|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
1-726 |
0e+00 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 1343.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 1 MAYKSLSSISVSDIESLGIEQEHAATLHQQLTEIIGIHQTDSPATWQSISRSILNPELPFSFHQMLYYGCFVDYGPD--- 77
Cdd:PLN03052 3 MAGKSVDEITVGDLEAAGLSPEEAEKFFKELQVILTRAGASPPSIWRRISQSLLTPSHPFALHQLMYYSCYKNWDSDtlg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 78 -PPAWIPDPESVTSTNVGRLLEMRGKEFLGSAYKDPITSFADFQKFSVSNPEVYWKTVLGEMNISFSKPPECILcesisD 156
Cdd:PLN03052 83 pPPAWFPSPEIAKLTNLGRLLEARGKELLGSKYKDPISSFSEFQRFSVENPEVYWSIVLDELSLVFSVPPRCIL-----D 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 157 DGSSSYPSGQWLPGASINPAHNCLNLNGERSLNDTVILWRNELQDDLPLQRMTLEELRQEVWLVAYALESLGLEKGSAIA 236
Cdd:PLN03052 158 TSDESNPGGQWLPGAVLNVAECCLTPKPSKTDDSIAIIWRDEGSDDLPVNRMTLSELRSQVSRVANALDALGFEKGDAIA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 237 IDMPMHCKSVVIYLAIVLAGYVVVSIADSFAPREISSRLKISNAKVIFTQDLILRGDKTLPLYSRIVDAESPMAIVIPTR 316
Cdd:PLN03052 238 IDMPMNVHAVIIYLAIILAGCVVVSIADSFAPSEIATRLKISKAKAIFTQDVIVRGGKSIPLYSRVVEAKAPKAIVLPAD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 317 GSEFSMKLRDGDLAWCNFMDGVNKI-KGKEFIAVEEPVETFTNILFSSGTTGDPKAIPWTNISPLKAAADAWCHLDVRKG 395
Cdd:PLN03052 318 GKSVRVKLREGDMSWDDFLARANGLrRPDEYKAVEQPVEAFTNILFSSGTTGEPKAIPWTQLTPLRAAADAWAHLDIRKG 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 396 DVVSWPTNLGWMMGPWLVYASLLNGASMALYNGSPLGSGFAKFVQDSKVTMLGVIPSLVRSWRNANSTSGFDWSAIRCFA 475
Cdd:PLN03052 398 DIVCWPTNLGWMMGPWLVYASLLNGATLALYNGSPLGRGFAKFVQDAKVTMLGTVPSIVKTWKNTNCMAGLDWSSIRCFG 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 476 STGEASNIDEYLWLMGRAHYKPIIEYCGGTEIGGGFVTGSLLQAQSLAAFSTPAMCCSLFILDDQGHPIPQNVPGMGELA 555
Cdd:PLN03052 478 STGEASSVDDYLWLMSRAGYKPIIEYCGGTELGGGFVTGSLLQPQAFAAFSTPAMGCKLFILDDSGNPYPDDAPCTGELA 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 556 LGPLMLGASNTLLNADHYGVYFKGMPIWNGKVLRRHGDVFERTARGYYHAHGRADDTMNLGGIKVSSVEIERICNGADSN 635
Cdd:PLN03052 558 LFPLMFGASSTLLNADHYKVYFKGMPVFNGKILRRHGDIFERTSGGYYRAHGRADDTMNLGGIKVSSVEIERVCNAADES 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 636 ILETAAIGIPPSGGGPEQLALAVVLKNSNVTSQDLLTLRMSFNSALQKTLNPLFRVSQVVPVPSLPRTASNKVMRRVLRQ 715
Cdd:PLN03052 638 VLETAAIGVPPPGGGPEQLVIAAVLKDPPGSNPDLNELKKIFNSAIQKKLNPLFKVSAVVIVPSFPRTASNKVMRRVLRQ 717
|
730
....*....|.
gi 502086856 716 QLVENTQSSRI 726
Cdd:PLN03052 718 QLAQELSRSKL 728
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
239-722 |
0e+00 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 688.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 239 MPMHCKSVVIYLAIVLAGYVVVSIADSFAPREISSRLKISNAKVIFTQDLILRGDKTLPLYSRIVDAESPMAIVIPTRGS 318
Cdd:PLN03051 1 MPMTVDAVIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFTQDVVLRGGRALPLYSKVVEAAPAKAIVLPAAGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 319 EFSMKLRDGDLAWCNFMDGVNKI---KGKEFIAVEEPVETFTNILFSSGTTGDPKAIPWTNISPLKAAADAWCHLDVRKG 395
Cdd:PLN03051 81 PVAVPLREQDLSWCDFLGVAAAQgsvGGNEYSPVYAPVESVTNILFSSGTTGEPKAIPWTHLSPLRCASDGWAHMDIQPG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 396 DVVSWPTNLGWMMGPWLVYASLLNGASMALYNGSPLGSGFAKFVQDSKVTMLGVIPSLVRSWR--NANSTSGFDWSAIRC 473
Cdd:PLN03051 161 DVVCWPTNLGWMMGPWLLYSAFLNGATLALYGGAPLGRGFGKFVQDAGVTVLGLVPSIVKAWRhtGAFAMEGLDWSKLRV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 474 FASTGEASNIDEYLWLM-GRAHYKPIIEYCGGTEIGGGFVTGSLLQAQSLAAFSTPAMCCSLFILDDQGHPIPQNVPGMG 552
Cdd:PLN03051 241 FASTGEASAVDDVLWLSsVRGYYKPVIEYCGGTELASGYISSTLLQPQAPGAFSTASLGTRFVLLNDNGVPYPDDQPCVG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 553 ELALGPLMLGASNTLLNADHYGVYFKGMPIW--NGKVLRRHGDVFERTARGYYHAHGRADDTMNLGGIKVSSVEIERICN 630
Cdd:PLN03051 321 EVALAPPMLGASDRLLNADHDKVYYKGMPMYgsKGMPLRRHGDIMKRTPGGYFCVQGRADDTMNLGGIKTSSVEIERACD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 631 GADSNILETAAIGIPPSGGGPEQLALAVVLKNSNVT--SQDLLTLRMSFNSALQKTLNPLFRVSQVVPVPSLPRTASNKV 708
Cdd:PLN03051 401 RAVAGIAETAAVGVAPPDGGPELLVIFLVLGEEKKGfdQARPEALQKKFQEAIQTNLNPLFKVSRVKIVPELPRNASNKL 480
|
490
....*....|....
gi 502086856 709 MRRVLRQQLVENTQ 722
Cdd:PLN03051 481 LRRVLRDQLKKELS 494
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
113-714 |
2.83e-104 |
|
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: 331.38 E-value: 2.83e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 113 ITSFADFQKFSVSNPEVYWKTVLGEMNISFSKPPECILcesisdDGSSSYPSGQWLPGASINPAHNCLnlngERSLNDT- 191
Cdd:cd05968 6 IPDLEAFLERSAEDNAWFWGEFVKDVGIEWYEPPYQTL------DLSGGKPWAAWFVGGRMNIVEQLL----DKWLADTr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 192 ---VILWRNElqdDLPLQRMTLEELRQEVWLVAYALESLGLEKGSAIAIDMPMHCKSVVIYLAIVLAGYVVVSIADSFAP 268
Cdd:cd05968 76 trpALRWEGE---DGTSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 269 REISSRLKISNAKVIFTQDLILRGDKTLPLYSRIVDAESPMA----IVIPTRGSEFSMKLRDGDLAWCNFMDGVNKikGK 344
Cdd:cd05968 153 EAAATRLQDAEAKALITADGFTRRGREVNLKEEADKACAQCPtvekVVVVRHLGNDFTPAKGRDLSYDEEKETAGD--GA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 345 EFIAVEEPVEtftnILFSSGTTGDPKAIPWTNIS-PLKAAADAWCHLDVRKGDVVSWPTNLGWMMGPWLVYASLLNGASM 423
Cdd:cd05968 231 ERTESEDPLM----IIYTSGTTGKPKGTVHVHAGfPLKAAQDMYFQFDLKPGDLLTWFTDLGWMMGPWLIFGGLILGATM 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 424 ALYNGSPlgsGFAK------FVQDSKVTMLGVIPSLVRSW--RNANSTSGFDWSAIRCFASTGEASNIDEYLWL---MGR 492
Cdd:cd05968 307 VLYDGAP---DHPKadrlwrMVEDHEITHLGLSPTLIRALkpRGDAPVNAHDLSSLRVLGSTGEPWNPEPWNWLfetVGK 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 493 AHyKPIIEYCGGTEIGGGFVTGSLLQAQSLAAFSTPAMCCSLFILDDQGHPIPQNVpgmGELALGPLMLGASNTLLNAD- 571
Cdd:cd05968 384 GR-NPIINYSGGTEISGGILGNVLIKPIKPSSFNGPVPGMKADVLDESGKPARPEV---GELVLLAPWPGMTRGFWRDEd 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 572 -HYGVYFKGMP-IWngkvlrRHGDVFERTARGYYHAHGRADDTMNLGGIKVSSVEIERICNgADSNILETAAIGIPPSGG 649
Cdd:cd05968 460 rYLETYWSRFDnVW------VHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLN-AHPAVLESAAIGVPHPVK 532
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502086856 650 GpEQLALAVVLKNSNVTSQDLLTLRMSF-NSALQKTLNPlfrvSQVVPVPSLPRTASNKVMRRVLR 714
Cdd:cd05968 533 G-EAIVCFVVLKPGVTPTEALAEELMERvADELGKPLSP----ERILFVKDLPKTRNAKVMRRVIR 593
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
166-717 |
1.62e-95 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 307.04 E-value: 1.62e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 166 QWLPGASINPAHNCL--NLNGERslNDTVILWRNELQDDlplQRMTLEELRQEVWLVAYALESLGLEKGSAIAIDMPMHC 243
Cdd:COG0365 1 RWFVGGRLNIAYNCLdrHAEGRG--DKVALIWEGEDGEE---RTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 244 KSVVIYLAIVLAGYVVVSIADSFAPREISSRLKISNAKVIFTQDLILRGDKTLPLYSRIVDA--ESPMA---IVIPTRGS 318
Cdd:COG0365 76 EAVIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGGLRGGKVIDLKEKVDEAleELPSLehvIVVGRTGA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 319 EFSMklrDGDLAWCNFMDGvnkiKGKEFiaveEPVET------FtnILFSSGTTGDPKAIPWTNISPL-KAAADAWCHLD 391
Cdd:COG0365 156 DVPM---EGDLDWDELLAA----ASAEF----EPEPTdaddplF--ILYTSGTTGKPKGVVHTHGGYLvHAATTAKYVLD 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 392 VRKGDVVSWPTNLGWMMGPW-LVYASLLNGASMALYNGSPL---GSGFAKFVQDSKVTMLGVIPSLVRSWRNA--NSTSG 465
Cdd:COG0365 223 LKPGDVFWCTADIGWATGHSyIVYGPLLNGATVVLYEGRPDfpdPGRLWELIEKYGVTVFFTAPTAIRALMKAgdEPLKK 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 466 FDWSAIRCFASTGEASNIDEYLWLmgRAHYK-PIIEYCGGTEIGGGFVTGSLLQAQSLAAFSTPAMCCSLFILDDQGHPI 544
Cdd:COG0365 303 YDLSSLRLLGSAGEPLNPEVWEWW--YEAVGvPIVDGWGQTETGGIFISNLPGLPVKPGSMGKPVPGYDVAVVDEDGNPV 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 545 PQNVpgMGELALGPLMLGASNTLLNADH--YGVYFKGMPIWNgkvlrRHGDVFERTARGYYHAHGRADDTMNLGGIKVSS 622
Cdd:COG0365 381 PPGE--EGELVIKGPWPGMFRGYWNDPEryRETYFGRFPGWY-----RTGDGARRDEDGYFWILGRSDDVINVSGHRIGT 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 623 VEIERICNGADSnILETAAIGIPPSGGGpEQLALAVVLKNSNVTSQDL-LTLRmsfnSALQKTLNPLFRVSQVVPVPSLP 701
Cdd:COG0365 454 AEIESALVSHPA-VAEAAVVGVPDEIRG-QVVKAFVVLKPGVEPSDELaKELQ----AHVREELGPYAYPREIEFVDELP 527
|
570
....*....|....*.
gi 502086856 702 RTASNKVMRRVLRQQL 717
Cdd:COG0365 528 KTRSGKIMRRLLRKIA 543
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
121-709 |
3.66e-74 |
|
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: 250.96 E-value: 3.66e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 121 KFSVSNPEVYWKTVLGEMNISFSKPPECILcesisdDGSSSYPSGQWLPGASINPAHNCLNLNGERSLNDTVILWRNelq 200
Cdd:cd17634 6 RQSINDPDTFWGEAGKILDWITPYQKVKNT------SFAPGAPSIKWFEDATLNLAANALDRHLRENGDRTAIIYEG--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 201 DDLPLQR-MTLEELRQEVWLVAYALESLGLEKGSAIAIDMPMHCKSVVIYLAIVLAGYVVVSIADSFAPREISSRLKISN 279
Cdd:cd17634 77 DDTSQSRtISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 280 AKVIFTQDLILRGDKTLPLYSRIVDAESPMAI----VIPTRGSEFSMKLRDG-DLAWCNFMDGVNKIKGKEFIAVEEPVE 354
Cdd:cd17634 157 SRLLITADGGVRAGRSVPLKKNVDDALNPNVTsvehVIVLKRTGSDIDWQEGrDLWWRDLIAKASPEHQPEAMNAEDPLF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 355 tftnILFSSGTTGDPKAIPWTNIS-PLKAAADAWCHLDVRKGDVVSWPTNLGWMMG-PWLVYASLLNGASMALYNGSPLG 432
Cdd:cd17634 237 ----ILYTSGTTGKPKGVLHTTGGyLVYAATTMKYVFDYGPGDIYWCTADVGWVTGhSYLLYGPLACGATTLLYEGVPNW 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 433 SGFAKF---VQDSKVTMLGVIPSLVRSWRNA--NSTSGFDWSAIRCFASTGEASNIDEYLWLMGR--AHYKPIIEYCGGT 505
Cdd:cd17634 313 PTPARMwqvVDKHGVNILYTAPTAIRALMAAgdDAIEGTDRSSLRILGSVGEPINPEAYEWYWKKigKEKCPVVDTWWQT 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 506 EIGGGFVTGSLLQAQSLAAFST-PAMCCSLFILDDQGHPIPqnvPGM-GELALGPLMLGASNTLLNADH-----YGVYFK 578
Cdd:cd17634 393 ETGGFMITPLPGAIELKAGSATrPVFGVQPAVVDNEGHPQP---GGTeGNLVITDPWPGQTRTLFGDHErfeqtYFSTFK 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 579 GMPIwngkvlrrHGDVFERTARGYYHAHGRADDTMNLGGIKVSSVEIERICNGaDSNILETAAIGIPPSGGGpeQLALAV 658
Cdd:cd17634 470 GMYF--------SGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVA-HPKVAEAAVVGIPHAIKG--QAPYAY 538
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 502086856 659 VLKNSNVTSQDllTLRMSFNSALQKTLNPLFRVSQVVPVPSLPRTASNKVM 709
Cdd:cd17634 539 VVLNHGVEPSP--ELYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKIM 587
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
76-720 |
1.46e-60 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 215.43 E-value: 1.46e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 76 PDPPAWIPDPESVTSTNVGRLLEmrgkeFLGSAYKDPITSFADFQKFSVSNPEVYWKTVLGEMNISFSKPPECILcesis 155
Cdd:PRK03584 1 MGDPLWTPSAERIAASRMTAFIR-----WLAARRGLSFDDYAALWRWSVEDLEAFWQSVWDFFGVIGSTPYTVVL----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 156 ddGSSSYPSGQWLPGASINPAHNCLnlnGERSLNDTVILWRNElqdDLPLQRMTLEELRQEVWLVAYALESLGLEKGSAI 235
Cdd:PRK03584 71 --AGRRMPGARWFPGARLNYAENLL---RHRRDDRPAIIFRGE---DGPRRELSWAELRRQVAALAAALRALGVGPGDRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 236 AIDMPMHCKSVVIYLAIVLAGYVVVSIADSFAPREISSRLKISNAKVIFTQDLILRGDKT---LPLYSRIVDAESPM--A 310
Cdd:PRK03584 143 AAYLPNIPETVVAMLATASLGAIWSSCSPDFGVQGVLDRFGQIEPKVLIAVDGYRYGGKAfdrRAKVAELRAALPSLehV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 311 IVIPTRGSEFSMKLRDGDLAWcnfmdgvnkikgKEFIAVEEPVE-TFTN--------ILFSSGTTGDPKAI----PWTNI 377
Cdd:PRK03584 223 VVVPYLGPAAAAAALPGALLW------------EDFLAPAEAAElEFEPvpfdhplwILYSSGTTGLPKCIvhghGGILL 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 378 SPLKAAAdawCHLDVRKGDVVSWPTNLGWMMGPWLVyASLLNGASMALYNGSPL---GSGFAKFVQDSKVTMLGVIPSLV 454
Cdd:PRK03584 291 EHLKELG---LHCDLGPGDRFFWYTTCGWMMWNWLV-SGLLVGATLVLYDGSPFypdPNVLWDLAAEEGVTVFGTSAKYL 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 455 RSWRNANSTSG--FDWSAIRCFASTGEASNIDEYLWLmgRAHYKP---IIEYCGGTEIGGGFVTGSLLQAQSLAAFSTPA 529
Cdd:PRK03584 367 DACEKAGLVPGetHDLSALRTIGSTGSPLPPEGFDWV--YEHVKAdvwLASISGGTDICSCFVGGNPLLPVYRGEIQCRG 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 530 MCCSLFILDDQGHPIpqnVPGMGELalgplmlgasnTLLNAdhygvyFKGMPI--WN---GKVLR-----------RHGD 593
Cdd:PRK03584 445 LGMAVEAWDEDGRPV---VGEVGEL-----------VCTKP------FPSMPLgfWNdpdGSRYRdayfdtfpgvwRHGD 504
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 594 VFERTARGYYHAHGRADDTMNLGGIKVSSVEIERICNGADSnILETAAIGIPPSGGGpEQLALAVVLKNsNVTSQDllTL 673
Cdd:PRK03584 505 WIEITEHGGVVIYGRSDATLNRGGVRIGTAEIYRQVEALPE-VLDSLVIGQEWPDGD-VRMPLFVVLAE-GVTLDD--AL 579
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 502086856 674 RMSFNSALQKTLNPLFRVSQVVPVPSLPRTASNKVM----RRVLRQQLVEN 720
Cdd:PRK03584 580 RARIRTTIRTNLSPRHVPDKIIAVPDIPRTLSGKKVelpvKKLLHGRPVKK 630
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
115-721 |
1.71e-58 |
|
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: 209.43 E-value: 1.71e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 115 SFADFQKFSVSNPEVYWKTVLGEMNISFSKPPECIlcesisDDGSSSYPSGQWLPGASINPAHNCLnlnGERSLNDTVIL 194
Cdd:cd05943 18 DYAALHRWSVDDPGAFWAAVWDFSGVRGSKPYDVV------VVSGRIMPGARWFPGARLNYAENLL---RHADADDPAAI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 195 WRNElqdDLPLQRMTLEELRQEVWLVAYALESLGLEKGSAIAIDMPMHCKSVVIYLAIVLAGYVVVSIADSFAPREISSR 274
Cdd:cd05943 89 YAAE---DGERTEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFGVPGVLDR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 275 LKISNAKVIFTQDLILRGDKTLPLYSRI--VDAESP---MAIVIPTRGSEFSMKLRDGDlAWCNFMDGVNKIKGKEFIAV 349
Cdd:cd05943 166 FGQIEPKVLFAVDAYTYNGKRHDVREKVaeLVKGLPsllAVVVVPYTVAAGQPDLSKIA-KALTLEDFLATGAAGELEFE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 350 EEPVETFTNILFSSGTTGDPKAI----PWTNISPLKAAAdawCHLDVRKGDVVSWPTNLGWMMGPWLVyASLLNGASMAL 425
Cdd:cd05943 245 PLPFDHPLYILYSSGTTGLPKCIvhgaGGTLLQHLKEHI---LHCDLRPGDRLFYYTTCGWMMWNWLV-SGLAVGATIVL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 426 YNGSPLGSGFA---KFVQDSKVTMLGVIPSLVRSWRNANSTSG--FDWSAIRCFASTGEASNIDEYLWLmgRAHYKPIIE 500
Cdd:cd05943 321 YDGSPFYPDTNalwDLADEEGITVFGTSAKYLDALEKAGLKPAetHDLSSLRTILSTGSPLKPESFDYV--YDHIKPDVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 501 YC---GGTEIGGGFVTGSLLQAQSLAAFSTPAMCCSLFILDDQGHPIpqnVPGMGELA-LGPlmlgasntllnadhygvy 576
Cdd:cd05943 399 LAsisGGTDIISCFVGGNPLLPVYRGEIQCRGLGMAVEAFDEEGKPV---WGEKGELVcTKP------------------ 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 577 FKGMPI--WN---GKVLR-----------RHGDVFERTARGYYHAHGRADDTMNLGGIKVSSVEIERICNGADsNILETA 640
Cdd:cd05943 458 FPSMPVgfWNdpdGSRYRaayfakypgvwAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIP-EVEDSL 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 641 AIGIPPSGGGpEQLALAVVLKNSNVTSQDlltLRMSFNSALQKTLNPLFRVSQVVPVPSLPRTASNKV----MRRVLRQQ 716
Cdd:cd05943 537 VVGQEWKDGD-ERVILFVKLREGVELDDE---LRKRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGKKvevaVKKIIAGR 612
|
....*
gi 502086856 717 LVENT 721
Cdd:cd05943 613 PVKNA 617
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
115-715 |
9.13e-55 |
|
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: 198.55 E-value: 9.13e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 115 SFADFQKFSVSNPEVYWKTVLGEmnISFSKPPECILcesisdDGSSSYPSGQWLPGASINPAHNCLNLNGERSLNDTVIL 194
Cdd:cd05966 2 QYKELYKQSIEDPEEFWGEIAKE--LDWFKPWDKVL------DWSKGPPFIKWFEGGKLNISYNCLDRHLKERGDKVAII 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 195 WRNELQDDlpLQRMTLEELRQEVWLVAYALESLGLEKGSAIAIDMPMHCKSVVIYLA---------IVLAGyvvvsiads 265
Cdd:cd05966 74 WEGDEPDQ--SRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLAcarigavhsVVFAG--------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 266 FAPREISSRLKISNAKVIFTQDLILRGDKTLPLySRIVDA---ESPM---AIVIPTRGSEFSMKlRDGDLAWCNFMDGVN 339
Cdd:cd05966 143 FSAESLADRINDAQCKLVITADGGYRGGKVIPL-KEIVDEaleKCPSvekVLVVKRTGGEVPMT-EGRDLWWHDLMAKQS 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 340 KIKGKEFIAVEEPVetFtnILFSSGTTGDPKAIPWTNisplkAAADAWCHL------DVRKGDVVsWPT-NLGWMMG-PW 411
Cdd:cd05966 221 PECEPEWMDSEDPL--F--ILYTSGSTGKPKGVVHTT-----GGYLLYAATtfkyvfDYHPDDIY-WCTaDIGWITGhSY 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 412 LVYASLLNGASMALYNGSPLGSGFAKF---VQDSKVTMLGVIPSLVRSWRNANS--TSGFDWSAIRCFASTGEASNIDEY 486
Cdd:cd05966 291 IVYGPLANGATTVMFEGTPTYPDPGRYwdiVEKHKVTIFYTAPTAIRALMKFGDewVKKHDLSSLRVLGSVGEPINPEAW 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 487 LWLmgrahYK-------PIIEYCGGTEIGGGFVTgsllqaqSL-AAFSTPAMCCS--LF-----ILDDQGHPIPQNVPGM 551
Cdd:cd05966 371 MWY-----YEvigkercPIVDTWWQTETGGIMIT-------PLpGATPLKPGSATrpFFgiepaILDEEGNEVEGEVEGY 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 552 geLALG---PLMLgasNTLLNaDHY---GVYFKGMPiwnGKVLRrhGDVFERTARGYYHAHGRADDTMNLGGIKVSSVEI 625
Cdd:cd05966 439 --LVIKrpwPGMA---RTIYG-DHEryeDTYFSKFP---GYYFT--GDGARRDEDGYYWITGRVDDVINVSGHRLGTAEV 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 626 ERICNgADSNILETAAIGIPPSGGGpEQLALAVVLKNSNVTSQDlltLRMSFNSALQKTLNPLFRVSQVVPVPSLPRTAS 705
Cdd:cd05966 508 ESALV-AHPAVAEAAVVGRPHDIKG-EAIYAFVTLKDGEEPSDE---LRKELRKHVRKEIGPIATPDKIQFVPGLPKTRS 582
|
650
....*....|
gi 502086856 706 NKVMRRVLRQ 715
Cdd:cd05966 583 GKIMRRILRK 592
|
|
| ac_ac_CoA_syn |
TIGR01217 |
acetoacetyl-CoA synthase; This enzyme catalyzes the first step of the mevalonate pathway of ... |
79-723 |
2.36e-53 |
|
acetoacetyl-CoA synthase; This enzyme catalyzes the first step of the mevalonate pathway of IPP biosynthesis. Most bacteria do not use this pathway, but rather the deoxyxylulose pathway. [Central intermediary metabolism, Other]
Pssm-ID: 273507 [Multi-domain] Cd Length: 652 Bit Score: 195.48 E-value: 2.36e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 79 PAWIPDPESVTSTNVGRLLEMRGKEFlGSAYKDpitsFADFQKFSVSNPEVYWKTVLGEMNISFSKPpecilCESISDDg 158
Cdd:TIGR01217 5 PLWQPDAQRIAQARMTRFQAWAGEHH-GAAEGG----YDALHRWSVDELDTFWKAVWEWFDVRFSTP-----CARVVDD- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 159 sSSYPSGQWLPGASINPAHNCLNLNGerslNDTVILWRNELQDDLPLqrmTLEELRQEVWLVAYALESLGLEKGSAIAID 238
Cdd:TIGR01217 74 -RTMPGAQWFPGARLNYAENLLRAAG----TEPALLYVDETHEPAPV---TWAELRRQVASLAAALRALGVRPGDRVSGY 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 239 MPMHCKSVVIYLAIVLAGYVVVSIADSFAPREISSRLKISNAKVIFTQDLILRGDKTLPLYSRI--VDAESPM---AIVI 313
Cdd:TIGR01217 146 LPNIPQAVVAMLATASVGAIWSSCSPDFGARGVLDRFQQIEPKLLFTVDGYRYNGKEHDRRDKVaeVRKELPTlraVVHI 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 314 PTRGSEFSMKLR-DGDLAWCNFMDGVnkiKGKEFIAVEEPVETFTNILFSSGTTGDPKAIPW----TNISPLKAAAdawC 388
Cdd:TIGR01217 226 PYLGPRETEAPKiDGALDLEDFTAAA---QAAELVFEQLPFDHPLWILFSSGTTGLPKCIVHsaggTLVQHLKEHG---L 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 389 HLDVRKGDVVSWPTNLGWMMGPWLVyASLLNGASMALYNGSPL---GSGFAKFVQDSKVTMLGVIPSLVRSWRNANSTSG 465
Cdd:TIGR01217 300 HCDLGPGDRLFYYTTTGWMMWNWLV-SGLATGATLVLYDGSPGfpaTNVLWDIAERTGATLFGTSAKYVMACRKAGVHPA 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 466 --FDWSAIRCFASTGEASNIDEYLWLmgRAHYKP---IIEYCGGTEIGGGFVTGSLLQAQSLAAFSTPAMCCSLFILDDQ 540
Cdd:TIGR01217 379 rtHDLSALQCVASTGSPLPPDGFRWV--YDEIKAdvwLASISGGTDICSCFAGANPTLPVHIGEIQAPGLGTAVQSWDPE 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 541 GHPIPQNVpgmGELALGPLMLGASNTLLN----ADHYGVYFKGMP-IWngkvlrRHGDVFERTARGYYHAHGRADDTMNL 615
Cdd:TIGR01217 457 GKPVTGEV---GELVCTNPMPSMPIRFWNdpdgSKYRDAYFDTYPgVW------RHGDWITLTPRGGIVIHGRSDSTLNP 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 616 GGIKVSSVEIERICNGADSnILETAAIGIPPSGGGpEQLALAVVLKnSNVTSQDLLTLRMsfNSALQKTLNPLFRVSQVV 695
Cdd:TIGR01217 528 QGVRMGSAEIYNAVERLDE-VRESLCIGQEQPDGG-YRVVLFVHLA-PGATLDDALLDRI--KRTIRAGLSPRHVPDEII 602
|
650 660 670
....*....|....*....|....*....|..
gi 502086856 696 PVPSLPRTASNKVM----RRVLRQQLVENTQS 723
Cdd:TIGR01217 603 EVPGIPHTLTGKRVevavKRVLQGTPVDNPGA 634
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
206-724 |
4.35e-49 |
|
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: 178.85 E-value: 4.35e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 206 QRMTLEELRQEVWLVAYALESLGLEKGSAIAIDMPMHCKSVVIYLAIVLAGYVVVSIADSFAPREISSRLKISNAKVIFT 285
Cdd:COG0318 23 RRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEELAYILEDSGARALVT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 286 qdlilrgdktlplysrivdaespmaiviptrgsefsmklrdgdlawcnfmdgvnkikgkefiAVeepvetftnILFSSGT 365
Cdd:COG0318 103 --------------------------------------------------------------AL---------ILYTSGT 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 366 TGDPKAIPWT--NISplkAAADAWC-HLDVRKGDVVSWPTNL----GWMMGPWlvyASLLNGASMALYnGSPLGSGFAKF 438
Cdd:COG0318 112 TGRPKGVMLThrNLL---ANAAAIAaALGLTPGDVVLVALPLfhvfGLTVGLL---APLLAGATLVLL-PRFDPERVLEL 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 439 VQDSKVTMLGVIPSLVRSWRNANSTSGFDWSAIRCFASTGEASN---IDEYLWLMGRahykPIIEYCGGTEiGGGFVTGS 515
Cdd:COG0318 185 IERERVTVLFGVPTMLARLLRHPEFARYDLSSLRLVVSGGAPLPpelLERFEERFGV----RIVEGYGLTE-TSPVVTVN 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 516 LLQAQSLAAFS--TPAMCCSLFILDDQGHPIPQNVPGmgELAL-GP-LMLGasntllnadhygvYFKgMPIWNGKVLR-- 589
Cdd:COG0318 260 PEDPGERRPGSvgRPLPGVEVRIVDEDGRELPPGEVG--EIVVrGPnVMKG-------------YWN-DPEATAEAFRdg 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 590 --RHGDVFERTARGYYHAHGRADDTMNLGGIKVSSVEIERICNGADSnILETAAIGIP-PSGGgpEQLALAVVLK-NSNV 665
Cdd:COG0318 324 wlRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPG-VAEAAVVGVPdEKWG--ERVVAFVVLRpGAEL 400
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 502086856 666 TSQDLLtlrmsfnSALQKTLNPLFRVSQVVPVPSLPRTASNKVMRRVLRQQLVENTQSS 724
Cdd:COG0318 401 DAEELR-------AFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRERYAAGALEA 452
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
116-715 |
1.60e-47 |
|
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: 177.89 E-value: 1.60e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 116 FADFQKFSVSNPEVYWKTVLGEmnISFSKPPECILcesisdDGSSSyPSGQWLPGASINPAHNCLNLNGERSLND-TVIL 194
Cdd:cd05967 1 YEEVYARSIAEPEAFWAEQARL--IDWFKPPEKIL------DNSNP-PFTRWFVGGRLNTCYNALDRHVEAGRGDqIALI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 195 WrnelqdDLPL----QRMTLEELRQEVWLVAYALESLGLEKGSAIAIDMPMHCKSVVIYLAIVLAGYVVVSIADSFAPRE 270
Cdd:cd05967 72 Y------DSPVtgteRTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAKE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 271 ISSRLKISNAKVIFTQDLILRGDKTLPlYSRIVD---AES---PMAIVIPTRGS-EFSMKLRDGDLAWCNFMDGVNKIkg 343
Cdd:cd05967 146 LASRIDDAKPKLIVTASCGIEPGKVVP-YKPLLDkalELSghkPHHVLVLNRPQvPADLTKPGRDLDWSELLAKAEPV-- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 344 kefiaveEPVETFTN----ILFSSGTTGDPKAIPWTNISPLKAAADAWCHL-DVRKGDVVSWPTNLGWMMG-PWLVYASL 417
Cdd:cd05967 223 -------DCVPVAATdplyILYTSGTTGKPKGVVRDNGGHAVALNWSMRNIyGIKPGDVWWAASDVGWVVGhSYIVYGPL 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 418 LNGASMALYNGSPLG----SGFAKFVQDSKVTMLGVIPSLVRSWR----NANSTSGFDWSAIRCFASTGEASNIDEYLWL 489
Cdd:cd05967 296 LHGATTVLYEGKPVGtpdpGAFWRVIEKYQVNALFTAPTAIRAIRkedpDGKYIKKYDLSSLRTLFLAGERLDPPTLEWA 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 490 MgRAHYKPIIEYCGGTEIGGGfVTGSL--LQAQSLAAFST--PAMCCSLFILDDQGHPIPQNVpgMGELAL-GPLMLGAS 564
Cdd:cd05967 376 E-NTLGVPVIDHWWQTETGWP-ITANPvgLEPLPIKAGSPgkPVPGYQVQVLDEDGEPVGPNE--LGNIVIkLPLPPGCL 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 565 NTLLNADH-----YGVYFKGmpiwngkvLRRHGDVFERTARGYYHAHGRADDTMNLGGIKVSSVEIERICnGADSNILET 639
Cdd:cd05967 452 LTLWKNDErfkklYLSKFPG--------YYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESV-LSHPAVAEC 522
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502086856 640 AAIGIPPSGGGPEQLALAVVLKNSNVTSQDLLTLRMSFnsaLQKTLNPLFRVSQVVPVPSLPRTASNKVMRRVLRQ 715
Cdd:cd05967 523 AVVGVRDELKGQVPLGLVVLKEGVKITAEELEKELVAL---VREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRK 595
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
359-709 |
5.73e-45 |
|
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: 164.38 E-value: 5.73e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 359 ILFSSGTTGDPKAIPWTNISPLKAAADAWCHLDVRKGDVVSWPTNLGWMMGPWLVYASLLNGASMALYNGSPLGSgFAKF 438
Cdd:cd04433 5 ILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKFDPEA-ALEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 439 VQDSKVTMLGVIPSLVRSWRNANSTSGFDWSAIRCFASTGEASNIDEYLWLMGRAHYKPIIEYcGGTEIGGGFVTGSLLQ 518
Cdd:cd04433 84 IEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLERFEEAPGIKLVNGY-GLTETGGTVATGPPDD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 519 AQSLAAFS-TPAMCCSLFILDDQGHPIPQNVPgmGELAL-GP-LMLGasntllnadhygvYFKgMPIWNGKVLR----RH 591
Cdd:cd04433 163 DARKPGSVgRPVPGVEVRIVDPDGGELPPGEI--GELVVrGPsVMKG-------------YWN-NPEATAAVDEdgwyRT 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 592 GDVFERTARGYYHAHGRADDTMNLGGIKVSSVEIERICNGADSnILETAAIGIPPSGGGpEQLALAVVLKN-SNVTSQDL 670
Cdd:cd04433 227 GDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPG-VAEAAVVGVPDPEWG-ERVVAVVVLRPgADLDAEEL 304
|
330 340 350
....*....|....*....|....*....|....*....
gi 502086856 671 ltlrmsfNSALQKTLNPLFRVSQVVPVPSLPRTASNKVM 709
Cdd:cd04433 305 -------RAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
206-616 |
7.23e-39 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 149.00 E-value: 7.23e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 206 QRMTLEELRQEVWLVAYALESLGLEKGSAIAIDMPMHCKSVVIYLAIVLAGYVVVSIADSFAPREISSRLKISNAKVIFT 285
Cdd:pfam00501 20 RRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSGAKVLIT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 286 QDlilrgdktLPLYSRIVDAESPMAIVIPTRGSEFSMKLRDGDLawcNFMDGVNKIKGKEFIAVEEpvETFTNILFSSGT 365
Cdd:pfam00501 100 DD--------ALKLEELLEALGKLEVVKLVLVLDRDPVLKEEPL---PEEAKPADVPPPPPPPPDP--DDLAYIIYTSGT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 366 TGDPKAIPWTNISPLKAAADAW----CHLDVRKGDVVSWPTNLGWMMG-PWLVYASLLNGASMALYNGSPL--GSGFAKF 438
Cdd:pfam00501 167 TGKPKGVMLTHRNLVANVLSIKrvrpRGFGLGPDDRVLSTLPLFHDFGlSLGLLGPLLAGATVVLPPGFPAldPAALLEL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 439 VQDSKVTMLGVIPSLVRSWRNANSTSGFDWSAIRCFASTGEASNIDEYLWLmgRAHYKPIIEYCGG-TEiGGGFVTGSLL 517
Cdd:pfam00501 247 IERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELARRF--RELFGGALVNGYGlTE-TTGVVTTPLP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 518 QAQSLAAFST---PAMCCSLFILDDQ-GHPIPQNVPgmGELAL-GP-LMLGasntllnadhygvYFKgMPIWNGKVLR-- 589
Cdd:pfam00501 324 LDEDLRSLGSvgrPLPGTEVKIVDDEtGEPVPPGEP--GELCVrGPgVMKG-------------YLN-DPELTAEAFDed 387
|
410 420 430
....*....|....*....|....*....|
gi 502086856 590 ---RHGDVFERTARGYYHAHGRADDTMNLG 616
Cdd:pfam00501 388 gwyRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
123-715 |
2.09e-36 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 145.67 E-value: 2.09e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 123 SVSNPEVYWKTVLGEmnISFSKPPECILcesisDDGSssyPSGQWLPGASINPAHNCLNLNGERSLNDTVILWrnELQDD 202
Cdd:PRK00174 26 SVEDPEGFWAEQAKR--LDWFKPFDTVL-----DWNA---PFIKWFEDGELNVSYNCLDRHLKTRGDKVAIIW--EGDDP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 203 LPLQRMTLEELRQEVWLVAYALESLGLEKGSAIAIDMPMHCKSVVIYLA---------IVLAGyvvvsiadsFAPREISS 273
Cdd:PRK00174 94 GDSRKITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLAcarigavhsVVFGG---------FSAEALAD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 274 RLKISNAKVIFTQDLILRGDKTLPLySRIVDAESPMA------IVIPTRGSEFSMKlrDG-DLAWCNFMDGVNKIKGKEF 346
Cdd:PRK00174 165 RIIDAGAKLVITADEGVRGGKPIPL-KANVDEALANCpsvekvIVVRRTGGDVDWV--EGrDLWWHELVAGASDECEPEP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 347 IAVEEPVetFtnILFSSGTTGDPKAIPWTNISPLkaaadAWCHL------DVRKGDVVsWPT-NLGWMMG-PWLVYASLL 418
Cdd:PRK00174 242 MDAEDPL--F--ILYTSGSTGKPKGVLHTTGGYL-----VYAAMtmkyvfDYKDGDVY-WCTaDVGWVTGhSYIVYGPLA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 419 NGASMALYNG---SPLGSGFAKFVQDSKVTMLGVIPSLVRS---WRNANSTsGFDWSAIRCFASTGEASNIDEYLWlmgr 492
Cdd:PRK00174 312 NGATTLMFEGvpnYPDPGRFWEVIDKHKVTIFYTAPTAIRAlmkEGDEHPK-KYDLSSLRLLGSVGEPINPEAWEW---- 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 493 aHYK-------PIIEYCGGTEIGGGFVT---GsllqaqslaAFSTPAMCCS--LF-----ILDDQGHPIPQNV------- 548
Cdd:PRK00174 387 -YYKvvggercPIVDTWWQTETGGIMITplpG---------ATPLKPGSATrpLPgiqpaVVDEEGNPLEGGEggnlvik 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 549 ---PGMgelalgplMLGasntlLNADH------Y-----GVYFKgmpiwngkvlrrhGDVFERTARGYYHAHGRADDTMN 614
Cdd:PRK00174 457 dpwPGM--------MRT-----IYGDHerfvktYfstfkGMYFT-------------GDGARRDEDGYYWITGRVDDVLN 510
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 615 LGGIKVSSVEIEricngadS------NILETAAIGIPPSGGGpeQLALA-VVLKNSNVTSQDlltLRMSFNSALQKTLNP 687
Cdd:PRK00174 511 VSGHRLGTAEIE-------SalvahpKVAEAAVVGRPDDIKG--QGIYAfVTLKGGEEPSDE---LRKELRNWVRKEIGP 578
|
650 660
....*....|....*....|....*...
gi 502086856 688 LFRVSQVVPVPSLPRTASNKVMRRVLRQ 715
Cdd:PRK00174 579 IAKPDVIQFAPGLPKTRSGKIMRRILRK 606
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
102-715 |
7.87e-34 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 138.11 E-value: 7.87e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 102 KEFLGSAYKDPITSFADFQKFSVSNPEVYWKTVLGEMNISFSKPPECILCESIsdDGSSSYPSGQWLPGASINPAHNCLN 181
Cdd:PLN02654 18 KDFSAQALVSSPQQYMEMYKRSVDDPAGFWSDIASQFYWKQKWEGDEVCSENL--DVRKGPISIEWFKGGKTNICYNCLD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 182 LNGERSLNDTV-ILWR-NELQDDLPLqrmTLEELRQEVWLVAYALESLGLEKGSAIAIDMPMHCKSVVIYLAIVLAGYVV 259
Cdd:PLN02654 96 RNVEAGNGDKIaIYWEgNEPGFDASL---TYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVH 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 260 VSIADSFAPREISSRLKISNAKVIFTQDLILRGDKTLPLySRIVDA-------ESPMAIVIPTRGSEFSMKLRDG----- 327
Cdd:PLN02654 173 SVVFAGFSAESLAQRIVDCKPKVVITCNAVKRGPKTINL-KDIVDAaldesakNGVSVGICLTYENQLAMKREDTkwqeg 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 328 -DLAWCNFMDGVNKIKGKEFIAVEEPVetftNILFSSGTTGDPKAIPWTNISPLKAAADAWCH-LDVRKGDVVSWPTNLG 405
Cdd:PLN02654 252 rDVWWQDVVPNYPTKCEVEWVDAEDPL----FLLYTSGSTGKPKGVLHTTGGYMVYTATTFKYaFDYKPTDVYWCTADCG 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 406 WMMG-PWLVYASLLNGASMALYNGSP--LGSGFA-KFVQDSKVTMLGVIPSLVRSWRNANS--TSGFDWSAIRCFASTGE 479
Cdd:PLN02654 328 WITGhSYVTYGPMLNGATVLVFEGAPnyPDSGRCwDIVDKYKVTIFYTAPTLVRSLMRDGDeyVTRHSRKSLRVLGSVGE 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 480 ASNIDEYLW---LMGRAHYkPIIEYCGGTEIGGGFVT---GSLLQAQSLAAFstPAMCCSLFILDDQGHPIPQNVPGMge 553
Cdd:PLN02654 408 PINPSAWRWffnVVGDSRC-PISDTWWQTETGGFMITplpGAWPQKPGSATF--PFFGVQPVIVDEKGKEIEGECSGY-- 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 554 LALGPLMLGASNTLLnADH---YGVYFKGMPIWNGKvlrrhGDVFERTARGYYHAHGRADDTMNLGGIKVSSVEIERICN 630
Cdd:PLN02654 483 LCVKKSWPGAFRTLY-GDHeryETTYFKPFAGYYFS-----GDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALV 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 631 gADSNILETAAIGIPPSGGGpeQLALAVVLKNSNVTSQDllTLRMSFNSALQKTLNPLFRVSQVVPVPSLPRTASNKVMR 710
Cdd:PLN02654 557 -SHPQCAEAAVVGIEHEVKG--QGIYAFVTLVEGVPYSE--ELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMR 631
|
....*
gi 502086856 711 RVLRQ 715
Cdd:PLN02654 632 RILRK 636
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
114-714 |
9.98e-33 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 134.31 E-value: 9.98e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 114 TSFADFQKFSVSNPEVYWktvlGEM--NISFSKPPECILcesisDDgsSSYPSGQWLPGASINPAHNCLNLNGERSLNDT 191
Cdd:PRK10524 2 MSYSEFYQRSIDDPEAFW----AEQarRIDWQTPFTQVL-----DY--SNPPFARWFVGGRTNLCHNAVDRHLAKRPEQL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 192 VILW-RNELQDDlplQRMTLEELRQEVWLVAYALESLGLEKGSAIAIDMPMHCKSVVIYLAIVLAGYVVVSIADSFAPRE 270
Cdd:PRK10524 71 ALIAvSTETDEE---RTYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIHSVVFGGFASHS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 271 ISSRLKISNAKVIFTQDLILRGDKTLPlYSRIVD-----AES-PMAIVIPTRGSEfSMKLRDG-DLAWCN----FMDGVN 339
Cdd:PRK10524 148 LAARIDDAKPVLIVSADAGSRGGKVVP-YKPLLDeaialAQHkPRHVLLVDRGLA-PMARVAGrDVDYATlraqHLGARV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 340 KIkgkEFIAVEEPvetfTNILFSSGTTGDPKAIPWTNISPLKAAADAWCHL-DVRKGDVVSWPTNLGWMMG-PWLVYASL 417
Cdd:PRK10524 226 PV---EWLESNEP----SYILYTSGTTGKPKGVQRDTGGYAVALATSMDTIfGGKAGETFFCASDIGWVVGhSYIVYAPL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 418 LNGASMALYNGSPL---GSGFAKFVQDSKVTMLGVIPSLVRSWRNANST--SGFDWSAIRCFASTGEAsnIDE--YLWLM 490
Cdd:PRK10524 299 LAGMATIMYEGLPTrpdAGIWWRIVEKYKVNRMFSAPTAIRVLKKQDPAllRKHDLSSLRALFLAGEP--LDEptASWIS 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 491 GrAHYKPIIEYCGGTEIGGGFVT---GSLLQAQSLAAFSTPAMCCSLFILDDQ-GHPIPQNVPGMgeLAL-GPLMLGASN 565
Cdd:PRK10524 377 E-ALGVPVIDNYWQTETGWPILAiarGVEDRPTRLGSPGVPMYGYNVKLLNEVtGEPCGPNEKGV--LVIeGPLPPGCMQ 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 566 TLLNADHYGV--YFKGMpiwnGKVLRRHGDVFERTARGYYHAHGRADDTMNLGGIKVSSVEIERiCNGADSNILETAAIG 643
Cdd:PRK10524 454 TVWGDDDRFVktYWSLF----GRQVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEE-SISSHPAVAEVAVVG 528
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502086856 644 IPPSGGGpeQLALA-VVLKNSNVTSQDllTLRMSFNSALQKT----LNPLFRVSQVVPVPSLPRTASNKVMRRVLR 714
Cdd:PRK10524 529 VKDALKG--QVAVAfVVPKDSDSLADR--EARLALEKEIMALvdsqLGAVARPARVWFVSALPKTRSGKLLRRAIQ 600
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
209-714 |
1.28e-31 |
|
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: 128.22 E-value: 1.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 209 TLEELRQEVWLVAYALESLGLEKGSAIAIDMPMHCKSVVIYLAIVLAGYVVVSIADSFAPREISSRLKISNAKVIftqdl 288
Cdd:cd05972 2 SFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAI----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 289 ilrgdktlplysrIVDAESPMAIviptrgsefsmklrdgdlawcnfmdgvnkikgkefiaveepvetftniLFSSGTTGD 368
Cdd:cd05972 77 -------------VTDAEDPALI------------------------------------------------YFTSGTTGL 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 369 PKAIPWTNISPLKAAADAWCHLDVRKGDVVSWPTNLGWMMGPWL-VYASLLNGASMALYNGSPL-GSGFAKFVQDSKVTM 446
Cdd:cd05972 96 PKGVLHTHSYPLGHIPTAAYWLGLRPDDIHWNIADPGWAKGAWSsFFGPWLLGATVFVYEGPRFdAERILELLERYGVTS 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 447 LGVIPSLVRSWRNANsTSGFDWSAIRCFASTGEASNIDEYLWlmGRAHYK-PIIEYCGGTEIGggfVTGSLLQAQSL--A 523
Cdd:cd05972 176 FCGPPTAYRMLIKQD-LSSYKFSHLRLVVSAGEPLNPEVIEW--WRAATGlPIRDGYGQTETG---LTVGNFPDMPVkpG 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 524 AFSTPAMCCSLFILDDQGHPIPQNVPGMGELALGP--LMLGasntllnadHYGVYFKGMPIWNGKVLRRhGDVFERTARG 601
Cdd:cd05972 250 SMGRPTPGYDVAIIDDDGRELPPGEEGDIAIKLPPpgLFLG---------YVGDPEKTEASIRGDYYLT-GDRAYRDEDG 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 602 YYHAHGRADDTMNLGGIKVSSVEIER--ICNGAdsnILETAAIGIP-PSGGgpeQLALA-VVLKN----SNVTSQDLLTL 673
Cdd:cd05972 320 YFWFVGRADDIIKSSGYRIGPFEVESalLEHPA---VAEAAVVGSPdPVRG---EVVKAfVVLTSgyepSEELAEELQGH 393
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 502086856 674 rmsfnsaLQKTLNPLFRVSQVVPVPSLPRTASNKVMRRVLR 714
Cdd:cd05972 394 -------VKKVLAPYKYPREIEFVEELPKTISGKIRRVELR 427
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
206-714 |
1.95e-29 |
|
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: 121.80 E-value: 1.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 206 QRMTLEELRQEVWLVAYALESLGLEKGSAIAIDMPMHCKSVVIYLAIVLAGYVVVSIADSFAPREISSRLKISNAKVIft 285
Cdd:cd05919 9 RSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLV-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 286 qdlilrgdktlplysrIVDAEspmaiviptrgsefsmklrdgDLAWcnfmdgvnkikgkefiaveepvetftnILFSSGT 365
Cdd:cd05919 87 ----------------VTSAD---------------------DIAY---------------------------LLYSSGT 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 366 TGDPKAIPWTNISPLkAAADAWCH--LDVRKGDVVSWPTNL--GWMMG-----PWLVyasllnGASMALYNGSPLGSGFA 436
Cdd:cd05919 103 TGPPKGVMHAHRDPL-LFADAMAReaLGLTPGDRVFSSAKMffGYGLGnslwfPLAV------GASAVLNPGWPTAERVL 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 437 KFVQDSKVTMLGVIPSLVRSWRNANSTSGFDWSAIRCFASTGEAsnIDEYLWLMGRAHY-KPIIEYCGGTEIGGGFVTGS 515
Cdd:cd05919 176 ATLARFRPTVLYGVPTFYANLLDSCAGSPDALRSLRLCVSAGEA--LPRGLGERWMEHFgGPILDGIGATEVGHIFLSNR 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 516 LLQAQsLAAFSTPAMCCSLFILDDQGHPIPQNVPGMGELALGPLMLGASNtllNADHYGVYFKGMpiWngkvlRRHGDVF 595
Cdd:cd05919 254 PGAWR-LGSTGRPVPGYEIRLVDEEGHTIPPGEEGDLLVRGPSAAVGYWN---NPEKSRATFNGG--W-----YRTGDKF 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 596 ERTARGYYHAHGRADDTMNLGGIKVSSVEIERiCNGADSNILETAAIGIPPSGGGpEQLALAVVLKNSNVTSQDLLTLRM 675
Cdd:cd05919 323 CRDADGWYTHAGRADDMLKVGGQWVSPVEVES-LIIQHPAVAEAAVVAVPESTGL-SRLTAFVVLKSPAAPQESLARDIH 400
|
490 500 510
....*....|....*....|....*....|....*....
gi 502086856 676 SFnsaLQKTLNPLFRVSQVVPVPSLPRTASNKVMRRVLR 714
Cdd:cd05919 401 RH---LLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
206-716 |
6.07e-29 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 121.55 E-value: 6.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 206 QRMTLEELRQEVWLVAYALESLGLEKGSAIAIDMPMHCKSVVIYLAIVLAGYVVVSIADSFAPREISSRLKISNAKVIFT 285
Cdd:PRK07656 29 QRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYILARGDAKALFV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 286 QDLILRGDKtlPLYSRIVDAESpmAIVIPTRGSEfsmKLRDGDLAWCNFMdgvnKIKGKEFIAVEEPVETFTNILFSSGT 365
Cdd:PRK07656 109 LGLFLGVDY--SATTRLPALEH--VVICETEEDD---PHTEKMKTFTDFL----AAGDPAERAPEVDPDDVADILFTSGT 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 366 TGDPKAIPWTNISPLKAAADaWCH-LDVRKGD--VVSWPT--NLGWMMGpWLvyASLLNGASMAlyngsPLgsgfAKF-- 438
Cdd:PRK07656 178 TGRPKGAMLTHRQLLSNAAD-WAEyLGLTEGDryLAANPFfhVFGYKAG-VN--APLMRGATIL-----PL----PVFdp 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 439 ------VQDSKVTMLGVIPSLVRSWRNANSTSGFDWSAIRcFASTGEAS-------NIDEYLwlmgraHYKPIIEYCGGT 505
Cdd:PRK07656 245 devfrlIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLR-LAVTGAASmpvalleRFESEL------GVDIVLTGYGLS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 506 EiGGGFVTGSLL--QAQSLAAFS-TPAMCCSLFILDDQGHPIPQNVPgmGELAL-GP-LMLGasntllnadhygvYFKgM 580
Cdd:PRK07656 318 E-ASGVTTFNRLddDRKTVAGTIgTAIAGVENKIVNELGEEVPVGEV--GELLVrGPnVMKG-------------YYD-D 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 581 PIWNGKVLR-----RHGDVFERTARGYYHAHGRADDTMNLGGIKVSSVEIERICnGADSNILETAAIGIPpsgggPEQLA 655
Cdd:PRK07656 381 PEATAAAIDadgwlHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVL-YEHPAVAEAAVIGVP-----DERLG 454
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 656 LA----VVLKN-SNVTSQDLLT---LRMSfNsalqktlnplFRV-SQVVPVPSLPRTASNKVMRRVLRQQ 716
Cdd:PRK07656 455 EVgkayVVLKPgAELTEEELIAycrEHLA-K----------YKVpRSIEFLDELPKNATGKVLKRALREK 513
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
209-714 |
1.97e-27 |
|
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: 116.06 E-value: 1.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 209 TLEELRQEVWLVAYALESLGLEKGSAIAIDMPMHCKSVVIYLAIVLAGYVVVSIADSFAPREISSRLKISNAKV-IFTQD 287
Cdd:cd05969 2 TFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVlITTEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 288 LILRGDKTLPLYsrivdaespmaiviptrgsefsmklrdgdlawcnfmdgvnkikgkefiaveepvetftnILFSSGTTG 367
Cdd:cd05969 82 LYERTDPEDPTL-----------------------------------------------------------LHYTSGTTG 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 368 DPKAIPWTNISPLKAAADAWCHLDVRKGDVVsWPT-NLGWMMGP-WLVYASLLNGASMALYNGSPLGSGFAKFVQDSKVT 445
Cdd:cd05969 103 TPKGVLHVHDAMIFYYFTGKYVLDLHPDDIY-WCTaDPGWVTGTvYGIWAPWLNGVTNVVYEGRFDAESWYGIIERVKVT 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 446 MLGVIPSLVRSWRNANS--TSGFDWSAIRCFASTGEASNIDEYLWLMgRAHYKPIIEYCGGTEIGGGFVTGSLLQAQSLA 523
Cdd:cd05969 182 VWYTAPTAIRMLMKEGDelARKYDLSSLRFIHSVGEPLNPEAIRWGM-EVFGVPIHDTWWQTETGSIMIANYPCMPIKPG 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 524 AFSTPAMCCSLFILDDQGHPIPQNVpgMGELALGP----LMLGASNtllNADHYGVYFKgmpiwNGKVLRrhGDVFERTA 599
Cdd:cd05969 261 SMGKPLPGVKAAVVDENGNELPPGT--KGILALKPgwpsMFRGIWN---DEERYKNSFI-----DGWYLT--GDLAYRDE 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 600 RGYYHAHGRADDTMNLGGIKVSSVEIEricngadSNIL------ETAAIGIP-PSGGgpEQLALAVVLKNSNVTSQDL-L 671
Cdd:cd05969 329 DGYFWFVGRADDIIKTSGHRVGPFEVE-------SALMehpavaEAGVIGKPdPLRG--EIIKAFISLKEGFEPSDELkE 399
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 502086856 672 TLRMSFNSALQKTLNPlfrvSQVVPVPSLPRTASNKVMRRVLR 714
Cdd:cd05969 400 EIINFVRQKLGAHVAP----REIEFVDNLPKTRSGKIMRRVLK 438
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
358-714 |
3.87e-26 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 111.61 E-value: 3.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 358 NILFSSGTTGDPKAIPWTNISPLKAAADAWCHLDVRKGDVVSWPTNLGWMMG-PWLVYASLLNGASMALYNG-SPlgSGF 435
Cdd:cd05934 85 SILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGEDDVYLTVLPLFHINAqAVSVLAALSVGATLVLLPRfSA--SRF 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 436 AKFVQDSKVTM---LGVIPSLV-----RSWRNANStsgfdwsaIR-CFASTGEASNIDEYLWLMGrahyKPIIEYCGGTE 506
Cdd:cd05934 163 WSDVRRYGATVtnyLGAMLSYLlaqppSPDDRAHR--------LRaAYGAPNPPELHEEFEERFG----VRLLEGYGMTE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 507 IGGGfVTGSLLQAQSLAAFSTPAMCCSLFILDDQGHPIPQNVPGmgELALGP-----LMLGasntllnadhygvYFkGMP 581
Cdd:cd05934 231 TIVG-VIGPRDEPRRPGSIGRPAPGYEVRIVDDDGQELPAGEPG--ELVIRGlrgwgFFKG-------------YY-NMP 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 582 IWNGKVLR----RHGDVFERTARGYYHAHGRADDTMNLGGIKVSSVEIERICNGADSnILETAAIGIPPSGGGpEQLALA 657
Cdd:cd05934 294 EATAEAMRngwfHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPA-VREAAVVAVPDEVGE-DEVKAV 371
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 502086856 658 VVLKNSNVTSQDlltlrmSFNSALQKTLNPLFRVSQVVPVPSLPRTASNKVMRRVLR 714
Cdd:cd05934 372 VVLRPGETLDPE------ELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
206-719 |
3.09e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 107.19 E-value: 3.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 206 QRMTLEELRQEVWLVAYALESLGLEKGSAIAI---DMPMHcksVVIYLAIVLAGYVVVSIADSFAPREISSRLKISNAKV 282
Cdd:PRK06187 30 RRTTYAELDERVNRLANALRALGVKKGDRVAVfdwNSHEY---LEAYFAVPKIGAVLHPINIRLKPEEIAYILNDAEDRV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 283 IFTqdlilrGDKTLPLYSR-----------IVDAESPMAIVIPTRGsEFSMKLRDGDLAwcnfmdgvnkikgKEFIAVEE 351
Cdd:PRK06187 107 VLV------DSEFVPLLAAilpqlptvrtvIVEGDGPAAPLAPEVG-EYEELLAAASDT-------------FDFPDIDE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 352 pvETFTNILFSSGTTGDPKAIPWT--NISPLKAAADAWchLDVRKGDV--VSWPTN----LGWMmgpwlvYASLLNGASM 423
Cdd:PRK06187 167 --NDAAAMLYTSGTTGHPKGVVLShrNLFLHSLAVCAW--LKLSRDDVylVIVPMFhvhaWGLP------YLALMAGAKQ 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 424 aLYNGSPLGSGFAKFVQDSKVTMLGVIPSLVRSWRNANSTSGFDWSAIRCFASTGEA---SNIDEYLWLMGRahykPIIE 500
Cdd:PRK06187 237 -VIPRRFDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFVDFSSLRLVIYGGAAlppALLREFKEKFGI----DLVQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 501 YCGGTEIGGgFVTGSLLQAQSLAAFS------TPAMCCSLFILDDQGHPIPQNVPGMGELAL-GP-LMLGasntllnadh 572
Cdd:PRK06187 312 GYGMTETSP-VVSVLPPEDQLPGQWTkrrsagRPLPGVEARIVDDDGDELPPDGGEVGEIIVrGPwLMQG---------- 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 573 ygvYFKgMPIWNGKVLR----RHGDVFERTARGYYHAHGRADDTMNLGGIKVSSVEIERICNGADSnILETAAIGIPPSG 648
Cdd:PRK06187 381 ---YWN-RPEATAETIDggwlHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPA-VAEVAVIGVPDEK 455
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502086856 649 GGPEQLALAVVLKNSNVTSQDLLTLrmsfnsaLQKTLNPLFRVSQVVPVPSLPRTASNKVMRRVLRQQLVE 719
Cdd:PRK06187 456 WGERPVAVVVLKPGATLDAKELRAF-------LRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLREQYAE 519
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
206-713 |
4.55e-23 |
|
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: 102.99 E-value: 4.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 206 QRMTLEELRQEVWLVAYALESLGLEKGSAIAIDMPMHCKSVVIYLAIVLAG--YVVVSIADsfaPRE-ISSRLKISNAKV 282
Cdd:cd05930 11 QSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGaaYVPLDPSY---PAErLAYILEDSGAKL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 283 IFTQDlilrgdktlplysrivdaespmaiviptrgsefsmklrdGDLAWcnfmdgvnkikgkefiaveepvetftnILFS 362
Cdd:cd05930 88 VLTDP---------------------------------------DDLAY---------------------------VIYT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 363 SGTTGDPK--AIPWTNISPLkaAADAWCHLDVRKGDVVSWPTNLGWMMGPWLVYASLLNGASMALYNGSPLGSG--FAKF 438
Cdd:cd05930 102 SGSTGKPKgvMVEHRGLVNL--LLWMQEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPeaLADL 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 439 VQDSKVTMLGVIPSLVRSWRNANSTSGFdwSAIRCFASTGEASNiDEYLWLMGRAHYKPIIEYCGG-TEIGGGFVTGSLL 517
Cdd:cd05930 180 LAEEGITVLHLTPSLLRLLLQELELAAL--PSLRLVLVGGEALP-PDLVRRWRELLPGARLVNLYGpTEATVDATYYRVP 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 518 QAQSLAAFST---PAMCCSLFILDDQGHPIPQNVPgmGELALGplmlGASNTL-------LNADHygvyFKGMPIWNGKV 587
Cdd:cd05930 257 PDDEEDGRVPigrPIPNTRVYVLDENLRPVPPGVP--GELYIG----GAGLARgylnrpeLTAER----FVPNPFGPGER 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 588 LRRHGDVFERTARG--YYhaHGRADDTMNLGGIKVSSVEIERICNgADSNILETAAIGIpPSGGGPEQLALAVVLKNSNV 665
Cdd:cd05930 327 MYRTGDLVRWLPDGnlEF--LGRIDDQVKIRGYRIELGEIEAALL-AHPGVREAAVVAR-EDGDGEKRLVAYVVPDEGGE 402
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 502086856 666 TSQDllTLRmsfnSALQKTLNPLFRVSQVVPVPSLPRTASNKVMRRVL 713
Cdd:cd05930 403 LDEE--ELR----AHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
167-714 |
5.17e-22 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 100.74 E-value: 5.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 167 WLPGASINPAHNCL--NLNGERSlNDTVILWRnelqDDLPLQRMTLEELRQEVWLVAYALESLGLEKGSAIAIDMPMHCK 244
Cdd:PRK04319 36 WLETGKVNIAYEAIdrHADGGRK-DKVALRYL----DASRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 245 SVVIYLAIVLAGYVVVSIADSFAPREISSRLKISNAKVIFTqdlilrgdkTLPLYSRIVDAESP--MAIVIPTRGSEfsm 322
Cdd:PRK04319 111 LYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLIT---------TPALLERKPADDLPslKHVLLVGEDVE--- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 323 kLRDGDLAWCNFMDGVNKIKGKEFIAVEEPVetftnIL-FSSGTTGDPK-AIPWTNISPLKAAADAWChLDVRKGDVVsW 400
Cdd:PRK04319 179 -EGPGTLDFNALMEQASDEFDIEWTDREDGA-----ILhYTSGSTGKPKgVLHVHNAMLQHYQTGKYV-LDLHEDDVY-W 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 401 PT-NLGWMMG-PWLVYASLLNGASMALYNGSPLGSGFAKFVQDSKVTMLGVIPSLVRSWRNANS--TSGFDWSAIRCFAS 476
Cdd:PRK04319 251 CTaDPGWVTGtSYGIFAPWLNGATNVIDGGRFSPERWYRILEDYKVTVWYTAPTAIRMLMGAGDdlVKKYDLSSLRHILS 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 477 TGEASNIDEYLWLMgRAHYKPIIEYCGGTEIGGgfvtgsllqaQSLAafSTPAM------------CCSLFILDDQGHPI 544
Cdd:PRK04319 331 VGEPLNPEVVRWGM-KVFGLPIHDNWWMTETGG----------IMIA--NYPAMdikpgsmgkplpGIEAAIVDDQGNEL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 545 PQNVpgMGELALGP----LMLGASNtllNADHYGVYFKGmpiwnGKVLRrhGDVFERTARGYYHAHGRADDTMNLGGIKV 620
Cdd:PRK04319 398 PPNR--MGNLAIKKgwpsMMRGIWN---NPEKYESYFAG-----DWYVS--GDSAYMDEDGYFWFQGRVDDVIKTSGERV 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 621 SSVEIEricngadSNILETAA------IGIP-PSGGgpEQLALAVVLKNSNVTSQDL-LTLRMSFNSALQKTLNPlfrvS 692
Cdd:PRK04319 466 GPFEVE-------SKLMEHPAvaeagvIGKPdPVRG--EIIKAFVALRPGYEPSEELkEEIRGFVKKGLGAHAAP----R 532
|
570 580
....*....|....*....|..
gi 502086856 693 QVVPVPSLPRTASNKVMRRVLR 714
Cdd:PRK04319 533 EIEFKDKLPKTRSGKIMRRVLK 554
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
201-709 |
2.39e-21 |
|
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: 98.05 E-value: 2.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 201 DDLPLQRMTLEELRQEVWLVAYALESLGLEKGSAIAIDMPMHCKSVVIYLAIVLAGYVVVSIADSFAPREISSRLKISNA 280
Cdd:cd05911 4 DADTGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 281 KVIFTQDlilrgdKTLPLYSRIVDAESPMAIVIPTRGSEFSMKLRDGDLAWcnfMDGVNKIKgkEFIAVEEPVETFTNIL 360
Cdd:cd05911 84 KVIFTDP------DGLEKVKEAAKELGPKDKIIVLDDKPDGVLSIEDLLSP---TLGEEDED--LPPPLKDGKDDTAAIL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 361 FSSGTTGDPKAIPWTN---ISPLKAAADAWCHLDvRKGDVVSWPTNLGWMMGPWLVYASLLNGASMALYNGSPLGSgFAK 437
Cdd:cd05911 153 YSSGTTGLPKGVCLSHrnlIANLSQVQTFLYGND-GSNDVILGFLPLYHIYGLFTTLASLLNGATVIIMPKFDSEL-FLD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 438 FVQDSKVTMLGVIPSLVRSWRNANSTSGFDWSAIRCFASTGEASNIDEYLWLMGRAHYKPIIEYCGGTEigggfvtgsll 517
Cdd:cd05911 231 LIEKYKITFLYLVPPIAAALAKSPLLDKYDLSSLRVILSGGAPLSKELQELLAKRFPNATIKQGYGMTE----------- 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 518 qaqslaafSTPAMCCSLFILDDQGHpIPQNVPGM--------GELALGPLMLGAsntllnadhygVYFKGMPIWNG---- 585
Cdd:cd05911 300 --------TGGILTVNPDGDDKPGS-VGRLLPNVeakivdddGKDSLGPNEPGE-----------ICVRGPQVMKGyynn 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 586 ----KVL------RRHGDVFERTARGYYHAHGRADDTMNLGGIKVSSVEIERICNgADSNILETAAIGIP-PSGGgpeQL 654
Cdd:cd05911 360 peatKETfdedgwLHTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLL-EHPGVADAAVIGIPdEVSG---EL 435
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 502086856 655 ALA-VVLK-NSNVTSQDLLTLrMSFNSALQKTLNplfrvSQVVPVPSLPRTASNKVM 709
Cdd:cd05911 436 PRAyVVRKpGEKLTEKEVKDY-VAKKVASYKQLR-----GGVVFVDEIPKSASGKIL 486
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
207-715 |
3.93e-21 |
|
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: 96.68 E-value: 3.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 207 RMTLEELRQEVWLVAYALESLGLEKGSAIAIDMPMHCKSVVIYLAIVLAGYVVVSIADSFAPREISSRLKISNAKVIFtq 286
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 287 dlilrgdktlplysrivdaespmaivIPTRGSEFSMklrdgdlawcnfmdgvnkikgkefiaVEEPVETfTNILFSSGTT 366
Cdd:cd05903 79 --------------------------VPERFRQFDP--------------------------AAMPDAV-ALLLFTSGTT 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 367 GDPKAIPWTNiSPLKAAADAWC-HLDVRKGDVVSWPTNLGWMMGpwlvyasLLNGASMALYNGSP--LGSGF-----AKF 438
Cdd:cd05903 106 GEPKGVMHSH-NTLSASIRQYAeRLGLGPGDVFLVASPMAHQTG-------FVYGFTLPLLLGAPvvLQDIWdpdkaLAL 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 439 VQDSKVTMLGVIPSLVRSWRNANSTSGFDWSAIRCFASTGEA--SNIDEYLWLMGRAHYKPIIeycGGTEIGGgfVTGSL 516
Cdd:cd05903 178 MREHGVTFMMGATPFLTDLLNAVEEAGEPLSRLRTFVCGGATvpRSLARRAAELLGAKVCSAY---GSTECPG--AVTSI 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 517 LQAQSLAAFST---PAMCCSLFILDDQGHPIPQNVPGmGELALGPLMLGAsntllnadhygvYFKGmPIWNGKVLR---- 589
Cdd:cd05903 253 TPAPEDRRLYTdgrPLPGVEIKVVDDTGATLAPGVEG-ELLSRGPSVFLG------------YLDR-PDLTADAAPegwf 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 590 RHGDVFERTARGYYHAHGRADDTMNLGGIKVSSVEIERICNGADSnILETAAIGIPPSGGGpEQLALAVVLKNSnvTSQD 669
Cdd:cd05903 319 RTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPG-VIEAAVVALPDERLG-ERACAVVVTKSG--ALLT 394
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 502086856 670 LLTLRMSFNS---ALQKTlnPlfrvSQVVPVPSLPRTASNKVMRRVLRQ 715
Cdd:cd05903 395 FDELVAYLDRqgvAKQYW--P----ERLVHVDDLPRTPSGKVQKFRLRE 437
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
205-715 |
5.80e-21 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 96.35 E-value: 5.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 205 LQRMTLEELRQEVWLVAYALESLGLEKGSAIAIDMPMHCKSVVIYLAIVLAGYVVVSIADSFAPREISSRLKISNAKVIF 284
Cdd:cd05971 4 PEKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 285 TqdlilrgdktlplysrivDAESPMAIVIptrgsefsmklrdgdlawcnfmdgvnkikgkefiaveepvetftnilFSSG 364
Cdd:cd05971 84 T------------------DGSDDPALII-----------------------------------------------YTSG 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 365 TTGDPKAIPWTNISPL-KAAADAWCH-LDVRKGDVVSWPTNLGWMMGpwlvyasLLNGASMALYNGSP-LGSGFAKF--- 438
Cdd:cd05971 99 TTGPPKGALHAHRVLLgHLPGVQFPFnLFPRDGDLYWTPADWAWIGG-------LLDVLLPSLYFGVPvLAHRMTKFdpk 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 439 -----VQDSKVTMLGVIPSLVRSWRNANSTSGFDWSAIRCFASTGEASNIDEYLWlmGRAHYK-PIIEYCGGTEigGGFV 512
Cdd:cd05971 172 aaldlMSRYGVTTAFLPPTALKMMRQQGEQLKHAQVKLRAIATGGESLGEELLGW--AREQFGvEVNEFYGQTE--CNLV 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 513 TGSLLQAQSL--AAFSTPAMCCSLFILDDQGHPIPQNVpgMGELALgplMLGASNTLLNadhygvYFKG-----MPIwNG 585
Cdd:cd05971 248 IGNCSALFPIkpGSMGKPIPGHRVAIVDDNGTPLPPGE--VGEIAV---ELPDPVAFLG------YWNNpsateKKM-AG 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 586 KVLRRhGDVFERTARGYYHAHGRADDTMNLGGIKVSSVEIERiCNGADSNILETAAIGIP-PSGGgpEQLALAVVLKNSN 664
Cdd:cd05971 316 DWLLT-GDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEE-CLLKHPAVLMAAVVGIPdPIRG--EIVKAFVVLNPGE 391
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 502086856 665 VTSQDLltlrmsfNSALQ---KT-LNPLFRVSQVVPVPSLPRTASNKVMRRVLRQ 715
Cdd:cd05971 392 TPSDAL-------AREIQelvKTrLAAHEYPREIEFVNELPRTATGKIRRRELRA 439
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
208-715 |
1.18e-19 |
|
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: 92.20 E-value: 1.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 208 MTLEELRQEVWLVAYALESLGLEKGSAIAIDMPMHCKSVVIYLAIVLAGYVVVSIADSFAPREISSRLKISNAKVIftqd 287
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLV---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 288 lilrgdktlplysrIVDAESpmaiviptrgsefSMKLRDGDLAwcnfmdgvnkikgkefiaveepvetftnILFSSGTTG 367
Cdd:cd05973 77 --------------VTDAAN-------------RHKLDSDPFV----------------------------MMFTSGTTG 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 368 DPKAIPwtniSPLKAAAdAWCH-----LDVRKGDVVSWPTNLGWMMGpwLVYA---SLLNGASMALYNGsplgsGFA--- 436
Cdd:cd05973 102 LPKGVP----VPLRALA-AFGAylrdaVDLRPEDSFWNAADPGWAYG--LYYAitgPLALGHPTILLEG-----GFSves 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 437 --KFVQDSKVTMLGVIPSLVRSWRNANSTSGFDWSA-IRCFASTGEASNIDEYLWLmGRAHYKPIIEYCGGTEIG----G 509
Cdd:cd05973 170 twRVIERLGVTNLAGSPTAYRLLMAAGAEVPARPKGrLRRVSSAGEPLTPEVIRWF-DAALGVPIHDHYGQTELGmvlaN 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 510 GFVTGSLLQAQSlAAFSTPAMCCSlfILDDQGHPIPQNVPGMgeLAL----GPLMLgasntllnadHYGVYFKGMPIWNG 585
Cdd:cd05973 249 HHALEHPVHAGS-AGRAMPGWRVA--VLDDDGDELGPGEPGR--LAIdianSPLMW----------FRGYQLPDTPAIDG 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 586 KVLRRhGDVFERTARGYYHAHGRADDTMNLGGIKVSSVEIERICNGADSnILETAAIGIPPSGGGpEQLALAVVLKNSNV 665
Cdd:cd05973 314 GYYLT-GDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPA-VAEAAVIGVPDPERT-EVVKAFVVLRGGHE 390
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 502086856 666 TSQDLLT-LRMSFNSALQKTLNPlfrvSQVVPVPSLPRTASNKVMRRVLRQ 715
Cdd:cd05973 391 GTPALADeLQLHVKKRLSAHAYP----RTIHFVDELPKTPSGKIQRFLLRR 437
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
220-714 |
1.44e-19 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 92.12 E-value: 1.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 220 VAYALESLGLEKGSAIAIDMPMHCKSVVIYLAIVLAG----YVVVSIADSFAPREISSRLKISNAKVIFTQD-LILRGDK 294
Cdd:cd05922 6 AASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGgrlgLVFVPLNPTLKESVLRYLVADAGGRIVLADAgAADRLRD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 295 TLPLYS---------RIVDAESPMAIVIPTrgsefsmklrDGDLAWcnfmdgvnkikgkefiaveepvetftnILFSSGT 365
Cdd:cd05922 86 ALPASPdpgtvldadGIRAARASAPAHEVS----------HEDLAL---------------------------LLYTSGS 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 366 TGDPKAIPWTNISPLKAAADAWCHLDVRKGDVVSWPTNLGWMMGPWLVYASLLNGASMALYNGSPLGSGFAKFVQDSKVT 445
Cdd:cd05922 129 TGSPKLVRLSHQNLLANARSIAEYLGITADDRALTVLPLSYDYGLSVLNTHLLRGATLVLTNDGVLDDAFWEDLREHGAT 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 446 MLGVIPSLVRSWRNAnstsGFDWSA---IRCFASTG---EASNIDEYLWLM--GRAHykpiIEYcGGTEiggGFVTGSLL 517
Cdd:cd05922 209 GLAGVPSTYAMLTRL----GFDPAKlpsLRYLTQAGgrlPQETIARLRELLpgAQVY----VMY-GQTE---ATRRMTYL 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 518 QAQSLA----AFSTPAMCCSLFILDDQGHPIPQNVPGmgELAL-GPL-MLGASNtllnaDHYGVYFKGMPiwnGKVLRRh 591
Cdd:cd05922 277 PPERILekpgSIGLAIPGGEFEILDDDGTPTPPGEPG--EIVHrGPNvMKGYWN-----DPPYRRKEGRG---GGVLHT- 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 592 GDVFERTARGYYHAHGRADDTMNLGGIKVSSVEIER-ICngADSNILETAAIGIPPSGGgpEQLALAVVLKnSNVTSQDL 670
Cdd:cd05922 346 GDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAaAR--SIGLIIEAAAVGLPDPLG--EKLALFVTAP-DKIDPKDV 420
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 502086856 671 LtlrmsfnSALQKTLNPLFRVSQVVPVPSLPRTASNKVMRRVLR 714
Cdd:cd05922 421 L-------RSLAERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
361-714 |
3.59e-19 |
|
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: 91.00 E-value: 3.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 361 FSSGTTGDPKAIPWTNISPLkAAADAWCH--LDVRKGD--VVSWPTNLGWMMG-----PWLVyasllnGASMALYNGSpL 431
Cdd:cd05958 104 FTSGTTGAPKATMHFHRDPL-ASADRYAVnvLRLREDDrfVGSPPLAFTFGLGgvllfPFGV------GASGVLLEEA-T 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 432 GSGFAKFVQDSKVTMLGVIPSLVRSWRNANSTSGFDWSAIRCFASTGEAsnideylwLMGRAHYK-------PIIEYCGG 504
Cdd:cd05958 176 PDLLLSAIARYKPTVLFTAPTAYRAMLAHPDAAGPDLSSLRKCVSAGEA--------LPAALHRAwkeatgiPIIDGIGS 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 505 TEIGGGFVTGSLLQAQSlAAFSTPAMCCSLFILDDQGHPIPQnvpgmGELalGPLML-GASNTLLNAD-HYGVYFKGMpi 582
Cdd:cd05958 248 TEMFHIFISARPGDARP-GATGKPVPGYEAKVVDDEGNPVPD-----GTI--GRLAVrGPTGCRYLADkRQRTYVQGG-- 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 583 WNGKvlrrhGDVFERTARGYYHAHGRADDTMNLGGIKVSSVEIERICNGADSnILETAAIGIPPSGGGPEQLALaVVLKN 662
Cdd:cd05958 318 WNIT-----GDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPA-VAECAVVGHPDESRGVVVKAF-VVLRP 390
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 502086856 663 SNVTSQDLLtlrmsfnSALQ----KTLNPLFRVSQVVPVPSLPRTASNKVMRRVLR 714
Cdd:cd05958 391 GVIPGPVLA-------RELQdhakAHIAPYKYPRAIEFVTELPRTATGKLQRFALR 439
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
206-713 |
1.01e-18 |
|
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: 89.95 E-value: 1.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 206 QRMTLEELRQEVWLVAYALESLGLEKGSAIAIDMPMHCKSVVIYLAIVLAGYVVVSIADSFAPREISSRLKISNAKVIFT 285
Cdd:cd12117 21 RSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAERLAFMLADAGAKVLLT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 286 QDL---ILRGDKTLPLYSRIVDAESPMAIVIPTRGsefsmklrdGDLAWcnfmdgvnkikgkefiaveepvetftnILFS 362
Cdd:cd12117 101 DRSlagRAGGLEVAVVIDEALDAGPAGNPAVPVSP---------DDLAY---------------------------VMYT 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 363 SGTTGDPKAIPWTNISPLKAAADAWcHLDVRKGDVVSWPTNLGWMMGPWLVYASLLNGASMALYNGSPLGSG--FAKFVQ 440
Cdd:cd12117 145 SGSTGRPKGVAVTHRGVVRLVKNTN-YVTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPdaLGALIA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 441 DSKVTMLGVIPSLVRSWRNANSTSgfdWSAIRCFASTGEASNIdeylwlmgrAHYKPIIEYCGGTEIGGG--------FV 512
Cdd:cd12117 224 EEGVTVLWLTAALFNQLADEDPEC---FAGLRELLTGGEVVSP---------PHVRRVLAACPGLRLVNGygptenttFT 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 513 TGSLLQAQSLAAFS----TPAMCCSLFILDDQGHPIPQNVP------GMGeLALGPLMLGAsntlLNADHygvyFKGMPI 582
Cdd:cd12117 292 TSHVVTELDEVAGSipigRPIANTRVYVLDEDGRPVPPGVPgelyvgGDG-LALGYLNRPA----LTAER----FVADPF 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 583 WNGKVLRRHGDVFERTARGYYHAHGRADDTMNLGGIKVSSVEIERICNGADSniLETAAIGIPPSGGGPEQLALAVVLKN 662
Cdd:cd12117 363 GPGERLYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPG--VREAVVVVREDAGGDKRLVAYVVAEG 440
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 502086856 663 SnVTSQDLltlrmsfNSALQKTLNPLFRVSQVVPVPSLPRTASNKVMRRVL 713
Cdd:cd12117 441 A-LDAAEL-------RAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
111-726 |
1.01e-18 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 90.57 E-value: 1.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 111 DPITSFADFqKFSVSNPEVYWKTVlGEMNISFSKppecILCESISDDGSssYPSgqWLPGASINPAHNCLNLNGERSL-- 188
Cdd:PTZ00237 6 DPFDYENDS-NYANSNPESFWDEV-AKKYVHWDK----MYDKVYSGDEI--YPD--WFKGGELNTCYNVLDIHVKNPLkr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 189 -NDTVILWRNELQDDLPLqrmTLEELRQEVWLVAYALESLGLEKGSAIAIDMP---------MHCKSVVIYLAIVLAGYV 258
Cdd:PTZ00237 76 dQDALIYECPYLKKTIKL---TYYQLYEKVCEFSRVLLNLNISKNDNVLIYMAntlepliamLSCARIGATHCVLFDGYS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 259 VVSIAD---SFAPREI-SSRLKISNAKVI-FTQDLI-------LRGDKTLPLYSRIVDAESPMAIV--IPTRGSEfsmkl 324
Cdd:PTZ00237 153 VKSLIDrieTITPKLIiTTNYGILNDEIItFTPNLKeaielstFKPSNVITLFRNDITSESDLKKIetIPTIPNT----- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 325 rdgdLAWcnfMDGVNKIKGK------EFIAVEEPVETFtnILFSSGTTGDPKAIPWTNISPLKAAADAWCHLDVRKGDVV 398
Cdd:PTZ00237 228 ----LSW---YDEIKKIKENnqspfyEYVPVESSHPLY--ILYTSGTTGNSKAVVRSNGPHLVGLKYYWRSIIEKDIPTV 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 399 SWP-TNLGWMMGPWLVYASLLNGASMALYNGSPLGSG-----FAKFVQDSKVTMLGVIPSLVRSWRN-----ANSTSGFD 467
Cdd:PTZ00237 299 VFShSSIGWVSFHGFLYGSLSLGNTFVMFEGGIIKNKhieddLWNTIEKHKVTHTLTLPKTIRYLIKtdpeaTIIRSKYD 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 468 WSAIRCFASTGEA--SNIDEYlwLMGRAHYKPIIEYcGGTEIGGGFVTGSLLQAQSLAAFSTPAMCCSLFILDDQGHPIP 545
Cdd:PTZ00237 379 LSNLKEIWCGGEVieESIPEY--IENKLKIKSSRGY-GQTEIGITYLYCYGHINIPYNATGVPSIFIKPSILSEDGKELN 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 546 QNvpGMGELALG-PLMLGASNTLL-NADHYGVYFKGMP-IWNGkvlrrhGDVFERTARGYYHAHGRADDTMNLGGIKVSS 622
Cdd:PTZ00237 456 VN--EIGEVAFKlPMPPSFATTFYkNDEKFKQLFSKFPgYYNS------GDLGFKDENGYYTIVSRSDDQIKISGNKVQL 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 623 VEIEricngaDS-----NILETAAIGIPPSGGGPEQLALaVVLKNSNVTSQ-DLLTLRMSFNSALQKTLNPLFRVSQVVP 696
Cdd:PTZ00237 528 NTIE------TSilkhpLVLECCSIGIYDPDCYNVPIGL-LVLKQDQSNQSiDLNKLKNEINNIITQDIESLAVLRKIII 600
|
650 660 670
....*....|....*....|....*....|....*..
gi 502086856 697 VPSLPRTASNKVMRRVLRQ-------QLVENTQSSRI 726
Cdd:PTZ00237 601 VNQLPKTKTGKIPRQIISKflndsnyQLPDNVNDSEI 637
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
204-714 |
1.86e-18 |
|
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: 89.35 E-value: 1.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 204 PLQRMTLEELRQEVWLVAYALESLGLEKGSAIAIDMPMHCKSVVIYLAIVLAGYVVVSIADSFAPREISSRLKISNAKVI 283
Cdd:cd05959 26 DAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 284 FTQDLILRGdktlpLYSRIVDAESPMAIVIPTRGSEFSMKlrDGDLAwcnfmdgvnkikgkEFIAVEEPVETFTNI---- 359
Cdd:cd05959 106 VVSGELAPV-----LAAALTKSEHTLVVLIVSGGAGPEAG--ALLLA--------------ELVAAEAEQLKPAAThadd 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 360 ----LFSSGTTGDPKAIPWTNiSPLKAAADAWCH--LDVRKGDVVSWPTNL--GWMMGPWLVYAsLLNGASMALYNGSPL 431
Cdd:cd05959 165 pafwLYSSGSTGRPKGVVHLH-ADIYWTAELYARnvLGIREDDVCFSAAKLffAYGLGNSLTFP-LSVGATTVLMPERPT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 432 GSGFAKFVQDSKVTMLGVIPSLVRSWRNANSTSGFDWSAIRCFASTGEAsnIDEYLWLMGRAHYK-PIIEYCGGTEIGGG 510
Cdd:cd05959 243 PAAVFKRIRRYRPTVFFGVPTLYAAMLAAPNLPSRDLSSLRLCVSAGEA--LPAEVGERWKARFGlDILDGIGSTEMLHI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 511 FVTgSLLQAQSLAAFSTPAMCCSLFILDDQGHPIPQNVPGmgELalgpLMLGASNTLL---NADHYGVYFKGMpiWNgkv 587
Cdd:cd05959 321 FLS-NRPGRVRYGTTGKPVPGYEVELRDEDGGDVADGEPG--EL----YVRGPSSATMywnNRDKTRDTFQGE--WT--- 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 588 lrRHGDVFERTARGYYHAHGRADDTMNLGGIKVSSVEIERiCNGADSNILETAAIGIPPSGGGPEQLALaVVLKnSNVTS 667
Cdd:cd05959 389 --RTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVES-ALVQHPAVLEAAVVGVEDEDGLTKPKAF-VVLR-PGYED 463
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 502086856 668 QDLLTLRMsfNSALQKTLNPLFRVSQVVPVPSLPRTASNKVMRRVLR 714
Cdd:cd05959 464 SEALEEEL--KEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
206-710 |
4.63e-18 |
|
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: 87.28 E-value: 4.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 206 QRMTLEELRQEVWLVAYALESLGLEKGSAIAIDMPMHCKSVVIYLAIVLAGYVVVSIADSFAPREISSRLKISNAKVIFt 285
Cdd:cd17631 19 RSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAYILADSGAKVLF- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 286 qdlilrgdktlplysrivdaespmaiviptrgsefsmklrdGDLAWcnfmdgvnkikgkefiaveepvetftnILFSSGT 365
Cdd:cd17631 98 -----------------------------------------DDLAL---------------------------LMYTSGT 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 366 TGDPKAIPWTNISPLKAAADAWCHLDVRKGDV--VSWP-TNLGWMMGPWLVYasLLNGASMALYNGSPLGSGFAkFVQDS 442
Cdd:cd17631 110 TGRPKGAMLTHRNLLWNAVNALAALDLGPDDVllVVAPlFHIGGLGVFTLPT--LLRGGTVVILRKFDPETVLD-LIERH 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 443 KVTMLGVIPSLVRSWRNANSTSGFDWSAIRCFASTGEASniDEYLWLMGRAHYKPIIEYCGGTEIGGG-FVTGSLLQAQS 521
Cdd:cd17631 187 RVTSFFLVPTMIQALLQHPRFATTDLSSLRAVIYGGAPM--PERLLRALQARGVKFVQGYGMTETSPGvTFLSPEDHRRK 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 522 LAAFSTPAMCCSLFILDDQGHPIPQNVPGmgELAL-GP-LMLGasntllnadhygvYFKgMPIWNGKVLR----RHGDVF 595
Cdd:cd17631 265 LGSAGRPVFFVEVRIVDPDGREVPPGEVG--EIVVrGPhVMAG-------------YWN-RPEATAAAFRdgwfHTGDLG 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 596 ERTARGYYHAHGRADDTMNLGGIKVSSVEIERICNGADSnILETAAIGIPPSGGGpEQLALAVVLKNSN-VTSQDLLT-L 673
Cdd:cd17631 329 RLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPA-VAEVAVIGVPDEKWG-EAVVAVVVPRPGAeLDEDELIAhC 406
|
490 500 510
....*....|....*....|....*....|....*..
gi 502086856 674 RmsfnSALQKTLNPlfrvSQVVPVPSLPRTASNKVMR 710
Cdd:cd17631 407 R----ERLARYKIP----KSVEFVDALPRNATGKILK 435
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
209-715 |
7.99e-18 |
|
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: 86.98 E-value: 7.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 209 TLEELRQEVWLVAYALESLGLEKGSAIAIDMPMHCKSVVIYLAIVLAGYVVVSIADSFAPREISSRLKISNAKVIFTQDL 288
Cdd:cd05926 16 TYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVLTPKG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 289 ----ILRGDKTLplYSRIVDAESPMAIVIPTrgsefsmkLRDGDLAWCNFMDGVNKIKGKefiaVEEPVETFtnILFSSG 364
Cdd:cd05926 96 elgpASRAASKL--GLAILELALDVGVLIRA--------PSAESLSNLLADKKNAKSEGV----PLPDDLAL--ILHTSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 365 TTGDPKAIPWTNISpLKAAADAWC---HLDVRKGDVVSWPtnL----GWMMGpwlVYASLLNGASMALyngsPLGSGFAK 437
Cdd:cd05926 160 TTGRPKGVPLTHRN-LAASATNITntyKLTPDDRTLVVMP--LfhvhGLVAS---LLSTLAAGGSVVL----PPRFSAST 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 438 F---VQDSKVTMLGVIPSLVRSW-RNANSTSGFDWSAIR----CFASTGEA--SNIDEYLwlmgRAhykPIIEYCGGTEi 507
Cdd:cd05926 230 FwpdVRDYNATWYTAVPTIHQILlNRPEPNPESPPPKLRfirsCSASLPPAvlEALEATF----GA---PVLEAYGMTE- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 508 gggfvtgsllqaQSLAAFSTP-------------AMCCSLFILDDQGHPIPQNVpgMGELAL-GP-LMLGASN----TLL 568
Cdd:cd05926 302 ------------AAHQMTSNPlppgprkpgsvgkPVGVEVRILDEDGEILPPGV--VGEICLrGPnVTRGYLNnpeaNAE 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 569 NADHYGvYFkgmpiwngkvlrRHGDVFERTARGYYHAHGRADDTMNLGGIKVSSVEIERICNGADsNILETAAIGIPPSG 648
Cdd:cd05926 368 AAFKDG-WF------------RTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHP-AVLEAVAFGVPDEK 433
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502086856 649 GGpEQLALAVVLK-NSNVTSQDLLtlrmsfnSALQKTLNPlFRV-SQVVPVPSLPRTASNKVMRRVLRQ 715
Cdd:cd05926 434 YG-EEVAAAVVLReGASVTEEELR-------AFCRKHLAA-FKVpKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
206-714 |
1.15e-17 |
|
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: 86.46 E-value: 1.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 206 QRMTLEELRQEVWLVAYALESLGLEKGSAIAIDMPMHCKSVVIYLAIVLAGYVVVSIADSFAPREISSRLKISNAKVIFT 285
Cdd:cd05936 23 RKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPRELEHILNDSGAKALIV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 286 qdlilrgdkTLPLYSRIVDAESPMAIVIPTRGSefsmklrdgdlawcnfmdgvnkikgkefIAVeepvetftnILFSSGT 365
Cdd:cd05936 103 ---------AVSFTDLLAAGAPLGERVALTPED----------------------------VAV---------LQYTSGT 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 366 TGDPKAIPWT--NISPLKAAADAWCHLDVRKGDVVSWPTNL----GWMMGpwlVYASLLNGASMAL-YNGSPLGsgFAKF 438
Cdd:cd05936 137 TGVPKGAMLThrNLVANALQIKAWLEDLLEGDDVVLAALPLfhvfGLTVA---LLLPLALGATIVLiPRFRPIG--VLKE 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 439 VQDSKVT-MLGViPSLVRSWRNANSTSGFDWSAIRCFASTGEAsnideylwlMGRAHYK--------PIIEYCGGTEigg 509
Cdd:cd05936 212 IRKHRVTiFPGV-PTMYIALLNAPEFKKRDFSSLRLCISGGAP---------LPVEVAErfeeltgvPIVEGYGLTE--- 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 510 gfvtgsllqaqslaafSTPAMCCSLF-------------------ILDDQGHPIPqnvPG-MGELAL-GP-LMLGasntl 567
Cdd:cd05936 279 ----------------TSPVVAVNPLdgprkpgsigiplpgtevkIVDDDGEELP---PGeVGELWVrGPqVMKG----- 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 568 lnadhygvYFKgMPIWNGKVLR----RHGDVFERTARGYYHAHGRADDTMNLGGIKVSSVEIERiCNGADSNILETAAIG 643
Cdd:cd05936 335 --------YWN-RPEETAEAFVdgwlRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEE-VLYEHPAVAEAAVVG 404
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502086856 644 IP-PSGGgpEQLALAVVLKN-SNVTSQDLltlrMSFnsaLQKTLNPLFRVSQVVPVPSLPRTASNKVMRRVLR 714
Cdd:cd05936 405 VPdPYSG--EAVKAFVVLKEgASLTEEEI----IAF---CREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
208-714 |
1.47e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 83.44 E-value: 1.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 208 MTLEELRQEVWLVAYALESLGLEKGSAIAIdmpMHCKSVVIYLAIVLAGYVVVSIA---DSFAP---REISSRLKIsnAK 281
Cdd:PRK07788 75 LTYAELDEQSNALARGLLALGVRAGDGVAV---LARNHRGFVLALYAAGKVGARIIllnTGFSGpqlAEVAAREGV--KA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 282 VIFTQDLILRGDKTLPLYSRI------VDAESPMAIVIPTrgsefsmkLRDgdlawcnFMDGVNKikgkefiaveEPVET 355
Cdd:PRK07788 150 LVYDDEFTDLLSALPPDLGRLrawggnPDDDEPSGSTDET--------LDD-------LIAGSST----------APLPK 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 356 FTN----ILFSSGTTGDPKAIPWTNISPLKAAADAWCHLDVRKGDVVSWPT----NLGWMMGpwlvyasllnGASMALYN 427
Cdd:PRK07788 205 PPKpggiVILTSGTTGTPKGAPRPEPSPLAPLAGLLSRVPFRAGETTLLPApmfhATGWAHL----------TLAMALGS 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 428 GSPLGSGF-----AKFVQDSKVTMLGVIPSLVRswR----NANSTSGFDWSAIRCFASTGEASNIdeylWLMGRAH--YK 496
Cdd:PRK07788 275 TVVLRRRFdpeatLEDIAKHKATALVVVPVMLS--RildlGPEVLAKYDTSSLKIIFVSGSALSP----ELATRALeaFG 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 497 PIIE--YcGGTEIGGGFVTG--SLLQAQSLAAfsTPAMCCSLFILDDQGHPIPQNVPGMGELALGPLMLGASNTllnadh 572
Cdd:PRK07788 349 PVLYnlY-GSTEVAFATIATpeDLAEAPGTVG--RPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGYTDG------ 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 573 ygvyfKGMPIWNGkvLRRHGDVFERTARGYYHAHGRADDTMNLGGIKVSSVEIERICNGADsNILETAAIGIPPSGGGpE 652
Cdd:PRK07788 420 -----RDKQIIDG--LLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHP-DVVEAAVIGVDDEEFG-Q 490
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502086856 653 QLALAVVLK-NSNVTSQDLltlrmsfnsalqKT--LNPLFRVS---QVVPVPSLPRTASNKVMRRVLR 714
Cdd:PRK07788 491 RLRAFVVKApGAALDEDAI------------KDyvRDNLARYKvprDVVFLDELPRNPTGKVLKRELR 546
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
206-713 |
1.25e-15 |
|
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.
Pssm-ID: 341244 [Multi-domain] Cd Length: 482 Bit Score: 80.06 E-value: 1.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 206 QRMTLEELRQEVWLVAYALESLGLEKGSAIAIDMPMHCKSVVIYLAIVLAGYVVVSIADSFAPREISSrlkisnakvift 285
Cdd:cd05920 39 RRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVLALPSHRRSELSA------------ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 286 qdlilrgdktlplysrIVDAESPMAIVIPTRGSEFsmklrdgdlawcnfmDGVNkikgkEFIAVEEPVETFTNILFSSGT 365
Cdd:cd05920 107 ----------------FCAHAEAVAYIVPDRHAGF---------------DHRA-----LARELAESIPEVALFLLSGGT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 366 TGDPKAIPWTN---ISPLKAAADaWCHLDVRKGDVVSWPTNLGWMMGPWLVYASLLNGASMALY-NGSPlGSGFAkFVQD 441
Cdd:cd05920 151 TGTPKLIPRTHndyAYNVRASAE-VCGLDQDTVYLAVLPAAHNFPLACPGVLGTLLAGGRVVLApDPSP-DAAFP-LIER 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 442 SKVTMLGVIPSLVRSWRNANSTSGFDWSAIRcFASTGEASnideylwlMGRAHYKPIIEYCGGT-----EIGGGFVTGSL 516
Cdd:cd05920 228 EGVTVTALVPALVSLWLDAAASRRADLSSLR-LLQVGGAR--------LSPALARRVPPVLGCTlqqvfGMAEGLLNYTR 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 517 LQAQSLAAFSTPAMCCS----LFILDDQGHPIPqnvPG-MGELAL-GPLML-------GASNTLLNADhyGVYfkgmpiw 583
Cdd:cd05920 299 LDDPDEVIIHTQGRPMSpddeIRVVDEEGNPVP---PGeEGELLTrGPYTIrgyyrapEHNARAFTPD--GFY------- 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 584 ngkvlrRHGDVFERTARGYYHAHGRADDTMNLGGIKVSSVEIERICNGADSnILETAAIGIPPSGGGpEQLALAVVLKNS 663
Cdd:cd05920 367 ------RTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPA-VHDAAVVAMPDELLG-ERSCAFVVLRDP 438
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 502086856 664 NVTSQDLLTLRMSFNSALQKtlnplfRVSQVVPVPSLPRTASNKVMRRVL 713
Cdd:cd05920 439 PPSAAQLRRFLRERGLAAYK------LPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
184-715 |
1.33e-15 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.
Pssm-ID: 341284 [Multi-domain] Cd Length: 518 Bit Score: 80.37 E-value: 1.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 184 GERSLNDTVILWRNelqDDLPLQRMTLEELRQEVWLVAYALESLGLEKGSAIAIDMPMHCKSVVIYLAIVLAGYVVVSIA 263
Cdd:cd12119 5 AARLHGDREIVSRT---HEGEVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTIN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 264 DSFAPREISSRLKISNAKVIFTqdlilrgDKT-LPLYSRIVDAESPMAIVIpTRGSEFSMKLRDGDLAWCNfmdgvnkik 342
Cdd:cd12119 82 PRLFPEQIAYIINHAEDRVVFV-------DRDfLPLLEAIAPRLPTVEHVV-VMTDDAAMPEPAGVGVLAY--------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 343 gKEFIAVEEPVETFTN--------ILFSSGTTGDPKAIPWTNISPL-----KAAADAwchLDVRKGDVV----------S 399
Cdd:cd12119 145 -EELLAAESPEYDWPDfdentaaaICYTSGTTGNPKGVVYSHRSLVlhamaALLTDG---LGLSESDVVlpvvpmfhvnA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 400 WptnlgwmmGpwLVYASLLNGASMALYNGSPLGSGFAKFVQDSKVTMLGVIPS---LVRSWRNANstsGFDWSAIRCFAS 476
Cdd:cd12119 221 W--------G--LPYAAAMVGAKLVLPGPYLDPASLAELIEREGVTFAAGVPTvwqGLLDHLEAN---GRDLSSLRRVVI 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 477 TGEA---SNIDEYlwlmgRAHYKPIIEYCGGTEIGG----GFVTGSLLQAQSLAAFSTPAM----CCS--LFILDDQGHP 543
Cdd:cd12119 288 GGSAvprSLIEAF-----EERGVRVIHAWGMTETSPlgtvARPPSEHSNLSEDEQLALRAKqgrpVPGveLRIVDDDGRE 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 544 IPQNVPGMGELAL-GPLMLGAsntllnadhygvYFKG----MPIWNGKVLRRhGDVFERTARGYYHAHGRADDTMNLGGI 618
Cdd:cd12119 363 LPWDGKAVGELQVrGPWVTKS------------YYKNdeesEALTEDGWLRT-GDVATIDEDGYLTITDRSKDVIKSGGE 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 619 KVSSVEIERICNGADSnILETAAIGIPPSGGGPEQLALAVVLKNSNVTSQDLLTLrmsFNSALQKTLNPlfrvSQVVPVP 698
Cdd:cd12119 430 WISSVELENAIMAHPA-VAEAAVIGVPHPKWGERPLAVVVLKEGATVTAEELLEF---LADKVAKWWLP----DDVVFVD 501
|
570
....*....|....*..
gi 502086856 699 SLPRTASNKVMRRVLRQ 715
Cdd:cd12119 502 EIPKTSTGKIDKKALRE 518
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
359-710 |
2.31e-15 |
|
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: 78.07 E-value: 2.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 359 ILFSSGTTGDPKAIPWTNISPLKAAADAWCH-LDVRKGDVVSWPTNLGWMMGPWLVYASLLNGASMALYNGSPLGSGFAK 437
Cdd:cd17635 6 VIFTSGTTGEPKAVLLANKTFFAVPDILQKEgLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGENTTYKSLFK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 438 FVQDSKVTMLGVIPS----LVRSWRNANSTSgfdwSAIRCFASTGEASNIDEYLWLMGRAHYKPIIEYcGGTEIGGGFVT 513
Cdd:cd17635 86 ILTTNAVTTTCLVPTllskLVSELKSANATV----PSLRLIGYGGSRAIAADVRFIEATGLTNTAQVY-GLSETGTALCL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 514 GSLLQAQSLAAFSTPAMCCSLFILDDQGHPIPQNvpGMGELAL-GPLMLGA--SNTLLNADHY-GVYFKGmpiwngkvlr 589
Cdd:cd17635 161 PTDDDSIEINAVGRPYPGVDVYLAATDGIAGPSA--SFGTIWIkSPANMLGywNNPERTAEVLiDGWVNT---------- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 590 rhGDVFERTARGYYHAHGRADDTMNLGGIKVSSVEIERICNGAdSNILETAAIGIPPSGGGpEQLALAVVL---KNSNVT 666
Cdd:cd17635 229 --GDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGV-SGVQECACYEISDEEFG-ELVGLAVVAsaeLDENAI 304
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 502086856 667 SQDLLTLRMSfnsalqktLNPLFRVSQVVPVPSLPRTASNKVMR 710
Cdd:cd17635 305 RALKHTIRRE--------LEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
206-714 |
2.28e-14 |
|
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: 76.23 E-value: 2.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 206 QRMTLEELRQEVWLVAYALESLGLEKGSAIAIDMPMHCKSVVIYLAIVLAGYVVVSIADSFAPREISSRLKISNAKVIFT 285
Cdd:cd17651 19 RRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFMLADAGPVLVLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 286 QD-LILRGDKTLPLYSRIVDAESPMAIVIPTRgsefsMKLRDGDLAWcnfmdgvnkikgkefiaveepvetftnILFSSG 364
Cdd:cd17651 99 HPaLAGELAVELVAVTLLDQPGAAAGADAEPD-----PALDADDLAY---------------------------VIYTSG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 365 TTGDPKA--IPWTNISPLKAAADAwcHLDVRKGDVVSWPTNLGWMMGPWLVYASLLNGASMALYNGS--PLGSGFAKFVQ 440
Cdd:cd17651 147 STGRPKGvvMPHRSLANLVAWQAR--ASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEvrTDPPALAAWLD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 441 DSKVTMLGVIPSLVRSWRNANSTSGFDWSAIRCFASTGEASNIDEYLWLMGRAH-YKPIIEYCGGTE---IGGGFVTGSL 516
Cdd:cd17651 225 EQRISRVFLPTVALRALAEHGRPLGVRLAALRYLLTGGEQLVLTEDLREFCAGLpGLRLHNHYGPTEthvVTALSLPGDP 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 517 LQAQSLAAFSTPAMCCSLFILDDQGHPIPQNVPgmGELALGPLMLgASNTLLNADHYGVYFKGMPIWNGKVLRRHGDVFE 596
Cdd:cd17651 305 AAWPAPPPIGRPIDNTRVYVLDAALRPVPPGVP--GELYIGGAGL-ARGYLNRPELTAERFVPDPFVPGARMYRTGDLAR 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 597 RTARGYYHAHGRADDTMNLGGIKVSSVEIERICNgADSNILETAAIGIPPSGGGPeQLALAVVLKNSnvTSQDLLTLRms 676
Cdd:cd17651 382 WLPDGELEFLGRADDQVKIRGFRIELGEIEAALA-RHPGVREAVVLAREDRPGEK-RLVAYVVGDPE--APVDAAELR-- 455
|
490 500 510
....*....|....*....|....*....|....*...
gi 502086856 677 fnSALQKTLNPLFRVSQVVPVPSLPRTASNKVMRRVLR 714
Cdd:cd17651 456 --AALATHLPEYMVPSAFVLLDALPLTPNGKLDRRALP 491
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
359-714 |
2.71e-14 |
|
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341304 [Multi-domain] Cd Length: 450 Bit Score: 75.87 E-value: 2.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 359 ILFSSGTTGDPKAIPWTNiSPLKAAADAWC-HLDVRKGDVVSWPTNLGWMMGPWLVYASLLNGASMALYNGSPLGSG--F 435
Cdd:cd17649 99 VIYTSGSTGTPKGVAVSH-GPLAAHCQATAeRYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASAdeL 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 436 AKFVQDSKVTMLGVIPSLVRSW-RNANSTSGFDWSAIRCFASTGEASNIDEY-LWLMGRAHYkpIIEYcGGTEiggGFVT 513
Cdd:cd17649 178 AEMVRELGVTVLDLPPAYLQQLaEEADRTGDGRPPSLRLYIFGGEALSPELLrRWLKAPVRL--FNAY-GPTE---ATVT 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 514 GSLLQAQSLAAFSTPAMCC-------SLFILDDQGHPIPQNVPGmgELALGPLML--------GASNTLLNADHYGVyfk 578
Cdd:cd17649 252 PLVWKCEAGAARAGASMPIgrplggrSAYILDADLNPVPVGVTG--ELYIGGEGLargylgrpELTAERFVPDPFGA--- 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 579 gmpiwNGKVLRRHGDVFERTARGYYHAHGRADDTMNLGGIKVSSVEIERiCNGADSNILETAAIGIPpsGGGPEQLALAV 658
Cdd:cd17649 327 -----PGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEA-ALLEHPGVREAAVVALD--GAGGKQLVAYV 398
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 502086856 659 VLKNSNVTSQDLLTLRmsfnSALQKTLNPLFRVSQVVPVPSLPRTASNKVMRRVLR 714
Cdd:cd17649 399 VLRAAAAQPELRAQLR----TALRASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
359-715 |
5.10e-14 |
|
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: 74.65 E-value: 5.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 359 ILFSSGTTGDPKAIPWTNISPLKAAADAWCHLDVRKGDVVSWPTNLGWMMGPWLVYASLLNGASMALYNGSPLGSGFAKf 438
Cdd:cd17653 110 IIFTSGSTGIPKGVMVPHRGVLNYVSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTLVLADPSDPFAHVAR- 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 439 vqdsKVTMLGVIPSLVRSWRNAnstsgfDWSAIRCFASTGEA---SNIDEylWLMGRAhykpIIEYCGGTEIGGGFVTGS 515
Cdd:cd17653 189 ----TVDALMSTPSILSTLSPQ------DFPNLKTIFLGGEAvppSLLDR--WSPGRR----LYNAYGPTECTISSTMTE 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 516 LL--QAQSLAAfstPAMCCSLFILDDQGHPIPQNVPGmgELAL-GP-LMLGASNtllNADHYGVYFKGMPIWNGKVLRRH 591
Cdd:cd17653 253 LLpgQPVTIGK---PIPNSTCYILDADLQPVPEGVVG--EICIsGVqVARGYLG---NPALTASKFVPDPFWPGSRMYRT 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 592 GDVFERTARGYYHAHGRADDTMNLGGIKVSSVEIERICNGADSNILETAAIGIppsgggpEQLALAVVLKnsnvTSQDLL 671
Cdd:cd17653 325 GDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQSQPEVTQAAAIVV-------NGRLVAFVTP----ETVDVD 393
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 502086856 672 TLRmsfnSALQKTLNPLFRVSQVVPVPSLPRTASNKVMRRVLRQ 715
Cdd:cd17653 394 GLR----SELAKHLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
206-713 |
7.64e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 75.76 E-value: 7.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 206 QRMTLEELRQEVWLVAYALESLGLEKGSAIAIDMPMHCKSVVIYLAIVLAGYVVVSIADSFAPREISSRLKISNAKVIFT 285
Cdd:PRK12316 3081 QRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLS 3160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 286 QDLIlrgdkTLPLysrivdaespmaivipTRGSEFSMKLRDGDLAwcnfmdgvnkikGKEFIAVEEPVETFTNILFSSGT 365
Cdd:PRK12316 3161 QSHL-----RLPL----------------AQGVQVLDLDRGDENY------------AEANPAIRTMPENLAYVIYTSGS 3207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 366 TGDPKAIPWTNISPLKAAADAWCHLDVRKGDVVSWPTNLGWMMGPWLVYASLLNGASMALyNGSPLGSGFAKFVQDSKVT 445
Cdd:PRK12316 3208 TGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVL-AGPEDWRDPALLVELINSE 3286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 446 MLGVIPSLVRSWRNA-NSTSGFDWSAIRCFASTGEASNIDeylwLMGRAHYK-PIIEYCGGTEIGGGFVTGSLLQAQSLA 523
Cdd:PRK12316 3287 GVDVLHAYPSMLQAFlEEEDAHRCTSLKRIVCGGEALPAD----LQQQVFAGlPLYNLYGPTEATITVTHWQCVEEGKDA 3362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 524 AF-STPAMCCSLFILDDQGHPIPQNVpgMGELALGPLMLgASNTLLNADHYGVYFKGMPIWNGKVLRRHGDVFERTARGY 602
Cdd:PRK12316 3363 VPiGRPIANRACYILDGSLEPVPVGA--LGELYLGGEGL-ARGYHNRPGLTAERFVPDPFVPGERLYRTGDLARYRADGV 3439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 603 YHAHGRADDTMNLGGIKVSSVEIERiCNGADSNILETAAIGIppsggGPEQLALAVVLKNSNVtsqdllTLRMSFNSALQ 682
Cdd:PRK12316 3440 IEYIGRVDHQVKIRGFRIELGEIEA-RLLEHPWVREAVVLAV-----DGRQLVAYVVPEDEAG------DLREALKAHLK 3507
|
490 500 510
....*....|....*....|....*....|..
gi 502086856 683 KTLnPLFRV-SQVVPVPSLPRTASNKVMRRVL 713
Cdd:PRK12316 3508 ASL-PEYMVpAHLLFLERMPLTPNGKLDRKAL 3538
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
220-719 |
9.11e-14 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 74.40 E-value: 9.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 220 VAYALESLGLEKGSAIAIDMPMHCKSVVIYLAIVLAGYVVVSIADSFAPREISSRLKISNAKVIFT---------QDLIL 290
Cdd:PRK06087 62 LANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFAptlfkqtrpVDLIL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 291 RGDKTLPLYSRI--VDAESPmaiviptrgsefsmklrdgdlawcnfmdGVNKIKGKEFIAVEEPVETFTN--------IL 360
Cdd:PRK06087 142 PLQNQLPQLQQIvgVDKLAP----------------------------ATSSLSLSQIIADYEPLTTAITthgdelaaVL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 361 FSSGTTGDPKAIPWTNISPLkAAADAWC-HLDVRKGDVVSWPTNL----GWMMGpwlVYASLLNGASMAL---YNGSPLg 432
Cdd:PRK06087 194 FTSGTEGLPKGVMLTHNNIL-ASERAYCaRLNLTWQDVFMMPAPLghatGFLHG---VTAPFLIGARSVLldiFTPDAC- 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 433 sgfAKFVQDSKVT-MLGVIPsLVRSWRNANSTSGFDWSAIRCFASTGEA--SNIDEYLWlmgRAHYKpIIEYCGGTEigg 509
Cdd:PRK06087 269 ---LALLEQQRCTcMLGATP-FIYDLLNLLEKQPADLSALRFFLCGGTTipKKVARECQ---QRGIK-LLSVYGSTE--- 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 510 gfvtgsllqaQSLAAFSTPAMCCSLF--------------ILDDQGHPIPQNVPGMgELALGPLML-------GASNTLL 568
Cdd:PRK06087 338 ----------SSPHAVVNLDDPLSRFmhtdgyaaagveikVVDEARKTLPPGCEGE-EASRGPNVFmgyldepELTARAL 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 569 NADhyGVYFKgmpiwngkvlrrhGDVFERTARGYYHAHGRADDTMNLGGIKVSSVEIERICNGAdSNILETAAIGIPPSG 648
Cdd:PRK06087 407 DEE--GWYYS-------------GDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQH-PKIHDACVVAMPDER 470
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502086856 649 GGPEQLALAVVLKNSNVTSQDLLTLRMSfNSALQKTLNPlfrvSQVVPVPSLPRTASNKVMRRVLRQQLVE 719
Cdd:PRK06087 471 LGERSCAYVVLKAPHHSLTLEEVVAFFS-RKRVAKYKYP----EHIVVIDKLPRTASGKIQKFLLRKDIMR 536
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
207-720 |
1.77e-13 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 73.55 E-value: 1.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 207 RMTLEELRQEVWLVAYALESLGLEKGSAIAIDMPMHCKSVVIYLAIVLAGYVVVSIADSFAPREISSRLKISNAKVI--- 283
Cdd:PRK13295 55 RFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAESKVLvvp 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 284 -----FTQDLILRGDK-TLPLYSRI--VDAESPMA----IVIPTRGSEfsmklRDGDLAWCNFMDGVNKIkgkefiavee 351
Cdd:PRK13295 135 ktfrgFDHAAMARRLRpELPALRHVvvVGGDGADSfealLITPAWEQE-----PDAPAILARLRPGPDDV---------- 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 352 pvetfTNILFSSGTTGDPKAI------PWTNISPLKAAadawchLDVRKGDVVSWPTNL----GWMMGPWLvyaSLLNGA 421
Cdd:PRK13295 200 -----TQLIYTSGTTGEPKGVmhtantLMANIVPYAER------LGLGADDVILMASPMahqtGFMYGLMM---PVMLGA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 422 SMALYN-GSPLgsGFAKFVQDSKVT-MLGVIPSLVRSWRNANStSGFDWSAIRCFASTGEAsnIDEYLWLMGRAHYKP-I 498
Cdd:PRK13295 266 TAVLQDiWDPA--RAAELIRTEGVTfTMASTPFLTDLTRAVKE-SGRPVSSLRTFLCAGAP--IPGALVERARAALGAkI 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 499 IEYCGGTEigGGFVTGSLLQAQSLAAFST-----PAMccSLFILDDQGHPIPQNVPGMgelalgPLMLGASNtllnadhY 573
Cdd:PRK13295 341 VSAWGMTE--NGAVTLTKLDDPDERASTTdgcplPGV--EVRVVDADGAPLPAGQIGR------LQVRGCSN-------F 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 574 GVYFKgMPIWNGKVLR---RHGDVFERTARGYYHAHGRADDTMNLGGIKVSSVEIERIC--NGAdsnILETAAIGIPPSG 648
Cdd:PRK13295 404 GGYLK-RPQLNGTDADgwfDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLyrHPA---IAQVAIVAYPDER 479
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502086856 649 GGpEQLALAVVLK-NSNVTSQDLLTLRMSFNSALQktlnplFRVSQVVPVPSLPRTASNKVMRRVLRQQLVEN 720
Cdd:PRK13295 480 LG-ERACAFVVPRpGQSLDFEEMVEFLKAQKVAKQ------YIPERLVVRDALPRTPSGKIQKFRLREMLRGE 545
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
209-626 |
2.47e-13 |
|
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: 72.68 E-value: 2.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 209 TLEELRQEVWLVAYALESL-GLEKGSAIAIDMPMHCKSVVIYLAIVLAGYVVVSIaDSFAPRE-ISSRLKISNAKVIFTQ 286
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPL-DPAYPAErLAFILEDAGARLLLTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 287 D--LILRGDKTLPlysrIVDAESPMAIVIPTRGSEF--SMKLRDGDLAWcnfmdgvnkikgkefiaveepvetftnILFS 362
Cdd:TIGR01733 80 SalASRLAGLVLP----VILLDPLELAALDDAPAPPppDAPSGPDDLAY---------------------------VIYT 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 363 SGTTGDPKAIPWTNISPLKAAADAWCHLDVRKGDVVSWPTNLGWMMGPWLVYASLLNGASMALYNGSPLGSGF---AKFV 439
Cdd:TIGR01733 129 SGSTGRPKGVVVTHRSLVNLLAWLARRYGLDPDDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAallAALI 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 440 QDSKVTMLGVIPSLVRSWRNAnstSGFDWSAIRCFASTGEASNIDEYLWLMGRAHYKPII-EYcGGTEiGGGFVTGSLLQ 518
Cdd:TIGR01733 209 AEHPVTVLNLTPSLLALLAAA---LPPALASLRLVILGGEALTPALVDRWRARGPGARLInLY-GPTE-TTVWSTATLVD 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 519 AQSLAAFS-----TPAMCCSLFILDDQGHPIPQNVPgmGELAL-GP-LMLG-ASNTLLNADHygvyFKGMPIWNGKVLR- 589
Cdd:TIGR01733 284 PDDAPRESpvpigRPLANTRLYVLDDDLRPVPVGVV--GELYIgGPgVARGyLNRPELTAER----FVPDPFAGGDGARl 357
|
410 420 430
....*....|....*....|....*....|....*...
gi 502086856 590 -RHGDVFERTARGYYHAHGRADDTMNLGGIKVSSVEIE 626
Cdd:TIGR01733 358 yRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIE 395
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
208-716 |
3.33e-13 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 72.76 E-value: 3.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 208 MTLEELRQEVWLVAYALESLGLEKGSAIAIDMPMHCKSVVIYLAIVLAGYVVVSIADSFAPREISSRLKISNAKVIFTQD 287
Cdd:PRK06710 50 ITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCLD 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 288 LIlrgdktlplYSRIVDAESPMAI--VIPTRGSEF----------SMKLRDGDLawcnfmdgVNKIKGKEFI----AVEE 351
Cdd:PRK06710 130 LV---------FPRVTNVQSATKIehVIVTRIADFlpfpknllypFVQKKQSNL--------VVKVSESETIhlwnSVEK 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 352 PVETFTNIL-----------FSSGTTGDPKAIPWT--NISPLKAAADAWCHLDVRKGDVVswptnLGWMmgPWL-VYA-- 415
Cdd:PRK06710 193 EVNTGVEVPcdpendlallqYTGGTTGFPKGVMLThkNLVSNTLMGVQWLYNCKEGEEVV-----LGVL--PFFhVYGmt 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 416 -----SLLNGASMALYNGSPLGSGFaKFVQDSKVTMLGVIPSLVRSWRNANSTSGFDWSAIRCFAStGEASNIDEYLWLM 490
Cdd:PRK06710 266 avmnlSIMQGYKMVLIPKFDMKMVF-EAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIRACIS-GSAPLPVEVQEKF 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 491 GRAHYKPIIEYCGGTEIGGGFVTGSLLQAQSLAAFSTP-----AMCCSLfildDQGHPIPqnvPG-MGELAL-GP-LMLG 562
Cdd:PRK06710 344 ETVTGGKLVEGYGLTESSPVTHSNFLWEKRVPGSIGVPwpdteAMIMSL----ETGEALP---PGeIGEIVVkGPqIMKG 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 563 ASNTllnadhygvyfkgmPIWNGKVLR----RHGDVFERTARGYYHAHGRADDTMNLGGIKVSSVEIERICNGADsNILE 638
Cdd:PRK06710 417 YWNK--------------PEETAAVLQdgwlHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHE-KVQE 481
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502086856 639 TAAIGIPPSGGGpEQLALAVVLKNSNVTSQDLLtlrmsfNSALQKTLnPLFRVSQVVPVPS-LPRTASNKVMRRVLRQQ 716
Cdd:PRK06710 482 VVTIGVPDPYRG-ETVKAFVVLKEGTECSEEEL------NQFARKYL-AAYKVPKVYEFRDeLPKTTVGKILRRVLIEE 552
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
208-713 |
4.31e-13 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 72.35 E-value: 4.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 208 MTLEELRQEVWLVAYALESLGLEKGSAIAIDMPMHCKSVVIYLAIVLAGYVVVSIADSFAPREISSRLKISNAKVIftqd 287
Cdd:PRK05857 42 LRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAAIERFCQITDPAAA---- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 288 LILRGDKtlplysriVDAESPMAIVIPTRGSEFSMKLRDGDLAwCNFmdGVNKIKGKEFIAVEEPVEtftnILFSSGTTG 367
Cdd:PRK05857 118 LVAPGSK--------MASSAVPEALHSIPVIAVDIAAVTRESE-HSL--DAASLAGNADQGSEDPLA----MIFTSGTTG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 368 DPKAIPWTNIS----P--LKAAADAWchLDVRKGDVVSWPTNLGWMMGPWLVYASLLNGASmaLYNGSPLGSGFAKFVQD 441
Cdd:PRK05857 183 EPKAVLLANRTffavPdiLQKEGLNW--VTWVVGETTYSPLPATHIGGLWWILTCLMHGGL--CVTGGENTTSLLEILTT 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 442 SKVTMLGVIPSLVRSWRNANSTSGFDWSAIRcFASTGEASNIDEYLWLMGRAHYKPIIEYcGGTEIGGGFV-----TGSL 516
Cdd:PRK05857 259 NAVATTCLVPTLLSKLVSELKSANATVPSLR-LVGYGGSRAIAADVRFIEATGVRTAQVY-GLSETGCTALclptdDGSI 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 517 LQAQSlAAFSTPAMCCSLFILD-DQGHPipqNVPGMGELA-LGPLMLGASNTLLNadhygvyFKGMPIWNGKVLR----R 590
Cdd:PRK05857 337 VKIEA-GAVGRPYPGVDVYLAAtDGIGP---TAPGAGPSAsFGTLWIKSPANMLG-------YWNNPERTAEVLIdgwvN 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 591 HGDVFERTARGYYHAHGRADDTMNLGGIKVSSVEIERICNGAdSNILETAAIGIPPSGGGPeQLALAVVlKNSNVTSQDL 670
Cdd:PRK05857 406 TGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGV-SGVREAACYEIPDEEFGA-LVGLAVV-ASAELDESAA 482
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 502086856 671 LTLRMSFNSALQKTLNPLFRVSQVVPVPSLPRTASNKVMRRVL 713
Cdd:PRK05857 483 RALKHTIAARFRRESEPMARPSTIVIVTDIPRTQSGKVMRASL 525
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
206-717 |
7.83e-13 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 71.42 E-value: 7.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 206 QRMTLEELRQEVWLVAYALESLGLEKGSAIAIDMpmhCKS---VVIYLAIVLAGYVVVSIaDSFAPRE-ISSRLKISNAK 281
Cdd:cd05918 23 GSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCF---EKSkwaVVAMLAVLKAGGAFVPL-DPSHPLQrLQEILQDTGAK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 282 VIFTqdlilrgdktlplysrivdaESPMaiviptrgsefsmklrdgDLAWcnfmdgvnkikgkefiaveepvetftnILF 361
Cdd:cd05918 99 VVLT--------------------SSPS------------------DAAY---------------------------VIF 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 362 SSGTTGDPKAIPWTNISpLKAAADAWCHLdvrkgdvvswptnlgWMMGP---WLVYASLLNGAS-----MALYNGSPLG- 432
Cdd:cd05918 114 TSGSTGKPKGVVIEHRA-LSTSALAHGRA---------------LGLTSesrVLQFASYTFDVSileifTTLAAGGCLCi 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 433 -------SGFAKFVQDSKVTMLGVIPSLVRSWRNANSTSgfdwsaIRCFASTGEA---SNIDEylWlMGRAH----YKPi 498
Cdd:cd05918 178 pseedrlNDLAGFINRLRVTWAFLTPSVARLLDPEDVPS------LRTLVLGGEAltqSDVDT--W-ADRVRlinaYGP- 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 499 ieycggTE--IgggFVTGSLLQAQSLAAFSTPAMCCSLFILDDQGHPIPqnVP-GM-GELAL-GPLMlgASNTLLNADHY 573
Cdd:cd05918 248 ------AEctI---AATVSPVVPSTDPRNIGRPLGATCWVVDPDNHDRL--VPiGAvGELLIeGPIL--ARGYLNDPEKT 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 574 GVYFKGMPIWNGKVLRRHGDVFERT---ARgyYHAHG------RADDTMNLGGIKVSSVEIERICNGADSNILE-TAAIG 643
Cdd:cd05918 315 AAAFIEDPAWLKQEGSGRGRRLYRTgdlVR--YNPDGsleyvgRKDTQVKIRGQRVELGEIEHHLRQSLPGAKEvVVEVV 392
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 644 IPPSGGGPEQLALAVVLKNSNVTSQDLLTLRMSFN-----------SALQKTLnPLFRVSQV-VPVPSLPRTASNKVMRR 711
Cdd:cd05918 393 KPKDGSSSPQLVAFVVLDGSSSGSGDGDSLFLEPSdefralvaelrSKLRQRL-PSYMVPSVfLPLSHLPLTASGKIDRR 471
|
....*.
gi 502086856 712 VLRQQL 717
Cdd:cd05918 472 ALRELA 477
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
359-715 |
8.30e-13 |
|
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.
Pssm-ID: 341264 [Multi-domain] Cd Length: 442 Bit Score: 71.17 E-value: 8.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 359 ILFSSGTTGDPKAIPWT--NI-SPLKAAADAWchlDVRKGDVVswptnlgWMMGPWLVYASLLNGASMALYNGSP--LGS 433
Cdd:cd05941 94 ILYTSGTTGRPKGVVLThaNLaANVRALVDAW---RWTEDDVL-------LHVLPLHHVHGLVNALLCPLFAGASveFLP 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 434 GF-AKFVQDSK----VTMLGVIPS----LVRSWRNANSTSGFDWSA----IRCFAStGEA----SNIDEYLWLMGRahyk 496
Cdd:cd05941 164 KFdPKEVAISRlmpsITVFMGVPTiytrLLQYYEAHFTDPQFARAAaaerLRLMVS-GSAalpvPTLEEWEAITGH---- 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 497 PIIEYCGGTEIGggFVTGSLLQAQSLAAF-STPAMCCSLFILDDQGHPiPQNVPGMGELAL-GPLMlgasntllnadhyg 574
Cdd:cd05941 239 TLLERYGMTEIG--MALSNPLDGERRPGTvGMPLPGVQARIVDEETGE-PLPRGEVGEIQVrGPSV-------------- 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 575 vyFKGMpiWN-----GKVLR-----RHGDVFERTARGYYHAHGR-ADDTMNLGGIKVSSVEIERICNGADSnILETAAIG 643
Cdd:cd05941 302 --FKEY--WNkpeatKEEFTddgwfKTGDLGVVDEDGYYWILGRsSVDIIKSGGYKVSALEIERVLLAHPG-VSECAVIG 376
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502086856 644 IP-PSGGgpeQLALAVVLKNSNVTSQDLLTLRmsfNSALQKtLNPLFRVSQVVPVPSLPRTASNKVMRRVLRQ 715
Cdd:cd05941 377 VPdPDWG---ERVVAVVVLRAGAAALSLEELK---EWAKQR-LAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
207-713 |
1.59e-12 |
|
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: 70.20 E-value: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 207 RMTLEELRQEVWLVAYALESLGLEKGSAIAIDMPMHCKSVVIYLAIVLAGYVVVSIADSFAPREISSRLKISNAKVIFTq 286
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 287 dlilrgdktlplysrivdaespmaiviptrGSEFSmklrdgDLAWcnfmdgvnkikgkefiaveepvetftnILFSSGTT 366
Cdd:cd05935 80 ------------------------------GSELD------DLAL---------------------------IPYTSGTT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 367 GDPKAIPWTNISPLKAAADAWCHLDVRKGDVVswptnLGWMmgPWLVYASLLNGASMALYNGSPL-------GSGFAKFV 439
Cdd:cd05935 97 GLPKGCMHTHFSAAANALQSAVWTGLTPSDVI-----LACL--PLFHVTGFVGSLNTAVYVGGTYvlmarwdRETALELI 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 440 QDSKVTMLGVIPSLVRSWRNANSTSGFDWSAIRCFASTGeasnideylWLMGRAHYKPIIEYCGGTEIGGGFVTGSL--- 516
Cdd:cd05935 170 EKYKVTFWTNIPTMLVDLLATPEFKTRDLSSLKVLTGGG---------APMPPAVAEKLLKLTGLRFVEGYGLTETMsqt 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 517 ---------LQAQSLAAFSTPAMCCSLfildDQGHPIPQNVpgMGELAL-GPLMlgasntllnadhygvyFKGMpiWN-- 584
Cdd:cd05935 241 htnpplrpkLQCLGIP*FGVDARVIDI----ETGRELPPNE--VGEIVVrGPQI----------------FKGY--WNrp 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 585 -----------GKVLRRHGDVFERTARGYYHAHGRADDTMNLGGIKVSSVEIERICNGADSnILETAAIGIPPSGGGPEQ 653
Cdd:cd05935 297 eeteesfieikGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPA-I*EVCVISVPDERVGEEV 375
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502086856 654 LALaVVLK---NSNVTSQDLLTLRMSFNSALQktlnplfRVSQVVPVPSLPRTASNKVMRRVL 713
Cdd:cd05935 376 KAF-IVLRpeyRGKVTEEDIIEWAREQMAAYK-------YPREVEFVDELPRSASGKILWRLL 430
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
207-713 |
4.79e-12 |
|
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: 69.07 E-value: 4.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 207 RMTLEELRQEVWLVAYALESLGLEKGSAIAIDMPMHCKSVVIYLAIVLAGYVVVSIADSFAPREISsrlkisnakviftq 286
Cdd:cd05923 28 RLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELA-------------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 287 DLILRGDKTLPLysRIVDAEsPMAIVIPTRGSEFSMKLRDGDlawcnfmdGVNKIKGKEFIAVEEPVETFTNILFSSGTT 366
Cdd:cd05923 94 ELIERGEMTAAV--IAVDAQ-VMDAIFQSGVRVLALSDLVGL--------GEPESAGPLIEDPPREPEQPAFVFYTSGTT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 367 GDPKA--IPWTNISPLKAAADAWCHLDVRKGDVVswptnLGWM-----MGPW--LVYASLLNGASMALYNGSPLGSgfAK 437
Cdd:cd05923 163 GLPKGavIPQRAAESRVLFMSTQAGLRHGRHNVV-----LGLMplyhvIGFFavLVAALALDGTYVVVEEFDPADA--LK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 438 FVQDSKVTMLGVIPSLVRSWRNANSTSGFDWSAIRCFASTGeASNIDEYLWLMGRAHYKPIIEYCGGTEIgggfVTGSLL 517
Cdd:cd05923 236 LIEQERVTSLFATPTHLDALAAAAEFAGLKLSSLRHVTFAG-ATMPDAVLERVNQHLPGEKVNIYGTTEA----MNSLYM 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 518 QAQSLAAFSTPAMCCSLFILDDQGHPIPQNVPGM-GELALGplmlgasntlLNADHYGVYFKGMPIWNGKVLR----RHG 592
Cdd:cd05923 311 RDARTGTEMRPGFFSEVRIVRIGGSPDEALANGEeGELIVA----------AAADAAFTGYLNQPEATAKKLQdgwyRTG 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 593 DVFERTARGYYHAHGRADDTMNLGGIKVSSVEIERICnGADSNILETAAIGIPPSGGGpeQLALAVVLKNSNVTSQDLLT 672
Cdd:cd05923 381 DVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVL-SRHPGVTEVVVIGVADERWG--QSVTACVVPREGTLSADELD 457
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 502086856 673 lRMSFNSALQKTLNPlfrvSQVVPVPSLPRTASNKVMRRVL 713
Cdd:cd05923 458 -QFCRASELADFKRP----RRYFFLDELPKNAMNKVLRRQL 493
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
359-713 |
5.23e-12 |
|
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341298 [Multi-domain] Cd Length: 450 Bit Score: 68.49 E-value: 5.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 359 ILFSSGTTGDPKAIPWT--NISPLKAAADAWchLDVRKGDVVSWPTNLGWMMGPWLVYASLLNGASMAL--YNGSPLGSG 434
Cdd:cd17643 98 VIYTSGSTGRPKGVVVShaNVLALFAATQRW--FGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVvpYEVARSPED 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 435 FAKFVQDSKVTMLGVIPSLVRSWRNANSTSGFDWSAIRCFASTGEASNIDeylwlMGRAHYKPIIEYC-------GGTEI 507
Cdd:cd17643 176 FARLLRDEGVTVLNQTPSAFYQLVEAADRDGRDPLALRYVIFGGEALEAA-----MLRPWAGRFGLDRpqlvnmyGITET 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 508 GGgFVTGSLLQAQSLAA-----FSTPAMCCSLFILDDQGHPIPQNVPGmgELALGplmlGASNTL-------LNADHYGV 575
Cdd:cd17643 251 TV-HVTFRPLDAADLPAaaaspIGRPLPGLRVYVLDADGRPVPPGVVG--ELYVS----GAGVARgylgrpeLTAERFVA 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 576 YFKGMPiwnGKVLRRHGDVFERTARGYYHAHGRADDTMNLGGIKVSSVEIERICNGADSniLETAAIGIPPSGGGPEQLA 655
Cdd:cd17643 324 NPFGGP---GSRMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPS--VRDAAVIVREDEPGDTRLV 398
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 502086856 656 LAVVLKNSnvTSQDLLTLRmsfnsALQKTLNPLFRV-SQVVPVPSLPRTASNKVMRRVL 713
Cdd:cd17643 399 AYVVADDG--AAADIAELR-----ALLKELLPDYMVpARYVPLDALPLTVNGKLDRAAL 450
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
207-720 |
6.44e-12 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 68.57 E-value: 6.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 207 RMTLEELRQEVWLVAYALESLGLEKGSAIAIDMPMHCKSVVIYLAIVLAGYVVVSIADSFAPREISSRLKISNAKVIFTQ 286
Cdd:PRK12406 11 RRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 287 DLILRG-DKTLPLYSRIVDAESPMAIVIPTRGSEFSMKLRDGDLAWcnfmdgvnkikgKEFIAVEEP-----VETFTNIL 360
Cdd:PRK12406 91 ADLLHGlASALPAGVTVLSVPTPPEIAAAYRISPALLTPPAGAIDW------------EGWLAQQEPydgppVPQPQSMI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 361 FSSGTTGDPKAIPWTNISPLKAAAdawchldvrkgdvvsWPTNLGWMMGPWLVYASLLNGasmALYNGSPLGSG------ 434
Cdd:PRK12406 159 YTSGTTGHPKGVRRAAPTPEQAAA---------------AEQMRALIYGLKPGIRALLTG---PLYHSAPNAYGlragrl 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 435 --------------FAKFVQDSKVTMLGVIPSL-VRSWR-NANSTSGFDWSAIR--------CFASTGEASnIDeylWlm 490
Cdd:PRK12406 221 ggvlvlqprfdpeeLLQLIERHRITHMHMVPTMfIRLLKlPEEVRAKYDVSSLRhvihaaapCPADVKRAM-IE---W-- 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 491 grahYKPII-EYCGGTEIGGgfVTGsllqAQSLAAFSTPAMC------CSLFILDDQGHPIPQNVPgmGELalgpLMLGA 563
Cdd:PRK12406 295 ----WGPVIyEYYGSTESGA--VTF----ATSEDALSHPGTVgkaapgAELRFVDEDGRPLPQGEI--GEI----YSRIA 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 564 SNTLlnadhygVYFKGMPIWNGKVLR----RHGDVFERTARGYYHAHGRADDTMNLGGIKVSSVEIERICNGAdSNILET 639
Cdd:PRK12406 359 GNPD-------FTYHNKPEKRAEIDRggfiTSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAV-PGVHDC 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 640 AAIGIPPSGGGpEQLAlAVVLKNSNVTsQDLLTLRMSFNSALQKtlnplFRVSQVVPV-PSLPRTASNKVMRRVLRQQLV 718
Cdd:PRK12406 431 AVFGIPDAEFG-EALM-AVVEPQPGAT-LDEADIRAQLKARLAG-----YKVPKHIEImAELPREDSGKIFKRRLRDPYW 502
|
..
gi 502086856 719 EN 720
Cdd:PRK12406 503 AN 504
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
206-713 |
6.54e-12 |
|
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341267 [Multi-domain] Cd Length: 449 Bit Score: 68.43 E-value: 6.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 206 QRMTLEELRQEVWLVAYALESLGLEKGSAIAIDMPMHCKSVVIYLAIVLAGYVVVSIADSFAPreisSRLKisnakvift 285
Cdd:cd05945 15 RTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPA----ERIR--------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 286 qdlilrgdktlplysRIVDAESPMAIVIptrgsefsmklrDG-DLAWcnfmdgvnkikgkefiaveepvetftnILFSSG 364
Cdd:cd05945 82 ---------------EILDAAKPALLIA------------DGdDNAY---------------------------IIFTSG 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 365 TTGDPKAIPWT--NISPLKAAADAwcHLDVRKGDVV----------SwptnlgwMMGpwlVYASLLNGASMALYNGSPLG 432
Cdd:cd05945 108 STGRPKGVQIShdNLVSFTNWMLS--DFPLGPGDVFlnqapfsfdlS-------VMD---LYPALASGATLVPVPRDATA 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 433 SG--FAKFVQDSKVTMLGVIPSLVRSWR-----NANSTSGFDWSAircFAstGEASNIDEYLWLMGRAHYKPIIEYCGGT 505
Cdd:cd05945 176 DPkqLFRFLAEHGITVWVSTPSFAAMCLlsptfTPESLPSLRHFL---FC--GEVLPHKTARALQQRFPDARIYNTYGPT 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 506 EIGGGfVTGSLLQAQSLAAFST-----PAMCCSLFILDDQGHPIPqnVPGMGELAL-GP-LMLGASNtllNADHYGVYFK 578
Cdd:cd05945 251 EATVA-VTYIEVTPEVLDGYDRlpigyAKPGAKLVILDEDGRPVP--PGEKGELVIsGPsVSKGYLN---NPEKTAAAFF 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 579 GMPiwnGKVLRRHGDVFERTARGYYHAHGRADDTMNLGGIKVSSVEIERICNGAdSNILETAAIGIPPSGGGPeQLALAV 658
Cdd:cd05945 325 PDE---GQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQV-PGVKEAVVVPKYKGEKVT-ELIAFV 399
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 502086856 659 VLKNsNVTSQDLLTLRmsfnSALQKTLNPLFRVSQVVPVPSLPRTASNKVMRRVL 713
Cdd:cd05945 400 VPKP-GAEAGLTKAIK----AELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
177-716 |
8.19e-12 |
|
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: 68.29 E-value: 8.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 177 HNCLNLNGERSLN---DTVILWRNELQDDLPL---------QRMTLEELRQEVWLVAYALESLGLEKGSAIAIDMPMHCK 244
Cdd:cd05970 5 HNNFSINVPENFNfayDVVDAMAKEYPDKLALvwcddageeRIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 245 SVVIYLAIVLAGYVVVSIADSFAPREISSRLKISNAKVIftqdlILRGDKTLPLYSRIVDAESPMAIVIPTRGSEfsmkL 324
Cdd:cd05970 85 FWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKMI-----VAIAEDNIPEEIEKAAPECPSKPKLVWVGDP----V 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 325 RDGdlaWCNFMDGVNKIKGkEFIAVEEPVETFTN----ILFSSGTTGDPKAIPWTNISPLKAAADAWCHLDVRKGDVVSW 400
Cdd:cd05970 156 PEG---WIDFRKLIKNASP-DFERPTANSYPCGEdillVYFSSGTTGMPKMVEHDFTYPLGHIVTAKYWQNVREGGLHLT 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 401 PTNLGWMMGPW-LVYASLLNGASMALYNgsplgsgFAKF--------VQDSKVTMLGVIPSLVRSWRNANsTSGFDWSAI 471
Cdd:cd05970 232 VADTGWGKAVWgKIYGQWIAGAAVFVYD-------YDKFdpkallekLSKYGVTTFCAPPTIYRFLIRED-LSRYDLSSL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 472 RCFASTGEASNIDEYLWLMGRAHYKpIIEYCGGTEIGGGFVTGSLLQAQSlAAFSTPAMCCSLFILDDQGHPIPqnVPGM 551
Cdd:cd05970 304 RYCTTAGEALNPEVFNTFKEKTGIK-LMEGFGQTETTLTIATFPWMEPKP-GSMGKPAPGYEIDLIDREGRSCE--AGEE 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 552 GELALGpLMLGASNTLLNadHYG--------VYFKGmpiwngkvLRRHGDVFERTARGYYHAHGRADDTMNLGGIKVSSV 623
Cdd:cd05970 380 GEIVIR-TSKGKPVGLFG--GYYkdaektaeVWHDG--------YYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPF 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 624 EIERICNgADSNILETAAIGIP-PSGGgpeQLALAVVLKNSNVTSQDLLTLRMSFNSalqKTLNPLFRVSQVVP-VPSLP 701
Cdd:cd05970 449 EVESALI-QHPAVLECAVTGVPdPIRG---QVVKATIVLAKGYEPSEELKKELQDHV---KKVTAPYKYPRIVEfVDELP 521
|
570
....*....|....*
gi 502086856 702 RTASNKVMRRVLRQQ 716
Cdd:cd05970 522 KTISGKIRRVEIRER 536
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
359-713 |
9.06e-12 |
|
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: 67.66 E-value: 9.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 359 ILFSSGTTGDPK--AIPWTNISPLKAAADAwcHLDVRKGDVVSWPTNLGWMMGPWLVYASLLNGASMALYNGSPLGSG-- 434
Cdd:cd17652 98 VIYTSGSTGRPKgvVVTHRGLANLAAAQIA--AFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGep 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 435 FAKFVQDSKVTMLGVIPSLVrswrnaNSTSGFDWSAIRCFASTGEA---SNIDEylWLMGRAhykpIIEYCGGTEigggf 511
Cdd:cd17652 176 LADLLREHRITHVTLPPAAL------AALPPDDLPDLRTLVVAGEAcpaELVDR--WAPGRR----MINAYGPTE----- 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 512 VTGSLLQAQSLAAFSTPAMCC-----SLFILDDQGHPIPQNVPGmgELALGplmlGASNTL-------LNADHYGVYFKG 579
Cdd:cd17652 239 TTVCATMAGPLPGGGVPPIGRpvpgtRVYVLDARLRPVPPGVPG--ELYIA----GAGLARgylnrpgLTAERFVADPFG 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 580 MPiwnGKVLRRHGDVFERTARGYYHAHGRADDTMNLGGIKVSSVEIERICNGADSniLETAAIGIPPSGGGPEQL-ALAV 658
Cdd:cd17652 313 AP---GSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPG--VAEAVVVVRDDRPGDKRLvAYVV 387
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 502086856 659 VLKNSNVTSQDLLtlrmsfnSALQKTLNPLFRVSQVVPVPSLPRTASNKVMRRVL 713
Cdd:cd17652 388 PAPGAAPTAAELR-------AHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
206-715 |
1.03e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 68.83 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 206 QRMTLEELRQEVWLVAYALESLGLEKGSAIAIDMPMHCKSVVIYLAIVLAGYVVVSIaDSFAPRE-ISSRLKISNAKVIF 284
Cdd:PRK12316 4575 EKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPL-DPEYPRErLAYMMEDSGAALLL 4653
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 285 TQDLILRGdktLPLysrivdAESPMAIVIPtrgsefsmklRDGDlaWCNF--MDGVNKIKGkefiaveepvETFTNILFS 362
Cdd:PRK12316 4654 TQSHLLQR---LPI------PDGLASLALD----------RDED--WEGFpaHDPAVRLHP----------DNLAYVIYT 4702
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 363 SGTTGDPKA-----------IPWTNISPLKAAADAWCHLDVRKGDVVSWptnlGWMMGpwlvyasLLNGASMALYN-GSP 430
Cdd:PRK12316 4703 SGSTGRPKGvavshgslvnhLHATGERYELTPDDRVLQFMSFSFDGSHE----GLYHP-------LINGASVVIRDdSLW 4771
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 431 LGSGFAKFVQDSKVTMLGVIPSLVRSWRNANSTSGfDWSAIRCFASTGEASNIDEYLWLMGRAHYKPIIEYCGGTEIGgg 510
Cdd:PRK12316 4772 DPERLYAEIHEHRVTVLVFPPVYLQQLAEHAERDG-EPPSLRVYCFGGEAVAQASYDLAWRALKPVYLFNGYGPTETT-- 4848
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 511 fVTGSLLQAQ-------SLAAFSTPAMCCSLFILDDQGHPIPqnVPGMGELALGPLMLGA---SNTLLNADHYGVYFKGM 580
Cdd:PRK12316 4849 -VTVLLWKARdgdacgaAYMPIGTPLGNRSGYVLDGQLNPLP--VGVAGELYLGGEGVARgylERPALTAERFVPDPFGA 4925
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 581 PiwnGKVLRRHGDVFERTARGYYHAHGRADDTMNLGGIKVSSVEIErICNGADSNILETAAIGIPPSGGgpEQLALAVVL 660
Cdd:PRK12316 4926 P---GGRLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIE-ARLREHPAVREAVVIAQEGAVG--KQLVGYVVP 4999
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 502086856 661 KNSNVTSQDLLT--LRMSFNSALQKTLnPLFRV-SQVVPVPSLPRTASNKVMRRVLRQ 715
Cdd:PRK12316 5000 QDPALADADEAQaeLRDELKAALRERL-PEYMVpAHLVFLARMPLTPNGKLDRKALPQ 5056
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
352-717 |
2.16e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 66.75 E-value: 2.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 352 PVETFTNILFSSGTTGDPKAIPWTNISPLKAAAD--AWCHLDVRKGDVVSWP--------TNlgwmmgpwlVYASLLNGA 421
Cdd:PRK09088 133 PPERVSLILFTSGTSGQPKGVMLSERNLQQTAHNfgVLGRVDAHSSFLCDAPmfhiigliTS---------VRPVLAVGG 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 422 SMALYNGSPLGSGFAKFV-QDSKVTMLGVIPSLVRSWRNansTSGFDWSAIRCFAS--TGEASNIDEYL--WLmgrAHYK 496
Cdd:PRK09088 204 SILVSNGFEPKRTLGRLGdPALGITHYFCVPQMAQAFRA---QPGFDAAALRHLTAlfTGGAPHAAEDIlgWL---DDGI 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 497 PIIEYCGGTEIGGGF---VTGSLLQAQSLAA-FSTPAMccSLFILDDQGHPIPQNVPgmGELAL-GP-LMLG------AS 564
Cdd:PRK09088 278 PMVDGFGMSEAGTVFgmsVDCDVIRAKAGAAgIPTPTV--QTRVVDDQGNDCPAGVP--GELLLrGPnLSPGywrrpqAT 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 565 NTLLNADHygvYFkgmpiwngkvlrRHGDVFERTARGYYHAHGRADDTMNLGGIKVSSVEIERICngAD-SNILETAAIG 643
Cdd:PRK09088 354 ARAFTGDG---WF------------RTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVL--ADhPGIRECAVVG 416
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502086856 644 IPPSGGGpEQLALAVVLKNSNVTsqDLLTLRMSFNSALQKTLNPlfrvSQVVPVPSLPRTASNKVMRRVLRQQL 717
Cdd:PRK09088 417 MADAQWG-EVGYLAIVPADGAPL--DLERIRSHLSTRLAKYKVP----KHLRLVDALPRTASGKLQKARLRDAL 483
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
206-719 |
3.53e-11 |
|
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: 66.32 E-value: 3.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 206 QRMTLEELRQEVWLVAYALESLGLEKGSAIAIDMPMHCKSVVIYLAIVLAGYVVVsiadsFAP-----REISSRLKISNA 280
Cdd:COG1021 49 RRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAIPV-----FALpahrrAEISHFAEQSEA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 281 KVIFTQDLILRGDkTLPLYSRIV-DAESPMAIVIptrgsefsmklrDGDLAwcnfmdgvnkikgkEFIA----VEEPVET 355
Cdd:COG1021 124 VAYIIPDRHRGFD-YRALARELQaEVPSLRHVLV------------VGDAG--------------EFTSldalLAAPADL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 356 FTN---------ILFSSGTTGDPKAIPWTN---ISPLKAAADAwCHLDvrKGDV------------VSWPTNLGwmmgpw 411
Cdd:COG1021 177 SEPrpdpddvafFQLSGGTTGLPKLIPRTHddyLYSVRASAEI-CGLD--ADTVylaalpaahnfpLSSPGVLG------ 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 412 lvyaSLLNGASMAL-YNGSPLgSGFAkFVQDSKVTMLGVIPSLVRSWRNANSTSGFDWSAIRcfastgeasnideylwlm 490
Cdd:COG1021 248 ----VLYAGGTVVLaPDPSPD-TAFP-LIERERVTVTALVPPLALLWLDAAERSRYDLSSLR------------------ 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 491 grahykpiieycggteigggfvtgsLLQ------AQSLAAFSTPAMCCSL---F-------------------------- 535
Cdd:COG1021 304 -------------------------VLQvggaklSPELARRVRPALGCTLqqvFgmaeglvnytrlddpeevilttqgrp 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 536 --------ILDDQGHPIPQNVPGmgELAL-GPLmlgasnTL--------LNA---DHYGVYfkgmpiwngkvlrRHGDVF 595
Cdd:COG1021 359 ispddevrIVDEDGNPVPPGEVG--ELLTrGPY------TIrgyyrapeHNArafTPDGFY-------------RTGDLV 417
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 596 ERTARGYYHAHGRADDTMNLGGIKVSSVEIERICNgADSNILETAAIGIP-PSGGgpEQLALAVVLKNSNVTSQDLLTLR 674
Cdd:COG1021 418 RRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLL-AHPAVHDAAVVAMPdEYLG--ERSCAFVVPRGEPLTLAELRRFL 494
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 502086856 675 MSFNSALQKtlnplfRVSQVVPVPSLPRTASNKVMRRVLRQQLVE 719
Cdd:COG1021 495 RERGLAAFK------LPDRLEFVDALPLTAVGKIDKKALRAALAA 533
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
206-719 |
3.73e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 65.96 E-value: 3.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 206 QRMTLEELRQEVWLVAYALESLGlEKGSAIAIDMPMHCKSVVIYLAIVLAGYVVVSIADSFAPREISSRLKISNAKVIFT 285
Cdd:PRK07638 25 RVLTYKDWFESVCKVANWLNEKE-SKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKERLAISNADMIVT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 286 QDLILrgdktlplySRIVDAESPmaiVIptrgsefsmklrdgDLAWCnfmdgvnkikgKEFIAVEEPVETFTNIL----- 360
Cdd:PRK07638 104 ERYKL---------NDLPDEEGR---VI--------------EIDEW-----------KRMIEKYLPTYAPIENVqnapf 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 361 ---FSSGTTGDPKAIPWTNISplkaaadaWCH--------LDVRKGDVVSWPTNLgwmmgpwlVYASLLNGASMALYNG- 428
Cdd:PRK07638 147 ymgFTSGSTGKPKAFLRAQQS--------WLHsfdcnvhdFHMKREDSVLIAGTL--------VHSLFLYGAISTLYVGq 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 429 --------SPLGSgfAKFVQDSKVTMLGVIPSLVRSWRNANST---------SGFDWSAIrcfaSTGEASNIDEYLWLMg 491
Cdd:PRK07638 211 tvhlmrkfIPNQV--LDKLETENISVMYTVPTMLESLYKENRVienkmkiisSGAKWEAE----AKEKIKNIFPYAKLY- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 492 rahykpiiEYCGGTEIGggFVTgSLLQAQSLAAFSTPAMCCslfilddqgHPIPQNVpgmgelalgplmLGASNTLLNAD 571
Cdd:PRK07638 284 --------EFYGASELS--FVT-ALVDEESERRPNSVGRPF---------HNVQVRI------------CNEAGEEVQKG 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 572 HYGVYFKGMPIW-----NGKVLRRHGDVFE-RTAR--------GYYHAHGRADDTMNLGGIKVSSVEIERICNGADSnIL 637
Cdd:PRK07638 332 EIGTVYVKSPQFfmgyiIGGVLARELNADGwMTVRdvgyedeeGFIYIVGREKNMILFGGINIFPEEIESVLHEHPA-VD 410
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 638 ETAAIGIPPSGGGpeQLALAVVLKNSNVTsqdllTLRmsfnSALQKTLNPLFRVSQVVPVPSLPRTASNKVMRRVLRQQL 717
Cdd:PRK07638 411 EIVVIGVPDSYWG--EKPVAIIKGSATKQ-----QLK----SFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAKSWI 479
|
..
gi 502086856 718 VE 719
Cdd:PRK07638 480 EN 481
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
361-710 |
1.63e-10 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 63.19 E-value: 1.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 361 FSSGTTGDPKAipwtnispLKAAADAWCH-LDVRKGDVVSWPTNLGWMMGPwLVYASLLNGASMALYNG---------SP 430
Cdd:cd17633 7 FTSGTTGLPKA--------YYRSERSWIEsFVCNEDLFNISGEDAILAPGP-LSHSLFLYGAISALYLGgtfigqrkfNP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 431 LGsgFAKFVQDSKVTMLGVIPSLVRSWRNANSTSgfdwSAIRCFASTGEASNIDEYLWLMGRAHYKPIIEYCGGTEIGgg 510
Cdd:cd17633 78 KS--WIRKINQYNATVIYLVPTMLQALARTLEPE----SKIKSIFSSGQKLFESTKKKLKNIFPKANLIEFYGTSELS-- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 511 FVTgsllqaqslaafstpamccslFILDDQGHPiPQNVpgmgelalGPLMLGASNTLLNADHYG---VYFKGMPIWNGKV 587
Cdd:cd17633 150 FIT---------------------YNFNQESRP-PNSV--------GRPFPNVEIEIRNADGGEigkIFVKSEMVFSGYV 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 588 LRRH---------GDVFERTARGYYHAHGRADDTMNLGGIKVSSVEIERICNGADSnILETAAIGIPPSGGGpeQLALAV 658
Cdd:cd17633 200 RGGFsnpdgwmsvGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPG-IEEAIVVGIPDARFG--EIAVAL 276
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 502086856 659 VLKNsNVTSQDLLtlrmsfnSALQKTLNPLFRVSQVVPVPSLPRTASNKVMR 710
Cdd:cd17633 277 YSGD-KLTYKQLK-------RFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
359-713 |
2.94e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 64.03 E-value: 2.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 359 ILFSSGTTGDPK--AIPWTNISPLKAAADAWCHLDVRkgDVVSWPTNLGWMMGPWLVYASLLNGASMAL--YNGSPLGSG 434
Cdd:PRK12467 661 VIYTSGSTGQPKgvAISHGALANYVCVIAERLQLAAD--DSMLMVSTFAFDLGVTELFGALASGATLHLlpPDCARDAEA 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 435 FAKFVQDSKVTMLGVIPSLVRSWRNANSTSGFdwSAIRCFASTGEASNID-EYLWLMGRAHYKPIIEYcGGTE--IGGGF 511
Cdd:PRK12467 739 FAALMADQGVTVLKIVPSHLQALLQASRVALP--RPQRALVCGGEALQVDlLARVRALGPGARLINHY-GPTEttVGVST 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 512 VTGSLLQAQSLAAF-STPAMCCSLFILDDQGHPIPqnVPGMGELALGPLML--------GASNTLLNADHYGVyfkgmpi 582
Cdd:PRK12467 816 YELSDEERDFGNVPiGQPLANLGLYILDHYLNPVP--VGVVGELYIGGAGLargyhrrpALTAERFVPDPFGA------- 886
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 583 wNGKVLRRHGDVFERTARGYYHAHGRADDTMNLGGIKVSSVEIERiCNGADSNILETAAIGIPPSGGgpEQLALAVVLKN 662
Cdd:PRK12467 887 -DGGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEA-RLLAQPGVREAVVLAQPGDAG--LQLVAYLVPAA 962
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 502086856 663 SNVTSQdlltlRMSFNSALQKTLN---PLFRV-SQVVPVPSLPRTASNKVMRRVL 713
Cdd:PRK12467 963 VADGAE-----HQATRDELKAQLRqvlPDYMVpAHLLLLDSLPLTPNGKLDRKAL 1012
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
357-710 |
3.47e-10 |
|
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.
Pssm-ID: 341293 [Multi-domain] Cd Length: 330 Bit Score: 62.13 E-value: 3.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 357 TNILFSSGTTGDPKAIPWTNISPLKAAAdAWCHL-DVRKGD----VVSWPTNLGWMMGpWLvyASLLNGAS---MALYNG 428
Cdd:cd17638 3 SDIMFTSGTTGRSKGVMCAHRQTLRAAA-AWADCaDLTEDDryliINPFFHTFGYKAG-IV--ACLLTGATvvpVAVFDV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 429 SPLgsgfAKFVQDSKVTMLGVIPSLVRSWRNANSTSGFDWSAIRcFASTGEASNIDEylwLMGRAH----YKPIIEYCGG 504
Cdd:cd17638 79 DAI----LEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLR-AAVTGAATVPVE---LVRRMRselgFETVLTAYGL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 505 TEIGggfvTGSLLQAQSlaAFSTPAMCCslfilddqGHPIPQ---NVPGMGELAL-GP-LMLG------ASNTLLNADHY 573
Cdd:cd17638 151 TEAG----VATMCRPGD--DAETVATTC--------GRACPGfevRIADDGEVLVrGYnVMQGylddpeATAEAIDADGW 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 574 gvyfkgmpiwngkvlRRHGDVFERTARGYYHAHGRADDTMNLGGIKVSSVEIERICNGADsNILETAAIGIPPSGGGPEQ 653
Cdd:cd17638 217 ---------------LHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHP-GVAQVAVIGVPDERMGEVG 280
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 502086856 654 LALaVVLKNSNVTSQDLLTLRMSFNSALQKTlnPLFrvsqVVPVPSLPRTASNKVMR 710
Cdd:cd17638 281 KAF-VVARPGVTLTEEDVIAWCRERLANYKV--PRF----VRFLDELPRNASGKVMK 330
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
235-708 |
3.79e-10 |
|
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: 62.73 E-value: 3.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 235 IAIDMPMHCKSVVIYLAIVLAGYVVVSIADSFAPREISSRLKISNAKVIFTQDLILRGDKTLPLysriVDAESPMAIV-- 312
Cdd:cd05909 34 VGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLTSKQFIEKLKLHHL----FDVEYDARIVyl 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 313 --IPTRGSeFSMKLRDGDLAWCNFMDGVNKikgkEFIAVEEPVETFTnILFSSGTTGDPKAIPWTNISPLKAAADAWCHL 390
Cdd:cd05909 110 edLRAKIS-KADKCKAFLAGKFPPKWLLRI----FGVAPVQPDDPAV-ILFTSGSEGLPKGVVLSHKNLLANVEQITAIF 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 391 DVRKGDVVSWPT----NLGWMMGPWLvyaSLLNGASMALYNgSPL-GSGFAKFVQDSKVTMLGVIPSLVRSW-RNANSTs 464
Cdd:cd05909 184 DPNPEDVVFGALpffhSFGLTGCLWL---PLLSGIKVVFHP-NPLdYKKIPELIYDKKATILLGTPTFLRGYaRAAHPE- 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 465 gfDWSAIRCFASTGEASNIDEYLWLMGRAHyKPIIEYCGGTEigggfvtgsllqAQSLAAFSTPAM-----CCSLF---- 535
Cdd:cd05909 259 --DFSSLRLVVAGAEKLKDTLRQEFQEKFG-IRILEGYGTTE------------CSPVISVNTPQSpnkegTVGRPlpgm 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 536 ---ILDDQGH-PIPQNVPGMgELALGP-LMLGASNtllnaDHYGVYFKGMPIWNGKvlrrhGDVFERTARGYYHAHGRAD 610
Cdd:cd05909 324 evkIVSVETHeEVPIGEGGL-LLVRGPnVMLGYLN-----EPELTSFAFGDGWYDT-----GDIGKIDGEGFLTITGRLS 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 611 DTMNLGGIKVSSVEIERICNGADSNILETAAIGIPPSGGGpEQLALAVVLKNSNVTsqdlltlrmSFNSALQKT-LNPLF 689
Cdd:cd05909 393 RFAKIAGEMVSLEAIEDILSEILPEDNEVAVVSVPDGRKG-EKIVLLTTTTDTDPS---------SLNDILKNAgISNLA 462
|
490
....*....|....*....
gi 502086856 690 RVSQVVPVPSLPRTASNKV 708
Cdd:cd05909 463 KPSYIHQVEEIPLLGTGKP 481
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
206-713 |
6.59e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 63.05 E-value: 6.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 206 QRMTLEELRQEVWLVAYALESLGLEKGSAIAIDMPMHCKSVVIYLAIVLAG--YVVVsiaDSFAPRE-ISSRLKISNAKV 282
Cdd:PRK12316 535 ETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGgaYVPL---DPEYPAErLAYMLEDSGVQL 611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 283 IFTQDLILRgdkTLPLYSRIVdaespmaiviptrgsefSMKLRDGDLAWCNFMDGVNKIkgkefiavEEPVETFTNILFS 362
Cdd:PRK12316 612 LLSQSHLGR---KLPLAAGVQ-----------------VLDLDRPAAWLEGYSEENPGT--------ELNPENLAYVIYT 663
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 363 SGTTGDPK--AIPWTNISPLKAAADAWCHLDVrkGDVVSWPTNLGWMMGPWLVYASLLNGASMALyngSPLGSGF--AKF 438
Cdd:PRK12316 664 SGSTGKPKgaGNRHRALSNRLCWMQQAYGLGV--GDTVLQKTPFSFDVSVWEFFWPLMSGARLVV---AAPGDHRdpAKL 738
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 439 VQDS---KVTMLGVIPSLVRSW-RNANSTSGFDWSAIRCfasTGEASNIDEYLWLMGRAHYKPIIEYCGGTEIGGGfVTG 514
Cdd:PRK12316 739 VELInreGVDTLHFVPSMLQAFlQDEDVASCTSLRRIVC---SGEALPADAQEQVFAKLPQAGLYNLYGPTEAAID-VTH 814
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 515 SLLQAQSLAAFST--PAMCCSLFILDDQGHPIPQNVpgMGELALGPLMLGAS---NTLLNADHygvyFKGMPIWNGKVLR 589
Cdd:PRK12316 815 WTCVEEGGDSVPIgrPIANLACYILDANLEPVPVGV--LGELYLAGRGLARGyhgRPGLTAER----FVPSPFVAGERMY 888
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 590 RHGDVFERTARGYYHAHGRADDTMNLGGIKVSSVEIERICNGADSnILETAAIGIppsggGPEQLALAVVLKNSNVtsqd 669
Cdd:PRK12316 889 RTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPW-VREAAVLAV-----DGKQLVGYVVLESEGG---- 958
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 502086856 670 llTLRMSFNSALQKTLnPLFRV-SQVVPVPSLPRTASNKVMRRVL 713
Cdd:PRK12316 959 --DWREALKAHLAASL-PEYMVpAQWLALERLPLTPNGKLDRKAL 1000
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
206-713 |
6.80e-10 |
|
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341310 [Multi-domain] Cd Length: 490 Bit Score: 61.96 E-value: 6.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 206 QRMTLEELRQEVWLVAYALESLGLEKGSAIAIDMPMHCKSVVIYLAIVLAGYVVVSIADSFAPREISSRLKISNAKVIFT 285
Cdd:cd17655 21 QTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEERIQYILEDSGADILLT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 286 QDlilrgdktlplysrivdaespmAIVIPTRGSEFSMKLRDGDLawcnfmdgvnKIKGKEFIAVEEPVETFTNILFSSGT 365
Cdd:cd17655 101 QS----------------------HLQPPIAFIGLIDLLDEDTI----------YHEESENLEPVSKSDDLAYVIYTSGS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 366 TGDPKAIPWT--NISPLKAAADAWCHLDvrKGDVVSWPTNLGWMMGPWLVYASLLNGASMALYNGSPLGSG--FAKFVQD 441
Cdd:cd17655 149 TGKPKGVMIEhrGVVNLVEWANKVIYQG--EHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGqaLTQYIRQ 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 442 SKVTMLGVIPSLVRSWRNANSTSGFDwsaIRCFASTGEASNIDEYLWLMGRAHYKPII--EYcGGTEIgggFVTGSLLQA 519
Cdd:cd17655 227 NRITIIDLTPAHLKLLDAADDSEGLS---LKHLIVGGEALSTELAKKIIELFGTNPTItnAY-GPTET---TVDASIYQY 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 520 QSLAAFS------TPAMCCSLFILDDQGHPIPQNVPgmGELALG--PLMLGASN--TLLNADhygvyFKGMPIWNGKVLR 589
Cdd:cd17655 300 EPETDQQvsvpigKPLGNTRIYILDQYGRPQPVGVA--GELYIGgeGVARGYLNrpELTAEK-----FVDDPFVPGERMY 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 590 RHGDVFERTARGYYHAHGRADDTMNLGGIKVSSVEIERICNGADSnILETAAIGIPPSGGGPeQLALAVVLKNSNVTSQd 669
Cdd:cd17655 373 RTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPD-IKEAVVIARKDEQGQN-YLCAYIVSEKELPVAQ- 449
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 502086856 670 lltLRmsfnSALQKTLnPLFRV-SQVVPVPSLPRTASNKVMRRVL 713
Cdd:cd17655 450 ---LR----EFLAREL-PDYMIpSYFIKLDEIPLTPNGKVDRKAL 486
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
209-724 |
7.95e-10 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 61.92 E-value: 7.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 209 TLEELRQEVWLVAYALESLGLEKGSAIAIDMPMHCKSVVIYLAIVLAGYVVVSIADSFAPREISSRLKISNAKVIFTQDL 288
Cdd:PLN02330 57 TYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTNDT 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 289 ilrgdktlpLYSRIVDAESPMAIVIPTRGSefsmklrdGDLAWCNFMDGVNKIKGKefIAVEEPVET-FTNILFSSGTTG 367
Cdd:PLN02330 137 ---------NYGKVKGLGLPVIVLGEEKIE--------GAVNWKELLEAADRAGDT--SDNEEILQTdLCALPFSSGTTG 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 368 DPKAIPWTNISPLkaaADAWCHLDVRKGDVVSWPTNLGWMmgPW--------LVYASLLNGASMALYNGSPLGSgFAKFV 439
Cdd:PLN02330 198 ISKGVMLTHRNLV---ANLCSSLFSVGPEMIGQVVTLGLI--PFfhiygitgICCATLRNKGKVVVMSRFELRT-FLNAL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 440 QDSKVTMLGVIPSLVRSWRNANSTSGFDWSAIRCFASTGEASNIDEYLWLMGRAHYK--PIIEYCGGTE------IGGGF 511
Cdd:PLN02330 272 ITQEVSFAPIVPPIILNLVKNPIVEEFDLSKLKLQAIMTAAAPLAPELLTAFEAKFPgvQVQEAYGLTEhscitlTHGDP 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 512 VTGSLLQAQSLAAFSTPAMCCSlFILDDQGHPIPQNVPGMGELALGPLMLGASN----TLLNADHYGVYFKGmpiwNGKV 587
Cdd:PLN02330 352 EKGHGIAKKNSVGFILPNLEVK-FIDPDTGRSLPKNTPGELCVRSQCVMQGYYNnkeeTDRTIDEDGWLHTG----DIGY 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 588 LRRHGDVFertargyyhAHGRADDTMNLGGIKVSSVEIERICNGADSnILETAAIGIPPSGGGPEQLALAVVLKNSNVTS 667
Cdd:PLN02330 427 IDDDGDIF---------IVDRIKELIKYKGFQVAPAELEAILLTHPS-VEDAAVVPLPDEEAGEIPAACVVINPKAKESE 496
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 502086856 668 QDLLTLrMSFNSALQKtlnplfRVSQVVPVPSLPRTASNKVMRRVLRQQLVENTQSS 724
Cdd:PLN02330 497 EDILNF-VAANVAHYK------KVRVVQFVDSIPKSLSGKIMRRLLKEKMLSINKAN 546
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
184-716 |
8.64e-10 |
|
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: 61.71 E-value: 8.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 184 GERSLNdTVILWRNELQDDLplqRMTLEELRQEVWLVAYAL-ESLGLEKGSAIAIDMPMHCKSVVIYLAIVLAGYVVVSI 262
Cdd:cd05928 22 GKRPPN-PALWWVNGKGDEV---KWSFRELGSLSRKAANVLsGACGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 263 ADSFAPREISSRLKISNAKVIFTqdlilrGDKTLPLYSRIVdAESPmAIVIPTRGSEFSmklRDGdlaWCNFMDGVNKIK 342
Cdd:cd05928 98 TIQLTAKDILYRLQASKAKCIVT------SDELAPEVDSVA-SECP-SLKTKLLVSEKS---RDG---WLNFKELLNEAS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 343 gKEFIAVEEPVETFTNILFSSGTTGDPKAIPWTNIS---PLKAAADAWchLDVRKGDVVSWPTNLGWMMGPW-LVYASLL 418
Cdd:cd05928 164 -TEHHCVETGSQEPMAIYFTSGTTGSPKMAEHSHSSlglGLKVNGRYW--LDLTASDIMWNTSDTGWIKSAWsSLFEPWI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 419 NGA-----SMALYNGSPLGSGFAKFvqdsKVTMLGVIPSLVRSWRNANSTSgFDWSAIRCFASTGEASN---IDEYLWLM 490
Cdd:cd05928 241 QGAcvfvhHLPRFDPLVILKTLSSY----PITTFCGAPTVYRMLVQQDLSS-YKFPSLQHCVTGGEPLNpevLEKWKAQT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 491 GRAHYkpiiEYCGGTEIG--GGFVTGSLLQAQSlaaFSTPAMCCSLFILDDQGHPIPQNVPGMGELALGPLMlgasntll 568
Cdd:cd05928 316 GLDIY----EGYGQTETGliCANFKGMKIKPGS---MGKASPPYDVQIIDDNGNVLPPGTEGDIGIRVKPIR-------- 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 569 nadHYGVY--FKGMPIWNGKVLRRH----GDVFERTARGYYHAHGRADDTMNLGGIKVSSVEIERICNGADSnILETAAI 642
Cdd:cd05928 381 ---PFGLFsgYVDNPEKTAATIRGDfyltGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPA-VVESAVV 456
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502086856 643 GIP-PSGGgpeQLALAVVLKNSNVTSQDLLTLRMSFNSALQKTLNPLFRVSQVVPVPSLPRTASNKVMRRVLRQQ 716
Cdd:cd05928 457 SSPdPIRG---EVVKAFVVLAPQFLSHDPEQLTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRDK 528
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
206-713 |
1.04e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 62.49 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 206 QRMTLEELRQEVWLVAYALESLGLEKGSAIAIDMPMHCKSVVIYLAIVLAGYVVVSIADSFAPREISSRLKISNAKVIFT 285
Cdd:PRK12467 1598 QELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLT 1677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 286 QDLILrgdktlplysrivdAESPMAIVIPtrgsefSMKLRDGDlAWCNFMDGVNKikgkefiAVEEPVETFTNILFSSGT 365
Cdd:PRK12467 1678 QSHLQ--------------ARLPLPDGLR------SLVLDQED-DWLEGYSDSNP-------AVNLAPQNLAYVIYTSGS 1729
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 366 TGDPK--AIPWTNISPLKAAADAWCHLDVrkGDVVSWPTNLGWMMGPWLVYASLLNGASMAL--YNGSPLGSGFAKFVQD 441
Cdd:PRK12467 1730 TGRPKgaGNRHGALVNRLCATQEAYQLSA--ADVVLQFTSFAFDVSVWELFWPLINGARLVIapPGAHRDPEQLIQLIER 1807
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 442 SKVTMLGVIPSLVRSW-----RNANSTSgfdwsaIRCFASTGEASNIDEYLWLMGRAHYKPIIEYCGGTE----IGGGFV 512
Cdd:PRK12467 1808 QQVTTLHFVPSMLQQLlqmdeQVEHPLS------LRRVVCGGEALEVEALRPWLERLPDTGLFNLYGPTEtavdVTHWTC 1881
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 513 TGSLLQAQSLAAFSTPAMCCSLFILDDQGHPIPQNVpgMGELALGPLML--------GASNTLLNADHYGVyfkgmpiwN 584
Cdd:PRK12467 1882 RRKDLEGRDSVPIGQPIANLSTYILDASLNPVPIGV--AGELYLGGVGLargylnrpALTAERFVADPFGT--------V 1951
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 585 GKVLRRHGDVFERTARGYYHAHGRADDTMNLGGIKVSSVEIEricngadSNILETAAIG----IPPSGGGPEQLALAVVL 660
Cdd:PRK12467 1952 GSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIE-------ARLREQGGVReavvIAQDGANGKQLVAYVVP 2024
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 502086856 661 KNSNVTSQDL--LTLRMSFNSALQKTLnPLFRV-SQVVPVPSLPRTASNKVMRRVL 713
Cdd:PRK12467 2025 TDPGLVDDDEaqVALRAILKNHLKASL-PEYMVpAHLVFLARMPLTPNGKLDRKAL 2079
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
206-557 |
2.09e-09 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 61.03 E-value: 2.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 206 QRMTLEELRQEVWLVAYALESLGLEKGSAIAIDMPmhcKS---VVIYLAIVLAG--YVVVsiaDSFAPRE-ISSRLKISN 279
Cdd:COG1020 500 QSLTYAELNARANRLAHHLRALGVGPGDLVGVCLE---RSlemVVALLAVLKAGaaYVPL---DPAYPAErLAYMLEDAG 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 280 AKVIFTQD-----LILRGDKTLPLYSRIVDAESPMAIVIPTRGSefsmklrdgDLAWcnfmdgvnkikgkefiaveepve 354
Cdd:COG1020 574 ARLVLTQSalaarLPELGVPVLALDALALAAEPATNPPVPVTPD---------DLAY----------------------- 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 355 tftnILFSSGTTGDPK--AIPWTNISPLKAAADAWCHLDvrKGDVVSWPTNLGWMMGPWLVYASLLNGASMALYNGSPLG 432
Cdd:COG1020 622 ----VIYTSGSTGRPKgvMVEHRALVNLLAWMQRRYGLG--PGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARR 695
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 433 SG--FAKFVQDSKVTMLGVIPSLVRSWRNANSTsgfDWSAIRCFASTGEAsnideylwlMGRAHYKPIIEYCGGTEI--G 508
Cdd:COG1020 696 DPaaLAELLARHRVTVLNLTPSLLRALLDAAPE---ALPSLRLVLVGGEA---------LPPELVRRWRARLPGARLvnL 763
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 502086856 509 GG------FVTGSLLQAQSLAAFS----TPAMCCSLFILDDQGHPIPQNVPgmGELALG 557
Cdd:COG1020 764 YGptettvDSTYYEVTPPDADGGSvpigRPIANTRVYVLDAHLQPVPVGVP--GELYIG 820
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
206-713 |
2.43e-09 |
|
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: 60.33 E-value: 2.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 206 QRMTLEELRQEVWLVAYALESLGLEKGSAIAIDMPMHCKSVVIYLAIVLAGyVVVSIADSFA-PREISSRLKISNAKVIF 284
Cdd:cd05904 31 RALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLG-AVVTTANPLStPAEIAKQVKDSGAKLAF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 285 TqdlilrgdkTLPLYSRIVDAESPMAIV--IPTRGSEFSMKLRDGDLAWCNfmdgVNKIKGKEFIAveepvetftnILFS 362
Cdd:cd05904 110 T---------TAELAEKLASLALPVVLLdsAEFDSLSFSDLLFEADEAEPP----VVVIKQDDVAA----------LLYS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 363 SGTTGDPKAIPWT--NISPLKAAADAWCHLDVRKGDVVSWPTNLGWMMG-PWLVYASLLNGAS---MALYNgspLGSgFA 436
Cdd:cd05904 167 SGTTGRSKGVMLThrNLIAMVAQFVAGEGSNSDSEDVFLCVLPMFHIYGlSSFALGLLRLGATvvvMPRFD---LEE-LL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 437 KFVQDSKVTMLGVIPSLVRSWRNANSTSGFDWSAIRcFASTGEASnideylwlMGrahyKPIIEYC-------------G 503
Cdd:cd05904 243 AAIERYKVTHLPVVPPIVLALVKSPIVDKYDLSSLR-QIMSGAAP--------LG----KELIEAFrakfpnvdlgqgyG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 504 GTEIGGGfVTGSLLQAQSLAAFST-----PAMCCSlfILD-DQGHPIPQNVPgmGELAL-GP-LMLGASN----TLLNAD 571
Cdd:cd05904 310 MTESTGV-VAMCFAPEKDRAKYGSvgrlvPNVEAK--IVDpETGESLPPNQT--GELWIrGPsIMKGYLNnpeaTAATID 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 572 HYGvyfkgmpiWngkvLRRhGDVFERTARGYYHAHGRADDTMNLGGIKVSSVEIERICNgADSNILETAAIGIPPSGGGP 651
Cdd:cd05904 385 KEG--------W----LHT-GDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLL-SHPEILDAAVIPYPDEEAGE 450
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502086856 652 EQLALAVVLKNSNVTSQDLltlrMSFnsaLQKTLNPLFRVSQVVPVPSLPRTASNKVMRRVL 713
Cdd:cd05904 451 VPMAFVVRKPGSSLTEDEI----MDF---VAKQVAPYKKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
592-716 |
2.69e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 60.08 E-value: 2.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 592 GDVFERTARGYYHAHGRADDTMNLGGIKVSSVEIERICNGADsNILETAAIGIPPSGGGpEQLALAVVLKNSNVTSQDLL 671
Cdd:PRK07867 386 GDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYP-DATEVAVYAVPDPVVG-DQVMAALVLAPGAKFDPDAF 463
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 502086856 672 TlrmSFNSAlQKTLNPLFRVSQVVPVPSLPRTASNKVMRRVLRQQ 716
Cdd:PRK07867 464 A---EFLAA-QPDLGPKQWPSYVRVCAELPRTATFKVLKRQLSAE 504
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
347-713 |
2.73e-09 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 60.17 E-value: 2.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 347 IAVEEPVETfTNILFSSGTTGDPKAIPWTNISPLKAAAdAW---CHLD---VRKGDVVSWPTNLgwMMGPWLVyaSLLNG 420
Cdd:cd17650 87 LLLTQPEDL-AYVIYTSGTTGKPKGVMVEHRNVAHAAH-AWrreYELDsfpVRLLQMASFSFDV--FAGDFAR--SLLNG 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 421 ASM------ALYNGSPLgsgfAKFVQDSKVTMLGVIPSLVRSWRNANSTSGFDWSAIRCFASTGEASNIDEYLWLMGR-- 492
Cdd:cd17650 161 GTLvicpdeVKLDPAAL----YDLILKSRITLMESTPALIRPVMAYVYRNGLDLSAMRLLIVGSDGCKAQDFKTLAARfg 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 493 AHYKPIIEYcGGTE--IGGGFVTGSLLQAQSLA--AFSTPAMCCSLFILDDQGHPIPQNVpgMGELALGPlmLGASNTLL 568
Cdd:cd17650 237 QGMRIINSY-GVTEatIDSTYYEEGRDPLGDSAnvPIGRPLPNTAMYVLDERLQPQPVGV--AGELYIGG--AGVARGYL 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 569 N-ADHYGVYFKGMPIWNGKVLRRHGDVFERTARGYYHAHGRADDTMNLGGIKVSSVEIERICngADSNILETAAIGIPPS 647
Cdd:cd17650 312 NrPELTAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQL--ARHPAIDEAVVAVRED 389
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502086856 648 GGGPEQLALAVVLKNsnvtSQDLLTLRmsfnSALQKTLnPLFRV-SQVVPVPSLPRTASNKVMRRVL 713
Cdd:cd17650 390 KGGEARLCAYVVAAA----TLNTAELR----AFLAKEL-PSYMIpSYYVQLDALPLTPNGKVDRRAL 447
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
206-713 |
5.29e-09 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.
Pssm-ID: 341280 [Multi-domain] Cd Length: 447 Bit Score: 59.25 E-value: 5.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 206 QRMTLEELRQEVWLVAYALESLGLEKGSAIAIDMPMHCKSVVIYLAIVLAGYVVVSIADSFaPREissRLkisnakvift 285
Cdd:cd12115 23 ESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAY-PPE---RL---------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 286 qDLILRgdktlplysrivDAESPMAIVIPTrgsefsmklrdgDLAWcnfmdgvnkikgkefiaveepvetftnILFSSGT 365
Cdd:cd12115 89 -RFILE------------DAQARLVLTDPD------------DLAY---------------------------VIYTSGS 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 366 TGDPK--AIPWTNISPLKAAADAWCHLDVRKGDVVSwpTNLGWMMGPWLVYASLLNGASMALYNG--SPLGSGFAKfvqd 441
Cdd:cd12115 117 TGRPKgvAIEHRNAAAFLQWAAAAFSAEELAGVLAS--TSICFDLSVFELFGPLATGGKVVLADNvlALPDLPAAA---- 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 442 sKVTMLGVIPSLVRSWRNANSTSgfdwSAIRCFASTGEASNIDEYLWLMGRAHYKPIIEYCGGTEiGGGFVTGSLLQAQS 521
Cdd:cd12115 191 -EVTLINTVPSAAAELLRHDALP----ASVRVVNLAGEPLPRDLVQRLYARLQVERVVNLYGPSE-DTTYSTVAPVPPGA 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 522 LAAFS--TPAMCCSLFILDDQGHPIPQNVPGmgELALG-----------PLMLGASntllnadhygvyFKGMPIWNGKVL 588
Cdd:cd12115 265 SGEVSigRPLANTQAYVLDRALQPVPLGVPG--ELYIGgagvargylgrPGLTAER------------FLPDPFGPGARL 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 589 RRHGDVFERTARGYYHAHGRADDTMNLGGIKVSSVEIERICNGADSniLETAAIGIPPSGGGPEQLALAVVLKNSN-VTS 667
Cdd:cd12115 331 YRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPG--VREAVVVAIGDAAGERRLVAYIVAEPGAaGLV 408
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 502086856 668 QDLLtlrmsfnSALQKTLnPLFRV-SQVVPVPSLPRTASNKVMRRVL 713
Cdd:cd12115 409 EDLR-------RHLGTRL-PAYMVpSRFVRLDALPLTPNGKIDRSAL 447
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
206-713 |
7.00e-09 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 58.84 E-value: 7.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 206 QRMTLEELRQEVWLVAYALESLGLEKGSAIAIDMPMHCKSVVIYLAIVLAGYVVVSIADSFaPRE-ISSRLKISNAKVIF 284
Cdd:cd12116 11 RSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDY-PADrLRYILEDAEPALVL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 285 TQDlilRGDKTLPLYSRIVDAESPMAIVIPTRGSEfsmKLRDGDLAWcnfmdgvnkikgkefiaveepvetftnILFSSG 364
Cdd:cd12116 90 TDD---ALPDRLPAGLPVLLLALAAAAAAPAAPRT---PVSPDDLAY---------------------------VIYTSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 365 TTGDPK--AIPWTNISP-LKAAADAwchLDVRKGDVVSWPTNLGW------MMGPwlvyasLLNGASMALYNGSPL--GS 433
Cdd:cd12116 137 STGRPKgvVVSHRNLVNfLHSMRER---LGLGPGDRLLAVTTYAFdislleLLLP------LLAGARVVIAPRETQrdPE 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 434 GFAKFVQDSKVTMLGVIPSLvrsWRNANSTsgfDWSAIRCFAST--GEA--SNIDEYLWLMGRAhykpIIEYCGGTEI-- 507
Cdd:cd12116 208 ALARLIEAHSITVMQATPAT---WRMLLDA---GWQGRAGLTALcgGEAlpPDLAARLLSRVGS----LWNLYGPTETti 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 508 --GGGFVTGSLLQAQslaaFSTPAMCCSLFILDDQGHPIPQNVPGmgELAL-GPlmlGASNTLLN----------ADHYG 574
Cdd:cd12116 278 wsTAARVTAAAGPIP----IGRPLANTQVYVLDAALRPVPPGVPG--ELYIgGD---GVAQGYLGrpaltaerfvPDPFA 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 575 VyfkgmpiwNGKVLRRHGDVFERTARGYYHAHGRADDTMNLGGIKVSSVEIERICnGADSNILETAAIGIPPsgGGPEQL 654
Cdd:cd12116 349 G--------PGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAAL-AAHPGVAQAAVVVRED--GGDRRL 417
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 655 ALAVVLKNSnvTSQDLLTLRmsfnSALQKTLnPLFRV-SQVVPVPSLPRTASNKVMRRVL 713
Cdd:cd12116 418 VAYVVLKAG--AAPDAAALR----AHLRATL-PAYMVpSAFVRLDALPLTANGKLDRKAL 470
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
206-713 |
1.43e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 58.63 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 206 QRMTLEELRQEVWLVAYALESLGLEKGSAIAIDMPMHCKSVVIYLAIVLAG--YVVVsiaDSFAPRE-ISSRLKISNAKV 282
Cdd:PRK12467 3119 QQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGgaYVPL---DPEYPRErLAYMIEDSGVKL 3195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 283 IFTQDLIL------RGDKTLPLysrivdaespmaiviptrgsefsmklrdGDLAWCNFMDG--VNKIKGkefiaveepvE 354
Cdd:PRK12467 3196 LLTQAHLLeqlpapAGDTALTL----------------------------DRLDLNGYSENnpSTRVMG----------E 3237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 355 TFTNILFSSGTTGDPK--AIPWTNISPLKAAADAWCHLDVRkgDVVSWPTNLGWMMGPWLVYASLLNGASMALYNGSPLG 432
Cdd:PRK12467 3238 NLAYVIYTSGSTGKPKgvGVRHGALANHLCWIAEAYELDAN--DRVLLFMSFSFDGAQERFLWTLICGGCLVVRDNDLWD 3315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 433 SgfAKFVQD---SKVTMLGVIPSLVRSWrnANSTSGFDWSAIRCFASTGEASNIDEYLWLmgRAHYKP--IIEYCGGTEI 507
Cdd:PRK12467 3316 P--EELWQAihaHRISIACFPPAYLQQF--AEDAGGADCASLDIYVFGGEAVPPAAFEQV--KRKLKPrgLTNGYGPTEA 3389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 508 GggfVTGSLLQAQSLAAFSTPAMCC-------SLFILDDQGHPIPQNVpgMGELALGPLMLGAS---NTLLNADHygvyF 577
Cdd:PRK12467 3390 V---VTVTLWKCGGDAVCEAPYAPIgrpvagrSIYVLDGQLNPVPVGV--AGELYIGGVGLARGyhqRPSLTAER----F 3460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 578 KGMPIW-NGKVLRRHGDVFERTARGYYHAHGRADDTMNLGGIKVSSVEIERiCNGADSNILETAAIGIPPSGGgpEQLAL 656
Cdd:PRK12467 3461 VADPFSgSGGRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEA-RLLQHPSVREAVVLARDGAGG--KQLVA 3537
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 502086856 657 AVVLknsNVTSQDLL-TLRMSFNSALQKTLNPlfrvSQVVPVPSLPRTASNKVMRRVL 713
Cdd:PRK12467 3538 YVVP---ADPQGDWReTLRDHLAASLPDYMVP----AQLLVLAAMPLGPNGKVDRKAL 3588
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
208-284 |
1.51e-08 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 57.72 E-value: 1.51e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502086856 208 MTLEELRQEVWLVAYALESLGLEKGSAIAIDMPMHCKSVVIYLAIVLAGYVVVSIADSFAPREISSRLKISNAKVIF 284
Cdd:PRK07059 49 ITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPLYTPRELEHQLKDSGAEAIV 125
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
200-719 |
1.60e-08 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 57.68 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 200 QDDLPLQRMTLEELRQEVWLVAYALESLGLEKGSAIAIDMPMHCKSVVIYLAIVLAGYVVVSIADSFAPREISSRL-KIS 278
Cdd:cd05906 32 DADGSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTVPPTYDEPNARLrKLR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 279 NAKVIFTQDLILRGDKTLPLYSRIvDAESPMAiviPTRGSEFSMKLR-DGDLAWcnfmdgvnKIKGKEFIAVeepvetft 357
Cdd:cd05906 112 HIWQLLGSPVVLTDAELVAEFAGL-ETLSGLP---GIRVLSIEELLDtAADHDL--------PQSRPDDLAL-------- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 358 nILFSSGTTGDPKAIPWTNISPLKAAADAWCHLDVRKGDVVswptnLGWMmgPWLVYASLLNGASMALYNGS-------- 429
Cdd:cd05906 172 -LMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVF-----LNWV--PLDHVGGLVELHLRAVYLGCqqvhvpte 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 430 -----PLGsgFAKFVQDSKVT-------MLGVIPSLVRSwrnaNSTSGFDWSAIRCFASTGEA---SNIDEYLWLMGRAH 494
Cdd:cd05906 244 eiladPLR--WLDLIDRYRVTitwapnfAFALLNDLLEE----IEDGTWDLSSLRYLVNAGEAvvaKTIRRLLRLLEPYG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 495 YKP--IIEYCGGTEIGGG------FVTGSLLQAQSLAAFSTPAMCCSLFILDDQGHPIPQNVPGMGELAlGPLMLGAsnt 566
Cdd:cd05906 318 LPPdaIRPAFGMTETCSGviysrsFPTYDHSQALEFVSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVR-GPVVTKG--- 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 567 llnadhygvYFKGmPIWNGKVLR-----RHGDVfertarGYYHA-----HGRADDTMNLGGIKVSSVEIERICNGADsnI 636
Cdd:cd05906 394 ---------YYNN-PEANAEAFTedgwfRTGDL------GFLDNgnltiTGRTKDTIIVNGVNYYSHEIEAAVEEVP--G 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 637 LE---TAAIGIPPSGGGPEQLALAVvlknsnVTSQDLLTLRMSFNSALQKTLNPLFRVS--QVVPVP--SLPRTASNKVM 709
Cdd:cd05906 456 VEpsfTAAFAVRDPGAETEELAIFF------VPEYDLQDALSETLRAIRSVVSREVGVSpaYLIPLPkeEIPKTSLGKIQ 529
|
570
....*....|
gi 502086856 710 RRVLRQQLVE 719
Cdd:cd05906 530 RSKLKAAFEA 539
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
359-713 |
2.16e-08 |
|
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341299 [Multi-domain] Cd Length: 465 Bit Score: 57.06 E-value: 2.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 359 ILFSSGTTGDPKAIPWTNISPLKAAADAWCHLDVRKGDVVSWPTNLGWMMGPWLVYASLLNGASMALYNGSPLGSG--FA 436
Cdd:cd17644 111 VIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLedFV 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 437 KFVQDSKVTMLGVIPSLVRSWRNANSTSGFDW-SAIRCFASTGEAsnIDEYLWLMGRAHYKPIIEYC---GGTEiggGFV 512
Cdd:cd17644 191 QYIQQWQLTVLSLPPAYWHLLVLELLLSTIDLpSSLRLVIVGGEA--VQPELVRQWQKNVGNFIQLInvyGPTE---ATI 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 513 TGSLLQAQSLA-------AFSTPAMCCSLFILDDQGHPIPQNVPgmGELALGPLML--GASN--TLLNADHYGVYFKGMP 581
Cdd:cd17644 266 AATVCRLTQLTernitsvPIGRPIANTQVYILDENLQPVPVGVP--GELHIGGVGLarGYLNrpELTAEKFISHPFNSSE 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 582 iwnGKVLRRHGDVFERTARGYYHAHGRADDTMNLGGIKVSSVEIERICNgaDSNILETAAIGIPPSGGGPEQLALAVVLK 661
Cdd:cd17644 344 ---SERLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLS--QHNDVKTAVVIVREDQPGNKRLVAYIVPH 418
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 502086856 662 NSNvtSQDLLTLRMSFNSALqktlnPLFRV-SQVVPVPSLPRTASNKVMRRVL 713
Cdd:cd17644 419 YEE--SPSTVELRQFLKAKL-----PDYMIpSAFVVLEELPLTPNGKIDRRAL 464
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
206-430 |
2.43e-08 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 57.42 E-value: 2.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 206 QRMTLEELRQEVWLVAYALESLGLEKGSAIAI---DMPMHcksVVIYLAIVLAGYVVVSIADSFAPREISSRLKISNAKV 282
Cdd:COG1022 39 QSLTWAEFAERVRALAAGLLALGVKPGDRVAIlsdNRPEW---VIADLAILAAGAVTVPIYPTSSAEEVAYILNDSGAKV 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 283 IFTQDLILRgDKTLPLYSRIVDAESpmAIVIPTRGsefsMKLRDGDLAWCNFMD-GVNKIKGKEFIAVEEPVE---TFTn 358
Cdd:COG1022 116 LFVEDQEQL-DKLLEVRDELPSLRH--IVVLDPRG----LRDDPRLLSLDELLAlGREVADPAELEARRAAVKpddLAT- 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502086856 359 ILFSSGTTGDPKAIPWT--NIspLKAAADAWCHLDVRKGDVV-SW-PtnLGWMMGPWLVYASLLNGASMAlYNGSP 430
Cdd:COG1022 188 IIYTSGTTGRPKGVMLThrNL--LSNARALLERLPLGPGDRTlSFlP--LAHVFERTVSYYALAAGATVA-FAESP 258
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
206-396 |
4.59e-08 |
|
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: 56.32 E-value: 4.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 206 QRMTLEELRQEVWLVAYALESLGLEKGSAIAIdMPMHCKSVVIY-LAIVLAGYVVVSIADSFAPREISSRLKISNAKVIF 284
Cdd:cd05932 5 VEFTWGEVADKARRLAAALRALGLEPGSKIAL-ISKNCAEWFITdLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 285 TQDLilrgdktlplysrivDAESPMAIVIPTRGSEFSMKLRDGdlawCNFMDGVNKIKGKEFIAVEEPV---ETFTNILF 361
Cdd:cd05932 84 VGKL---------------DDWKAMAPGVPEGLISISLPPPSA----ANCQYQWDDLIAQHPPLEERPTrfpEQLATLIY 144
|
170 180 190
....*....|....*....|....*....|....*
gi 502086856 362 SSGTTGDPKAIPWTNISPLKAAADAWCHLDVRKGD 396
Cdd:cd05932 145 TSGTTGQPKGVMLTFGSFAWAAQAGIEHIGTEEND 179
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
207-719 |
7.97e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 55.32 E-value: 7.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 207 RMTLEELRQEVWLVAYALESLGLEKGSAIAIdMPMHCKS-VVIYLAIVLAGYVVVSIADSFAPREISSRLKISNAKVIFT 285
Cdd:PRK08316 36 SWTYAELDAAVNRVAAALLDLGLKKGDRVAA-LGHNSDAyALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAFLV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 286 Q-DLILRGDKTLPLYSRivdAESPMAIVIPTRGSEfsmklrDGDLAWCNFMDGVNKIKGKEFIAVEEPVetftNILFSSG 364
Cdd:PRK08316 115 DpALAPTAEAALALLPV---DTLILSLVLGGREAP------GGWLDFADWAEAGSVAEPDVELADDDLA----QILYTSG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 365 TTGDPK-------AIPWTNISPLKAaadawchLDVRKGD--VVSWP----TNLGWMMGPWLvyaslLNGASMALYNGSPL 431
Cdd:PRK08316 182 TESLPKgamlthrALIAEYVSCIVA-------GDMSADDipLHALPlyhcAQLDVFLGPYL-----YVGATNVILDAPDP 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 432 GSGFAKfVQDSKVTMLGVIP----SLVRSwrnanstSGF---DWSAIRcfastgeasnideylwlmgRAHY------KPI 498
Cdd:PRK08316 250 ELILRT-IEAERITSFFAPPtvwiSLLRH-------PDFdtrDLSSLR-------------------KGYYgasimpVEV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 499 IE-------------YCGGTEIGG-GFVTGSLLQAQSLAAFSTPAMCCSLFILDDQGHPIPqnvPG-MGELA-LGP-LML 561
Cdd:PRK08316 303 LKelrerlpglrfynCYGQTEIAPlATVLGPEEHLRRPGSAGRPVLNVETRVVDDDGNDVA---PGeVGEIVhRSPqLML 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 562 GASNtllNADHYGVYFKGMpiWngkvlRRHGDVFERTARGYYHAHGRADDTMNLGGIKVSSVEIERiCNGADSNILETAA 641
Cdd:PRK08316 380 GYWD---DPEKTAEAFRGG--W-----FHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEE-ALYTHPAVAEVAV 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 642 IGIPpsggGP---EQLALAVVLKNSN-VTSQDLLTLrmsfnsaLQKTLNPlFRV-SQVVPVPSLPRTASNKVMRRVLRQQ 716
Cdd:PRK08316 449 IGLP----DPkwiEAVTAVVVPKAGAtVTEDELIAH-------CRARLAG-FKVpKRVIFVDELPRNPSGKILKRELRER 516
|
...
gi 502086856 717 LVE 719
Cdd:PRK08316 517 YAG 519
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
206-724 |
1.07e-07 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 54.87 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 206 QRMTLEELRQEVWLVAYAL-ESLGLEKGSAIAIDMPMHCKSVVIYLAIVLAGYVVVSIADSFAPREISSRLKISNAKVIF 284
Cdd:PRK06839 26 EEMTYKQLHEYVSKVAAYLiYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTTVLF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 285 TQdlilrgdKTLPLYSRIVDAESPMAIVIptrgsefsmklrdgdlawcnFMDGVNKIKGKEFIAVEEPVETFTNIL-FSS 363
Cdd:PRK06839 106 VE-------KTFQNMALSMQKVSYVQRVI--------------------SITSLKEIEDRKIDNFVEKNESASFIIcYTS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 364 GTTGDPKAIPWTNISPLKAAADAWCHLDVRKGDV---------------VSWPTnlgWMMGPWLVYASLLNgASMALyng 428
Cdd:PRK06839 159 GTTGKPKGAVLTQENMFWNALNNTFAIDLTMHDRsivllplfhiggiglFAFPT---LFAGGVIIVPRKFE-PTKAL--- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 429 splgsgfaKFVQDSKVTMLGVIPSLVRSWRNANSTSGFDWSAIRCFASTGEASNIDEYLWLMGRAHykPIIEYCGGTEIG 508
Cdd:PRK06839 232 --------SMIEKHKVTVVMGVPTIHQALINCSKFETTNLQSVRWFYNGGAPCPEELMREFIDRGF--LFGQGFGMTETS 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 509 GG-FVTGSLLQAQSLAAFSTPAMCCSLFILDDQGHPIPQNvpGMGELAL-GPLMLGA--------SNTLLNADHYGvyfk 578
Cdd:PRK06839 302 PTvFMLSEEDARRKVGSIGKPVLFCDYELIDENKNKVEVG--EVGELLIrGPNVMKEywnrpdatEETIQDGWLCT---- 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 579 gmpiwngkvlrrhGDVFERTARGYYHAHGRADDTMNLGGIKVSSVEIERICNGADSnILETAAIGIPPSGGGPEQLALAV 658
Cdd:PRK06839 376 -------------GDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSD-VYEVAVVGRQHVKWGEIPIAFIV 441
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502086856 659 VLKNSNVTSQDLLTLRMSFnsaLQKTLNPlfrvSQVVPVPSLPRTASNKVMrrvlRQQLVENTQSS 724
Cdd:PRK06839 442 KKSSSVLIEKDVIEHCRLF---LAKYKIP----KEIVFLKELPKNATGKIQ----KAQLVNQLKSR 496
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
206-713 |
1.36e-07 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 55.44 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 206 QRMTLEELRQEVWLVAYALESLGLEKGSAIAIDMPMHCKSVVIYLAIVLAGYVVVSIaDSFAPREissRLK--ISNAK-- 281
Cdd:PRK10252 482 YQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPL-DTGYPDD---RLKmmLEDARps 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 282 -VIFTQDLILR----GDKTLPLYsrivDAESPMAIVIPTRGSefsmklRDGDLAWcnfmdgvnkikgkefiaveepvetf 356
Cdd:PRK10252 558 lLITTADQLPRfadvPDLTSLCY----NAPLAPQGAAPLQLS------QPHHTAY------------------------- 602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 357 tnILFSSGTTGDPK-------AIpwtnISPLKaaadaWC--HLDVRKGDVVSWPTNLGWMMGPWLVYASLLNGAS--MAL 425
Cdd:PRK10252 603 --IIFTSGSTGRPKgvmvgqtAI----VNRLL-----WMqnHYPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKlvMAE 671
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 426 YNGSPLGSGFAKFVQDSKVTMLGVIPSLVRSWRNANSTSGfdwsAIRCFAS------TGEASNIDEYLWLMGRAHyKPII 499
Cdd:PRK10252 672 PEAHRDPLAMQQFFAEYGVTTTHFVPSMLAAFVASLTPEG----ARQSCASlrqvfcSGEALPADLCREWQQLTG-APLH 746
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 500 EYCGGTEIGGGfVTGSLLQAQSLAAFST-------PAMCCSLFILDDQGHPIPQNVPgmGELALGPLMLgASNTLLNADH 572
Cdd:PRK10252 747 NLYGPTEAAVD-VSWYPAFGEELAAVRGssvpigyPVWNTGLRILDARMRPVPPGVA--GDLYLTGIQL-AQGYLGRPDL 822
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 573 YGVYFKGMPIWNGKVLRRHGDVFERTARGYYHAHGRADDTMNLGGIKVSSVEIER----ICNGADSNILETAAIGIPPSG 648
Cdd:PRK10252 823 TASRFIADPFAPGERMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRamqaLPDVEQAVTHACVINQAAATG 902
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502086856 649 GGPEQLALAVVLKNSnvTSQDLLTLRmsfnSALQKTLNPLFRVSQVVPVPSLPRTASNKVMRRVL 713
Cdd:PRK10252 903 GDARQLVGYLVSQSG--LPLDTSALQ----AQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKAL 961
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
361-716 |
2.76e-07 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 53.88 E-value: 2.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 361 FSSGTTGDPKAIPWTNISPLkAAADAWCHLDVRKGdvvswPTNLG---------WMMGPwLVYASLLNGASmALYNGSPL 431
Cdd:PRK06060 152 YTSGTTGPPKAAIHRHADPL-TFVDAMCRKALRLT-----PEDTGlcsarmyfaYGLGN-SVWFPLATGGS-AVINSAPV 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 432 GSGFAKFVQDS-KVTMLGVIPSLVRSWRNANSTSGFdwSAIRCFASTGEASNIDEYLWLMGRAHYKPIIEYCGGTEIGGG 510
Cdd:PRK06060 224 TPEAAAILSARfGPSVLYGVPNFFARVIDSCSPDSF--RSLRCVVSAGEALELGLAERLMEFFGGIPILDGIGSTEVGQT 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 511 FVTGSL--LQAQSLAAFSTPAmccSLFILDDQGHPIPQNvpGMGELAL-GPLMlgasntllnADHYgvyfkgmpiWN-GK 586
Cdd:PRK06060 302 FVSNRVdeWRLGTLGRVLPPY---EIRVVAPDGTTAGPG--VEGDLWVrGPAI---------AKGY---------WNrPD 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 587 VLRRHGDVFERTAR------GYYHAHGRADDTMNLGGIKVSSVEIERICNGADSnILETAAIGIPPSGGGPEQLALAVVL 660
Cdd:PRK06060 359 SPVANEGWLDTRDRvcidsdGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEA-VAEAAVVAVRESTGASTLQAFLVAT 437
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 502086856 661 KNSNVTSQDLLTLRMSFNSALQKtlnplFRVS-QVVPVPSLPRTASNKVMRRVLRQQ 716
Cdd:PRK06060 438 SGATIDGSVMRDLHRGLLNRLSA-----FKVPhRFAVVDRLPRTPNGKLVRGALRKQ 489
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
528-716 |
4.01e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 53.45 E-value: 4.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 528 PAMCCSLFILDDQGHPIPQNVPGmgELAL-GPLMLGAsntllnadhygvYFKgMPIWNGKVLR----RHGDVFERTARGY 602
Cdd:PRK06188 344 PTPGLRVALLDEDGREVAQGEVG--EICVrGPLVMDG------------YWN-RPEETAEAFRdgwlHTGDVAREDEDGF 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 603 YHAHGRADDTMNLGGIKVSSVEIERiCNGADSNILETAAIGIPPSGGGpEQLALAVVLK-NSNVTSQDLLTLRMSFNSAL 681
Cdd:PRK06188 409 YYIVDRKKDMIVTGGFNVFPREVED-VLAEHPAVAQVAVIGVPDEKWG-EAVTAVVVLRpGAAVDAAELQAHVKERKGSV 486
|
170 180 190
....*....|....*....|....*....|....*
gi 502086856 682 QKtlnPlfrvSQVVPVPSLPRTASNKVMRRVLRQQ 716
Cdd:PRK06188 487 HA---P----KQVDFVDSLPLTALGKPDKKALRAR 514
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
204-717 |
4.95e-07 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 52.83 E-value: 4.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 204 PLQRMTLEELRQEVWLVAYALESLGLEKG---SAIAIDMPMHCKSvviYLAIVLAGYVVVSIADSFAPREISSRLKISNA 280
Cdd:PRK06018 36 PIVRTTYAQIHDRALKVSQALDRDGIKLGdrvATIAWNTWRHLEA---WYGIMGIGAICHTVNPRLFPEQIAWIINHAED 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 281 KVIFTqdlilrgDKT-LPLYSRIVDA-ESPMAIVIPTRGS-------------EFSMKLRDGDLAWCNFMDGvnkikgke 345
Cdd:PRK06018 113 RVVIT-------DLTfVPILEKIADKlPSVERYVVLTDAAhmpqttlknavayEEWIAEADGDFAWKTFDEN-------- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 346 fiaveepveTFTNILFSSGTTGDPKAIPWTNISPLKAA-----ADAwchLDVRKGDVV----------SWPTNL-GWMMG 409
Cdd:PRK06018 178 ---------TAAGMCYTSGTTGDPKGVLYSHRSNVLHAlmannGDA---LGTSAADTMlpvvplfhanSWGIAFsAPSMG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 410 PWLVyaslLNGASMAlyngsplGSGFAKFVQDSKVTMLGVIPSLVRSWRNANSTSGFDWSAIRCFASTGEAsnideylwl 489
Cdd:PRK06018 246 TKLV----MPGAKLD-------GASVYELLDTEKVTFTAGVPTVWLMLLQYMEKEGLKLPHLKMVVCGGSA--------- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 490 MGRAHYKPIIEY-------CGGTEIGGGFVTGSL---------------LQAQSLAAFSTpAMCcslfILDDQGHPIPQN 547
Cdd:PRK06018 306 MPRSMIKAFEDMgvevrhaWGMTEMSPLGTLAALkppfsklpgdarldvLQKQGYPPFGV-EMK----ITDDAGKELPWD 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 548 VPGMGELAL-GPLMLGAsntllnadhygvYFKGmpiwNGKVLRRH-----GDVFERTARGYYHAHGRADDTMNLGGIKVS 621
Cdd:PRK06018 381 GKTFGRLKVrGPAVAAA------------YYRV----DGEILDDDgffdtGDVATIDAYGYMRITDRSKDVIKSGGEWIS 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 622 SVEIERICNGaDSNILETAAIGIPPSGGGPEQLALAVVLKNSNVTSQDLLTlrmSFNSALQKTLNPlfrvSQVVPVPSLP 701
Cdd:PRK06018 445 SIDLENLAVG-HPKVAEAAVIGVYHPKWDERPLLIVQLKPGETATREEILK---YMDGKIAKWWMP----DDVAFVDAIP 516
|
570
....*....|....*.
gi 502086856 702 RTASNKVMRRVLRQQL 717
Cdd:PRK06018 517 HTATGKILKTALREQF 532
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
184-716 |
1.07e-06 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 52.07 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 184 GERSLnDTVILWRNELQDDLPL-----QRMTLEELRQEVWLVAYALESLGLEKGSAIAIDmpmhCKSVVIYLAIVLA--- 255
Cdd:PRK06155 19 SERTL-PAMLARQAERYPDRPLlvfggTRWTYAEAARAAAAAAHALAAAGVKRGDRVALM----CGNRIEFLDVFLGcaw 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 256 -GYVVVSIADSFAPREISSRLKISNAKVIFTQ-------DLILRGDKTLPlYSRIVDAESpmAIVIPTRGSEFSMKLRDG 327
Cdd:PRK06155 94 lGAIAVPINTALRGPQLEHILRNSGARLLVVEaallaalEAADPGDLPLP-AVWLLDAPA--SVSVPAGWSTAPLPPLDA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 328 DLAwcnfmdgvnkikgkefIAVEEPVETFTnILFSSGTTGDPKAI--P-----WTNISplkAAADawchLDVRKGDVVSw 400
Cdd:PRK06155 171 PAP----------------AAAVQPGDTAA-ILYTSGTTGPSKGVccPhaqfyWWGRN---SAED----LEIGADDVLY- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 401 pTNLgwmmgPwLVYASLLNGASMALYNGSPL-------GSGFAKFVQDSKVT---MLGVIPSLVRSWRNANSTSGfdwSA 470
Cdd:PRK06155 226 -TTL-----P-LFHTNALNAFFQALLAGATYvleprfsASGFWPAVRRHGATvtyLLGAMVSILLSQPARESDRA---HR 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 471 IRCFASTGEASNI-DEYLWLMGrahyKPIIEYCGGTEIGggFVTGSLLQAQSLAAFSTPAMCCSLFILDDQGHPIPQNVP 549
Cdd:PRK06155 296 VRVALGPGVPAALhAAFRERFG----VDLLDGYGSTETN--FVIAVTHGSQRPGSMGRLAPGFEARVVDEHDQELPDGEP 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 550 GmgELalgplmlgasntLLNADHYGV----YFkGMP-----IWNGkvLRRH-GDVFERTARGYYHAHGRADDTMNLGGIK 619
Cdd:PRK06155 370 G--EL------------LLRADEPFAfatgYF-GMPektveAWRN--LWFHtGDRVVRDADGWFRFVDRIKDAIRRRGEN 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 620 VSSVEIERICNgADSNILETAAIGIPPSGGGPEQLALAVVLKNSNVTSQDLLTL---RMsfnsalqktlnPLFRVSQVVP 696
Cdd:PRK06155 433 ISSFEVEQVLL-SHPAVAAAAVFPVPSELGEDEVMAAVVLRDGTALEPVALVRHcepRL-----------AYFAVPRYVE 500
|
570 580
....*....|....*....|.
gi 502086856 697 -VPSLPRTASNKVMRRVLRQQ 716
Cdd:PRK06155 501 fVAALPKTENGKVQKFVLREQ 521
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
536-723 |
1.11e-06 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 51.91 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 536 ILDDQGHPIPQNVPGMgelalgpLMLGASNTLLNadhygvYFKGmPIWNGKVLRRH-----GDVFERTARGYYHAHGRAD 610
Cdd:PRK10946 367 VADADGNPLPQGEVGR-------LMTRGPYTFRG------YYKS-PQHNASAFDANgfycsGDLVSIDPDGYITVVGREK 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 611 DTMNLGGIKVSSVEIERICNGADSnILETAAIGIPPSGGGPEQLALAVV---LKnsnvtsqdlltlrmsfNSALQKTLNP 687
Cdd:PRK10946 433 DQINRGGEKIAAEEIENLLLRHPA-VIHAALVSMEDELMGEKSCAFLVVkepLK----------------AVQLRRFLRE 495
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 502086856 688 L----FRV-SQVVPVPSLPRTASNKVMRRVLRQQLVENTQS 723
Cdd:PRK10946 496 QgiaeFKLpDRVECVDSLPLTAVGKVDKKQLRQWLASRASA 536
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
206-720 |
1.17e-06 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 51.89 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 206 QRMTLEELRQEVWLVAYALESLGLEKGSAIAIDMPMHCKSVVIYLAIVLAGYVVVSIADSFAPREISSRLKISNAKVIFT 285
Cdd:PRK03640 26 KKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKCLIT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 286 QDlilrgdktlplysrivDAESPMAIVIPTRGSEFSmklrdgdlawcnfmdgvnkikgKEFIAVEEPVETF-----TNIL 360
Cdd:PRK03640 106 DD----------------DFEAKLIPGISVKFAELM----------------------NGPKEEAEIQEEFdldevATIM 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 361 FSSGTTGDPKAIPWTNISPLKAAADAWCHLDVRKGDvvSW----P----TNLGWMMgpwlvyASLLNGASMALYngsplg 432
Cdd:PRK03640 148 YTSGTTGKPKGVIQTYGNHWWSAVGSALNLGLTEDD--CWlaavPifhiSGLSILM------RSVIYGMRVVLV------ 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 433 SGF-AKFV----QDSKVTMLGVIPS----LVRSWRNANSTSGFdwsaiRCFASTGeaSNIDEYLWLMGRAHYKPIIEYCG 503
Cdd:PRK03640 214 EKFdAEKInkllQTGGVTIISVVSTmlqrLLERLGEGTYPSSF-----RCMLLGG--GPAPKPLLEQCKEKGIPVYQSYG 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 504 GTEIGGGFVT----GSLLQAQSLAafsTPAMCCSLFILDDqGHPIPQNVPGmgELAL-GP-LMLGASN---TLLNADHYG 574
Cdd:PRK03640 287 MTETASQIVTlspeDALTKLGSAG---KPLFPCELKIEKD-GVVVPPFEEG--EIVVkGPnVTKGYLNredATRETFQDG 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 575 vYFKGmpiwngkvlrrhGDVFERTARGYYHAHGRADDTMNLGGIKVSSVEIERICnGADSNILETAAIGIPPSGGGpeQL 654
Cdd:PRK03640 361 -WFKT------------GDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVL-LSHPGVAEAGVVGVPDDKWG--QV 424
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502086856 655 ALAVVLKNSNVTSQDLLTLrmsfnsaLQKTLNPLFRVSQVVPVPSLPRTASNKVMRRVLRQQLVEN 720
Cdd:PRK03640 425 PVAFVVKSGEVTEEELRHF-------CEEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQLVEEM 483
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
351-714 |
2.51e-06 |
|
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.
Pssm-ID: 341252 [Multi-domain] Cd Length: 473 Bit Score: 50.45 E-value: 2.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 351 EPVETFTNILFSSGTTGDPKAIpwtnisplKAaadawcHLDVRKGD---VVSWPTNLGWMMGP-WLVYASLLNGA----- 421
Cdd:cd05929 122 EDEAAGWKMLYSGGTTGRPKGI--------KR------GLPGGPPDndtLMAAALGFGPGADSvYLSPAPLYHAApfrws 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 422 SMALYNGSPL-------GSGFAKFVQDSKVTMLGVIPSL-VRSW------RNAnstsgFDWSAIRCFASTG-------EA 480
Cdd:cd05929 188 MTALFMGGTLvlmekfdPEEFLRLIERYRVTFAQFVPTMfVRLLklpeavRNA-----YDLSSLKRVIHAAapcppwvKE 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 481 SNIDeylWLMGRahykpIIEYCGGTE-IGGGFVTGS--LLQAQSLAAFSTPAMCcslfILDDQGHPIPQNVPGmgelalg 557
Cdd:cd05929 263 QWID---WGGPI-----IWEYYGGTEgQGLTIINGEewLTHPGSVGRAVLGKVH----ILDEDGNEVPPGEIG------- 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 558 plmlgasnTLLNADHYGVYFKGMPIWNGKVLRRH-----GDVFERTARGYYHAHGRADDTMNLGGIKVSSVEIERICNgA 632
Cdd:cd05929 324 --------EVYFANGPGFEYTNDPEKTAAARNEGgwstlGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALI-A 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 633 DSNILETAAIGIPPSGGGpeQLALAVVLKNSNVTSQDLLTLRM-SFnsaLQKTLNPlFRVSQVVP-VPSLPRTASNKVMR 710
Cdd:cd05929 395 HPKVLDAAVVGVPDEELG--QRVHAVVQPAPGADAGTALAEELiAF---LRDRLSR-YKCPRSIEfVAELPRDDTGKLYR 468
|
....
gi 502086856 711 RVLR 714
Cdd:cd05929 469 RLLR 472
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
592-717 |
2.75e-06 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 50.02 E-value: 2.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 592 GDVFERTARGYYHAHGRADDTMNLGGIKVSSVEIERiCNGADSNILETAAIGIPPSGGGpeQLALAVVLKNSNVTSQDLl 671
Cdd:cd17630 210 KDLGELHADGRLTVLGRADNMIISGGENIQPEEIEA-ALAAHPAVRDAFVVGVPDEELG--QRPVAVIVGRGPADPAEL- 285
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 502086856 672 tlrmsfNSALQKTLNPLFRVSQVVPVPSLPRTASNKVMRRVLRQQL 717
Cdd:cd17630 286 ------RAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRAWL 325
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
195-716 |
2.77e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 50.55 E-value: 2.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 195 WRNEL------QDDLPLQR-----MTLEELRQEVWLVAYALESLGLEKGSAIAIDMPMHCKSVVIYLAIVLAGYVVVSIA 263
Cdd:PRK07786 19 WVNQLarhalmQPDAPALRflgntTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 264 DSFAPREISSRLKISNAKVIFTQDLILrgdktlPLYSRIVDAESPMAIVIPTRGSEfsmklRDGDLAWcnfmDGVNKIKG 343
Cdd:PRK07786 99 FRLTPPEIAFLVSDCGAHVVVTEAALA------PVATAVRDIVPLLSTVVVAGGSS-----DDSVLGY----EDLLAEAG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 344 KEFIAVEEPVETFTNILFSSGTTGDPKAipwTNISPLKAAADAWCHLDVRKGDVvswPTNLGWMMGPWLVYASLLNGASM 423
Cdd:PRK07786 164 PAHAPVDIPNDSPALIMYTSGTTGRPKG---AVLTHANLTGQAMTCLRTNGADI---NSDVGFVGVPLFHIAGIGSMLPG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 424 ALYNGS----PLGS----GFAKFVQDSKVTMLGVIPSLVRSWRNANSTSGFDWsAIRcFASTGEASNIDEYLWLMGRAHY 495
Cdd:PRK07786 238 LLLGAPtviyPLGAfdpgQLLDVLEAEKVTGIFLVPAQWQAVCAEQQARPRDL-ALR-VLSWGAAPASDTLLRQMAATFP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 496 KP-IIEYCGGTEIGGgfVTGSLL---QAQSLAAFSTPAMCCSLFILDDQGHPIPqnvPG-MGELAL-GP-LMLGA-SNTL 567
Cdd:PRK07786 316 EAqILAAFGQTEMSP--VTCMLLgedAIRKLGSVGKVIPTVAARVVDENMNDVP---VGeVGEIVYrAPtLMSGYwNNPE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 568 LNADHY-GVYFKGmpiwngkvlrrhGDVFERTARGYYHAHGRADDTMNLGGIKVSSVEIERICnGADSNILETAAIGIPP 646
Cdd:PRK07786 391 ATAEAFaGGWFHS------------GDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVL-ASHPDIVEVAVIGRAD 457
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 647 SGGGpeQLALAVVLKNSNVTSQDLLTLRMSFNSALQKTLNPLFrvsqVVPVPSLPRTASNKVMRRVLRQQ 716
Cdd:PRK07786 458 EKWG--EVPVAVAAVRNDDAALTLEDLAEFLTDRLARYKHPKA----LEIVDALPRNPAGKVLKTELRER 521
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
221-714 |
3.75e-06 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 50.26 E-value: 3.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 221 AYALESLGLEKGSAIAIDMPMHCKSVVIYLAIVLAGYVVVSIADSFAPREISSRLKISNAKVIFTQDLIlrGDKTlplys 300
Cdd:PRK08751 65 AYLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLVVIDNF--GTTV----- 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 301 RIVDAESPMAIVIPTrgsEFSMKLRDGDLAWCNF-MDGVNK----------IKGKEFIA---------VEEPVETFTNIL 360
Cdd:PRK08751 138 QQVIADTPVKQVITT---GLGDMLGFPKAALVNFvVKYVKKlvpeyringaIRFREALAlgrkhsmptLQIEPDDIAFLQ 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 361 FSSGTTGDPKAIPWT--NISPLKAAADAWC----HLDVRKGDVVSwptnlgwMMGPWLVYASLLNGASMALYNG------ 428
Cdd:PRK08751 215 YTGGTTGVAKGAMLThrNLVANMQQAHQWLagtgKLEEGCEVVIT-------ALPLYHIFALTANGLVFMKIGGcnhlis 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 429 SPLG-SGFAKFVQDSKVTMLGVIPSLVRSWRNANSTSGFDWSAIRCFASTGEA--SNIDEYlWlmGRAHYKPIIEYCGGT 505
Cdd:PRK08751 288 NPRDmPGFVKELKKTRFTAFTGVNTLFNGLLNTPGFDQIDFSSLKMTLGGGMAvqRSVAER-W--KQVTGLTLVEAYGLT 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 506 EIGGGFVTGSLLQAQSLAAFSTPAMCCSLFILDDQGHPIPqnVPGMGELAL-GP-LMLG------ASNTLLNADHYgvyf 577
Cdd:PRK08751 365 ETSPAACINPLTLKEYNGSIGLPIPSTDACIKDDAGTVLA--IGEIGELCIkGPqVMKGywkrpeETAKVMDADGW---- 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 578 kgmpiwngkvlRRHGDVFERTARGYYHAHGRADDTMNLGGIKVSSVEIERICnGADSNILETAAIGIPPSGGGpEQLALA 657
Cdd:PRK08751 439 -----------LHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVI-AMMPGVLEVAAVGVPDEKSG-EIVKVV 505
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 502086856 658 VVLKNSNVTSQDLltlrmsfnSALQKTLNPLFRVSQVVPV-PSLPRTASNKVMRRVLR 714
Cdd:PRK08751 506 IVKKDPALTAEDV--------KAHARANLTGYKQPRIIEFrKELPKTNVGKILRRELR 555
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
206-400 |
5.80e-06 |
|
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: 49.66 E-value: 5.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 206 QRMTLEELRQEVWLVAYALESLGLEKGSAIAIdMPMHCKSVVIY-LAIVLAGYVVVSIADSFAPREISSRLKISNAKVIF 284
Cdd:cd05933 7 HTLTYKEYYEACRQAAKAFLKLGLERFHGVGI-LGFNSPEWFIAaVGAIFAGGIAVGIYTTNSPEACQYVAETSEANILV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 285 TQDlilrgDKTLPLYSRIVDAESPMAIVIPTRGsEFSMKlRDGDLAWCNFMDGVNKIKGKEFIAVEE---PVETFTNIlF 361
Cdd:cd05933 86 VEN-----QKQLQKILQIQDKLPHLKAIIQYKE-PLKEK-EPNLYSWDEFMELGRSIPDEQLDAIISsqkPNQCCTLI-Y 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 502086856 362 SSGTTGDPKA-------IPWTNISPLKAAADAwcHLDVRKGDVVSW 400
Cdd:cd05933 158 TSGTTGMPKGvmlshdnITWTAKAASQHMDLR--PATVGQESVVSY 201
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
207-716 |
5.81e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 49.57 E-value: 5.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 207 RMTLEELRQEV-WLVAYALESLGLEKGSAIAIDMPMHCKSVVIYLAIVLAGYVVVSIADSFAPREISSRLKISNAKVIFT 285
Cdd:PRK08314 35 AISYRELLEEAeRLAGYLQQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGARVAIV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 286 -QDL---ILRGDKTLPL-------YSRIVDAESPmaIVIP---TRGSEFSMKLRDGDLAWCNFMDgvnkiKGKEFIAVEE 351
Cdd:PRK08314 115 gSELapkVAPAVGNLRLrhvivaqYSDYLPAEPE--IAVPawlRAEPPLQALAPGGVVAWKEALA-----AGLAPPPHTA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 352 PVETFTNILFSSGTTGDPKAIPWTNISPLKAAADAWCHLDVRKGDVVswptnLGWMmgPWLVYASLLNGASMALYNGSPL 431
Cdd:PRK08314 188 GPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVV-----LAVL--PLFHVTGMVHSMNAPIYAGATV 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 432 -------GSGFAKFVQDSKVTMLGVIPSLVRSWRNANSTSGFDWSAIRCFASTGEA--SNIDEYLW-LMGrahykpiIEY 501
Cdd:PRK08314 261 vlmprwdREAAARLIERYRVTHWTNIPTMVVDFLASPGLAERDLSSLRYIGGGGAAmpEAVAERLKeLTG-------LDY 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 502 CGG---TEigggfvTGSL----------LQAQSLAAFSTPAMccslfILD-DQGHPIPQNVpgMGELAL-GP-LMLGASN 565
Cdd:PRK08314 334 VEGyglTE------TMAQthsnppdrpkLQCLGIPTFGVDAR-----VIDpETLEELPPGE--VGEIVVhGPqVFKGYWN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 566 tllNADHYGVYFkgMPIwNGKVLRRHGDVFERTARGYYHAHGRADDTMNLGGIKVSSVEIERICNGADSnILETAAIGIP 645
Cdd:PRK08314 401 ---RPEATAEAF--IEI-DGKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPA-IQEACVIATP 473
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502086856 646 PSGGGPEQLALaVVLK---NSNVTSQDLLTL---RMSfnsalqktlnpLFRVSQVVP-VPSLPRTASNKVMRRVLRQQ 716
Cdd:PRK08314 474 DPRRGETVKAV-VVLRpeaRGKTTEEEIIAWareHMA-----------AYKYPRIVEfVDSLPKSGSGKILWRQLQEQ 539
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
206-723 |
5.85e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 49.52 E-value: 5.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 206 QRMTLEELRQEVWLVAYALESLGLEKGSAIAIDMPMHCKSVVIYLAIVLAGYVVVSIADSFAPREISSRLKISNAKVIFT 285
Cdd:PRK08276 10 EVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVLIV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 286 QDlilrgdktlplysRIVDAESPMAIVIPTRGSEFSMKL--RDGDLAWCNFMDGVNkikgkefiAVEEPVETF-TNILFS 362
Cdd:PRK08276 90 SA-------------ALADTAAELAAELPAGVPLLLVVAgpVPGFRSYEEALAAQP--------DTPIADETAgADMLYS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 363 SGTTGDPKAI--PWTNISPLKAAadawchldvrkgDVVSWPTNLGWMMGPWLVYASllngaSMALYNGSPLG-SGFA--- 436
Cdd:PRK08276 149 SGTTGRPKGIkrPLPGLDPDEAP------------GMMLALLGFGMYGGPDSVYLS-----PAPLYHTAPLRfGMSAlal 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 437 --------KF--------VQDSKVTMLGVIP-------SLVRSWRNAnstsgFDWSAIRCFASTG-------EASNIDey 486
Cdd:PRK08276 212 ggtvvvmeKFdaeealalIERYRVTHSQLVPtmfvrmlKLPEEVRAR-----YDVSSLRVAIHAAapcpvevKRAMID-- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 487 lWlMGrahykPII-EYCGGTEIGGGFVTGSllqAQSLAAFST--PAMCCSLFILDDQGHPIPQNVPGMGELALGplmlGA 563
Cdd:PRK08276 285 -W-WG-----PIIhEYYASSEGGGVTVITS---EDWLAHPGSvgKAVLGEVRILDEDGNELPPGEIGTVYFEMD----GY 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 564 SNTLLNADHygvyfKGMPIWNGKVLRRHGDVFERTARGYYHAHGRADDTMNLGGIKVSSVEIEricngadsNILET---- 639
Cdd:PRK08276 351 PFEYHNDPE-----KTAAARNPHGWVTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIE--------NLLVThpkv 417
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 640 ---AAIGIPPSGGGpEQLaLAVVLKNSNVTSQDLLTLR-MSFnsaLQKTLNPLFRVSQVVPVPSLPRTASNKVMRRVLRQ 715
Cdd:PRK08276 418 advAVFGVPDEEMG-ERV-KAVVQPADGADAGDALAAElIAW---LRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLRD 492
|
....*...
gi 502086856 716 QLVENTQS 723
Cdd:PRK08276 493 RYWEGRQR 500
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
592-722 |
5.88e-06 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 49.22 E-value: 5.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 592 GDVFERTARGYYHAHGRADDTMNLGGIKVSSVEIEricngadSNILET------AAIGIPPSGGGpEQLALAVVLKNSNV 665
Cdd:PRK07445 329 DDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVE-------AAILATglvqdvCVLGLPDPHWG-EVVTAIYVPKDPSI 400
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 502086856 666 TsqdlltlRMSFNSALQKTLNPLFRVSQVVPVPSLPRTASNKVMRRVLRQQLVENTQ 722
Cdd:PRK07445 401 S-------LEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQIAVQRLG 450
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
590-717 |
7.13e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 49.11 E-value: 7.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 590 RHGDVFERTARGYYHAHGRADDTMNLGGIKVSSVEIERICNGAdSNILETAAIGIPPSGGGpEQLALAVVLKNSNVTSQD 669
Cdd:PRK06145 376 RSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYEL-PEVAEAAVIGVHDDRWG-ERITAVVVLNPGATLTLE 453
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 502086856 670 LLTLRMSFNSALQKTlnPlfrvSQVVPVPSLPRTASNKVMRRVLRQQL 717
Cdd:PRK06145 454 ALDRHCRQRLASFKV--P----RQLKVRDELPRNPSGKVLKRVLRDEL 495
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
220-716 |
8.02e-06 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 49.11 E-value: 8.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 220 VAYALESLGLEKGSAIAIDMPMHCKSVVIYLAIVLAGYVVVSIADSFAPREISSRLKISNAKVIFTqDLILRGDKTLPLY 299
Cdd:PRK05852 56 LAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLI-DADGPHDRAEPTT 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 300 SRivdaeSPMAI-VIPTRGSEFSMKLRDGDlawcnfmdgvnkikgkefIAVEEPVETFTN---------ILFSSGTTGDP 369
Cdd:PRK05852 135 RW-----WPLTVnVGGDSGPSGGTLSVHLD------------------AATEPTPATSTPeglrpddamIMFTGGTTGLP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 370 KAIPWT--NISPLKAAADAWCHLDVRKGDVVSWPTNLGWMMGPWLVyASLLNGASMAL-YNGSPLGSGFAKFVQDSKVTM 446
Cdd:PRK05852 192 KMVPWThaNIASSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALL-ATLASGGAVLLpARGRFSAHTFWDDIKAVGATW 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 447 LGVIPSLVRSW--RNANSTSGFDWSAIRcFASTGEASNIDEYLWLMGRAHYKPIIEYCGGTE---------IGGGFVTGS 515
Cdd:PRK05852 271 YTAVPTIHQILleRAATEPSGRKPAALR-FIRSCSAPLTAETAQALQTEFAAPVVCAFGMTEathqvtttqIEGIGQTEN 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 516 LLQAQSLAAFSTPAmccSLFILDDQGHPIPqnvPG-MGELAL-GPLM----LG-ASNTLLNADHYgvyfkgmpiWngkvl 588
Cdd:PRK05852 350 PVVSTGLVGRSTGA---QIRIVGSDGLPLP---AGaVGEVWLrGTTVvrgyLGdPTITAANFTDG---------W----- 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 589 RRHGDVFERTARGYYHAHGRADDTMNLGGIKVSSVEIERICNGADsNILETAAIGIPPSGGGpEQLALAVVLKNS-NVTS 667
Cdd:PRK05852 410 LRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHP-NVMEAAVFGVPDQLYG-EAVAAVIVPRESaPPTA 487
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 502086856 668 QDLLtlrmsfnSALQKTLNPLFRVSQVVPVPSLPRTASNKVMRRVLRQQ 716
Cdd:PRK05852 488 EELV-------QFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAVAEQ 529
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
208-715 |
8.35e-06 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 48.99 E-value: 8.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 208 MTLEELRQEVWLVAYALESLGLEKGSAIAIDMPMHCKSVVIYLAIVLAGYVVVSIADSFAP---REISSRLKISnaKVIF 284
Cdd:PRK13382 69 LTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGpalAEVVTREGVD--TVIY 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 285 TQDLILRGDKTL---PLYSRIVDAESpmaivipTRGSEFSMKLRDGDLawcnfmdgvnkikGKEFIAVEEPVETftnILF 361
Cdd:PRK13382 147 DEEFSATVDRALadcPQATRIVAWTD-------EDHDLTVEVLIAAHA-------------GQRPEPTGRKGRV---ILL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 362 SSGTTGDPKAIPWT---NISPLKAAAD--AWCHldvRKGDVVSWPtnlgwMMGPW----LVYASLLNGASMALYNGSPLG 432
Cdd:PRK13382 204 TSGTTGTPKGARRSgpgGIGTLKAILDrtPWRA---EEPTVIVAP-----MFHAWgfsqLVLAASLACTIVTRRRFDPEA 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 433 SgfAKFVQDSKVTMLGVIPSLVRSW-----RNANSTSGfdwSAIRCFASTGEASNIDEYLWLMGRahYKPII--EYcGGT 505
Cdd:PRK13382 276 T--LDLIDRHRATGLAVVPVMFDRImdlpaEVRNRYSG---RSLRFAAASGSRMRPDVVIAFMDQ--FGDVIynNY-NAT 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 506 EIG-GGFVTGSLLQAQSLAAfSTPAMCCSLFILDDQGHPIPQnvpgmGELalGPLMLgASNTLlnadhygvyFKGMPiwN 584
Cdd:PRK13382 348 EAGmIATATPADLRAAPDTA-GRPAEGTEIRILDQDFREVPT-----GEV--GTIFV-RNDTQ---------FDGYT--S 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 585 GKVLRRH------GDVfertarGYYHAHGR-----ADDTMNL-GGIKVSSVEIERICNGADSnILETAAIGIPPSGGGpE 652
Cdd:PRK13382 408 GSTKDFHdgfmasGDV------GYLDENGRlfvvgRDDEMIVsGGENVYPIEVEKTLATHPD-VAEAAVIGVDDEQYG-Q 479
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502086856 653 QLALAVVLKNSNVTSQDLLTLRMSFNSALQKTlnPlfrvSQVVPVPSLPRTASNKVMRRVLRQ 715
Cdd:PRK13382 480 RLAAFVVLKPGASATPETLKQHVRDNLANYKV--P----RDIVVLDELPRGATGKILRRELQA 536
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
536-717 |
8.53e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 48.93 E-value: 8.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 536 ILDDQGHPIPQNVPGMGELAL-GPLMLgasntllnaDHYgvyFKGmpiwNGKVLRRH----GDVFERTARGYYHAHGRAD 610
Cdd:PRK07008 369 IVGDDGRELPWDGKAFGDLQVrGPWVI---------DRY---FRG----DASPLVDGwfptGDVATIDADGFMQITDRSK 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 611 DTMNLGGIKVSSVEIERICnGADSNILETAAIGIPpsggGP---EQLALAVVLK-NSNVTSQDLLTLrmsFNSALQKTLN 686
Cdd:PRK07008 433 DVIKSGGEWISSIDIENVA-VAHPAVAEAACIACA----HPkwdERPLLVVVKRpGAEVTREELLAF---YEGKVAKWWI 504
|
170 180 190
....*....|....*....|....*....|.
gi 502086856 687 PlfrvSQVVPVPSLPRTASNKVMRRVLRQQL 717
Cdd:PRK07008 505 P----DDVVFVDAIPHTATGKLQKLKLREQF 531
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
353-715 |
1.18e-05 |
|
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.
Pssm-ID: 341238 [Multi-domain] Cd Length: 411 Bit Score: 48.50 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 353 VETFTNILFSSGTTGDPKAIPWTnisplkaAADAWCHldvrkgdVVSWPTNLG------WMM--------GPWLVYASLL 418
Cdd:cd05912 76 LDDIATIMYTSGTTGKPKGVQQT-------FGNHWWS-------AIGSALNLGlteddnWLCalplfhisGLSILMRSVI 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 419 NGASMALYNgsplgsgfaKF--------VQDSKVTMLGVIPSLVRswRNANSTSGFDWSAIRCFASTGEAsnIDEYLWLM 490
Cdd:cd05912 142 YGMTVYLVD---------KFdaeqvlhlINSGKVTIISVVPTMLQ--RLLEILGEGYPNNLRCILLGGGP--APKPLLEQ 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 491 GRAHYKPIIEYCGGTEIGGGFVTGSLLQAQS-LAAFSTPAMCCSLFILDDQGHPipqnvPGMGELAL-GPLMLGAsntll 568
Cdd:cd05912 209 CKEKGIPVYQSYGMTETCSQIVTLSPEDALNkIGSAGKPLFPVELKIEDDGQPP-----YEVGEILLkGPNVTKG----- 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 569 nadhygvYFkGMPIWNGKVLR----RHGDVFERTARGYYHAHGRADDTMNLGGIKVSSVEIERICnGADSNILETAAIGI 644
Cdd:cd05912 279 -------YL-NRPDATEESFEngwfKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVL-LSHPAIKEAGVVGI 349
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502086856 645 PPSGGGpeQLALAVVLKNSNVTSQDLLtlrmsfnSALQKTLNPLFRVSQVVPVPSLPRTASNKVMRRVLRQ 715
Cdd:cd05912 350 PDDKWG--QVPVAFVVSERPISEEELI-------AYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHELKQ 411
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
206-371 |
1.39e-05 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 48.46 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 206 QRMTLEELRQEVWLVAYALESLGLEKGSAIAIDMPMHCKSVVIYLAIVLAGYVVVSIADSFAPREISSRLKISNAKVIFT 285
Cdd:PRK05605 56 ATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVEHNPLYTAHELEHPFEDHGARVAIV 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 286 QDLI------LRGDKTLPlysRIVDAESPMAIVIPTRgseFSMKL--------RD-------GDLAWCNFMDGVnkiKGK 344
Cdd:PRK05605 136 WDKVaptverLRRTTPLE---TIVSVNMIAAMPLLQR---LALRLpipalrkaRAaltgpapGTVPWETLVDAA---IGG 206
|
170 180 190
....*....|....*....|....*....|
gi 502086856 345 EFIAVEEPVETFTN---ILFSSGTTGDPKA 371
Cdd:PRK05605 207 DGSDVSHPRPTPDDvalILYTSGTTGKPKG 236
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
206-713 |
2.01e-05 |
|
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: 47.65 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 206 QRMTLEELRQEVWLVAYALESLGLEKGSAIAIDMPMHCKSVVIYLAIVLAG--YVVVSIAdsfAPREisSRLKI---SNA 280
Cdd:cd12114 11 GTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGaaYVPVDID---QPAA--RREAIladAGA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 281 KVIFTQDLILRGDKTLPLYSR-IVDAESPMAIVIPTRgsefsmkLRDGDLAWcnfmdgvnkikgkefiaveepvetftnI 359
Cdd:cd12114 86 RLVLTDGPDAQLDVAVFDVLIlDLDALAAPAPPPPVD-------VAPDDLAY---------------------------V 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 360 LFSSGTTGDPKAIPWTNISPLKAAADAWCHLDVRKGDVVSWPTNLGWMMGPWLVYASLLNGASMALYNGSPLG--SGFAK 437
Cdd:cd12114 132 IFTSGSTGTPKGVMISHRAALNTILDINRRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRdpAHWAE 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 438 FVQDSKVTMLGVIPSLV--------------RSWRNAnSTSGfDW------SAIRC------FASTG---EASnideyLW 488
Cdd:cd12114 212 LIERHGVTLWNSVPALLemlldvleaaqallPSLRLV-LLSG-DWipldlpARLRAlapdarLISLGgatEAS-----IW 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 489 lmgrAHYKPI---------IEYcggteigggfvtGSLLQAQslaafstpamccSLFILDDQGHPIPQNVPgmGELALG-- 557
Cdd:cd12114 285 ----SIYHPIdevppdwrsIPY------------GRPLANQ------------RYRVLDPRGRDCPDWVP--GELWIGgr 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 558 PLMLG-ASNTLLNADHYgvyfkgMPIWNGKVLRRHGDVFERTARGYYHAHGRADDTMNLGGIKVSSVEIERICNgADSNI 636
Cdd:cd12114 335 GVALGyLGDPELTAARF------VTHPDGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQ-AHPGV 407
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502086856 637 LETAAIGIPpsGGGPEQLALAVVLKN-SNVTSQDLLTLRmsfnsaLQKTLNPLFRVSQVVPVPSLPRTASNKVMRRVL 713
Cdd:cd12114 408 ARAVVVVLG--DPGGKRLAAFVVPDNdGTPIAPDALRAF------LAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
592-716 |
3.48e-05 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 47.18 E-value: 3.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 592 GDVFERTARGYYHAHGRADDTMNLGGIKVSSVEIERICNGADSnILETAAIGIP-PSGGgpeQLALAVVLKNSNVTSqDL 670
Cdd:PRK07514 382 GDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPG-VVESAVIGVPhPDFG---EGVTAVVVPKPGAAL-DE 456
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 502086856 671 LTLRMSFNSALQKtlnplFRV-SQVVPVPSLPRTASNKVMRRVLRQQ 716
Cdd:PRK07514 457 AAILAALKGRLAR-----FKQpKRVFFVDELPRNTMGKVQKNLLREQ 498
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
528-713 |
4.04e-05 |
|
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341311 [Multi-domain] Cd Length: 479 Bit Score: 46.70 E-value: 4.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 528 PAMCCSLFILDDQGHPIPQNVPgmGELALGPLMLG---ASNTLLNADHygvyFKGMPIWNGKVLRRHGDVFERTARGYYH 604
Cdd:cd17656 306 PISNTWIYILDQEQQLQPQGIV--GELYISGASVArgyLNRQELTAEK----FFPDPFDPNERMYRTGDLARYLPDGNIE 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 605 AHGRADDTMNLGGIKVSSVEIERICNGADsNILETAAIGIPPSGGGPEQLALAVVLKNSNvTSQdlltLRMSFNSALQKT 684
Cdd:cd17656 380 FLGRADHQVKIRGYRIELGEIEAQLLNHP-GVSEAVVLDKADDKGEKYLCAYFVMEQELN-ISQ----LREYLAKQLPEY 453
|
170 180
....*....|....*....|....*....
gi 502086856 685 LNPlfrvSQVVPVPSLPRTASNKVMRRVL 713
Cdd:cd17656 454 MIP----SFFVPLDQLPLTPNGKVDRKAL 478
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
538-715 |
6.01e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 46.14 E-value: 6.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 538 DDQGHPIPQNVPGMGELAL-GPLMLG-------ASNTLLNADhyGVYfkgmpiwngkvlrRHGDVFERTARGYYHAHGR- 608
Cdd:PRK07787 308 DEDGGPVPHDGETVGELQVrGPTLFDgylnrpdATAAAFTAD--GWF-------------RTGDVAVVDPDGMHRIVGRe 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 609 ADDTMNLGGIKVSSVEIERICNGADSnILETAAIGIPPSGGGpeQLALAVVLKNSNVTSQDLLTLrmsfnsaLQKTLNPL 688
Cdd:PRK07787 373 STDLIKSGGYRIGAGEIETALLGHPG-VREAAVVGVPDDDLG--QRIVAYVVGADDVAADELIDF-------VAQQLSVH 442
|
170 180
....*....|....*....|....*..
gi 502086856 689 FRVSQVVPVPSLPRTASNKVMRRVLRQ 715
Cdd:PRK07787 443 KRPREVRFVDALPRNAMGKVLKKQLLS 469
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
590-716 |
8.23e-05 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 45.79 E-value: 8.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 590 RHG-----DVFERTARGYYHAHGRADDTMNLGGIKVSSVEIERICNGADSnILETAAIGIPPSGGGpEQLALAVVLKNSN 664
Cdd:PRK13388 378 RHGmywsgDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPA-INRVAVYAVPDERVG-DQVMAALVLRDGA 455
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 502086856 665 VTSQDLLTlrmSFNSAlQKTLNP-----LFRVSQvvpvpSLPRTASNKVMRRVLRQQ 716
Cdd:PRK13388 456 TFDPDAFA---AFLAA-QPDLGTkawprYVRIAA-----DLPSTATNKVLKRELIAQ 503
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
207-714 |
8.49e-05 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.
Pssm-ID: 341283 [Multi-domain] Cd Length: 486 Bit Score: 45.75 E-value: 8.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 207 RMTLEELRQEVWLVAYALESLGLEKG---SAIAIDMPMHCKSvviYLAIVLAGYVVVSIADSFAPREISSRLKISNAKVI 283
Cdd:cd12118 29 RYTWRQTYDRCRRLASALAALGISRGdtvAVLAPNTPAMYEL---HFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 284 FT------QDLILRGDKTlPLYSRIVDAESPMAiviptrgsefsmklrdgdlawcnfmdgVNkikgkefiaveepvetft 357
Cdd:cd12118 106 FVdrefeyEDLLAEGDPD-FEWIPPADEWDPIA---------------------------LN------------------ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 358 nilFSSGTTGDPKAIPWTNISPLKAAADAWCHLDVRKGDVVSWPTNL----GWMmGPWLVYAslLNGASMALYNGSPlgS 433
Cdd:cd12118 140 ---YTSGTTGRPKGVVYHHRGAYLNALANILEWEMKQHPVYLWTLPMfhcnGWC-FPWTVAA--VGGTNVCLRKVDA--K 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 434 GFAKFVQDSKVTMLGVIPSLVRSWRNANS--TSGFDWsaiRCFASTGEASNIDEYLWLMGRAHYKPIIEYcGGTEIGGGF 511
Cdd:cd12118 212 AIYDLIEKHKVTHFCGAPTVLNMLANAPPsdARPLPH---RVHVMTAGAPPPAAVLAKMEELGFDVTHVY-GLTETYGPA 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 512 VTG--------------SLLQA-QSLAAFSTPAmccsLFILDDQGH-PIPQNVPGMGELAL--GPLMLGasntllnadhy 573
Cdd:cd12118 288 TVCawkpewdelpteerARLKArQGVRYVGLEE----VDVLDPETMkPVPRDGKTIGEIVFrgNIVMKG----------- 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 574 gvYFKGmPIWNGKVLR----RHGDVFERTARGYYHAHGRADDTMNLGGIKVSSVEIERICNgADSNILETAAIGIPPSGG 649
Cdd:cd12118 353 --YLKN-PEATAEAFRggwfHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLY-KHPAVLEAAVVARPDEKW 428
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502086856 650 GpEQLALAVVLKN-SNVTSQDLltlrMSFnsaLQKTLnPLFRVSQVVPVPSLPRTASNKVMRRVLR 714
Cdd:cd12118 429 G-EVPCAFVELKEgAKVTEEEI----IAF---CREHL-AGFMVPKTVVFGELPKTSTGKIQKFVLR 485
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
535-718 |
1.14e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 45.93 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 535 FILDDQGHPIPQNvpGMGELALGPLML--------GASNTLLNADHYGVyfkgmpiwNGKVLRRHGDVFERTARGYYHAH 606
Cdd:PRK05691 2518 YILDADLALVPQG--ATGELYVGGAGLaqgyhdrpGLTAERFVADPFAA--------DGGRLYRTGDLVRLRADGLVEYV 2587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 607 GRADDTMNLGGIKVSSVEIE-RICNGADsnILETAAIGIPPSGGgpEQLALAVVLKNSNVTSQDLLTLRMSFNSALQKTL 685
Cdd:PRK05691 2588 GRIDHQVKIRGFRIELGEIEsRLLEHPA--VREAVVLALDTPSG--KQLAGYLVSAVAGQDDEAQAALREALKAHLKQQL 2663
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 502086856 686 nPLFRV-SQVVPVPSLPRTASNKVMRRVL--------RQQLV 718
Cdd:PRK05691 2664 -PDYMVpAHLILLDSLPLTANGKLDRRALpapdpelnRQAYQ 2704
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
220-372 |
2.18e-04 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 44.59 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 220 VAYALESLGLEKGSAIAIDMPMHCKSVVIYLAIVLAGYVVVSIADSFAPREISSRLKISNAKVIFTQdlilrgdktlply 299
Cdd:PLN02246 63 VAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLIITQ------------- 129
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502086856 300 SRIVDAESPMAiviptRGSEFSMKLRDGDLAWCNFMDGVNKIKGKEFIAVEEPVETFTNILFSSGTTGDPKAI 372
Cdd:PLN02246 130 SCYVDKLKGLA-----EDDGVTVVTIDDPPEGCLHFSELTQADENELPEVEISPDDVVALPYSSGTTGLPKGV 197
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
221-283 |
2.43e-04 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 44.27 E-value: 2.43e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502086856 221 AYALESLGLEKGSAIAIDMPMHCKSVVIYLAIVLAGYVVVSIADSFAPREISSRLKISNAKVI 283
Cdd:PRK08974 63 AYLQNGLGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAKAI 125
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
531-713 |
6.30e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 43.62 E-value: 6.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 531 CCSlfILDDQGHPIPQNVPGmgELALGPLMLgASNTL----LNADHYGVYFKGMPiwnGKVLRRHGDVFERTARGYYHAH 606
Cdd:PRK05691 1453 LCR--VLDAELNLLPPGVAG--ELCIGGAGL-ARGYLgrpaLTAERFVPDPLGED---GARLYRTGDRARWNADGALEYL 1524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 607 GRADDTMNLGGIKVSSVEIE-RICNGADsniLETAAIGIPPSGGGPEQLALAVVLKNSNVTSQDLLtlrmsfnSALQKTL 685
Cdd:PRK05691 1525 GRLDQQVKLRGFRVEPEEIQaRLLAQPG---VAQAAVLVREGAAGAQLVGYYTGEAGQEAEAERLK-------AALAAEL 1594
|
170 180
....*....|....*....|....*....
gi 502086856 686 nPLFRV-SQVVPVPSLPRTASNKVMRRVL 713
Cdd:PRK05691 1595 -PEYMVpAQLIRLDQMPLGPSGKLDRRAL 1622
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
590-726 |
6.81e-04 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 42.91 E-value: 6.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 590 RHGDVFERTARGYYHAHGRADDTMNLGGIKVSSVEIERICNgADSNILETAAIGIPPSGGGPEQLALAVVLKNSNVTSQD 669
Cdd:PLN02574 433 RTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLI-SHPEIIDAAVTAVPDKECGEIPVAFVVRRQGSTLSQEA 511
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 502086856 670 LLtlrmsfnSALQKTLNPLFRVSQVVPVPSLPRTASNKVMRRVLRQQLVeNTQSSRI 726
Cdd:PLN02574 512 VI-------NYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELKRSLT-NSVSSRL 560
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
209-372 |
2.82e-03 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 40.95 E-value: 2.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 209 TLEELRQEVWLVAYALESLGLEKGSAIAIdMPMHCKSVVIYLAIVLA-GYVVVSIADSFAPREISSRLKISNAKVIFTQD 287
Cdd:PLN02430 78 TYKEVYEEVLQIGSALRASGAEPGSRVGI-YGSNCPQWIVAMEACAAhSLICVPLYDTLGPGAVDYIVDHAEIDFVFVQD 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 288 L----ILRGD-------KTLPLYSRIVDAESpmaivipTRGSEFSMKLrdgdLAWCNFMDgvnkiKGKEfiaveEPVETF 356
Cdd:PLN02430 157 KkikeLLEPDcksakrlKAIVSFTSVTEEES-------DKASQIGVKT----YSWIDFLH-----MGKE-----NPSETN 215
|
170 180
....*....|....*....|...
gi 502086856 357 T-------NILFSSGTTGDPKAI 372
Cdd:PLN02430 216 PpkpldicTIMYTSGTSGDPKGV 238
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
359-447 |
6.29e-03 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 39.91 E-value: 6.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502086856 359 ILFSSGTTGDPKAIPWT--NI-SPLKAAADAwchLDVRKGDVV--SWPT--NLGWMMGPWLVyasLLNGASMAlYNGSPL 431
Cdd:PRK08633 787 IIFSSGSEGEPKGVMLShhNIlSNIEQISDV---FNLRNDDVIlsSLPFfhSFGLTVTLWLP---LLEGIKVV-YHPDPT 859
|
90
....*....|....*..
gi 502086856 432 -GSGFAKFVQDSKVTML 447
Cdd:PRK08633 860 dALGIAKLVAKHRATIL 876
|
|
| |
