEAALKNCPLID 599
Cdd:cd17639 334 LIRGPNVFKGYYKNPEKTKEAF----DGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQNGEYIALEKLESIYRSNPLVN 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 600 NICAFAKSDQSYVISFVVPNQKKLTLLAQQKGV-EGSWVDICNNPAMEAEILKEIREAANAMKLERFEIPIKVRLSPEPW 678
Cdd:cd17639 410 NICVYADPDKSYPVAIVVPNEKHLTKLAEKHGViNSEWEELCEDKKLQKAVLKSLAETARAAGLEKFEIPQGVVLLDEEW 489
|
570
....*....|....*...
gi 1720435377 679 TPETGLVTDAFKLKRKEL 696
Cdd:cd17639 490 TPENGLVTAAQKLKRKEI 507
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
32-708 |
0e+00 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 811.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 32 FLTNAKKKnamAKRIKAKPTSDKPGSPYRSvTHFDSLavIDIP--GADTLDKLFDHAVAKFGKKDSLGTREILSEENEMQ 109
Cdd:PLN02387 17 LLRGSKKG---KKRGVPVDVGGEPGYAIRN-ARFPEL--VETPweGATTLAALFEQSCKKYSDKRLLGTRKLISREFETS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 110 PNGKVFKKLILGNYKWINYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAV 189
Cdd:PLN02387 91 SDGRKFEKLHLGEYEWITYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEAL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 190 VHGLNESEASYLITSVELLEsKLKAALVDINCVKHIIYVDNKTINRAEYPEGLE---IHSMQSVEELGakpENLSVPPSR 266
Cdd:PLN02387 171 CHSLNETEVTTVICDSKQLK-KLIDISSQLETVKRVIYMDDEGVDSDSSLSGSSnwtVSSFSEVEKLG---KENPVDPDL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 267 PTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPGLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSSPL 346
Cdd:PLN02387 247 PSPNDIAVIMYTSGSTGLPKGVMMTHGNIVATVAGVMTVVPKLGKNDVYLAYLPLAHILELAAESVMAAVGAAIGYGSPL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 347 TLSDQSSKIKKGSKGDCTVLKPTLMAAVPEIMDRIYKNVMSKVQEMNYVQKTLFKIGYDYKLEQIKK------GYDAPLC 420
Cdd:PLN02387 327 TLTDTSNKIKKGTKGDASALKPTLMTAVPAILDRVRDGVRKKVDAKGGLAKKLFDIAYKRRLAAIEGswfgawGLEKLLW 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 421 NLILFKKVKALLGGNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLK 500
Cdd:PLN02387 407 DALVFKKIRAVLGGRIRFMLSGGAPLSGDTQRFINICLGAPIGQGYGLTETCAGATFSEWDDTSVGRVGPPLPCCYVKLV 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 501 DWQEGGYTVHDKPNPRGEIVIGGQNISMGYFKNEEKTAEDYCVDENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAG 580
Cdd:PLN02387 487 SWEEGGYLISDKPMPRGEIVIGGPSVTLGYFKNQEKTDEVYKVDERGMRWFYTGDIGQFHPDGCLEIIDRKKDIVKLQHG 566
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 581 EYVSLGKVEAALKNCPLIDNICAFAKSDQSYVISFVVPNQKKLTLLAQQKGVE-GSWVDICNNPAMEAEILKEIREAANA 659
Cdd:PLN02387 567 EYVSLGKVEAALSVSPYVDNIMVHADPFHSYCVALVVPSQQALEKWAKKAGIDySNFAELCEKEEAVKEVQQSLSKAAKA 646
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 1720435377 660 MKLERFEIPIKVRLSPEPWTPETGLVTDAFKLKRKELKNHYLKDIERMY 708
Cdd:PLN02387 647 ARLEKFEIPAKIKLLPEPWTPESGLVTAALKLKREQIRKKFKDDLKKLY 695
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
121-708 |
0e+00 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.
Pssm-ID: 341250 [Multi-domain] Cd Length: 545 Bit Score: 534.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 121 GNYKWINYLEVNCRVNNFGSGLTALGLKPKNT--IAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEA 198
Cdd:cd05927 1 GPYEWISYKEVAERADNIGSALRSLGGKPAPAsfVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 199 SylitsvellesklkaalvdincvkhIIYVDnktinraeypEGLEIHSMQSVEELGAKPEnlsVPPSRPTPSDMAIVMYT 278
Cdd:cd05927 81 S-------------------------IVFCD----------AGVKVYSLEEFEKLGKKNK---VPPPPPKPEDLATICYT 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 279 SGSTGRPKGVMMHHSNLIAGMTGQC---ERIPGLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSS--PLTLSDqss 353
Cdd:cd05927 123 SGTTGNPKGVMLTHGNIVSNVAGVFkilEILNKINPTDVYISYLPLAHIFERVVEALFLYHGAKIGFYSgdIRLLLD--- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 354 kikkgskgDCTVLKPTLMAAVPEIMDRIYKNVMSKVQEMNYVQKTLFKIGYDYKLEQIKKG--YDAPLCNLILFKKVKAL 431
Cdd:cd05927 200 --------DIKALKPTVFPGVPRVLNRIYDKIFNKVQAKGPLKRKLFNFALNYKLAELRSGvvRASPFWDKLVFNKIKQA 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 432 LGGNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDWQEGGYTVhD 511
Cdd:cd05927 272 LGGNVRLMLTGSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAEVKLVDVPEMNYDA-K 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 512 KPNPRGEIVIGGQNISMGYFKNEEKTAEDycVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGEYVSLGKVEAA 591
Cdd:cd05927 351 DPNPRGEVCIRGPNVFSGYYKDPEKTAEA--LDEDG--WLHTGDIGEWLPNGTLKIIDRKKNIFKLSQGEYVAPEKIENI 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 592 LKNCPLIDNICAFAKSDQSYVISFVVPNQKKLTLLAQQK-GVEGSWVDICNNPAMEAEILKEIREAANAMKLERFEIPIK 670
Cdd:cd05927 427 YARSPFVAQIFVYGDSLKSFLVAIVVPDPDVLKEWAASKgGGTGSFEELCKNPEVKKAILEDLVRLGKENGLKGFEQVKA 506
|
570 580 590
....*....|....*....|....*....|....*...
gi 1720435377 671 VRLSPEPWTPETGLVTDAFKLKRKELKNHYLKDIERMY 708
Cdd:cd05927 507 IHLEPEPFSVENGLLTPTFKLKRPQLKKYYKKQIDEMY 544
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
72-711 |
1.51e-151 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 453.40 E-value: 1.51e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 72 DIPGADTLDKLFDHAVAKFGKKDSLGTREilseenemqpngkvfkkliLGNYKWINYLEVNCRVNNFGSGLTALGLKPKN 151
Cdd:COG1022 6 DVPPADTLPDLLRRRAARFPDRVALREKE-------------------DGIWQSLTWAEFAERVRALAAGLLALGVKPGD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 152 TIAIFCETRAEWMIA--------AQTcfkynfplVTLYATLGREAVVHGLNESEASYLITSVELLESKLKAALVDINCVK 223
Cdd:COG1022 67 RVAILSDNRPEWVIAdlailaagAVT--------VPIYPTSSAEEVAYILNDSGAKVLFVEDQEQLDKLLEVRDELPSLR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 224 HIIYVDNKTInraeyPEGLEIHSMQSVEELGAK---PENLSVPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMT 300
Cdd:COG1022 139 HIVVLDPRGL-----RDDPRLLSLDELLALGREvadPAELEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNAR 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 301 GQCERIPgLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYS-SPLTLSDqsskikkgskgDCTVLKPTLMAAVPEIMD 379
Cdd:COG1022 214 ALLERLP-LGPGDRTLSFLPLAHVFERTVSYYALAAGATVAFAeSPDTLAE-----------DLREVKPTFMLAVPRVWE 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 380 RIYKNVMSKVQEMNYVQKTLF----KIGYDYKlEQIKKGYDAP--------LCNLILFKKVKALLGGNVRMMLSGGAPLS 447
Cdd:COG1022 282 KVYAGIQAKAEEAGGLKRKLFrwalAVGRRYA-RARLAGKSPSlllrlkhaLADKLVFSKLREALGGRLRFAVSGGAALG 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 448 PQTHRF---MNVcfccPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLkdwqeggytvhdkpNPRGEIVIGGQ 524
Cdd:COG1022 361 PELARFfraLGI----PVLEGYGLTETSPVITVNRPGDNRIGTVGPPLPGVEVKI--------------AEDGEILVRGP 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 525 NISMGYFKNEEKTAEDycVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGEYVSLGKVEAALKNCPLIDNICAF 604
Cdd:COG1022 423 NVMKGYYKNPEATAEA--FDADG--WLHTGDIGELDEDGFLRITGRKKDLIVTSGGKNVAPQPIENALKASPLIEQAVVV 498
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 605 AkSDQSYVISFVVPNQKKLTLLAQQKGVE-GSWVDICNNPAMEAEILKEIrEAANAmKLERFEIPIKVRLSPEPWTPETG 683
Cdd:COG1022 499 G-DGRPFLAALIVPDFEALGEWAEENGLPyTSYAELAQDPEVRALIQEEV-DRANA-GLSRAEQIKRFRLLPKEFTIENG 575
|
650 660
....*....|....*....|....*...
gi 1720435377 684 LVTDAFKLKRKELKNHYLKDIERMYGGK 711
Cdd:COG1022 576 ELTPTLKLKRKVILEKYADLIEALYAGA 603
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
56-708 |
4.70e-151 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 453.79 E-value: 4.70e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 56 GSPYRSVTHFDslaviDIPGADTLDKLFDHAVAKFGKKDSLGTReilseeneMQPNGKVfkklilGNYKWINYLEVNCRV 135
Cdd:PLN02736 28 RSPLKLVSRFP-----DHPEIGTLHDNFVYAVETFRDYKYLGTR--------IRVDGTV------GEYKWMTYGEAGTAR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 136 NNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASYLITSVELLESKLkAA 215
Cdd:PLN02736 89 TAIGSGLVQHGIPKGACVGLYFINRPEWLIVDHACSAYSYVSVPLYDTLGPDAVKFIVNHAEVAAIFCVPQTLNTLL-SC 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 216 LVDINCVKHIIYVDNKTINRAEYPE--GLEIHSMQSVEELGAKPenlSVPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHS 293
Cdd:PLN02736 168 LSEIPSVRLIVVVGGADEPLPSLPSgtGVEIVTYSKLLAQGRSS---PQPFRPPKPEDVATICYTSGTTGTPKGVVLTHG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 294 NLIAGMTGQCERIPgLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSSP--LTLSDqsskikkgskgDCTVLKPTLM 371
Cdd:PLN02736 245 NLIANVAGSSLSTK-FYPSDVHISYLPLAHIYERVNQIVMLHYGVAVGFYQGdnLKLMD-----------DLAALRPTIF 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 372 AAVPEIMDRIYKNVMSKVQEMNYVQKTLFKIGYDYKLEQIKKGYD-APLCNLILFKKVKALLGGNVRMMLSGGAPLSPQT 450
Cdd:PLN02736 313 CSVPRLYNRIYDGITNAVKESGGLKERLFNAAYNAKKQALENGKNpSPMWDRLVFNKIKAKLGGRVRFMSSGASPLSPDV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 451 HRFMNVCFCCPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDWQEGGYTVHDKPNPRGEIVIGGQNISMGY 530
Cdd:PLN02736 393 MEFLRICFGGRVLEGYGMTETSCVISGMDEGDNLSGHVGSPNPACEVKLVDVPEMNYTSEDQPYPRGEICVRGPIIFKGY 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 531 FKNEEKTAEdyCVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGEYVSLGKVEAALKNCPLIDNICAFAKSDQS 610
Cdd:PLN02736 473 YKDEVQTRE--VIDEDG--WLHTGDIGLWLPGGRLKIIDRKKNIFKLAQGEYIAPEKIENVYAKCKFVAQCFVYGDSLNS 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 611 YVISFVVPNQKKLTLLAQQKGVE-GSWVDICNNPAMEAEILKEIREAANAMKLERFEIPIKVRLSPEPWTPETGLVTDAF 689
Cdd:PLN02736 549 SLVAVVVVDPEVLKAWAASEGIKyEDLKQLCNDPRVRAAVLADMDAVGREAQLRGFEFAKAVTLVPEPFTVENGLLTPTF 628
|
650
....*....|....*....
gi 1720435377 690 KLKRKELKNHYLKDIERMY 708
Cdd:PLN02736 629 KVKRPQAKAYFAKAISDMY 647
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
124-708 |
3.03e-144 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 437.87 E-value: 3.03e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 124 KWINYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASYLIT 203
Cdd:PTZ00216 120 RYITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAIVC 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 204 S---VELLESKLKAALVDiNCVkhIIYVDnktinraEYPEGLEIHSMQ-----SVEELGAKPENlSVPPSRPTPSD-MAI 274
Cdd:PTZ00216 200 NgknVPNLLRLMKSGGMP-NTT--IIYLD-------SLPASVDTEGCRlvawtDVVAKGHSAGS-HHPLNIPENNDdLAL 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 275 VMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPGL-GPK---DTYIGYLPLAHVLELTAEISCFTYGCRIGYSSPLTLSD 350
Cdd:PTZ00216 269 IMYTSGTTGDPKGVMHTHGSLTAGILALEDRLNDLiGPPeedETYCSYLPLAHIMEFGVTNIFLARGALIGFGSPRTLTD 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 351 QSSKikkgSKGDCTVLKPTLMAAVPEIMDRIYKNVMSKVQEMNYVQKTLFKIGYDYKLEQIKKGYDAPLCNLILFKKVKA 430
Cdd:PTZ00216 349 TFAR----PHGDLTEFRPVFLIGVPRIFDTIKKAVEAKLPPVGSLKRRVFDHAYQSRLRALKEGKDTPYWNEKVFSAPRA 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 431 LLGGNVRMMLSGGAPLSPQTHRFMNVCFcCPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDWQEGGYTvh 510
Cdd:PTZ00216 425 VLGGRVRAMLSGGGPLSAATQEFVNVVF-GMVIQGWGLTETVCCGGIQRTGDLEPNAVGQLLKGVEMKLLDTEEYKHT-- 501
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 511 DKPNPRGEIVIGGQNISMGYFKNEEKTAEdyCVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGEYVSLGKVEA 590
Cdd:PTZ00216 502 DTPEPRGEILLRGPFLFKGYYKQEELTRE--VLDEDG--WFHTGDVGSIAANGTLRIIGRVKALAKNCLGEYIALEALEA 577
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 591 ALKNCPLIDN--ICAFAKSDQSYVISFVVPNQKKLTLLAQQKGVEGSWVDICNNPAMEAEILKEIREAANAMKLERFEIP 668
Cdd:PTZ00216 578 LYGQNELVVPngVCVLVHPARSYICALVLTDEAKAMAFAKEHGIEGEYPAILKDPEFQKKATESLQETARAAGRKSFEIV 657
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 1720435377 669 IKVRLSPEPWTPETGLVTDAFKLKRKELKNHYLKDIERMY 708
Cdd:PTZ00216 658 RHVRVLSDEWTPENGVLTAAMKLKRRVIDERYADLIKELF 697
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
121-696 |
2.68e-134 |
|
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341233 [Multi-domain] Cd Length: 452 Bit Score: 403.51 E-value: 2.68e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 121 GNYKWINYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASY 200
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 201 LITSvellesklkaalvdincvkhiiyvdnktinraeypegleihsmqsveelgakpenlsvppsrpTPSDMAIVMYTSG 280
Cdd:cd05907 81 LFVE---------------------------------------------------------------DPDDLATIIYTSG 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 281 STGRPKGVMMHHSNLIAGMTGQCERIPgLGPKDTYIGYLPLAHVLE-LTAEISCFTYGCRIGYSSPL-TLSDQSSKIkkg 358
Cdd:cd05907 98 TTGRPKGVMLSHRNILSNALALAERLP-ATEGDRHLSFLPLAHVFErRAGLYVPLLAGARIYFASSAeTLLDDLSEV--- 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 359 skgdctvlKPTLMAAVPEIMDRIYKNVmsKVQEMNYVQKTLFKIGydykleqikkgydaplcnlilfkkvkalLGGNVRM 438
Cdd:cd05907 174 --------RPTVFLAVPRVWEKVYAAI--KVKAVPGLKRKLFDLA----------------------------VGGRLRF 215
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 439 MLSGGAPLSPQTHRFMNVcFCCPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDwqeggytvhdkpnpRGE 518
Cdd:cd05907 216 AASGGAPLPAELLHFFRA-LGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVEVRIAD--------------DGE 280
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 519 IVIGGQNISMGYFKNEEKTAEDycVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGEYVSLGKVEAALKNCPLI 598
Cdd:cd05907 281 ILVRGPNVMLGYYKNPEATAEA--LDADG--WLHTGDLGEIDEDGFLHITGRKKDLIITSGGKNISPEPIENALKASPLI 356
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 599 DNICAFAkSDQSYVISFVVPNQKKLTLLAQQKGVEG-SWVDICNNPAMEAEILKEIrEAANAmKLERFEIPIKVRLSPEP 677
Cdd:cd05907 357 SQAVVIG-DGRPFLVALIVPDPEALEAWAEEHGIAYtDVAELAANPAVRAEIEAAV-EAANA-RLSRYEQIKKFLLLPEP 433
|
570
....*....|....*....
gi 1720435377 678 WTPETGLVTDAFKLKRKEL 696
Cdd:cd05907 434 FTIENGELTPTLKLKRPVI 452
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
44-708 |
1.32e-122 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 380.31 E-value: 1.32e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 44 KRIKAKPTSdkpGSPYRSVTHFDSLAVIDiPGADTLDKLFDHAVAKFGKKDSLGTREILseenemqpNGKVfkklilGNY 123
Cdd:PLN02430 13 KGKDGKPSV---GPVYRNLLSKKGFPPID-SDITTAWDIFSKSVEKYPDNKMLGWRRIV--------DGKV------GPY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 124 KWINYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEasylIT 203
Cdd:PLN02430 75 MWKTYKEVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVAMEACAAHSLICVPLYDTLGPGAVDYIVDHAE----ID 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 204 SVELLESKLKAaLVDINC-----VKHIIYVDNKTINRAEYPEGLEIHSMQSVEELGAKPENLSvPPSRPTPSDMAIVMYT 278
Cdd:PLN02430 151 FVFVQDKKIKE-LLEPDCksakrLKAIVSFTSVTEEESDKASQIGVKTYSWIDFLHMGKENPS-ETNPPKPLDICTIMYT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 279 SGSTGRPKGVMMHHSNLIAGMTG------QCEriPGLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSSpltlSDQS 352
Cdd:PLN02430 229 SGTSGDPKGVVLTHEAVATFVRGvdlfmeQFE--DKMTHDDVYLSFLPLAHILDRMIEEYFFRKGASVGYYH----GDLN 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 353 SKikkgsKGDCTVLKPTLMAAVPEIMDRIYKNVMSKVQEMNYVQKTLFKIGYDYKLEQIKKGYD----APLCNLILFKKV 428
Cdd:PLN02430 303 AL-----RDDLMELKPTLLAGVPRVFERIHEGIQKALQELNPRRRLIFNALYKYKLAWMNRGYShkkaSPMADFLAFRKV 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 429 KALLGGNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVTEVTDYTT-GRVGAPLICCEIKLKDWQEGGY 507
Cdd:PLN02430 378 KAKLGGRLRLLISGGAPLSTEIEEFLRVTSCAFVVQGYGLTETLGPTTLGFPDEMCMlGTVGAPAVYNELRLEEVPEMGY 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 508 TVHDKPnPRGEIVIGGQNISMGYFKNEEKTAEdycVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGEYVSLGK 587
Cdd:PLN02430 458 DPLGEP-PRGEICVRGKCLFSGYYKNPELTEE---VMKDG--WFHTGDIGEILPNGVLKIIDRKKNLIKLSQGEYVALEY 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 588 VEAALKNCPLIDNICAFAKSDQSYVISFVVPNQKKLTLLAQQKGVEGSWVDICNNPAMEAEILKEIREAANAMKLERFEI 667
Cdd:PLN02430 532 LENVYGQNPIVEDIWVYGDSFKSMLVAVVVPNEENTNKWAKDNGFTGSFEELCSLPELKEHILSELKSTAEKNKLRGFEY 611
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1720435377 668 PIKVRLSPEPWTPETGLVTDAFKLKRKELKNHYLKDIERMY 708
Cdd:PLN02430 612 IKGVILETKPFDVERDLVTATLKKRRNNLLKYYQVEIDEMY 652
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
47-708 |
1.70e-114 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 359.54 E-value: 1.70e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 47 KAKPTSD-KP--GSPYRSVTHFDSLavIDIP-GADTLDKLFDHAVAKFGKKDSLGTREILseenemqpNGKVfkklilGN 122
Cdd:PLN02861 11 ESRPATGgKPsaGPVYRSIYAKDGL--LDLPaDIDSPWQFFSDAVKKYPNNQMLGRRQVT--------DSKV------GP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 123 YKWINYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASylI 202
Cdd:PLN02861 75 YVWLTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVS--I 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 203 TSVEllESKLKAAL-VDINCVKHIIYV----DNKTINRAEYPE-GLEIHSMQSVEELGAKPENLsvPPSRPTpsDMAIVM 276
Cdd:PLN02861 153 AFVQ--ESKISSILsCLPKCSSNLKTIvsfgDVSSEQKEEAEElGVSCFSWEEFSLMGSLDCEL--PPKQKT--DICTIM 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 277 YTSGSTGRPKGVMMHHSNLIAG------MTGQCERIpgLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSSpltlSD 350
Cdd:PLN02861 227 YTSGTTGEPKGVILTNRAIIAEvlstdhLLKVTDRV--ATEEDSYFSYLPLAHVYDQVIETYCISKGASIGFWQ----GD 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 351 QSSKIKkgskgDCTVLKPTLMAAVPEIMDRIYKNVMSKVQEMNYVQKTLFKIGYDYKLEQIKKGYD----APLCNLILFK 426
Cdd:PLN02861 301 IRYLME-----DVQALKPTIFCGVPRVYDRIYTGIMQKISSGGMLRKKLFDFAYNYKLGNLRKGLKqeeaSPRLDRLVFD 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 427 KVKALLGGNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGaGTVTEVTDY--TTGRVGAPLICCEIKLKDWQE 504
Cdd:PLN02861 376 KIKEGLGGRVRLLLSGAAPLPRHVEEFLRVTSCSVLSQGYGLTESCG-GCFTSIANVfsMVGTVGVPMTTIEARLESVPE 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 505 GGYTVHDKPnPRGEIVIGGQNISMGYFKNEEKTAEdycVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGEYVS 584
Cdd:PLN02861 455 MGYDALSDV-PRGEICLRGNTLFSGYHKRQDLTEE---VLIDG--WFHTGDIGEWQPNGAMKIIDRKKNIFKLSQGEYVA 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 585 LGKVEAALKNCPLIDNICAFAKSDQSYVISFVVPNQKKLTLLAQQKGVEGSWVDICNNPAMEAEILKEIREAANAMKLER 664
Cdd:PLN02861 529 VENLENTYSRCPLIASIWVYGNSFESFLVAVVVPDRQALEDWAANNNKTGDFKSLCKNLKARKYILDELNSTGKKLQLRG 608
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 1720435377 665 FEIPIKVRLSPEPWTPETGLVTDAFKLKRKELKNHYLKDIERMY 708
Cdd:PLN02861 609 FEMLKAIHLEPNPFDIERDLITPTFKLKRPQLLKYYKDCIDQLY 652
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
118-578 |
1.40e-112 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 346.22 E-value: 1.40e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 118 LILGNYKWINYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESE 197
Cdd:pfam00501 14 LEVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 198 ASYLITSVELLESKLKAALVDINCVKHIIYVDNKTINRAEypegleihsmqSVEELGAKPENLSVPPSRPTPSDMAIVMY 277
Cdd:pfam00501 94 AKVLITDDALKLEELLEALGKLEVVKLVLVLDRDPVLKEE-----------PLPEEAKPADVPPPPPPPPDPDDLAYIIY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 278 TSGSTGRPKGVMMHHSNLIAGMTGQ---CERIPGLGPKDTYIGYLPLAHVLELTAEI-SCFTYGCRIGYSSPLTLSDQss 353
Cdd:pfam00501 163 TSGTTGKPKGVMLTHRNLVANVLSIkrvRPRGFGLGPDDRVLSTLPLFHDFGLSLGLlGPLLAGATVVLPPGFPALDP-- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 354 kikKGSKGDCTVLKPTLMAAVPEIMDRIYKNvmskvqemnyvqktlfkigydykleqikkgydaplcnlilfKKVKALLG 433
Cdd:pfam00501 241 ---AALLELIERYKVTVLYGVPTLLNMLLEA-----------------------------------------GAPKRALL 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 434 GNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVT---EVTDYTTGRVGAPLICCEIKLKDWQEGGYTVH 510
Cdd:pfam00501 277 SSLRLVLSGGAPLPPELARRFRELFGGALVNGYGLTETTGVVTTPlplDEDLRSLGSVGRPLPGTEVKIVDDETGEPVPP 356
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720435377 511 DKPnprGEIVIGGQNISMGYFKNEEKTAEDYCVDengqRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQ 578
Cdd:pfam00501 357 GEP---GELCVRGPGVMKGYLNDPELTAEAFDED----GWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
48-708 |
3.46e-112 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 353.56 E-value: 3.46e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 48 AKPTSD-KP--GSPYRSVTHFDSLAViDIPGADTLDKLFDHAVAKFGKKDSLGTREILseenemqpNGKVfkklilGNYK 124
Cdd:PLN02614 14 GKEGSDgRPsvGPVYRSIFAKDGFPN-PIEGMDSCWDVFRMSVEKYPNNPMLGRREIV--------DGKP------GKYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 125 WINYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASYLITS 204
Cdd:PLN02614 79 WQTYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 205 VELLESKLKAALVDINCVKHIIYVDNKTINRAEYPE--GLEIHSMQSVEELGaKPENLSVPPSRPtpSDMAIVMYTSGST 282
Cdd:PLN02614 159 EKKISELFKTCPNSTEYMKTVVSFGGVSREQKEEAEtfGLVIYAWDEFLKLG-EGKQYDLPIKKK--SDICTIMYTSGTT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 283 GRPKGVMMHHSNLIAGMTGQCERI----PGLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSSpltlSDQSSKIKkg 358
Cdd:PLN02614 236 GDPKGVMISNESIVTLIAGVIRLLksanAALTVKDVYLSYLPLAHIFDRVIEECFIQHGAAIGFWR----GDVKLLIE-- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 359 skgDCTVLKPTLMAAVPEIMDRIYKNVMSKVQEMNYVQKTLFKIGYDYKLEQIKKGYD----APLCNLILFKKVKALLGG 434
Cdd:PLN02614 310 ---DLGELKPTIFCAVPRVLDRVYSGLQKKLSDGGFLKKFVFDSAFSYKFGNMKKGQShveaSPLCDKLVFNKVKQGLGG 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 435 NVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCgAGTVTEVTDY--TTGRVGAPLICCEIKLKDWQEGGYTVHDK 512
Cdd:PLN02614 387 NVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTESC-AGTFVSLPDEldMLGTVGPPVPNVDIRLESVPEMEYDALAS 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 513 pNPRGEIVIGGQNISMGYFKNEEKTAEDYcVDEngqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGEYVSLGKVEAAL 592
Cdd:PLN02614 466 -TPRGEICIRGKTLFSGYYKREDLTKEVL-IDG----WLHTGDVGEWQPNGSMKIIDRKKNIFKLSQGEYVAVENIENIY 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 593 KNCPLIDNICAFAKSDQSYVISFVVPNQKKLTLLAQQKGVEGSWVDICNNPAMEAEILKEIREAANAMKLERFEIPIKVR 672
Cdd:PLN02614 540 GEVQAVDSVWVYGNSFESFLVAIANPNQQILERWAAENGVSGDYNALCQNEKAKEFILGELVKMAKEKKMKGFEIIKAIH 619
|
650 660 670
....*....|....*....|....*....|....*.
gi 1720435377 673 LSPEPWTPETGLVTDAFKLKRKELKNHYLKDIERMY 708
Cdd:PLN02614 620 LDPVPFDMERDLLTPTFKKKRPQLLKYYQSVIDEMY 655
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
121-693 |
4.88e-70 |
|
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: 236.49 E-value: 4.88e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 121 GNYKWINYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFkynfplvtlyaTLGREAVVHGLNES--EA 198
Cdd:cd17640 1 KPPKRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIM-----------ALGAVDVVRGSDSSveEL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 199 SYLITSVEllesklkaalvdinCVkhIIYVDNktinraeypegleihsmqsveelgakpenlsvppsrpTPSDMAIVMYT 278
Cdd:cd17640 70 LYILNHSE--------------SV--ALVVEN-------------------------------------DSDDLATIIYT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 279 SGSTGRPKGVMMHHSNLIAGMTGQCERIPGlGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSSPLTLSDqsskikkg 358
Cdd:cd17640 97 SGTTGNPKGVMLTHANLLHQIRSLSDIVPP-QPGDRFLSILPIWHSYERSAEYFIFACGCSQAYTSIRTLKD-------- 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 359 skgDCTVLKPTLMAAVPEIMDRIYKNVMSKVQEMNYVQKTLFKIgydykleqikkgydaplcnlilfkkvkALLGGNVRM 438
Cdd:cd17640 168 ---DLKRVKPHYIVSVPRLWESLYSGIQKQVSKSSPIKQFLFLF---------------------------FLSGGIFKF 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 439 MLSGGAPLSPQTHRFMNVcFCCPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDWQEGGYTvhdKPNPRGE 518
Cdd:cd17640 218 GISGGGALPPHVDTFFEA-IGIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIVDPEGNVVL---PPGEKGI 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 519 IVIGGQNISMGYFKNEEKTAEdyCVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGEYVSLGKVEAALKNCPLI 598
Cdd:cd17640 294 VWVRGPQVMKGYYKNPEATSK--VLDSDG--WFNTGDLGWLTCGGELVLTGRAKDTIVLSNGENVEPQPIEEALMRSPFI 369
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 599 DNICAFAKsDQSYVISFVVPNQKKLTLLAQQKGV---EGSWVDICNNPAMEAEILKEIREAANAMKLERFEIPIKVRLSP 675
Cdd:cd17640 370 EQIMVVGQ-DQKRLGALIVPNFEELEKWAKESGVklaNDRSQLLASKKVLKLYKNEIKDEISNRPGFKSFEQIAPFALLE 448
|
570
....*....|....*...
gi 1720435377 676 EPWTpETGLVTDAFKLKR 693
Cdd:cd17640 449 EPFI-ENGEMTQTMKIKR 465
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
126-703 |
3.31e-63 |
|
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: 217.37 E-value: 3.31e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 126 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASYLITsv 205
Cdd:COG0318 25 LTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEELAYILEDSGARALVT-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 206 ellesklkaalvdincvkhiiyvdnktinraeypegleihsmqsveelgakpenlsvppsrptpsdmAIVMYTSGSTGRP 285
Cdd:COG0318 103 -------------------------------------------------------------------ALILYTSGTTGRP 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 286 KGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLAHVLELTAEI-SCFTYGCRI---GYSSPLTLSDQsskIKKGskg 361
Cdd:COG0318 116 KGVMLTHRNLLANAAAIAAAL-GLTPGDVVLVALPLFHVFGLTVGLlAPLLAGATLvllPRFDPERVLEL---IERE--- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 362 dctvlKPTLMAAVPEIMDRIyknvmskvqeMNYVQKTlfkigydykleqikkGYDAPlcnlilfkkvkallggNVRMMLS 441
Cdd:COG0318 189 -----RVTVLFGVPTMLARL----------LRHPEFA---------------RYDLS----------------SLRLVVS 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 442 GGAPLSPQT-HRFMNVcFCCPIGQGYGLTESCGAGTVT--EVTDYTTGRVGAPLICCEIKLKDwqEGGYTVhdKPNPRGE 518
Cdd:COG0318 223 GGAPLPPELlERFEER-FGVRIVEGYGLTETSPVVTVNpeDPGERRPGSVGRPLPGVEVRIVD--EDGREL--PPGEVGE 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 519 IVIGGQNISMGYFKNEEKTAEdycVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLqAGEYVSLGKVEAALKNCPLI 598
Cdd:COG0318 298 IVVRGPNVMKGYWNDPEATAE---AFRDG--WLRTGDLGRLDEDGYLYIVGRKKDMIIS-GGENVYPAEVEEVLAAHPGV 371
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 599 DNICAFAKSDQSY---VISFVVPNqkkltllaqqkgvEGSWVDicnnpamEAEILKEIREaanamKLERFEIPIKVRLSP 675
Cdd:COG0318 372 AEAAVVGVPDEKWgerVVAFVVLR-------------PGAELD-------AEELRAFLRE-----RLARYKVPRRVEFVD 426
|
570 580
....*....|....*....|....*....
gi 1720435377 676 E-PWTPeTGlvtdafKLKRKELKNHYLKD 703
Cdd:COG0318 427 ElPRTA-SG------KIDRRALRERYAAG 448
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
125-665 |
1.74e-59 |
|
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: 210.36 E-value: 1.74e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 125 WINYLEvncRVNNFGSGLTALGLKPKNTIAIFCETRAEW---MIAAQTCFKYNFPLvtlYATLGREAVVHGLNESEASYL 201
Cdd:cd17641 14 WADYAD---RVRAFALGLLALGVGRGDVVAILGDNRPEWvwaELAAQAIGALSLGI---YQDSMAEEVAYLLNYTGARVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 202 ITSVELLESKLKAALVDINCVKHIIYVDNKTINRAEYPEgleIHSMQSVEELG-----AKPENLSVPPSRPTPSDMAIVM 276
Cdd:cd17641 88 IAEDEEQVDKLLEIADRIPSVRYVIYCDPRGMRKYDDPR---LISFEDVVALGraldrRDPGLYEREVAAGKGEDVAVLC 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 277 YTSGSTGRPKGVMMHHSNLIaGMTGQCERIPGLGPKDTYIGYLPLAHVLELT-----AEISCFTYGCrigYSSPLTLsdq 351
Cdd:cd17641 165 TTSGTTGKPKLAMLSHGNFL-GHCAAYLAADPLGPGDEYVSVLPLPWIGEQMysvgqALVCGFIVNF---PEEPETM--- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 352 sskikkgsKGDCTVLKPTLMAAVPEIMDRIYKNVMSKVQEMNYVQKTLFKIGYD--YK-LEQIKKGYDAP--------LC 420
Cdd:cd17641 238 --------MEDLREIGPTFVLLPPRVWEGIAADVRARMMDATPFKRFMFELGMKlgLRaLDRGKRGRPVSlwlrlaswLA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 421 NLILFKKVKALLG-GNVRMMLSGGAPLSPQTHRF---MNVcfccPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCE 496
Cdd:cd17641 310 DALLFRPLRDRLGfSRLRSAATGGAALGPDTFRFfhaIGV----PLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGTE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 497 IKLKDwqeggytvhdkpnpRGEIVIGGQNISMGYFKNEEKTAEDycVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVK 576
Cdd:cd17641 386 VRIDE--------------VGEILVRSPGVFVGYYKNPEATAED--FDEDG--WLHTGDAGYFKENGHLVVIDRAKDVGT 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 577 LQAGEYVSLGKVEAALKNCPLIDNICAFAKsDQSYVISFVVPNQKKLTLLAQQKGVE-GSWVDICNNPAMEAEILKEIRE 655
Cdd:cd17641 448 TSDGTRFSPQFIENKLKFSPYIAEAVVLGA-GRPYLTAFICIDYAIVGKWAEQRGIAfTTYTDLASRPEVYELIRKEVEK 526
|
570
....*....|....
gi 1720435377 656 A----ANAMKLERF 665
Cdd:cd17641 527 VnaslPEAQRIRRF 540
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
121-700 |
2.35e-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: 197.69 E-value: 2.35e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 121 GNYKWINYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASY 200
Cdd:cd05932 2 GQVVEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 201 LITsvellesklkAALVDINCVKHIIyvdnktinraeyPEGLEIHSMQSVEELGAKPE--------NLSVPPSRPTPSDM 272
Cdd:cd05932 82 LFV----------GKLDDWKAMAPGV------------PEGLISISLPPPSAANCQYQwddliaqhPPLEERPTRFPEQL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 273 AIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLAHVLELTA-EISCFTYGCRIGYSSPLTLSDQ 351
Cdd:cd05932 140 ATLIYTSGTTGQPKGVMLTFGSFAWAAQAGIEHI-GTEENDRMLSYLPLAHVTERVFvEGGSLYGGVLVAFAESLDTFVE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 352 sskikkgskgDCTVLKPTLMAAVPEIMDRIYKNVMSKV--QEMNyvqkTLFKIgydykleqikkgydaPLCNLILFKKVK 429
Cdd:cd05932 219 ----------DVQRARPTLFFSVPRLWTKFQQGVQDKIpqQKLN----LLLKI---------------PVVNSLVKRKVL 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 430 ALLGGN-VRMMLSGGAPLSPQT-HRFMNVCFccPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDwqeggy 507
Cdd:cd05932 270 KGLGLDqCRLAGCGSAPVPPALlEWYRSLGL--NILEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRISE------ 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 508 tvhdkpnpRGEIVIGGQNISMGYFKNEEKTAEDYcvDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGEYVSLGK 587
Cdd:cd05932 342 --------DGEILVRSPALMMGYYKDPEATAEAF--TADG--FLRTGDKGELDADGNLTITGRVKDIFKTSKGKYVAPAP 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 588 VEAALKNCPLIDNICAFAkSDQSYVISFVVPNQ--KKLTLLAQQKGVEGSwvdicnnpameaeiLKEIREAANAmKLERF 665
Cdd:cd05932 410 IENKLAEHDRVEMVCVIG-SGLPAPLALVVLSEeaRLRADAFARAELEAS--------------LRAHLARVNS-TLDSH 473
|
570 580 590
....*....|....*....|....*....|....*
gi 1720435377 666 EIPIKVRLSPEPWTPETGLVTDAFKLKRKELKNHY 700
Cdd:cd05932 474 EQLAGIVVVKDPWSIDNGILTPTLKIKRNVLEKAY 508
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
271-620 |
2.69e-53 |
|
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341228 [Multi-domain] Cd Length: 336 Bit Score: 187.11 E-value: 2.69e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 271 DMAIVMYTSGSTGRPKGVMMHHSNLIAgMTGQCERIPGLGPKDTYIGYLPLAHVLELTAEISCFTYGCRI---GYSSPLT 347
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLA-AAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVvllPKFDPEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 348 LSDqssKIKKgskgdctvLKPTLMAAVPEIMDRIyknvmskvqemnyvqktlfkigydykLEQIK-KGYDAPlcnlilfk 426
Cdd:cd04433 80 ALE---LIER--------EKVTILLGVPTLLARL--------------------------LKAPEsAGYDLS-------- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 427 kvkallggNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVTEVTDYTTGR--VGAPLICCEIKLKDwQE 504
Cdd:cd04433 115 --------SLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTVATGPPDDDARKPgsVGRPVPGVEVRIVD-PD 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 505 GGytvHDKPNPRGEIVIGGQNISMGYFKNEEKTAEdycVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVS 584
Cdd:cd04433 186 GG---ELPPGEIGELVVRGPSVMKGYWNNPEATAA---VDEDG--WYRTGDLGRLDEDGYLYIVGRLKDMIKSG-GENVY 256
|
330 340 350
....*....|....*....|....*....|....*....
gi 1720435377 585 LGKVEAALKNCPLIDNICAFAKSDQSY---VISFVVPNQ 620
Cdd:cd04433 257 PAEVEAVLLGHPGVAEAAVVGVPDPEWgerVVAVVVLRP 295
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
126-608 |
1.02e-51 |
|
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341237 [Multi-domain] Cd Length: 486 Bit Score: 187.03 E-value: 1.02e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 126 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASYLITSV 205
Cdd:cd05911 11 LTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTDP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 206 ELLEsKLKAALVDINCVKHIIYVDNKtinrAEYPEGLEihsmQSVEELGAKPENLSVPPSRPTPSDMAIVMYTSGSTGRP 285
Cdd:cd05911 91 DGLE-KVKEAAKELGPKDKIIVLDDK----PDGVLSIE----DLLSPTLGEEDEDLPPPLKDGKDDTAAILYSSGTTGLP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 286 KGVMMHHSNLIAGMTGQCERIPG-LGPKDTYIGYLPLAHVleltaeiscftYGCRIGYSSPLtlsdqsskikkgsKGdCT 364
Cdd:cd05911 162 KGVCLSHRNLIANLSQVQTFLYGnDGSNDVILGFLPLYHI-----------YGLFTTLASLL-------------NG-AT 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 365 VLkptlmaavpeIMDRIYKNVMskvqeMNYVQKtlfkigydYKLEQIkkgYDAPLCNLILFK---KVKALLGgNVRMMLS 441
Cdd:cd05911 217 VI----------IMPKFDSELF-----LDLIEK--------YKITFL---YLVPPIAAALAKsplLDKYDLS-SLRVILS 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 442 GGAPLSPQTHRFMNVCFC-CPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDWQEGGYTvhdKPNPRGEIV 520
Cdd:cd05911 270 GGAPLSKELQELLAKRFPnATIKQGYGMTETGGILTVNPDGDDKPGSVGRLLPNVEAKIVDDDGKDSL---GPNEPGEIC 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 521 IGGQNISMGYFKNEEKTAEdyCVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVSLGKVEAALKNCPLIDN 600
Cdd:cd05911 347 VRGPQVMKGYYNNPEATKE--TFDEDG--WLHTGDIGYFDEDGYLYIVDRKKELIKYK-GFQVAPAELEAVLLEHPGVAD 421
|
....*...
gi 1720435377 601 ICAFAKSD 608
Cdd:cd05911 422 AAVIGIPD 429
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
78-596 |
1.08e-51 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 187.70 E-value: 1.08e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 78 TLDKLFDHAVAKFGKKdslgtrEILSEEnemqpnGKVFkklilgnykwiNYLEVNCRVNNFGSGLTALGLKPKNTIAIFC 157
Cdd:PRK06187 7 TIGRILRHGARKHPDK------EAVYFD------GRRT-----------TYAELDERVNRLANALRALGVKKGDRVAVFD 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 158 ETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASYLITSVELLESkLKAALVDINCVKHIIYVDnktinraE 237
Cdd:PRK06187 64 WNSHEYLEAYFAVPKIGAVLHPINIRLKPEEIAYILNDAEDRVVLVDSEFVPL-LAAILPQLPTVRTVIVEG-------D 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 238 YPEGLEIHSMQSVEE-LGAKPENLSVPPsrPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAgMTGQCERIPGLGPKDTYI 316
Cdd:PRK06187 136 GPAAPLAPEVGEYEElLAAASDTFDFPD--IDENDAAAMLYTSGTTGHPKGVVLSHRNLFL-HSLAVCAWLKLSRDDVYL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 317 GYLPLAHVLELTAEISCFTYGCRIGYS---SPLTLSDQsskIKKgskgdctvLKPTLMAAVPEIMdriyknvmskvqemN 393
Cdd:PRK06187 213 VIVPMFHVHAWGLPYLALMAGAKQVIPrrfDPENLLDL---IET--------ERVTFFFAVPTIW--------------Q 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 394 YVQKTLFKIGYDYkleqikkgydaplcnlilfkkvkallgGNVRMMLSGGAPLSPQT-HRFMNVcFCCPIGQGYGLTESC 472
Cdd:PRK06187 268 MLLKAPRAYFVDF---------------------------SSLRLVIYGGAALPPALlREFKEK-FGIDLVQGYGMTETS 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 473 GAGTVTEVTDYTTGR------VGAPLICCEIKLKD--WQE---GGYTVhdkpnprGEIVIGGQNISMGYFKNEEKTAEDY 541
Cdd:PRK06187 320 PVVSVLPPEDQLPGQwtkrrsAGRPLPGVEARIVDddGDElppDGGEV-------GEIIVRGPWLMQGYWNRPEATAETI 392
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1720435377 542 cvdENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKlQAGEYVSLGKVEAALKNCP 596
Cdd:PRK06187 393 ---DGG--WLHTGDVGYIDEDGYLYITDRIKDVII-SGGENIYPRELEDALYGHP 441
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
79-686 |
3.62e-51 |
|
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: 187.66 E-value: 3.62e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 79 LDKLFDHAVAKFGKKDSLGTREilSEENEMQPNGKVFKKLiLGNYKWINYLEVNCRVNNFGSGL-TALGLKPKNTIAIFC 157
Cdd:cd17632 24 LAQIIATVMTGYADRPALGQRA--TELVTDPATGRTTLRL-LPRFETITYAELWERVGAVAAAHdPEQPVRPGDFVAVLG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 158 ETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASYLITSVELLESKLKAALvDINCVKHIIYVDNK---TIN 234
Cdd:cd17632 101 FTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAVSAEHLDLAVEAVL-EGGTPPRLVVFDHRpevDAH 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 235 R----------AEYPEGLEIHSMQSVEELGAKPenlsVPPSRPTPSDMAIVM--YTSGSTGRPKGVMMHHSNLIAGMTGQ 302
Cdd:cd17632 180 RaalesarerlAAVGIPVTTLTLIAVRGRDLPP----APLFRPEPDDDPLALliYTSGSTGTPKGAMYTERLVATFWLKV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 303 CERIPGLGPKDTYIGYLPLAHVLeltAEISCFTYGCRIGYSSPLTLSDQSSKIKkgskgDCTVLKPTLMAAVPEIMDRIY 382
Cdd:cd17632 256 SSIQDIRPPASITLNFMPMSHIA---GRISLYGTLARGGTAYFAAASDMSTLFD-----DLALVRPTELFLVPRVCDMLF 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 383 KNVMSKVqemnyvqktlfkigyDYKLEQikkGYDAplcnLILFKKVKA-----LLGGNVRMMLSGGAPLSPQTHRFMNVC 457
Cdd:cd17632 328 QRYQAEL---------------DRRSVA---GADA----ETLAERVKAelrerVLGGRLLAAVCGSAPLSAEMKAFMESL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 458 FCCPIGQGYGLTEscgAGTVT--------EVTDYttgrvgaplicceiKLKDWQEGGYTVHDKPNPRGEIVIGGQNISMG 529
Cdd:cd17632 386 LDLDLHDGYGSTE---AGAVIldgvivrpPVLDY--------------KLVDVPELGYFRTDRPHPRGELLVKTDTLFPG 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 530 YFKNEEKTAEDYcvDENGqrWFCTGDI-GEFHPDGcLQIIDRKKDLVKLQAGEYVSLGKVEAALKNCPLIDNICAFAKSD 608
Cdd:cd17632 449 YYKRPEVTAEVF--DEDG--FYRTGDVmAELGPDR-LVYVDRRNNVLKLSQGEFVTVARLEAVFAASPLVRQIFVYGNSE 523
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720435377 609 QSYVISFVVPNQKKLTLLAQQkgvegswvdicnnpAMEAEILKEIREAANAMKLERFEIPIKVRLSPEPWTPETGLVT 686
Cdd:cd17632 524 RAYLLAVVVPTQDALAGEDTA--------------RLRAALAESLQRIAREAGLQSYEIPRDFLIETEPFTIANGLLS 587
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
126-693 |
3.51e-50 |
|
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: 182.26 E-value: 3.51e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 126 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASYLITSv 205
Cdd:cd05914 8 LTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFVS- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 206 ellesklkaalvdincvkhiiyvdnktinraeypegleihsmqsveelgakpenlsvppsrpTPSDMAIVMYTSGSTGRP 285
Cdd:cd05914 87 --------------------------------------------------------------DEDDVALINYTSGTTGNS 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 286 KGVMMHHSNLIAGMTGqCERIPGLGPKDTYIGYLPLAHVLELtaeisCFTYGCRIGYSSPLTLSDQ--SSKIKKGSKGDc 363
Cdd:cd05914 105 KGVMLTYRNIVSNVDG-VKEVVLLGKGDKILSILPLHHIYPL-----TFTLLLPLLNGAHVVFLDKipSAKIIALAFAQ- 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 364 tvLKPTLMAAVPEIMDRIYKNVmskVQEMNYVQKTLFKIGYDYKLEQIKKgydaplcnlILFKKVKALLGGNVRMMLSGG 443
Cdd:cd05914 178 --VTPTLGVPVPLVIEKIFKMD---IIPKLTLKKFKFKLAKKINNRKIRK---------LAFKKVHEAFGGNIKEFVIGG 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 444 APLSPQTHRF---MNVCFCcpigQGYGLTES----CGAGTVTEVTDyttgRVGAPLICCEIKLkdwqeggytvhDKPNPR 516
Cdd:cd05914 244 AKINPDVEEFlrtIGFPYT----IGYGMTETapiiSYSPPNRIRLG----SAGKVIDGVEVRI-----------DSPDPA 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 517 ---GEIVIGGQNISMGYFKNEEKTAEdyCVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGEYVSLGKVEAALK 593
Cdd:cd05914 305 tgeGEIIVRGPNVMKGYYKNPEATAE--AFDKDG--WFHTGDLGKIDAEGYLYIRGRKKEMIVLSSGKNIYPEEIEAKIN 380
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 594 NCPLIdnicafaksdqsyVISFVVPNQKKLTLLA-------QQKGVegswvdicNNPAMEAEILKEIREAANaMKLERFE 666
Cdd:cd05914 381 NMPFV-------------LESLVVVQEKKLVALAyidpdflDVKAL--------KQRNIIDAIKWEVRDKVN-QKVPNYK 438
|
570 580
....*....|....*....|....*..
gi 1720435377 667 IPIKVRLSPEPWtPETGLvtdaFKLKR 693
Cdd:cd05914 439 KISKVKIVKEEF-EKTPK----GKIKR 460
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
121-708 |
3.37e-46 |
|
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: 173.70 E-value: 3.37e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 121 GNYKW--INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAA-QTCFKYNFpLVTLYATLGREAVVHGLNESE 197
Cdd:cd05933 2 RGDKWhtLTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAvGAIFAGGI-AVGIYTTNSPEACQYVAETSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 198 ASYLITSVELLESKLKAALVDINCVKHIIyvdnktINRAEYPEGL-EIHSMQSVEELGakpenLSVPP-------SRPTP 269
Cdd:cd05933 81 ANILVVENQKQLQKILQIQDKLPHLKAII------QYKEPLKEKEpNLYSWDEFMELG-----RSIPDeqldaiiSSQKP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 270 SDMAIVMYTSGSTGRPKGVMMHHSNL--IAGMTGQ-CERIPGLGPKDTYIGYLPLAHVLELTAEI-SCFTYGCRIGYSSP 345
Cdd:cd05933 150 NQCCTLIYTSGTTGMPKGVMLSHDNItwTAKAASQhMDLRPATVGQESVVSYLPLSHIAAQILDIwLPIKVGGQVYFAQP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 346 LTLsdqsskikKGSKGDcTV--LKPTLMAAVPEIMDRIYKNVMSKVQEMNYVQKTLF----KIGYDYKLEQIKKGYDAPL 419
Cdd:cd05933 230 DAL--------KGTLVK-TLreVRPTAFMGVPRVWEKIQEKMKAVGAKSGTLKRKIAswakGVGLETNLKLMGGESPSPL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 420 C----NLILFKKVKALLG-GNVRMMLSGGAPLSPQTHRF---MNVcfccPIGQGYGLTESCGAGTVTEVTDYTTGRVGAP 491
Cdd:cd05933 301 FyrlaKKLVFKKVRKALGlDRCQKFFTGAAPISRETLEFflsLNI----PIMELYGMSETSGPHTISNPQAYRLLSCGKA 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 492 LICCEIKLkdwqeggytvhDKPNPR--GEIVIGGQNISMGYFKNEEKTAEdyCVDENGqrWFCTGDIGEFHPDGCLQIID 569
Cdd:cd05933 377 LPGCKTKI-----------HNPDADgiGEICFWGRHVFMGYLNMEDKTEE--AIDEDG--WLHSGDLGKLDEDGFLYITG 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 570 RKKDLVKLQAGEYVSLGKVEAALKN-CPLIDNicAFAKSDQSYVISFVVP-----NQK------KLTLLA----QQKGVE 633
Cdd:cd05933 442 RIKELIITAGGENVPPVPIEDAVKKeLPIISN--AMLIGDKRKFLSMLLTlkcevNPEtgepldELTEEAiefcRKLGSQ 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 634 GSWVDICNN---PAMEAEILKEIREA-----ANAMKLERFEIpikvrlSPEPWTPETGLVTDAFKLKRKELKNHYLKDIE 705
Cdd:cd05933 520 ATRVSEIAGgkdPKVYEAIEEGIKRVnkkaiSNAQKIQKWVI------LEKDFSVPGGELGPTMKLKRPVVAKKYKDEID 593
|
...
gi 1720435377 706 RMY 708
Cdd:cd05933 594 KLY 596
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
124-575 |
2.02e-42 |
|
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: 160.42 E-value: 2.02e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 124 KWINYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASYLIT 203
Cdd:cd05936 23 RKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPRELEHILNDSGAKALIV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 204 SVELlesklkaalvdincvkhiiyvdnktinraeypegleihsmqsvEELGAKPENLSVPPSRpTPSDMAIVMYTSGSTG 283
Cdd:cd05936 103 AVSF-------------------------------------------TDLLAAGAPLGERVAL-TPEDVAVLQYTSGTTG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 284 RPKGVMMHHSNLIAGMTgQCERI--PGLGPKDTYIGYLPLAHVLELTAeisCFTYGCRIGYS-------SPLTLSDQssk 354
Cdd:cd05936 139 VPKGAMLTHRNLVANAL-QIKAWleDLLEGDDVVLAALPLFHVFGLTV---ALLLPLALGATivliprfRPIGVLKE--- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 355 IKKGskgdctvlKPTLMAAVPeimdriyknvmskvqemnyvqkTLFkIGydykleqikkgydaplcnLILFKKVKALLGG 434
Cdd:cd05936 212 IRKH--------RVTIFPGVP----------------------TMY-IA------------------LLNAPEFKKRDFS 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 435 NVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVTEVTDYT-TGRVGAPLICCEIKLKDwqeggytVHDKP 513
Cdd:cd05936 243 SLRLCISGGAPLPVEVAERFEELTGVPIVEGYGLTETSPVVAVNPLDGPRkPGSIGIPLPGTEVKIVD-------DDGEE 315
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720435377 514 NPR---GEIVIGGQNISMGYFKNEEKTAEDYcVDEngqrWFCTGDIGEFHPDGCLQIIDRKKDLV 575
Cdd:cd05936 316 LPPgevGELWVRGPQVMKGYWNRPEETAEAF-VDG----WLRTGDIGYMDEDGYFFIVDRKKDMI 375
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
126-576 |
2.62e-40 |
|
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.
Pssm-ID: 341230 [Multi-domain] Cd Length: 505 Bit Score: 155.09 E-value: 2.62e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 126 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEwmiaaqtcfkynFPLVTLyATLGREAVVHGLN----------- 194
Cdd:cd05904 33 LTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIE------------FPVAFL-AVLSLGAVVTTANplstpaeiakq 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 195 --ESEASYLITSVELLEsKLKAALVDINCVkhiiyvdnktinraeypEGLEIHSMQSVEELGAKPENlSVPPSRPTPSDM 272
Cdd:cd05904 100 vkDSGAKLAFTTAELAE-KLASLALPVVLL-----------------DSAEFDSLSFSDLLFEADEA-EPPVVVIKQDDV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 273 AIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERI-PGLGPKDTYIGYLPLAHVLELTAeiscFTYGcrigyssplTLSdq 351
Cdd:cd05904 161 AALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEgSNSDSEDVFLCVLPMFHIYGLSS----FALG---------LLR-- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 352 sskikkgskgdctvLKPTLMaavpeimdriyknVMSK---VQEMNYVQKtlFKIGYdykleqikkgydAPLCNLILFKKV 428
Cdd:cd05904 226 --------------LGATVV-------------VMPRfdlEELLAAIER--YKVTH------------LPVVPPIVLALV 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 429 KALLGGN-----VRMMLSGGAPLSPQT-----HRFMNVcfccPIGQGYGLTESCGAGTVTEVTDYTTGRVG-----APLI 493
Cdd:cd05904 265 KSPIVDKydlssLRQIMSGAAPLGKELieafrAKFPNV----DLGQGYGMTESTGVVAMCFAPEKDRAKYGsvgrlVPNV 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 494 ccEIKLKDWQEGGytvHDKPNPRGEIVIGGQNISMGYFKNEEKTAEdyCVDENGqrWFCTGDIGEFHPDGCLQIIDRKKD 573
Cdd:cd05904 341 --EAKIVDPETGE---SLPPNQTGELWIRGPSIMKGYLNNPEATAA--TIDKEG--WLHTGDLCYIDEDGYLFIVDRLKE 411
|
...
gi 1720435377 574 LVK 576
Cdd:cd05904 412 LIK 414
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
269-583 |
7.04e-39 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 154.11 E-value: 7.04e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 269 PSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCER--IPGLGPKdTYIGYLPLAHVLELTAEISCFTYGCRIgysspl 346
Cdd:PTZ00342 303 PDFITSIVYTSGTSGKPKGVMLSNKNLYNTVVPLCKHsiFKKYNPK-THLSYLPISHIYERVIAYLSFMLGGTI------ 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 347 tlsDQSSK-IKKGSKgDCTVLKPTLMAAVPEIMDRIYKNVMSKVQEMNYVQKTLFKigydyKLEQIKKG-YDAPLCNLI- 423
Cdd:PTZ00342 376 ---NIWSKdINYFSK-DIYNSKGNILAGVPKVFNRIYTNIMTEINNLPPLKRFLVK-----KILSLRKSnNNGGFSKFLe 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 424 ----LFKKVKALLGGNVRMMLSGGAPLSPQTHR----FMNVCFCcpigQGYGLTESCGAGTVTEVTDYTTGRVGAPlIC- 494
Cdd:PTZ00342 447 githISSKIKDKVNPNLEVILNGGGKLSPKIAEelsvLLNVNYY----QGYGLTETTGPIFVQHADDNNTESIGGP-ISp 521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 495 -CEIKLKDWQEggYTVHDKPnPRGEIVIGGQNISMGYFKNEEKTAEDYCVDengqRWFCTGDIGEFHPDGCLQIIDRKKD 573
Cdd:PTZ00342 522 nTKYKVRTWET--YKATDTL-PKGELLIKSDSIFSGYFLEKEQTKNAFTED----GYFKTGDIVQINKNGSLTFLDRSKG 594
|
330
....*....|
gi 1720435377 574 LVKLQAGEYV 583
Cdd:PTZ00342 595 LVKLSQGEYI 604
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
121-698 |
1.37e-38 |
|
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: 149.77 E-value: 1.37e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 121 GNYKWINYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAaqtcfkynfplvtLYATLGREAVVHGLN----ES 196
Cdd:cd05926 10 GSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVA-------------FLAAARAGAVVAPLNpaykKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 197 EASYLitsveLLESKLKAALVDincvkhiiYVDNKTINRAEYPEGLEI----------HSMQSVEELGAKPENLSVPPSR 266
Cdd:cd05926 77 EFEFY-----LADLGSKLVLTP--------KGELGPASRAASKLGLAIlelaldvgvlIRAPSAESLSNLLADKKNAKSE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 267 --PTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCeRIPGLGPKDTYIGYLPLAHVLELTAEI--SCFTYGCrigy 342
Cdd:cd05926 144 gvPLPDDLALILHTSGTTGRPKGVPLTHRNLAASATNIT-NTYKLTPDDRTLVVMPLFHVHGLVASLlsTLAAGGS---- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 343 sspLTLSDQSSkikkGSK--GDCTVLKPTLMAAVPEIMDRIYKNVMSKvqemnyvqktlfkigydykleqikkgydaplc 420
Cdd:cd05926 219 ---VVLPPRFS----ASTfwPDVRDYNATWYTAVPTIHQILLNRPEPN-------------------------------- 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 421 nlilFKKVKALLggnvRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVT--EVTDYTTGRVGAPLiccEIK 498
Cdd:cd05926 260 ----PESPPPKL----RFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEAAHQMTSNplPPGPRKPGSVGKPV---GVE 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 499 LKDWQEGGYTVhdKPNPRGEIVIGGQNISMGYFKNEEKTAEDYCVDengqRWFCTGDIGEFHPDGCLQIIDRKKDLVKlQ 578
Cdd:cd05926 329 VRILDEDGEIL--PPGVVGEICLRGPNVTRGYLNNPEANAEAAFKD----GWFRTGDLGYLDADGYLFLTGRIKELIN-R 401
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 579 AGEYVSLGKVEAALKNCPLIDNICAFAKSDQSY---VISFVVPNQKKltllaqqkgvegswvdicnnPAMEAEILKEIRE 655
Cdd:cd05926 402 GGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYgeeVAAAVVLREGA--------------------SVTEEELRAFCRK 461
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1720435377 656 aanamKLERFEIPIKVRLSPE-PWTPeTGlvtdafKLKRKELKN 698
Cdd:cd05926 462 -----HLAAFKVPKKVYFVDElPKTA-TG------KIQRRKVAE 493
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
126-575 |
1.10e-34 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 138.88 E-value: 1.10e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 126 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAqtcfkynfplvtlYATLGREAVVHGLNE----SEASY- 200
Cdd:PRK07656 31 LTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAA-------------LGALKAGAVVVPLNTrytaDEAAYi 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 201 -------LITSVELLESKLKAALVDINCVKHIIYVDNktinRAEYPEGLEIHSMQSVEELGAKPEnlsVPPSRpTPSDMA 273
Cdd:PRK07656 98 largdakALFVLGLFLGVDYSATTRLPALEHVVICET----EEDDPHTEKMKTFTDFLAAGDPAE---RAPEV-DPDDVA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 274 IVMYTSGSTGRPKGVMMHHSNLIAGMTGQCErIPGLGPKDTYIGYLPLAHVLELTAEI-SCFTYGcrigysspltlsdqs 352
Cdd:PRK07656 170 DILFTSGTTGRPKGAMLTHRQLLSNAADWAE-YLGLTEGDRYLAANPFFHVFGYKAGVnAPLMRG--------------- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 353 skikkgskgdCTVLkPTLMAAVPEIMDRIYK---NVMSKVQEMnyvqktlfkigYDYkLEQIKKGYDAPLCNLilfkkvk 429
Cdd:PRK07656 234 ----------ATIL-PLPVFDPDEVFRLIETeriTVLPGPPTM-----------YNS-LLQHPDRSAEDLSSL------- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 430 allggnvRMMLSGGAPLSPQ-THRFMNVCFCCPIGQGYGLTESCGAGTVTEVTD---YTTGRVGAPLICCEIKLKDWQEG 505
Cdd:PRK07656 284 -------RLAVTGAASMPVAlLERFESELGVDIVLTGYGLSEASGVTTFNRLDDdrkTVAGTIGTAIAGVENKIVNELGE 356
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 506 GYTVHDKpnprGEIVIGGQNISMGYFKNEEKTAEdyCVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLV 575
Cdd:PRK07656 357 EVPVGEV----GELLVRGPNVMKGYYDDPEATAA--AIDADG--WLHTGDLGRLDEEGYLYIVDRKKDMF 418
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
118-617 |
3.53e-34 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 136.63 E-value: 3.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 118 LILGNYKWiNYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESE 197
Cdd:PRK03640 21 IEFEEKKV-TFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 198 ASYLITSvellesklkaalvdincvkhiiyvdnktinrAEYPEGLEIHSMQSVEELGAKPENLSVPPSRPTPSDMAIVMY 277
Cdd:PRK03640 100 VKCLITD-------------------------------DDFEAKLIPGISVKFAELMNGPKEEAEIQEEFDLDEVATIMY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 278 TSGSTGRPKGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIgyssplTLSDQ--SSKI 355
Cdd:PRK03640 149 TSGTTGKPKGVIQTYGNHWWSAVGSALNL-GLTEDDCWLAAVPIFHISGLSILMRSVIYGMRV------VLVEKfdAEKI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 356 KKGSKGDctvlKPTLMAAVPEIMDRIyknvMSKVQEMNYvqktlfkigydykleqikkgydaplcnlilfkkvkallGGN 435
Cdd:PRK03640 222 NKLLQTG----GVTIISVVSTMLQRL----LERLGEGTY--------------------------------------PSS 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 436 VRMMLSGGAPLSPQT------HRFmnvcfccPIGQGYGLTESCgAGTVTEVTDYTT---GRVGAPLICCEIKL-KDWQEG 505
Cdd:PRK03640 256 FRCMLLGGGPAPKPLleqckeKGI-------PVYQSYGMTETA-SQIVTLSPEDALtklGSAGKPLFPCELKIeKDGVVV 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 506 gytvhdKPNPRGEIVIGGQNISMGYFKNEEKTAEdycVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVkLQAGEYVSL 585
Cdd:PRK03640 328 ------PPFEEGEIVVKGPNVTKGYLNREDATRE---TFQDG--WFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYP 395
|
490 500 510
....*....|....*....|....*....|....*
gi 1720435377 586 GKVEAALKNCPLIDNICAFAKSDQSY---VISFVV 617
Cdd:PRK03640 396 AEIEEVLLSHPGVAEAGVVGVPDDKWgqvPVAFVV 430
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
128-618 |
6.45e-33 |
|
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: 132.12 E-value: 6.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 128 YLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASYLITsvel 207
Cdd:cd05903 4 YSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVV---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 208 lesklkaalvdincvkhiiyvdnktinraeyPEGLEIHSMQsveelgakpenlsvppsrPTPSDMAIVMYTSGSTGRPKG 287
Cdd:cd05903 80 -------------------------------PERFRQFDPA------------------AMPDAVALLLFTSGTTGEPKG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 288 VMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLAHvleltaeISCFTYGcrigysspltlsdqsskikkgskgdctVLK 367
Cdd:cd05903 111 VMHSHNTLSASIRQYAERL-GLGPGDVFLVASPMAH-------QTGFVYG---------------------------FTL 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 368 PTLMAAvPEIMDRIYkNVMSKVQEMNyVQKTLFKIGYDYKLEQIKKGYD---APLCNLilfkkvkallggnvRMMLSGGA 444
Cdd:cd05903 156 PLLLGA-PVVLQDIW-DPDKALALMR-EHGVTFMMGATPFLTDLLNAVEeagEPLSRL--------------RTFVCGGA 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 445 PLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVTEVTD-----YTTGRVGAPLiccEIKLKDwqEGGYTVhdKPNPRGEI 519
Cdd:cd05903 219 TVPRSLARRAAELLGAKVCSAYGSTECPGAVTSITPAPedrrlYTDGRPLPGV---EIKVVD--DTGATL--APGVEGEL 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 520 VIGGQNISMGYFKNEEKTAEDYcvdenGQRWFCTGDIGEFHPDGCLQIIDRKKDLVkLQAGEYVSLGKVEAALKNCPLID 599
Cdd:cd05903 292 LSRGPSVFLGYLDRPDLTADAA-----PEGWFRTGDLARLDEDGYLRITGRSKDII-IRGGENIPVLEVEDLLLGHPGVI 365
|
490 500
....*....|....*....|..
gi 1720435377 600 NICAFAKSDQ---SYVISFVVP 618
Cdd:cd05903 366 EAAVVALPDErlgERACAVVVT 387
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
126-608 |
4.05e-31 |
|
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: 127.98 E-value: 4.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 126 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIA------AQTCFKYNFPLvtlyatLGREAVVHGLNESEAS 199
Cdd:TIGR03098 26 LTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAmfgaalAGGVFVPINPL------LKAEQVAHILADCNVR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 200 YLITSVELLEsKLKAALVDINCVKHIIYVDNKTINRAEYPeGLEIHSMQSVEELGAkpenlSVPPSRPTPSDMAIVMYTS 279
Cdd:TIGR03098 100 LLVTSSERLD-LLHPALPGCHDLRTLIIVGDPAHASEGHP-GEEPASWPKLLALGD-----ADPPHPVIDSDMAAILYTS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 280 GSTGRPKGVMMHHSNLIAGMTGQCERIPgLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSSPLTLSDQSSKIKKGs 359
Cdd:TIGR03098 173 GSTGRPKGVVLSHRNLVAGAQSVATYLE-NRPDDRLLAVLPLSFDYGFNQLTTAFYVGATVVLHDYLLPRDVLKALEKH- 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 360 kgdctvlKPTLMAAVPEImdriyknvmskvqemnYVQktLFKIgyDYKLEqikkgyDAPLCNLIlfkkvkALLGGNV-RM 438
Cdd:TIGR03098 251 -------GITGLAAVPPL----------------WAQ--LAQL--DWPES------AAPSLRYL------TNSGGAMpRA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 439 MLSGGAPLSPQTHRFMNvcfccpigqgYGLTESCGAGTV-TEVTDYTTGRVGAPLICCEIklkdwqeggYTVHDK----- 512
Cdd:TIGR03098 292 TLSRLRSFLPNARLFLM----------YGLTEAFRSTYLpPEEVDRRPDSIGKAIPNAEV---------LVLREDgseca 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 513 PNPRGEIVIGGQNISMGYFKNEEKTAEdyCVDENGQR-----------WfcTGDIGEFHPDGCLQIIDRKKDLVKlQAGE 581
Cdd:TIGR03098 353 PGEEGELVHRGALVAMGYWNDPEKTAE--RFRPLPPFpgelhlpelavW--SGDTVRRDEEGFLYFVGRRDEMIK-TSGY 427
|
490 500
....*....|....*....|....*..
gi 1720435377 582 YVSLGKVEAALKNCPLIDNICAFAKSD 608
Cdd:TIGR03098 428 RVSPTEVEEVAYATGLVAEAVAFGVPD 454
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
128-592 |
9.97e-31 |
|
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: 125.80 E-value: 9.97e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 128 YLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASYLItsvel 207
Cdd:cd17631 23 YAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAYILADSGAKVLF----- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 208 lesklkaalvdincvkhiiyvdnktinraeypegleihsmqsveelgakpenlsvppsrptpSDMAIVMYTSGSTGRPKG 287
Cdd:cd17631 98 --------------------------------------------------------------DDLALLMYTSGTTGRPKG 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 288 VMMHHSNL-----IAGMTGqceripGLGPKDTYIGYLPLAHVleltAEISCFTygcrigysSPLTLSDQSSKIKKGSKGD 362
Cdd:cd17631 116 AMLTHRNLlwnavNALAAL------DLGPDDVLLVVAPLFHI----GGLGVFT--------LPTLLRGGTVVILRKFDPE 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 363 cTVL------KPTLMAAVPEIMDRIyknvmskvqemnyVQKTLFKigydykleqikkGYDAPlcnlilfkkvkallggNV 436
Cdd:cd17631 178 -TVLdlierhRVTSFFLVPTMIQAL-------------LQHPRFA------------TTDLS----------------SL 215
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 437 RMMLSGGAPLSPQTHRFMNVcFCCPIGQGYGLTESCGAGTVTEVTDYTT--GRVGAPLICCEIKLKDwqEGGYTVhdKPN 514
Cdd:cd17631 216 RAVIYGGAPMPERLLRALQA-RGVKFVQGYGMTETSPGVTFLSPEDHRRklGSAGRPVFFVEVRIVD--PDGREV--PPG 290
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720435377 515 PRGEIVIGGQNISMGYFKNEEKTAEDYcvdENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKlQAGEYVSLGKVEAAL 592
Cdd:cd17631 291 EVGEIVVRGPHVMAGYWNRPEATAAAF---RDG--WFHTGDLGRLDEDGYLYIVDRKKDMII-SGGENVYPAEVEDVL 362
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
122-598 |
3.59e-29 |
|
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: 122.64 E-value: 3.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 122 NYKWINYLEVNCRVnnfGSGLTALGLKPKNTIAIFCETRAEW---MIAAQTCFKYNFPLVTLYATlgREaVVHGLNESEA 198
Cdd:cd17642 44 NYSYAEYLEMSVRL---AEALKKYGLKQNDRIAVCSENSLQFflpVIAGLFIGVGVAPTNDIYNE--RE-LDHSLNISKP 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 199 SYLITSVELLESKLKAAlVDINCVKHIIYVDNKTinraEYPEGLEIHSMQSVEELGAKPENLSVPPSRPTPSDMAIVMYT 278
Cdd:cd17642 118 TIVFCSKKGLQKVLNVQ-KKLKIIKTIIILDSKE----DYKGYQCLYTFITQNLPPGFNEYDFKPPSFDRDEQVALIMNS 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 279 SGSTGRPKGVMMHHSNLIAGMTGQCERIPG--LGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGY----SSPLTLSD-Q 351
Cdd:cd17642 193 SGSTGLPKGVQLTHKNIVARFSHARDPIFGnqIIPDTAILTVIPFHHGFGMFTTLGYLICGFRVVLmykfEEELFLRSlQ 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 352 SSKIKKgskgdcTVLKPTLMAAVPeimdriyknvmskvqemnyvqktlfkigydyKLEQIKKgYDapLCNLIlfkkvkal 431
Cdd:cd17642 273 DYKVQS------ALLVPTLFAFFA-------------------------------KSTLVDK-YD--LSNLH-------- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 432 lggnvrMMLSGGAPLSPQTHRFMNVCFCCP-IGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDWQEGGYTvh 510
Cdd:cd17642 305 ------EIASGGAPLSKEVGEAVAKRFKLPgIRQGYGLTETTSAILITPEGDDKPGAVGKVVPFFYAKVVDLDTGKTL-- 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 511 dKPNPRGEIVIGGQNISMGYFKNEEKTAEdyCVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVSLGKVEA 590
Cdd:cd17642 377 -GPNERGELCVKGPMIMKGYVNNPEATKA--LIDKDG--WLHSGDIAYYDEDGHFFIVDRLKSLIKYK-GYQVPPAELES 450
|
....*...
gi 1720435377 591 ALKNCPLI 598
Cdd:cd17642 451 ILLQHPKI 458
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
270-621 |
3.66e-29 |
|
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: 120.53 E-value: 3.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 270 SDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIgyssplTLS 349
Cdd:cd05912 77 DDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNL-GLTEDDNWLCALPLFHISGLSILMRSVIYGMTV------YLV 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 350 DQ--SSKIKKGSKGDctvlKPTLMAAVPEIMDRIyknvmskvqemnyvqktlfkigydykLEQIKKGYDAplcnlilfkk 427
Cdd:cd05912 150 DKfdAEQVLHLINSG----KVTIISVVPTMLQRL--------------------------LEILGEGYPN---------- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 428 vkallggNVRMMLSGGAPLSPQThrfMNVC--FCCPIGQGYGLTESCgAGTVTEVTDYT---TGRVGAPLICCEIKLKDW 502
Cdd:cd05912 190 -------NLRCILLGGGPAPKPL---LEQCkeKGIPVYQSYGMTETC-SQIVTLSPEDAlnkIGSAGKPLFPVELKIEDD 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 503 QEGGYTVhdkpnprGEIVIGGQNISMGYFKNEEKTAEdycVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVkLQAGEY 582
Cdd:cd05912 259 GQPPYEV-------GEILLKGPNVTKGYLNRPDATEE---SFENG--WFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGEN 325
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1720435377 583 VSLGKVEAALKNCPLIDNICAFAKSDQSY---VISFVVPNQK 621
Cdd:cd05912 326 IYPAEIEEVLLSHPAIKEAGVVGIPDDKWgqvPVAFVVSERP 367
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
262-600 |
1.92e-27 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 117.41 E-value: 1.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 262 VPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIA-GMTGQCeRIPGLGPKD-TYIGYLPLAHVLELTAeisCFTYGCR 339
Cdd:PRK05605 211 VSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFAnAAQGKA-WVPGLGDGPeRVLAALPMFHAYGLTL---CLTLAVS 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 340 IG--------YSSPLTLsdqsSKIKKGskgdctvlKPTLMAAVPEimdrIYKNVMSKVQEmnyvqktlfkigydykleqi 411
Cdd:PRK05605 287 IGgelvllpaPDIDLIL----DAMKKH--------PPTWLPGVPP----LYEKIAEAAEE-------------------- 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 412 kKGYDaplcnlilfkkvkalLGGnVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVTEVTDY-TTGRVGA 490
Cdd:PRK05605 331 -RGVD---------------LSG-VRNAFSGAMALPVSTVELWEKLTGGLLVEGYGLTETSPIIVGNPMSDDrRPGYVGV 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 491 PLICCEIKLKDWQEGGYTVHDkpNPRGEIVIGGQNISMGYFKNEEKTAEdycVDENGqrWFCTGDIGEFHPDGCLQIIDR 570
Cdd:PRK05605 394 PFPDTEVRIVDPEDPDETMPD--GEEGELLVRGPQVFKGYWNRPEETAK---SFLDG--WFRTGDVVVMEEDGFIRIVDR 466
|
330 340 350
....*....|....*....|....*....|
gi 1720435377 571 KKDLVkLQAGEYVSLGKVEAALKNCPLIDN 600
Cdd:PRK05605 467 IKELI-ITGGFNVYPAEVEEVLREHPGVED 495
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
126-701 |
2.35e-27 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 117.13 E-value: 2.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 126 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASYLITSV 205
Cdd:COG0365 40 LTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITAD 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 206 ELLE--------SKLKAALVDINCVKHIIYVDNkTINRAEYPEGLEIHsmqsvEELGAKPENLsvpPSRPTPS-DMAIVM 276
Cdd:COG0365 120 GGLRggkvidlkEKVDEALEELPSLEHVIVVGR-TGADVPMEGDLDWD-----ELLAAASAEF---EPEPTDAdDPLFIL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 277 YTSGSTGRPKGVMMHHSNLIAGMTGQCERIPGLGPKDTY-----IG---------YLPLAHvleltaEISCFTYGCRIGY 342
Cdd:COG0365 191 YTSGTTGKPKGVVHTHGGYLVHAATTAKYVLDLKPGDVFwctadIGwatghsyivYGPLLN------GATVVLYEGRPDF 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 343 SSPLTLSDQSSKikkgskgdctvLKPTLMAAVPeimdRIYKNVMskvqemnyvqktlfKIGydyklEQIKKGYDapLCNL 422
Cdd:COG0365 265 PDPGRLWELIEK-----------YGVTVFFTAP----TAIRALM--------------KAG-----DEPLKKYD--LSSL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 423 ilfkkvkallggnvRMMLSGGAPLSPQT-HRFMNVcFCCPIGQGYGLTESCGA-GTVTEVTDYTTGRVGAPLICCEIKLk 500
Cdd:COG0365 309 --------------RLLGSAGEPLNPEVwEWWYEA-VGVPIVDGWGQTETGGIfISNLPGLPVKPGSMGKPVPGYDVAV- 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 501 dWQEGGYTVhdKPNPRGEIVIGGQNISM--GYFKNEEKTAEDYCVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLq 578
Cdd:COG0365 373 -VDEDGNPV--PPGEEGELVIKGPWPGMfrGYWNDPERYRETYFGRFPG--WYRTGDGARRDEDGYFWILGRSDDVINV- 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 579 AGEYVSLGKVEAALKNCPLIDNICAFAKSDQ---SYVISFVVPNqkkltllaqqKGVEGSwvdicnnPAMEAEILKEIRE 655
Cdd:COG0365 447 SGHRIGTAEIESALVSHPAVAEAAVVGVPDEirgQVVKAFVVLK----------PGVEPS-------DELAKELQAHVRE 509
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 1720435377 656 aanamKLERFEIPIKVRLSPE-PWTPeTGlvtdafKLKRKELKNHYL 701
Cdd:COG0365 510 -----ELGPYAYPREIEFVDElPKTR-SG------KIMRRLLRKIAE 544
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
128-603 |
9.57e-27 |
|
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: 113.13 E-value: 9.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 128 YLEVNCRVNNFGSGL-TALGLKPKNTIAIFCEtRAEWMIAAQ-TCFK----YnFPLVTLYATLGREAVvhgLNESEASYL 201
Cdd:TIGR01733 2 YRELDERANRLARHLrAAGGVGPGDRVAVLLE-RSAELVVAIlAVLKagaaY-VPLDPAYPAERLAFI---LEDAGARLL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 202 ITSVELLESKLKAALVDINCVkhiiyvdnktinraeypegleihsmQSVEELGAKPENLSVPPSRPTPSDMAIVMYTSGS 281
Cdd:TIGR01733 77 LTDSALASRLAGLVLPVILLD-------------------------PLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGS 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 282 TGRPKGVMMHHSNLIAgMTGQCERIPGLGPKDTYIGYLPLAH---VLELTAeiscftygcrigyssPLTLsdqsskikkg 358
Cdd:TIGR01733 132 TGRPKGVVVTHRSLVN-LLAWLARRYGLDPDDRVLQFASLSFdasVEEIFG---------------ALLA---------- 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 359 skGDCTVLKPTLMAAVPEIMDRIYKNVMsKVQEMNYVqKTLFKigydykleqikkgydaplcnliLFKKVKALLGGNVRM 438
Cdd:TIGR01733 186 --GATLVVPPEDEERDDAALLAALIAEH-PVTVLNLT-PSLLA----------------------LLAAALPPALASLRL 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 439 MLSGGAPLSPQTH-RFMNVCFCCPIGQGYGLTESCGAGTVTEVTDYTTGR-----VGAPLICCEIKLKDwqeggytVHDK 512
Cdd:TIGR01733 240 VILGGEALTPALVdRWRARGPGARLINLYGPTETTVWSTATLVDPDDAPRespvpIGRPLANTRLYVLD-------DDLR 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 513 PNPR---GEIVIGGQNISMGYFKNEEKTAEDYCVD----ENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVSL 585
Cdd:TIGR01733 313 PVPVgvvGELYIGGPGVARGYLNRPELTAERFVPDpfagGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIR-GYRIEL 391
|
490
....*....|....*...
gi 1720435377 586 GKVEAALKNCPLIDNICA 603
Cdd:TIGR01733 392 GEIEAALLRHPGVREAVV 409
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
268-629 |
1.04e-26 |
|
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: 113.88 E-value: 1.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 268 TPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPgLGPkdtyigylplahvleltaeiscftyGCRIGYSSPLT 347
Cdd:cd05945 95 DGDDNAYIIFTSGSTGRPKGVQISHDNLVSFTNWMLSDFP-LGP-------------------------GDVFLNQAPFS 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 348 LsdqsskikkgskgDCTV--LKPTLMA-----AVPEIMDRIYKNVMSKVQEMnyvqktlfkigydykleQIKKGYDAP-- 418
Cdd:cd05945 149 F-------------DLSVmdLYPALASgatlvPVPRDATADPKQLFRFLAEH-----------------GITVWVSTPsf 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 419 --LCnlILFKKVKALLGGNVRMMLSGGAPLSPQTHRFMNVCF-CCPIGQGYGLTESCGAGTVTEVT-----DYTTGRVGA 490
Cdd:cd05945 199 aaMC--LLSPTFTPESLPSLRHFLFCGEVLPHKTARALQQRFpDARIYNTYGPTEATVAVTYIEVTpevldGYDRLPIGY 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 491 PLICCEIKLKDwqEGGYTVhdKPNPRGEIVIGGQNISMGYFKNEEKTAEdYCVDENGQRWFCTGDIGEFHPDGCLQIIDR 570
Cdd:cd05945 277 AKPGAKLVILD--EDGRPV--PPGEKGELVISGPSVSKGYLNNPEKTAA-AFFPDEGQRAYRTGDLVRLEADGLLFYRGR 351
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720435377 571 KKDLVKLQaGEYVSLGKVEAALKNCPLIDNICAFAKSDQSYV---ISFVVP----NQKKLTLLAQQ 629
Cdd:cd05945 352 LDFQVKLN-GYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVtelIAFVVPkpgaEAGLTKAIKAE 416
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
271-609 |
1.28e-26 |
|
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: 113.16 E-value: 1.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 271 DMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLAH----VLELTAEISCftyGCRIgysspl 346
Cdd:cd05934 82 DPASILYTSGTTGPPKGVVITHANLTFAGYYSARRF-GLGEDDVYLTVLPLFHinaqAVSVLAALSV---GATL------ 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 347 tlsdqsskikkgskgdctVLKPTLMAAvpeimdriykNVMSKVQE-----MNYVQKTLfkigyDYKLEQIKKGYDAplcn 421
Cdd:cd05934 152 ------------------VLLPRFSAS----------RFWSDVRRygatvTNYLGAML-----SYLLAQPPSPDDR---- 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 422 lilfkkvkallGGNVRmmLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKD 501
Cdd:cd05934 195 -----------AHRLR--AAYGAPNPPELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIVD 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 502 wqeggytVHDKPNPR---GEIVI---GGQNISMGYFKNEEKTAEdycVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLV 575
Cdd:cd05934 262 -------DDGQELPAgepGELVIrglRGWGFFKGYYNMPEATAE---AMRNG--WFHTGDLGYRDADGFFYFVDRKKDMI 329
|
330 340 350
....*....|....*....|....*....|....
gi 1720435377 576 KlQAGEYVSLGKVEAALKNCPLIDNICAFAKSDQ 609
Cdd:cd05934 330 R-RRGENISSAEVERAILRHPAVREAAVVAVPDE 362
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
126-629 |
3.24e-26 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 115.34 E-value: 3.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 126 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCEtRAEWMIAAqtcfkynfplvtLYATL--G-----------REAVVHG 192
Cdd:COG1020 502 LTYAELNARANRLAHHLRALGVGPGDLVGVCLE-RSLEMVVA------------LLAVLkaGaayvpldpaypAERLAYM 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 193 LNESEASYLITsvellESKLKAALVDINCvkHIIYVDNKTInrAEYPEgleihsmqsveelgakpenlSVPPSRPTPSDM 272
Cdd:COG1020 569 LEDAGARLVLT-----QSALAARLPELGV--PVLALDALAL--AAEPA--------------------TNPPVPVTPDDL 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 273 AIVMYTSGSTGRPKGVMMHH---SNLIAGMTGQCeripGLGPKDTYIGYLPLAH---VLELtaeISCFTYGCRIGYSSPL 346
Cdd:COG1020 620 AYVIYTSGSTGRPKGVMVEHralVNLLAWMQRRY----GLGPGDRVLQFASLSFdasVWEI---FGALLSGATLVLAPPE 692
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 347 TLSD--------QSSKIkkgskgdcTVLK--PTLMAAVPEimdriyknvmskvqemnyvqktlfkigydykleqikkgYD 416
Cdd:COG1020 693 ARRDpaalaellARHRV--------TVLNltPSLLRALLD--------------------------------------AA 726
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 417 APLCnlilfkkvkallgGNVRMMLSGGAPLSPQT-HRFMNVCFCCPIGQGYGLTESCGAGTVTEVT--DYTTGRV--GAP 491
Cdd:COG1020 727 PEAL-------------PSLRLVLVGGEALPPELvRRWRARLPGARLVNLYGPTETTVDSTYYEVTppDADGGSVpiGRP 793
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 492 LicceiklkdwqeGGYTV-----HDKPNP---RGEIVIGGQNISMGYFKNEEKTAEDYCVD---ENGQRWFCTGDIGEFH 560
Cdd:COG1020 794 I------------ANTRVyvldaHLQPVPvgvPGELYIGGAGLARGYLNRPELTAERFVADpfgFPGARLYRTGDLARWL 861
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720435377 561 PDGCLQIIDRKKDLVKLQaGEYVSLGKVEAALKNCPLIDNICAFAKSDQS---YVISFVVPNQKKLTLLAQQ 629
Cdd:COG1020 862 PDGNLEFLGRADDQVKIR-GFRIELGEIEAALLQHPGVREAVVVAREDAPgdkRLVAYVVPEAGAAAAAALL 932
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
127-596 |
3.44e-26 |
|
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: 113.11 E-value: 3.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 127 NYLEVNCRVNNFGSGLTALGLKPKNTIAIFCetraeWmiaaqTCFKYnfpLVTLYATLGREAVVHGLN------------ 194
Cdd:cd12119 27 TYAEVAERARRLANALRRLGVKPGDRVATLA-----W-----NTHRH---LELYYAVPGMGAVLHTINprlfpeqiayii 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 195 -ESEASYLITSVELLeSKLKAALVDINCVKHIIYVDNKTINRAEYPEGLE-----IHSMQSVEELGAKPENlsvppsrpt 268
Cdd:cd12119 94 nHAEDRVVFVDRDFL-PLLEAIAPRLPTVEHVVVMTDDAAMPEPAGVGVLayeelLAAESPEYDWPDFDEN--------- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 269 psDMAIVMYTSGSTGRPKGVMM-HHSNLIAGMTGQCERIPGLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSSPLT 347
Cdd:cd12119 164 --TAAAICYTSGTTGNPKGVVYsHRSLVLHAMAALLTDGLGLSESDVVLPVVPMFHVNAWGLPYAAAMVGAKLVLPGPYL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 348 LSDQSSKIKKGSKgdctvlkPTLMAAVPEImdriYKNVMSKVQEMNYVQKTLfkigydykleqikkgydaplcnlilfkk 427
Cdd:cd12119 242 DPASLAELIEREG-------VTFAAGVPTV----WQGLLDHLEANGRDLSSL---------------------------- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 428 vkallggnvRMMLSGGAPLSP---QTHRFMNVcfccPIGQGYGLTESCGAGTVTEVTDY--------------TTGRVgA 490
Cdd:cd12119 283 ---------RRVVIGGSAVPRsliEAFEERGV----RVIHAWGMTETSPLGTVARPPSEhsnlsedeqlalraKQGRP-V 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 491 PLIccEIKLKDwQEGGYTVHDkPNPRGEIVIGGQNISMGYFKNEEKTAEdycVDENGqrWFCTGDIGEFHPDGCLQIIDR 570
Cdd:cd12119 349 PGV--ELRIVD-DDGRELPWD-GKAVGELQVRGPWVTKSYYKNDEESEA---LTEDG--WLRTGDVATIDEDGYLTITDR 419
|
490 500
....*....|....*....|....*.
gi 1720435377 571 KKDLVKlQAGEYVSLGKVEAALKNCP 596
Cdd:cd12119 420 SKDVIK-SGGEWISSVELENAIMAHP 444
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
183-610 |
5.42e-26 |
|
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: 112.42 E-value: 5.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 183 TLGREAVVHGLNESEASYLITSVELLEsKLKAA-LVDINCVKHIIYVDN--KTINRAEYPEGLeIHSMQSVEELgakpen 259
Cdd:cd05909 64 TAGLRELRACIKLAGIKTVLTSKQFIE-KLKLHhLFDVEYDARIVYLEDlrAKISKADKCKAF-LAGKFPPKWL------ 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 260 LSVPPSRPT-PSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTgQCERIPGLGPKDTYIGYLPLAHVLELT-AEISCFTYG 337
Cdd:cd05909 136 LRIFGVAPVqPDDPAVILFTSGSEGLPKGVVLSHKNLLANVE-QITAIFDPNPEDVVFGALPFFHSFGLTgCLWLPLLSG 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 338 CRIG-YSSPLTLSDQSSKIKKGSkgdCTVL--KPTLMaavpeimdRIYknvmskvqeMNYVQKTLFKigydykleqikkg 414
Cdd:cd05909 215 IKVVfHPNPLDYKKIPELIYDKK---ATILlgTPTFL--------RGY---------ARAAHPEDFS------------- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 415 ydaplcnlilfkkvkallggNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTV-TEVTDYTTGRVGAPLI 493
Cdd:cd05909 262 --------------------SLRLVVAGAEKLKDTLRQEFQEKFGIRILEGYGTTECSPVISVnTPQSPNKEGTVGRPLP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 494 CCEIKLKDwQEGGytvhdKPNPRGE---IVIGGQNISMGYFKNEEKTAEDYcvdenGQRWFCTGDIGEFHPDGCLQIIDR 570
Cdd:cd05909 322 GMEVKIVS-VETH-----EEVPIGEgglLLVRGPNVMLGYLNEPELTSFAF-----GDGWYDTGDIGKIDGEGFLTITGR 390
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1720435377 571 KKDLVKLqAGEYVSLGKVE-AALKNCPLIDNICAFAKSDQS 610
Cdd:cd05909 391 LSRFAKI-AGEMVSLEAIEdILSEILPEDNEVAVVSVPDGR 430
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
271-676 |
7.85e-26 |
|
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: 111.23 E-value: 7.85e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 271 DMAIVMYTSGSTGRPKGVMMHHSNLIAgmtgQCERIP---GLGPKDTYIGYLPLAHVLELTAEISCFTYgCRigySSPLT 347
Cdd:cd05941 90 DPALILYTSGTTGRPKGVVLTHANLAA----NVRALVdawRWTEDDVLLHVLPLHHVHGLVNALLCPLF-AG---ASVEF 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 348 LSDQSSKIKKGSKGDCTVlkpTLMAAVPEIMDRIYKNVMSKVQEMNYVQKTLFKigydykleqikkgydaplcnlilfkk 427
Cdd:cd05941 162 LPKFDPKEVAISRLMPSI---TVFMGVPTIYTRLLQYYEAHFTDPQFARAAAAE-------------------------- 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 428 vkallggNVRMMLSGGAPLSPQTHRFmnvcFCCPIGQG----YGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDwQ 503
Cdd:cd05941 213 -------RLRLMVSGSAALPVPTLEE----WEAITGHTllerYGMTEIGMALSNPLDGERRPGTVGMPLPGVQARIVD-E 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 504 EGGytvhdKPNPR---GEIVIGGQNISMGYFKNEEKTAEDYCVDengqRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAG 580
Cdd:cd05941 281 ETG-----EPLPRgevGEIQVRGPSVFKEYWNKPEATKEEFTDD----GWFKTGDLGVVDEDGYYWILGRSSVDIIKSGG 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 581 EYVSLGKVEAALKNCPLIDNICAFAKSDQSY---VISFVVPnqkkltllaqQKGVegswvdicnnPAMEAEILKEireaA 657
Cdd:cd05941 352 YKVSALEIERVLLAHPGVSECAVIGVPDPDWgerVVAVVVL----------RAGA----------AALSLEELKE----W 407
|
410
....*....|....*....
gi 1720435377 658 NAMKLERFEIPIKVRLSPE 676
Cdd:cd05941 408 AKQRLAPYKRPRRLILVDE 426
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
268-620 |
2.33e-25 |
|
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: 109.54 E-value: 2.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 268 TPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPgLGPKDTYIGYLPLAHVLELTAEISCFTYGCRI------G 341
Cdd:cd05930 91 DPDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAYP-LTPGDRVLQFTSFSFDVSVWEIFGALLAGATLvvlpeeV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 342 YSSPLTLSD--QSSKIkkgskgdcTVLK--PTLMAAVpeimdriyknvmskvqeMNYVQKTLFKigydykleqikkgyda 417
Cdd:cd05930 170 RKDPEALADllAEEGI--------TVLHltPSLLRLL-----------------LQELELAALP---------------- 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 418 plcnlilfkkvkallggNVRMMLSGGAPLSPQT-HRFMNVCFCCPIGQGYGLTESCGAGTVTEVT--DYTTGRV--GAPL 492
Cdd:cd05930 209 -----------------SLRLVLVGGEALPPDLvRRWRELLPGARLVNLYGPTEATVDATYYRVPpdDEEDGRVpiGRPI 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 493 ICCEIklkdwqeggYTVHDKPNPR-----GEIVIGGQNISMGYFKNEEKTAEDYCVD--ENGQRWFCTGDIGEFHPDGCL 565
Cdd:cd05930 272 PNTRV---------YVLDENLRPVppgvpGELYIGGAGLARGYLNRPELTAERFVPNpfGPGERMYRTGDLVRWLPDGNL 342
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720435377 566 QIIDRKKDLVKLqAGEYVSLGKVEAALKNCPLIDNICAFAKSD---QSYVISFVVPNQ 620
Cdd:cd05930 343 EFLGRIDDQVKI-RGYRIELGEIEAALLAHPGVREAAVVAREDgdgEKRLVAYVVPDE 399
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
126-619 |
5.92e-25 |
|
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341310 [Multi-domain] Cd Length: 490 Bit Score: 108.95 E-value: 5.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 126 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASYLITsv 205
Cdd:cd17655 23 LTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEERIQYILEDSGADILLT-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 206 ellESKLKAALVDIncvKHIIYVDNKTInrAEYPEgleihsmqsveelgakpENLSvPPSRPtpSDMAIVMYTSGSTGRP 285
Cdd:cd17655 101 ---QSHLQPPIAFI---GLIDLLDEDTI--YHEES-----------------ENLE-PVSKS--DDLAYVIYTSGSTGKP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 286 KGVMMHHSNLIAGMTGQCERIPgLGPKDTYIGYLPLAhvLELTAEiSCFTygcrigyssPLTLSDQSSKIKKGSKGDctv 365
Cdd:cd17655 153 KGVMIEHRGVVNLVEWANKVIY-QGEHLRVALFASIS--FDASVT-EIFA---------SLLSGNTLYIVRKETVLD--- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 366 lkptlmaaVPEIMDRIYKNVMSKVqemnyvqktlfkigydykleqikkgyDAPLCNLILFKKVKALLGGNVRMMLSGGAP 445
Cdd:cd17655 217 --------GQALTQYIRQNRITII--------------------------DLTPAHLKLLDAADDSEGLSLKHLIVGGEA 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 446 LSPQT-----HRFMNvcfCCPIGQGYGLTESC-GAGT-VTEVTDYTTGRV--GAPLICCEIKLKDwQEGgytvhdKPNP- 515
Cdd:cd17655 263 LSTELakkiiELFGT---NPTITNAYGPTETTvDASIyQYEPETDQQVSVpiGKPLGNTRIYILD-QYG------RPQPv 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 516 --RGEIVIGGQNISMGYFKNEEKTAEDYCVDE--NGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVSLGKVEAA 591
Cdd:cd17655 333 gvAGELYIGGEGVARGYLNRPELTAEKFVDDPfvPGERMYRTGDLARWLPDGNIEFLGRIDHQVKIR-GYRIELGEIEAR 411
|
490 500 510
....*....|....*....|....*....|.
gi 1720435377 592 LKNCPLIDNICAFAKSDQS---YVISFVVPN 619
Cdd:cd17655 412 LLQHPDIKEAVVIARKDEQgqnYLCAYIVSE 442
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
201-575 |
6.54e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 106.39 E-value: 6.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 201 LITSVELLESKLKAALVDiNCVKHIiyvdNKTINRAEYPEGLEIHSMQSveelgaKPENLSVPPSRPTPSDMAIVMYTSG 280
Cdd:PRK05677 149 IVTEVADMLPPLKRLLIN-AVVKHV----KKMVPAYHLPQAVKFNDALA------KGAGQPVTEANPQADDVAVLQYTGG 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 281 STGRPKGVMMHHSNLIAGMTgQCERIPG--LGP-KDTYIGYLPLAHvleltaeISCFTYGCRIgysspLTLSdqsskikk 357
Cdd:PRK05677 218 TTGVAKGAMLTHRNLVANML-QCRALMGsnLNEgCEILIAPLPLYH-------IYAFTFHCMA-----MMLI-------- 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 358 gskGDCTVLKPTlmaavPEIMDRIYKnVMSKVQEMNYVQ-KTLFkigydykleqikkgydAPLCNLILFKKV--KALlgg 434
Cdd:PRK05677 277 ---GNHNILISN-----PRDLPAMVK-ELGKWKFSGFVGlNTLF----------------VALCNNEAFRKLdfSAL--- 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 435 nvRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDwQEGGYTVHDKPn 514
Cdd:PRK05677 329 --KLTLSGGMALQLATAERWKEVTGCAICEGYGMTETSPVVSVNPSQAIQVGTIGIPVPSTLCKVID-DDGNELPLGEV- 404
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720435377 515 prGEIVIGGQNISMGYFKNEEKTAEdyCVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLV 575
Cdd:PRK05677 405 --GELCVKGPQVMKGYWQRPEATDE--ILDSDG--WLKTGDIALIQEDGYMRIVDRKKDMI 459
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
126-609 |
6.78e-24 |
|
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.
Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 105.25 E-value: 6.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 126 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASYLITSV 205
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 206 ELlesklkaalvdincvkhiiyvdnktinraeypegleihsmqsveelgakpenlsvppsrptpSDMAIVMYTSGSTGRP 285
Cdd:cd05935 82 EL--------------------------------------------------------------DDLALIPYTSGTTGLP 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 286 KGVMMHHSNLIAGMTGQCeRIPGLGPKDTYIGYLPLAHVLELTAEISCFTYGCriGYSSPLTLSDQSSKIKKGSKGDCTV 365
Cdd:cd05935 100 KGCMHTHFSAAANALQSA-VWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVG--GTYVLMARWDRETALELIEKYKVTF 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 366 LkptlMAAVPEIMDriyknVMSKVQEMNYVQKTLfkigydykleqikkgydaplcnlilfkkvkallggnvRMMLSGGAP 445
Cdd:cd05935 177 W----TNIPTMLVD-----LLATPEFKTRDLSSL-------------------------------------KVLTGGGAP 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 446 LSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDWQEGgytVHDKPNPRGEIVIGGQN 525
Cdd:cd05935 211 MPPAVAEKLLKLTGLRFVEGYGLTETMSQTHTNPPLRPKLQCLGIP*FGVDARVIDIETG---RELPPNEVGEIVVRGPQ 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 526 ISMGYFKNEEKTAEDYcVDENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLqAGEYVSLGKVEAALKNCPLIDNICAFA 605
Cdd:cd05935 288 IFKGYWNRPEETEESF-IEIKGRRFFRTGDLGYMDEEGYFFFVDRVKRMINV-SGFKVWPAEVEAKLYKHPAI*EVCVIS 365
|
....
gi 1720435377 606 KSDQ 609
Cdd:cd05935 366 VPDE 369
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
271-700 |
2.17e-23 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 101.64 E-value: 2.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 271 DMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPgLGPKDTYIGYLPLAHVLELTAEISCFTYGcrigysSPLTLSD 350
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLG-FGGGDSWLLSLPLYHVGGLAILVRSLLAG------AELVLLE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 351 QSSKIKKgskgDCTVLKPTLMAAVPEimdriyknvmskvqemnyvqktlfkigydykleQIKKGYDAPLCNLILFkkvka 430
Cdd:cd17630 74 RNQALAE----DLAPPGVTHVSLVPT---------------------------------QLQRLLDSGQGPAALK----- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 431 llggNVRMMLSGGAPLSPQ-THRFMnvCFCCPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDwqeggytv 509
Cdd:cd17630 112 ----SLRAVLLGGAPIPPElLERAA--DRGIPLYTTYGMTETASQVATKRPDGFGRGGVGVLLPGRELRIVE-------- 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 510 hdkpnpRGEIVIGGQNISMGYFKNEEKTAedycVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVkLQAGEYVSLGKVE 589
Cdd:cd17630 178 ------DGEIWVGGASLAMGYLRGQLVPE----FNEDG--WFTTKDLGELHADGRLTVLGRADNMI-ISGGENIQPEEIE 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 590 AALKNCPLIDNICAFAKSDQSY---VISFVVPnqkkltllaqqkgvegswvdicNNPAMEAEILKEIREaanamKLERFE 666
Cdd:cd17630 245 AALAAHPAVRDAFVVGVPDEELgqrPVAVIVG----------------------RGPADPAELRAWLKD-----KLARFK 297
|
410 420 430
....*....|....*....|....*....|....
gi 1720435377 667 IPIkvRLSPEPWTPETGLVtdafKLKRKELKNHY 700
Cdd:cd17630 298 LPK--RIYPVPELPRTGGG----KVDRRALRAWL 325
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
128-625 |
8.61e-23 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 102.90 E-value: 8.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 128 YLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASYLI----- 202
Cdd:PRK06087 52 YSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFaptlf 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 203 --TSVELLESKLKAalvDINCVKHIIYVDNktinraEYPEgleiHSMQSVEELGAKPENLSVPPsrPTPSD-MAIVMYTS 279
Cdd:PRK06087 132 kqTRPVDLILPLQN---QLPQLQQIVGVDK------LAPA----TSSLSLSQIIADYEPLTTAI--TTHGDeLAAVLFTS 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 280 GSTGRPKGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLAHVLE-LTAEISCFTYGCRigySSPLTLSDQSSKIKKG 358
Cdd:PRK06087 197 GTEGLPKGVMLTHNNILASERAYCARL-NLTWQDVFMMPAPLGHATGfLHGVTAPFLIGAR---SVLLDIFTPDACLALL 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 359 SKGDCTvlkpTLMAAVPEIMDriyknVMSKVQEMNYVQKTLfkigydykleqikkgydaplcnlilfkkvkallggnvRM 438
Cdd:PRK06087 273 EQQRCT----CMLGATPFIYD-----LLNLLEKQPADLSAL-------------------------------------RF 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 439 MLSGGAP----LSPQTHRFmNVCFCcpigQGYGLTESCGAGTVT--EVTDYTTGRVGAPLICCEIKLKDwqeggytVHDK 512
Cdd:PRK06087 307 FLCGGTTipkkVARECQQR-GIKLL----SVYGSTESSPHAVVNldDPLSRFMHTDGYAAAGVEIKVVD-------EARK 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 513 PNPRG---EIVIGGQNISMGYFKNEEKTAEdyCVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVkLQAGEYVSLGKVE 589
Cdd:PRK06087 375 TLPPGcegEEASRGPNVFMGYLDEPELTAR--ALDEEG--WYYSGDLCRMDEAGYIKITGRKKDII-VRGGENISSREVE 449
|
490 500 510
....*....|....*....|....*....|....*....
gi 1720435377 590 AALKNCPLIDNICAFAKSDQSY---VISFVVPNQKKLTL 625
Cdd:PRK06087 450 DILLQHPKIHDACVVAMPDERLgerSCAYVVLKAPHHSL 488
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
126-618 |
1.41e-22 |
|
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: 101.58 E-value: 1.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 126 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAqtcfkynfpLVTLYAtlgreavvhGlneseASYLITSV 205
Cdd:cd12114 13 LTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAV---------LGILAA---------G-----AAYVPVDI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 206 ELLESKLKAALVD--INCVkhiiyvdnktINRAEYPEGLEIHSMQSVEELGAKPENLSVPPSRPTPSDMAIVMYTSGSTG 283
Cdd:cd12114 70 DQPAARREAILADagARLV----------LTDGPDAQLDVAVFDVLILDLDALAAPAPPPPVDVAPDDLAYVIFTSGSTG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 284 RPKGVMMHH---SNLIAGMTgqcERIpGLGPKDTYIGYLPLAH---VLELTAEIScftygcrIGYSspLTLSDQsskikk 357
Cdd:cd12114 140 TPKGVMISHraaLNTILDIN---RRF-AVGPDDRVLALSSLSFdlsVYDIFGALS-------AGAT--LVLPDE------ 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 358 GSKGDCTVLKP-------TLMAAVPEIMDRIyknvmskvqeMNYVQKTlfkigydykleqikkgyDAPLCNLilfkkvka 430
Cdd:cd12114 201 ARRRDPAHWAElierhgvTLWNSVPALLEML----------LDVLEAA-----------------QALLPSL-------- 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 431 llggnvRM-MLSG---GAPLSPQTHRFmnVCFCCPIGQGyGLTESCGAGTVTEVTDYTTGRV----GAPLI--CCEIkLK 500
Cdd:cd12114 246 ------RLvLLSGdwiPLDLPARLRAL--APDARLISLG-GATEASIWSIYHPIDEVPPDWRsipyGRPLAnqRYRV-LD 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 501 DWQEggytvhDKPN-PRGEIVIGGQNISMGYFKNEEKTAEDYCVDENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQa 579
Cdd:cd12114 316 PRGR------DCPDwVPGELWIGGRGVALGYLGDPELTAARFVTHPDGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVR- 388
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1720435377 580 GEYVSLGKVEAALKNCPLIDNICAFAKSD--QSYVISFVVP 618
Cdd:cd12114 389 GYRIELGEIEAALQAHPGVARAVVVVLGDpgGKRLAAFVVP 429
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
125-609 |
4.11e-22 |
|
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: 100.06 E-value: 4.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 125 WINYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASYLITS 204
Cdd:cd12116 12 SLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALVLTD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 205 VELLESklkaalvdincvkhiiyvdnktinraeYPEGLEIhSMQSVEELGAKPENLSVPPSrptPSDMAIVMYTSGSTGR 284
Cdd:cd12116 92 DALPDR---------------------------LPAGLPV-LLLALAAAAAAPAAPRTPVS---PDDLAYVIYTSGSTGR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 285 PKGVMMHHSNLIAGMTGQCERiPGLGPKDTYIG-------------YLPL---AHVLELTAEIScftygcrigySSPLTL 348
Cdd:cd12116 141 PKGVVVSHRNLVNFLHSMRER-LGLGPGDRLLAvttyafdisllelLLPLlagARVVIAPRETQ----------RDPEAL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 349 SDQSSKIkkgskgdctvlKPTLMAAVPEimdriyknvmskvqemnyVQKTLFKIGYdykleQIKKGYDApLCnlilfkkv 428
Cdd:cd12116 210 ARLIEAH-----------SITVMQATPA------------------TWRMLLDAGW-----QGRAGLTA-LC-------- 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 429 kallggnvrmmlsGGAPLSPQTHRFmnvcFCCPIGQG---YGLTESCGAGTVTEVTDYTTG-RVGAPLicceiklkdwqe 504
Cdd:cd12116 247 -------------GGEALPPDLAAR----LLSRVGSLwnlYGPTETTIWSTAARVTAAAGPiPIGRPL------------ 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 505 GGYTVH--D---KPNPR---GEIVIGGQNISMGYFKNEEKTAEDYCVD---ENGQRWFCTGDIGEFHPDGCLQIIDRKKD 573
Cdd:cd12116 298 ANTQVYvlDaalRPVPPgvpGELYIGGDGVAQGYLGRPALTAERFVPDpfaGPGSRLYRTGDLVRRRADGRLEYLGRADG 377
|
490 500 510
....*....|....*....|....*....|....*.
gi 1720435377 574 LVKLQaGEYVSLGKVEAALKNCPLIDNICAFAKSDQ 609
Cdd:cd12116 378 QVKIR-GHRIELGEIEAALAAHPGVAQAAVVVREDG 412
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
128-620 |
1.40e-21 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 98.97 E-value: 1.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 128 YLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFK----YNfPLVTLYatlgRE-AVVHGLNESEASYLI 202
Cdd:PRK13295 58 YRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRigavLN-PLMPIF----RErELSFMLKHAESKVLV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 203 T-------SVELLESKLKAALVDIncvKHIIYVDnktinrAEYPEGLEIHSMQSVEELGAKPENLSVPPsRPTPSDMAIV 275
Cdd:PRK13295 133 VpktfrgfDHAAMARRLRPELPAL---RHVVVVG------GDGADSFEALLITPAWEQEPDAPAILARL-RPGPDDVTQL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 276 MYTSGSTGRPKGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLAHvleLTAeiscFTYGCRIgyssPLTLsdqsski 355
Cdd:PRK13295 203 IYTSGTTGEPKGVMHTANTLMANIVPYAERL-GLGADDVILMASPMAH---QTG----FMYGLMM----PVML------- 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 356 kkgskGDCTVLK----PTL-------------MAAVPEIMDriyknvMSKVQEMNyvqktlfkigydykleqikkGYDAP 418
Cdd:PRK13295 264 -----GATAVLQdiwdPARaaelirtegvtftMASTPFLTD------LTRAVKES--------------------GRPVS 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 419 lcnlilfkkvkallggNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTEsCGAGTVT------EVTDYTTGRvgaPL 492
Cdd:PRK13295 313 ----------------SLRTFLCAGAPIPGALVERARAALGAKIVSAWGMTE-NGAVTLTklddpdERASTTDGC---PL 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 493 ICCEIKLKDWQeggytvhDKPNPRGEI---VIGGQNISMGYFKNEEKTAEDycvdenGQRWFCTGDIGEFHPDGCLQIID 569
Cdd:PRK13295 373 PGVEVRVVDAD-------GAPLPAGQIgrlQVRGCSNFGGYLKRPQLNGTD------ADGWFDTGDLARIDADGYIRISG 439
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1720435377 570 RKKDLVkLQAGEYVSLGKVEAALKNCPLIDNICAFAKSD---QSYVISFVVPNQ 620
Cdd:PRK13295 440 RSKDVI-IRGGENIPVVEIEALLYRHPAIAQVAIVAYPDerlGERACAFVVPRP 492
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
178-592 |
1.71e-21 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 100.00 E-value: 1.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 178 VTLYATLGREAVVHGLNESEASYLITSVELLEsKLKAALVDincvkhiiyvdnktinrAEYPEGLEIHSMqsvEELGAKP 257
Cdd:PRK08633 693 VNLNYTASEAALKSAIEQAQIKTVITSRKFLE-KLKNKGFD-----------------LELPENVKVIYL---EDLKAKI 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 258 ENL---------SVPPSR---------PTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTgQCERIPGLGPKDTYIGYL 319
Cdd:PRK08633 752 SKVdkltallaaRLLPARllkrlygptFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIE-QISDVFNLRNDDVILSSL 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 320 PLAHVLELTAE--------ISCftygcrIGYSSPLtlsdQSSKIKKgskgdcTVLK--PTLMAAVPEIMdRIY-KNvmsk 388
Cdd:PRK08633 831 PFFHSFGLTVTlwlpllegIKV------VYHPDPT----DALGIAK------LVAKhrATILLGTPTFL-RLYlRN---- 889
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 389 vqemnyvqktlfkigydykleqikkgydaplcnlilfKKVKALLGGNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGL 468
Cdd:PRK08633 890 -------------------------------------KKLHPLMFASLRLVVAGAEKLKPEVADAFEEKFGIRILEGYGA 932
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 469 TESCGAGTV----TEVTDYTT------GRVGAPLICCEIKLKDwQEGGYTVhdKPNPRGEIVIGGQNISMGYFKNEEKTA 538
Cdd:PRK08633 933 TETSPVASVnlpdVLAADFKRqtgskeGSVGMPLPGVAVRIVD-PETFEEL--PPGEDGLILIGGPQVMKGYLGDPEKTA 1009
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1720435377 539 EdYCVDENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLqAGEYVSLGKVEAAL 592
Cdd:PRK08633 1010 E-VIKDIDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKI-GGEMVPLGAVEEEL 1061
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
263-683 |
2.41e-21 |
|
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: 97.75 E-value: 2.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 263 PPSRPTPSDMAIVM-YTSGSTGRPKGVMMHH--------SNLIAGmtgqceripGLGPKDTYIGYLPLAHvleltAEISC 333
Cdd:cd12118 125 EWIPPADEWDPIALnYTSGTTGRPKGVVYHHrgaylnalANILEW---------EMKQHPVYLWTLPMFH-----CNGWC 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 334 FTYGcrigysspltlsdqsskikkgskgdctvlkptlMAAV------------PEIMDRIYKNvmsKVQEMNyvqktlfk 401
Cdd:cd12118 191 FPWT---------------------------------VAAVggtnvclrkvdaKAIYDLIEKH---KVTHFC-------- 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 402 igydykleqikkgyDAPLCNLILF---KKVKALLGGNVRMMlSGGAPLSPQTHRFMNvcfccPIG----QGYGLTESCGA 474
Cdd:cd12118 227 --------------GAPTVLNMLAnapPSDARPLPHRVHVM-TAGAPPPAAVLAKME-----ELGfdvtHVYGLTETYGP 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 475 GTV-----------TEVTDYTTGRVGAPLICCEiklkdwqegGYTVHD----KPNPR-----GEIVIGGQNISMGYFKNE 534
Cdd:cd12118 287 ATVcawkpewdelpTEERARLKARQGVRYVGLE---------EVDVLDpetmKPVPRdgktiGEIVFRGNIVMKGYLKNP 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 535 EKTAEDYcvdENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVkLQAGEYVSLGKVEAALKNCPLIDNICAFAKSDQSYVIS 614
Cdd:cd12118 358 EATAEAF---RGG--WFHSGDLAVIHPDGYIEIKDRSKDII-ISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEV 431
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720435377 615 ---FVvpnqkklTLlaqQKGVEgswvdicnnpAMEAEILKEIREaanamKLERFEIPIKVRLSPEPWTPeTG 683
Cdd:cd12118 432 pcaFV-------EL---KEGAK----------VTEEEIIAFCRE-----HLAGFMVPKTVVFGELPKTS-TG 477
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
135-611 |
2.42e-21 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 98.31 E-value: 2.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 135 VNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASYLITS---------- 204
Cdd:PRK12583 55 VDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVICAdafktsdyha 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 205 --VELLESKLKAALVDINC-----VKHIIYVDnktinrAEYPEG-LEIHSMQSVEElGAKPENLSVPPSRPTPSDMAIVM 276
Cdd:PRK12583 135 mlQELLPGLAEGQPGALACerlpeLRGVVSLA------PAPPPGfLAWHELQARGE-TVSREALAERQASLDRDDPINIQ 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 277 YTSGSTGRPKGVMMHHSNLI--AGMTGqcERIpGLGPKDTYIGYLPLAHVLELT-AEISCFTYGCRIGYssPLTLSDQSS 353
Cdd:PRK12583 208 YTSGTTGFPKGATLSHHNILnnGYFVA--ESL-GLTEHDRLCVPVPLYHCFGMVlANLGCMTVGACLVY--PNEAFDPLA 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 354 KIKKGSKGDCTVLK--PTLMAAvpeimdriyknvmskvqEMNYVQKTLFKIGydykleqikkgydaplcnlilfkkvkal 431
Cdd:PRK12583 283 TLQAVEEERCTALYgvPTMFIA-----------------ELDHPQRGNFDLS---------------------------- 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 432 lggNVRMMLSGGAPLSPQT-HRFMNVCFCCPIGQGYGLTESCGAGTVTEVTD------YTTGRVGAPLiccEIKLKDwqE 504
Cdd:PRK12583 318 ---SLRTGIMAGAPCPIEVmRRVMDEMHMAEVQIAYGMTETSPVSLQTTAADdlerrvETVGRTQPHL---EVKVVD--P 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 505 GGYTVhdKPNPRGEIVIGGQNISMGYFKNEEKTAEdyCVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVkLQAGEYVS 584
Cdd:PRK12583 390 DGATV--PRGEIGELCTRGYSVMKGYWNNPEATAE--SIDEDG--WMHTGDLATMDEQGYVRIVGRSKDMI-IRGGENIY 462
|
490 500
....*....|....*....|....*..
gi 1720435377 585 LGKVEAALKNCPLIDNICAFAKSDQSY 611
Cdd:PRK12583 463 PREIEEFLFTHPAVADVQVFGVPDEKY 489
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
69-698 |
4.04e-21 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 97.64 E-value: 4.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 69 AVIDIPGADTLDKLFDHAVAKFGKKdslgtreilseenemqPNGKVFKKLIlgnykwiNYLEVNCRVNNFGSGLTA-LGL 147
Cdd:PRK08751 17 AEIDLEQFRTVAEVFATSVAKFADR----------------PAYHSFGKTI-------TYREADQLVEQFAAYLLGeLQL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 148 KPKNTIAIFCETRAEWMIAAQTCFKYNFPLVT---LYATlgREaVVHGLNESEASYLI------TSVE----------LL 208
Cdd:PRK08751 74 KKGDRVALMMPNCLQYPIATFGVLRAGLTVVNvnpLYTP--RE-LKHQLIDSGASVLVvidnfgTTVQqviadtpvkqVI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 209 ESKL-------KAALVDInCVKHII-YVDNKTINRA-EYPEGLEihsmqsveeLGAKPenlSVPPSRPTPSDMAIVMYTS 279
Cdd:PRK08751 151 TTGLgdmlgfpKAALVNF-VVKYVKkLVPEYRINGAiRFREALA---------LGRKH---SMPTLQIEPDDIAFLQYTG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 280 GSTGRPKGVMMHHSNLIAGMTGQCERIPGLGP----KDTYIGYLPLAHVLELTAEISCFTY--GCRIGYSSPltlSDQSS 353
Cdd:PRK08751 218 GTTGVAKGAMLTHRNLVANMQQAHQWLAGTGKleegCEVVITALPLYHIFALTANGLVFMKigGCNHLISNP---RDMPG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 354 KIKKgskgdctvLKPTLMAAVPEImdriyknvmskvqemnyvqKTLFkigydykleqiKKGYDAPLCNLILFKKVKALLG 433
Cdd:PRK08751 295 FVKE--------LKKTRFTAFTGV-------------------NTLF-----------NGLLNTPGFDQIDFSSLKMTLG 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 434 GNVRMMLSGGAPLSPQTHrfmnvcfcCPIGQGYGLTESCGAGTVTEVT--DYtTGRVGAPLICCEIKLKDwqeggytVHD 511
Cdd:PRK08751 337 GGMAVQRSVAERWKQVTG--------LTLVEAYGLTETSPAACINPLTlkEY-NGSIGLPIPSTDACIKD-------DAG 400
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 512 KPNPRGEI---VIGGQNISMGYFKNEEKTAEdyCVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVkLQAGEYVSLGKV 588
Cdd:PRK08751 401 TVLAIGEIgelCIKGPQVMKGYWKRPEETAK--VMDADG--WLHTGDIARMDEQGFVYIVDRKKDMI-LVSGFNVYPNEI 475
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 589 EAALKNCPLIDNICAFAksdqsyvisfvVPNQKkltllaqqKGVEGSWVDICNNPAMEAEILKEiREAANamkLERFEIP 668
Cdd:PRK08751 476 EDVIAMMPGVLEVAAVG-----------VPDEK--------SGEIVKVVIVKKDPALTAEDVKA-HARAN---LTGYKQP 532
|
650 660 670
....*....|....*....|....*....|
gi 1720435377 669 IKVRLSPEpwTPEtglvTDAFKLKRKELKN 698
Cdd:PRK08751 533 RIIEFRKE--LPK----TNVGKILRRELRD 556
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
119-618 |
4.96e-21 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 97.24 E-value: 4.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 119 ILGNYKWINYLEVNCRVNNFGSGLT-ALGLKPKNTIAIFcetraewmiaAQTCFKYnfpLVTLYATLGREAVVHGLN--- 194
Cdd:PRK06839 21 IITEEEEMTYKQLHEYVSKVAAYLIyELNVKKGERIAIL----------SQNSLEY---IVLLFAIAKVECIAVPLNirl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 195 -ESEASYLI----TSVELLESKLKAALVDIncvKHIIYVDNKTinRAEYPEGLEIHSMQSVEElgakpenlsvppsrPTP 269
Cdd:PRK06839 88 tENELIFQLkdsgTTVLFVEKTFQNMALSM---QKVSYVQRVI--SITSLKEIEDRKIDNFVE--------------KNE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 270 SDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLAHVleltAEISCFTY-----GCRIGYSS 344
Cdd:PRK06839 149 SASFIICYTSGTTGKPKGAVLTQENMFWNALNNTFAI-DLTMHDRSIVLLPLFHI----GGIGLFAFptlfaGGVIIVPR 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 345 PLTLSDQSSKIKKGskgdctvlKPTLMAAVPEIMDRiyknvmskvqemnyvqktlfkigydykleqikkgydapLCNLIL 424
Cdd:PRK06839 224 KFEPTKALSMIEKH--------KVTVVMGVPTIHQA--------------------------------------LINCSK 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 425 FKKVKAllgGNVRMMLSGGAPLS-PQTHRFMNVCFccPIGQGYGLTEScgAGTV----TEVTDYTTGRVGAPLICCEIKL 499
Cdd:PRK06839 258 FETTNL---QSVRWFYNGGAPCPeELMREFIDRGF--LFGQGFGMTET--SPTVfmlsEEDARRKVGSIGKPVLFCDYEL 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 500 KDwqEGGYTVhdKPNPRGEIVIGGQNISMGYFKNEEKTAEDYcvdENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVkLQA 579
Cdd:PRK06839 331 ID--ENKNKV--EVGEVGELLIRGPNVMKEYWNRPDATEETI---QDG--WLCTGDLARVDEDGFVYIVGRKKEMI-ISG 400
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1720435377 580 GEYVSLGKVEAALKNCPLIDNICAFAKSDQSY---VISFVVP 618
Cdd:PRK06839 401 GENIYPLEVEQVINKLSDVYEVAVVGRQHVKWgeiPIAFIVK 442
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
193-625 |
5.05e-21 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 97.59 E-value: 5.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 193 LNESEASYLI-TSVELLESKLKAALVDInCVKHIiyvdNKTINRAEYPEGLeihSMQSVEELGAkpeNLSVPPSRPTPSD 271
Cdd:PRK12492 140 LPDTGIEYLIeAKMGDLLPAAKGWLVNT-VVDKV----KKMVPAYHLPQAV---PFKQALRQGR---GLSLKPVPVGLDD 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 272 MAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPGLGP---------KDTYIGYLPLAHVLELTAEISCFTYgcrigy 342
Cdd:PRK12492 209 IAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSQLGPdgqplmkegQEVMIAPLPLYHIYAFTANCMCMMV------ 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 343 sspltlsdqsskikkgsKGDCTVLKpTLMAAVPEIMDRIYKNVMSKVQEMNyvqkTLFkigydykleqikkgydAPLCNL 422
Cdd:PRK12492 283 -----------------SGNHNVLI-TNPRDIPGFIKELGKWRFSALLGLN----TLF----------------VALMDH 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 423 ILFKKVKAllgGNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTEScgaGTVTEVTDYTT----GRVGAPLICCEIK 498
Cdd:PRK12492 325 PGFKDLDF---SALKLTNSGGTALVKATAERWEQLTGCTIVEGYGLTET---SPVASTNPYGElarlGTVGIPVPGTALK 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 499 LKDwQEGgytVHDKPNPRGEIVIGGQNISMGYFKNEEKTAEdyCVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVkLQ 578
Cdd:PRK12492 399 VID-DDG---NELPLGERGELCIKGPQVMKGYWQQPEATAE--ALDAEG--WFKTGDIAVIDPDGFVRIVDRKKDLI-IV 469
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1720435377 579 AGEYVSLGKVEAALKNCPLIDNICAFAKSDQ---SYVISFVVPNQKKLTL 625
Cdd:PRK12492 470 SGFNVYPNEIEDVVMAHPKVANCAAIGVPDErsgEAVKLFVVARDPGLSV 519
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
271-608 |
8.76e-21 |
|
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341292 [Multi-domain] Cd Length: 333 Bit Score: 94.26 E-value: 8.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 271 DMAIVMYTSGSTGRPKGVMMHHSNLI-AGMtgQCERIPGLGPKDTYIGYLPLAHVLELTAEISCFTYGCR---IGYSSPL 346
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIaANL--QLIHAMGLTEADVYLNMLPLFHIAGLNLALATFHAGGAnvvMEKFDPA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 347 TLSD--QSSKIkkgskgdctvlkpTLMAAVPEIMDRIyknvmskvqemnyvqktlfkigydykLEQIKK-GYDAPlcnli 423
Cdd:cd17637 79 EALEliEEEKV-------------TLMGSFPPILSNL--------------------------LDAAEKsGVDLS----- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 424 lfkKVKALLGGNVrmmlsggaplsPQT----HRFMNVCFCCpigqGYGLTESCGAGTVTEVTDyTTGRVGAPLICCEIKL 499
Cdd:cd17637 115 ---SLRHVLGLDA-----------PETiqrfEETTGATFWS----LYGQTETSGLVTLSPYRE-RPGSAGRPGPLVRVRI 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 500 KDwqeggytVHDKPNPR---GEIVIGGQNISMGYFKNEEKTAEDYcvdENGqrWFCTGDIGEFHPDGCLQIIDRK--KDL 574
Cdd:cd17637 176 VD-------DNDRPVPAgetGEIVVRGPLVFQGYWNLPELTAYTF---RNG--WHHTGDLGRFDEDGYLWYAGRKpeKEL 243
|
330 340 350
....*....|....*....|....*....|....
gi 1720435377 575 VKlQAGEYVSLGKVEAALKNCPLIDNICAFAKSD 608
Cdd:cd17637 244 IK-PGGENVYPAEVEKVILEHPAIAEVCVIGVPD 276
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
125-592 |
1.53e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 95.78 E-value: 1.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 125 WINYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEwMIAAQtcfkYNFP-----LVTLYATLGREAVVHGLNESEAS 199
Cdd:PRK08162 43 RRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPA-MVEAH----FGVPmagavLNTLNTRLDAASIAFMLRHGEAK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 200 YLITSVELLESkLKAALVDINcVKHIIYVDnktINRAEYPEGLEIHSMqSVEELGAK--PEnlsVPPSRPTPSDMAIVM- 276
Cdd:PRK08162 118 VLIVDTEFAEV-AREALALLP-GPKPLVID---VDDPEYPGGRFIGAL-DYEAFLASgdPD---FAWTLPADEWDAIALn 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 277 YTSGSTGRPKGVMMHH--------SNLIAGmtgqceripGLGPKDTYIGYLPLAHvleltaeiscftygCRiGYSSPLTL 348
Cdd:PRK08162 189 YTSGTTGNPKGVVYHHrgaylnalSNILAW---------GMPKHPVYLWTLPMFH--------------CN-GWCFPWTV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 349 sdqsskikkgskgdctvlkpTLMAAVpeimdriykNV-MSKVQEmnyvqKTLFKIGYDyklEQIKKGYDAP-----LCNL 422
Cdd:PRK08162 245 --------------------AARAGT---------NVcLRKVDP-----KLIFDLIRE---HGVTHYCGAPivlsaLINA 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 423 IlfKKVKALLGGNVRMMLSGGAPLSPQTHRFMNVCFCcpIGQGYGLTESCGAGTV----TEVTDYTTGRvgapliccEIK 498
Cdd:PRK08162 288 P--AEWRAGIDHPVHAMVAGAAPPAAVIAKMEEIGFD--LTHVYGLTETYGPATVcawqPEWDALPLDE--------RAQ 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 499 LKDWQ------EGGYTVHD----KPNPR-----GEIVIGGqNISM-GYFKNEEKTAEDYcvdENGqrWFCTGDIGEFHPD 562
Cdd:PRK08162 356 LKARQgvryplQEGVTVLDpdtmQPVPAdgetiGEIMFRG-NIVMkGYLKNPKATEEAF---AGG--WFHTGDLAVLHPD 429
|
490 500 510
....*....|....*....|....*....|
gi 1720435377 563 GCLQIIDRKKDLVkLQAGEYVSLGKVEAAL 592
Cdd:PRK08162 430 GYIKIKDRSKDII-ISGGENISSIEVEDVL 458
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
126-696 |
1.54e-20 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 97.72 E-value: 1.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 126 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASYLITSV 205
Cdd:PRK12316 4577 LTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALLLTQS 4656
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 206 ELLEsklkaalvdincvkhiiyvdnktinRAEYPEGLEIHSMQSVEELGAKPENlsVPPSRPTPSDMAIVMYTSGSTGRP 285
Cdd:PRK12316 4657 HLLQ-------------------------RLPIPDGLASLALDRDEDWEGFPAH--DPAVRLHPDNLAYVIYTSGSTGRP 4709
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 286 KGVMMHHSNLIAGMTGQCERiPGLGPKDTYIGYLPLAhvLELTAEiscftygcriGYSSPLTlsdqsskikkgsKGDCTV 365
Cdd:PRK12316 4710 KGVAVSHGSLVNHLHATGER-YELTPDDRVLQFMSFS--FDGSHE----------GLYHPLI------------NGASVV 4764
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 366 LKPTlMAAVPEimdRIYKNVM-SKVQEMNYVQKTLFKIgydykLEQIKKGYDAPLCNLILFKKvKALLGGNVRMMLSGGA 444
Cdd:PRK12316 4765 IRDD-SLWDPE---RLYAEIHeHRVTVLVFPPVYLQQL-----AEHAERDGEPPSLRVYCFGG-EAVAQASYDLAWRALK 4834
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 445 PLSpqthrfmnvcfccpIGQGYGLTESCGAGTVTEVTDYTT-GRVGAPlicceIKLKDWQEGGYTVHDKPNPR-----GE 518
Cdd:PRK12316 4835 PVY--------------LFNGYGPTETTVTVLLWKARDGDAcGAAYMP-----IGTPLGNRSGYVLDGQLNPLpvgvaGE 4895
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 519 IVIGGQNISMGYFKNEEKTAEDYC---VDENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVSLGKVEAALKNC 595
Cdd:PRK12316 4896 LYLGGEGVARGYLERPALTAERFVpdpFGAPGGRLYRTGDLARYRADGVIDYLGRVDHQVKIR-GFRIELGEIEARLREH 4974
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 596 PLIDNICAFAK--SDQSYVISFVVPNQKKLTllaqqkgvegswvdicNNPAMEAEILKEIREAANAmKLERFEIPIK-VR 672
Cdd:PRK12316 4975 PAVREAVVIAQegAVGKQLVGYVVPQDPALA----------------DADEAQAELRDELKAALRE-RLPEYMVPAHlVF 5037
|
570 580
....*....|....*....|....
gi 1720435377 673 LSPEPWTPETglvtdafKLKRKEL 696
Cdd:PRK12316 5038 LARMPLTPNG-------KLDRKAL 5054
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
126-620 |
1.75e-20 |
|
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: 95.51 E-value: 1.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 126 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASYLITSV 205
Cdd:cd05959 30 LTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVVSG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 206 ELLESKLKAALVDINCVKHIIYVDnktinraeyPEGLEIHSMQSVEELGAKPENLsvPPSRPTPSDMAIVMYTSGSTGRP 285
Cdd:cd05959 110 ELAPVLAAALTKSEHTLVVLIVSG---------GAGPEAGALLLAELVAAEAEQL--KPAATHADDPAFWLYSSGSTGRP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 286 KGVMMHHSNLIAGMTGQCERIPGLGPKDTYigylplahvleLTAEISCFTYGCRIGYSSPLtlsdqsskikkgSKGDCTV 365
Cdd:cd05959 179 KGVVHLHADIYWTAELYARNVLGIREDDVC-----------FSAAKLFFAYGLGNSLTFPL------------SVGATTV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 366 LKPTLMAAvpeimDRIYKnvmskvqEMNYVQKTLFkigydYKLEQIkkgYDAPLCNlilfKKVKALLGGNVRMMLSGGAP 445
Cdd:cd05959 236 LMPERPTP-----AAVFK-------RIRRYRPTVF-----FGVPTL---YAAMLAA----PNLPSRDLSSLRLCVSAGEA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 446 LSPQTHRFMNVCFCCPIGQGYGLTE------SCGAGTVtevtdyTTGRVGAPLICCEIKLKDwqEGGYTVHD-KPnprGE 518
Cdd:cd05959 292 LPAEVGERWKARFGLDILDGIGSTEmlhiflSNRPGRV------RYGTTGKPVPGYEVELRD--EDGGDVADgEP---GE 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 519 IVIGGQNISMGYFKNEEKTAEDYcvdeNGQrWFCTGDIGEFHPDGCLQIIDRKKDLVKLqAGEYVSLGKVEAALKNCPLI 598
Cdd:cd05959 361 LYVRGPSSATMYWNNRDKTRDTF----QGE-WTRTGDKYVRDDDGFYTYAGRADDMLKV-SGIWVSPFEVESALVQHPAV 434
|
490 500
....*....|....*....|....*
gi 1720435377 599 DNICAFAKSDQSYVI---SFVVPNQ 620
Cdd:cd05959 435 LEAAVVGVEDEDGLTkpkAFVVLRP 459
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
252-617 |
3.08e-20 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 95.05 E-value: 3.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 252 ELGAKPENlSVPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCE-RIPGLG--PKDTYIGYLPLAHVLELT 328
Cdd:PLN02246 162 ELTQADEN-ELPEVEISPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVAQQVDgENPNLYfhSDDVILCVLPMFHIYSLN 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 329 AEISCftyGCRIGysspltlsdqsSKIKKGSKGDCTVL-------KPTLMAAVPEIMDRIYKNVMSKvqemnyvqktlfk 401
Cdd:PLN02246 241 SVLLC---GLRVG-----------AAILIMPKFEIGALleliqrhKVTIAPFVPPIVLAIAKSPVVE------------- 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 402 igyDYKLEQIkkgydaplcnlilfkkvkallggnvRMMLSGGAPLSPQTH-----RFMNVCfccpIGQGYGLTEscgAGT 476
Cdd:PLN02246 294 ---KYDLSSI-------------------------RMVLSGAAPLGKELEdafraKLPNAV----LGQGYGMTE---AGP 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 477 V--------TEVTDYTTGRVGAPLICCEIKLKDWQEGGYTVHDKPnprGEIVIGGQNISMGYFKNEEKTAEdyCVDENGq 548
Cdd:PLN02246 339 VlamclafaKEPFPVKSGSCGTVVRNAELKIVDPETGASLPRNQP---GEICIRGPQIMKGYLNDPEATAN--TIDKDG- 412
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720435377 549 rWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVSLGKVEAALKNCPLIDNICAFAKSDQS---YVISFVV 617
Cdd:PLN02246 413 -WLHTGDIGYIDDDDELFIVDRLKELIKYK-GFQVAPAELEALLISHPSIADAAVVPMKDEVageVPVAFVV 482
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
269-621 |
4.30e-20 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 93.69 E-value: 4.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 269 PSDMAIVMYTSGSTGRPKGVMMHHSNlIAGMTGQCERIPGLGPKdtyigylPLAHVleltaEISCFTYGCRIG-YSSPLT 347
Cdd:cd17650 92 PEDLAYVIYTSGTTGKPKGVMVEHRN-VAHAAHAWRREYELDSF-------PVRLL-----QMASFSFDVFAGdFARSLL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 348 LSDQSSKIKKGSKGDCTVL-------KPTLMAAVPE----IMDRIYKNvmskvqEMNYVQKTLFKIGYDykleqikkgyd 416
Cdd:cd17650 159 NGGTLVICPDEVKLDPAALydlilksRITLMESTPAlirpVMAYVYRN------GLDLSAMRLLIVGSD----------- 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 417 apLCNLILFKKVKALLGGNVRMMLSggaplspqthrfmnvcfccpigqgYGLTESCGAGTVTEVTDYTTGR-----VGAP 491
Cdd:cd17650 222 --GCKAQDFKTLAARFGQGMRIINS------------------------YGVTEATIDSTYYEEGRDPLGDsanvpIGRP 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 492 LICCEIKLKDwqeggytVHDKPNP---RGEIVIGGQNISMGYFKNEEKTAEDYCVD--ENGQRWFCTGDIGEFHPDGCLQ 566
Cdd:cd17650 276 LPNTAMYVLD-------ERLQPQPvgvAGELYIGGAGVARGYLNRPELTAERFVENpfAPGERMYRTGDLARWRADGNVE 348
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720435377 567 IIDRKKDLVKLQaGEYVSLGKVEAALKNCPLIDNICAFAKSD---QSYVISFVVPNQK 621
Cdd:cd17650 349 LLGRVDHQVKIR-GFRIELGEIESQLARHPAIDEAVVAVREDkggEARLCAYVVAAAT 405
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
125-656 |
9.37e-20 |
|
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: 93.46 E-value: 9.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 125 WINYLEVNCRVNNFGSGLTALGlKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLN---ESEASYL 201
Cdd:cd05931 24 TLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPPTPGRHAERLAAilaDAGPRVV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 202 ITSvelleSKLKAALVDIncvkhiiyvdnktinrAEYPEGLEIHSMQSVEELGAKPENLSVPPSrPTPSDMAIVMYTSGS 281
Cdd:cd05931 103 LTT-----AAALAAVRAF----------------AASRPAAGTPRLLVVDLLPDTSAADWPPPS-PDPDDIAYLQYTSGS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 282 TGRPKGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLAH----VLELTAEISCftyGCRIGYSSPLT-LSDQSSKIK 356
Cdd:cd05931 161 TGTPKGVVVTHRNLLANVRQIRRAY-GLDPGDVVVSWLPLYHdmglIGGLLTPLYS---GGPSVLMSPAAfLRRPLRWLR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 357 KGSKGDCTvlkptlMAAVPeimdriyknvmskvqemNYvqktlfkiGYDYkleQIKKGYDAPLCNLILfkkvkallgGNV 436
Cdd:cd05931 237 LISRYRAT------ISAAP-----------------NF--------AYDL---CVRRVRDEDLEGLDL---------SSW 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 437 RMMLSGGAPLSPQT-HRFMNV---------CFCCpigqGYGLTESCGAgtVtevtdyTTGRVGAPLICCEIkLKDWQEGG 506
Cdd:cd05931 274 RVALNGAEPVRPATlRRFAEAfapfgfrpeAFRP----SYGLAEATLF--V------SGGPPGTGPVVLRV-DRDALAGR 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 507 YTVHDKPNPR--------------------------------GEIVIGGQNISMGYFKNEEKTAEDYCV----DENGqrW 550
Cdd:cd05931 341 AVAVAADDPAarelvscgrplpdqevrivdpetgrelpdgevGEIWVRGPSVASGYWGRPEATAETFGAlaatDEGG--W 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 551 FCTGDIGEFHpDGCLQIIDRKKDLVkLQAGEYVSLGKVEAALKNCPlidnicafAKSDQSYVISFVVPNQKKLTLLAQQK 630
Cdd:cd05931 419 LRTGDLGFLH-DGELYITGRLKDLI-IVRGRNHYPQDIEATAEEAH--------PALRPGCVAAFSVPDDGEERLVVVAE 488
|
570 580
....*....|....*....|....*.
gi 1720435377 631 gVEGSWVdicnnPAMEAEILKEIREA 656
Cdd:cd05931 489 -VERGAD-----PADLAAIAAAIRAA 508
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
268-619 |
1.22e-19 |
|
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: 92.61 E-value: 1.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 268 TPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLA---HVLE-LTAEISCftyGCRIGYS 343
Cdd:cd05918 104 SPSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRAL-GLTSESRVLQFASYTfdvSILEiFTTLAAG---GCLCIPS 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 344 SPLTLSDQSSKIKKgSKGDCTVLKPTLMA-----AVPEImdriyknvmskvqemnyvqKTLFKIGydyklEQIKKgydap 418
Cdd:cd05918 180 EEDRLNDLAGFINR-LRVTWAFLTPSVARlldpeDVPSL-------------------RTLVLGG-----EALTQ----- 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 419 lcnlilfkKVKALLGGNVRMMlsggaplspqthrfmnvcfccpigQGYGLTESCGAGTVTEVTDYTTGR-VGAPL--ICC 495
Cdd:cd05918 230 --------SDVDTWADRVRLI------------------------NAYGPAECTIAATVSPVVPSTDPRnIGRPLgaTCW 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 496 EIKLKDwqeggytvHDKPNPR---GEIVIGGQNISMGYFKNEEKTAEDY---------CVDENGQRWFCTGDIGEFHPDG 563
Cdd:cd05918 278 VVDPDN--------HDRLVPIgavGELLIEGPILARGYLNDPEKTAAAFiedpawlkqEGSGRGRRLYRTGDLVRYNPDG 349
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720435377 564 CLQIIDRKKDLVKLQaGEYVSLGKVEAALKNC-PLIDNICAFA-----KSDQSYVISFVVPN 619
Cdd:cd05918 350 SLEYVGRKDTQVKIR-GQRVELGEIEHHLRQSlPGAKEVVVEVvkpkdGSSSPQLVAFVVLD 410
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
269-668 |
2.94e-19 |
|
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: 90.03 E-value: 2.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 269 PSDMAIVMYTSGSTGRPKGVMMHHSNLI--AGMTGqcERIpGLGPKDTYIGYLPLAHVLELT-AEISCFTYGCRIGYSSP 345
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNIVnnGYFIG--ERL-GLTEQDRLCIPVPLFHCFGSVlGVLACLTHGATMVFPSP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 346 LTlsDQSSKIKKGSKGDCTVLK--PTLMAAVpeimdriyknvmskvqemnyvqktlfkigydykLEQIKKG-YDAplcnl 422
Cdd:cd05917 78 SF--DPLAVLEAIEKEKCTALHgvPTMFIAE---------------------------------LEHPDFDkFDL----- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 423 ilfkkvkallgGNVRMMLSGGAPLSPQT-HRFMNVCFCCPIGQGYGLTESCGAGTVTEVTDYTTGR---VGAPLICCEIK 498
Cdd:cd05917 118 -----------SSLRTGIMAGAPCPPELmKRVIEVMNMKDVTIAYGMTETSPVSTQTRTDDSIEKRvntVGRIMPHTEAK 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 499 LKDwQEGGYTVhdKPNPRGEIVIGGQNISMGYFKNEEKTAEdyCVDenGQRWFCTGDIGEFHPDGCLQIIDRKKDLVkLQ 578
Cdd:cd05917 187 IVD-PEGGIVP--PVGVPGELCIRGYSVMKGYWNDPEKTAE--AID--GDGWLHTGDLAVMDEDGYCRIVGRIKDMI-IR 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 579 AGEYVSLGKVEAALKNCPLIDNICAFAKSDQSYvisfvvpnqkkltllaqqkGVE-GSWVDICNNPAMEAEilkEIREAA 657
Cdd:cd05917 259 GGENIYPREIEEFLHTHPKVSDVQVVGVPDERY-------------------GEEvCAWIRLKEGAELTEE---DIKAYC 316
|
410
....*....|.
gi 1720435377 658 NAmKLERFEIP 668
Cdd:cd05917 317 KG-KIAHYKVP 326
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
126-598 |
4.12e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 91.10 E-value: 4.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 126 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRA---EWMIAAQTCFKYNFPLvtlYATLGREAVVHGLNESEASYLI 202
Cdd:PRK06145 28 ISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAaflELAFAASYLGAVFLPI---NYRLAADEVAYILGDAGAKLLL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 203 TSVELlesKLKAALVDINCVkhiiyvdnktinraeypegLEIHSMQSVEELGAKpeNLSVPPSRPT-PSDMAIVMYTSGS 281
Cdd:PRK06145 105 VDEEF---DAIVALETPKIV-------------------IDAAAQADSRRLAQG--GLEIPPQAAVaPTDLVRLMYTSGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 282 TGRPKGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLAHV--LELTAeISCFTYGCRIGYSSPLTLSDQSSKIKKgS 359
Cdd:PRK06145 161 TDRPKGVMHSYGNLHWKSIDHVIAL-GLTASERLLVVGPLYHVgaFDLPG-IAVLWVGGTLRIHREFDPEAVLAAIER-H 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 360 KGDCTVLKPTLMAAVPEIMDRiyknvmskvqemnyvqktlfkigYDYKLeqikkgydaplcnlilfkkvkallgGNVRMM 439
Cdd:PRK06145 238 RLTCAWMAPVMLSRVLTVPDR-----------------------DRFDL-------------------------DSLAWC 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 440 LSGGAPLSPQTHR-----FMNVCFCcpigQGYGLTESCGAGTVTEVTDY--TTGRVGAPLICCEIKLKDwQEGGYTvhdK 512
Cdd:PRK06145 270 IGGGEKTPESRIRdftrvFTRARYI----DAYGLTETCSGDTLMEAGREieKIGSTGRALAHVEIRIAD-GAGRWL---P 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 513 PNPRGEIVIGGQNISMGYFKNEEKTAEDYCVDengqrWFCTGDIGEFHPDGCLQIIDRKKDLVkLQAGEYVSLGKVEAAL 592
Cdd:PRK06145 342 PNMKGEICMRGPKVTKGYWKDPEKTAEAFYGD-----WFRSGDVGYLDEEGFLYLTDRKKDMI-ISGGENIASSEVERVI 415
|
....*.
gi 1720435377 593 KNCPLI 598
Cdd:PRK06145 416 YELPEV 421
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
142-575 |
5.82e-19 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 90.71 E-value: 5.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 142 LTALGLKPKNTIAIFCETRAEWMIaaqtcfkynfplvtLY-ATLGREAVVHGLN----ESEASYLITSVEllesklkAAL 216
Cdd:PRK07514 45 LVALGVKPGDRVAVQVEKSPEALA--------------LYlATLRAGAVFLPLNtaytLAELDYFIGDAE-------PAL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 217 VdincvkhiiYVDNKtiNRAEYPEGLEIHSMQSVEELGAKPEN------LSVPPSRPT----PSDMAIVMYTSGSTGRPK 286
Cdd:PRK07514 104 V---------VCDPA--NFAWLSKIAAAAGAPHVETLDADGTGslleaaAAAPDDFETvprgADDLAAILYTSGTTGRSK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 287 GVMMHHSNLIA-GMTgqCERIPGLGPKDTYIGYLPLAHVLELTAEISCftygcrigyssplTLSDQSSKIkkgskgdctv 365
Cdd:PRK07514 173 GAMLSHGNLLSnALT--LVDYWRFTPDDVLIHALPIFHTHGLFVATNV-------------ALLAGASMI---------- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 366 LKPTL-MAAVPEIMDRiyKNVMSKVqemnyvqKTLfkigYDYKLEQikKGYDAPLCnlilfkkvkallgGNVRMMLSGGA 444
Cdd:PRK07514 228 FLPKFdPDAVLALMPR--ATVMMGV-------PTF----YTRLLQE--PRLTREAA-------------AHMRLFISGSA 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 445 PLSPQTHRfmnvCFCCPIGQG----YGLTESC--------G---AGTVtevtdyttgrvGAPLICCEIKLKDWQEGgytv 509
Cdd:PRK07514 280 PLLAETHR----EFQERTGHAilerYGMTETNmntsnpydGerrAGTV-----------GFPLPGVSLRVTDPETG---- 340
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720435377 510 hdKPNPRGE---IVIGGQNISMGYFKNEEKTAEDYCVDenGqrWFCTGDIGEFHPDGCLQIIDRKKDLV 575
Cdd:PRK07514 341 --AELPPGEigmIEVKGPNVFKGYWRMPEKTAEEFRAD--G--FFITGDLGKIDERGYVHIVGRGKDLI 403
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
251-620 |
6.09e-19 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 91.06 E-value: 6.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 251 EELGAKPENLSVPPSRPtpSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTG----QCERIPGLGPKDTYIGYLPLAHVLE 326
Cdd:PLN02574 181 ELIKEDFDFVPKPVIKQ--DDVAAIMYSSGTTGASKGVVLTHRNLIAMVELfvrfEASQYEYPGSDNVYLAALPMFHIYG 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 327 LtaeiSCFTYGcrigyssplTLSDQSSKIkkgskgdctvlkptlmaavpeIMDRIYKNVMSKVQEMNYVqkTLFKIgydy 406
Cdd:PLN02574 259 L----SLFVVG---------LLSLGSTIV---------------------VMRRFDASDMVKVIDRFKV--THFPV---- 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 407 kleqikkgydAPLCNLILFKKVKALLGG---NVRMMLSGGAPLSPQT-HRFMNVCFCCPIGQGYGLTESCGAGT----VT 478
Cdd:PLN02574 299 ----------VPPILMALTKKAKGVCGEvlkSLKQVSCGAAPLSGKFiQDFVQTLPHVDFIQGYGMTESTAVGTrgfnTE 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 479 EVTDYTTGRVGAPLIccEIKLKDWQEGGYTvhdKPNPRGEIVIGGQNISMGYFKNEEKTaeDYCVDENGqrWFCTGDIGE 558
Cdd:PLN02574 369 KLSKYSSVGLLAPNM--QAKVVDWSTGCLL---PPGNCGELWIQGPGVMKGYLNNPKAT--QSTIDKDG--WLRTGDIAY 439
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720435377 559 FHPDGCLQIIDRKKDLVKLQaGEYVSLGKVEAALKNCPLIDNICAFAKSDQ---SYVISFVVPNQ 620
Cdd:PLN02574 440 FDEDGYLYIVDRLKEIIKYK-GFQIAPADLEAVLISHPEIIDAAVTAVPDKecgEIPVAFVVRRQ 503
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
184-575 |
7.43e-19 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 90.78 E-value: 7.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 184 LGREAVVHGLNESEASYLITSVELLES----KLKAALVDINCVKHIIYVDnktINRAEYPEGLEIHSMQSV--------- 250
Cdd:PRK07529 116 LEPEQIAELLRAAGAKVLVTLGPFPGTdiwqKVAEVLAALPELRTVVEVD---LARYLPGPKRLAVPLIRRkaharildf 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 251 -EELGAKPENLSVPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAgMTGQCERIPGLGPKDTYIGYLPLAHVLELTA 329
Cdd:PRK07529 193 dAELARQPGDRLFSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVA-NAWLGALLLGLGPGDTVFCGLPLFHVNALLV 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 330 EI-SCFTYGCRIGYSSPLtlsdqsskikkGSKGdctvlkPTLMAAVPEIMDRIYKNVMSKVqemnyvqKTLfkigYDYKL 408
Cdd:PRK07529 272 TGlAPLARGAHVVLATPQ-----------GYRG------PGVIANFWKIVERYRINFLSGV-------PTV----YAALL 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 409 EQIKKGYDAplcnlilfkkvkallgGNVRMMLSGGAPLSPQTHR-FMNVCfCCPIGQGYGLTESCGAGTVTEV-TDYTTG 486
Cdd:PRK07529 324 QVPVDGHDI----------------SSLRYALCGAAPLPVEVFRrFEAAT-GVRIVEGYGLTEATCVSSVNPPdGERRIG 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 487 RVGAPLICCEIKLKDWQEGGYTVHD-KPNPRGEIVIGGQNISMGYFknEEKTAEDYCVDEngqRWFCTGDIGEFHPDGCL 565
Cdd:PRK07529 387 SVGLRLPYQRVRVVILDDAGRYLRDcAVDEVGVLCIAGPNVFSGYL--EAAHNKGLWLED---GWLNTGDLGRIDADGYF 461
|
410
....*....|
gi 1720435377 566 QIIDRKKDLV 575
Cdd:PRK07529 462 WLTGRAKDLI 471
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
77-575 |
8.84e-19 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 90.26 E-value: 8.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 77 DTLDKLFDHAVAKFGKKDSLGTREilseenemqpngkvfkklilGNYKWiNYLEVNCRVNNFGSGLTALGLKPKNTIAIF 156
Cdd:PRK08315 16 QTIGQLLDRTAARYPDREALVYRD--------------------QGLRW-TYREFNEEVDALAKGLLALGIEKGDRVGIW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 157 CETRAEWmiaaqtcfkynfpLVTLYAT--LG----------REA-VVHGLNESEASYLITS--------VELLES----- 210
Cdd:PRK08315 75 APNVPEW-------------VLTQFATakIGailvtinpayRLSeLEYALNQSGCKALIAAdgfkdsdyVAMLYElapel 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 211 ------KLKAALVDinCVKHIIYV-DNKTINRAEYPEGLEIHSMQSVEELGAKPENLSvppsrptPSDmAIVM-YTSGST 282
Cdd:PRK08315 142 atcepgQLQSARLP--ELRRVIFLgDEKHPGMLNFDELLALGRAVDDAELAARQATLD-------PDD-PINIqYTSGTT 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 283 GRPKGVMMHHSNLI--AGMTGQCERipgLGPKDTYIGYLPLAH----VLeltAEISCFTYGCRIGYssPLTLSDQSSKIK 356
Cdd:PRK08315 212 GFPKGATLTHRNILnnGYFIGEAMK---LTEEDRLCIPVPLYHcfgmVL---GNLACVTHGATMVY--PGEGFDPLATLA 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 357 KGSKGDCTVLK--PTL----------------------MAAVP---EIMdriyKNVMSKvqeMNYVQKTLfkigydykle 409
Cdd:PRK08315 284 AVEEERCTALYgvPTMfiaeldhpdfarfdlsslrtgiMAGSPcpiEVM----KRVIDK---MHMSEVTI---------- 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 410 qikkgydaplcnlilfkkvkallggnvrmmlsggaplspqthrfmnvcfccpigqGYGLTESCGAGTVTEVTD-----YT 484
Cdd:PRK08315 347 -------------------------------------------------------AYGMTETSPVSTQTRTDDplekrVT 371
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 485 TgrVGAPLICCEIKLKDwQEGGYTVhdKPNPRGEIVIGGQNISMGYFKNEEKTAEdyCVDENGqrWFCTGDIGEFHPDGC 564
Cdd:PRK08315 372 T--VGRALPHLEVKIVD-PETGETV--PRGEQGELCTRGYSVMKGYWNDPEKTAE--AIDADG--WMHTGDLAVMDEEGY 442
|
570
....*....|.
gi 1720435377 565 LQIIDRKKDLV 575
Cdd:PRK08315 443 VNIVGRIKDMI 453
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
268-628 |
1.33e-18 |
|
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: 89.29 E-value: 1.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 268 TPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGqCERIPGLGPKDTYIgylpLAH-------VLELtaeISCFTYGCRI 340
Cdd:cd17643 91 DPDDLAYVIYTSGSTGRPKGVVVSHANVLALFAA-TQRWFGFNEDDVWT----LFHsyafdfsVWEI---WGALLHGGRL 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 341 gysspltlsdqsskikkgskgdctVLKPTLMAAVPEIMDRIYKNvmSKVQEMNYVqKTLFkigydYKLEQIKKGYDAPLC 420
Cdd:cd17643 163 ------------------------VVVPYEVARSPEDFARLLRD--EGVTVLNQT-PSAF-----YQLVEAADRDGRDPL 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 421 NLilfkkvkallggnvRMMLSGGAPLSPQTHRFMNVCFCCPIGQ---GYGLTESCGAGTVTEVTDYTTGRVGAPLICCEI 497
Cdd:cd17643 211 AL--------------RYVIFGGEALEAAMLRPWAGRFGLDRPQlvnMYGITETTVHVTFRPLDAADLPAAAASPIGRPL 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 498 klkdwqeGGYTVH-----DKPNPR---GEIVIGGQNISMGYFKNEEKTAEDYCVDEN---GQRWFCTGDIGEFHPDGCLQ 566
Cdd:cd17643 277 -------PGLRVYvldadGRPVPPgvvGELYVSGAGVARGYLGRPELTAERFVANPFggpGSRMYRTGDLARRLPDGELE 349
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720435377 567 IIDRKKDLVKLQaGEYVSLGKVEAALKNCPLIDNICAFAKSD---QSYVISFVVPNQKKLTLLAQ 628
Cdd:cd17643 350 YLGRADEQVKIR-GFRIELGEIEAALATHPSVRDAAVIVREDepgDTRLVAYVVADDGAAADIAE 413
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
134-608 |
1.79e-18 |
|
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: 88.65 E-value: 1.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 134 RVNNFGSGLTALGLKPKNTIAI-------FCETRAEWMIAAQTCFKYnfpLVTLYATLgREAVVHGLNESEASYLITSVE 206
Cdd:cd05922 2 GVSAAASALLEAGGVRGERVVLilpnrftYIELSFAVAYAGGRLGLV---FVPLNPTL-KESVLRYLVADAGGRIVLADA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 207 LLESKLKAALVDincvkhiiYVDNKTINRAEypegleihsmqsveelGAKPENLSVPPSRPTPSDMAIVMYTSGSTGRPK 286
Cdd:cd05922 78 GAADRLRDALPA--------SPDPGTVLDAD----------------GIRAARASAPAHEVSHEDLALLLYTSGSTGSPK 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 287 GVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLAHVLELTAEISCFTYGCRI----GYSSPLTLSDqsskikkgskgD 362
Cdd:cd05922 134 LVRLSHQNLLANARSIAEYL-GITADDRALTVLPLSYDYGLSVLNTHLLRGATLvltnDGVLDDAFWE-----------D 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 363 CTVLKPTLMAAVP---EIMDRiyknvmskvqemnyvqktlfkIGYDykleqikkgyDAPLCNLilfkkvkallggnvRMM 439
Cdd:cd05922 202 LREHGATGLAGVPstyAMLTR---------------------LGFD----------PAKLPSL--------------RYL 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 440 LSGGAPLSPQT-HRFmnvcfcCPIGQG------YGLTEsCGAGTVT---EVTDYTTGRVGAPLICCEIKLKDwQEGGYTv 509
Cdd:cd05922 237 TQAGGRLPQETiARL------RELLPGaqvyvmYGQTE-ATRRMTYlppERILEKPGSIGLAIPGGEFEILD-DDGTPT- 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 510 hdKPNPRGEIVIGGQNISMGYFKNEEKTAEDycVDENGQRWfcTGDIGEFHPDGCLQIIDRKKDLVKLqAGEYVSLGKVE 589
Cdd:cd05922 308 --PPGEPGEIVHRGPNVMKGYWNDPPYRRKE--GRGGGVLH--TGDLARRDEDGFLFIVGRRDRMIKL-FGNRISPTEIE 380
|
490
....*....|....*....
gi 1720435377 590 AALKNCPLIDNICAFAKSD 608
Cdd:cd05922 381 AAARSIGLIIEAAAVGLPD 399
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
271-596 |
2.16e-18 |
|
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.
Pssm-ID: 341293 [Multi-domain] Cd Length: 330 Bit Score: 86.79 E-value: 2.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 271 DMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCErIPGLGPKDTYIGYLPLAHvleltaeiscfTYGCRIGYSSPLTlsd 350
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWAD-CADLTEDDRYLIINPFFH-----------TFGYKAGIVACLL--- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 351 qsskikKGSkgdcTVLkPTLMAAVPEIMDRIYKNVMSKVQEMNYVQKTLFKIGY--DYKLEQIKKGYD-APLCNLILFKK 427
Cdd:cd17638 66 ------TGA----TVV-PVAVFDVDAILEAIERERITVLPGPPTLFQSLLDHPGrkKFDLSSLRAAVTgAATVPVELVRR 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 428 VKALLGgnvrmmlsggaplspqthrFMNVCfccpigQGYGLTEsCGAGTVTEVTDYTT---GRVGAPLICCEIKLKDwqe 504
Cdd:cd17638 135 MRSELG-------------------FETVL------TAYGLTE-AGVATMCRPGDDAEtvaTTCGRACPGFEVRIAD--- 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 505 ggytvhdkpnpRGEIVIGGQNISMGYFKNEEKTAEdyCVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVkLQAGEYVS 584
Cdd:cd17638 186 -----------DGEVLVRGYNVMQGYLDDPEATAE--AIDADG--WLHTGDVGELDERGYLRITDRLKDMY-IVGGFNVY 249
|
330
....*....|..
gi 1720435377 585 LGKVEAALKNCP 596
Cdd:cd17638 250 PAEVEGALAEHP 261
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
101-605 |
3.25e-18 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 88.66 E-value: 3.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 101 ILSEENEMQPNgkvfKKLILGNYKWINYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAE---------WMIAAQTcf 171
Cdd:PRK06155 26 MLARQAERYPD----RPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEfldvflgcaWLGAIAV-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 172 kynfPLVTLYATLGREavvHGLNESEASYLITSVELLESkLKAALVDINCVKHIIYVDNKTINRAeyPEGLEIHSMqsve 251
Cdd:PRK06155 100 ----PINTALRGPQLE---HILRNSGARLLVVEAALLAA-LEAADPGDLPLPAVWLLDAPASVSV--PAGWSTAPL---- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 252 elgaKPENLSVPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNL-IAG-MTGqceRIPGLGPKDTYIGYLPLAHVLELTA 329
Cdd:PRK06155 166 ----PPLDAPAPAAAVQPGDTAAILYTSGTTGPSKGVCCPHAQFyWWGrNSA---EDLEIGADDVLYTTLPLFHTNALNA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 330 EISCFTYGCRIgysspltlsdqsskikkgskgdctVLKPTLMAAvpEIMDRIYKNvmskvqemnyvQKTLFkigydYKLe 409
Cdd:PRK06155 239 FFQALLAGATY------------------------VLEPRFSAS--GFWPAVRRH-----------GATVT-----YLL- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 410 qikkGYDAPlcnlILFKKVK--ALLGGNVRMMLSGGAPlsPQTHRFMNVCFCCPIGQGYGLTES---CGaGTVTEVTDYT 484
Cdd:PRK06155 276 ----GAMVS----ILLSQPAreSDRAHRVRVALGPGVP--AALHAAFRERFGVDLLDGYGSTETnfvIA-VTHGSQRPGS 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 485 TGRVgAPLIccEIKLKDwqeggytVHDKPNPR---GEIVIGGQN---ISMGYFKNEEKTAEDYcvdenGQRWFCTGDIGE 558
Cdd:PRK06155 345 MGRL-APGF--EARVVD-------EHDQELPDgepGELLLRADEpfaFATGYFGMPEKTVEAW-----RNLWFHTGDRVV 409
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1720435377 559 FHPDGCLQIIDRKKDLVKLQaGEYVSLGKVEAALKNCPLIDNICAFA 605
Cdd:PRK06155 410 RDADGWFRFVDRIKDAIRRR-GENISSFEVEQVLLSHPAVAAAAVFP 455
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
233-620 |
6.09e-18 |
|
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: 87.72 E-value: 6.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 233 INRAEYPEGLEIHSMQSVEELGAKPENLSVPPSRPTpsDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCeRIPGLGPK 312
Cdd:cd05906 132 FAGLETLSGLPGIRVLSIEELLDTAADHDLPQSRPD--DLALLMLTSGSTGFPKAVPLTHRNILARSAGKI-QHNGLTPQ 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 313 DTYIGYLPLAHVLELT-AEISCFTYGCR-IGYSSPLTLSDqsskikkgskgdctvlkPTLMAavpEIMDRiyknvmskvq 390
Cdd:cd05906 209 DVFLNWVPLDHVGGLVeLHLRAVYLGCQqVHVPTEEILAD-----------------PLRWL---DLIDR---------- 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 391 emnyvqktlFKIGYDYkleqikkgydAP--LCNLIL-----FKKVKALLgGNVRMMLSGGAPLSPQTHRFM--------- 454
Cdd:cd05906 259 ---------YRVTITW----------APnfAFALLNdlleeIEDGTWDL-SSLRYLVNAGEAVVAKTIRRLlrllepygl 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 455 --NVcfccpIGQGYGLTESCgAGTVTEVTDYTTGR--------VGAPLICCEIKLKDwqeggytVHDKPNPRGEI---VI 521
Cdd:cd05906 319 ppDA-----IRPAFGMTETC-SGVIYSRSFPTYDHsqalefvsLGRPIPGVSMRIVD-------DEGQLLPEGEVgrlQV 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 522 GGQNISMGYFKNEEKTAEDYCVDEngqrWFCTGDIGEFHpDGCLQIIDRKKDLVKLQAGEYvSLGKVEAALKNCPLIDN- 600
Cdd:cd05906 386 RGPVVTKGYYNNPEANAEAFTEDG----WFRTGDLGFLD-NGNLTITGRTKDTIIVNGVNY-YSHEIEAAVEEVPGVEPs 459
|
410 420
....*....|....*....|....*.
gi 1720435377 601 -ICAFAKSDQS-----YVIsFVVPNQ 620
Cdd:cd05906 460 fTAAFAVRDPGaeteeLAI-FFVPEY 484
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
261-618 |
6.86e-18 |
|
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: 87.33 E-value: 6.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 261 SVPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPgLGPKDTYIGYLPLA---HVLELTAEISCftyG 337
Cdd:cd17646 129 TPPLVPPRPDNLAYVIYTSGSTGRPKGVMVTHAGIVNRLLWMQDEYP-LGPGDRVLQKTPLSfdvSVWELFWPLVA---G 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 338 CRIGYSSPLTLSDqsskikkgskgdctvlkptlMAAVPEIMDRiyknvmSKVQEMNYVQKTLfkigyDYKLEQIKKGYDA 417
Cdd:cd17646 205 ARLVVARPGGHRD--------------------PAYLAALIRE------HGVTTCHFVPSML-----RVFLAEPAAGSCA 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 418 PLcnlilfkkvkallggnvRMMLSGGAPLSPQT-HRFMNVcFCCPIGQGYGLTEscgagTVTEVTDYT-TGRVGAPLIcc 495
Cdd:cd17646 254 SL-----------------RRVFCSGEALPPELaARFLAL-PGAELHNLYGPTE-----AAIDVTHWPvRGPAETPSV-- 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 496 EIKLKDWQEGGYTVHDKPNPR-----GEIVIGGQNISMGYFKNEEKTAEDYCVD--ENGQRWFCTGDIGEFHPDGCLQII 568
Cdd:cd17646 309 PIGRPVPNTRLYVLDDALRPVpvgvpGELYLGGVQLARGYLGRPALTAERFVPDpfGPGSRMYRTGDLARWRPDGALEFL 388
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1720435377 569 DRKKDLVKLQaGEYVSLGKVEAALKNCPLIDNICAFAKSDQS---YVISFVVP 618
Cdd:cd17646 389 GRSDDQVKIR-GFRVEPGEIEAALAAHPAVTHAVVVARAAPAgaaRLVGYVVP 440
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
126-620 |
7.24e-18 |
|
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: 87.20 E-value: 7.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 126 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASYLITSV 205
Cdd:TIGR02262 31 LSYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLGAIRAGIVPVALNTLLTADDYAYMLEDSRARVVFVSG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 206 ELLESkLKAALVDINCVKHIIYVdnktiNRAEYPEgleihsMQSVEELGAKPENLSVPPSRPtpSDMAIVMYTSGSTGRP 285
Cdd:TIGR02262 111 ALLPV-IKAALGKSPHLEHRVVV-----GRPEAGE------VQLAELLATESEQFKPAATQA--DDPAFWLYSSGSTGMP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 286 KGVMMHHSNLIAGMTGQCERIPGLGPKDTYigylplahvleLTAEISCFTYGCRIGYSSPLTLsdqsskikkgskGDCTV 365
Cdd:TIGR02262 177 KGVVHTHSNPYWTAELYARNTLGIREDDVC-----------FSAAKLFFAYGLGNALTFPMSV------------GATTV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 366 lkptLMAAVPeIMDRIYKnvmskvqEMNYVQKTLFKigydykleQIKKGYDAPLCNlilfKKVKALLGGNVRMMLSGGAP 445
Cdd:TIGR02262 234 ----LMGERP-TPDAVFD-------RLRRHQPTIFY--------GVPTLYAAMLAD----PNLPSEDQVRLRLCTSAGEA 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 446 LSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDwqEGGYTVHDkpNPRGEIVIGGQN 525
Cdd:TIGR02262 290 LPAEVGQRWQARFGVDIVDGIGSTEMLHIFLSNLPGDVRYGTSGKPVPGYRLRLVG--DGGQDVAD--GEPGELLISGPS 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 526 ISMGYFKNEEKTAEDYcvdeNGQrWFCTGDIGEFHPDGCLQIIDRKKDLVKLqAGEYVSLGKVEAALKNCPLIDNICAFA 605
Cdd:TIGR02262 366 SATMYWNNRAKSRDTF----QGE-WTRSGDKYVRNDDGSYTYAGRTDDMLKV-SGIYVSPFEIESALIQHPAVLEAAVVG 439
|
490
....*....|....*...
gi 1720435377 606 KSDQSYVI---SFVVPNQ 620
Cdd:TIGR02262 440 VADEDGLIkpkAFVVLRP 457
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
126-593 |
8.02e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 87.25 E-value: 8.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 126 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTL-YATLGREaVVHGLNESEASYLITS 204
Cdd:PRK07798 29 LTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVnYRYVEDE-LRYLLDDSDAVALVYE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 205 VELLEsKLKAALVDINCVKHIIYVDNKTINrAEYPEGLEIHSMQSveelGAKPENLSVPPSrptPSDMaIVMYTSGSTGR 284
Cdd:PRK07798 108 REFAP-RVAEVLPRLPKLRTLVVVEDGSGN-DLLPGAVDYEDALA----AGSPERDFGERS---PDDL-YLLYTGGTTGM 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 285 PKGVMMHHSNLiagmtgqceRIPGLGPKDTYIGylPLAHVLELTAEISCFTYGCRIGYSSPL--------TLSDQSSkik 356
Cdd:PRK07798 178 PKGVMWRQEDI---------FRVLLGGRDFATG--EPIEDEEELAKRAAAGPGMRRFPAPPLmhgagqwaAFAALFS--- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 357 kgskGDCTVLKPTLMAAVPEIMDRIYKNvmsKVQEMnyvqktlFKIGydykleqikkgyDA---PLcnlilfkkVKALLG 433
Cdd:PRK07798 244 ----GQTVVLLPDVRFDADEVWRTIERE---KVNVI-------TIVG------------DAmarPL--------LDALEA 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 434 GN------VRMMLSGGAPLSPQTHR-----FMNVCfccpIGQGYGLTES--CGAGTVTEVTDYTTG-RVGAPLICCEIkl 499
Cdd:PRK07798 290 RGpydlssLFAIASGGALFSPSVKEallelLPNVV----LTDSIGSSETgfGGSGTVAKGAVHTGGpRFTIGPRTVVL-- 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 500 kdwQEGGYTVHDKPNPRGEIVIGGqNISMGYFKNEEKTAEDYCVdENGQRWFCTGDIGEFHPDGCLQIIDRkKDLVKLQA 579
Cdd:PRK07798 364 ---DEDGNPVEPGSGEIGWIARRG-HIPLGYYKDPEKTAETFPT-IDGVRYAIPGDRARVEADGTITLLGR-GSVCINTG 437
|
490
....*....|....
gi 1720435377 580 GEYVSLGKVEAALK 593
Cdd:PRK07798 438 GEKVFPEEVEEALK 451
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
263-620 |
1.60e-17 |
|
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: 86.24 E-value: 1.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 263 PPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPgLGPKDTYIGYLPL---AHVLELtaeiscFTYGCr 339
Cdd:cd17651 129 PDPALDADDLAYVIYTSGSTGRPKGVVMPHRSLANLVAWQARASS-LGPGARTLQFAGLgfdVSVQEI------FSTLC- 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 340 igysspltlsdqsskikkgsKGDCTVLKP--------TLMAAVPEimdriyknvmskvqemnyvqktlfkigydYKLEQI 411
Cdd:cd17651 201 --------------------AGATLVLPPeevrtdppALAAWLDE-----------------------------QRISRV 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 412 kkgyDAP---LCNLILFKKVKALLGGNVRMMLSGGAPLS--------PQTHRFMNVCFccpigqGYGLTESCGAgTVTEV 480
Cdd:cd17651 232 ----FLPtvaLRALAEHGRPLGVRLAALRYLLTGGEQLVltedlrefCAGLPGLRLHN------HYGPTETHVV-TALSL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 481 TDYTTGR-----VGAPLICCEIKLKDwqeggytVHDKPNPR---GEIVIGGQNISMGYFKNEEKTAEDYCVDE--NGQRW 550
Cdd:cd17651 301 PGDPAAWpapppIGRPIDNTRVYVLD-------AALRPVPPgvpGELYIGGAGLARGYLNRPELTAERFVPDPfvPGARM 373
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720435377 551 FCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVSLGKVEAALKNCPLIDNICAFAKSDQS---YVISFVVPNQ 620
Cdd:cd17651 374 YRTGDLARWLPDGELEFLGRADDQVKIR-GFRIELGEIEAALARHPGVREAVVLAREDRPgekRLVAYVVGDP 445
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
267-618 |
1.70e-17 |
|
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: 85.44 E-value: 1.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 267 PTPSDMAIVMYTSGSTGRPKGVMMHHSNLI-------AGMTgqceripgLGPKDTyigylpLAHVLELTAEISCFTYGCR 339
Cdd:cd17653 102 DSPDDLAYIIFTSGSTGIPKGVMVPHRGVLnyvsqppARLD--------VGPGSR------VAQVLSIAFDACIGEIFST 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 340 IGYSSPLTLSDQSSKIKKGSKG-DCTVLKPTLMAAVPeimdriyknvmskvqemnyvqktlfkigydykleqiKKGYDap 418
Cdd:cd17653 168 LCNGGTLVLADPSDPFAHVARTvDALMSTPSILSTLS------------------------------------PQDFP-- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 419 lcnlilfkkvkallggNVRMMLSGGAPLSP-------QTHRFMNvcfccpigqGYGLTESCGAGTVTEVTDYTTGRVGAP 491
Cdd:cd17653 210 ----------------NLKTIFLGGEAVPPslldrwsPGRRLYN---------AYGPTECTISSTMTELLPGQPVTIGKP 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 492 LICCEIKLKDWQEggytvhdKPNP---RGEIVIGGQNISMGYFKNEEKTAEDYCVD--ENGQRWFCTGDIGEFHPDGCLQ 566
Cdd:cd17653 265 IPNSTCYILDADL-------QPVPegvVGEICISGVQVARGYLGNPALTASKFVPDpfWPGSRMYRTGDYGRWTEDGGLE 337
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1720435377 567 IIDRKKDLVKLQaGEYVSLGKVEA-ALKNCPLIDNICAFAKSDQsyVISFVVP 618
Cdd:cd17653 338 FLGREDNQVKVR-GFRINLEEIEEvVLQSQPEVTQAAAIVVNGR--LVAFVTP 387
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
270-609 |
2.15e-17 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 86.19 E-value: 2.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 270 SDMAIVMYTSGSTGRPKGVMMHHSNLIAGMtgqCERIPGLGP----KDTYIGYLPLAHVLELTAeISCFTYgcrigyssp 345
Cdd:PLN02330 184 TDLCALPFSSGTTGISKGVMLTHRNLVANL---CSSLFSVGPemigQVVTLGLIPFFHIYGITG-ICCATL--------- 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 346 ltlsDQSSKIKKGSKGDCTVLKPTLMAA-------VPEIMDRIYKNVMskVQEmnyvqktlfkigydYKLEQIKkgydap 418
Cdd:PLN02330 251 ----RNKGKVVVMSRFELRTFLNALITQevsfapiVPPIILNLVKNPI--VEE--------------FDLSKLK------ 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 419 lcnlilfkkvkallggnVRMMLSGGAPLSPQ-----THRFMNVcfccPIGQGYGLTE-SCGagTVTEvTDYTTGR----- 487
Cdd:PLN02330 305 -----------------LQAIMTAAAPLAPElltafEAKFPGV----QVQEAYGLTEhSCI--TLTH-GDPEKGHgiakk 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 488 --VGAPLICCEIKLKDWQEGGYTVHDKPnprGEIVIGGQNISMGYFKNEEKTAEdyCVDENGqrWFCTGDIGEFHPDGCL 565
Cdd:PLN02330 361 nsVGFILPNLEVKFIDPDTGRSLPKNTP---GELCVRSQCVMQGYYNNKEETDR--TIDEDG--WLHTGDIGYIDDDGDI 433
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1720435377 566 QIIDRKKDLVKLQaGEYVSLGKVEAALKNCPLIDNICAFAKSDQ 609
Cdd:PLN02330 434 FIVDRIKELIKYK-GFQVAPAELEAILLTHPSVEDAAVVPLPDE 476
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
128-596 |
2.72e-17 |
|
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: 85.33 E-value: 2.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 128 YLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEwMIAAQtcfkynfpLVTLYAtlgreavvhGlneseASYLITSVEL 207
Cdd:cd12117 25 YAELNERANRLARRLRAAGVGPGDVVGVLAERSPE-LVVAL--------LAVLKA---------G-----AAYVPLDPEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 208 LESKLKAALVDINCVkhIIYVDNKTINRAEYPEGLEIHsmqsVEELGAKPEnlSVPPSRPTPSDMAIVMYTSGSTGRPKG 287
Cdd:cd12117 82 PAERLAFMLADAGAK--VLLTDRSLAGRAGGLEVAVVI----DEALDAGPA--GNPAVPVSPDDLAYVMYTSGSTGRPKG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 288 VMMHHSNLIAGMTGQCERipGLGPKDTYIGYLPL---AHVLELtaeiscftYGCRIgysspltlsdqsskikkgSKGDCT 364
Cdd:cd12117 154 VAVTHRGVVRLVKNTNYV--TLGPDDRVLQTSPLafdASTFEI--------WGALL------------------NGARLV 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 365 VLKPTLMAAVPEIMDRIYKNVMSkvqemnyvqkTLFKIgydykleqikkgydAPLCNLILFKKVKALLGgnVRMMLSGGA 444
Cdd:cd12117 206 LAPKGTLLDPDALGALIAEEGVT----------VLWLT--------------AALFNQLADEDPECFAG--LRELLTGGE 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 445 PLSPQ-THRFMNVCFCCPIGQGYGLTESCGAGTVTEVT--DYTTGRV--GAPLicceiklkdwqeGGYTV-----HDKPN 514
Cdd:cd12117 260 VVSPPhVRRVLAACPGLRLVNGYGPTENTTFTTSHVVTelDEVAGSIpiGRPI------------ANTRVyvldeDGRPV 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 515 PR---GEIVIGGQNISMGYFKNEEKTAEDYCVD--ENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVSLGKVE 589
Cdd:cd12117 328 PPgvpGELYVGGDGLALGYLNRPALTAERFVADpfGPGERLYRTGDLARWLPDGRLEFLGRIDDQVKIR-GFRIELGEIE 406
|
....*..
gi 1720435377 590 AALKNCP 596
Cdd:cd12117 407 AALRAHP 413
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
122-621 |
2.90e-17 |
|
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: 85.22 E-value: 2.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 122 NYKWiNYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASYL 201
Cdd:cd17656 11 NQKL-TYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRVV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 202 ITSVELlESKLKaalvdincvkhiiyvDNKTINRAEYPegleIHSMQSVEELGAKPENlsvppsrptpSDMAIVMYTSGS 281
Cdd:cd17656 90 LTQRHL-KSKLS---------------FNKSTILLEDP----SISQEDTSNIDYINNS----------DDLLYIIYTSGT 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 282 TGRPKGVMMHHSNLIAGMtgQCERipglgpkdTYIGYLPLAHVLELTAeiscftygcrigYSSPLTLSDQSSKIKKGskG 361
Cdd:cd17656 140 TGKPKGVQLEHKNMVNLL--HFER--------EKTNINFSDKVLQFAT------------CSFDVCYQEIFSTLLSG--G 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 362 DCTVLKPTLMAAVPEIMDRIYKNVMSKVQEMNYVQKTLFKigydykleqiKKGYDAPLcnlilFKKVKALLGGNVRMMLS 441
Cdd:cd17656 196 TLYIIREETKRDVEQLFDLVKRHNIEVVFLPVAFLKFIFS----------EREFINRF-----PTCVKHIITAGEQLVIT 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 442 ggaplspQTHRFMNVCFCCPIGQGYGLTEScgagtvTEVTDYTTGR---------VGAPLICCEIKLKDWQEggytvhdK 512
Cdd:cd17656 261 -------NEFKEMLHEHNVHLHNHYGPSET------HVVTTYTINPeaeipelppIGKPISNTWIYILDQEQ-------Q 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 513 PNPRG---EIVIGGQNISMGYFKNEEKTAEDYCVD--ENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVSLGK 587
Cdd:cd17656 321 LQPQGivgELYISGASVARGYLNRQELTAEKFFPDpfDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIR-GYRIELGE 399
|
490 500 510
....*....|....*....|....*....|....*..
gi 1720435377 588 VEAALKNCPLIDNICAFAKSD---QSYVISFVVPNQK 621
Cdd:cd17656 400 IEAQLLNHPGVSEAVVLDKADdkgEKYLCAYFVMEQE 436
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
249-711 |
4.02e-17 |
|
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: 85.18 E-value: 4.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 249 SVEELGAKPENLSVPPSRP--TPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPGLGPKD-TYIGYLPLAHvl 325
Cdd:cd05921 142 SFAELAATPPTAAVDAAFAavGPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEPpVLVDWLPWNH-- 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 326 eltaeiscfTYGCRIGYSspLTLSDQSS-KIKKGskgdctvlKP------TLMAAVPEIMDRIYKNVmskvqemnyvqkt 398
Cdd:cd05921 220 ---------TFGGNHNFN--LVLYNGGTlYIDDG--------KPmpggfeETLRNLREISPTVYFNV------------- 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 399 lfKIGYDYKLEQIKKgyDAPLCNLiLFKkvkallggNVRMMLSGGAPLSPQT-------------HRFmnvcfccPIGQG 465
Cdd:cd05921 268 --PAGWEMLVAALEK--DEALRRR-FFK--------RLKLMFYAGAGLSQDVwdrlqalavatvgERI-------PMMAG 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 466 YGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLkdwqeggYTVHDKPnprgEIVIGGQNISMGYFKNEEKTAEDYcvDE 545
Cdd:cd05921 328 LGATETAPTATFTHWPTERSGLIGLPAPGTELKL-------VPSGGKY----EVRVKGPNVTPGYWRQPELTAQAF--DE 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 546 NGqrWFCTGDIGEF----HPDGCLQIIDRKKDLVKLQAGEYVSLGKVEAALKNC--PLIDNIcAFAKSDQSYVISFVVPN 619
Cdd:cd05921 395 EG--FYCLGDAAKLadpdDPAKGLVFDGRVAEDFKLASGTWVSVGPLRARAVAAcaPLVHDA-VVAGEDRAEVGALVFPD 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 620 QKKLTLLAQqkgvegswvdicNNPAMEAEILK--EIREAANAMkLERFE--------IPIKVRLSPEPWTPETGLVTDAF 689
Cdd:cd05921 472 LLACRRLVG------------LQEASDAEVLRhaKVRAAFRDR-LAALNgeatgsssRIARALLLDEPPSIDKGEITDKG 538
|
490 500
....*....|....*....|..
gi 1720435377 690 KLKRKELKNHYLKDIERMYGGK 711
Cdd:cd05921 539 YINQRAVLERRAALVERLYADT 560
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
271-618 |
4.49e-17 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 84.94 E-value: 4.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 271 DMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLAHVLELTAEI-SCFTYGCRI-----GYSS 344
Cdd:PRK05852 177 DDAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGY-RLSPRDATVAVMPLYHGHGLIAALlATLASGGAVllparGRFS 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 345 PLTLSDqsskikkgskgDCTVLKPTLMAAVPeimdriyknvmskvqemnyvqkTLFKIGYDYKLEQIKKGYDAPLcnlil 424
Cdd:PRK05852 256 AHTFWD-----------DIKAVGATWYTAVP----------------------TIHQILLERAATEPSGRKPAAL----- 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 425 fkkvkallggnvRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVTEVTDY--------TTGRVG---APLI 493
Cdd:PRK05852 298 ------------RFIRSCSAPLTAETAQALQTEFAAPVVCAFGMTEATHQVTTTQIEGIgqtenpvvSTGLVGrstGAQI 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 494 ccEIKLKDWQEGGytvhdkPNPRGEIVIGGQNISMGYFKNEEKTAEDYCvdeNGqrWFCTGDIGEFHPDGCLQIIDRKKD 573
Cdd:PRK05852 366 --RIVGSDGLPLP------AGAVGEVWLRGTTVVRGYLGDPTITAANFT---DG--WLRTGDLGSLSAAGDLSIRGRIKE 432
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1720435377 574 LVKlQAGEYVSLGKVEAALKNCPLIDNICAFAKSDQSY---VISFVVP 618
Cdd:PRK05852 433 LIN-RGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYgeaVAAVIVP 479
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
255-624 |
9.82e-17 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 83.92 E-value: 9.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 255 AKPENLSVPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTgQCE-------RIPGLGPKDTYIGYLPLAHVLEL 327
Cdd:PRK07059 189 AEGARQTFKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVL-QMEawlqpafEKKPRPDQLNFVCALPLYHIFAL 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 328 TAeisCFTYGCRIGYSSPLTLS--DQSSKIKKGSKgdctvLKPTLMAAVpeimdriyknvmskvqemnyvqKTLfkigyd 405
Cdd:PRK07059 268 TV---CGLLGMRTGGRNILIPNprDIPGFIKELKK-----YQVHIFPAV----------------------NTL------ 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 406 ykleqikkgYDAPLCN----LILFKKVKALLGGnvrmmlsGGAPLSPQTHRFMNVCfCCPIGQGYGLTESCGAGTV--TE 479
Cdd:PRK07059 312 ---------YNALLNNpdfdKLDFSKLIVANGG-------GMAVQRPVAERWLEMT-GCPITEGYGLSETSPVATCnpVD 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 480 VTDYTtGRVGAPLICCEIKLKDwqEGGYTVhdKPNPRGEIVIGGQNISMGYFKNEEKTAEdyCVDENGqrWFCTGDIGEF 559
Cdd:PRK07059 375 ATEFS-GTIGLPLPSTEVSIRD--DDGNDL--PLGEPGEICIRGPQVMAGYWNRPDETAK--VMTADG--FFRTGDVGVM 445
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720435377 560 HPDGCLQIIDRKKDLVkLQAGEYVSLGKVEAALKNCPLIDNICAFAKSDQ---SYVISFVVPNQKKLT 624
Cdd:PRK07059 446 DERGYTKIVDRKKDMI-LVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEhsgEAVKLFVVKKDPALT 512
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
270-697 |
1.44e-16 |
|
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.
Pssm-ID: 341276 [Multi-domain] Cd Length: 428 Bit Score: 82.77 E-value: 1.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 270 SDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGqCERIPGLGPKDTYigylplahvleLTAEISCFTYGCRIGYSSPLTLS 349
Cdd:cd05972 81 EDPALIYFTSGTTGLPKGVLHTHSYPLGHIPT-AAYWLGLRPDDIH-----------WNIADPGWAKGAWSSFFGPWLLG 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 350 dqsskikkgskgdCTVLKPTLMAAVPEimdRIYKnVMSKvqemnyvqktlfkigydyklEQIKKGYDAPlcnlILFKKVK 429
Cdd:cd05972 149 -------------ATVFVYEGPRFDAE---RILE-LLER--------------------YGVTSFCGPP----TAYRMLI 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 430 ALLG-----GNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDwQE 504
Cdd:cd05972 188 KQDLssykfSHLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDVAIID-DD 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 505 GGYTvhdKPNPRGEIVIGGQNISM--GYFKNEEKTAEDYCVDengqrWFCTGDIGEFHPDGCLQIIDRKKDLVKlQAGEY 582
Cdd:cd05972 267 GREL---PPGEEGDIAIKLPPPGLflGYVGDPEKTEASIRGD-----YYLTGDRAYRDEDGYFWFVGRADDIIK-SSGYR 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 583 VSLGKVEAALKNCPLIDNICAFAKSDQSY---VISFVVpnqkkltllaQQKGVEGSwvdicnnPAMEAEILKEIREaana 659
Cdd:cd05972 338 IGPFEVESALLEHPAVAEAAVVGSPDPVRgevVKAFVV----------LTSGYEPS-------EELAEELQGHVKK---- 396
|
410 420 430
....*....|....*....|....*....|....*....
gi 1720435377 660 mKLERFEIPIKVRLSPE-PWTPeTGlvtdafKLKRKELK 697
Cdd:cd05972 397 -VLAPYKYPREIEFVEElPKTI-SG------KIRRVELR 427
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
126-618 |
2.15e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 84.24 E-value: 2.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 126 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASYLITsv 205
Cdd:PRK12316 3083 LSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLS-- 3160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 206 ellESKLKAALVDincvkhiiYVDNKTINRAeyPEGLEIHSmqsveelgakpenlsvPPSRPTPSDMAIVMYTSGSTGRP 285
Cdd:PRK12316 3161 ---QSHLRLPLAQ--------GVQVLDLDRG--DENYAEAN----------------PAIRTMPENLAYVIYTSGSTGKP 3211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 286 KGVMMHHSNLI--AGMTGQCEripGLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSSPLTLSDQsskikkgskgdc 363
Cdd:PRK12316 3212 KGVGIRHSALSnhLCWMQQAY---GLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDP------------ 3276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 364 tvlkptlmAAVPEIMDRIYKNVMSKVQEMNYVqktlfkigydykleqikkgydaplcnliLFKKVKALLGGNVRMMLSGG 443
Cdd:PRK12316 3277 --------ALLVELINSEGVDVLHAYPSMLQA----------------------------FLEEEDAHRCTSLKRIVCGG 3320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 444 APLSPQTHRFMNVCFccPIGQGYGLTESCGAGTVTEVTDYTTGR--VGAPLICCEIKLKDwqeggytVHDKPNPRG---E 518
Cdd:PRK12316 3321 EALPADLQQQVFAGL--PLYNLYGPTEATITVTHWQCVEEGKDAvpIGRPIANRACYILD-------GSLEPVPVGalgE 3391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 519 IVIGGQNISMGYFKNEEKTAEDYCVD--ENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVSLGKVEAALKNCP 596
Cdd:PRK12316 3392 LYLGGEGLARGYHNRPGLTAERFVPDpfVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIR-GFRIELGEIEARLLEHP 3470
|
490 500
....*....|....*....|..
gi 1720435377 597 LIDNICAFAKSDQSyVISFVVP 618
Cdd:PRK12316 3471 WVREAVVLAVDGRQ-LVAYVVP 3491
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
126-618 |
2.51e-16 |
|
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: 82.10 E-value: 2.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 126 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASYLITsv 205
Cdd:cd17644 26 LTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDPNYPQERLTYILEDAQISVLLT-- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 206 ellesklkaalvdincvkhiiyvdnktinraeypegleihsmqsveelgaKPENLsvppsrptpsdmAIVMYTSGSTGRP 285
Cdd:cd17644 104 --------------------------------------------------QPENL------------AYVIYTSGSTGKP 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 286 KGVMMHHSNLIAGMTGQCERIpGLGPKDtyigylplaHVLELtaeiSCFTYGCRIGYSSPLTLSdqsskikkgskGDCTV 365
Cdd:cd17644 122 KGVMIEHQSLVNLSHGLIKEY-GITSSD---------RVLQF----ASIAFDVAAEEIYVTLLS-----------GATLV 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 366 LKPTLMAAVPEIMdriyknvMSKVQEMnyvQKTLFKIGYDYKLEQIKKGydaplcnlilfKKVKALLGGNVRMMLSGGAP 445
Cdd:cd17644 177 LRPEEMRSSLEDF-------VQYIQQW---QLTVLSLPPAYWHLLVLEL-----------LLSTIDLPSSLRLVIVGGEA 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 446 LSPQTH-----------RFMNVcfccpigqgYGLTESCGAGTVTEVTDYTTGR-----VGAPLICCEIKLKDwqeggytV 509
Cdd:cd17644 236 VQPELVrqwqknvgnfiQLINV---------YGPTEATIAATVCRLTQLTERNitsvpIGRPIANTQVYILD-------E 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 510 HDKPNP---RGEIVIGGQNISMGYFKNEEKTAEDYCVD----ENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEY 582
Cdd:cd17644 300 NLQPVPvgvPGELHIGGVGLARGYLNRPELTAEKFISHpfnsSESERLYKTGDLARYLPDGNIEYLGRIDNQVKIR-GFR 378
|
490 500 510
....*....|....*....|....*....|....*....
gi 1720435377 583 VSLGKVEAALKNCPLIDNICAFAKSDQS---YVISFVVP 618
Cdd:cd17644 379 IELGEIEAVLSQHNDVKTAVVIVREDQPgnkRLVAYIVP 417
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
248-598 |
3.51e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 81.78 E-value: 3.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 248 QSVEELGAKPENlSVPPSRPTpsdmaIVMYTSGSTGRPKGVMMHHSNLIA-----GMTGQceripgLGPKDTYIGYLPLA 322
Cdd:PRK09088 119 ASADALEPADTP-SIPPERVS-----LILFTSGTSGQPKGVMLSERNLQQtahnfGVLGR------VDAHSSFLCDAPMF 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 323 HVLELTAEI-SCFTYGCRI----GYSSPLTLsdqsskikkGSKGDCTvLKPTLMAAVPEIMDRIyknvmskvqemnyvqk 397
Cdd:PRK09088 187 HIIGLITSVrPVLAVGGSIlvsnGFEPKRTL---------GRLGDPA-LGITHYFCVPQMAQAF---------------- 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 398 tlfkigydykleQIKKGYDAplcnlilfkkvKALlgGNVRMMLSGGAPlSPQTHRFMNVCFCCPIGQGYGLTEscgAGTV 477
Cdd:PRK09088 241 ------------RAQPGFDA-----------AAL--RHLTALFTGGAP-HAAEDILGWLDDGIPMVDGFGMSE---AGTV 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 478 ------TEVTDYTTGRVGAPLICCEIKLKDWQEggytvHD-KPNPRGEIVIGGQNISMGYFKNEEKTAEDYcvDENGqrW 550
Cdd:PRK09088 292 fgmsvdCDVIRAKAGAAGIPTPTVQTRVVDDQG-----NDcPAGVPGELLLRGPNLSPGYWRRPQATARAF--TGDG--W 362
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1720435377 551 FCTGDIGEFHPDGCLQIIDRKKDLVkLQAGEYVSLGKVEAALKNCPLI 598
Cdd:PRK09088 363 FRTGDIARRDADGFFWVVDRKKDMF-ISGGENVYPAEIEAVLADHPGI 409
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
271-592 |
3.85e-16 |
|
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: 81.35 E-value: 3.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 271 DMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPGLGPKDTYigylplahvleLTAEISCFTYGCRIGYSSPLtlsd 350
Cdd:cd05919 92 DIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMAREALGLTPGDRV-----------FSSAKMFFGYGLGNSLWFPL---- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 351 qsskikkgSKGDCTVLKPTlmAAVPEimdriykNVMSKVQEMnyvQKTLFkigydykleqikkgYDAP--LCNLILFKKV 428
Cdd:cd05919 157 --------AVGASAVLNPG--WPTAE-------RVLATLARF---RPTVL--------------YGVPtfYANLLDSCAG 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 429 KALLGGNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDwqEGGYT 508
Cdd:cd05919 203 SPDALRSLRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVGHIFLSNRPGAWRLGSTGRPVPGYEIRLVD--EEGHT 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 509 VhdKPNPRGEIVIGGQNISMGYFKNEEKTAEDYcvdeNGQrWFCTGDIGEFHPDGCLQIIDRKKDLVKLqAGEYVSLGKV 588
Cdd:cd05919 281 I--PPGEEGDLLVRGPSAAVGYWNNPEKSRATF----NGG-WYRTGDKFCRDADGWYTHAGRADDMLKV-GGQWVSPVEV 352
|
....
gi 1720435377 589 EAAL 592
Cdd:cd05919 353 ESLI 356
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
268-697 |
5.23e-16 |
|
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: 81.26 E-value: 5.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 268 TPSDMAIVMYTSGSTGRPKGVMMHHSNLIAgmtgQCE---RIPGLGPKDTYIGYLPL---AHVLELTAEISCftygcrig 341
Cdd:cd17649 92 HPRQLAYVIYTSGSTGTPKGVAVSHGPLAA----HCQataERYGLTPGDRELQFASFnfdGAHEQLLPPLIC-------- 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 342 ysspltlsdqsskikkgskGDCTVLKPTLMAAVPEIMDRIYKNvmskvQEMNYVQktlFKIGYDYKLeqikkgydaplcn 421
Cdd:cd17649 160 -------------------GACVVLRPDELWASADELAEMVRE-----LGVTVLD---LPPAYLQQL------------- 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 422 LILFKKVKALLGGNVRMMLSGGAPLSPQTHRFMNVCFCCPIgQGYGLTESCGAGTVTEVTDYTTGR-----VGAPLicce 496
Cdd:cd17649 200 AEEADRTGDGRPPSLRLYIFGGEALSPELLRRWLKAPVRLF-NAYGPTEATVTPLVWKCEAGAARAgasmpIGRPL---- 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 497 iklkdwqeGGYTVH--DK------PNPRGEIVIGGQNISMGYFKNEEKTAEDYCVD---ENGQRWFCTGDIGEFHPDGCL 565
Cdd:cd17649 275 --------GGRSAYilDAdlnpvpVGVTGELYIGGEGLARGYLGRPELTAERFVPDpfgAPGSRLYRTGDLARWRDDGVI 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 566 QIIDRKKDLVKLQaGEYVSLGKVEAALKNCPLIDNICAFAKSDQS--YVISFVVPNQkkltllaqqkgvegswvdicnnP 643
Cdd:cd17649 347 EYLGRVDHQVKIR-GFRIELGEIEAALLEHPGVREAAVVALDGAGgkQLVAYVVLRA----------------------A 403
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1720435377 644 AMEAEILKEIReAANAMKLERFEIPIK-VRLSPEPWTPETglvtdafKLKRKELK 697
Cdd:cd17649 404 AAQPELRAQLR-TALRASLPDYMVPAHlVFLARLPLTPNG-------KLDRKALP 450
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
268-618 |
6.20e-16 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.
Pssm-ID: 341280 [Multi-domain] Cd Length: 447 Bit Score: 80.82 E-value: 6.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 268 TPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPglgpKDTyigylpLAHVLELTA---EISCF------TYGC 338
Cdd:cd12115 103 DPDDLAYVIYTSGSTGRPKGVAIEHRNAAAFLQWAAAAFS----AEE------LAGVLASTSicfDLSVFelfgplATGG 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 339 RIGY-SSPLTLSDQSSKikkgskgdCTVlkpTLMAAVPEIMDRIyknvmskvqemnyvqktlfkigydykLEQikkgyDA 417
Cdd:cd12115 173 KVVLaDNVLALPDLPAA--------AEV---TLINTVPSAAAEL--------------------------LRH-----DA 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 418 plcnlilfkkvkalLGGNVRMMLSGGAPLS----------PQTHRFMNVcfccpigqgYGLTESCGAGTVTEVTDYTTGR 487
Cdd:cd12115 211 --------------LPASVRVVNLAGEPLPrdlvqrlyarLQVERVVNL---------YGPSEDTTYSTVAPVPPGASGE 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 488 V--GAPLicceiklkdwqeGGYTV-----HDKPNP---RGEIVIGGQNISMGYFKNEEKTAEDYCVD--ENGQRWFCTGD 555
Cdd:cd12115 268 VsiGRPL------------ANTQAyvldrALQPVPlgvPGELYIGGAGVARGYLGRPGLTAERFLPDpfGPGARLYRTGD 335
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720435377 556 IGEFHPDGCLQIIDRKKDLVKLQaGEYVSLGKVEAALKNCPLIDNICAFAKSDQS---YVISFVVP 618
Cdd:cd12115 336 LVRWRPDGLLEFLGRADNQVKVR-GFRIELGEIEAALRSIPGVREAVVVAIGDAAgerRLVAYIVA 400
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
269-697 |
7.27e-16 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 81.38 E-value: 7.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 269 PSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCErIPGLGPKDTYIGYLPLAHVleltaeiscftyGcriGYSSPLTL 348
Cdd:PLN02860 171 PDDAVLICFTSGTTGRPKGVTISHSALIVQSLAKIA-IVGYGEDDVYLHTAPLCHI------------G---GLSSALAM 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 349 SdqsskikkgSKGDCTVLKPTLMA-AVPEIMDRIYKNVMSKVQEMnyvqktlfkigydykleqikkgydapLCNLILFKK 427
Cdd:PLN02860 235 L---------MVGACHVLLPKFDAkAALQAIKQHNVTSMITVPAM--------------------------MADLISLTR 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 428 VKALLGGN--VRMMLSGGAPLSPQTHRFMNVCF-CCPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPL-ICCEIKLKDWQ 503
Cdd:PLN02860 280 KSMTWKVFpsVRKILNGGGSLSSRLLPDAKKLFpNAKLFSAYGMTEACSSLTFMTLHDPTLESPKQTLqTVNQTKSSSVH 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 504 EGGYTVHDKPNPRGEIVIG-------------GQNISMGYFKNEEKTAEDyCVDENgqrWFCTGDIGEFHPDGCLQIIDR 570
Cdd:PLN02860 360 QPQGVCVGKPAPHVELKIGldessrvgriltrGPHVMLGYWGQNSETASV-LSNDG---WLDTGDIGWIDKAGNLWLIGR 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 571 KKDLVKlQAGEYVSLGKVEAALKNCP--------------LIDNICAFAKSDQSYVISFV-VPNQKKLTLLAQQkgvegs 635
Cdd:PLN02860 436 SNDRIK-TGGENVYPEEVEAVLSQHPgvasvvvvgvpdsrLTEMVVACVRLRDGWIWSDNeKENAKKNLTLSSE------ 508
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720435377 636 wvdicnnpameaeilkEIREAANAMKLERFEIP--IKVRLSPEPWTpETGlvtdafKLKRKELK 697
Cdd:PLN02860 509 ----------------TLRHHCREKNLSRFKIPklFVQWRKPFPLT-TTG------KIRRDEVR 549
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
266-624 |
7.83e-16 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 81.25 E-value: 7.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 266 RP--TPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTgQCERI--PGLGP-KDTYIGYLPLAHVLELTaeISCFTYgcri 340
Cdd:PRK08974 200 KPelVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLE-QAKAAygPLLHPgKELVVTALPLYHIFALT--VNCLLF---- 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 341 gysspltlsdqsskIKKGSKGdctvLKPTLMAAVPEIMDRIYKNVMSKVQEMNyvqkTLFKigydykleqikkgydaPLC 420
Cdd:PRK08974 273 --------------IELGGQN----LLITNPRDIPGFVKELKKYPFTAITGVN----TLFN----------------ALL 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 421 NLILFKKVKAllgGNVRMMLSGGAPL-SPQTHRFMNVCfCCPIGQGYGLTEsCG---AGTVTEVTDYTtGRVGAPLICCE 496
Cdd:PRK08974 315 NNEEFQELDF---SSLKLSVGGGMAVqQAVAERWVKLT-GQYLLEGYGLTE-CSplvSVNPYDLDYYS-GSIGLPVPSTE 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 497 IKLKDwQEGGYTVHDKPnprGEIVIGGQNISMGYFKNEEKTAEdycVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVk 576
Cdd:PRK08974 389 IKLVD-DDGNEVPPGEP---GELWVKGPQVMLGYWQRPEATDE---VIKDG--WLATGDIAVMDEEGFLRIVDRKKDMI- 458
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1720435377 577 LQAGEYVSLGKVEAALKNCPLIDNICAFAKSDQS---YVISFVVPNQKKLT 624
Cdd:PRK08974 459 LVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVsgeAVKIFVVKKDPSLT 509
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
118-700 |
1.44e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 79.98 E-value: 1.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 118 LILGNYKWiNYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESE 197
Cdd:PRK08316 30 LVFGDRSW-TYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 198 ASYLITSVELLEsKLKAALVDINCVKHIiyVDNKTINRaEYPEGleihsMQSVEELgAKPENLSVPPSRPTPSDMAIVMY 277
Cdd:PRK08316 109 ARAFLVDPALAP-TAEAALALLPVDTLI--LSLVLGGR-EAPGG-----WLDFADW-AEAGSVAEPDVELADDDLAQILY 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 278 TSGSTGRPKGVMMHHSNLIAGMTGqCERIPGLGPKDTYIGYLPLAHvlelTAEISCFTygcrigysSPLTLSDQSSKIkk 357
Cdd:PRK08316 179 TSGTESLPKGAMLTHRALIAEYVS-CIVAGDMSADDIPLHALPLYH----CAQLDVFL--------GPYLYVGATNVI-- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 358 gskgdctVLKPTLmaavPEIMDRIYKnvmskvqemnYVQKTLFK-----IG------YD-YKLEQIKKGYdaplcnlilf 425
Cdd:PRK08316 244 -------LDAPDP----ELILRTIEA----------ERITSFFApptvwISllrhpdFDtRDLSSLRKGY---------- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 426 kkvkallggnvrmmlsGGAPLSPQT------HRFMNVCF--CcpigqgYGLTESCGAGTV--TEVTDYTTGRVGAPLICC 495
Cdd:PRK08316 293 ----------------YGASIMPVEvlkelrERLPGLRFynC------YGQTEIAPLATVlgPEEHLRRPGSAGRPVLNV 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 496 EIKLKDwqEGGYTVhdKPNPRGEIVIGGQNISMGYFKNEEKTAEDYcvdENGqrWFCTGDIGEFHPDGCLQIIDRKKDLV 575
Cdd:PRK08316 351 ETRVVD--DDGNDV--APGEVGEIVHRSPQLMLGYWDDPEKTAEAF---RGG--WFHSGDLGVMDEEGYITVVDRKKDMI 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 576 KlQAGEYVSLGKVEAALKNCPLIDNICAFAKSDQSY---VISFVVPnqkkltllaqqkgVEGSWVDicnnpamEAEILKE 652
Cdd:PRK08316 422 K-TGGENVASREVEEALYTHPAVAEVAVIGLPDPKWieaVTAVVVP-------------KAGATVT-------EDELIAH 480
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 1720435377 653 IREaanamKLERFEIPIKVRLSPE-PWTPeTGlvtdafKLKRKELKNHY 700
Cdd:PRK08316 481 CRA-----RLAGFKVPKRVIFVDElPRNP-SG------KILKRELRERY 517
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
126-619 |
1.56e-15 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 81.36 E-value: 1.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 126 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASYLITSV 205
Cdd:PRK12467 1600 LTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQS 1679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 206 ELLEsklkaalvdincvkhiiyvdnktinRAEYPEGLEIHSM-QSVEELGAKPEnlSVPPSRPTPSDMAIVMYTSGSTGR 284
Cdd:PRK12467 1680 HLQA-------------------------RLPLPDGLRSLVLdQEDDWLEGYSD--SNPAVNLAPQNLAYVIYTSGSTGR 1732
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 285 PKGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLAHvleltaEISCFtygcriGYSSPLTlsdqsskikkgsKGDCT 364
Cdd:PRK12467 1733 PKGAGNRHGALVNRLCATQEAY-QLSAADVVLQFTSFAF------DVSVW------ELFWPLI------------NGARL 1787
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 365 VLKPTLMAAVPE-IMDRIYKNvmsKVQEMNYVQKTLfkigydYKLEQIKKGYDAPLcnlilfkkvkallggNVRMMLSGG 443
Cdd:PRK12467 1788 VIAPPGAHRDPEqLIQLIERQ---QVTTLHFVPSML------QQLLQMDEQVEHPL---------------SLRRVVCGG 1843
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 444 APLSPQTHR-FMNVCFCCPIGQGYGLTEscgagTVTEVTDYT------TGRVGAPLiccEIKLKDWqeGGYTVHDKPNPR 516
Cdd:PRK12467 1844 EALEVEALRpWLERLPDTGLFNLYGPTE-----TAVDVTHWTcrrkdlEGRDSVPI---GQPIANL--STYILDASLNPV 1913
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 517 -----GEIVIGGQNISMGYFKNEEKTAEDYCVD---ENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVSLGKV 588
Cdd:PRK12467 1914 pigvaGELYLGGVGLARGYLNRPALTAERFVADpfgTVGSRLYRTGDLARYRADGVIEYLGRIDHQVKIR-GFRIELGEI 1992
|
490 500 510
....*....|....*....|....*....|...
gi 1720435377 589 EAALKNCPLIDNICAFAK--SDQSYVISFVVPN 619
Cdd:PRK12467 1993 EARLREQGGVREAVVIAQdgANGKQLVAYVVPT 2025
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
126-618 |
1.77e-15 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 81.16 E-value: 1.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 126 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASYLITSV 205
Cdd:PRK12316 537 LDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQS 616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 206 ELLEsklkaaLVDINCVKHIIYVDNKTINRAEYPEGleihsmqsveelgakpenlsVPPSRPTPSDMAIVMYTSGSTGRP 285
Cdd:PRK12316 617 HLGR------KLPLAAGVQVLDLDRPAAWLEGYSEE--------------------NPGTELNPENLAYVIYTSGSTGKP 670
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 286 KGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSSPLTLSDqsskikkgskgdctv 365
Cdd:PRK12316 671 KGAGNRHRALSNRLCWMQQAY-GLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRD--------------- 734
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 366 lkptlMAAVPEIMDRIYKNVMSKVQEMnyvqktlfkigydykleqikkgydapLCNLILFKKVKALLggNVRMMLSGGAP 445
Cdd:PRK12316 735 -----PAKLVELINREGVDTLHFVPSM--------------------------LQAFLQDEDVASCT--SLRRIVCSGEA 781
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 446 LS-----------PQTHRFmNVcfccpigqgYGLTESCGAGT----VTEVTDytTGRVGAPLICCEIKLKDWQEGgytvh 510
Cdd:PRK12316 782 LPadaqeqvfaklPQAGLY-NL---------YGPTEAAIDVThwtcVEEGGD--SVPIGRPIANLACYILDANLE----- 844
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 511 dkPNP---RGEIVIGGQNISMGYFKNEEKTAEDYCVDE--NGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVSL 585
Cdd:PRK12316 845 --PVPvgvLGELYLAGRGLARGYHGRPGLTAERFVPSPfvAGERMYRTGDLARYRADGVIEYAGRIDHQVKLR-GLRIEL 921
|
490 500 510
....*....|....*....|....*....|...
gi 1720435377 586 GKVEAALKNCPLIDNICAFAKSDQSYViSFVVP 618
Cdd:PRK12316 922 GEIEARLLEHPWVREAAVLAVDGKQLV-GYVVL 953
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
249-710 |
2.66e-15 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 79.54 E-value: 2.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 249 SVEELGAKPENLSVPPS--RPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAG--MTGQCERIPGLGPKdTYIGYLPLAHV 324
Cdd:PRK08180 186 PFAALLATPPTAAVDAAhaAVGPDTIAKFLFTSGSTGLPKAVINTHRMLCANqqMLAQTFPFLAEEPP-VLVDWLPWNHT 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 325 LeltaeiscftygcriGYSSPLTLsdqsskikkgskgdctVL-----------KPTlmaavPEIMDRIYKNvmskvqeMN 393
Cdd:PRK08180 265 F---------------GGNHNLGI----------------VLynggtlyiddgKPT-----PGGFDETLRN-------LR 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 394 YVQKTLF---KIGYDYKLEQIKKgyDAPLCNLiLFKKVkallggnvRMMLSGGAPLSPQT----HRF-MNVC-----FCC 460
Cdd:PRK08180 302 EISPTVYfnvPKGWEMLVPALER--DAALRRR-FFSRL--------KLLFYAGAALSQDVwdrlDRVaEATCgerirMMT 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 461 pigqGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDwqeggytVHDKPnprgEIVIGGQNISMGYFKNEEKTAED 540
Cdd:PRK08180 371 ----GLGMTETAPSATFTTGPLSRAGNIGLPAPGCEVKLVP-------VGGKL----EVRVKGPNVTPGYWRAPELTAEA 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 541 YcvDENGqrWFCTGDIGEFH-PDgclqiiDRKKDLV---------KLQAGEYVSLG----KVEAALKncPLIDNICaFAK 606
Cdd:PRK08180 436 F--DEEG--YYRSGDAVRFVdPA------DPERGLMfdgriaedfKLSSGTWVSVGplraRAVSAGA--PLVQDVV-ITG 502
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 607 SDQSYVISFVVPNQKKLTLLAQQkGVEGSWVDICNNPAMEA---EILKEIREAA--NAMKLERfeipikVRLSPEPWTPE 681
Cdd:PRK08180 503 HDRDEIGLLVFPNLDACRRLAGL-LADASLAEVLAHPAVRAafrERLARLNAQAtgSSTRVAR------ALLLDEPPSLD 575
|
490 500 510
....*....|....*....|....*....|....*.
gi 1720435377 682 TGLVTD-------AFKLKRKELknhylkdIERMYGG 710
Cdd:PRK08180 576 AGEITDkgyinqrAVLARRAAL-------VEALYAD 604
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
277-696 |
2.68e-15 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 79.50 E-value: 2.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 277 YTSGSTGRPKGVMMHHSNLIAgMTGQCERIPGLGPKDTYIGYLPLAHvleltAEISCFTYGCRIGYSSPLTLSDQSSKIK 356
Cdd:PLN02479 202 YTSGTTASPKGVVLHHRGAYL-MALSNALIWGMNEGAVYLWTLPMFH-----CNGWCFTWTLAALCGTNICLRQVTAKAI 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 357 KGSKGDCTVlkpTLMAAVPEIMDRIYknvmskvqemnyvqktlfkigydykleqikkgyDAPLCNLILfkkvkaLLGGNV 436
Cdd:PLN02479 276 YSAIANYGV---THFCAAPVVLNTIV---------------------------------NAPKSETIL------PLPRVV 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 437 RMMLSGGAP-------LSPQTHRfmnvcfccpIGQGYGLTESCGAGTVT-------EVTDYTTGRVGAPLICCEIKLKdw 502
Cdd:PLN02479 314 HVMTAGAAPppsvlfaMSEKGFR---------VTHTYGLSETYGPSTVCawkpewdSLPPEEQARLNARQGVRYIGLE-- 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 503 qegGYTVHD----KPNPR-----GEIVIGGQNISMGYFKNEEKTAEDYcvdENGqrWFCTGDIGEFHPDGCLQIIDRKKD 573
Cdd:PLN02479 383 ---GLDVVDtktmKPVPAdgktmGEIVMRGNMVMKGYLKNPKANEEAF---ANG--WFHSGDLGVKHPDGYIEIKDRSKD 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 574 LVkLQAGEYVSLGKVEAALKNCPLIDNICAFAKSDQSYVIS---FVVPNQKkltllaqqkgvegswVDICNNPAMEAEIL 650
Cdd:PLN02479 455 II-ISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESpcaFVTLKPG---------------VDKSDEAALAEDIM 518
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1720435377 651 KEIREaanamKLERFEIPIKVRLSPEPWTPETGLVTDAFKLKRKEL 696
Cdd:PLN02479 519 KFCRE-----RLPAYWVPKSVVFGPLPKTATGKIQKHVLRAKAKEM 559
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
269-575 |
4.72e-15 |
|
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: 78.30 E-value: 4.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 269 PSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPgLGPKDTYIGYLPLAHVLELTAeiscftygcriGYSSPLTl 348
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTE-WKTKDRILSWMPLTHDMGLIA-----------FHLAPLI- 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 349 sdqsskikkgsKGDCTVLKPTLMAAVPEImdriykNVMSKVQEMNYVQKTLFKIGYDYKLEQIK--KGYDAPLcnlilfk 426
Cdd:cd05908 172 -----------AGMNQYLMPTRLFIRRPI------LWLKKASEHKATIVSSPNFGYKYFLKTLKpeKANDWDL------- 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 427 kvkallgGNVRMMLSGGAPLSPQ-THRFMNVCFCCPIGQG-----YGLTE-SCGA---------------------GTVT 478
Cdd:cd05908 228 -------SSIRMILNGAEPIDYElCHEFLDHMSKYGLKRNailpvYGLAEaSVGAslpkaqspfktitlgrrhvthGEPE 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 479 EVTD------YTTGRVGAPLICCEIKLKDWQ----EGGYTvhdkpnprGEIVIGGQNISMGYFKNEEKTAEdyCVDENGq 548
Cdd:cd05908 301 PEVDkkdsecLTFVEVGKPIDETDIRICDEDnkilPDGYI--------GHIQIRGKNVTPGYYNNPEATAK--VFTDDG- 369
|
330 340
....*....|....*....|....*..
gi 1720435377 549 rWFCTGDIGeFHPDGCLQIIDRKKDLV 575
Cdd:cd05908 370 -WLKTGDLG-FIRNGRLVITGREKDII 394
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
268-624 |
5.04e-15 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 78.21 E-value: 5.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 268 TPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPGLGPKDTYIGYLPlAHVLELTAEiscftygcrigyssPLT 347
Cdd:cd17648 92 NSTDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSLSERYFGRDNGDEAVLFFS-NYVFDFFVE--------------QMT 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 348 LSDQSskikkgskGDCTVLKPTLMAAVPeimDRIYKnVMSKvQEMNYVQKTlfkigyDYKLEQikkgYDAPLCNlilfkk 427
Cdd:cd17648 157 LALLN--------GQKLVVPPDEMRFDP---DRFYA-YINR-EKVTYLSGT------PSVLQQ----YDLARLP------ 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 428 vkallggNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTEScgagTVTE-VTDYTTGRVGAPLICCEIKLKDWqegg 506
Cdd:cd17648 208 -------HLKRVDAAGEEFTAPVFEKLRSRFAGLIINAYGPTET----TVTNhKRFFPGDQRFDKSLGRPVRNTKC---- 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 507 YTVHD--KPNP---RGEIVIGGQNISMGYFKNEEKTAEDYC----------VDENGQRWFCTGDIGEFHPDGCLQIIDRK 571
Cdd:cd17648 273 YVLNDamKRVPvgaVGELYLGGDGVARGYLNRPELTAERFLpnpfqteqerARGRNARLYKTGDLVRWLPSGELEYLGRN 352
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720435377 572 KDLVKLQaGEYVSLGKVEAALKNCPLIDNICAFAKSD--------QSYVISFVVPNQKKLT 624
Cdd:cd17648 353 DFQVKIR-GQRIEPGEVEAALASYPGVRECAVVAKEDasqaqsriQKYLVGYYLPEPGHVP 412
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
124-575 |
5.53e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 78.54 E-value: 5.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 124 KWINYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASYL-- 201
Cdd:PRK06710 48 KDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVIlc 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 202 ----------ITSVELLESKLKAALVD-INCVKHIIY--VDNKTINR-AEYPEGLEIHSMQSVEelgaKPENLSVPPSRP 267
Cdd:PRK06710 128 ldlvfprvtnVQSATKIEHVIVTRIADfLPFPKNLLYpfVQKKQSNLvVKVSESETIHLWNSVE----KEVNTGVEVPCD 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 268 TPSDMAIVMYTSGSTGRPKGVMMHHSNLIAG-MTGQCERIPGLGPKDTYIGYLPLAHVLELTAEISCftygcrigysspl 346
Cdd:PRK06710 204 PENDLALLQYTGGTTGFPKGVMLTHKNLVSNtLMGVQWLYNCKEGEEVVLGVLPFFHVYGMTAVMNL------------- 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 347 tlsdqssKIKKGSKgdctvlkptlMAAVPEI-MDRIYKNVMSKvqemnyvQKTLFKigydykleqikkgyDAPLCNLILF 425
Cdd:PRK06710 271 -------SIMQGYK----------MVLIPKFdMKMVFEAIKKH-------KVTLFP--------------GAPTIYIALL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 426 KK--VKALLGGNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTEScgaGTVTEVT----DYTTGRVGAPLICCEIKL 499
Cdd:PRK06710 313 NSplLKEYDISSIRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTES---SPVTHSNflweKRVPGSIGVPWPDTEAMI 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720435377 500 KDWQEGGYTvhdKPNPRGEIVIGGQNISMGYFKNEEKTAedyCVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLV 575
Cdd:PRK06710 390 MSLETGEAL---PPGEIGEIVVKGPQIMKGYWNKPEETA---AVLQDG--WLHTGDVGYMDEDGFFYVKDRKKDMI 457
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
263-592 |
1.02e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 77.34 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 263 PPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLAHVleltaeiscftYGCRIGY 342
Cdd:PRK07787 121 RYPEPDPDAPALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAW-QWTADDVLVHGLPLFHV-----------HGLVLGV 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 343 SSPLTLSDQSSKIKKGSK---GDCTVLKPTLMAAVPEIMDRIYKNVmskvqemnyvqktlfkigydykleqikkgyDAPl 419
Cdd:PRK07787 189 LGPLRIGNRFVHTGRPTPeayAQALSEGGTLYFGVPTVWSRIAADP------------------------------EAA- 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 420 cnlilfkkvKALlgGNVRMMLSGGAPLS-PQTHRFMNVCFCCPIgQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIK 498
Cdd:PRK07787 238 ---------RAL--RGARLLVSGSAALPvPVFDRLAALTGHRPV-ERYGMTETLITLSTRADGERRPGWVGLPLAGVETR 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 499 LKDwQEGGYTVHDkPNPRGEIVIGGQNISMGYFKNEEKTAEdyCVDENGqrWFCTGDIGEFHPDGCLQIIDRKK-DLVKl 577
Cdd:PRK07787 306 LVD-EDGGPVPHD-GETVGELQVRGPTLFDGYLNRPDATAA--AFTADG--WFRTGDVAVVDPDGMHRIVGREStDLIK- 378
|
330
....*....|....*.
gi 1720435377 578 qAGEY-VSLGKVEAAL 592
Cdd:PRK07787 379 -SGGYrIGAGEIETAL 393
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
269-610 |
1.95e-14 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 77.06 E-value: 1.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 269 PSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTgQCERIPGLGPKDTYIGYLPLAHVLELTaeISCFT---YGCRIG-YSS 344
Cdd:PRK08043 364 PEDAALILFTSGSEGHPKGVVHSHKSLLANVE-QIKTIADFTPNDRFMSALPLFHSFGLT--VGLFTpllTGAEVFlYPS 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 345 PL-------TLSDQsskikkgskgDCTVL--KPTLMAavpeimdriyknvmskvqemNYVQktlFKIGYDYkleqikkgy 415
Cdd:PRK08043 441 PLhyrivpeLVYDR----------NCTVLfgTSTFLG--------------------NYAR---FANPYDF--------- 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 416 daplcnlilfkkvkallgGNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTE-----------SCGAGTVTEVTDYT 484
Cdd:PRK08043 479 ------------------ARLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTEcapvvsinvpmAAKPGTVGRILPGM 540
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 485 TGRVgaplicceIKLKDWQEGgytvhdkpnprGEIVIGGQNISMGYFKNEE------KTAEdycvDENGQR---WFCTGD 555
Cdd:PRK08043 541 DARL--------LSVPGIEQG-----------GRLQLKGPNIMNGYLRVEKpgvlevPTAE----NARGEMergWYDTGD 597
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1720435377 556 IGEFHPDGCLQIIDRKKDLVKLqAGEYVSLGKVEA-ALKNCPLIDNiCAFAKSDQS 610
Cdd:PRK08043 598 IVRFDEQGFVQIQGRAKRFAKI-AGEMVSLEMVEQlALGVSPDKQH-ATAIKSDAS 651
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
126-620 |
2.42e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 77.51 E-value: 2.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 126 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASYLITSV 205
Cdd:PRK12467 538 LSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQS 617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 206 ELLEsklkaalvdincvkhiiyvdnktinRAEYPEGLeihSMQSVEELGAKPENLSV--PPSRPTPSDMAIVMYTSGSTG 283
Cdd:PRK12467 618 HLLA-------------------------QLPVPAGL---RSLCLDEPADLLCGYSGhnPEVALDPDNLAYVIYTSGSTG 669
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 284 RPKGVMMHHSNLiAGMTGQCERIPGLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSSPLTLSDQSSKIKKGSKGDC 363
Cdd:PRK12467 670 QPKGVAISHGAL-ANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPDCARDAEAFAALMADQGV 748
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 364 TVLKptlmaAVPeimdriyknvmSKVQEMnyvqktlfkigydykLEQIKKGYDAPLCNLIlfkkvkalLGGNVrMMLSGG 443
Cdd:PRK12467 749 TVLK-----IVP-----------SHLQAL---------------LQASRVALPRPQRALV--------CGGEA-LQVDLL 788
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 444 AP---LSPQThRFMNVcfccpigqgYGLTEscgagTVTEVTDYTTGRVGAPLICCEIKLKDWQEGGYTVHDKPNP----- 515
Cdd:PRK12467 789 ARvraLGPGA-RLINH---------YGPTE-----TTVGVSTYELSDEERDFGNVPIGQPLANLGLYILDHYLNPvpvgv 853
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 516 RGEIVIGGQNISMGYFKNEEKTAEDYCVD---ENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVSLGKVEAAL 592
Cdd:PRK12467 854 VGELYIGGAGLARGYHRRPALTAERFVPDpfgADGGRLYRTGDLARYRADGVIEYLGRMDHQVKIR-GFRIELGEIEARL 932
|
490 500 510
....*....|....*....|....*....|
gi 1720435377 593 KNCPLIDN--ICAFAKSDQSYVISFVVPNQ 620
Cdd:PRK12467 933 LAQPGVREavVLAQPGDAGLQLVAYLVPAA 962
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
126-618 |
2.50e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 77.30 E-value: 2.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 126 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASYLITSV 205
Cdd:PRK12316 2029 LSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQR 2108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 206 ELLEsklkaalvdincvkhiiyvdnktinRAEYPEGLEIHSMQSVEELGAKPEnlSVPPSRPTPSDMAIVMYTSGSTGRP 285
Cdd:PRK12316 2109 HLLE-------------------------RLPLPAGVARLPLDRDAEWADYPD--TAPAVQLAGENLAYVIYTSGSTGLP 2161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 286 KGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLAhvLELTAEiSCFTygcrigyssPLTlsdqsskikkgsKGDCTV 365
Cdd:PRK12316 2162 KGVAVSHGALVAHCQAAGERY-ELSPADCELQFMSFS--FDGAHE-QWFH---------PLL------------NGARVL 2216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 366 LKPTLMAAVPEIMDRIYKNVMSKVqemnyvqktlfkigydykleqikkgyDAPLCNLILFKKVKALLGG--NVRMMLSGG 443
Cdd:PRK12316 2217 IRDDELWDPEQLYDEMERHGVTIL--------------------------DFPPVYLQQLAEHAERDGRppAVRVYCFGG 2270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 444 ----APLSPQTHRFMNVCFccpIGQGYGLTEscgagTVTEVTDYTTGRV---GAPLICCEIKLKDwqEGGYTVHDKPNP- 515
Cdd:PRK12316 2271 eavpAASLRLAWEALRPVY---LFNGYGPTE-----AVVTPLLWKCRPQdpcGAAYVPIGRALGN--RRAYILDADLNLl 2340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 516 ----RGEIVIGGQNISMGYFKNEEKTAEDYCVD---ENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVSLGKV 588
Cdd:PRK12316 2341 apgmAGELYLGGEGLARGYLNRPGLTAERFVPDpfsASGERLYRTGDLARYRADGVVEYLGRIDHQVKIR-GFRIELGEI 2419
|
490 500 510
....*....|....*....|....*....|..
gi 1720435377 589 EAALKNCPLIDNICAFAKSDQS--YVISFVVP 618
Cdd:PRK12316 2420 EARLQAHPAVREAVVVAQDGASgkQLVAYVVP 2451
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
268-618 |
3.65e-14 |
|
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).
Pssm-ID: 341307 [Multi-domain] Cd Length: 436 Bit Score: 75.37 E-value: 3.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 268 TPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPL---AHVLELTAeisCFTYGCR--IGY 342
Cdd:cd17652 91 TPDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAAF-DVGPGSRVLQFASPsfdASVWELLM---ALLAGATlvLAP 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 343 SSPLTLSDQSSKIKKGSKGDCTVLKPTLMAAVPEimdriyknvmskvqemnyvqktlfkigydykleqikkgydaplcnl 422
Cdd:cd17652 167 AEELLPGEPLADLLREHRITHVTLPPAALAALPP---------------------------------------------- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 423 ilfkkvKALLGGnvRMMLSGGAPLSPQ-------THRFMNvcfccpigqGYGLTESCGAGTVTEV-TDYTTGRVGAPLIC 494
Cdd:cd17652 201 ------DDLPDL--RTLVVAGEACPAElvdrwapGRRMIN---------AYGPTETTVCATMAGPlPGGGVPPIGRPVPG 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 495 CEIK-LKDWQEggytvhdkPNP---RGEIVIGGQNISMGYFKNEEKTAEDYCVD---ENGQRWFCTGDIGEFHPDGCLQI 567
Cdd:cd17652 264 TRVYvLDARLR--------PVPpgvPGELYIAGAGLARGYLNRPGLTAERFVADpfgAPGSRMYRTGDLARWRADGQLEF 335
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1720435377 568 IDRKKDLVKLQaGEYVSLGKVEAALKNCPLIDNICAFAKSDQSYV---ISFVVP 618
Cdd:cd17652 336 LGRADDQVKIR-GFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDkrlVAYVVP 388
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
269-618 |
3.94e-14 |
|
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: 75.28 E-value: 3.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 269 PSDMAIVMYTSGSTGRPKGVMMHHSNLIagmtGQCEripglgpkdtyigylplahvleltAEISCFTygcrigysspLTL 348
Cdd:cd17645 103 PDDLAYVIYTSGSTGLPKGVMIEHHNLV----NLCE------------------------WHRPYFG----------VTP 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 349 SDQSSKIKkGSKGDCTVLK--PTLMA-AVPEIMDRIYKNVMSKVQEmnYVQKTLFKIGYdykleqikkgYDAPLCnlilf 425
Cdd:cd17645 145 ADKSLVYA-SFSFDASAWEifPHLTAgAALHVVPSERRLDLDALND--YFNQEGITISF----------LPTGAA----- 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 426 KKVKALLGGNVRMMLSGGAPLSpqthRFMNVCFccPIGQGYGLTESCGAGTVTEV-TDYTTGRVGAPLICCEIKL--KDW 502
Cdd:cd17645 207 EQFMQLDNQSLRVLLTGGDKLK----KIERKGY--KLVNNYGPTENTVVATSFEIdKPYANIPIGKPIDNTRVYIldEAL 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 503 QEGGYTVhdkpnpRGEIVIGGQNISMGYFKNEEKTAEDYCVD--ENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaG 580
Cdd:cd17645 281 QLQPIGV------AGELCIAGEGLARGYLNRPELTAEKFIVHpfVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIR-G 353
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1720435377 581 EYVSLGKVEAALKNCPLIDNICAFAKSD---QSYVISFVVP 618
Cdd:cd17645 354 YRIEPGEIEPFLMNHPLIELAAVLAKEDadgRKYLVAYVTA 394
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
144-608 |
1.04e-13 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 74.23 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 144 ALGLKPKNTIAIFCETRAEWMIAAqtcfkynfplvtlYATLGREAVV-------------HGLNESEASYLITSVELLEs 210
Cdd:PRK08314 55 ECGVRKGDRVLLYMQNSPQFVIAY-------------YAILRANAVVvpvnpmnreeelaHYVTDSGARVAIVGSELAP- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 211 KLKAALVDINcVKHIIYVDNKTINRAEY----PEGLEI-HSMQSVEELGAKP------ENLSVPPSRPTPSDMAIVMYTS 279
Cdd:PRK08314 121 KVAPAVGNLR-LRHVIVAQYSDYLPAEPeiavPAWLRAePPLQALAPGGVVAwkealaAGLAPPPHTAGPDDLAVLPYTS 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 280 GSTGRPKGVMMHHSNLIAGMTGQCeRIPGLGPKDTYIGYLPLAHVLeltaeiscftyGCRIGYSSPLTLsdqsskikkgs 359
Cdd:PRK08314 200 GTTGVPKGCMHTHRTVMANAVGSV-LWSNSTPESVVLAVLPLFHVT-----------GMVHSMNAPIYA----------- 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 360 kGDCTVLKPTL-MAAVPEIMDRIYKNVMSKVQEMnyVQKTLFKIGYDykleqikkGYDapLCNLilfkkvkALLGGnvrm 438
Cdd:PRK08314 257 -GATVVLMPRWdREAAARLIERYRVTHWTNIPTM--VVDFLASPGLA--------ERD--LSSL-------RYIGG---- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 439 mlsGGAPLsPQT-----HRFMNVCFCcpigQGYGLTESCGA-------------------GTVTEVTDYTTGRVGAplic 494
Cdd:PRK08314 313 ---GGAAM-PEAvaerlKELTGLDYV----EGYGLTETMAQthsnppdrpklqclgiptfGVDARVIDPETLEELP---- 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 495 ceiklkdwqeggytvhdkPNPRGEIVIGGQNISMGYFKNEEKTAEDYcVDENGQRWFCTGDIGEFHPDGCLQIIDRKKDL 574
Cdd:PRK08314 381 ------------------PGEVGEIVVHGPQVFKGYWNRPEATAEAF-IEIDGKRFFRTGDLGRMDEEGYFFITDRLKRM 441
|
490 500 510
....*....|....*....|....*....|....
gi 1720435377 575 VKlQAGEYVSLGKVEAALKNCPLIDNICAFAKSD 608
Cdd:PRK08314 442 IN-ASGFKVWPAEVENLLYKHPAIQEACVIATPD 474
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
72-619 |
1.14e-13 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 73.95 E-value: 1.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 72 DIPGADTLDKLFDHAVAKFGKKDSLgtreilseenemqpngkVFKKLIlGNYKWINYLEVNCRVNNFGSGLTALGLKPKN 151
Cdd:PRK08008 2 DIVGGQHLRQMWDDLADVYGHKTAL-----------------IFESSG-GVVRRYSYLELNEEINRTANLFYSLGIRKGD 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 152 TIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASYLITSVELLESKLKAALVDINCVKHIIyvdnk 231
Cdd:PRK08008 64 KVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLVTSAQFYPMYRQIQQEDATPLRHIC----- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 232 tINRAEYPEGLEIHSMQsvEELGAKPENLS-VPPSrpTPSDMAIVMYTSGSTGRPKGVMMHHSNLI-AGMTG--QCerip 307
Cdd:PRK08008 139 -LTRVALPADDGVSSFT--QLKAQQPATLCyAPPL--STDDTAEILFTSGTTSRPKGVVITHYNLRfAGYYSawQC---- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 308 GLGPKDTYIGYLPLAHV-LELTAEISCFTYGCRI----GYSSPlTLSDQSSKIKkgskgdctvlkptlmAAVPEIMDRIY 382
Cdd:PRK08008 210 ALRDDDVYLTVMPAFHIdCQCTAAMAAFSAGATFvlleKYSAR-AFWGQVCKYR---------------ATITECIPMMI 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 383 KNVMSKVQEMNYVQKTLFKIGYDYKL-EQIKKGYDAPLcnlilfkkvkallggNVRMMLSggaplspqthrfmnvcfccp 461
Cdd:PRK08008 274 RTLMVQPPSANDRQHCLREVMFYLNLsDQEKDAFEERF---------------GVRLLTS-------------------- 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 462 igqgYGLTEScgagTVTEVTDYTTGR-----VGAPLICCEIKLKDwqEGGYTVhdKPNPRGEIVIG---GQNISMGYFKN 533
Cdd:PRK08008 319 ----YGMTET----IVGIIGDRPGDKrrwpsIGRPGFCYEAEIRD--DHNRPL--PAGEIGEICIKgvpGKTIFKEYYLD 386
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 534 EEKTAEdyCVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKlQAGEYVSLGKVEAALKNCPLIDNICAFAKSD---QS 610
Cdd:PRK08008 387 PKATAK--VLEADG--WLHTGDTGYVDEEGFFYFVDRRCNMIK-RGGENVSCVELENIIATHPKIQDIVVVGIKDsirDE 461
|
....*....
gi 1720435377 611 YVISFVVPN 619
Cdd:PRK08008 462 AIKAFVVLN 470
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
267-671 |
1.21e-13 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 74.29 E-value: 1.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 267 PTPSDMAIVM------------YTSGSTGRPKGVMMHH--------SNLIAGMTGQCEripglgpkdTYIGYLPLAHVLE 326
Cdd:PLN03102 171 PTPSLVARMFriqdehdpislnYTSGTTADPKGVVISHrgaylstlSAIIGWEMGTCP---------VYLWTLPMFHCNG 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 327 LTaeiscFTYGCrigysspltlsdqsskikkGSKGDCTVLKPTLMAavPEImdriYKNV-MSKVQEMNYVqKTLFKIgyd 405
Cdd:PLN03102 242 WT-----FTWGT-------------------AARGGTSVCMRHVTA--PEI----YKNIeMHNVTHMCCV-PTVFNI--- 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 406 ykleqIKKGYDAPLCNLilfkkvkallGGNVRMMLSGGAPLSPQTHRFMNVCFccPIGQGYGLTESCGAGTVTEVTD--- 482
Cdd:PLN03102 288 -----LLKGNSLDLSPR----------SGPVHVLTGGSPPPAALVKKVQRLGF--QVMHAYGLTEATGPVLFCEWQDewn 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 483 --------YTTGRVGAPLIC---CEIKLKDWQEggyTVHDKPNPRGEIVIGGQNISMGYFKNEEKTAEDYcvdENGqrWF 551
Cdd:PLN03102 351 rlpenqqmELKARQGVSILGladVDVKNKETQE---SVPRDGKTMGEIVIKGSSIMKGYLKNPKATSEAF---KHG--WL 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 552 CTGDIGEFHPDGCLQIIDRKKDLVkLQAGEYVSLGKVEAALKNCPlidnicafaKSDQSYVISFVVP--NQKKLTLLAQQ 629
Cdd:PLN03102 423 NTGDVGVIHPDGHVEIKDRSKDII-ISGGENISSVEVENVLYKYP---------KVLETAVVAMPHPtwGETPCAFVVLE 492
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1720435377 630 KGVEGSWVDICNNPAMEAEILKEIREaanamKLERFEIPIKV 671
Cdd:PLN03102 493 KGETTKEDRVDKLVTRERDLIEYCRE-----NLPHFMCPRKV 529
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
136-608 |
1.99e-13 |
|
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.
Pssm-ID: 341273 [Multi-domain] Cd Length: 442 Bit Score: 72.92 E-value: 1.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 136 NNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASYLITSVELLEsklkaa 215
Cdd:cd05969 11 ARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTEELYE------ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 216 lvdincvkhiiyvdnktinraeypegleihsmqsveelgakpenlsvppsRPTPSDMAIVMYTSGSTGRPKGVMMHHSNL 295
Cdd:cd05969 85 --------------------------------------------------RTDPEDPTLLHYTSGTTGTPKGVLHVHDAM 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 296 IA-GMTGQceRIPGLGPKDTYIgylplahvleLTAEISCFTyGCRIGYSSPLTlsDQSSKIKKGSKGDctvlkptlmaav 374
Cdd:cd05969 115 IFyYFTGK--YVLDLHPDDIYW----------CTADPGWVT-GTVYGIWAPWL--NGVTNVVYEGRFD------------ 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 375 PEimdRIYKNVMS-KVQEMnYVQKTLFKIGYDYKLEQIKKgYDAplcnlilfkkvkallgGNVRMMLSGGAPLSPQTHRF 453
Cdd:cd05969 168 AE---SWYGIIERvKVTVW-YTAPTAIRMLMKEGDELARK-YDL----------------SSLRFIHSVGEPLNPEAIRW 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 454 MNVCFCCPIGQGYGLTESCGAGTVTEV-TDYTTGRVGAPLICCEIKLKDwQEGGYTvhdKPNPRGEIVIGGQNISM--GY 530
Cdd:cd05969 227 GMEVFGVPIHDTWWQTETGSIMIANYPcMPIKPGSMGKPLPGVKAAVVD-ENGNEL---PPGTKGILALKPGWPSMfrGI 302
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720435377 531 FKNEEKTAEDYcvdENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLqAGEYVSLGKVEAALKNCPLIDNICAFAKSD 608
Cdd:cd05969 303 WNDEERYKNSF---IDG--WYLTGDLAYRDEDGYFWFVGRADDIIKT-SGHRVGPFEVESALMEHPAVAEAGVIGKPD 374
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
130-697 |
2.05e-13 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 72.85 E-value: 2.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 130 EVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASYLITSVelle 209
Cdd:cd05971 11 ELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVTDG---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 210 sklkaalvdincvkhiiyvdnktinraeypegleihsmqsveelgakpenlsvppsrptPSDMAIVMYTSGSTGRPKGVM 289
Cdd:cd05971 87 -----------------------------------------------------------SDDPALIIYTSGTTGPPKGAL 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 290 MHHSNLIaGMTGQCERIPGLGPKDTYIGYLPlahvleltAEISCftygcrIGysspltlsdqsskikkgskGDCTVLKPT 369
Cdd:cd05971 108 HAHRVLL-GHLPGVQFPFNLFPRDGDLYWTP--------ADWAW------IG-------------------GLLDVLLPS 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 370 LMAAVPEIMDRIYKnvmskvqemnYVQKTLFKIGYDYKLEQIKkgydAPLCNLILFKKVKALL---GGNVRMMLSGGAPL 446
Cdd:cd05971 154 LYFGVPVLAHRMTK----------FDPKAALDLMSRYGVTTAF----LPPTALKMMRQQGEQLkhaQVKLRAIATGGESL 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 447 SPQTHRFMNVCFCCPIGQGYGLTEsCGA--GTVTEVTDYTTGRVGAPLICCEIKLKDwQEGgytVHDKPNPRGEIVIGGQ 524
Cdd:cd05971 220 GEELLGWAREQFGVEVNEFYGQTE-CNLviGNCSALFPIKPGSMGKPIPGHRVAIVD-DNG---TPLPPGEVGEIAVELP 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 525 NISM--GYFKNEEKTAEDYCVDengqrWFCTGDIGEFHPDGCLQIIDRKKDLVKlQAGEYVSLGKVEAALKNCPLIDNIC 602
Cdd:cd05971 295 DPVAflGYWNNPSATEKKMAGD-----WLLTGDLGRKDSDGYFWYVGRDDDVIT-SSGYRIGPAEIEECLLKHPAVLMAA 368
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 603 AFAKSDQ---SYVISFVVPNQkkltllaqqkGVEGSwvdicnnpameAEILKEIREAANAmKLERFEIPIKVRLSPEPWT 679
Cdd:cd05971 369 VVGIPDPirgEIVKAFVVLNP----------GETPS-----------DALAREIQELVKT-RLAAHEYPREIEFVNELPR 426
|
570
....*....|....*...
gi 1720435377 680 PETGlvtdafKLKRKELK 697
Cdd:cd05971 427 TATG------KIRRRELR 438
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
252-659 |
2.10e-13 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 73.54 E-value: 2.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 252 ELGAKPENLSVPPSRP--TPSDMAIVMYTSGSTGRPKGVMMHHSNL---IAGMTGQCERIPGLGPKDtYIGYLPLAHvle 326
Cdd:PRK12582 200 DLAATPPTAAVAAAIAaiTPDTVAKYLFTSGSTGMPKAVINTQRMMcanIAMQEQLRPREPDPPPPV-SLDWMPWNH--- 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 327 ltaeiscfTYGCRIGYSsPLTLSDQSSKIKKGskgdctvlKP------TLMAAVPEIMDRIYKNVmskvqemnyvqktlf 400
Cdd:PRK12582 276 --------TMGGNANFN-GLLWGGGTLYIDDG--------KPlpgmfeETIRNLREISPTVYGNV--------------- 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 401 KIGYDYKLEQIKKgyDAPLCNLiLFKkvkallggNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQ------GYGLTEScgA 474
Cdd:PRK12582 324 PAGYAMLAEAMEK--DDALRRS-FFK--------NLRLMAYGGATLSDDLYERMQALAVRTTGHripfytGYGATET--A 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 475 GTVTEVTDYT--TGRVGAPLICCEIKLKdwqeggytvhdkpnPRG---EIVIGGQNISMGYFKNEEKTAEDYcvDENGqr 549
Cdd:PRK12582 391 PTTTGTHWDTerVGLIGLPLPGVELKLA--------------PVGdkyEVRVKGPNVTPGYHKDPELTAAAF--DEEG-- 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 550 WFCTGDIGEF-HPDGCLQ--IID-RKKDLVKLQAGEYVSLGKVEA-ALKNC-PLIDNIcAFAKSDQSYVISFVVPNQKKL 623
Cdd:PRK12582 453 FYRLGDAARFvDPDDPEKglIFDgRVAEDFKLSTGTWVSVGTLRPdAVAACsPVIHDA-VVAGQDRAFIGLLAWPNPAAC 531
|
410 420 430
....*....|....*....|....*....|....*.
gi 1720435377 624 TLLAQQKGVEGSwvDICNNPAMeAEILKEIREAANA 659
Cdd:PRK12582 532 RQLAGDPDAAPE--DVVKHPAV-LAILREGLSAHNA 564
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
250-611 |
3.32e-13 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 72.89 E-value: 3.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 250 VEELGAKPENLSVPPSRPtpsdmAIVMYTSGSTGRPKGVMMHHSNLiAGMTGQCERIPGLGPKDTyIGYL--PLAHVLEL 327
Cdd:PRK07786 159 LAEAGPAHAPVDIPNDSP-----ALIMYTSGTTGRPKGAVLTHANL-TGQAMTCLRTNGADINSD-VGFVgvPLFHIAGI 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 328 TAEISCFTYGCRigysspltlsdqsskikkgskgdcTVLKPTLMAAVPEIMDriyknvmskVQEMNYVQkTLFKIGYDYK 407
Cdd:PRK07786 232 GSMLPGLLLGAP------------------------TVIYPLGAFDPGQLLD---------VLEAEKVT-GIFLVPAQWQ 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 408 L---EQIKKGYDAPLcnlilfkkvkallggnvRMMLSGGAPLSPQTHRFMNVCFccPIGQ---GYGLTEscgAGTVTEVT 481
Cdd:PRK07786 278 AvcaEQQARPRDLAL-----------------RVLSWGAAPASDTLLRQMAATF--PEAQilaAFGQTE---MSPVTCML 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 482 D-----YTTGRVGAPLICCEIKLKDwqeggYTVHD-KPNPRGEIVIGGQNISMGYFKNEEKTAEDYcvdENGqrWFCTGD 555
Cdd:PRK07786 336 LgedaiRKLGSVGKVIPTVAARVVD-----ENMNDvPVGEVGEIVYRAPTLMSGYWNNPEATAEAF---AGG--WFHSGD 405
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1720435377 556 IGEFHPDGCLQIIDRKKDLVkLQAGEYVSLGKVEAALKNCPLIDNICAFAKSDQSY 611
Cdd:PRK07786 406 LVRQDEEGYVWVVDRKKDMI-ISGGENIYCAEVENVLASHPDIVEVAVIGRADEKW 460
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
126-631 |
1.23e-12 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 71.73 E-value: 1.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 126 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASYLITSV 205
Cdd:PRK12467 3121 LSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQA 3200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 206 ELLEsKLKAALVDincvkHIIYVDNKTINrAEYPEGLEIHSMqsveelgakPENLsvppsrptpsdmAIVMYTSGSTGRP 285
Cdd:PRK12467 3201 HLLE-QLPAPAGD-----TALTLDRLDLN-GYSENNPSTRVM---------GENL------------AYVIYTSGSTGKP 3252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 286 KGVMMHHSNLiAGMTGQCERIPGLGPKDTYIGYLPLAhvLELTAEISCFTYGCrigysspltlsdqsskikkgskGDCTV 365
Cdd:PRK12467 3253 KGVGVRHGAL-ANHLCWIAEAYELDANDRVLLFMSFS--FDGAQERFLWTLIC----------------------GGCLV 3307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 366 LKPTLMAAvPEimdriyknvmSKVQEMNYVQKTL--FKIGYDYKLEQIKKGYDAPlcnlilfkkvkallggNVRMMLSGG 443
Cdd:PRK12467 3308 VRDNDLWD-PE----------ELWQAIHAHRISIacFPPAYLQQFAEDAGGADCA----------------SLDIYVFGG 3360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 444 APLSPQT-----HRFMNVCfccpIGQGYGLTEscgagTVTEVTDYTTGRVGAP-LICCEIKLKDWQEGGYTVHDKPNP-- 515
Cdd:PRK12467 3361 EAVPPAAfeqvkRKLKPRG----LTNGYGPTE-----AVVTVTLWKCGGDAVCeAPYAPIGRPVAGRSIYVLDGQLNPvp 3431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 516 ---RGEIVIGGQNISMGYFKNEEKTAEDYCVD---ENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVSLGKVE 589
Cdd:PRK12467 3432 vgvAGELYIGGVGLARGYHQRPSLTAERFVADpfsGSGGRLYRTGDLARYRADGVIEYLGRIDHQVKIR-GFRIELGEIE 3510
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1720435377 590 AALKNCPLIDNICAFAKSDQS--YVISFVVPNQKKLTLLAQQKG 631
Cdd:PRK12467 3511 ARLLQHPSVREAVVLARDGAGgkQLVAYVVPADPQGDWRETLRD 3554
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
269-608 |
2.67e-12 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 69.05 E-value: 2.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 269 PSDMAIVMYTSGSTGRPKGVMMHHSNLIAgMTGQCERIPGLGPKDTYIGYLPLAHVL-ELTAEISCFTYGCRIGYSSPLT 347
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVY-NAWMLALNSLFDPDDVLLCGLPLFHVNgSVVTLLTPLASGAHVVLAGPAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 348 LSDqsskikKGSKGDCTVL----KPTLMAAVPEIMDriyknvmskvqemnyvqktlfkigydyKLEQIKKGYDAplcnli 423
Cdd:cd05944 80 YRN------PGLFDNFWKLveryRITSLSTVPTVYA---------------------------ALLQVPVNADI------ 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 424 lfkkvkallgGNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTE-SCGAGTVTEVTDYTTGRVGAPLICCEIKLKDW 502
Cdd:cd05944 121 ----------SSLRFAMSGAAPLPVELRARFEDATGLPVVEGYGLTEaTCLVAVNPPDGPKRPGSVGLRLPYARVRIKVL 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 503 QEGGYTVHD-KPNPRGEIVIGGQNISMGYFKNEEKTAEDYcvdenGQRWFCTGDIGEFHPDGCLQIIDRKKDLVkLQAGE 581
Cdd:cd05944 191 DGVGRLLRDcAPDEVGEICVAGPGVFGGYLYTEGNKNAFV-----ADGWLNTGDLGRLDADGYLFITGRAKDLI-IRGGH 264
|
330 340
....*....|....*....|....*..
gi 1720435377 582 YVSLGKVEAALKNCPLIDNICAFAKSD 608
Cdd:cd05944 265 NIDPALIEEALLRHPAVAFAGAVGQPD 291
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
466-622 |
2.98e-12 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 69.54 E-value: 2.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 466 YGLTESCGAGTVTEVTD-----YTTGRVGAPLICCEIKLKDwqEGGYTVhdkPNP-RGEIVIGGQNISMGYFKNEEKTAE 539
Cdd:PRK04813 293 YGPTEATVAVTSIEITDemldqYKRLPIGYAKPDSPLLIID--EEGTKL---PDGeQGEIVISGPSVSKGYLNNPEKTAE 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 540 DYcVDENGQRWFCTGDIGEFhPDGCLQIIDRKKDLVKLqAGEYVSLGKVEAALKNCPLIDNICAFAKSDQS---YVISFV 616
Cdd:PRK04813 368 AF-FTFDGQPAYHTGDAGYL-EDGLLFYQGRIDFQIKL-NGYRIELEEIEQNLRQSSYVESAVVVPYNKDHkvqYLIAYV 444
|
....*.
gi 1720435377 617 VPNQKK 622
Cdd:PRK04813 445 VPKEED 450
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
271-618 |
4.52e-12 |
|
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.
Pssm-ID: 341268 [Multi-domain] Cd Length: 439 Bit Score: 68.66 E-value: 4.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 271 DMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPGLGPKDTYIGYLPLAhvleltaeiscFTYGCRIGYSSPLtlsd 350
Cdd:cd05958 98 DICILAFTSGTTGAPKATMHFHRDPLASADRYAVNVLRLREDDRFVGSPPLA-----------FTFGLGGVLLFPF---- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 351 qsskikkgSKGDCTVLKPtlmAAVPEimdriykNVMSKVQEmnYVQKTLFKIGYDYKLEQIKKGYDAPLcnlilfkkvka 430
Cdd:cd05958 163 --------GVGASGVLLE---EATPD-------LLLSAIAR--YKPTVLFTAPTAYRAMLAHPDAAGPD----------- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 431 llGGNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDwQEGgytvh 510
Cdd:cd05958 212 --LSSLRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEMFHIFISARPGDARPGATGKPVPGYEAKVVD-DEG----- 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 511 dKPNPRGEI---VIGGQNismGYFKNEEKTAEDYCVDEngqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLqAGEYVSLGK 587
Cdd:cd05958 284 -NPVPDGTIgrlAVRGPT---GCRYLADKRQRTYVQGG----WNITGDTYSRDPDGYFRHQGRSDDMIVS-GGYNIAPPE 354
|
330 340 350
....*....|....*....|....*....|....
gi 1720435377 588 VEAALKNCPLIDNICAFAKSDQS---YVISFVVP 618
Cdd:cd05958 355 VEDVLLQHPAVAECAVVGHPDESrgvVVKAFVVL 388
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
262-633 |
5.53e-12 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 69.61 E-value: 5.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 262 VPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPgLGPKDTYIGYLPLAHVLELTAeiscftygcriG 341
Cdd:PRK06814 785 VYFCNRDPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARID-FSPEDKVFNALPVFHSFGLTG-----------G 852
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 342 YSSPLtlsdqSSKIKkgskgdcTVLKPTLM--AAVPEImdrIYKnvmskvqemnyVQKTLFkIGYDYKLeqikKGYdAPL 419
Cdd:PRK06814 853 LVLPL-----LSGVK-------VFLYPSPLhyRIIPEL---IYD-----------TNATIL-FGTDTFL----NGY-ARY 900
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 420 CNLILFKkvkallggNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTES-----------CGAGTVtevtdyttGRV 488
Cdd:PRK06814 901 AHPYDFR--------SLRYVFAGAEKVKEETRQTWMEKFGIRILEGYGVTETapvialntpmhNKAGTV--------GRL 964
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 489 gAPLIccEIKLKD---WQEGgytvhdkpnprGEIVIGGQNISMGYFKNE-----EKTAEDycvdengqrWFCTGDIGEFH 560
Cdd:PRK06814 965 -LPGI--EYRLEPvpgIDEG-----------GRLFVRGPNVMLGYLRAEnpgvlEPPADG---------WYDTGDIVTID 1021
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720435377 561 PDGCLQIIDRKKDLVKLqAGEYVSLGKVEAAlkncplidnICAFAKSDQSYVISfvVPNQKK---LTLLAQQKGVE 633
Cdd:PRK06814 1022 EEGFITIKGRAKRFAKI-AGEMISLAAVEEL---------AAELWPDALHAAVS--IPDARKgerIILLTTASDAT 1085
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
126-297 |
6.50e-12 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 68.77 E-value: 6.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 126 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKyNFPLVT-LYATLGREAVVHGLNESEASYLITS 204
Cdd:PRK04319 74 YTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALK-NGAIVGpLFEAFMEEAVRDRLEDSEAKVLITT 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 205 VELLESKLKAalvDINCVKHIIYVDnktinrAEYPEGLEIHSMQsvEELGAKPENLSVPPSrpTPSDMAIVMYTSGSTGR 284
Cdd:PRK04319 153 PALLERKPAD---DLPSLKHVLLVG------EDVEEGPGTLDFN--ALMEQASDEFDIEWT--DREDGAILHYTSGSTGK 219
|
170
....*....|...
gi 1720435377 285 PKGVMMHHSNLIA 297
Cdd:PRK04319 220 PKGVLHVHNAMLQ 232
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
270-617 |
8.37e-12 |
|
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: 67.29 E-value: 8.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 270 SDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPGLGPKDTYIGYLPLAHVLE-------LTAEISCFTYGCRIGY 342
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWVVGDVTYLPLPATHIGGlwwiltcLIHGGLCVTGGENTTY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 343 SSPLtlsdqssKIKKGSKGDCTVLKPTLMAAVPEImdriYKNVMSKVQEMNYVQktlfkIGYDYKLEQikkgydaplcnl 422
Cdd:cd17635 81 KSLF-------KILTTNAVTTTCLVPTLLSKLVSE----LKSANATVPSLRLIG-----YGGSRAIAA------------ 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 423 ilfKKVKALLGGNVRmmlsggaplspqthrfmnvcfccpIGQGYGLTESCGAGTVTEVTDYT-TGRVGAPLICCEIKLKD 501
Cdd:cd17635 133 ---DVRFIEATGLTN------------------------TAQVYGLSETGTALCLPTDDDSIeINAVGRPYPGVDVYLAA 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 502 wQEGGYTVHDKpnpRGEIVIGGQNISMGYFKNEEKTAEDYcVDEngqrWFCTGDIGEFHPDGCLQIIDRKKDLVkLQAGE 581
Cdd:cd17635 186 -TDGIAGPSAS---FGTIWIKSPANMLGYWNNPERTAEVL-IDG----WVNTGDLGERREDGFLFITGRSSESI-NCGGV 255
|
330 340 350
....*....|....*....|....*....|....*....
gi 1720435377 582 YVSLGKVEAALKNCPLIDNICAFAKSDQSY---VISFVV 617
Cdd:cd17635 256 KIAPDEVERIAEGVSGVQECACYEISDEEFgelVGLAVV 294
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
126-575 |
1.13e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 67.62 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 126 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKynfplVTLYATlgreAVVHGLNESEASY----- 200
Cdd:PRK08276 12 VTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARR-----SGLYYT----PINWHLTAAEIAYivdds 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 201 ----LITSVELLESKLKAAlvdincvkhiiyvdnktinrAEYPEGLEIHSM--------QSVEELGA-KPEnlsVPPSRP 267
Cdd:PRK08276 83 gakvLIVSAALADTAAELA--------------------AELPAGVPLLLVvagpvpgfRSYEEALAaQPD---TPIADE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 268 TP-SDMAivmYTSGSTGRPKGVM-----MHHSNLIAGMTGQCERIPGLGPKDTYIGYLPLAHvleltaeiscftygcrig 341
Cdd:PRK08276 140 TAgADML---YSSGTTGRPKGIKrplpgLDPDEAPGMMLALLGFGMYGGPDSVYLSPAPLYH------------------ 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 342 ySSPLTLSDQSSKIkkgskGDCTVLkptlmaavpeiMDRiyknvMSKVQEMNYVQKtlFKIGYDY----------KL-EQ 410
Cdd:PRK08276 199 -TAPLRFGMSALAL-----GGTVVV-----------MEK-----FDAEEALALIER--YRVTHSQlvptmfvrmlKLpEE 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 411 IKKGYDaplcnlilfkkVKALlggnvRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAgTVTEVTDYTT--GRV 488
Cdd:PRK08276 255 VRARYD-----------VSSL-----RVAIHAAAPCPVEVKRAMIDWWGPIIHEYYASSEGGGV-TVITSEDWLAhpGSV 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 489 GAPLIcCEIKLKDwqEGGytvhdKPNPRGEI-----VIGGQNISmgYFKNEEKTAEDYcvdeNGQRWFCTGDIGEFHPDG 563
Cdd:PRK08276 318 GKAVL-GEVRILD--EDG-----NELPPGEIgtvyfEMDGYPFE--YHNDPEKTAAAR----NPHGWVTVGDVGYLDEDG 383
|
490
....*....|..
gi 1720435377 564 CLQIIDRKKDLV 575
Cdd:PRK08276 384 YLYLTDRKSDMI 395
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
271-627 |
1.94e-11 |
|
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: 66.97 E-value: 1.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 271 DMAIVMYTSGSTGRPKGVMMHHSNLIAGMTgQCERIPGLGPKDTYIGYLPLAHVLELTAE--ISCFTYGCRIGYSSPltl 348
Cdd:cd05920 140 EVALFLLSGGTTGTPKLIPRTHNDYAYNVR-ASAEVCGLDQDTVYLAVLPAAHNFPLACPgvLGTLLAGGRVVLAPD--- 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 349 sdqsskikkGSKGDCTVL----KPTLMAAVPEImdriyknVMSKVQEmnyvqktlfkigydykleqiKKGYDAPLCNLil 424
Cdd:cd05920 216 ---------PSPDAAFPLiereGVTVTALVPAL-------VSLWLDA--------------------AASRRADLSSL-- 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 425 fkkvkallggnvRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTEscgaGTVT--------EVTDYTTGRVGAPLIccE 496
Cdd:cd05920 258 ------------RLLQVGGARLSPALARRVPPVLGCTLQQVFGMAE----GLLNytrlddpdEVIIHTQGRPMSPDD--E 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 497 IKLKDwqEGGYTVhdKPNPRGEIVIGGQNISMGYFKNEEKTAEDYcvDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVK 576
Cdd:cd05920 320 IRVVD--EEGNPV--PPGEEGELLTRGPYTIRGYYRAPEHNARAF--TPDG--FYRTGDLVRRTPDGYLVVEGRIKDQIN 391
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1720435377 577 lQAGEYVSLGKVEAALKNCPLIDNICAFAKSDQSY---VISFVVPNQKKLTLLA 627
Cdd:cd05920 392 -RGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLgerSCAFVVLRDPPPSAAQ 444
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
247-582 |
4.75e-11 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 65.69 E-value: 4.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 247 MQSVEELGAKPENLSVPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAgmtgQCERIpglgpKDTYigylplahvle 326
Cdd:PRK09274 151 GTTLATLLRDGAAAPFPMADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEA----QIEAL-----REDY----------- 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 327 ltaeiscftygcrigysspltlsdqssKIKKGSKGDCT-----VLKPTL-MAAV-PEiMDriyknvMSKVQEMNYvqktl 399
Cdd:PRK09274 211 ---------------------------GIEPGEIDLPTfplfaLFGPALgMTSViPD-MD------PTRPATVDP----- 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 400 fkigyDYKLEQI-KKGYDAPLCNLILFKKV------KALLGGNVRMMLSGGAPLSPQTH-RFMNVcfccpIGQG------ 465
Cdd:PRK09274 252 -----AKLFAAIeRYGVTNLFGSPALLERLgrygeaNGIKLPSLRRVISAGAPVPIAVIeRFRAM-----LPPDaeiltp 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 466 YGLTESCGAGTVT--EVTDYTTGR--------VGAPLICCEIKL--------KDWQEggytvhDKPNPR---GEIVIGGQ 524
Cdd:PRK09274 322 YGATEALPISSIEsrEILFATRAAtdngagicVGRPVDGVEVRIiaisdapiPEWDD------ALRLATgeiGEIVVAGP 395
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720435377 525 NISMGYFKNEEKTAEDYCVDENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGEY 582
Cdd:PRK09274 396 MVTRSYYNRPEATRLAKIPDGQGDVWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTL 453
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
126-592 |
1.42e-10 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 65.19 E-value: 1.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 126 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASYLITSV 205
Cdd:PRK05691 1157 LDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQS 1236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 206 ELLEsklkaalvDINCVKHIIYVDNKTINRAEYPE---GLEIHSmqsveelgakpENLsvppsrptpsdmAIVMYTSGST 282
Cdd:PRK05691 1237 HLLE--------RLPQAEGVSAIALDSLHLDSWPSqapGLHLHG-----------DNL------------AYVIYTSGST 1285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 283 GRPKGVMMHHSNLIagmtgqcERIPGLgpKDTYIgyLPLAHVLELTAEIS-------CF---TYGCRIgysspltlsdqs 352
Cdd:PRK05691 1286 GQPKGVGNTHAALA-------ERLQWM--QATYA--LDDSDVLMQKAPISfdvsvweCFwplITGCRL------------ 1342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 353 skikkgskgdctvlkptLMAAVPEIMD--RIYKNVMSK-VQEMNYVqktlfkigydykleqikkgydAPLcnLILFKKVK 429
Cdd:PRK05691 1343 -----------------VLAGPGEHRDpqRIAELVQQYgVTTLHFV---------------------PPL--LQLFIDEP 1382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 430 ALLG-GNVRMMLSGGAPLSPQ-THRFMNVCFCCPIGQGYGLTEScgAGTVT----EVTDYTTGRVGAPL--ICCEIKLKD 501
Cdd:PRK05691 1383 LAAAcTSLRRLFSGGEALPAElRNRVLQRLPQVQLHNRYGPTET--AINVThwqcQAEDGERSPIGRPLgnVLCRVLDAE 1460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 502 WQeggytvhdkPNPRG---EIVIGGQNISMGYFKNEEKTAEDYCVD---ENGQRWFCTGDIGEFHPDGCLQIIDRKKDLV 575
Cdd:PRK05691 1461 LN---------LLPPGvagELCIGGAGLARGYLGRPALTAERFVPDplgEDGARLYRTGDRARWNADGALEYLGRLDQQV 1531
|
490
....*....|....*..
gi 1720435377 576 KLQaGEYVSLGKVEAAL 592
Cdd:PRK05691 1532 KLR-GFRVEPEEIQARL 1547
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
130-608 |
1.78e-10 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 63.95 E-value: 1.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 130 EVNCRVNNFGSGLTALGLKP--------KNTIAIFCETRAEWMIAAqtcfkYNFPlVTLYATlgREAVVHGLNESEASYL 201
Cdd:PRK12406 16 ELAQRAARAAGGLAALGVRPgdcvallmRNDFAFFEAAYAAMRLGA-----YAVP-VNWHFK--PEEIAYILEDSGARVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 202 ITSVELLESkLKAALvdincvkhiiyvdnktinraeyPEGLEIHSMQSVEELGAK----PENLSVP-------------- 263
Cdd:PRK12406 88 IAHADLLHG-LASAL----------------------PAGVTVLSVPTPPEIAAAyrisPALLTPPagaidwegwlaqqe 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 264 ----PSRPTPSDMaivMYTSGSTGRPKGVmmhhsnliagmtgqcERIPGLgPKDTyigylplAHVLELTAEISCFTYGCR 339
Cdd:PRK12406 145 pydgPPVPQPQSM---IYTSGTTGHPKGV---------------RRAAPT-PEQA-------AAAEQMRALIYGLKPGIR 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 340 IGYSSPLTLSDQSS-KIKKGSKGDCTVLKPTLMAAvpEIMDRIYKNvmsKVQEMNYVQKTLFKIgydYKL-EQIKKGYDa 417
Cdd:PRK12406 199 ALLTGPLYHSAPNAyGLRAGRLGGVLVLQPRFDPE--ELLQLIERH---RITHMHMVPTMFIRL---LKLpEEVRAKYD- 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 418 plcnlilfkkVKALlggnvRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTEScgaGTVTEVT--DYTT--GRVGAPLI 493
Cdd:PRK12406 270 ----------VSSL-----RHVIHAAAPCPADVKRAMIEWWGPVIYEYYGSTES---GAVTFATseDALShpGTVGKAAP 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 494 CCEIKLKDwQEGgytvhdKPNPRGEI-----VIGGqNISMGYFKNEEKTAEdycVDENGqrWFCTGDIGEFHPDGCLQII 568
Cdd:PRK12406 332 GAELRFVD-EDG------RPLPQGEIgeiysRIAG-NPDFTYHNKPEKRAE---IDRGG--FITSGDVGYLDADGYLFLC 398
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1720435377 569 DRKKDLVkLQAGEYVSLGKVEAALKNCPLIDNICAFAKSD 608
Cdd:PRK12406 399 DRKRDMV-ISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPD 437
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
78-584 |
2.38e-10 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 63.62 E-value: 2.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 78 TLDKLFDHAVAKFGKkdslgtREILSEENEmqpngkvfkklilGNYKWINYLEVNCRVNNFGSGLTALGLKPKNTIAifc 157
Cdd:PRK06018 11 LCHRIIDHAARIHGN------REVVTRSVE-------------GPIVRTTYAQIHDRALKVSQALDRDGIKLGDRVA--- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 158 eTRAeWMIAAQtcfkynfpLVTLYATLGREAVVHGLN---------------ESEASYL-ITSVELLEsKLKAALVDINc 221
Cdd:PRK06018 69 -TIA-WNTWRH--------LEAWYGIMGIGAICHTVNprlfpeqiawiinhaEDRVVITdLTFVPILE-KIADKLPSVE- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 222 vKHIIYVDNKTI------NRAEYPEGLEIHSMQSVeeLGAKPENLSvppsrptpsdmAIVMYTSGSTGRPKGVMM-HHSN 294
Cdd:PRK06018 137 -RYVVLTDAAHMpqttlkNAVAYEEWIAEADGDFA--WKTFDENTA-----------AGMCYTSGTTGDPKGVLYsHRSN 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 295 LIAGMTGQCERIPGLGPKDTYIGYLPLAHVleltaeiscFTYGcrIGYSSPltlSDQSSKIKKGSKGDCTVL-------K 367
Cdd:PRK06018 203 VLHALMANNGDALGTSAADTMLPVVPLFHA---------NSWG--IAFSAP---SMGTKLVMPGAKLDGASVyelldteK 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 368 PTLMAAVPEIMDRIyknvmskvqeMNYVQKTlfkigyDYKLEQIKK----GYDAPLCNLILFKKvkalLGGNVRmmlsgg 443
Cdd:PRK06018 269 VTFTAGVPTVWLML----------LQYMEKE------GLKLPHLKMvvcgGSAMPRSMIKAFED----MGVEVR------ 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 444 aplspqthrfmnvcfccpigQGYGLTESCGAGTVTEVT---DYTTG--------RVGAPLICCEIKLKDwQEGGYTVHDK 512
Cdd:PRK06018 323 --------------------HAWGMTEMSPLGTLAALKppfSKLPGdarldvlqKQGYPPFGVEMKITD-DAGKELPWDG 381
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720435377 513 PNPrGEIVIGGQNISMGYFKneektAEDYCVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKlQAGEYVS 584
Cdd:PRK06018 382 KTF-GRLKVRGPAVAAAYYR-----VDGEILDDDG--FFDTGDVATIDAYGYMRITDRSKDVIK-SGGEWIS 444
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
126-323 |
4.27e-10 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 62.97 E-value: 4.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 126 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAqtcfkynFPLVTLYATLG-------REAVVHGLNESEA 198
Cdd:PRK08279 63 ISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAW-------LGLAKLGAVVAllntqqrGAVLAHSLNLVDA 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 199 SYLITSVELLESkLKAALVDINcVKHIIYVDNKTINRAeyPEGL-EIHSMQSveelGAKPENlsvPPSRP--TPSDMAIV 275
Cdd:PRK08279 136 KHLIVGEELVEA-FEEARADLA-RPPRLWVAGGDTLDD--PEGYeDLAAAAA----GAPTTN---PASRSgvTAKDTAFY 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1720435377 276 MYTSGSTGRPKGVMMHHSNLI---AGMTGQCeripGLGPKDTYIGYLPLAH 323
Cdd:PRK08279 205 IYTSGTTGLPKAAVMSHMRWLkamGGFGGLL----RLTPDDVLYCCLPLYH 251
|
|
| PTZ00297 |
PTZ00297 |
pantothenate kinase; Provisional |
63-437 |
5.06e-10 |
|
pantothenate kinase; Provisional
Pssm-ID: 140318 [Multi-domain] Cd Length: 1452 Bit Score: 63.34 E-value: 5.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 63 THFDSLAvidipGADTLDKLFDHAVAKFGKKDSLGtreilsEENEmqpngkvfkkliLGNYKWINYLEVNCRVNNFGSGL 142
Cdd:PTZ00297 418 REYNPLA-----GVRSLGEMWERSVTRHSTFRCLG------QTSE------------SGESEWLTYGTVDARARELGSGL 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 143 TALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLyatLGREAVVHGLneseasylitsveLLESKLKAALVDINCV 222
Cdd:PTZ00297 475 LALGVRPGDVIGVDCEASRNIVILEVACALYGFTTLPL---VGKGSTMRTL-------------IDEHKIKVVFADRNSV 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 223 KHIIYVDNKTINRAEYPE--------------GLEIHSMQSVEELGakpeNLSVPPSRPTPSDMAIVMY-----TSGSTG 283
Cdd:PTZ00297 539 AAILTCRSRKLETVVYTHsfydeddhavardlNITLIPYEFVEQKG----RLCPVPLKEHVTTDTVFTYvvdntTSASGD 614
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 284 RPKGVMMHHSNLIAG-----MTGQcerIPGLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSSPLTLSDQSSKIkkg 358
Cdd:PTZ00297 615 GLAVVRVTHADVLRDistlvMTGV---LPSSFKKHLMVHFTPFAMLFNRVFVLGLFAHGSAVATVDAAHLQRAFVKF--- 688
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 359 skgdctvlKPTLMAAVPEIMDRIYKNVMSKVQEMNYVQKTLFKIGYDYKLEQIK-KGYDAPLCNLILFKKVKALLGGNVR 437
Cdd:PTZ00297 689 --------QPTILVAAPSLFSTSRLQLSRANERYSAVYSWLFERAFQLRSRLINiHRRDSSLLRFIFFRATQELLGGCVE 760
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
118-575 |
5.65e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 62.31 E-value: 5.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 118 LILGNYKWiNYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAE-W--MIAAQTC-FKYnfplVTLYATLGREAVVHGL 193
Cdd:PRK06188 31 LVLGDTRL-TYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEvLmaIGAAQLAgLRR----TALHPLGSLDDHAYVL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 194 NESEASYLITSVELLESKLKAALVDINCVKHIIyvdnkTINRAEYPEGLeihsMQSVEELGAKPenlSVPPSRPTpsDMA 273
Cdd:PRK06188 106 EDAGISTLIVDPAPFVERALALLARVPSLKHVL-----TLGPVPDGVDL----LAAAAKFGPAP---LVAAALPP--DIA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 274 IVMYTSGSTGRPKGVMMHHSNlIAGMTGQCERIPGLGPKDTYIGYLPLAHVLELTaeiscFTygcrigyssPLTLsdqss 353
Cdd:PRK06188 172 GLAYTGGTTGKPKGVMGTHRS-IATMAQIQLAEWEWPADPRFLMCTPLSHAGGAF-----FL---------PTLL----- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 354 kikkgsKGDCTVLKPTLMAAvpEIMDRIyknvmsKVQEMNYvqkTLFKIGYDYKLEQIKKGYDAPLCNLilfkkvkallg 433
Cdd:PRK06188 232 ------RGGTVIVLAKFDPA--EVLRAI------EEQRITA---TFLVPTMIYALLDHPDLRTRDLSSL----------- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 434 gnvRMMLSGGAPLSPQ-----THRFMNVcfccpIGQGYGLTESCGAGTVTEVTDYTTGRV------GAPLICCEIKLKDw 502
Cdd:PRK06188 284 ---ETVYYGASPMSPVrlaeaIERFGPI-----FAQYYGQTEAPMVITYLRKRDHDPDDPkrltscGRPTPGLRVALLD- 354
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720435377 503 qEGGYTVhdKPNPRGEIVIGGQNISMGYFKNEEKTAEDYcvdENGqrWFCTGDIGEFHPDGCLQIIDRKKDLV 575
Cdd:PRK06188 355 -EDGREV--AQGEVGEICVRGPLVMDGYWNRPEETAEAF---RDG--WLHTGDVAREDEDGFYYIVDRKKDMI 419
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
124-598 |
6.32e-10 |
|
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341289 [Multi-domain] Cd Length: 587 Bit Score: 62.21 E-value: 6.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 124 KWINYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASYLIT 203
Cdd:cd17634 83 RTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLIT 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 204 ---------SVELLESKLKAALVDINCVKHIIYVDnKTINRAEYPEGLEIHSMQSVEElgAKPENlsvPPSRPTPSDMAI 274
Cdd:cd17634 163 adggvragrSVPLKKNVDDALNPNVTSVEHVIVLK-RTGSDIDWQEGRDLWWRDLIAK--ASPEH---QPEAMNAEDPLF 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 275 VMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPGLGPKDTYIgylplahvleLTAEISCFTYGCRIGYsSPLTLsdqssk 354
Cdd:cd17634 237 ILYTSGTTGKPKGVLHTTGGYLVYAATTMKYVFDYGPGDIYW----------CTADVGWVTGHSYLLY-GPLAC------ 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 355 ikkgskGDCTVL---KPTLMAAvPEIMDRIYKNVMSKVQEMNYVQKTLFKIGYDYkleqiKKGYDAplcnlilfkkvkal 431
Cdd:cd17634 300 ------GATTLLyegVPNWPTP-ARMWQVVDKHGVNILYTAPTAIRALMAAGDDA-----IEGTDR-------------- 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 432 lgGNVRMMLSGGAPLSPQTHR-FMNVCFC--CPIGQGYGLTEScGAGTVTEVTDYTTGRVGA---PLICCEIKLKDwqEG 505
Cdd:cd17634 354 --SSLRILGSVGEPINPEAYEwYWKKIGKekCPVVDTWWQTET-GGFMITPLPGAIELKAGSatrPVFGVQPAVVD--NE 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 506 GYTVhdKPNPRGEIVIG----GQniSMGYFKNEEKTAEDYCVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLqAGE 581
Cdd:cd17634 429 GHPQ--PGGTEGNLVITdpwpGQ--TRTLFGDHERFEQTYFSTFKG--MYFSGDGARRDEDGYYWITGRSDDVINV-AGH 501
|
490
....*....|....*..
gi 1720435377 582 YVSLGKVEAALKNCPLI 598
Cdd:cd17634 502 RLGTAEIESVLVAHPKV 518
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
246-575 |
1.18e-09 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 62.11 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 246 SMQSVEELGAK--PENLSVPPSRPT-----------PSDMAIVMYTSGSTGRPKGVMMHHSNLIAG--MTGQCERIPgLG 310
Cdd:PRK05691 129 SLLQMEELAAAnaPELLCVDTLDPAlaeawqepalqPDDIAFLQYTSGSTALPKGVQVSHGNLVANeqLIRHGFGID-LN 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 311 PKDTYIGYLPLAHVLELtaeiscftygcrIGysspltlsdqsskikkgskgdcTVLKPtLMAAVPEIMdriyknvMSKVQ 390
Cdd:PRK05691 208 PDDVIVSWLPLYHDMGL------------IG----------------------GLLQP-IFSGVPCVL-------MSPAY 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 391 EMNYVQKTLFKIG-----------YDYKL--EQIKkgyDAPLCNLILfkkvkallgGNVRMMLSGGAPLSPQT-HRFMNV 456
Cdd:PRK05691 246 FLERPLRWLEAISeyggtisggpdFAYRLcsERVS---ESALERLDL---------SRWRVAYSGSEPIRQDSlERFAEK 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 457 CFCCPIGQ-----GYGLTESC--------GAG-TVTEVTDYTTGR------VGAPLICC-------EIKLKDWQEGGyTV 509
Cdd:PRK05691 314 FAACGFDPdsffaSYGLAEATlfvsggrrGQGiPALELDAEALARnraepgTGSVLMSCgrsqpghAVLIVDPQSLE-VL 392
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720435377 510 HDkpNPRGEIVIGGQNISMGYFKNEEKTAEDYcVDENGQRWFCTGDIGeFHPDGCLQIIDRKKDLV 575
Cdd:PRK05691 393 GD--NRVGEIWASGPSIAHGYWRNPEASAKTF-VEHDGRTWLRTGDLG-FLRDGELFVTGRLKDML 454
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
121-322 |
3.19e-09 |
|
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: 59.95 E-value: 3.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 121 GNYKWINYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASY 200
Cdd:TIGR02188 84 GEVRKITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIHSVVFGGFSAEALADRINDAGAKL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 201 LITSVELLE----SKLKA----ALVDINC-VKHIIYVDNKTINRAEYPEGLEIHSMQSVEelGAKPEnlsVPPSRPTPSD 271
Cdd:TIGR02188 164 VITADEGLRggkvIPLKAivdeALEKCPVsVEHVLVVRRTGNPVVPWVEGRDVWWHDLMA--KASAY---CEPEPMDSED 238
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720435377 272 MAIVMYTSGSTGRPKGVMmhHS----NLIAGMTgqCERIPGLGPKD--------------TYIGYLPLA 322
Cdd:TIGR02188 239 PLFILYTSGSTGKPKGVL--HTtggyLLYAAMT--MKYVFDIKDGDifwctadvgwitghSYIVYGPLA 303
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
121-293 |
4.76e-09 |
|
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: 59.50 E-value: 4.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 121 GNYKWINYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASY 200
Cdd:cd05966 80 DQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFAGFSAESLADRINDAQCKL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 201 LITSVEL--------LESKLKAALVDINCVKHIIYVDNkTINRAEYPEGLEI--HSMQSveelGAKPEnlsVPPSRPTPS 270
Cdd:cd05966 160 VITADGGyrggkvipLKEIVDEALEKCPSVEKVLVVKR-TGGEVPMTEGRDLwwHDLMA----KQSPE---CEPEWMDSE 231
|
170 180
....*....|....*....|...
gi 1720435377 271 DMAIVMYTSGSTGRPKGVMmhHS 293
Cdd:cd05966 232 DPLFILYTSGSTGKPKGVV--HT 252
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
118-632 |
7.78e-09 |
|
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: 58.62 E-value: 7.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 118 LILGNYKWiNYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYN-FPLVTLYATLGREaVVHGLNES 196
Cdd:COG1021 44 VVDGERRL-SYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGaIPVFALPAHRRAE-ISHFAEQS 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 197 EASYLITS--------VELLESkLKAALvdiNCVKHIIYVDnktinraeypeglEIHSMQSVEELGAKPENLSVPpsRPT 268
Cdd:COG1021 122 EAVAYIIPdrhrgfdyRALARE-LQAEV---PSLRHVLVVG-------------DAGEFTSLDALLAAPADLSEP--RPD 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 269 PSDMAIVMYTSGSTGRPKgvmmhhsnLI-------AGMTGQCERIPGLGPKDTYIGYLPLAHVLELtaeiscftygcrig 341
Cdd:COG1021 183 PDDVAFFQLSGGTTGLPK--------LIprthddyLYSVRASAEICGLDADTVYLAALPAAHNFPL-------------- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 342 ySSPLTLsdqsskikkG--SKGDCTVLKP----------------TLMAAVPEIMDRIyknvmskvqeMNYVQKtlfkig 403
Cdd:COG1021 241 -SSPGVL---------GvlYAGGTVVLAPdpspdtafplierervTVTALVPPLALLW----------LDAAER------ 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 404 YDYKLeqikkgydaplcnlilfkkvkallgGNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTEscgaGTVT----- 478
Cdd:COG1021 295 SRYDL-------------------------SSLRVLQVGGAKLSPELARRVRPALGCTLQQVFGMAE----GLVNytrld 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 479 ---EVTDYTTGRvgaPlICC--EIKLKDwqeggytVHDKPNPRGE----IVIGGQNISmGYFKNEEKTAEdyCVDENGqr 549
Cdd:COG1021 346 dpeEVILTTQGR---P-ISPddEVRIVD-------EDGNPVPPGEvgelLTRGPYTIR-GYYRAPEHNAR--AFTPDG-- 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 550 WFCTGDIGEFHPDGCLQIIDRKKDLVKlQAGEYVSLGKVEAALKNCPLIDNICAFAKSDQSY---VISFVVPNQKKLTLL 626
Cdd:COG1021 410 FYRTGDLVRRTPDGYLVVEGRAKDQIN-RGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLgerSCAFVVPRGEPLTLA 488
|
570
....*....|.
gi 1720435377 627 A-----QQKGV 632
Cdd:COG1021 489 ElrrflRERGL 499
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
263-575 |
8.56e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 58.47 E-value: 8.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 263 PPSRP---TPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPGLGPKDTYIGYLPLAHVLELtaeiscftygcr 339
Cdd:PRK07768 142 DPIDPvetGEDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVETDVMVSWLPLFHDMGM------------ 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 340 IGY-SSPLTLSdqsskikkgskgdCTVLKPTLMAAV------PEIMDRiYKNVMSKVQEMNY--VQKTLFKigydykleQ 410
Cdd:PRK07768 210 VGFlTVPMYFG-------------AELVKVTPMDFLrdpllwAELISK-YRGTMTAAPNFAYalLARRLRR--------Q 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 411 IKKG-YDAplcnlilfkkvkallgGNVRMMLSGGAPLSPQT-HRFMNV---------CFCCpigqGYGLTES-------- 471
Cdd:PRK07768 268 AKPGaFDL----------------SSLRFALNGAEPIDPADvEDLLDAgarfglrpeAILP----AYGMAEAtlavsfsp 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 472 CGAGTVTEVTD------------YTTGRV------GAPLICCEIKLKDwqEGGyTVHDkpnPR--GEIVIGGQNISMGYF 531
Cdd:PRK07768 328 CGAGLVVDEVDadllaalrravpATKGNTrrlatlGPPLPGLEVRVVD--EDG-QVLP---PRgvGVIELRGESVTPGYL 401
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1720435377 532 kneekTAEDY--CVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLV 575
Cdd:PRK07768 402 -----TMDGFipAQDADG--WLDTGDLGYLTEEGEVVVCGRVKDVI 440
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
189-594 |
1.18e-08 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 58.26 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 189 VVHGLNESEASYLITSVELLEsKLKAALVDINCVKHIIYV--DNKTINRAEYPEGLEIHSMQSveELGAKPENLSVPPSR 266
Cdd:PRK05620 103 IVHIINHAEDEVIVADPRLAE-QLGEILKECPCVRAVVFIgpSDADSAAAHMPEGIKVYSYEA--LLDGRSTVYDWPELD 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 267 PTpsDMAIVMYTSGSTGRPKGVMMHHSNL-IAGMTGQCERIPGLGPKDTYIGYLPLAHVLELTAEISCFTYGcrigysSP 345
Cdd:PRK05620 180 ET--TAAAICYSTGTTGAPKGVVYSHRSLyLQSLSLRTTDSLAVTHGESFLCCVPIYHVLSWGVPLAAFMSG------TP 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 346 LTLSDQSskikkgskgdctVLKPTLMAAVPEIMDRIYKNVMSK-VQEMNYVQKTLFKigydykleqikkgydaplcnlil 424
Cdd:PRK05620 252 LVFPGPD------------LSAPTLAKIIATAMPRVAHGVPTLwIQLMVHYLKNPPE----------------------- 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 425 fkkvkallggnvRMML----SGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVT--------EVTD---YTTGRVG 489
Cdd:PRK05620 297 ------------RMSLqeiyVGGSAVPPILIKAWEERYGVDVVHVWGMTETSPVGTVArppsgvsgEARWayrVSQGRFP 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 490 APLiccEIKLKDwqeGGYTVHDKPNPRGEIVIGGQNISMGYFKNEEKTA-------EDYCVDENGQR-----WFCTGDIG 557
Cdd:PRK05620 365 ASL---EYRIVN---DGQVMESTDRNEGEIQVRGNWVTASYYHSPTEEGggaastfRGEDVEDANDRftadgWLRTGDVG 438
|
410 420 430
....*....|....*....|....*....|....*..
gi 1720435377 558 EFHPDGCLQIIDRKKDLVKlQAGEYVslgkVEAALKN 594
Cdd:PRK05620 439 SVTRDGFLTIHDRARDVIR-SGGEWI----YSAQLEN 470
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
126-702 |
1.24e-08 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 58.16 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 126 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRA---EWMIAAQTCFKYnFPLVTLYATLGREAVVhgLNESEASYLI 202
Cdd:PRK13391 25 VTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLrylEVCWAAERSGLY-YTCVNSHLTPAEAAYI--VDDSGARALI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 203 TSVELLESkLKAALVDINCVKHIIYVDNKtinrAEYP--EGLEihsmQSVEELGAKPEnlsvpPSRPTPSDMaivMYTSG 280
Cdd:PRK13391 102 TSAAKLDV-ARALLKQCPGVRHRLVLDGD----GELEgfVGYA----EAVAGLPATPI-----ADESLGTDM---LYSSG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 281 STGRPKGVM--MHHSNLIA--GMTGQCERIPGLGPKDTYIGYLPLAHvleltaeiscftygcrigySSPLTLSdqSSKIK 356
Cdd:PRK13391 165 TTGRPKGIKrpLPEQPPDTplPLTAFLQRLWGFRSDMVYLSPAPLYH-------------------SAPQRAV--MLVIR 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 357 KGSkgdcTVLkptlmaavpeIMDR---------IYKNVMSKVQemnyVQKTLFKigYDYKL-EQIKKGYDaplcnlilfk 426
Cdd:PRK13391 224 LGG----TVI----------VMEHfdaeqylalIEEYGVTHTQ----LVPTMFS--RMLKLpEEVRDKYD---------- 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 427 kVKALlggnvRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAgTVTEVTDY-----TTGRV--GAPLICceikl 499
Cdd:PRK13391 274 -LSSL-----EVAIHAAAPCPPQVKEQMIDWWGPIIHEYYAATEGLGF-TACDSEEWlahpgTVGRAmfGDLHIL----- 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 500 kdwQEGGytvhdKPNPRGEIvigGQ-----NISMGYFKNEEKTAEDYcvDENGQrWFCTGDIGEFHPDGCLQIIDRKKDL 574
Cdd:PRK13391 342 ---DDDG-----AELPPGEP---GTiwfegGRPFEYLNDPAKTAEAR--HPDGT-WSTVGDIGYVDEDGYLYLTDRAAFM 407
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 575 VkLQAGEYVSLGKVEAALKNCPLIDNICAFAksdqsyvisfvVPNQKkltlLAQQ-KGVEGSWVDICNNPAMEAEILKEI 653
Cdd:PRK13391 408 I-ISGGVNIYPQEAENLLITHPKVADAAVFG-----------VPNED----LGEEvKAVVQPVDGVDPGPALAAELIAFC 471
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 1720435377 654 REaanamKLERFEIPIKVRLSPE-PWTPeTGlvtdafKLKRKELKNHYLK 702
Cdd:PRK13391 472 RQ-----RLSRQKCPRSIDFEDElPRLP-TG------KLYKRLLRDRYWG 509
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
261-624 |
1.72e-08 |
|
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: 57.52 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 261 SVPPSRPTPSDMAIVMYTSGSTGRPKGVMM---HHSNLIAGMTGQCeripGL--GPKDTYIGYLPLAHVleltaeiscft 335
Cdd:cd05923 141 LIEDPPREPEQPAFVFYTSGTTGLPKGAVIpqrAAESRVLFMSTQA----GLrhGRHNVVLGLMPLYHV----------- 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 336 ygcrIGYSSPLTLSdqsskikkgSKGDCTVLkptlmaaVPEIMDRiyknvmskVQEMNYVQKtlfkigydyklEQIKKGY 415
Cdd:cd05923 206 ----IGFFAVLVAA---------LALDGTYV-------VVEEFDP--------ADALKLIEQ-----------ERVTSLF 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 416 DAP-----LCNLILFKKVKAllgGNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTEscgAGTVTEVTDYTTGRVGA 490
Cdd:cd05923 247 ATPthldaLAAAAEFAGLKL---SSLRHVTFAGATMPDAVLERVNQHLPGEKVNIYGTTE---AMNSLYMRDARTGTEMR 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 491 PLICCEIKLKdwQEGGYTVHDKPN-PRGEIVI--GGQNISMGYFKNEEKTAEDYcvdenGQRWFCTGDIGEFHPDGCLQI 567
Cdd:cd05923 321 PGFFSEVRIV--RIGGSPDEALANgEEGELIVaaAADAAFTGYLNQPEATAKKL-----QDGWYRTGDVGYVDPSGDVRI 393
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 568 IDRKKDLVkLQAGEYVSLGKVEAALKNCPLIDNICAFAKSDQSY---VISFVVPNQKKLT 624
Cdd:cd05923 394 LGRVDDMI-ISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWgqsVTACVVPREGTLS 452
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
434-620 |
2.03e-08 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 57.31 E-value: 2.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 434 GNVRMMLSGGAPLSP---QTHRFMNVcfccPIGQGYGLTEScgAGTVTEVT--DYTTGR--VGAPLICCEIKLKdwqegg 506
Cdd:PRK07445 230 AQFRTILLGGAPAWPsllEQARQLQL----RLAPTYGMTET--ASQIATLKpdDFLAGNnsSGQVLPHAQITIP------ 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 507 ytvhdkPNPRGEIVIGGQNISMGYFKNEEktaedycvdeNGQRWFCTGDIGEFHPDGCLQIIDRKKDLVkLQAGEYVSLG 586
Cdd:PRK07445 298 ------ANQTGNITIQAQSLALGYYPQIL----------DSQGIFETDDLGYLDAQGYLHILGRNSQKI-ITGGENVYPA 360
|
170 180 190
....*....|....*....|....*....|....*..
gi 1720435377 587 KVEAALKNCPLIDNICAFAKSDQSY---VISFVVPNQ 620
Cdd:PRK07445 361 EVEAAILATGLVQDVCVLGLPDPHWgevVTAIYVPKD 397
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
142-703 |
3.13e-08 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 56.94 E-value: 3.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 142 LTALGLKPKNTIAIFCETRAEWMIAAQTCfKYN----FPLVTLYATLGREAVVHGLN----ESEASYLITSVELLESKLK 213
Cdd:PRK09192 66 LLALGLKPGDRVALIAETDGDFVEAFFAC-QYAglvpVPLPLPMGFGGRESYIAQLRgmlaSAQPAAIITPDELLPWVNE 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 214 AAlvdincvkhiiyvdnktiNRAEYPEGLeihsmqSVEELGAKPENlSVPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHS 293
Cdd:PRK09192 145 AT------------------HGNPLLHVL------SHAWFKALPEA-DVALPRPTPDDIAYLQYSSGSTRFPRGVIITHR 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 294 NLIAGMTGQCERIPGLGPKDTYIGYLPLAHVLELtaeISCFTygcrigysSPLTlsDQSSkikkgskgdcTVLKPTLMAA 373
Cdd:PRK09192 200 ALMANLRAISHDGLKVRPGDRCVSWLPFYHDMGL---VGFLL--------TPVA--TQLS----------VDYLPTRDFA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 374 VPEI--MDRIYKNVMSkvqeMNYVQktlfKIGYDykleqikkgydapLCNLILFKKVKALL-------GGNvrmmlsGGA 444
Cdd:PRK09192 257 RRPLqwLDLISRNRGT----ISYSP----PFGYE-------------LCARRVNSKDLAELdlscwrvAGI------GAD 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 445 PLSPQT-HRFMNvCFcCPIG-------QGYGLTESC--------GAGTVTEVTDYT--------------TGRV------ 488
Cdd:PRK09192 310 MIRPDVlHQFAE-AF-APAGfddkafmPSYGLAEATlavsfsplGSGIVVEEVDRDrleyqgkavapgaeTRRVrtfvnc 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 489 GAPLICCEIKLKDwqEGGytvHDKPNPR-GEIVIGGQNISMGYFKNEEkTAEDYCVDEngqrWFCTGDIGeFHPDGCLQI 567
Cdd:PRK09192 388 GKALPGHEIEIRN--EAG---MPLPERVvGHICVRGPSLMSGYFRDEE-SQDVLAADG----WLDTGDLG-YLLDGYLYI 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 568 IDRKKDLVKLQaGEYVSLGKVEAALKNCPLID--NICAFAKSDqsyvisfvvPNQKKLTLLAQqkgvegswvdiCNnpAM 645
Cdd:PRK09192 457 TGRAKDLIIIN-GRNIWPQDIEWIAEQEPELRsgDAAAFSIAQ---------ENGEKIVLLVQ-----------CR--IS 513
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720435377 646 EAEILKEIREAANAMKLERFEIPIKVRLSPepwtPETGLVTDAFKLKRKELKNHYLKD 703
Cdd:PRK09192 514 DEERRGQLIHALAALVRSEFGVEAAVELVP----PHSLPRTSSGKLSRAKAKKRYLSG 567
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
126-618 |
4.69e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 56.29 E-value: 4.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 126 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCfkynfplvtlyATLGreAVVHGLN----ESEASYL 201
Cdd:PRK06164 36 LSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLAC-----------ARLG--ATVIAVNtryrSHEVAHI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 202 ITS-----------------VELLESKLKAALVDincVKHIIYVDNKTinrAEYPEGLEIHSMQSVE-ELGAKPENLSVP 263
Cdd:PRK06164 103 LGRgrarwlvvwpgfkgidfAAILAAVPPDALPP---LRAIAVVDDAA---DATPAPAPGARVQLFAlPDPAPPAAAGER 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 264 PSrpTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAgMTGQCERIPGLGPKDTYIGYLPLAHVLELTAEISCFTYG----CR 339
Cdd:PRK06164 177 AA--DPDAGALLFTTSGTTSGPKLVLHRQATLLR-HARAIARAYGYDPGAVLLAALPFCGVFGFSTLLGALAGGaplvCE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 340 IGYSSPLTLSD-QSSKIKKGSKGDctvlkptlmaavpEIMDRIYKnvmSKVQEMNYVQKTLFKIGyDY-----KLEQIKK 413
Cdd:PRK06164 254 PVFDAARTARAlRRHRVTHTFGND-------------EMLRRILD---TAGERADFPSARLFGFA-SFapalgELAALAR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 414 GYDAPLCNLILFKKVKALLGG-------NVRMmLSGGAPLSPQThrfmnvcfccpigqgygltescgagtvtevtdyttg 486
Cdd:PRK06164 317 ARGVPLTGLYGSSEVQALVALqpatdpvSVRI-EGGGRPASPEA------------------------------------ 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 487 rvgapliccEIKLKDWQEGGYTVHDKPnprGEIVIGGQNISMGYFKNEEKTAEDYCVDEngqrWFCTGDIGEFHPDGCLQ 566
Cdd:PRK06164 360 ---------RVRARDPQDGALLPDGES---GEIEIRAPSLMRGYLDNPDATARALTDDG----YFRTGDLGYTRGDGQFV 423
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1720435377 567 IIDRKKDLVKLqAGEYVSLGKVEAALKNCPLIDN--ICAFAKSDQSYVISFVVP 618
Cdd:PRK06164 424 YQTRMGDSLRL-GGFLVNPAEIEHALEALPGVAAaqVVGATRDGKTVPVAFVIP 476
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
121-292 |
6.58e-08 |
|
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.
Pssm-ID: 341272 [Multi-domain] Cd Length: 610 Bit Score: 55.96 E-value: 6.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 121 GNYKWINYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASY 200
Cdd:cd05968 87 GTSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKA 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 201 LITS---------VELLESKLKAALVDINcVKHIIYVdnktiNRAEYPEGLEIHSMQSVEELGAKPEnlsVPPSRPTPSD 271
Cdd:cd05968 167 LITAdgftrrgreVNLKEEADKACAQCPT-VEKVVVV-----RHLGNDFTPAKGRDLSYDEEKETAG---DGAERTESED 237
|
170 180
....*....|....*....|.
gi 1720435377 272 MAIVMYTSGSTGRPKGVMMHH 292
Cdd:cd05968 238 PLMIIYTSGTTGKPKGTVHVH 258
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
264-609 |
7.22e-08 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 55.05 E-value: 7.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 264 PSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPGLGpkdTYIGYLPLAHVLELTAEISCFTYGcrigyS 343
Cdd:PRK07824 29 VGEPIDDDVALVVATSGTTGTPKGAMLTAAALTASADATHDRLGGPG---QWLLALPAHHIAGLQVLVRSVIAG-----S 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 344 SPLTLsDQSSKIKkgskgdctvlKPTLMAAVPEI-MDRIYKNVMSKvqemnyvqktlfkigydykleQIKKGYDAPlcnl 422
Cdd:PRK07824 101 EPVEL-DVSAGFD----------PTALPRAVAELgGGRRYTSLVPM---------------------QLAKALDDP---- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 423 ilfKKVKALLGGNVrmMLSGGAPLSPQTHRfMNVCFCCPIGQGYGLTESCGaGTVTEvtdyttgrvGAPLICCEIKLKDw 502
Cdd:PRK07824 145 ---AATAALAELDA--VLVGGGPAPAPVLD-AAAAAGINVVRTYGMSETSG-GCVYD---------GVPLDGVRVRVED- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 503 qeggytvhdkpnprGEIVIGGQNISMGYFKNEEKTAedycVDENGqrWFCTGDIGEFHpDGCLQIIDRKKDLVKlQAGEY 582
Cdd:PRK07824 208 --------------GRIALGGPTLAKGYRNPVDPDP----FAEPG--WFRTDDLGALD-DGVLTVLGRADDAIS-TGGLT 265
|
330 340
....*....|....*....|....*..
gi 1720435377 583 VSLGKVEAALKNCPLIDNICAFAKSDQ 609
Cdd:PRK07824 266 VLPQVVEAALATHPAVADCAVFGLPDD 292
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
267-596 |
7.64e-08 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 55.08 E-value: 7.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 267 PTPSDMAIvMYTSGSTGRPKGVMMHHsnliagmtGQCERIPGLGPKDTYIGYLPLAHVLELTAEIScftyGCRIGYSSPL 346
Cdd:cd05924 1 RSADDLYI-LYTGGTTGMPKGVMWRQ--------EDIFRMLMGGADFGTGEFTPSEDAHKAAAAAA----GTVMFPAPPL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 347 TLSDQSSKIKKGSKGDCTVLKPTLMAAVPEIMDRIYKNvmsKVQEMNYVQKTLFKIgydyKLEQIKKGYDAPLCNLilfk 426
Cdd:cd05924 68 MHGTGSWTAFGGLLGGQTVVLPDDRFDPEEVWRTIEKH---KVTSMTIVGDAMARP----LIDALRDAGPYDLSSL---- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 427 kvkallggnvRMMLSGGAPLSPQT-HRFMNVCFCCPIGQGYGLTESCGAGT-VTEVTDYTTG---RVGAPLICCEiklkd 501
Cdd:cd05924 137 ----------FAISSGGALLSPEVkQGLLELVPNITLVDAFGSSETGFTGSgHSAGSGPETGpftRANPDTVVLD----- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 502 wqEGGYTVHDKPNPRGEIVIGGqNISMGYFKNEEKTAEDYcVDENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKlQAGE 581
Cdd:cd05924 202 --DDGRVVPPGSGGVGWIARRG-HIPLGYYGDEAKTAETF-PEVDGVRYAVPGDRATVEADGTVTLLGRGSVCIN-TGGE 276
|
330
....*....|....*
gi 1720435377 582 YVSLGKVEAALKNCP 596
Cdd:cd05924 277 KVFPEEVEEALKSHP 291
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
251-586 |
8.37e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 55.43 E-value: 8.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 251 EELGAKPENLSVppSRPTPsdmAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQ-CERIPGLGPKDTYIGYLPLAHvlelta 329
Cdd:PRK07470 149 RHLGARVANAAV--DHDDP---CWFFFTSGTTGRPKAAVLTHGQMAFVITNHlADLMPGTTEQDASLVVAPLSH------ 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 330 eiscftyGCRIgysspltlsDQSSKIKKGSKgdcTVLKPTLMAAVPEIMDRIYKNvmsKVQEMNYVqKTLFKIgydykle 409
Cdd:PRK07470 218 -------GAGI---------HQLCQVARGAA---TVLLPSERFDPAEVWALVERH---RVTNLFTV-PTILKM------- 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 410 qikkgydaplcnLILFKKVKALLGGNVRMMLSGGAPL--SPQTH---RFMNVcfccpIGQGYGLTESCGAGTVT-----E 479
Cdd:PRK07470 268 ------------LVEHPAVDRYDHSSLRYVIYAGAPMyrADQKRalaKLGKV-----LVQYFGLGEVTGNITVLppalhD 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 480 VTDYTTGRVGapliCC-------EIKLKDwqEGGYTVhdKPNPRGEIVIGGQNISMGYFKNEEKTAEDYcvdENGqrWFC 552
Cdd:PRK07470 331 AEDGPDARIG----TCgfertgmEVQIQD--DEGREL--PPGETGEICVIGPAVFAGYYNNPEANAKAF---RDG--WFR 397
|
330 340 350
....*....|....*....|....*....|....
gi 1720435377 553 TGDIGEFHPDGCLQIIDRKKDLvklqageYVSLG 586
Cdd:PRK07470 398 TGDLGHLDARGFLYITGRASDM-------YISGG 424
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
457-618 |
1.08e-07 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 54.88 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 457 CFCcpigqGYGLTEScgAGTVTEV-TDYTTGrVGAPLICCEIKLKDwqeggytvhdkpnprGEIVIGGQNISMGYFKNEE 535
Cdd:PRK09029 267 CWC-----GYGLTEM--ASTVCAKrADGLAG-VGSPLPGREVKLVD---------------GEIWLRGASLALGYWRQGQ 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 536 KTAedyCVDENGqrWFCTGDIGEFHpDGCLQIIDRKKDLVkLQAGEYVSLGKVEAALKNCPLIDNicafaksdqsyviSF 615
Cdd:PRK09029 324 LVP---LVNDEG--WFATRDRGEWQ-NGELTILGRLDNLF-FSGGEGIQPEEIERVINQHPLVQQ-------------VF 383
|
...
gi 1720435377 616 VVP 618
Cdd:PRK09029 384 VVP 386
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
262-575 |
2.62e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 53.96 E-value: 2.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 262 VPPSrPTPSDMAIVMYTSGSTGRPKGVMMHHSNLiagMTGQCERIPGLGPK--DTYIGYLPLAHVLELTAEISCFTYGCR 339
Cdd:PRK07769 173 VPPE-ANEDTIAYLQYTSGSTRIPAGVQITHLNL---PTNVLQVIDALEGQegDRGVSWLPFFHDMGLITVLLPALLGHY 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 340 IGYSSPLTLsdqsskikkgskgdctVLKP----TLMAAVPEIMDRIyknvmskvqemnyvqktlFKIGYDYKLEQ----- 410
Cdd:PRK07769 249 ITFMSPAAF----------------VRRPgrwiRELARKPGGTGGT------------------FSAAPNFAFEHaaarg 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 411 IKKGYDAPLcNLilfkkvkallgGNVRMMLSGGAPLSPQTHRFMNVCFCcPIG-------QGYGLTESC----------- 472
Cdd:PRK07769 295 LPKDGEPPL-DL-----------SNVKGLLNGSEPVSPASMRKFNEAFA-PYGlpptaikPSYGMAEATlfvsttpmdee 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 473 -----------GAGTVTEVTDYTTGRVgAPLICCEIKLKDWQE--GGYTVHDKPNPR-GEIVIGGQNISMGYFKNEEKTA 538
Cdd:PRK07769 362 ptviyvdrdelNAGRFVEVPADAPNAV-AQVSAGKVGVSEWAVivDPETASELPDGQiGEIWLHGNNIGTGYWGKPEETA 440
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1720435377 539 EDY--------------CVDENGqRWFCTGDIGEFHpDGCLQIIDRKKDLV 575
Cdd:PRK07769 441 ATFqnilksrlseshaeGAPDDA-LWVRTGDYGVYF-DGELYITGRVKDLV 489
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
261-575 |
2.63e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 53.79 E-value: 2.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 261 SVPPSRPTPSdMAIVMYTSGSTGRPKGVMMHHSNLIA----GMTGQCERIPGLGPKD-TYIGYLPLAH----VLELTAEI 331
Cdd:PRK05850 152 SDARPRDLPS-TAYLQYTSGSTRTPAGVMVSHRNVIAnfeqLMSDYFGDTGGVPPPDtTVVSWLPFYHdmglVLGVCAPI 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 332 SCftyGCRIGYSSPLTLsdqsskikkgskgdctVLKPT----LMAAVPEImdriyknvmskvqemnyvqktlFKIGYDYK 407
Cdd:PRK05850 231 LG---GCPAVLTSPVAF----------------LQRPArwmqLLASNPHA----------------------FSAAPNFA 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 408 LE-QIKKGYDAPLCNLILfkkvkallgGNVRMMLSGGAPLSPQT-HRFMN--VCFCCP---IGQGYGLTE------SCGA 474
Cdd:PRK05850 270 FElAVRKTSDDDMAGLDL---------GGVLGIISGSERVHPATlKRFADrfAPFNLRetaIRPSYGLAEatvyvaTREP 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 475 GTVTEVTDY-----TTGRV-------GAPLIcceiklkdwqegGYTVHDKPNPR---------------GEIVIGGQNIS 527
Cdd:PRK05850 341 GQPPESVRFdyeklSAGHAkrcetggGTPLV------------SYGSPRSPTVRivdpdtciecpagtvGEIWVHGDNVA 408
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1720435377 528 MGYFKNEEKTAEDY---CVDEN----GQRWFCTGDIGEFHpDGCLQIIDRKKDLV 575
Cdd:PRK05850 409 AGYWQKPEETERTFgatLVDPSpgtpEGPWLRTGDLGFIS-EGELFIVGRIKDLL 462
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
466-598 |
5.41e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 52.74 E-value: 5.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 466 YGLTESCGAGTVT---EVTDYT-TGR---VGAPLICCEIKLKDWQEGgytvhdKPNP---RGEIVIGGQNISMGYFKNEE 535
Cdd:PRK06178 360 WGMTETHTCDTFTagfQDDDFDlLSQpvfVGLPVPGTEFKICDFETG------ELLPlgaEGEIVVRTPSLLKGYWNKPE 433
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720435377 536 KTAEdycVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVSLGKVEAALKNCPLI 598
Cdd:PRK06178 434 ATAE---ALRDG--WLHTGDIGKIDEQGFLHYLGRRKEMLKVN-GMSVFPSEVEALLGQHPAV 490
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
263-605 |
5.43e-07 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 53.12 E-value: 5.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 263 PPSRPTPSDMAIVMYTSGSTGRPKGVMMHHS---NLIAGMTGQCeripGLGPKDTyigylplahVLELTAeiscftygCR 339
Cdd:PRK10252 591 PLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTaivNRLLWMQNHY----PLTADDV---------VLQKTP--------CS 649
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 340 IGYSS-----PLTLsdqsskikkgskGDCTVLKPTLMAAVPEIMDRIYKNvmSKVQEMNYVQKTLfkigydykleqikKG 414
Cdd:PRK10252 650 FDVSVweffwPFIA------------GAKLVMAEPEAHRDPLAMQQFFAE--YGVTTTHFVPSML-------------AA 702
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 415 YDAPLCNLILFKKVKALlggnVRMMLSGGA---PLSPQTHRFMNVcfccPIGQGYGLTEScgAGTVT------EVTDYTT 485
Cdd:PRK10252 703 FVASLTPEGARQSCASL----RQVFCSGEAlpaDLCREWQQLTGA----PLHNLYGPTEA--AVDVSwypafgEELAAVR 772
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 486 GR---VGAPLicceiklkdWQEGGYTVHDKPNP-----RGEIVIGGQNISMGYFKNEEKTAEDYCVD--ENGQRWFCTGD 555
Cdd:PRK10252 773 GSsvpIGYPV---------WNTGLRILDARMRPvppgvAGDLYLTGIQLAQGYLGRPDLTASRFIADpfAPGERMYRTGD 843
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1720435377 556 IGEFHPDGCLQIIDRKKDLVKLQaGEYVSLGKVEAALKNCPLIDNICAFA 605
Cdd:PRK10252 844 VARWLDDGAVEYLGRSDDQLKIR-GQRIELGEIDRAMQALPDVEQAVTHA 892
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
250-580 |
5.79e-07 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 52.85 E-value: 5.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 250 VEELGAKPENLSVPPsrPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPGLGPKDTYIGYLPLAHVLELTA 329
Cdd:PRK05851 134 LATAAHTNRSASLTP--PDSGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVGLDAATDVGCSWLPLYHDMGLAF 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 330 EISCFTYGcrigysSPLTLSDQSSkikkgskgdctvlkptlMAAVPeimdriyknvMSKVQEMNYVQKTLFK---IGYDY 406
Cdd:PRK05851 212 LLTAALAG------APLWLAPTTA-----------------FSASP----------FRWLSWLSDSRATLTAapnFAYNL 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 407 kleqIKKgYDaplcnlilfKKVKALLGGNVRMMLSGGAPLSPQ-THRFMNVcfCCPIG-------QGYGLTES------- 471
Cdd:PRK05851 259 ----IGK-YA---------RRVSDVDLGALRVALNGGEPVDCDgFERFATA--MAPFGfdagaaaPSYGLAEStcavtvp 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 472 -CGAG-TVTEVTDYTTG------RVGAPLICCEIKLKDWQE----GGYTVhdkpnprGEIVIGGQNISMGYFKNEEKTAE 539
Cdd:PRK05851 323 vPGIGlRVDEVTTDDGSgarrhaVLGNPIPGMEVRISPGDGaagvAGREI-------GEIEIRGASMMSGYLGQAPIDPD 395
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1720435377 540 DycvdengqrWFCTGDIGEFhPDGCLQIIDRKKDLVKLqAG 580
Cdd:PRK05851 396 D---------WFPTGDLGYL-VDGGLVVCGRAKELITV-AG 425
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
269-625 |
1.46e-06 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 51.36 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 269 PSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGqCERIPGLGPKDTYIGYLPLAHvleltaeiscfTYGCrigysspltl 348
Cdd:PRK06334 182 PEDVAVILFTSGTEKLPKGVPLTHANLLANQRA-CLKFFSPKEDDVMMSFLPPFH-----------AYGF---------- 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 349 sdqsskikkgskgDCTVLKPtLMAAVPEIMDriYKNVMSK--VQEMNYVQKTLF---KIGYDYKLEQIKKGyDAPLCNLI 423
Cdd:PRK06334 240 -------------NSCTLFP-LLSGVPVVFA--YNPLYPKkiVEMIDEAKVTFLgstPVFFDYILKTAKKQ-ESCLPSLR 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 424 LfkkvkALLGGNV--RMMLSGGAPLSPQTHrfmnvcfccpIGQGYGLTESCGAGTVTEVTDYTTGR-VGAPLICCEIKLK 500
Cdd:PRK06334 303 F-----VVIGGDAfkDSLYQEALKTFPHIQ----------LRQGYGTTECSPVITINTVNSPKHEScVGMPIRGMDVLIV 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 501 dwQEGGYTvhdkPNPRGE---IVIGGQNISMGYFKNEEKTAedyCVDENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKL 577
Cdd:PRK06334 368 --SEETKV----PVSSGEtglVLTRGTSLFSGYLGEDFGQG---FVELGGETWYVTGDLGYVDRHGELFLKGRLSRFVKI 438
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1720435377 578 qAGEYVSLGKVEAALkncplidnICAFAKSDQSYVISFVV---PNQK-KLTL 625
Cdd:PRK06334 439 -GAEMVSLEALESIL--------MEGFGQNAADHAGPLVVcglPGEKvRLCL 481
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
126-300 |
1.95e-06 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 51.29 E-value: 1.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 126 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCfkynfplvtlyATLGreA---VVHG---------- 192
Cdd:PRK00174 99 ITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLAC-----------ARIG--AvhsVVFGgfsaealadr 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 193 LNESEASYLITSVELLE----SKLKA----ALVDINCVKHIIYVdNKTINRAEYPEGLEI--HSMQSveelGAKPEnlsV 262
Cdd:PRK00174 166 IIDAGAKLVITADEGVRggkpIPLKAnvdeALANCPSVEKVIVV-RRTGGDVDWVEGRDLwwHELVA----GASDE---C 237
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1720435377 263 PPSRPTPSDMAIVMYTSGSTGRPKGVMmhHS----NLIAGMT 300
Cdd:PRK00174 238 EPEPMDAEDPLFILYTSGSTGKPKGVL--HTtggyLVYAAMT 277
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
268-697 |
2.33e-06 |
|
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: 50.51 E-value: 2.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 268 TPSDMAIVMYTSGSTGRPKGVMMHHSNliagmtgqceripglgpkdTYIGYLPLAHVLELTAEIScfTYGCRIGYSSPLT 347
Cdd:cd05937 85 DPDDPAILIYTSGTTGLPKAAAISWRR-------------------TLVTSNLLSHDLNLKNGDR--TYTCMPLYHGTAA 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 348 LSDQSSKIKKGSkgdCTVLKPTLMAAvpEIMDRIYKNVMSKVQemnYVQKTLfkigyDYKLEQIKKGYDAplcnlilfkk 427
Cdd:cd05937 144 FLGACNCLMSGG---TLALSRKFSAS--QFWKDVRDSGATIIQ---YVGELC-----RYLLSTPPSPYDR---------- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 428 vkallGGNVRMMLSGGapLSPQT-HRFMNVcFCCP-IGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDWQ-- 503
Cdd:cd05937 201 -----DHKVRVAWGNG--LRPDIwERFRER-FNVPeIGEFYAATEGVFALTNHNVGDFGAGAIGHHGLIRRWKFENQVvl 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 504 --------------EGGYTVHDKPNPRGEIV--IGGQNISM--GYFKNEEKTAEDYCVD--ENGQRWFCTGDIGEFHPDG 563
Cdd:cd05937 273 vkmdpetddpirdpKTGFCVRAPVGEPGEMLgrVPFKNREAfqGYLHNEDATESKLVRDvfRKGDIYFRTGDLLRQDADG 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 564 CLQIIDRKKDLVKLQaGEYVSLGKVEaalkncpliDNICAFAKSDQSYVISFVVPNqkkltllaqQKGVEGSW-VDICNN 642
Cdd:cd05937 353 RWYFLDRLGDTFRWK-SENVSTTEVA---------DVLGAHPDIAEANVYGVKVPG---------HDGRAGCAaITLEES 413
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1720435377 643 PAMEAEILKEIREAANAMKLERFEIPIKVRLSPEpwtpetGLVTDAFKLKRKELK 697
Cdd:cd05937 414 SAVPTEFTKSLLASLARKNLPSYAVPLFLRLTEE------VATTDNHKQQKGVLR 462
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
517-589 |
3.30e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 50.48 E-value: 3.30e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720435377 517 GEIVIGGQNISMGYFKNEEKTAEDycvdengqRWFCTGDIGEFHPDGCLQIIDRKKDLVKlQAGEYVSLGKVE 589
Cdd:PRK07008 385 GDLQVRGPWVIDRYFRGDASPLVD--------GWFPTGDVATIDADGFMQITDRSKDVIK-SGGEWISSIDIE 448
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
126-592 |
4.74e-06 |
|
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: 49.66 E-value: 4.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 126 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEAsylitsv 205
Cdd:cd05940 4 LTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSA------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 206 ellesklkaalvdincvKHIIYvdnktinraeypegleihsmqsveelgakpenlsvppsrptpsDMAIVMYTSGSTGRP 285
Cdd:cd05940 77 -----------------KHLVV-------------------------------------------DAALYIYTSGTTGLP 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 286 KGVMMHHSNLIAGMTGqCERIPGLGPKDTYIGYLPLAHVlelTAEISCFTYGCRIGYSspltlsdqsskikkgskgdcTV 365
Cdd:cd05940 97 KAAIISHRRAWRGGAF-FAGSGGALPSDVLYTCLPLYHS---TALIVGWSACLASGAT--------------------LV 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 366 LKPTLMAAvpEIMDRIYKNVMSKVQemnYVQKTLfkigyDYKLEQIKKGYDAplcnlilfkkvkallGGNVRMMLSGGap 445
Cdd:cd05940 153 IRKKFSAS--NFWDDIRKYQATIFQ---YIGELC-----RYLLNQPPKPTER---------------KHKVRMIFGNG-- 205
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 446 LSPQTHRFMNVCFCCP-IGQGYGLTE-SCGAGTVTEVtDYTTGRVGAPLICC-EIKL-KDWQEGGYTVHD-----KPNPR 516
Cdd:cd05940 206 LRPDIWEEFKERFGVPrIAEFYAATEgNSGFINFFGK-PGAIGRNPSLLRKVaPLALvKYDLESGEPIRDaegrcIKVPR 284
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 517 GEI------VIGGQNISmGYFKN---EEKTAEDycVDENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVSLGK 587
Cdd:cd05940 285 GEPgllisrINPLEPFD-GYTDPaatEKKILRD--VFKKGDAWFNTGDLMRLDGEGFWYFVDRLGDTFRWK-GENVSTTE 360
|
....*
gi 1720435377 588 VEAAL 592
Cdd:cd05940 361 VAAVL 365
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
274-619 |
5.35e-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: 49.22 E-value: 5.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 274 IVMYTSGSTGRPKGVMMHHSNLIAgMTGQCERIPGLGPKDTYIGYLPLAHVLELTAEISCFTYGcrigysspltlsdqss 353
Cdd:cd17636 4 LAIYTAAFSGRPNGALLSHQALLA-QALVLAVLQAIDEGTVFLNSGPLFHIGTLMFTLATFHAG---------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 354 kikkgskGDCTVLKPTLMAAVPEIMDRiyknvmSKVQEMNYVQKTLfkigydyklEQIKKGYDAPLCNLILFKKVKALLG 433
Cdd:cd17636 67 -------GTNVFVRRVDAEEVLELIEA------ERCTHAFLLPPTI---------DQIVELNADGLYDLSSLRSSPAAPE 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 434 GNvrMMLSggAPLSPQTHRFMnvcfccpigqGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDwqEGGYTVHDkp 513
Cdd:cd17636 125 WN--DMAT--VDTSPWGRKPG----------GYGQTEVMGLATFAALGGGAIGGAGRPSPLVQVRILD--EDGREVPD-- 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 514 NPRGEIVIGGQNISMGYFKNEEktaedycvdENGQR----WFCTGDIGEFHPDGCLQIIDRKKDLVKlQAGEYVSLGKVE 589
Cdd:cd17636 187 GEVGEIVARGPTVMAGYWNRPE---------VNARRtrggWHHTNDLGRREPDGSLSFVGPKTRMIK-SGAENIYPAEVE 256
|
330 340 350
....*....|....*....|....*....|....
gi 1720435377 590 AALKNCPLIDNICAFAKSD----QSyVISFVVPN 619
Cdd:cd17636 257 RCLRQHPAVADAAVIGVPDprwaQS-VKAIVVLK 289
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
242-323 |
2.92e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 47.37 E-value: 2.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 242 LEIHSMQSVEELGAKPENLsVPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNL-IAGMTgQCERIpGLGPKDTYIGYLP 320
Cdd:PRK07867 125 INVDSPAWADELAAHRDAE-PPFRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVaSAGVM-LAQRF-GLGPDDVCYVSMP 201
|
...
gi 1720435377 321 LAH 323
Cdd:PRK07867 202 LFH 204
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
277-601 |
9.14e-05 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 45.09 E-value: 9.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 277 YTSGSTGRPKGVMMHHSNLIAGMTGQcERIPGLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSSPLTLSDQSSKIK 356
Cdd:cd17633 7 FTSGTTGLPKAYYRSERSWIESFVCN-EDLFNISGEDAILAPGPLSHSLFLYGAISALYLGGTFIGQRKFNPKSWIRKIN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 357 KGSKgdctvlkpTLMAAVPEIMDRIYK--NVMSKVQEMNYVQKTLFKIgydyKLEQIKKGydAPLCNLILFkkvkallgg 434
Cdd:cd17633 86 QYNA--------TVIYLVPTMLQALARtlEPESKIKSIFSSGQKLFES----TKKKLKNI--FPKANLIEF--------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 435 nvrmmlSGGAPLSPQTHRFMNvcfccpigqgygltescgagtvtevTDYTTGRVGAPLICCEIKLKDwQEGGYTvhdkpn 514
Cdd:cd17633 143 ------YGTSELSFITYNFNQ-------------------------ESRPPNSVGRPFPNVEIEIRN-ADGGEI------ 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 515 prGEIVIGGQNISMGYFKNEEktaedYCVDEngqrWFCTGDIGEFHPDGCLQIIDRKKDLVkLQAGEYVSLGKVEAALKN 594
Cdd:cd17633 185 --GKIFVKSEMVFSGYVRGGF-----SNPDG----WMSVGDIGYVDEEGYLYLVGRESDMI-IIGGINIFPTEIESVLKA 252
|
....*..
gi 1720435377 595 CPLIDNI 601
Cdd:cd17633 253 IPGIEEA 259
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
128-324 |
1.32e-04 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 44.97 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 128 YLEVNCRVNNFGSGL-TALGLKPKNTIAIFC--ETRAEWM---IAAQTCfkynfPLVTLYATLGREAVVHGLNESEASYL 201
Cdd:cd05938 8 YRDVDRRSNQAARALlAHAGLRPGDTVALLLgnEPAFLWIwlgLAKLGC-----PVAFLNTNIRSKSLLHCFRCCGAKVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 202 ITSVELLES------KLKAALVdincvkHIIYVDNKTInraeyPEGleihsmqsVEELGAKPENLS---VPPS---RPTP 269
Cdd:cd05938 83 VVAPELQEAveevlpALRADGV------SVWYLSHTSN-----TEG--------VISLLDKVDAASdepVPASlraHVTI 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1720435377 270 SDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQceRIPGLGPKDTYIGYLPLAHV 324
Cdd:cd05938 144 KSPALYIYTSGTTGLPKAARISHLRVLQCSGFL--SLCGVTADDVIYITLPLYHS 196
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
519-680 |
2.82e-04 |
|
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: 43.96 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 519 IVIGGQNISMGYFKNEEKTaeDYCVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLqAGEYVSLGKVEAALKNCPLI 598
Cdd:cd05915 363 VQLKGPWITGGYYGNEEAT--RSALTPDG--FFRTGDIAVWDEEGYVEIKDRLKDLIKS-GGEWISSVDLENALMGHPKV 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 599 DNICAFAKSDQSYVISFVvpnqkkltllaqqkgvegSWVDICNNPAMEAEILKEIREAANAMKLerfeIPIKVRLSPE-P 677
Cdd:cd05915 438 KEAAVVAIPHPKWQERPL------------------AVVVPRGEKPTPEELNEHLLKAGFAKWQ----LPDAYVFAEEiP 495
|
...
gi 1720435377 678 WTP 680
Cdd:cd05915 496 RTS 498
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
268-310 |
4.08e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 44.00 E-value: 4.08e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1720435377 268 TPSDMAIVMYTSGSTGRPKGVMMHHsnliAGM-TGQCERIPGLG 310
Cdd:PRK05691 3867 GPDNLAYVIYTSGSTGLPKGVMVEQ----RGMlNNQLSKVPYLA 3906
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
263-599 |
6.79e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 43.23 E-value: 6.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 263 PPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPL---AHVLELTAEISCftyGCR 339
Cdd:PRK05691 2326 LPFLSLPQHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERF-GMRADDCELHFYSInfdAASERLLVPLLC---GAR 2401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 340 IgysspltlsdqsskikkgskgdctVLKPTLMAAVPEIMDRIyknvmsKVQEMNYVQktlFKIGYDYKLEQIKKGYDAPL 419
Cdd:PRK05691 2402 V------------------------VLRAQGQWGAEEICQLI------REQQVSILG---FTPSYGSQLAQWLAGQGEQL 2448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 420 cnlilfkkvkallggNVRMMLSGGAPLSPQTHRFMNVCFCcP--IGQGYGLTESC--------------GAGTVTeVTDY 483
Cdd:PRK05691 2449 ---------------PVRMCITGGEALTGEHLQRIRQAFA-PqlFFNAYGPTETVvmplaclapeqleeGAASVP-IGRV 2511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 484 TTGRVGAPLiccEIKLKDWQEGGytvhdkpnpRGEIVIGGQNISMGYFKNEEKTAEDYCVD---ENGQRWFCTGDIGEFH 560
Cdd:PRK05691 2512 VGARVAYIL---DADLALVPQGA---------TGELYVGGAGLAQGYHDRPGLTAERFVADpfaADGGRLYRTGDLVRLR 2579
|
330 340 350
....*....|....*....|....*....|....*....
gi 1720435377 561 PDGCLQIIDRKKDLVKLQaGEYVSLGKVEAALKNCPLID 599
Cdd:PRK05691 2580 ADGLVEYVGRIDHQVKIR-GFRIELGEIESRLLEHPAVR 2617
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
443-596 |
7.88e-04 |
|
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: 42.48 E-value: 7.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 443 GAPLSPQT-HRFMNVCfCCPIGQGYGLTEScgagTVTEVT----DYTTGRVGAPLICCEIKLKDwQEGGYTvhdKPNPRG 517
Cdd:cd05970 310 GEALNPEVfNTFKEKT-GIKLMEGFGQTET----TLTIATfpwmEPKPGSMGKPAPGYEIDLID-REGRSC---EAGEEG 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 518 EIVI---GGQNISM--GYFKNEEKTAEdycVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKlQAGEYVSLGKVEAAL 592
Cdd:cd05970 381 EIVIrtsKGKPVGLfgGYYKDAEKTAE---VWHDG--YYHTGDAAWMDEDGYLWFVGRTDDLIK-SSGYRIGPFEVESAL 454
|
....
gi 1720435377 593 KNCP 596
Cdd:cd05970 455 IQHP 458
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
267-599 |
9.70e-04 |
|
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: 42.45 E-value: 9.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 267 PTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPL----AHVLELTAEIScftygcRIGY 342
Cdd:cd05910 82 PKADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLY-GIRPGEVDLATFPLfalfGPALGLTSVIP------DMDP 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 343 SSPLTLSDQS--SKIKKgskgdctvLKPTLMAAVPEIMDRIyknvmSKVQEMNyvQKTLfkigydykleqikkgydaplc 420
Cdd:cd05910 155 TRPARADPQKlvGAIRQ--------YGVSIVFGSPALLERV-----ARYCAQH--GITL--------------------- 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 421 nlilfkkvkallgGNVRMMLSGGAPLSPQTH-RFMN-VCFCCPIGQGYGLTESC------GAGTVTEVTDYTTGR----V 488
Cdd:cd05910 199 -------------PSLRRVLSAGAPVPIALAaRLRKmLSDEAEILTPYGATEALpvssigSRELLATTTAATSGGagtcV 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 489 GAPLICCEIKL-----KDWQEGGYTVHDKPNPRGEIVIGGQNISMGYFKNEEKTAEDYCVDENGQRWFCTGDIGEFHPDG 563
Cdd:cd05910 266 GRPIPGVRVRIieiddEPIAEWDDTLELPRGEIGEITVTGPTVTPTYVNRPVATALAKIDDNSEGFWHRMGDLGYLDDEG 345
|
330 340 350
....*....|....*....|....*....|....*.
gi 1720435377 564 CLQIIDRKKDLVKLQAGEYVSLgKVEAALKNCPLID 599
Cdd:cd05910 346 RLWFCGRKAHRVITTGGTLYTE-PVERVFNTHPGVR 380
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
239-295 |
2.11e-03 |
|
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.
Pssm-ID: 274582 [Multi-domain] Cd Length: 1389 Bit Score: 41.59 E-value: 2.11e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720435377 239 PEGLEIHSMQSVEELGAKPENLSV-PPSRPTPSdmaivmYTSGSTGRPKGVMMHHSNL 295
Cdd:TIGR03443 389 LEGGETDVLAPYQALKDTPTGVVVgPDSNPTLS------FTSGSEGIPKGVLGRHFSL 440
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
517-575 |
4.12e-03 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 40.49 E-value: 4.12e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720435377 517 GEIVIGGQNISMGYFKNEEKTAEDYC---------------VDENGqRWFCTGDIGeFHPDGCLQIIDRKKDLV 575
Cdd:PRK12476 430 GEIWLHGDNIGRGYWGRPEETERTFGaklqsrlaegshadgAADDG-TWLRTGDLG-VYLDGELYITGRIADLI 501
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
118-573 |
4.79e-03 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 39.97 E-value: 4.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 118 LILGNYKWiNYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIaaqtcfkynfplvTLYATLgrEAVVHGLNese 197
Cdd:PRK10946 42 VICGERQF-SYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYI-------------TFFALL--KLGVAPVN--- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 198 ASYLITSVELLE--SKLKAALVdINCVKHIIYVDNKTIN--RAEYPEGLEIH-----SMQSVEELGAKPENLSVPpsRPT 268
Cdd:PRK10946 103 ALFSHQRSELNAyaSQIEPALL-IADRQHALFSDDDFLNtlVAEHSSLRVVLllnddGEHSLDDAINHPAEDFTA--TPS 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 269 PSD-MAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCErIPGLGPKDTYIGYLPLAHVLELtaeiscftygcrigySSPlt 347
Cdd:PRK10946 180 PADeVAFFQLSGGSTGTPKLIPRTHNDYYYSVRRSVE-ICGFTPQTRYLCALPAAHNYPM---------------SSP-- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 348 lsdqsskikkGS-----KGDCTVlkptlMAAVPE------IMDRIYKNVMSKVQEmnyvQKTLFkigydykLEQIKK-GY 415
Cdd:PRK10946 242 ----------GAlgvflAGGTVV-----LAPDPSatlcfpLIEKHQVNVTALVPP----AVSLW-------LQAIAEgGS 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 416 DAPLCNLilfkkvkallggnvRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTEscgaGTV--TEVTD-----YTTGrv 488
Cdd:PRK10946 296 RAQLASL--------------KLLQVGGARLSETLARRIPAELGCQLQQVFGMAE----GLVnyTRLDDsderiFTTQ-- 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435377 489 GAPlICC--EIKLKDwQEGgytvhdKPNPRGEI---VIGGQNISMGYFKNEEKTAEdyCVDENGqrWFCTGDIGEFHPDG 563
Cdd:PRK10946 356 GRP-MSPddEVWVAD-ADG------NPLPQGEVgrlMTRGPYTFRGYYKSPQHNAS--AFDANG--FYCSGDLVSIDPDG 423
|
490
....*....|
gi 1720435377 564 CLQIIDRKKD 573
Cdd:PRK10946 424 YITVVGREKD 433
|
|
| |
