|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
1-583 |
0e+00 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 1098.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 1 MAYKSLNSITKSDIEALGISGDVSEKLLRDLEDIIHGS-STPPETWIQISRRILHPNLPFSFHQMMYYGCYKDFGPDL-- 77
Cdd:PLN03052 3 MAGKSVDEITVGDLEAAGLSPEEAEKFFKELQVILTRAgASPPSIWRRISQSLLTPSHPFALHQLMYYSCYKNWDSDTlg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 78 --PAWIPDPKVASLTNVGKLLEKRGKEFLGGNYKNPVSSFSSFQEFSVSNPEVYWKTVLDELNILFSVPPKCILEKdTSG 155
Cdd:PLN03052 83 ppPAWFPSPEIAKLTNLGRLLEARGKELLGSKYKDPISSFSEFQRFSVENPEVYWSIVLDELSLVFSVPPRCILDT-SDE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 156 DNPGGKWLPGAYLNPARNCLTNGFKRRLDDIVIRWRDEGSDDLPVNTMTLLELRSQVWLAAHALSALGLEEESAIAVDMP 235
Cdd:PLN03052 162 SNPGGQWLPGAVLNVAECCLTPKPSKTDDSIAIIWRDEGSDDLPVNRMTLSELRSQVSRVANALDALGFEKGDAIAIDMP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 236 MNVESVIIYLAIVLAGHVVVSIADSFSPREISTRLKISKAKAIFTQDVIIRGDKSIPLYRRVVDAEAPLAIVVPARGSSC 315
Cdd:PLN03052 242 MNVHAVIIYLAIILAGCVVVSIADSFAPSEIATRLKISKAKAIFTQDVIVRGGKSIPLYSRVVEAKAPKAIVLPADGKSV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 316 RMKLREKDLSWNNFLGNARNL-RGVEYVAAEKPAGAYTNILFSSGTTGEPKAIPWTNISPLKSAADAWCHLDVQRGDVVA 394
Cdd:PLN03052 322 RVKLREGDMSWDDFLARANGLrRPDEYKAVEQPVEAFTNILFSSGTTGEPKAIPWTQLTPLRAAADAWAHLDIRKGDIVC 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 395 WPTNLGWMMGPWLVYASLINGACMGLYNGSPLGPTFAKFVQDAEVSVLGVIPSIVRTWQNSNSTSGYDWSRIRCFGSTGE 474
Cdd:PLN03052 402 WPTNLGWMMGPWLVYASLLNGATLALYNGSPLGRGFAKFVQDAKVTMLGTVPSIVKTWKNTNCMAGLDWSSIRCFGSTGE 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 475 ASNIDEYLWLMGRAHYKPVIEYCGGTEIGGSFISGSLLQPQSLAAFSTAAMGCKLFILDEDSNPIPPYAAGVGELALCPH 554
Cdd:PLN03052 482 ASSVDDYLWLMSRAGYKPIIEYCGGTELGGGFVTGSLLQPQAFAAFSTPAMGCKLFILDDSGNPYPDDAPCTGELALFPL 561
|
570 580
....*....|....*....|....*....
gi 1063733435 555 MFGASSTLLNGNHFKVYFQGMPTFQGQVI 583
Cdd:PLN03052 562 MFGASSTLLNADHYKVYFKGMPVFNGKIL 590
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
234-578 |
1.25e-172 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 499.34 E-value: 1.25e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 234 MPMNVESVIIYLAIVLAGHVVVSIADSFSPREISTRLKISKAKAIFTQDVIIRGDKSIPLYRRVVDAEAPLAIVVPARGS 313
Cdd:PLN03051 1 MPMTVDAVIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFTQDVVLRGGRALPLYSKVVEAAPAKAIVLPAAGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 314 SCRMKLREKDLSWNNFLGNAR---NLRGVEYVAAEKPAGAYTNILFSSGTTGEPKAIPWTNISPLKSAADAWCHLDVQRG 390
Cdd:PLN03051 81 PVAVPLREQDLSWCDFLGVAAaqgSVGGNEYSPVYAPVESVTNILFSSGTTGEPKAIPWTHLSPLRCASDGWAHMDIQPG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 391 DVVAWPTNLGWMMGPWLVYASLINGACMGLYNGSPLGPTFAKFVQDAEVSVLGVIPSIVRTWQNSN--STSGYDWSRIRC 468
Cdd:PLN03051 161 DVVCWPTNLGWMMGPWLLYSAFLNGATLALYGGAPLGRGFGKFVQDAGVTVLGLVPSIVKAWRHTGafAMEGLDWSKLRV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 469 FGSTGEASNIDEYLWLM-GRAHYKPVIEYCGGTEIGGSFISGSLLQPQSLAAFSTAAMGCKLFILDEDSNPIPPYAAGVG 547
Cdd:PLN03051 241 FASTGEASAVDDVLWLSsVRGYYKPVIEYCGGTELASGYISSTLLQPQAPGAFSTASLGTRFVLLNDNGVPYPDDQPCVG 320
|
330 340 350
....*....|....*....|....*....|.
gi 1063733435 548 ELALCPHMFGASSTLLNGNHFKVYFQGMPTF 578
Cdd:PLN03051 321 EVALAPPMLGASDRLLNADHDKVYYKGMPMY 351
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
126-551 |
8.21e-77 |
|
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: 255.49 E-value: 8.21e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 126 PEVYWKTVLDELNILFSVPPKCILekDTSGDNPGGKWLPGAYLNPARNCLTNGFKRRLDDIVIRWRDEgsdDLPVNTMTL 205
Cdd:cd05968 20 NAWFWGEFVKDVGIEWYEPPYQTL--DLSGGKPWAAWFVGGRMNIVEQLLDKWLADTRTRPALRWEGE---DGTSRTLTY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 206 LELRSQVWLAAHALSALGLEEESAIAVDMPMNVESVIIYLAIVLAGHVVVSIADSFSPREISTRLKISKAKAIFTQDVII 285
Cdd:cd05968 95 GELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALITADGFT 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 286 RGDKSIPLYRRVVDAEAPLA----IVVPARGSSCRMKLREKDLSWNNFLgnARNLRGVEYVAAEKPagayTNILFSSGTT 361
Cdd:cd05968 175 RRGREVNLKEEADKACAQCPtvekVVVVRHLGNDFTPAKGRDLSYDEEK--ETAGDGAERTESEDP----LMIIYTSGTT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 362 GEPKAIPWTNIS-PLKSAADAWCHLDVQRGDVVAWPTNLGWMMGPWLVYASLINGACMGLYNGSPLGPT---FAKFVQDA 437
Cdd:cd05968 249 GKPKGTVHVHAGfPLKAAQDMYFQFDLKPGDLLTWFTDLGWMMGPWLIFGGLILGATMVLYDGAPDHPKadrLWRMVEDH 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 438 EVSVLGVIPSIVRTW--QNSNSTSGYDWSRIRCFGSTGEASNIDEYLWL---MGRAHyKPVIEYCGGTEIGGSFISGSLL 512
Cdd:cd05968 329 EITHLGLSPTLIRALkpRGDAPVNAHDLSSLRVLGSTGEPWNPEPWNWLfetVGKGR-NPIINYSGGTEISGGILGNVLI 407
|
410 420 430
....*....|....*....|....*....|....*....
gi 1063733435 513 QPQSLAAFSTAAMGCKLFILDEDSNPIPPYaagVGELAL 551
Cdd:cd05968 408 KPIKPSSFNGPVPGMKADVLDESGKPARPE---VGELVL 443
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
161-556 |
4.73e-70 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 236.16 E-value: 4.73e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 161 KWLPGAYLNPARNCLTNGFKRRLDDIVIRWRDEgsdDLPVNTMTLLELRSQVWLAAHALSALGLEEESAIAVDMPMNVES 240
Cdd:COG0365 1 RWFVGGRLNIAYNCLDRHAEGRGDKVALIWEGE---DGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 241 VIIYLAIVLAGHVVVSIADSFSPREISTRLKISKAKAIFTQDVIIRGDKSIPLYRRVVDAEAPLA-----IVVPARGSSC 315
Cdd:COG0365 78 VIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGGLRGGKVIDLKEKVDEALEELPslehvIVVGRTGADV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 316 RMklrEKDLSWNNFLGNARNLRGVEYVAAEKPagAYtnILFSSGTTGEPKAIPWTNISPL-KSAADAWCHLDVQRGDVVA 394
Cdd:COG0365 158 PM---EGDLDWDELLAAASAEFEPEPTDADDP--LF--ILYTSGTTGKPKGVVHTHGGYLvHAATTAKYVLDLKPGDVFW 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 395 WPTNLGWMMGPW-LVYASLINGACMGLYNGSPLGPT---FAKFVQDAEVSVLGVIPSIVRTW--QNSNSTSGYDWSRIRC 468
Cdd:COG0365 231 CTADIGWATGHSyIVYGPLLNGATVVLYEGRPDFPDpgrLWELIEKYGVTVFFTAPTAIRALmkAGDEPLKKYDLSSLRL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 469 FGSTGEASNIDEYLWLmgRAHYK-PVIEYCGGTEIGGSFISGSLLQPQSLAAFSTAAMGCKLFILDEDSNPIPPyaAGVG 547
Cdd:COG0365 311 LGSAGEPLNPEVWEWW--YEAVGvPIVDGWGQTETGGIFISNLPGLPVKPGSMGKPVPGYDVAVVDEDGNPVPP--GEEG 386
|
410
....*....|..
gi 1063733435 548 ELAL---CPHMF 556
Cdd:COG0365 387 ELVIkgpWPGMF 398
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
125-580 |
2.58e-58 |
|
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: 205.12 E-value: 2.58e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 125 NPEVYWKTVLDELNILFSVPPKCILekDTSGDNPGGKWLPGAYLNPARNCLTNGFKRRLDDIVIRWrdEGSDDLPVNTMT 204
Cdd:cd17634 11 DPDTFWGEAGKILDWITPYQKVKNT--SFAPGAPSIKWFEDATLNLAANALDRHLRENGDRTAIIY--EGDDTSQSRTIS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 205 LLELRSQVWLAAHALSALGLEEESAIAVDMPMNVESVIIYLAIVLAGHVVVSIADSFSPREISTRLKISKAKAIFTQDVI 284
Cdd:cd17634 87 YRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITADGG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 285 IRGDKSIPLYRRVVDAEAPLA-----IVVPARGSSCRMKLREKDLSWNNFLGNARNLRGVEYVAAEKPAgaytNILFSSG 359
Cdd:cd17634 167 VRAGRSVPLKKNVDDALNPNVtsvehVIVLKRTGSDIDWQEGRDLWWRDLIAKASPEHQPEAMNAEDPL----FILYTSG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 360 TTGEPKAIPWTNIS-PLKSAADAWCHLDVQRGDVVAWPTNLGWMMG-PWLVYASLINGACMGLYNGSPLGPTFAKF---V 434
Cdd:cd17634 243 TTGKPKGVLHTTGGyLVYAATTMKYVFDYGPGDIYWCTADVGWVTGhSYLLYGPLACGATTLLYEGVPNWPTPARMwqvV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 435 QDAEVSVLGVIPSIVRTW--QNSNSTSGYDWSRIRCFGSTGEASNIDEYLWLMGR--AHYKPVIEYCGGTEIGGSFISG- 509
Cdd:cd17634 323 DKHGVNILYTAPTAIRALmaAGDDAIEGTDRSSLRILGSVGEPINPEAYEWYWKKigKEKCPVVDTWWQTETGGFMITPl 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063733435 510 SLLQPQSLAAFSTAAMGCKLFILDEDSNPIPPyaAGVGELALCPHMFGASSTLLnGNHFKVYFQGMPTFQG 580
Cdd:cd17634 403 PGAIELKAGSATRPVFGVQPAVVDNEGHPQPG--GTEGNLVITDPWPGQTRTLF-GDHERFEQTYFSTFKG 470
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
125-549 |
5.19e-42 |
|
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.
Pssm-ID: 341265 [Multi-domain] Cd Length: 629 Bit Score: 160.51 E-value: 5.19e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 125 NPEVYWKTVLDELNILFSVPPKCILEkdTSGDNPGGKWLPGAYLNPARNCLTNgfKRRLDDIVI-RWRDEGSDDLpvntm 203
Cdd:cd05943 29 DPGAFWAAVWDFSGVRGSKPYDVVVV--SGRIMPGARWFPGARLNYAENLLRH--ADADDPAAIyAAEDGERTEV----- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 204 TLLELRSQVWLAAHALSALGLEEESAIAVDMPMNVESVIIYLAIVLAGHVVVSIADSFSPREISTRLKISKAKAIFTQDV 283
Cdd:cd05943 100 TWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFGVPGVLDRFGQIEPKVLFAVDA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 284 IIRGDKSIPLYRRV--VDAEAP---LAIVVPARGSSCRMKLRE--KDLSWNNFLGNARnlrGVEYVAAEKPAGAYTNILF 356
Cdd:cd05943 180 YTYNGKRHDVREKVaeLVKGLPsllAVVVVPYTVAAGQPDLSKiaKALTLEDFLATGA---AGELEFEPLPFDHPLYILY 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 357 SSGTTGEPKAI----PWTNISPLKSAAdawCHLDVQRGDVVAWPTNLGWMMGPWLVyASLINGACMGLYNGSPLGPTFA- 431
Cdd:cd05943 257 SSGTTGLPKCIvhgaGGTLLQHLKEHI---LHCDLRPGDRLFYYTTCGWMMWNWLV-SGLAVGATIVLYDGSPFYPDTNa 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 432 --KFVQDAEVSVLGVIPSIVRTWQNSNSTSG--YDWSRIRCFGSTGEASNIDEYLWLmgRAHYKPVIEYC---GGTEIGG 504
Cdd:cd05943 333 lwDLADEEGITVFGTSAKYLDALEKAGLKPAetHDLSSLRTILSTGSPLKPESFDYV--YDHIKPDVLLAsisGGTDIIS 410
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1063733435 505 SFISGSLLQPQSLAAFSTAAMGCKLFILDEDSNPIPpyaAGVGEL 549
Cdd:cd05943 411 CFVGGNPLLPVYRGEIQCRGLGMAVEAFDEEGKPVW---GEKGEL 452
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
125-549 |
1.67e-39 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 153.41 E-value: 1.67e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 125 NPEVYWKTVLDELNILFSVPPKCILEKDTSgdnPGGKWLPGAYLNPARNCLTNgfkRRLDDIVIRWRDEgsdDLPVNTMT 204
Cdd:PRK03584 46 DLEAFWQSVWDFFGVIGSTPYTVVLAGRRM---PGARWFPGARLNYAENLLRH---RRDDRPAIIFRGE---DGPRRELS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 205 LLELRSQVWLAAHALSALGLEEESAIAVDMPMNVESVIIYLAIVLAGHVVVSIADSFSPREISTRLKISKAKAIFTQD-- 282
Cdd:PRK03584 117 WAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLGAIWSSCSPDFGVQGVLDRFGQIEPKVLIAVDgy 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 283 -----VIIRGDKsiplYRRVVDAEAPL--AIVVPARGSSCRMKLREKDLSWNNFLGNARNlRGVEY--VAAEKPAgaYtn 353
Cdd:PRK03584 197 ryggkAFDRRAK----VAELRAALPSLehVVVVPYLGPAAAAAALPGALLWEDFLAPAEA-AELEFepVPFDHPL--W-- 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 354 ILFSSGTTGEPKAI----PWTNISPLKSAAdawCHLDVQRGDVVAWPTNLGWMMGPWLVyASLINGACMGLYNGSPLGPT 429
Cdd:PRK03584 268 ILYSSGTTGLPKCIvhghGGILLEHLKELG---LHCDLGPGDRFFWYTTCGWMMWNWLV-SGLLVGATLVLYDGSPFYPD 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 430 FA---KFVQDAEVSVLGVIPSIVRTWQNSNSTSG--YDWSRIRCFGSTGEASNIDEYLWLmgRAHYKP---VIEYCGGTE 501
Cdd:PRK03584 344 PNvlwDLAAEEGVTVFGTSAKYLDACEKAGLVPGetHDLSALRTIGSTGSPLPPEGFDWV--YEHVKAdvwLASISGGTD 421
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1063733435 502 IGGSFISGSLLQPQSLAAFSTAAMGCKLFILDEDSNPIppyAAGVGEL 549
Cdd:PRK03584 422 ICSCFVGGNPLLPVYRGEIQCRGLGMAVEAWDEDGRPV---VGEVGEL 466
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
125-546 |
1.63e-31 |
|
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: 129.22 E-value: 1.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 125 NPEVYWKTVLDELNilFSVPPKCILekDTSGDNPGGKWLPGAYLNPARNCLTNGFKRRLDDIVIRW-RDEGSDDlpvNTM 203
Cdd:cd05966 13 DPEEFWGEIAKELD--WFKPWDKVL--DWSKGPPFIKWFEGGKLNISYNCLDRHLKERGDKVAIIWeGDEPDQS---RTI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 204 TLLELRSQVWLAAHALSALGLEEESAIAVDMPMNVESVIIYLAIVLAG--HVVVSIAdsFSPREISTRLKISKAKAIFTQ 281
Cdd:cd05966 86 TYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGavHSVVFAG--FSAESLADRINDAQCKLVITA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 282 DVIIRGDKSIPLyRRVVDA---EAPL---AIVVPARGSSCRMKlREKDLSWNNFLGNARNLRGVEYVAAEKPAgaytNIL 355
Cdd:cd05966 164 DGGYRGGKVIPL-KEIVDEaleKCPSvekVLVVKRTGGEVPMT-EGRDLWWHDLMAKQSPECEPEWMDSEDPL----FIL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 356 FSSGTTGEPKAIPWTNISPLksaadAWCHL------DVQRGDVVaWPT-NLGWMMG-PWLVYASLINGACMGLYNGSPLG 427
Cdd:cd05966 238 YTSGSTGKPKGVVHTTGGYL-----LYAATtfkyvfDYHPDDIY-WCTaDIGWITGhSYIVYGPLANGATTVMFEGTPTY 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 428 PTFAKF---VQDAEVSVLGVIPSIVRTW--QNSNSTSGYDWSRIRCFGSTGEASNIDEYLWlmgrahYKPVIeycGG--- 499
Cdd:cd05966 312 PDPGRYwdiVEKHKVTIFYTAPTAIRALmkFGDEWVKKHDLSSLRVLGSVGEPINPEAWMW------YYEVI---GKerc 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1063733435 500 --------TEIGGSFIS---GSL-LQPQSlAAFSTaaMGCKLFILDEDSNPIPPYAAGV 546
Cdd:cd05966 383 pivdtwwqTETGGIMITplpGATpLKPGS-ATRPF--FGIEPAILDEEGNEVEGEVEGY 438
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
207-549 |
2.29e-31 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 126.27 E-value: 2.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 207 ELRSQVWLAAHALSALGLEEESAIAVDMPMNVESVIIYLAIVLAGHVVVSIADSFSPREISTRLKISKAKAIFTQDVIIr 286
Cdd:pfam00501 26 ELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSGAKVLITDDALK- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 287 gdksIPLYRRVVDAEAPLAIVVPARGSSCRMKLREKDLSWNNFLGNARnlrgVEYVAAEKPAgaytNILFSSGTTGEPKA 366
Cdd:pfam00501 105 ----LEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPPP----PPPPDPDDLA----YIIYTSGTTGKPKG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 367 IPWTNISPLKSAADAW----CHLDVQRGDVVAWPTNLGWMMG-PWLVYASLINGACMGLYNGSPL--GPTFAKFVQDAEV 439
Cdd:pfam00501 173 VMLTHRNLVANVLSIKrvrpRGFGLGPDDRVLSTLPLFHDFGlSLGLLGPLLAGATVVLPPGFPAldPAALLELIERYKV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 440 SVLGVIPSIVRTWQNSNSTSGYDWSRIRCFGSTGEASNIDEYLWLmgRAHYKPVIEYCGG-TEiGGSFISGSLLQPQSLA 518
Cdd:pfam00501 253 TVLYGVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELARRF--RELFGGALVNGYGlTE-TTGVVTTPLPLDEDLR 329
|
330 340 350
....*....|....*....|....*....|....*
gi 1063733435 519 AFSTA---AMGCKLFILDEDS-NPIPPYAagVGEL 549
Cdd:pfam00501 330 SLGSVgrpLPGTEVKIVDDETgEPVPPGE--PGEL 362
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
125-576 |
1.20e-30 |
|
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.
Pssm-ID: 341271 [Multi-domain] Cd Length: 617 Bit Score: 126.66 E-value: 1.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 125 NPEVYWKTVLDELNilFSVPPKCILEkdtsGDNPG-GKWLPGAYLNPARNCLTNGFKR-RLDDIVIRWrdegsdDLPV-- 200
Cdd:cd05967 11 EPEAFWAEQARLID--WFKPPEKILD----NSNPPfTRWFVGGRLNTCYNALDRHVEAgRGDQIALIY------DSPVtg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 201 --NTMTLLELRSQVWLAAHALSALGLEEESAIAVDMPMNVESVIIYLAIVLAG--HVVVsiADSFSPREISTRLKISKAK 276
Cdd:cd05967 79 teRTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGaiHSVV--FGGFAAKELASRIDDAKPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 277 AIFTQDVIIRGDKSIPlYRRVVDAEAPLAIVVPA------RGS-SCRMKLREKDLSWNNFLGNARNlRGVEYVAAEKPag 349
Cdd:cd05967 157 LIVTASCGIEPGKVVP-YKPLLDKALELSGHKPHhvlvlnRPQvPADLTKPGRDLDWSELLAKAEP-VDCVPVAATDP-- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 350 AYtnILFSSGTTGEPKAIPWTNISPLKSAADAWCHL-DVQRGDVVAWPTNLGWMMG-PWLVYASLINGACMGLYNGSPLG 427
Cdd:cd05967 233 LY--ILYTSGTTGKPKGVVRDNGGHAVALNWSMRNIyGIKPGDVWWAASDVGWVVGhSYIVYGPLLHGATTVLYEGKPVG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 428 -P---TFAKFVQDAEVSVLGVIPSIVRTWQ----NSNSTSGYDWSRIRCFGSTGEASNIDEYLWLMgRAHYKPVIEYCGG 499
Cdd:cd05967 311 tPdpgAFWRVIEKYQVNALFTAPTAIRAIRkedpDGKYIKKYDLSSLRTLFLAGERLDPPTLEWAE-NTLGVPVIDHWWQ 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 500 TEiGGSFISGSL--LQPQSLAAFST--AAMGCKLFILDEDSNPIPPYAAG--VGELALCPhmfGASSTLLNgNH--FK-V 570
Cdd:cd05967 390 TE-TGWPITANPvgLEPLPIKAGSPgkPVPGYQVQVLDEDGEPVGPNELGniVIKLPLPP---GCLLTLWK-NDerFKkL 464
|
....*.
gi 1063733435 571 YFQGMP 576
Cdd:cd05967 465 YLSKFP 470
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
125-545 |
2.30e-24 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 107.53 E-value: 2.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 125 NPEVYWKTVLDELNilFSVPPKCILEKDtsgdNPGGKWLPGAYLNPARNCLTNGFKRRLDDIVIRWrdEGSDDLPVNTMT 204
Cdd:PRK00174 29 DPEGFWAEQAKRLD--WFKPFDTVLDWN----APFIKWFEDGELNVSYNCLDRHLKTRGDKVAIIW--EGDDPGDSRKIT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 205 LLELRSQVWLAAHALSALGLEEESAIAVDMPMNVESVIIYLA---------IVLAGhvvvsiadsFSPREISTRLKISKA 275
Cdd:PRK00174 101 YRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLAcarigavhsVVFGG---------FSAEALADRIIDAGA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 276 KAIFTQDVIIRGDKSIPLyRRVVDaEApLA--------IVVPARGSSCRMKlREKDLSWNNFLGNARNLRGVEYVAAEKP 347
Cdd:PRK00174 172 KLVITADEGVRGGKPIPL-KANVD-EA-LAncpsvekvIVVRRTGGDVDWV-EGRDLWWHELVAGASDECEPEPMDAEDP 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 348 agayTNILFSSGTTGEPKAIpwtnispLKSAAD--AWCHL------DVQRGDVVaWPT-NLGWMMG-PWLVYASLINGAC 417
Cdd:PRK00174 248 ----LFILYTSGSTGKPKGV-------LHTTGGylVYAAMtmkyvfDYKDGDVY-WCTaDVGWVTGhSYIVYGPLANGAT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 418 MGLYNGSPLGPT---FAKFVQDAEVSVLGVIPSIVRTW--QNSNSTSGYDWSRIRCFGSTGEASNIDEYLWlmgrahYKP 492
Cdd:PRK00174 316 TLMFEGVPNYPDpgrFWEVIDKHKVTIFYTAPTAIRALmkEGDEHPKKYDLSSLRLLGSVGEPINPEAWEW------YYK 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063733435 493 VIeycGG-----------TEIGGSFIS----------GSLLQPqslaafstaamgckLF-----ILDEDSNPIPPYAAG 545
Cdd:PRK00174 390 VV---GGercpivdtwwqTETGGIMITplpgatplkpGSATRP--------------LPgiqpaVVDEEGNPLEGGEGG 451
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
180-556 |
1.33e-21 |
|
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: 97.96 E-value: 1.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 180 KRRLDDIVIRWRDEgsddlpvnTMTLLELRSQVWLAAHALSALGLEEESAIAVDMPMNVESVIIYLAIVLAGHVVVSIAD 259
Cdd:COG0318 10 ARHPDRPALVFGGR--------RLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 260 SFSPREISTRLKISKAKAIFTqdviirgdksiplyrrvvdaeaplaivvpargsscrmklrekdlswnnflgnarnlrgv 339
Cdd:COG0318 82 RLTAEELAYILEDSGARALVT----------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 340 eyvaaekpagAYtnILFSSGTTGEPKAIPWTNISPLKSAADAWCHLDVQRGDVVAWPTNL----GWMMGPWlvyASLING 415
Cdd:COG0318 103 ----------AL--ILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLfhvfGLTVGLL---APLLAG 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 416 ACMGLYnGSPLGPTFAKFVQDAEVSVLGVIPSIVRTWQNSNSTSGYDWSRIRCFGSTGEASN---IDEYLWLMGRahykP 492
Cdd:COG0318 168 ATLVLL-PRFDPERVLELIERERVTVLFGVPTMLARLLRHPEFARYDLSSLRLVVSGGAPLPpelLERFEERFGV----R 242
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063733435 493 VIEYCGGTEIGGsFISGSLLQPQSLAAFS--TAAMGCKLFILDEDSNPIPPYAagVGELALC-PHMF 556
Cdd:COG0318 243 IVEGYGLTETSP-VVTVNPEDPGERRPGSvgRPLPGVEVRIVDEDGRELPPGE--VGEIVVRgPNVM 306
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
127-539 |
1.60e-20 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 95.73 E-value: 1.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 127 EVYWKTVLDElnilfsvPPKCILEKDTSGDNPGGKWLPGAYLNPARNCLTNGFKR-RLDDIVIRWrdEGSDDLPVNTMTL 205
Cdd:PLN02654 53 QFYWKQKWEG-------DEVCSENLDVRKGPISIEWFKGGKTNICYNCLDRNVEAgNGDKIAIYW--EGNEPGFDASLTY 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 206 LELRSQVWLAAHALSALGLEEESAIAVDMPMNVESVIIYLAIVLAGHVVVSIADSFSPREISTRLKISKAKAIFTQDVII 285
Cdd:PLN02654 124 SELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVITCNAVK 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 286 RGDKSIPLyRRVVDAeaplAIVVPAR-GSSCRMKL---------RE-------KDLSWNNFLGNARNLRGVEYVAAEKPa 348
Cdd:PLN02654 204 RGPKTINL-KDIVDA----ALDESAKnGVSVGICLtyenqlamkREdtkwqegRDVWWQDVVPNYPTKCEVEWVDAEDP- 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 349 gayTNILFSSGTTGEPKAIPWTNISPLKSAADAWCH-LDVQRGDVVAWPTNLGWMMG-PWLVYASLINGACMGLYNGSPL 426
Cdd:PLN02654 278 ---LFLLYTSGSTGKPKGVLHTTGGYMVYTATTFKYaFDYKPTDVYWCTADCGWITGhSYVTYGPMLNGATVLVFEGAPN 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 427 GPTFAK---FVQDAEVSVLGVIPSIVRTWQNSNSTSGYDWSR--IRCFGSTGEASNIDEYLW---LMGRAHYkPVIEYCG 498
Cdd:PLN02654 355 YPDSGRcwdIVDKYKVTIFYTAPTLVRSLMRDGDEYVTRHSRksLRVLGSVGEPINPSAWRWffnVVGDSRC-PISDTWW 433
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1063733435 499 GTEIGGSFIS---GSLLQPQSLAAFSTaaMGCKLFILDEDSNPI 539
Cdd:PLN02654 434 QTETGGFMITplpGAWPQKPGSATFPF--FGVQPVIVDEKGKEI 475
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
207-551 |
2.98e-20 |
|
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.
Pssm-ID: 341276 [Multi-domain] Cd Length: 428 Bit Score: 93.56 E-value: 2.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 207 ELRSQVWLAAHALSALGLEEESAIAVDMPMNVESVIIYLAIVLAGHVVVSIADSFSPREISTRLKISKAKAIftqdviir 286
Cdd:cd05972 5 ELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAI-------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 287 gdksiplyrrVVDAEAPLAIvvpargsscrmklrekdlswnnflgnarnlrgveyvaaekpagaytniLFSSGTTGEPKA 366
Cdd:cd05972 77 ----------VTDAEDPALI------------------------------------------------YFTSGTTGLPKG 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 367 IPWTNISPLKSAADAWCHLDVQRGDVVAWPTNLGWMMGPWL-VYASLINGACMGLYNGSPLGPTFA-KFVQDAEVSVLGV 444
Cdd:cd05972 99 VLHTHSYPLGHIPTAAYWLGLRPDDIHWNIADPGWAKGAWSsFFGPWLLGATVFVYEGPRFDAERIlELLERYGVTSFCG 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 445 IPSIVRTWQNSNsTSGYDWSRIRCFGSTGEASNIDEYLWlmGRAHYK-PVIEYCGGTEIgGSFISGSLLQPQSLAAFSTA 523
Cdd:cd05972 179 PPTAYRMLIKQD-LSSYKFSHLRLVVSAGEPLNPEVIEW--WRAATGlPIRDGYGQTET-GLTVGNFPDMPVKPGSMGRP 254
|
330 340
....*....|....*....|....*...
gi 1063733435 524 AMGCKLFILDEDSNPIPPYAagVGELAL 551
Cdd:cd05972 255 TPGYDVAIIDDDGRELPPGE--EGDIAI 280
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
202-473 |
4.50e-20 |
|
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: 93.43 E-value: 4.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 202 TMTLLELRSQVWLAAHALSALGLEEESAIAVDMPMNVESVIIYLAIVLAGHVVVSIADSFSPREISTRLKISKAKAIFT- 280
Cdd:cd05911 10 ELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTd 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 281 ---QDVIIRGDKSIPLYRRVvdaeaplaIVVPARGSSCrmkLREKDLSWNNFLGNARNLRGVEYVAAEKPAGaytnILFS 357
Cdd:cd05911 90 pdgLEKVKEAAKELGPKDKI--------IVLDDKPDGV---LSIEDLLSPTLGEEDEDLPPPLKDGKDDTAA----ILYS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 358 SGTTGEPKAIPWTN---ISPLKSAADAWCHLDvQRGDVVAWPTNLGWMMGPWLVYASLINGACM-GLYNGSPLgpTFAKF 433
Cdd:cd05911 155 SGTTGLPKGVCLSHrnlIANLSQVQTFLYGND-GSNDVILGFLPLYHIYGLFTTLASLLNGATViIMPKFDSE--LFLDL 231
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1063733435 434 VQDAEVSVLGVIPSIVRTWQNSNSTSGYDWSRIRCFGSTG 473
Cdd:cd05911 232 IEKYKITFLYLVPPIAAALAKSPLLDKYDLSSLRVILSGG 271
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
202-476 |
5.21e-19 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 90.35 E-value: 5.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 202 TMTLLELRSQVWLAAHALSALGLEEESAIAVDMPMNVESVIIYLAIVLAGHVVVSIADSFSPREISTRLKISKAKAIFTQ 281
Cdd:PRK07656 30 RLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYILARGDAKALFVL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 282 D----VIIRGDKSIPLYRRVVdaeaplaiVVPARGSSCrmkLREKDLSWNNFLGNARNLRGVEYVAAEKPAgaytNILFS 357
Cdd:PRK07656 110 GlflgVDYSATTRLPALEHVV--------ICETEEDDP---HTEKMKTFTDFLAAGDPAERAPEVDPDDVA----DILFT 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 358 SGTTGEPKAIPWTNISPLkSAADAWCH-LDVQRGD--VVAWPT--NLGWMMGpWLvyASLINGACMglyngSPLgPTFA- 431
Cdd:PRK07656 175 SGTTGRPKGAMLTHRQLL-SNAADWAEyLGLTEGDryLAANPFfhVFGYKAG-VN--APLMRGATI-----LPL-PVFDp 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1063733435 432 ----KFVQDAEVSVLGVIPSIVRTWQNSNSTSGYDWSRIRcFGSTGEAS 476
Cdd:PRK07656 245 devfRLIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLR-LAVTGAAS 292
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
354-551 |
8.43e-19 |
|
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: 87.73 E-value: 8.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 354 ILFSSGTTGEPKAIPWTNISPLKSAADAWCHLDVQRGDVVAWPTNLGWMMGPWLVYASLINGACMGLYNGSPLGpTFAKF 433
Cdd:cd04433 5 ILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKFDPE-AALEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 434 VQDAEVSVLGVIPSIVRTWQNSNSTSGYDWSRIRCFGSTGEASNIDEYLWLMGRAHYKPVIEYcGGTEIGGSFISGSLLQ 513
Cdd:cd04433 84 IEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLERFEEAPGIKLVNGY-GLTETGGTVATGPPDD 162
|
170 180 190
....*....|....*....|....*....|....*....
gi 1063733435 514 PQSLAAFS-TAAMGCKLFILDEDSNPIPPYaaGVGELAL 551
Cdd:cd04433 163 DARKPGSVgRPVPGVEVRIVDPDGGELPPG--EIGELVV 199
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
215-574 |
1.34e-15 |
|
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: 79.47 E-value: 1.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 215 AAHALSALGLEEESAIAVDMPMNVESVIIYLAIVLAGHVVVSIADSFSPREISTRLKISKAK-AIFTQDVIIRGDKSIPL 293
Cdd:cd05969 13 FANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKvLITTEELYERTDPEDPT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 294 YrrvvdaeaplaivvpargsscrmklrekdlswnnflgnarnlrgveyvaaekpagaytnILFSSGTTGEPKAIPWTNIS 373
Cdd:cd05969 93 L-----------------------------------------------------------LHYTSGTTGTPKGVLHVHDA 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 374 PLKSAADAWCHLDVQRGDVVaWPT-NLGWMMGP-WLVYASLINGACMGLYNGSPLGPTFAKFVQDAEVSVLGVIPSIVRT 451
Cdd:cd05969 114 MIFYYFTGKYVLDLHPDDIY-WCTaDPGWVTGTvYGIWAPWLNGVTNVVYEGRFDAESWYGIIERVKVTVWYTAPTAIRM 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 452 WQNSNS--TSGYDWSRIRCFGSTGEASNIDEYLWLMgRAHYKPVIEYCGGTEIGGSFISGSLLQPQSLAAFSTAAMGCKL 529
Cdd:cd05969 193 LMKEGDelARKYDLSSLRFIHSVGEPLNPEAIRWGM-EVFGVPIHDTWWQTETGSIMIANYPCMPIKPGSMGKPLPGVKA 271
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1063733435 530 FILDEDSNPIPPYAagVGELAL---CPHMFGAssTLLNGNHFKVYFQG 574
Cdd:cd05969 272 AVVDENGNELPPGT--KGILALkpgWPSMFRG--IWNDEERYKNSFID 315
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
214-549 |
8.16e-15 |
|
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: 76.54 E-value: 8.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 214 LAAHALSALGLEEESAIAVDMPMNVESVIIYLAIVLAGHVVVSIaDSFSPRE-ISTRLKISKAKAIFTQDVIirgdksip 292
Cdd:TIGR01733 12 LARHLRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPL-DPAYPAErLAFILEDAGARLLLTDSAL-------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 293 lyrRVVDAEAPLAIVVPargsscrmklrekDLSWNNFLGNArnlrGVEYVAAEKPAG---AYtnILFSSGTTGEPKAIPW 369
Cdd:TIGR01733 83 ---ASRLAGLVLPVILL-------------DPLELAALDDA----PAPPPPDAPSGPddlAY--VIYTSGSTGRPKGVVV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 370 TNISPLKSAADAWCHLDVQRGDVVAWPTNLGWMMGPWLVYASLINGACMGLYNGSPLGPTF---AKFVQDAEVSVLGVIP 446
Cdd:TIGR01733 141 THRSLVNLLAWLARRYGLDPDDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAallAALIAEHPVTVLNLTP 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 447 SIVRTWQNSNSTSGydwSRIRCFGSTGEASNIDEYLWLMGRAHYKPVI-EYcGGTEigGSFISGSLLQPQSLAAFSTAAM 525
Cdd:TIGR01733 221 SLLALLAAALPPAL---ASLRLVILGGEALTPALVDRWRARGPGARLInLY-GPTE--TTVWSTATLVDPDDAPRESPVP 294
|
330 340 350
....*....|....*....|....*....|
gi 1063733435 526 ------GCKLFILDEDSNPIPPyaAGVGEL 549
Cdd:TIGR01733 295 igrplaNTRLYVLDDDLRPVPV--GVVGEL 322
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
162-556 |
2.06e-13 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 73.01 E-value: 2.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 162 WLPGAYLNPARNCL---TNGFKRrlDDIVIRWRDEGSDDlpvnTMTLLELRSQVWLAAHALSALGLEEESAIAVDMPMNV 238
Cdd:PRK04319 36 WLETGKVNIAYEAIdrhADGGRK--DKVALRYLDASRKE----KYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIP 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 239 ESVIIYLAIVLAGHVVVSIADSFSPREISTRLKISKAKAIFTQDviirgdksiPLYRRVVDAEAP---LAIVVPARGSsc 315
Cdd:PRK04319 110 ELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLITTP---------ALLERKPADDLPslkHVLLVGEDVE-- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 316 rmkLREKDLSWNNFLGNARNLRGVEYVAAEKPAgaytnIL-FSSGTTGEPK-AIPWTNISPLKSAADAWChLDVQRGDVV 393
Cdd:PRK04319 179 ---EGPGTLDFNALMEQASDEFDIEWTDREDGA-----ILhYTSGSTGKPKgVLHVHNAMLQHYQTGKYV-LDLHEDDVY 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 394 aWPT-NLGWMMG-------PWLvyasliNGACMGLYNGSPLGPTFAKFVQDAEVSVLGVIPSIVRTWQNSNS--TSGYDW 463
Cdd:PRK04319 250 -WCTaDPGWVTGtsygifaPWL------NGATNVIDGGRFSPERWYRILEDYKVTVWYTAPTAIRMLMGAGDdlVKKYDL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 464 SRIRCFGSTGEASNIDEYLWLMgRAHYKPVIEYCGGTEIGGSFISgsllqpqslaafSTAAM------------GCKLFI 531
Cdd:PRK04319 323 SSLRHILSVGEPLNPEVVRWGM-KVFGLPIHDNWWMTETGGIMIA------------NYPAMdikpgsmgkplpGIEAAI 389
|
410 420
....*....|....*....|....*...
gi 1063733435 532 LDEDSNPIPPYAagVGELAL---CPHMF 556
Cdd:PRK04319 390 VDDQGNELPPNR--MGNLAIkkgWPSMM 415
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
144-546 |
2.53e-13 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 72.67 E-value: 2.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 144 PPKCILEKDtsgDNPGGKWLPGAYLNPARNCLTNGFKRRLDDIVIRWRDEGSDDlpVNTMTLLELRSQVWLAAHALSALG 223
Cdd:PRK10524 31 PFTQVLDYS---NPPFARWFVGGRTNLCHNAVDRHLAKRPEQLALIAVSTETDE--ERTYTFRQLHDEVNRMAAMLRSLG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 224 LEEESAIAVDMPMNVESVIIYLAIVLAG--HVVVsiADSFSPREISTRLKISKAKAIFTQDVIIRGDKSIPlYRRVVDAE 301
Cdd:PRK10524 106 VQRGDRVLIYMPMIAEAAFAMLACARIGaiHSVV--FGGFASHSLAARIDDAKPVLIVSADAGSRGGKVVP-YKPLLDEA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 302 APLAIVVPA------RGSSCRMKLREKDLSWNNflgnarnLRG--------VEYVAAEKPAgaYtnILFSSGTTGEPK-- 365
Cdd:PRK10524 183 IALAQHKPRhvllvdRGLAPMARVAGRDVDYAT-------LRAqhlgarvpVEWLESNEPS--Y--ILYTSGTTGKPKgv 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 366 -------AIpwtnisPLKSAADawcHL-DVQRGDVVAWPTNLGWMMG-PWLVYASLINGACMGLYNGSPLGPTFA---KF 433
Cdd:PRK10524 252 qrdtggyAV------ALATSMD---TIfGGKAGETFFCASDIGWVVGhSYIVYAPLLAGMATIMYEGLPTRPDAGiwwRI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 434 VQDAEVSVLGVIPSIVRTW--QNSNSTSGYDWSRIRCFGSTGEAsnIDE--YLWLMGrAHYKPVIEYCGGTEIGGSFIS- 508
Cdd:PRK10524 323 VEKYKVNRMFSAPTAIRVLkkQDPALLRKHDLSSLRALFLAGEP--LDEptASWISE-ALGVPVIDNYWQTETGWPILAi 399
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1063733435 509 --GSLLQPQSLAAFSTAAMGCKLFILDE-DSNPIPPYAAGV 546
Cdd:PRK10524 400 arGVEDRPTRLGSPGVPMYGYNVKLLNEvTGEPCGPNEKGV 440
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
202-551 |
9.19e-13 |
|
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: 70.63 E-value: 9.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 202 TMTLLELRSQVWLAAHALSALGLEEESAIAVDMPMNVESVIIYLAIVLAGHVVVSIADSFSPREISTRLKISKAKAIFTQ 281
Cdd:cd05930 12 SLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYILEDSGAKLVLTD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 282 dviirgdksiplyrrvvdaeaplaivvpargsscrmklrekdlswnnflgnARNLrgveyvaaekpagAYtnILFSSGTT 361
Cdd:cd05930 92 ---------------------------------------------------PDDL-------------AY--VIYTSGST 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 362 GEPK--AIPWTNISPLksAADAWCHLDVQRGDVVAWPTNLGWMMGPWLVYASLINGACmgLYNGSP----LGPTFAKFVQ 435
Cdd:cd05930 106 GKPKgvMVEHRGLVNL--LLWMQEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGAT--LVVLPEevrkDPEALADLLA 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 436 DAEVSVLGVIPSIVRTWQNSNSTSGYDWSRIRCFGstGEASNiDEYLWLMGRAHYKPVIEYCGG-TEIGGSFISGSLLQP 514
Cdd:cd05930 182 EEGITVLHLTPSLLRLLLQELELAALPSLRLVLVG--GEALP-PDLVRRWRELLPGARLVNLYGpTEATVDATYYRVPPD 258
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1063733435 515 QSLAAFST---AAMGCKLFILDEDSNPIPPyaaGV-GELAL 551
Cdd:cd05930 259 DEEDGRVPigrPIPNTRVYVLDENLRPVPP---GVpGELYI 296
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
211-467 |
4.83e-11 |
|
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: 65.43 E-value: 4.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 211 QVWLAAHALSALgLEEESA----IAVDMPMNVESVIIYLAIVLAGHVVVSIADSFSPREISTRLKISKAKAIFTQDVIIR 286
Cdd:cd05909 12 KLLTGAIALARK-LAKMTKegenVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLTSKQFIE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 287 GDKSIPLyrrvVDAEAPLAIV----VPARGS---SCR----MKLREKDLSWNNFLGNarnlrgveyVAAEKPAgaytNIL 355
Cdd:cd05909 91 KLKLHHL----FDVEYDARIVyledLRAKISkadKCKaflaGKFPPKWLLRIFGVAP---------VQPDDPA----VIL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 356 FSSGTTGEPKAIPWTNISPLKSAADAWCHLDVQRGDVV--AWP-------TNLGWM---MGPWLVYASlingacmglyng 423
Cdd:cd05909 154 FTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVfgALPffhsfglTGCLWLpllSGIKVVFHP------------ 221
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1063733435 424 SPLGP-TFAKFVQDAEVSVLGVIPS----IVRTWQNsnstsgYDWSRIR 467
Cdd:cd05909 222 NPLDYkKIPELIYDKKATILLGTPTflrgYARAAHP------EDFSSLR 264
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
207-371 |
7.39e-10 |
|
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: 61.56 E-value: 7.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 207 ELRSQVWLAAHALSALGLEEESAIAVDMPMNVESVIIYLAIVLAGHVVVSIADSFSPREISTRLKISKAKAIFTQDV--- 283
Cdd:cd05926 19 DLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVLTPKGelg 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 284 -IIRGDKSIPLYRRVVDAEAPLAIVVPargsscrmklREKDLSWNNFLGNARNLRGVeyvaAEKPAGAYtnILFSSGTTG 362
Cdd:cd05926 99 pASRAASKLGLAILELALDVGVLIRAP----------SAESLSNLLADKKNAKSEGV----PLPDDLAL--ILHTSGTTG 162
|
....*....
gi 1063733435 363 EPKAIPWTN 371
Cdd:cd05926 163 RPKGVPLTH 171
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
180-442 |
8.92e-10 |
|
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: 61.06 E-value: 8.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 180 KRRLDDIVIRWRDEgsddlpvnTMTLLELRSQVWLAAHALSALGLEEESAIAVDMPMNVESVIIYLAIVLAGHVVVSIAD 259
Cdd:cd12117 8 ARTPDAVAVVYGDR--------SLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 260 SFSPREISTRLKISKAKAIFTQDviirgdksiPLYRRVVDAEAPLAIVVPARGsscrmklrekdlswnnflGNARNLRGV 339
Cdd:cd12117 80 ELPAERLAFMLADAGAKVLLTDR---------SLAGRAGGLEVAVVIDEALDA------------------GPAGNPAVP 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 340 eyVAAEKPAgaytNILFSSGTTGEPKAIPWTNISPLKSAADAWcHLDVQRGDVVAWPTNLGWMMGPWLVYASLINGACMG 419
Cdd:cd12117 133 --VSPDDLA----YVMYTSGSTGRPKGVAVTHRGVVRLVKNTN-YVTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLV 205
|
250 260
....*....|....*....|....*
gi 1063733435 420 LYN-GSPLGPT-FAKFVQDAEVSVL 442
Cdd:cd12117 206 LAPkGTLLDPDaLGALIAEEGVTVL 230
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
180-430 |
9.57e-10 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 61.27 E-value: 9.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 180 KRRLDDIVIRWRDEGsddlPVNTMTLLELRSQVWLAAHALSALGLEEESAIAVDMPMNVESVIIYLAIVLAGHVVVSIAD 259
Cdd:COG1022 22 ARFPDRVALREKEDG----IWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVPIYP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 260 SFSPREISTRLKISKAKAIFTQD-----VIIRGDKSIPLYRRVV--DAEAplaivvpargsscrMKLREKDLSWNNFLGN 332
Cdd:COG1022 98 TSSAEEVAYILNDSGAKVLFVEDqeqldKLLEVRDELPSLRHIVvlDPRG--------------LRDDPRLLSLDELLAL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 333 ARNLRGVEYVAAEKPAGAYT---NILFSSGTTGEPKAIPWT--NISplkSAADAWCH-LDVQRGDVV-AW-PtnLGWMMG 404
Cdd:COG1022 164 GREVADPAELEARRAAVKPDdlaTIIYTSGTTGRPKGVMLThrNLL---SNARALLErLPLGPGDRTlSFlP--LAHVFE 238
|
250 260 270
....*....|....*....|....*....|....*
gi 1063733435 405 PWLVYASLINGACMGlYNGSP---------LGPTF 430
Cdd:COG1022 239 RTVSYYALAAGATVA-FAESPdtlaedlreVKPTF 272
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
202-546 |
1.42e-09 |
|
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: 60.55 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 202 TMTLLELRSQVWLAAHALSALGLEEESAIAVDMPMNVESVIIYLAIVLAGHVVVSIadsfspreiSTRLKiskakaiftq 281
Cdd:cd05919 10 SVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVI---------NPLLH---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 282 dviirgdksiplyrrvvdaeaPLAIVVPARGSSCRMKLREKDlswnnflgnarnlrgveyvaaekpAGAYtnILFSSGTT 361
Cdd:cd05919 71 ---------------------PDDYAYIARDCEARLVVTSAD------------------------DIAY--LLYSSGTT 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 362 GEPKAIPWTNISPLkSAADAWCH--LDVQRGDVV--------AWPTNlGWMMGPWLVYASLIngacmgLYNGSPLGPTFA 431
Cdd:cd05919 104 GPPKGVMHAHRDPL-LFADAMAReaLGLTPGDRVfssakmffGYGLG-NSLWFPLAVGASAV------LNPGWPTAERVL 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 432 KFVQDAEVSVLGVIPSIVRTWQNSNSTSGYDWSRIRCFGSTGEAsnIDEYLWLMGRAHY-KPVIEYCGGTEIGGSFISGs 510
Cdd:cd05919 176 ATLARFRPTVLYGVPTFYANLLDSCAGSPDALRSLRLCVSAGEA--LPRGLGERWMEHFgGPILDGIGATEVGHIFLSN- 252
|
330 340 350
....*....|....*....|....*....|....*...
gi 1063733435 511 llQPQSLAAFSTAAM--GCKLFILDEDSNPIPPYAAGV 546
Cdd:cd05919 253 --RPGAWRLGSTGRPvpGYEIRLVDEEGHTIPPGEEGD 288
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
207-541 |
1.72e-09 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 60.56 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 207 ELRSQVWLAAHALS-ALGLEEESAIAVDMPMNVESVIIYLAIVLAGHVVVSIADSFSPREISTRLKISKAKAIFTQDVIi 285
Cdd:cd05928 46 ELGSLSRKAANVLSgACGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSDEL- 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 286 rgdksiplyrrvvdaeAPLAIVVPARGSSCRMKLREKDLSWNNFLgnarNLRGVEYVAAEKPAGAYTN------ILFSSG 359
Cdd:cd05928 125 ----------------APEVDSVASECPSLKTKLLVSEKSRDGWL----NFKELLNEASTEHHCVETGsqepmaIYFTSG 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 360 TTGEPKAIPWTNIS---PLKSAADAWchLDVQRGDVVAWPTNLGWMMGPW-LVYASLINGACMGLYNGSPLGP-TFAKFV 434
Cdd:cd05928 185 TTGSPKMAEHSHSSlglGLKVNGRYW--LDLTASDIMWNTSDTGWIKSAWsSLFEPWIQGACVFVHHLPRFDPlVILKTL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 435 QDAEVSVLGVIPSIVRTWQNSNSTSgYDWSRIRCFGSTGEASN---IDEYLWLMGRAHYkpviEYCGGTEIG---GSFiS 508
Cdd:cd05928 263 SSYPITTFCGAPTVYRMLVQQDLSS-YKFPSLQHCVTGGEPLNpevLEKWKAQTGLDIY----EGYGQTETGlicANF-K 336
|
330 340 350
....*....|....*....|....*....|...
gi 1063733435 509 GSLLQPQSlaaFSTAAMGCKLFILDEDSNPIPP 541
Cdd:cd05928 337 GMKIKPGS---MGKASPPYDVQIIDDNGNVLPP 366
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
207-367 |
1.26e-08 |
|
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: 57.63 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 207 ELRSQVWLAAHALSALGLEEESAIAVDMPMNVESVIIYLAIVLAGhVVVSIAD-SFSPREISTRLKISKAKAIFTQDvii 285
Cdd:cd05904 37 ELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLG-AVVTTANpLSTPAEIAKQVKDSGAKLAFTTA--- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 286 rgdksiPLYRRVVDAEAPLAIVVPARGSSCRMKLREKDLSWNNflgnarnlRGVEYVAAEKPAGaytnILFSSGTTGEPK 365
Cdd:cd05904 113 ------ELAEKLASLALPVVLLDSAEFDSLSFSDLLFEADEAE--------PPVVVIKQDDVAA----LLYSSGTTGRSK 174
|
..
gi 1063733435 366 AI 367
Cdd:cd05904 175 GV 176
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
216-549 |
2.64e-08 |
|
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: 56.58 E-value: 2.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 216 AHALSALGLEEESAIAVDMPMNVESVIIYLAIVLAGHVVVSIADSFSPREISTRLKISKAKAIFTQDViirgdksiPLYR 295
Cdd:cd17651 34 AHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFMLADAGPVLVLTHPA--------LAGE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 296 RVVDAEAPLAIVVPargsscrmklrekdlSWNNFLGNARNLRgveyVAAEKPAgaYtnILFSSGTTGEPKAI-----PWT 370
Cdd:cd17651 106 LAVELVAVTLLDQP---------------GAAAGADAEPDPA----LDADDLA--Y--VIYTSGSTGRPKGVvmphrSLA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 371 NIsplksaaDAWcH---LDVQRGDVVAWPTNLGWMMGPWLVYASLINGACMGLYNGS--PLGPTFAKFVQDAEVSVLGVI 445
Cdd:cd17651 163 NL-------VAW-QaraSSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEvrTDPPALAAWLDEQRISRVFLP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 446 PSIVRTWQNSNSTSGYDWSRIRCFGSTGEASNIDEYLWLMGRAH-YKPVIEYCGGTEigGSFISGSLLQPQSLAAFSTAA 524
Cdd:cd17651 235 TVALRALAEHGRPLGVRLAALRYLLTGGEQLVLTEDLREFCAGLpGLRLHNHYGPTE--THVVTALSLPGDPAAWPAPPP 312
|
330 340 350
....*....|....*....|....*....|.
gi 1063733435 525 MG-----CKLFILDEDSNPIPPyaaGV-GEL 549
Cdd:cd17651 313 IGrpidnTRVYVLDAALRPVPP---GVpGEL 340
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
202-556 |
3.48e-08 |
|
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: 56.08 E-value: 3.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 202 TMTLLELRSQVWLAAHALSALGLEEESAIAVDMPMNVESVIIYLAIVLAGHVVVSIADSFSPREISTRLKISKAKAIFtq 281
Cdd:cd17631 20 SLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAYILADSGAKVLF-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 282 dviirgdksiplyrrvvdaeaplaivvpargsscrmklreKDLSWnnflgnarnlrgveyvaaekpagaytnILFSSGTT 361
Cdd:cd17631 98 ----------------------------------------DDLAL---------------------------LMYTSGTT 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 362 GEPKAIPWTNISPLKSAADAWCHLDVQRGDVVawptnlgwmmgpwLVYASLINGACMGLYngspLGPTFAK--------- 432
Cdd:cd17631 111 GRPKGAMLTHRNLLWNAVNALAALDLGPDDVL-------------LVVAPLFHIGGLGVF----TLPTLLRggtvvilrk 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 433 --------FVQDAEVSVLGVIPSIVRTWQNSNSTSGYDWSRIRCFGSTGEASniDEYLWLMGRAHYKPVIEYCGGTEIGG 504
Cdd:cd17631 174 fdpetvldLIERHRVTSFFLVPTMIQALLQHPRFATTDLSSLRAVIYGGAPM--PERLLRALQARGVKFVQGYGMTETSP 251
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1063733435 505 sfiSGSLLQPQS----LAAFSTAAMGCKLFILDEDSNPIPPYaaGVGELALC-PHMF 556
Cdd:cd17631 252 ---GVTFLSPEDhrrkLGSAGRPVFFVEVRIVDPDGREVPPG--EVGEIVVRgPHVM 303
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
216-545 |
5.50e-08 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 55.68 E-value: 5.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 216 AHALSALGLEEESAIAVDMPMNVESVIIYLAIVLAGHVVVSIADSFSPREISTRLKISKAKAIFTQdviirgdksiplyR 295
Cdd:PRK08276 25 AHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVLIVS-------------A 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 296 RVVDAEAPLAIVVPARGSSCRMKLREKD--LSWNNFLGNARnlrgvEYVAAEKPAGAytNILFSSGTTGEPKAI--PWTN 371
Cdd:PRK08276 92 ALADTAAELAAELPAGVPLLLVVAGPVPgfRSYEEALAAQP-----DTPIADETAGA--DMLYSSGTTGRPKGIkrPLPG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 372 ISPLksaadawchldvQRGDVVAWPTNLGWMMGPWLVYASlingaCMGLYNGSPLGptFAKFVQ------------DAE- 438
Cdd:PRK08276 165 LDPD------------EAPGMMLALLGFGMYGGPDSVYLS-----PAPLYHTAPLR--FGMSALalggtvvvmekfDAEe 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 439 ---------VSVLGVIPSI----------VRTwqnsnstsGYDWSRIRCFGSTG-------EASNIDeylWlMGrahykP 492
Cdd:PRK08276 226 alalieryrVTHSQLVPTMfvrmlklpeeVRA--------RYDVSSLRVAIHAAapcpvevKRAMID---W-WG-----P 288
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1063733435 493 VI-EYCGGTEIGGSFISGS---LLQPQSLAafstAAMGCKLFILDEDSNPIPPYAAG 545
Cdd:PRK08276 289 IIhEYYASSEGGGVTVITSedwLAHPGSVG----KAVLGEVRILDEDGNELPPGEIG 341
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
202-557 |
6.38e-08 |
|
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: 55.08 E-value: 6.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 202 TMTLLELRSQVWLAAHALSALGLEEESAIAVDMPMNVESVIIYLAIVLAGHVVVSIADSFSPREISTRLKISKAKAIFTQ 281
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 282 DViirgdksiplYRRVVDAEAPlaivvpargsscrmklrekdlswnnflgnarnlrgveyvaaekpaGAYTNILFSSGTT 361
Cdd:cd05903 81 ER----------FRQFDPAAMP---------------------------------------------DAVALLLFTSGTT 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 362 GEPKAIPWTNiSPLKSAADAWC-HLDVQRGDVVAWPTNLGWMMGpwlvyasLINGACMGLYNGSP--LGPTF-----AKF 433
Cdd:cd05903 106 GEPKGVMHSH-NTLSASIRQYAeRLGLGPGDVFLVASPMAHQTG-------FVYGFTLPLLLGAPvvLQDIWdpdkaLAL 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 434 VQDAEVSVLGVIPSIVRTWQNSNSTSGYDWSRIRCFGSTGEA--SNIDEYLWLMGRAHYKPVIeycGGTEIGGsfISGSL 511
Cdd:cd05903 178 MREHGVTFMMGATPFLTDLLNAVEEAGEPLSRLRTFVCGGATvpRSLARRAAELLGAKVCSAY---GSTECPG--AVTSI 252
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1063733435 512 LQPQSLAAFST---AAMGCKLFILDEDSNPIPPYAAGvGELALCPHMFG 557
Cdd:cd05903 253 TPAPEDRRLYTdgrPLPGVEIKVVDDTGATLAPGVEG-ELLSRGPSVFL 300
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
203-546 |
6.73e-08 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 55.22 E-value: 6.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 203 MTLLELRSQVWLAAHALSALGLEEESAIAVDMPMNVESVIIYLAIVLAGHVVVSIADSFSPREISTRLKISKAKAIftqd 282
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLV---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 283 viirgdksiplyrrVVDAEAplaivvpargsscRMKLREKDLSwnnflgnarnlrgveyvaaekpagaytnILFSSGTTG 362
Cdd:cd05973 77 --------------VTDAAN-------------RHKLDSDPFV----------------------------MMFTSGTTG 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 363 EPKAIPwtniSPLKSAAdAWCH-----LDVQRGDVVAWPTNLGWMMGpwLVYA---SLINGACMGLYNGSPLGPTFAKFV 434
Cdd:cd05973 102 LPKGVP----VPLRALA-AFGAylrdaVDLRPEDSFWNAADPGWAYG--LYYAitgPLALGHPTILLEGGFSVESTWRVI 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 435 QDAEVSVLGVIPSIVRTWQNSNSTSGYDWS-RIRCFGSTGEASNIDEYLWLmGRAHYKPVIEYCGGTEIgGSFISG--SL 511
Cdd:cd05973 175 ERLGVTNLAGSPTAYRLLMAAGAEVPARPKgRLRRVSSAGEPLTPEVIRWF-DAALGVPIHDHYGQTEL-GMVLANhhAL 252
|
330 340 350
....*....|....*....|....*....|....*
gi 1063733435 512 LQPQSLAAFSTAAMGCKLFILDEDSNPIPPYAAGV 546
Cdd:cd05973 253 EHPVHAGSAGRAMPGWRVAVLDDDGDELGPGEPGR 287
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
183-393 |
6.89e-08 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 55.44 E-value: 6.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 183 LDDIVIRWRDE------GSDDLPVNTMTLLELRSQVWLAAHALSALGLEEESAIAVDMPMNVESVIIYLAIVLAGHVVVS 256
Cdd:PRK13295 30 LDACVASCPDKtavtavRLGTGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNP 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 257 IADSFSPREISTRLKISKAKAIFTQDViIRGDKSIPLYRRVVDAEAPLAIVVPARGsscrmklrEKDLSWNNFL-----G 331
Cdd:PRK13295 110 LMPIFRERELSFMLKHAESKVLVVPKT-FRGFDHAAMARRLRPELPALRHVVVVGG--------DGADSFEALLitpawE 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063733435 332 NARNLRGVeyVAAEKP-AGAYTNILFSSGTTGEPKAI------PWTNISPLKSAadawchLDVQRGDVV 393
Cdd:PRK13295 181 QEPDAPAI--LARLRPgPDDVTQLIYTSGTTGEPKGVmhtantLMANIVPYAER------LGLGADDVI 241
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
199-549 |
1.58e-07 |
|
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: 54.30 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 199 PVNTMTLLELRSQVWLAAHALSALGLEEESAIAVDMPMNVESVIIYLAIVLAGHVVVSIADSFSPREISTRLKISKAkai 278
Cdd:cd05959 26 DAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRA--- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 279 ftqdviirgdksiplyrRVVDAEAPLAIVVPARGSSCRMKLREKDLSwnnflGNARNLRGV----EYVAAEKPAGAYTNI 354
Cdd:cd05959 103 -----------------RVVVVSGELAPVLAAALTKSEHTLVVLIVS-----GGAGPEAGAlllaELVAAEAEQLKPAAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 355 --------LFSSGTTGEPKAIPWTNiSPLKSAADAWCH--LDVQRGDVVAWPTNL--GWMMGPWLVYAsLINGACMGLYN 422
Cdd:cd05959 161 haddpafwLYSSGSTGRPKGVVHLH-ADIYWTAELYARnvLGIREDDVCFSAAKLffAYGLGNSLTFP-LSVGATTVLMP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 423 GSPLGPTFAKFVQDAEVSVLGVIPSIVRTWQNSNSTSGYDWSRIRCFGSTGEAsnIDEYLWLMGRAHYK-PVIEYCGGTE 501
Cdd:cd05959 239 ERPTPAAVFKRIRRYRPTVFFGVPTLYAAMLAAPNLPSRDLSSLRLCVSAGEA--LPAEVGERWKARFGlDILDGIGSTE 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1063733435 502 IGGSFISGsllQPQSLAAFST--AAMGCKLFILDEDSNPIPpyAAGVGEL 549
Cdd:cd05959 317 MLHIFLSN---RPGRVRYGTTgkPVPGYEVELRDEDGGDVA--DGEPGEL 361
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
207-391 |
1.72e-07 |
|
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: 54.01 E-value: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 207 ELRSQVWLAAHALSALGLEEESAIAVDMPMNVESVIIYLAIVLAGHVVVSIADSFSPREISTRLKISKAKAIFTQDviir 286
Cdd:cd05932 11 EVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFVGK---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 287 gdksiplyrrvVDAEAPLAIVVPARGSSCRMKLREK---DLSWNNFLGNARNLRGVEYVAAEKPAgaytNILFSSGTTGE 363
Cdd:cd05932 87 -----------LDDWKAMAPGVPEGLISISLPPPSAancQYQWDDLIAQHPPLEERPTRFPEQLA----TLIYTSGTTGQ 151
|
170 180
....*....|....*....|....*...
gi 1063733435 364 PKAIPWTNISPLKSAADAWCHLDVQRGD 391
Cdd:cd05932 152 PKGVMLTFGSFAWAAQAGIEHIGTEEND 179
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
173-551 |
5.54e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 52.50 E-value: 5.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 173 NCLTNGFKRRLDDIVIRWRDEGsddlpvntMTLLELRSQVWLAAHALSALGLEEESAIAVDMPMNVESVIIYLAIVLAGH 252
Cdd:PRK06187 10 RILRHGARKHPDKEAVYFDGRR--------TTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 253 VVVSIADSFSPREISTRLKISKAKAIFTqdviirGDKSIPLYRRVVDAEAPLAIVVpARGSSCRMKLREKDLSWNNFLGN 332
Cdd:PRK06187 82 VLHPINIRLKPEEIAYILNDAEDRVVLV------DSEFVPLLAAILPQLPTVRTVI-VEGDGPAAPLAPEVGEYEELLAA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 333 ARNlrgvEYVAAE-KPAGAYTnILFSSGTTGEPKAIPWT--NISPLKSAADAWchLDVQRGDVV----------AWptnl 399
Cdd:PRK06187 155 ASD----TFDFPDiDENDAAA-MLYTSGTTGHPKGVVLShrNLFLHSLAVCAW--LKLSRDDVYlvivpmfhvhAW---- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 400 GWMMGPWLVYASLIngaCMGLYNGSPLgptfAKFVQDAEVSVLGVIPSIvrtWQ---NSNSTSGYDWSRIRCFGSTGEA- 475
Cdd:PRK06187 224 GLPYLALMAGAKQV---IPRRFDPENL----LDLIETERVTFFFAVPTI---WQmllKAPRAYFVDFSSLRLVIYGGAAl 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 476 --SNIDEYLWLMGRahykPVIEYCGGTEIGGSfISGSLLQPQSLAAFS------TAAMGCKLFILDEDSNPIPPYAAGVG 547
Cdd:PRK06187 294 ppALLREFKEKFGI----DLVQGYGMTETSPV-VSVLPPEDQLPGQWTkrrsagRPLPGVEARIVDDDGDELPPDGGEVG 368
|
....
gi 1063733435 548 ELAL 551
Cdd:PRK06187 369 EIIV 372
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
181-467 |
1.07e-06 |
|
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: 51.56 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 181 RRLDDIVIRWRDEGSDDLPV----NTMTLLELRSQVWLAAHALSALGLEEESAIAVDMPMNVESVIIYLAIVLAGHVVVS 256
Cdd:cd05920 15 EPLGDLLARSAARHPDRIAVvdgdRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 257 IADSFSPREISTRLKISKAKAIFTQDVIiRGDKSIPLYRRVvdaeaplaivvpargsscrmklrekdlswnnflgnarnl 336
Cdd:cd05920 95 ALPSHRRSELSAFCAHAEAVAYIVPDRH-AGFDHRALAREL--------------------------------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 337 rgveyvAAEKPAGAYtnILFSSGTTGEPKAIPWT------NIsplkSAADAWCHLDVQRGDVVAWPTNLGWMMGPWLVYA 410
Cdd:cd05920 135 ------AESIPEVAL--FLLSGGTTGTPKLIPRThndyayNV----RASAEVCGLDQDTVYLAVLPAAHNFPLACPGVLG 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1063733435 411 SLINGACMGLynGSPLGPTFA-KFVQDAEVSVLGVIPSIVRTWQNSNSTSGYDWSRIR 467
Cdd:cd05920 203 TLLAGGRVVL--APDPSPDAAfPLIEREGVTVTALVPALVSLWLDAAASRRADLSSLR 258
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
216-372 |
3.10e-06 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 50.13 E-value: 3.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 216 AHALSALGLEEESAIAVDMPMNVESVIIYLAIVLAGHVVVSIADSFSPREISTRLKISKAKAIFT---------QDVIIR 286
Cdd:PRK06087 63 ANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFAptlfkqtrpVDLILP 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 287 GDKSIPLYRRV--VDAEAPlaivvpargsscrmklREKDLSWNNFLGNARNLRGVEYVAAEKPAGaytnILFSSGTTGEP 364
Cdd:PRK06087 143 LQNQLPQLQQIvgVDKLAP----------------ATSSLSLSQIIADYEPLTTAITTHGDELAA----VLFTSGTEGLP 202
|
170
....*....|
gi 1063733435 365 KAIPWT--NI 372
Cdd:PRK06087 203 KGVMLThnNI 212
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
202-367 |
3.13e-06 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.
Pssm-ID: 341279 [Multi-domain] Cd Length: 477 Bit Score: 49.96 E-value: 3.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 202 TMTLLELRSQVWLAAHALSALGLEEESAIAVDMPMNVESVIIYLAIVLAGHVVVSIaDSFSPRE-ISTRLKISKAKAIFT 280
Cdd:cd12114 12 TLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPV-DIDQPAArREAILADAGARLVLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 281 QDVIIRGDKS-IPLYRRVVDAEAPLAIVVPARgsscrmklrekdlswnnflgnarnlrgveyVAAEKPagAYtnILFSSG 359
Cdd:cd12114 91 DGPDAQLDVAvFDVLILDLDALAAPAPPPPVD------------------------------VAPDDL--AY--VIFTSG 136
|
....*...
gi 1063733435 360 TTGEPKAI 367
Cdd:cd12114 137 STGTPKGV 144
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
207-549 |
4.39e-06 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 49.70 E-value: 4.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 207 ELRSQVWLAAHALSALGLEEESAIAVDMPMNVESVIIYLAIVLAGHVVVSIADSFSPREISTRLKISKAKAIFTQDVIIR 286
Cdd:PRK12406 16 ELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAHADLLH 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 287 GDKS-IPLYRRVVDAEAPLAIVVPARGSSCRMKLREKDLSWNNFLGNARnlrgvEYVAAEKPAGAytNILFSSGTTGEPK 365
Cdd:PRK12406 96 GLASaLPAGVTVLSVPTPPEIAAAYRISPALLTPPAGAIDWEGWLAQQE-----PYDGPPVPQPQ--SMIYTSGTTGHPK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 366 AIPWTNISPLKSAAdawchldvqRGDVVAW-----PTNLGWMMGPwlVYASLINGacMGLYNGS-----PLGPTFA---- 431
Cdd:PRK12406 169 GVRRAAPTPEQAAA---------AEQMRALiyglkPGIRALLTGP--LYHSAPNA--YGLRAGRlggvlVLQPRFDpeel 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 432 -KFVQDAEVSVLGVIPSI----------VRtwqnsnstSGYDWSRIR--------CFGSTGEASnIDeylWlmgrahYKP 492
Cdd:PRK12406 236 lQLIERHRITHMHMVPTMfirllklpeeVR--------AKYDVSSLRhvihaaapCPADVKRAM-IE---W------WGP 297
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063733435 493 VI-EYCGGTEIGGSFISGS---LLQPQSLAafsTAAMGCKLFILDEDSNPIPPyaAGVGEL 549
Cdd:PRK12406 298 VIyEYYGSTESGAVTFATSedaLSHPGTVG---KAAPGAELRFVDEDGRPLPQ--GEIGEI 353
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
216-556 |
8.18e-06 |
|
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: 48.58 E-value: 8.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 216 AHALSALGLEEESAIAVDMPMNVESVIIYLAIVLAGHVVVSIADSFSPREISTRLKISKAKAIFTqdviirgdksiplyr 295
Cdd:cd05971 20 ANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVT--------------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 296 rvvdaeaplaivvpargsscrmklrekDLSwnnflgnarnlrgveyvaaEKPAgaytNILFSSGTTGEPKAIPWTNISPL 375
Cdd:cd05971 85 ---------------------------DGS-------------------DDPA----LIIYTSGTTGPPKGALHAHRVLL 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 376 KSA-ADAWCH-LDVQRGDVVAWPTNLGWMMGpwlvyasLINGACMGLYNGSP-LGPTFAKFVQDAEVSVL---GVI---- 445
Cdd:cd05971 115 GHLpGVQFPFnLFPRDGDLYWTPADWAWIGG-------LLDVLLPSLYFGVPvLAHRMTKFDPKAALDLMsryGVTtafl 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 446 -PSIVRTWQNSNSTSGYDWSRIRCFGSTGEASNIDEYLWlmGRAHYK-PVIEYCGGTEigGSFISG--SLLQPQSLAAFS 521
Cdd:cd05971 188 pPTALKMMRQQGEQLKHAQVKLRAIATGGESLGEELLGW--AREQFGvEVNEFYGQTE--CNLVIGncSALFPIKPGSMG 263
|
330 340 350
....*....|....*....|....*....|....*...
gi 1063733435 522 TAAMGCKLFILDEDSNPIPPYAagVGELAL---CPHMF 556
Cdd:cd05971 264 KPIPGHRVAIVDDNGTPLPPGE--VGEIAVelpDPVAF 299
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
203-279 |
1.02e-05 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 48.48 E-value: 1.02e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063733435 203 MTLLELRSQVWLAAHALSALGLEEESAIAVDMPMNVESVIIYLAIVLAGHVVVSIADSFSPREISTRLKISKAKAIF 279
Cdd:PRK07059 49 ITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPLYTPRELEHQLKDSGAEAIV 125
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
216-473 |
1.03e-05 |
|
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: 48.33 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 216 AHALSALGLEEESAIAVDMPMNVESVIIYLAIVLAGHVVVSIADSFSPREISTRLKISKAKAIFTqdviirgdksiplyr 295
Cdd:cd05936 38 AAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPRELEHILNDSGAKALIV--------------- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 296 rvvdaeaplaivvpargsscrmklrekDLSWNNFLGNARNLRGVEYVAAEKPAgaytNILFSSGTTGEPKAIPWT--NIS 373
Cdd:cd05936 103 ---------------------------AVSFTDLLAAGAPLGERVALTPEDVA----VLQYTSGTTGVPKGAMLThrNLV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 374 PLKSAADAWCHLDVQRGDVV--AWPT--NLGWMMGpwlVYASLINGACMGL-YNGSPlgPTFAKFVQDAEVSVLGVIPSI 448
Cdd:cd05936 152 ANALQIKAWLEDLLEGDDVVlaALPLfhVFGLTVA---LLLPLALGATIVLiPRFRP--IGVLKEIRKHRVTIFPGVPTM 226
|
250 260
....*....|....*....|....*
gi 1063733435 449 VRTWQNSNSTSGYDWSRIRCFGSTG 473
Cdd:cd05936 227 YIALLNAPEFKKRDFSSLRLCISGG 251
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
201-365 |
1.32e-05 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 47.85 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 201 NTMTLLELRSQVWLAAHALSALGLEEESAIAVDMPMNVESVIIYLAIVLAGHVVVSIADSFSPREISTRLKISKAKAIFT 280
Cdd:PRK07786 41 NTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVVT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 281 QDVIIrgdksiPLYRRVVDAEAPLAIVVPARGSScrmklREKDLSWNNFLGNArnlrGVEYVAAEKPAGAYTNILFSSGT 360
Cdd:PRK07786 121 EAALA------PVATAVRDIVPLLSTVVVAGGSS-----DDSVLGYEDLLAEA----GPAHAPVDIPNDSPALIMYTSGT 185
|
....*
gi 1063733435 361 TGEPK 365
Cdd:PRK07786 186 TGRPK 190
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
201-282 |
1.56e-05 |
|
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: 47.59 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 201 NTMTLLELRSQVWLAAHALSALGLEEESAIAVDMPMNVESVIIYLAIVLAGHVVVSIADSFSPREISTRLKISKAKAIFT 280
Cdd:cd05907 4 QPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFV 83
|
..
gi 1063733435 281 QD 282
Cdd:cd05907 84 ED 85
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
202-449 |
3.74e-05 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 46.49 E-value: 3.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 202 TMTLLELRSQVWLAAHALSALGLEEESAIAVDMPMNVESVIIYLAIVLAGhVVVSIADSFSPREISTRLKISKAKAIFT- 280
Cdd:PRK07529 58 TWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAG-IANPINPLLEPEQIAELLRAAGAKVLVTl 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 281 -----QDViirGDKSIPLYRRVVDAEAPLAI-----VVPARGSSCRMKLREKDLSWNNFLGNARNLRGVEYVAAEKPAGA 350
Cdd:PRK07529 137 gpfpgTDI---WQKVAEVLAALPELRTVVEVdlaryLPGPKRLAVPLIRRKAHARILDFDAELARQPGDRLFSGRPIGPD 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 351 YTNILF-SSGTTGEPKaipwtnISPLKSA---ADAWC---HLDVQRGDVVAWPTNL-------GWMMGPWLVYASLINGA 416
Cdd:PRK07529 214 DVAAYFhTGGTTGMPK------LAQHTHGnevANAWLgalLLGLGPGDTVFCGLPLfhvnallVTGLAPLARGAHVVLAT 287
|
250 260 270
....*....|....*....|....*....|...
gi 1063733435 417 CMGlYNGSPLGPTFAKFVQDAEVSVLGVIPSIV 449
Cdd:PRK07529 288 PQG-YRGPGVIANFWKIVERYRINFLSGVPTVY 319
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
202-547 |
8.25e-05 |
|
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: 45.32 E-value: 8.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 202 TMTLLELRSQVWLAAHALSALGLEEESAIAVDMPMNVESVIIYLAIVLAGHVVVSIADSFSPREISTRLKISKAKAIFTQ 281
Cdd:cd17652 12 TLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYMLADARPALLLTT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 282 dviirgdksiplyrrvvdAEAPlaivvpargsscrmklrekdlswnnflgnarnlrgveyvaaekpagAYtnILFSSGTT 361
Cdd:cd17652 92 ------------------PDNL----------------------------------------------AY--VIYTSGST 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 362 GEPK--AIPWTNISPLksAADAWCHLDVQRGDVVAWPTNLGWMMGPWLVYASLINGACMGLYNGSPL--GPTFAKFVQDA 437
Cdd:cd17652 106 GRPKgvVVTHRGLANL--AAAQIAAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELlpGEPLADLLREH 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 438 EVSVLGVIPSIVrtwqnsNSTSGYDWSRIRCFGSTGEA---SNIDEylWLMGRAhykpVIEYCGGTEIGGSFISGSLLQP 514
Cdd:cd17652 184 RITHVTLPPAAL------AALPPDDLPDLRTLVVAGEAcpaELVDR--WAPGRR----MINAYGPTETTVCATMAGPLPG 251
|
330 340 350
....*....|....*....|....*....|....*....
gi 1063733435 515 QSLAAFSTAAMGCKLFILDEDSNPIPP------YAAGVG 547
Cdd:cd17652 252 GGVPPIGRPVPGTRVYVLDARLRPVPPgvpgelYIAGAG 290
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
349-551 |
8.54e-05 |
|
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: 45.38 E-value: 8.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 349 GAYtnILFSSGTTGEPKAIPWT--NISPLKSAADAwcHLDVQRGDVVAWPTNLGWMMGPWLVYASLINGACMGLYNGSpl 426
Cdd:cd17653 107 LAY--IIFTSGSTGIPKGVMVPhrGVLNYVSQPPA--RLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTLVLADPS-- 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 427 gPTFAKFVQdaEVSVLGVIPSIVRTWQNSnstsgyDWSRIRCFGSTGEA---SNIDEylWLMGRAHYKpvieYCGGTEIG 503
Cdd:cd17653 181 -DPFAHVAR--TVDALMSTPSILSTLSPQ------DFPNLKTIFLGGEAvppSLLDR--WSPGRRLYN----AYGPTECT 245
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1063733435 504 GSFISGSLL--QPQSLAAfstAAMGCKLFILDEDSNPIPpyAAGVGELAL 551
Cdd:cd17653 246 ISSTMTELLpgQPVTIGK---PIPNSTCYILDADLQPVP--EGVVGEICI 290
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
185-479 |
1.15e-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: 45.18 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 185 DIVIRWRDEGSDDLPV---------NTMTLLELRSQVWLAAHALSALGLEEESAIAVDMPMNVESVIIYLAIVLAGHVVV 255
Cdd:cd05970 21 DVVDAMAKEYPDKLALvwcddageeRIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 256 SIADSFSPREISTRLKISKAKAIftqdvIIRGDKSIPlyrRVVDAEAPLAIVVPARgSSCRMKLREKDLSWNNFLGNA-- 333
Cdd:cd05970 101 PATHQLTAKDIVYRIESADIKMI-----VAIAEDNIP---EEIEKAAPECPSKPKL-VWVGDPVPEGWIDFRKLIKNAsp 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 334 --RNLRGVEYVAAEKPAGAYtnilFSSGTTGEPKAIPWTNISPLKSAADAWCHLDVQRGDVVAWPTNLGWMMGPW-LVYA 410
Cdd:cd05970 172 dfERPTANSYPCGEDILLVY----FSSGTTGMPKMVEHDFTYPLGHIVTAKYWQNVREGGLHLTVADTGWGKAVWgKIYG 247
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 411 SLINGACMGLYNGSPLGP-TFAKFVQDAEVSVLGVIPSIVRTWQNSNsTSGYDWSRIRCFGSTGEASNID 479
Cdd:cd05970 248 QWIAGAAVFVYDYDKFDPkALLEKLSKYGVTTFCAPPTIYRFLIRED-LSRYDLSSLRYCTTAGEALNPE 316
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
353-551 |
1.17e-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. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 44.97 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 353 NILFSSGTTGEPKAIPWTNISPLKSAADAWCHLDVQRGDVvawptnlgwmmgpwlVYASL----INGACMGLYNGSPLGP 428
Cdd:cd05934 85 SILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGEDDV---------------YLTVLplfhINAQAVSVLAALSVGA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 429 TFA---KFvqdaevsvlgvipsivrtwqnsnSTSGYdWSRIRCFGSTgeasnIDEYLWLMGRAHYK-------------- 491
Cdd:cd05934 150 TLVllpRF-----------------------SASRF-WSDVRRYGAT-----VTNYLGAMLSYLLAqppspddrahrlra 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 492 --------------------PVIEYCGGTEIGGSFIsGSLLQPQSLAAFSTAAMGCKLFILDEDSNPIPpyAAGVGELAL 551
Cdd:cd05934 201 aygapnppelheefeerfgvRLLEGYGMTETIVGVI-GPRDEPRRPGSIGRPAPGYEVRIVDDDGQELP--AGEPGELVI 277
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
203-371 |
1.30e-04 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 45.02 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 203 MTLLELRSQVWLAAHALSALGLEEESAIAVDMPMNVESVIIYLAIVLAGHVVVSIADSFSPREISTRLKISKAKAIFTQD 282
Cdd:PRK06710 50 ITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCLD 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 283 VIIRGDKSIP--------LYRRVVD-AEAPLAIVVP---ARGSSCRMKLREKDLS--WNNfLGNARNlRGVEYVAaeKPA 348
Cdd:PRK06710 130 LVFPRVTNVQsatkiehvIVTRIADfLPFPKNLLYPfvqKKQSNLVVKVSESETIhlWNS-VEKEVN-TGVEVPC--DPE 205
|
170 180
....*....|....*....|...
gi 1063733435 349 GAYTNILFSSGTTGEPKAIPWTN 371
Cdd:PRK06710 206 NDLALLQYTGGTTGFPKGVMLTH 228
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
202-378 |
1.56e-04 |
|
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: 44.66 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 202 TMTLLELRSQVWLAAHALSALGLEEESAIAVdMPMN-VESVIIYLAIVLAGHVVVSIADSFSPREISTRLKISKAKAIFT 280
Cdd:cd05933 8 TLTYKEYYEACRQAAKAFLKLGLERFHGVGI-LGFNsPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEANILVV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 281 QDviirgDKSIPLYRRVVDAEAPLAIVVPARGSscrMKLREKDL-SWNNFLGNARNLRGVEYVAAEK--PAGAYTNILFS 357
Cdd:cd05933 87 EN-----QKQLQKILQIQDKLPHLKAIIQYKEP---LKEKEPNLySWDEFMELGRSIPDEQLDAIISsqKPNQCCTLIYT 158
|
170 180
....*....|....*....|....*...
gi 1063733435 358 SGTTGEPKA-------IPWTNISPLKSA 378
Cdd:cd05933 159 SGTTGMPKGvmlshdnITWTAKAASQHM 186
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
184-365 |
1.99e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 44.15 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 184 DDIVIRWRDEgsddlpvnTMTLLELRSQVWLAAHALSALGLEEESAIAVDMPMNVESVIIYLAIVLAGHVVVSIADSFSP 263
Cdd:PRK08316 26 DKTALVFGDR--------SWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 264 REISTRLKISKAKAIFTQDviirgdksiPLYRRVVDAEAPLAIVVParGSSCRMKLREKDLSWNNFLGNARNLRGVE--- 340
Cdd:PRK08316 98 EELAYILDHSGARAFLVDP---------ALAPTAEAALALLPVDTL--ILSLVLGGREAPGGWLDFADWAEAGSVAEpdv 166
|
170 180
....*....|....*....|....*
gi 1063733435 341 YVAAEKPAgaytNILFSSGTTGEPK 365
Cdd:PRK08316 167 ELADDDLA----QILYTSGTESLPK 187
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
319-551 |
2.06e-04 |
|
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: 44.01 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 319 LREKDLSWnnFLGNARNLRGVeYVAAEKPAGAYTNILFSSGTTGEPKAIPWTNISPLkSAADAWCH--LDVQRGDVVAWP 396
Cdd:cd05958 70 LRPKELAY--ILDKARITVAL-CAHALTASDDICILAFTSGTTGAPKATMHFHRDPL-ASADRYAVnvLRLREDDRFVGS 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 397 TNLGWMMG-------PWLVYASlingaCMGLYNGSPlgPTFAKFVQDAEVSVLGVIPSIVRTWQNSNSTSGYDWSRIRCF 469
Cdd:cd05958 146 PPLAFTFGlggvllfPFGVGAS-----GVLLEEATP--DLLLSAIARYKPTVLFTAPTAYRAMLAHPDAAGPDLSSLRKC 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 470 GSTGEAsnideylwLMGRAHYK-------PVIEYCGGTEIGGSFIS--GSLLQPQSLAafsTAAMGCKLFILDEDSNPIP 540
Cdd:cd05958 219 VSAGEA--------LPAALHRAwkeatgiPIIDGIGSTEMFHIFISarPGDARPGATG---KPVPGYEAKVVDDEGNPVP 287
|
250
....*....|.
gi 1063733435 541 PyaAGVGELAL 551
Cdd:cd05958 288 D--GTIGRLAV 296
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
202-370 |
2.18e-04 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 44.10 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 202 TMTLLELRSQVWLAAHALSALGLEEESAIAVDMPMNVESVIIYLAIVLAG--HVVVSIADSFSPREIStRLK----ISKA 275
Cdd:PRK08180 69 RLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMYAGvpYAPVSPAYSLVSQDFG-KLRhvleLLTP 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 276 KAIFTQDviirgdksIPLYRRVVDAEAPLAI-VVPARGSSCRMKLrekdLSWNNFLGNARnLRGVEyvAAEKPAGAYT-- 352
Cdd:PRK08180 148 GLVFADD--------GAAFARALAAVVPADVeVVAVRGAVPGRAA----TPFAALLATPP-TAAVD--AAHAAVGPDTia 212
|
170
....*....|....*...
gi 1063733435 353 NILFSSGTTGEPKAIPWT 370
Cdd:PRK08180 213 KFLFTSGSTGLPKAVINT 230
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
340-507 |
2.42e-04 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 43.96 E-value: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 340 EYVAAEKPAGAYtnILFSSGTTGEPKAIPWTNISPLKSAADAWCHLDVQRGDVVAWP-TNLGWMMGPWLVYASLINGACM 418
Cdd:PTZ00237 247 EYVPVESSHPLY--ILYTSGTTGNSKAVVRSNGPHLVGLKYYWRSIIEKDIPTVVFShSSIGWVSFHGFLYGSLSLGNTF 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 419 GLYNGSPLGPT-----FAKFVQDAEVSVLGVIPSIVRTWQN-----SNSTSGYDWSRIR--CFGSTGEASNIDEYlwLMG 486
Cdd:PTZ00237 325 VMFEGGIIKNKhieddLWNTIEKHKVTHTLTLPKTIRYLIKtdpeaTIIRSKYDLSNLKeiWCGGEVIEESIPEY--IEN 402
|
170 180
....*....|....*....|.
gi 1063733435 487 RAHYKPVIEYcGGTEIGGSFI 507
Cdd:PTZ00237 403 KLKIKSSRGY-GQTEIGITYL 422
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
202-278 |
2.52e-04 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 43.89 E-value: 2.52e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063733435 202 TMTL--LELRSQVWlAAHALSALGLEEESAIAVDMPMNVESVIIYLAIVLAGHVVVSIADSFSPREISTRLKISKAKAI 278
Cdd:PRK08974 48 VMTFrkLEERSRAF-AAYLQNGLGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAKAI 125
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
202-367 |
4.33e-04 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 43.49 E-value: 4.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 202 TMTLLELRSQVWLAAHALSALGLEEESAIAVDMPMNVESVIIYLAIVLAGHVVVSIADSFSPREISTRLKISKAKAIFT- 280
Cdd:PRK10252 483 QFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITt 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 281 QDVIIR---GDKSIPLyrrVVDAEAPLAIVVPARGSSCrmklrekdlswnnflGNArnlrgveyvaaekpagAYtnILFS 357
Cdd:PRK10252 563 ADQLPRfadVPDLTSL---CYNAPLAPQGAAPLQLSQP---------------HHT----------------AY--IIFT 606
|
170
....*....|
gi 1063733435 358 SGTTGEPKAI 367
Cdd:PRK10252 607 SGSTGRPKGV 616
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
201-366 |
5.45e-04 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 43.02 E-value: 5.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 201 NTMTLLELRSQV-WLAAHALSALGLEEESAIAVDMPMNVESVIIYLAIVLAGHVVVSIADSFSPREISTRLKISKAK-AI 278
Cdd:PRK08314 34 RAISYRELLEEAeRLAGYLQQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGARvAI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 279 FTQDVIirgDKSIPL-------------YRRVVDAEAPLAIVVPARGSSCRMKLR-EKDLSWNnflgnarnlrgvEYVAA 344
Cdd:PRK08314 114 VGSELA---PKVAPAvgnlrlrhvivaqYSDYLPAEPEIAVPAWLRAEPPLQALApGGVVAWK------------EALAA 178
|
170 180
....*....|....*....|....*....
gi 1063733435 345 EKPAGAYTN-------ILFSSGTTGEPKA 366
Cdd:PRK08314 179 GLAPPPHTAgpddlavLPYTSGTTGVPKG 207
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
216-371 |
6.97e-04 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 42.66 E-value: 6.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 216 AHALSALGLEEESAIAVDMPMNVESVIIYLAIVLAGHVVVSIADSFSPREISTRLKISKAKAIFTQDViirgdksipLYR 295
Cdd:PLN02330 69 AKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTNDT---------NYG 139
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063733435 296 RVVDAEAPLAIVvparGSSCRmklrEKDLSWNNFLgNARNLRGVEYVAAEKPAGAYTNILFSSGTTGEPKAIPWTN 371
Cdd:PLN02330 140 KVKGLGLPVIVL----GEEKI----EGAVNWKELL-EAADRAGDTSDNEEILQTDLCALPFSSGTTGISKGVMLTH 206
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
207-467 |
8.53e-04 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 42.05 E-value: 8.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 207 ELRSQVWLAAHALSALGLEEESAIAVDMPMNVESVIIYLAIVLAGhvVVSIADSFSPR--EISTRLKISKAKAIFTQDVI 284
Cdd:COG1021 55 ELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAG--AIPVFALPAHRraEISHFAEQSEAVAYIIPDRH 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 285 iRGDKSIPLYRRVVdAEAPLAIVVPARGSScrmklrEKDLSWNNFLGNARNLRGVEyVAAEKPAgaytniLF--SSGTTG 362
Cdd:COG1021 133 -RGFDYRALARELQ-AEVPSLRHVLVVGDA------GEFTSLDALLAAPADLSEPR-PDPDDVA------FFqlSGGTTG 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 363 EPKAIPWTN---ISPLKSAADAwCHLDVQrgDV--VAWPT--NLGW----MMGPWLVyaslinGACMGL-YNGSPLgPTF 430
Cdd:COG1021 198 LPKLIPRTHddyLYSVRASAEI-CGLDAD--TVylAALPAahNFPLsspgVLGVLYA------GGTVVLaPDPSPD-TAF 267
|
250 260 270
....*....|....*....|....*....|....*..
gi 1063733435 431 AkFVQDAEVSVLGVIPSIVRTWQNSNSTSGYDWSRIR 467
Cdd:COG1021 268 P-LIERERVTVTALVPPLALLWLDAAERSRYDLSSLR 303
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
354-474 |
9.54e-04 |
|
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: 41.86 E-value: 9.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 354 ILFSSGTTGEPKAIPWTNisplKSAADAWCHL-----DVQRGDVVAWPTNLGWMMGPWLVYASLINGACMGLYNGSPLGP 428
Cdd:cd17635 6 VIFTSGTTGEPKAVLLAN----KTFFAVPDILqkeglNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGENTTYK 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1063733435 429 TFAKFVQDAEVSVLGVIPS----IVRTWQNSNSTSgydwSRIRCFGSTGE 474
Cdd:cd17635 82 SLFKILTTNAVTTTCLVPTllskLVSELKSANATV----PSLRLIGYGGS 127
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
203-280 |
2.30e-03 |
|
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: 40.54 E-value: 2.30e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063733435 203 MTLLELRSQVWLAAHALSALGLEEESAIAVDMPMNVESVIIYLAIVLAGHVVVSIADSFSPREISTRLKISKAKAIFT 280
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVV 79
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
203-368 |
2.38e-03 |
|
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: 40.57 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 203 MTLLELRSQVWLAAHALSALGLEEESAIAVDMPMNVESVIIYLAIVLAGHVVVSIADSFSPREIStrlkiskakaiftqD 282
Cdd:cd05923 29 LTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELA--------------E 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063733435 283 VIIRGDksiplYRRVVdaEAPLAIVVPARGSSCRMKLREKDLSWNNFLGNARNLrgVEYVAAEKPAGAYtnILFSSGTTG 362
Cdd:cd05923 95 LIERGE-----MTAAV--IAVDAQVMDAIFQSGVRVLALSDLVGLGEPESAGPL--IEDPPREPEQPAF--VFYTSGTTG 163
|
....*...
gi 1063733435 363 EPKA--IP 368
Cdd:cd05923 164 LPKGavIP 171
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
230-282 |
4.14e-03 |
|
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: 40.12 E-value: 4.14e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1063733435 230 IAVDMPMNVESVIIYLAIVLAGHVVVSIADSFSPREISTRLKISKAKAIFTQD 282
Cdd:cd05914 35 VALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFVSD 87
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
216-253 |
6.00e-03 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 39.47 E-value: 6.00e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1063733435 216 AHALSALGLEEESAIAVDMPMNVESVIIYLAIVLAGHV 253
Cdd:PRK07514 42 ANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAV 79
|
|
| |
