|
Name |
Accession |
Description |
Interval |
E-value |
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
55-569 |
0e+00 |
|
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: 689.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 55 DRIALIDKYGHHTYRELYDRSLCLAQEICRlqgcKVGDLQEERVSFLCSNDVSYVVAQWASWMSGGVAVPLYWKHPEAQL 134
Cdd:cd05941 1 DRIAIVDDGDSITYADLVARAARLANRLLA----LGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 135 EYFIQDSRSSLVVvgqeylerlsplaqrlgvpllpltpavyhgatekpteqpveesgwrdRGAMIFYTSGTTGRPKGALS 214
Cdd:cd05941 77 EYVITDSEPSLVL-----------------------------------------------DPALILYTSGTTGRPKGVVL 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 215 THRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSAQQVWekfLSSEAPQITVFMAVP 294
Cdd:cd05941 110 THANLAANVRALVDAWRWTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFLPKFDPKEVA---ISRLMPSITVFMGVP 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 295 TVYSKLLDYYDKHFTQPhvqDFVRAVCKERIRLMVSGSAALPVPLLEKWRSATGHTLLERYGMTEIGMALSNPLTEARVP 374
Cdd:cd05941 187 TIYTRLLQYYEAHFTDP---QFARAAAAERLRLMVSGSAALPVPTLEEWEAITGHTLLERYGMTEIGMALSNPLDGERRP 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 375 GSVGTPLPGVEVRIISENPQKgspyiihaegnergtkvtPGFEEKEGELLVRGPSVFREYWDKPEETKSAFTSDGWFRTG 454
Cdd:cd05941 264 GTVGMPLPGVQARIVDEETGE------------------PLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGWFKTG 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 455 DTAVFK-DARYWIRGRTSVDIIKTGGYKVSALEIERHLLAHPSITDVAVIGVPDMTWGQRVTAVVALQEG-HSLSHGDLK 532
Cdd:cd05941 326 DLGVVDeDGYYWILGRSSVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGaAALSLEELK 405
|
490 500 510
....*....|....*....|....*....|....*..
gi 1720427507 533 EWARGVLAPYAVPSELLLVEEIPRNQMGKVNKKELLK 569
Cdd:cd05941 406 EWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
49-571 |
1.69e-147 |
|
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: 432.70 E-value: 1.69e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 49 RALAFGDRIALIDKYGHHTYRELYDRSLCLAQEICRLqGCKVGDlqeeRVSFLCSNDVSYVVAQWASWMSGGVAVPLYWK 128
Cdd:COG0318 8 AAARHPDRPALVFGGRRLTYAELDARARRLAAALRAL-GVGPGD----RVALLLPNSPEFVVAFLAALRAGAVVVPLNPR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 129 HPEAQLEYFIQDSRSSLVVVgqeylerlsplaqrlgvpllpltpavyhgatekpteqpveesgwrdrgAMIFYTSGTTGR 208
Cdd:COG0318 83 LTAEELAYILEDSGARALVT------------------------------------------------ALILYTSGTTGR 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 209 PKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSAQQVWEKFlssEAPQIT 288
Cdd:COG0318 115 PKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPRFDPERVLELI---ERERVT 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 289 VFMAVPTVYSKLLDYYDKHFTQPHvqdfvravckeRIRLMVSGSAALPVPLLEKWRSATGHTLLERYGMTEIGMALSNPL 368
Cdd:COG0318 192 VLFGVPTMLARLLRHPEFARYDLS-----------SLRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTETSPVVTVNP 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 369 TE--ARVPGSVGTPLPGVEVRIIsenpqkgspyiihaegNERGTKVTPGfeeKEGELLVRGPSVFREYWDKPEETKSAFt 446
Cdd:COG0318 261 EDpgERRPGSVGRPLPGVEVRIV----------------DEDGRELPPG---EVGEIVVRGPNVMKGYWNDPEATAEAF- 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 447 SDGWFRTGDTAVF-KDARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSITDVAVIGVPDMTWGQRVTAVVALQEGHS 525
Cdd:COG0318 321 RDGWLRTGDLGRLdEDGYLYIVGRKK-DMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAE 399
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1720427507 526 LSHGDLKEWARGVLAPYAVPSELLLVEEIPRNQMGKVNKKELLKQL 571
Cdd:COG0318 400 LDAEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRERY 445
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
53-567 |
1.60e-116 |
|
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: 354.18 E-value: 1.60e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 53 FGDRIALIDKYGHHTYRELYDRSLCLAQeicRLQ--GCKVGDlqeeRVSFLCSNDVSYVVAQWASWMSGGVAVPLYWKHP 130
Cdd:cd05936 12 FPDKTALIFMGRKLTYRELDALAEAFAA---GLQnlGVQPGD----RVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 131 EAQLEYFIQDSRSSLVVVGQEYLERLSPlaqrlgvpllpltpavyhGATEKPTEQPVEESGwrdrgAMIFYTSGTTGRPK 210
Cdd:cd05936 85 PRELEHILNDSGAKALIVAVSFTDLLAA------------------GAPLGERVALTPEDV-----AVLQYTSGTTGVPK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 211 GALSTHRNLAAVVTGlvhSWAWTK-----NDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSAQQVWEKFlssEAP 285
Cdd:cd05936 142 GAMLTHRNLVANALQ---IKAWLEdllegDDVVLAALPLFHVFGLTVALLLPLALGATIVLIPRFRPIGVLKEI---RKH 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 286 QITVFMAVPTVYSKLLDYYDKHFTQPhvqdfvravckERIRLMVSGSAALPVPLLEKWRSATGHTLLERYGMTEIG-MAL 364
Cdd:cd05936 216 RVTIFPGVPTMYIALLNAPEFKKRDF-----------SSLRLCISGGAPLPVEVAERFEELTGVPIVEGYGLTETSpVVA 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 365 SNPLTEARVPGSVGTPLPGVEVRIISEnpqkgspyiihaEGNErgtkVTPGfeeKEGELLVRGPSVFREYWDKPEETKSA 444
Cdd:cd05936 285 VNPLDGPRKPGSIGIPLPGTEVKIVDD------------DGEE----LPPG---EVGELWVRGPQVMKGYWNRPEETAEA 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 445 FTsDGWFRTGDTAVF-KDARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSITDVAVIGVPDMTWGQRVTAVVALQEG 523
Cdd:cd05936 346 FV-DGWLRTGDIGYMdEDGYFFIVDRKK-DMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEG 423
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1720427507 524 HSLSHGDLKEWARGVLAPYAVPSELLLVEEIPRNQMGKVNKKEL 567
Cdd:cd05936 424 ASLTEEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRREL 467
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
50-572 |
4.54e-114 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 348.79 E-value: 4.54e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 50 ALAFGDRIALIDKYG-HHTYRELYDRSLCLAQEICRLqGCKVGDlqeeRVSFLCSNDVSYVVAQWASWMSGGVAVPLYWK 128
Cdd:PRK07514 12 AFADRDAPFIETPDGlRYTYGDLDAASARLANLLVAL-GVKPGD----RVAVQVEKSPEALALYLATLRAGAVFLPLNTA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 129 HPEAQLEYFIQDSRSSLVVVGQEYLERLSPLAQRLGVPLL---------PLTPAvyhGATEKPTEQPVEESGwrDRGAMI 199
Cdd:PRK07514 87 YTLAELDYFIGDAEPALVVCDPANFAWLSKIAAAAGAPHVetldadgtgSLLEA---AAAAPDDFETVPRGA--DDLAAI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 200 FYTSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSAQQVWEKF 279
Cdd:PRK07514 162 LYTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIHALPIFHTHGLFVATNVALLAGASMIFLPKFDPDAVLALM 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 280 lsseaPQITVFMAVPTVYSKLLDyyDKHFTqphvqdfvRAVCKeRIRLMVSGSAalpvPLL----EKWRSATGHTLLERY 355
Cdd:PRK07514 242 -----PRATVMMGVPTFYTRLLQ--EPRLT--------REAAA-HMRLFISGSA----PLLaethREFQERTGHAILERY 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 356 GMTEIGMALSNPLTEARVPGSVGTPLPGVEVRIIsenpqkgspyiihaeGNERGTKVTPGfeeKEGELLVRGPSVFREYW 435
Cdd:PRK07514 302 GMTETNMNTSNPYDGERRAGTVGFPLPGVSLRVT---------------DPETGAELPPG---EIGMIEVKGPNVFKGYW 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 436 DKPEETKSAFTSDGWFRTGDTAVFkDAR--YWIRGRtSVDIIKTGGYKVSALEIERHLLAHPSITDVAVIGVPDMTWGQR 513
Cdd:PRK07514 364 RMPEKTAEEFRADGFFITGDLGKI-DERgyVHIVGR-GKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEG 441
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720427507 514 VTAVVALQEGHSLSHGDLKEWARGVLAPYAVPSELLLVEEIPRNQMGKVnKKELLKQLY 572
Cdd:PRK07514 442 VTAVVVPKPGAALDEAAILAALKGRLARFKQPKRVFFVDELPRNTMGKV-QKNLLREQY 499
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
30-568 |
3.38e-111 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 340.43 E-value: 3.38e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 30 SLLPTTPEAHTDGSvpvfiRALAFGDRialidkygHHTYRELYDRSLCLAQEICRLQgckvgdlqeeRVSFLCSNDVSYV 109
Cdd:PRK07787 3 SLNPAAVAAAADIA-----DAVRIGGR--------VLSRSDLAGAATAVAERVAGAR----------RVAVLATPTLATV 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 110 VAQWASWMSGGVAVPLYWKHPEAQLEYFIQDSRSSLVVVGqeylerlsPLAQRLGVPLLP--LTPAVYHGATEKPTEQPv 187
Cdd:PRK07787 60 LAVVGALIAGVPVVPVPPDSGVAERRHILADSGAQAWLGP--------APDDPAGLPHVPvrLHARSWHRYPEPDPDAP- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 188 eesgwrdrgAMIFYTSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVML 267
Cdd:PRK07787 131 ---------ALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAWQWTADDVLVHGLPLFHVHGLVLGVLGPLRIGNRFVHT 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 268 PEFSAQQVWEkflsSEAPQITVFMAVPTVYSKLLDyydkhftqphVQDFVRAVckERIRLMVSGSAALPVPLLEKWRSAT 347
Cdd:PRK07787 202 GRPTPEAYAQ----ALSEGGTLYFGVPTVWSRIAA----------DPEAARAL--RGARLLVSGSAALPVPVFDRLAALT 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 348 GHTLLERYGMTEIGMALSNPLTEARVPGSVGTPLPGVEVRIISENpqkGSPyiIHAEGnergtkvtpgfeEKEGELLVRG 427
Cdd:PRK07787 266 GHRPVERYGMTETLITLSTRADGERRPGWVGLPLAGVETRLVDED---GGP--VPHDG------------ETVGELQVRG 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 428 PSVFREYWDKPEETKSAFTSDGWFRTGDTAVFkDARYWIR--GRTSVDIIKTGGYKVSALEIERHLLAHPSITDVAVIGV 505
Cdd:PRK07787 329 PTLFDGYLNRPDATAAAFTADGWFRTGDVAVV-DPDGMHRivGRESTDLIKSGGYRIGAGEIETALLGHPGVREAAVVGV 407
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720427507 506 PDMTWGQRVTAVVALQEGhsLSHGDLKEWARGVLAPYAVPSELLLVEEIPRNQMGKVNKKELL 568
Cdd:PRK07787 408 PDDDLGQRIVAYVVGADD--VAADELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLL 468
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
49-564 |
2.80e-106 |
|
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: 326.49 E-value: 2.80e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 49 RALAFGDRIALIDKYGHHTYRELYDRSLCLAQEICRLqGCKVGDlqeeRVSFLCSNDVSYVVAQWASWMSGGVAVPLYWK 128
Cdd:cd17631 4 RARRHPDRTALVFGGRSLTYAELDERVNRLAHALRAL-GVAKGD----RVAVLSKNSPEFLELLFAAARLGAVFVPLNFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 129 HPEAQLEYFIQDSRSSLVVvgqeylerlsplaqrlgvpllpltpavyhgatekpteqpveesgwrDRGAMIFYTSGTTGR 208
Cdd:cd17631 79 LTPPEVAYILADSGAKVLF----------------------------------------------DDLALLMYTSGTTGR 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 209 PKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSAQQVWEKFlssEAPQIT 288
Cdd:cd17631 113 PKGAMLTHRNLLWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVILRKFDPETVLDLI---ERHRVT 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 289 VFMAVPTVYSKLLDYYDkhFTQPHVQdfvravckeRIRLMVSGSAALPVPLLEKWRsATGHTLLERYGMTEIGM---ALS 365
Cdd:cd17631 190 SFFLVPTMIQALLQHPR--FATTDLS---------SLRAVIYGGAPMPERLLRALQ-ARGVKFVQGYGMTETSPgvtFLS 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 366 NPLTEARvPGSVGTPLPGVEVRIISENpqkgspyiihaegnerGTKVTPGfeeKEGELLVRGPSVFREYWDKPEETKSAF 445
Cdd:cd17631 258 PEDHRRK-LGSAGRPVFFVEVRIVDPD----------------GREVPPG---EVGEIVVRGPHVMAGYWNRPEATAAAF 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 446 tSDGWFRTGDTAVF-KDARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSITDVAVIGVPDMTWGQRVTAVVALQEGH 524
Cdd:cd17631 318 -RDGWFHTGDLGRLdEDGYLYIVDRKK-DMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGA 395
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1720427507 525 SLSHGDLKEWARGVLAPYAVPSELLLVEEIPRNQMGKVNK 564
Cdd:cd17631 396 ELDEDELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
52-567 |
1.82e-105 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 327.14 E-value: 1.82e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 52 AFGDRIALIDKYGHHTYRELYDRSLCLAQEIcRLQGCKVGDlqeeRVSFLCSNDVSYVVAQWASWMSGGVAVPLYWKHPE 131
Cdd:PRK06187 18 KHPDKEAVYFDGRRTTYAELDERVNRLANAL-RALGVKKGD----RVAVFDWNSHEYLEAYFAVPKIGAVLHPINIRLKP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 132 AQLEYFIQDSRSSLVVVGQEYLERLSPLAQRL----------GVPLLPLTPAVYHGAT---EKPTEQPVEESGWRDRGAM 198
Cdd:PRK06187 93 EEIAYILNDAEDRVVLVDSEFVPLLAAILPQLptvrtvivegDGPAAPLAPEVGEYEEllaAASDTFDFPDIDENDAAAM 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 199 iFYTSGTTGRPKGALSTHRNLAAVVTGlVHSW-AWTKNDVILHVLPLHHVHG----VVnkllcPLWVGATCVMLPEFSAQ 273
Cdd:PRK06187 173 -LYTSGTTGHPKGVVLSHRNLFLHSLA-VCAWlKLSRDDVYLVIVPMFHVHAwglpYL-----ALMAGAKQVIPRRFDPE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 274 QVWEKFlssEAPQITVFMAVPTVYSKLLDYYDKHFtqphvQDFVRavckerIRLMVSGSAALPVPLLEKWRSATGHTLLE 353
Cdd:PRK06187 246 NLLDLI---ETERVTFFFAVPTIWQMLLKAPRAYF-----VDFSS------LRLVIYGGAALPPALLREFKEKFGIDLVQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 354 RYGMTEIGMALS-NPLTE-----ARVPGSVGTPLPGVEVRIIsenpqkgspyiihaegNERGTKVTPGFEEKeGELLVRG 427
Cdd:PRK06187 312 GYGMTETSPVVSvLPPEDqlpgqWTKRRSAGRPLPGVEARIV----------------DDDGDELPPDGGEV-GEIIVRG 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 428 PSVFREYWDKPEETKSAFTsDGWFRTGDTAVFKDARY-WIRGRTSvDIIKTGGYKVSALEIERHLLAHPSITDVAVIGVP 506
Cdd:PRK06187 375 PWLMQGYWNRPEATAETID-GGWLHTGDVGYIDEDGYlYITDRIK-DVIISGGENIYPRELEDALYGHPAVAEVAVIGVP 452
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720427507 507 DMTWGQRVTAVVALQEGHSLSHGDLKEWARGVLAPYAVPSELLLVEEIPRNQMGKVNKKEL 567
Cdd:PRK06187 453 DEKWGERPVAVVVLKPGATLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVL 513
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
197-562 |
1.25e-103 |
|
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: 316.15 E-value: 1.25e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 197 AMIFYTSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVhGVVNKLLCPLWVGATCVMLPEFSAQQVW 276
Cdd:cd04433 3 ALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHI-GGLFGLLGALLAGGTVVLLPKFDPEAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 277 EKFlssEAPQITVFMAVPTVYSKLLDYYDKHftqPHVQDFVRAVCkerirlmvSGSAALPVPLLEKWRSATGHTLLERYG 356
Cdd:cd04433 82 ELI---EREKVTILLGVPTLLARLLKAPESA---GYDLSSLRALV--------SGGAPLPPELLERFEEAPGIKLVNGYG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 357 MTEIG--MALSNPLTEARVPGSVGTPLPGVEVRIISENpqkgspyiihaegnerGTKVTPGFEekeGELLVRGPSVFREY 434
Cdd:cd04433 148 LTETGgtVATGPPDDDARKPGSVGRPVPGVEVRIVDPD----------------GGELPPGEI---GELVVRGPSVMKGY 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 435 WDKPEETkSAFTSDGWFRTGDTAVFKDARY-WIRGRTSvDIIKTGGYKVSALEIERHLLAHPSITDVAVIGVPDMTWGQR 513
Cdd:cd04433 209 WNNPEAT-AAVDEDGWYRTGDLGRLDEDGYlYIVGRLK-DMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGER 286
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1720427507 514 VTAVVALQEGHSLSHGDLKEWARGVLAPYAVPSELLLVEEIPRNQMGKV 562
Cdd:cd04433 287 VVAVVVLRPGADLDAEELRAHVRERLAPYKVPRRVVFVDALPRTASGKI 335
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
50-567 |
6.19e-101 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 315.31 E-value: 6.19e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 50 ALAFGDRIALIDKYGHHTYRELYDRSLCLAQEICRLqGCKVGDlqeeRVSFLCSNDVSYVVAQWASWMSGGVAVPLYWKH 129
Cdd:PRK07656 15 ARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAAL-GIGKGD----RVAIWAPNSPHWVIAALGALKAGAVVVPLNTRY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 130 PEAQLEYFIQDSRSSLVVVGQEYLERLSPLAQRLgvpllPLTPAVYHGATEKPTEQPVEESGWRD---RG---------- 196
Cdd:PRK07656 90 TADEAAYILARGDAKALFVLGLFLGVDYSATTRL-----PALEHVVICETEEDDPHTEKMKTFTDflaAGdpaerapevd 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 197 ----AMIFYTSGTTGRPKGALSTHRNLaavvTGLVHSWA----WTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLP 268
Cdd:PRK07656 165 pddvADILFTSGTTGRPKGAMLTHRQL----LSNAADWAeylgLTEGDRYLAANPFFHVFGYKAGVNAPLMRGATILPLP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 269 EFSAQQVwekFLSSEAPQITVFMAVPTVYSKLLDYYDKHFTqphvqDFvravckERIRLMVSGSAALPVPLLEKWRSATG 348
Cdd:PRK07656 241 VFDPDEV---FRLIETERITVLPGPPTMYNSLLQHPDRSAE-----DL------SSLRLAVTGAASMPVALLERFESELG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 349 -HTLLERYGMTE-IGMALSNPLTEAR--VPGSVGTPLPGVEVRIISENpqkgspyiihaeGNERGTKVTpgfeekeGELL 424
Cdd:PRK07656 307 vDIVLTGYGLSEaSGVTTFNRLDDDRktVAGTIGTAIAGVENKIVNEL------------GEEVPVGEV-------GELL 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 425 VRGPSVFREYWDKPEETKSAFTSDGWFRTGDTAVFKDARY-WIRGRTSvDIIKTGGYKVSALEIERHLLAHPSITDVAVI 503
Cdd:PRK07656 368 VRGPNVMKGYYDDPEATAAAIDADGWLHTGDLGRLDEEGYlYIVDRKK-DMFIVGGFNVYPAEVEEVLYEHPAVAEAAVI 446
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720427507 504 GVPDMTWGQRVTAVVALQEGHSLSHGDLKEWARGVLAPYAVPSELLLVEEIPRNQMGKVNKKEL 567
Cdd:PRK07656 447 GVPDERLGEVGKAYVVLKPGAELTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRAL 510
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
67-569 |
2.28e-98 |
|
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: 308.09 E-value: 2.28e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 67 TYRELYDRSLCLAQEICRLqGCKVGDlqeeRVSFLCSNDVSYVVAQWASWMSGGVAVPLYWKHPEAQLEYFIQDSRSSLV 146
Cdd:cd05926 16 TYADLAELVDDLARQLAAL-GIKKGD----RVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 147 VVGQEYLERLSPLAQRLGVPLLPLT--PAVYH---------GATEKPTEQPVEESGWRDRGAMIFYTSGTTGRPKGALST 215
Cdd:cd05926 91 LTPKGELGPASRAASKLGLAILELAldVGVLIrapsaeslsNLLADKKNAKSEGVPLPDDLALILHTSGTTGRPKGVPLT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 216 HRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSAQQVWEKFlssEAPQITVFMAVPT 295
Cdd:cd05926 171 HRNLAASATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVLPPRFSASTFWPDV---RDYNATWYTAVPT 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 296 VYSKLLDYYDKHFTQPHVqdfvravckeRIRLMVSGSAALPVPLLEKWRSATGHTLLERYGMTEIG--MAlSNPL-TEAR 372
Cdd:cd05926 248 IHQILLNRPEPNPESPPP----------KLRFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEAAhqMT-SNPLpPGPR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 373 VPGSVGTPLpGVEVRIIsenpqkgspyiihaegNERGTKVTPGfeeKEGELLVRGPSVFREYWDKPEETKSAFTSDGWFR 452
Cdd:cd05926 317 KPGSVGKPV-GVEVRIL----------------DEDGEILPPG---VVGEICLRGPNVTRGYLNNPEANAEAAFKDGWFR 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 453 TGDTAVFKDARY-WIRGRTSvDIIKTGGYKVSALEIERHLLAHPSITDVAVIGVPDMTWGQRVTAVVALQEGHSLSHGDL 531
Cdd:cd05926 377 TGDLGYLDADGYlFLTGRIK-ELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGASVTEEEL 455
|
490 500 510
....*....|....*....|....*....|....*...
gi 1720427507 532 KEWARGVLAPYAVPSELLLVEEIPRNQMGKVNKKELLK 569
Cdd:cd05926 456 RAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
49-478 |
3.90e-92 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 289.21 E-value: 3.90e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 49 RALAFGDRIAL-IDKYGHHTYRELYDRSLCLAQEIcRLQGCKVGDlqeeRVSFLCSNDVSYVVAQWASWMSGGVAVPLYW 127
Cdd:pfam00501 4 QAARTPDKTALeVGEGRRLTYRELDERANRLAAGL-RALGVGKGD----RVAILLPNSPEWVVAFLACLKAGAVYVPLNP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 128 KHPEAQLEYFIQDSRSSLVVVGQE-YLERLSPLAQRLGVPLLPLtpaVYHGATEKPTEQPVEESGWRDRG---------- 196
Cdd:pfam00501 79 RLPAEELAYILEDSGAKVLITDDAlKLEELLEALGKLEVVKLVL---VLDRDPVLKEEPLPEEAKPADVPpppppppdpd 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 197 --AMIFYTSGTTGRPKGALSTHRNLAAVVTGL----VHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEF 270
Cdd:pfam00501 156 dlAYIIYTSGTTGKPKGVMLTHRNLVANVLSIkrvrPRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPGF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 271 SAQQVWEKFLSSEAPQITVFMAVPTVYSKLLDyydkhftqphvQDFVRAVCKERIRLMVSGSAALPVPLLEKWRSATGHT 350
Cdd:pfam00501 236 PALDPAALLELIERYKVTVLYGVPTLLNMLLE-----------AGAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 351 LLERYGMTEIGMALSNPLTE---ARVPGSVGTPLPGVEVRIISENpqkgspyiihaEGNErgtkVTPGfeeKEGELLVRG 427
Cdd:pfam00501 305 LVNGYGLTETTGVVTTPLPLdedLRSLGSVGRPLPGTEVKIVDDE-----------TGEP----VPPG---EPGELCVRG 366
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1720427507 428 PSVFREYWDKPEETKSAFTSDGWFRTGDTAVF-KDARYWIRGRTSvDIIKTG 478
Cdd:pfam00501 367 PGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRdEDGYLEIVGRKK-DQIKLG 417
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
40-577 |
8.08e-91 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 290.75 E-value: 8.08e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 40 TDGS-VPVFIRALA-FGDRIALiDKYGHH-TYRELyDRSLCLAQEICRLQGCKVGDlqeeRVSFLCSNDVSYVVAQWASW 116
Cdd:PRK05605 30 GDTTlVDLYDNAVArFGDRPAL-DFFGATtTYAEL-GKQVRRAAAGLRALGVRPGD----RVAIVLPNCPQHIVAFYAVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 117 MSGGVAV---PLYWKHpeaQLEYFIQDSRSSLVVV---GQEYLERLS-----------------PLAQRLG----VPLLP 169
Cdd:PRK05605 104 RLGAVVVehnPLYTAH---ELEHPFEDHGARVAIVwdkVAPTVERLRrttpletivsvnmiaamPLLQRLAlrlpIPALR 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 170 LTPAVYHGATEK--PTEQPVEESGWRDRG------------AMIFYTSGTTGRPKGALSTHRNLAAvvtGLVHSWAWT-- 233
Cdd:PRK05605 181 KARAALTGPAPGtvPWETLVDAAIGGDGSdvshprptpddvALILYTSGTTGKPKGAQLTHRNLFA---NAAQGKAWVpg 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 234 ---KNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSAQQVWeKFLSSEAPqiTVFMAVPTVYSKLLDYYDKHftq 310
Cdd:PRK05605 258 lgdGPERVLAALPMFHAYGLTLCLTLAVSIGGELVLLPAPDIDLIL-DAMKKHPP--TWLPGVPPLYEKIAEAAEER--- 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 311 phvqdfvrAVCKERIRLMVSGSAALPVPLLEKWRSATGHTLLERYGMTEIG-MALSNPLTEARVPGSVGTPLPGVEVRII 389
Cdd:PRK05605 332 --------GVDLSGVRNAFSGAMALPVSTVELWEKLTGGLLVEGYGLTETSpIIVGNPMSDDRRPGYVGVPFPDTEVRIV 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 390 S-ENPQKGSPyiihaegnergtkvtPGfeeKEGELLVRGPSVFREYWDKPEETKSAFTsDGWFRTGDTAVFkDARYWIRg 468
Cdd:PRK05605 404 DpEDPDETMP---------------DG---EEGELLVRGPQVFKGYWNRPEETAKSFL-DGWFRTGDVVVM-EEDGFIR- 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 469 rtSVDIIK----TGGYKVSALEIERHLLAHPSITDVAVIGVPDMTWGQRVTAVVALQEGHSLSHGDLKEWARGVLAPYAV 544
Cdd:PRK05605 463 --IVDRIKeliiTGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPGAALDPEGLRAYCREHLTRYKV 540
|
570 580 590
....*....|....*....|....*....|...
gi 1720427507 545 PSELLLVEEIPRNQMGKVNKKELLKQLYPSGQR 577
Cdd:PRK05605 541 PRRFYHVDELPRDQLGKVRRREVREELLEKLGA 573
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
54-568 |
6.05e-90 |
|
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: 286.57 E-value: 6.05e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 54 GDRIALIDKYGHHTYRELYDRSLCLAQEICRLqgckvGDLQEERVSFLCSNDVSYVVAQWASWMSGGVAVPLYWKHPEAQ 133
Cdd:cd05959 18 GDKTAFIDDAGSLTYAELEAEARRVAGALRAL-----GVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 134 LEYFIQDSRSSLVVVGQEYLERLSPLAQRLGVPLLPL--------TPAVYHGATEKPTEQPVEESG--WRDRGAMIFYTS 203
Cdd:cd05959 93 YAYYLEDSRARVVVVSGELAPVLAAALTKSEHTLVVLivsggagpEAGALLLAELVAAEAEQLKPAatHADDPAFWLYSS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 204 GTTGRPKGALSTHRNLAAV-------VTGLvhswawTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSAQQVW 276
Cdd:cd05959 173 GSTGRPKGVVHLHADIYWTaelyarnVLGI------REDDVCFSAAKLFFAYGLGNSLTFPLSVGATTVLMPERPTPAAV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 277 EKFLSSEAPqiTVFMAVPTVYSKLLDYYDkhftqPHVQDFVravckeRIRLMVSGSAALPVPLLEKWRSATGHTLLERYG 356
Cdd:cd05959 247 FKRIRRYRP--TVFFGVPTLYAAMLAAPN-----LPSRDLS------SLRLCVSAGEALPAEVGERWKARFGLDILDGIG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 357 MTEIG-MALSNpLTEARVPGSVGTPLPGVEVRIIsenpqkgspyiihaegNERGTKVTPGfeeKEGELLVRGPSVFREYW 435
Cdd:cd05959 314 STEMLhIFLSN-RPGRVRYGTTGKPVPGYEVELR----------------DEDGGDVADG---EPGELYVRGPSSATMYW 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 436 DKPEETKSAFTSdGWFRTGDTAVFK-DARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSITDVAVIGVPDMTWGQRV 514
Cdd:cd05959 374 NNRDKTRDTFQG-EWTRTGDKYVRDdDGFYTYAGRAD-DMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKP 451
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720427507 515 TAVVAL---QEGHSLSHGDLKEWARGVLAPYAVPSELLLVEEIPRNQMGKVNKKELL 568
Cdd:cd05959 452 KAFVVLrpgYEDSEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
54-571 |
1.14e-85 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 276.99 E-value: 1.14e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 54 GDRIALI--DKYGHH---TYRELYDRSlclaqeiCRL------QGCKVGDlqeeRVSFLCSNDVSYVVAQWASWMSGGVA 122
Cdd:COG0365 23 GDKVALIweGEDGEErtlTYAELRREV-------NRFanalraLGVKKGD----RVAIYLPNIPEAVIAMLACARIGAVH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 123 VPLYwkH---PEAqLEYFIQDSRSSLVVVGQEY----------------LERLSPLAQRLGVPLLPLTPAV-----YHGA 178
Cdd:COG0365 92 SPVF--PgfgAEA-LADRIEDAEAKVLITADGGlrggkvidlkekvdeaLEELPSLEHVIVVGRTGADVPMegdldWDEL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 179 TEKPTEQPVEESGWRDRGAMIFYTSGTTGRPKGALSTHRN-LAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCP 257
Cdd:COG0365 169 LAAASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGyLVHAATTAKYVLDLKPGDVFWCTADIGWATGHSYIVYGP 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 258 LWVGATCVML---PEF-SAQQVW---EKFlsseapQITVFMAVPTVYSKLLDYYDKHFTQPhvqDFVRavckerIRLMVS 330
Cdd:COG0365 249 LLNGATVVLYegrPDFpDPGRLWeliEKY------GVTVFFTAPTAIRALMKAGDEPLKKY---DLSS------LRLLGS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 331 GSAALPVPLLEKWRSATGHTLLERYGMTEIGMA-LSNPLTEARVPGSVGTPLPGVEVRIISEnpqkgspyiihaEGNErg 409
Cdd:COG0365 314 AGEPLNPEVWEWWYEAVGVPIVDGWGQTETGGIfISNLPGLPVKPGSMGKPVPGYDVAVVDE------------DGNP-- 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 410 tkVTPGfeeKEGELLVRG--PSVFREYWDKPEETKSAF--TSDGWFRTGDTAVfKDAR--YWIRGRTSvDIIKTGGYKVS 483
Cdd:COG0365 380 --VPPG---EEGELVIKGpwPGMFRGYWNDPERYRETYfgRFPGWYRTGDGAR-RDEDgyFWILGRSD-DVINVSGHRIG 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 484 ALEIERHLLAHPSITDVAVIGVPDMTWGQRVTAVVALQEGHSLS---HGDLKEWARGVLAPYAVPSELLLVEEIPRNQMG 560
Cdd:COG0365 453 TAEIESALVSHPAVAEAAVVGVPDEIRGQVVKAFVVLKPGVEPSdelAKELQAHVREELGPYAYPREIEFVDELPKTRSG 532
|
570
....*....|.
gi 1720427507 561 KVNKKELLKQL 571
Cdd:COG0365 533 KIMRRLLRKIA 543
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
67-563 |
1.52e-83 |
|
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: 269.08 E-value: 1.52e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 67 TYRELYDRSLCLAqeiCRLQgcKVGDLQEERVSFLCSNDVSYVVAQWASWMSGGVAVPLYWKHPEAQLEYFIQDSRSSLV 146
Cdd:cd05911 12 TYAQLRTLSRRLA---AGLR--KLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 147 VVGQEYLERLSPLAQRLG----VPLLPLTPAvYHGATEKPTEQPVEESGWR---------DRGAMIFYTSGTTGRPKGAL 213
Cdd:cd05911 87 FTDPDGLEKVKEAAKELGpkdkIIVLDDKPD-GVLSIEDLLSPTLGEEDEDlppplkdgkDDTAAILYSSGTTGLPKGVC 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 214 STHRNLAAVV--TGLVHSWAWTKNDVILHVLPLHHVHGVvNKLLCPLWVGATCVMLPEFSAqqvwEKFLSS-EAPQITVF 290
Cdd:cd05911 166 LSHRNLIANLsqVQTFLYGNDGSNDVILGFLPLYHIYGL-FTTLASLLNGATVIIMPKFDS----ELFLDLiEKYKITFL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 291 MAVPTVYSKLLDY--YDKHftqphvqDFvravckERIRLMVSGSAALP---VPLLEKWRSATghTLLERYGMTEIGMALS 365
Cdd:cd05911 241 YLVPPIAAALAKSplLDKY-------DL------SSLRVILSGGAPLSkelQELLAKRFPNA--TIKQGYGMTETGGILT 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 366 -NPLTEArVPGSVGTPLPGVEVRIISENPQKGSPYiihaegNERGtkvtpgfeekegELLVRGPSVFREYWDKPEETKSA 444
Cdd:cd05911 306 vNPDGDD-KPGSVGRLLPNVEAKIVDDDGKDSLGP------NEPG------------EICVRGPQVMKGYYNNPEATKET 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 445 FTSDGWFRTGDTAVF-KDARYWIRGRtSVDIIKTGGYKVSALEIERHLLAHPSITDVAVIGVPDMTWGQRVTAVVALQEG 523
Cdd:cd05911 367 FDEDGWLHTGDIGYFdEDGYLYIVDR-KKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPG 445
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1720427507 524 HSLSHGDLKEWARGVLAPYavpSEL----LLVEEIPRNQMGKVN 563
Cdd:cd05911 446 EKLTEKEVKDYVAKKVASY---KQLrggvVFVDEIPKSASGKIL 486
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
65-567 |
3.15e-79 |
|
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: 256.06 E-value: 3.15e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 65 HHTYRELYDRSLCLAQEICRLqGCKVGDlqeeRVSFLCSNDVSYVVAQWASWMSGGVAVPLYWKHPEAQLEYFIQDSRSS 144
Cdd:cd05934 3 RWTYAELLRESARIAAALAAL-GIRPGD----RVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 145 LVVVgqeylerlSPlaqrlgvpllpltpavyhgatekpteqpveesgwrdrgAMIFYTSGTTGRPKGALSTHRNLAAVVT 224
Cdd:cd05934 78 LVVV--------DP--------------------------------------ASILYTSGTTGPPKGVVITHANLTFAGY 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 225 GLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSAQQVWEKFLSSEApqiTVFMAVPTVYSKLLDyy 304
Cdd:cd05934 112 YSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLPRFSASRFWSDVRRYGA---TVTNYLGAMLSYLLA-- 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 305 dkhfTQPHVQDfvravCKERIRlmVSGSAALPVPLLEKWRSATGHTLLERYGMTEIGMALSNPLTEARVPGSVGTPLPGV 384
Cdd:cd05934 187 ----QPPSPDD-----RAHRLR--AAYGAPNPPELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGY 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 385 EVRIISENPQKgspyiihaegNERGTKvtpgfeekeGELLVR---GPSVFREYWDKPEETKSAFtSDGWFRTGDTAVFkD 461
Cdd:cd05934 256 EVRIVDDDGQE----------LPAGEP---------GELVIRglrGWGFFKGYYNMPEATAEAM-RNGWFHTGDLGYR-D 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 462 ARYWIR--GRTSvDIIKTGGYKVSALEIERHLLAHPSITDVAVIGVPDMTWGQRVTAVVALQEGHSLSHGDLKEWARGVL 539
Cdd:cd05934 315 ADGFFYfvDRKK-DMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPEELFAFCEGQL 393
|
490 500
....*....|....*....|....*...
gi 1720427507 540 APYAVPSELLLVEEIPRNQMGKVNKKEL 567
Cdd:cd05934 394 AYFKVPRYIRFVDDLPKTPTEKVAKAQL 421
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
48-567 |
1.20e-78 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 258.35 E-value: 1.20e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 48 IRALAFGDRIALIdKYGHH-TYRELYDRSLCLAQEICRLQGCKVGDlqeeRVSFLCSNDVSYVVAQWASWMSGGVAVPLY 126
Cdd:PRK08314 18 VSARRYPDKTAIV-FYGRAiSYRELLEEAERLAGYLQQECGVRKGD----RVLLYMQNSPQFVIAYYAILRANAVVVPVN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 127 WKHPEAQLEYFIQDSRSSLVVVGQEYLERLSPLAQRLGVP---------LLPLTP--AVYHGATEKPTEQPVEESGW--- 192
Cdd:PRK08314 93 PMNREEELAHYVTDSGARVAIVGSELAPKVAPAVGNLRLRhvivaqysdYLPAEPeiAVPAWLRAEPPLQALAPGGVvaw 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 193 ----------------RDRGAMIFYTSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLC 256
Cdd:PRK08314 173 kealaaglappphtagPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPLFHVTGMVHSMNA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 257 PLWVGATCVMLPEfsaqqvWEKFLSSEA---PQITVFMAVPTVyskLLDYydkhFTQPHVQDFvravCKERIRLMVSGSA 333
Cdd:PRK08314 253 PIYAGATVVLMPR------WDREAAARLierYRVTHWTNIPTM---VVDF----LASPGLAER----DLSSLRYIGGGGA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 334 ALPVPLLEKWRSATGHTLLERYGMTE-IGMALSNPLTEARvPGSVGTPLPGVEVRIIseNPqkgspyiihaegnERGTKV 412
Cdd:PRK08314 316 AMPEAVAERLKELTGLDYVEGYGLTEtMAQTHSNPPDRPK-LQCLGIPTFGVDARVI--DP-------------ETLEEL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 413 TPGfeeKEGELLVRGPSVFREYWDKPEETKSAF-TSDG--WFRTGDTA-VFKDARYWIRGRTSvDIIKTGGYKVSALEIE 488
Cdd:PRK08314 380 PPG---EVGEIVVHGPQVFKGYWNRPEATAEAFiEIDGkrFFRTGDLGrMDEEGYFFITDRLK-RMINASGFKVWPAEVE 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 489 RHLLAHPSITDVAVIGVPDMTWGQRVTAVVALQEGH--SLSHGDLKEWARGVLAPYAVPSELLLVEEIPRNQMGKVNKKE 566
Cdd:PRK08314 456 NLLYKHPAIQEACVIATPDPRRGETVKAVVVLRPEArgKTTEEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQ 535
|
.
gi 1720427507 567 L 567
Cdd:PRK08314 536 L 536
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
53-567 |
1.33e-77 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 254.86 E-value: 1.33e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 53 FGDRIALIDKYGHHTYRELYDRSLCLAQEICRLqGCKVGDlqeeRVSFLCSNDVSYVVAQWASWMSGGVAVPLYWKHPEA 132
Cdd:PRK08316 24 YPDKTALVFGDRSWTYAELDAAVNRVAAALLDL-GLKKGD----RVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 133 QLEYFIQDSRSSLVVVGQEYLERLSPLAQRLGVPLLPLTPAVYHGATEKP--------TEQPVEESGWRDRG---AMIFY 201
Cdd:PRK08316 99 ELAYILDHSGARAFLVDPALAPTAEAALALLPVDTLILSLVLGGREAPGGwldfadwaEAGSVAEPDVELADddlAQILY 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 202 TSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSAQQVWEKFls 281
Cdd:PRK08316 179 TSGTESLPKGAMLTHRALIAEYVSCIVAGDMSADDIPLHALPLYHCAQLDVFLGPYLYVGATNVILDAPDPELILRTI-- 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 282 sEAPQITVFMAVPTVYSKLLDYYDkhFTQPHVQDFVRAVckerirlmvSGSAALPVPLLEKwrsatghtLLER------- 354
Cdd:PRK08316 257 -EAERITSFFAPPTVWISLLRHPD--FDTRDLSSLRKGY---------YGASIMPVEVLKE--------LRERlpglrfy 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 355 --YGMTEIG---MALsNPLTEARVPGSVGTPLPGVEVRIIsenpqkgspyiihaegNERGTKVTPGfeeKEGELLVRGPS 429
Cdd:PRK08316 317 ncYGQTEIAplaTVL-GPEEHLRRPGSAGRPVLNVETRVV----------------DDDGNDVAPG---EVGEIVHRSPQ 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 430 VFREYWDKPEETKSAFtSDGWFRTGDTAVFKDARY-WIRGRTSvDIIKTGGYKVSALEIERHLLAHPSITDVAVIGVPDM 508
Cdd:PRK08316 377 LMLGYWDDPEKTAEAF-RGGWFHSGDLGVMDEEGYiTVVDRKK-DMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDP 454
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720427507 509 TWGQRVTAVVALQEGHSLSHGDLKEWARGVLAPYAVPSELLLVEEIPRNQMGKVNKKEL 567
Cdd:PRK08316 455 KWIEAVTAVVVPKAGATVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKREL 513
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
33-565 |
6.32e-76 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 252.33 E-value: 6.32e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 33 PTTPEAHTDGSVP--VFIRALAFGDRIALIDKYGH----HTYRELYDRSLCLAQEICRLqGCKVGDlqeeRVSFLCSNDV 106
Cdd:COG1022 2 SEFSDVPPADTLPdlLRRRAARFPDRVALREKEDGiwqsLTWAEFAERVRALAAGLLAL-GVKPGD----RVAILSDNRP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 107 SYVVAQWASWMSGGVAVPLYWKHPEAQLEYFIQDSRSSLVVVG-QEYLERLSPLAQRLgvpllpltPAVYH-------GA 178
Cdd:COG1022 77 EWVIADLAILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEdQEQLDKLLEVRDEL--------PSLRHivvldprGL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 179 TEKPTEQPVEEsgWRDRG---------------------AMIFYTSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDV 237
Cdd:COG1022 149 RDDPRLLSLDE--LLALGrevadpaelearraavkpddlATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDR 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 238 ILHVLPLHHVHGVVNKLLCpLWVGATCVMLPefSAQQVWEKfLSSEAPqiTVFMAVPTVYSKLLD--------------- 302
Cdd:COG1022 227 TLSFLPLAHVFERTVSYYA-LAAGATVAFAE--SPDTLAED-LREVKP--TFMLAVPRVWEKVYAgiqakaeeagglkrk 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 303 -----------YYDKHFTQPHVQDF---------------VRAVCKERIRLMVSGSAALPVPLLEKWRSAtGHTLLERYG 356
Cdd:COG1022 301 lfrwalavgrrYARARLAGKSPSLLlrlkhaladklvfskLREALGGRLRFAVSGGAALGPELARFFRAL-GIPVLEGYG 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 357 MTEI-GMALSNPLTEARvPGSVGTPLPGVEVRIisenpqkgspyiihAEgnergtkvtpgfeekEGELLVRGPSVFREYW 435
Cdd:COG1022 380 LTETsPVITVNRPGDNR-IGTVGPPLPGVEVKI--------------AE---------------DGEILVRGPNVMKGYY 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 436 DKPEETKSAFTSDGWFRTGDTAVFKDARY-WIRGRTSvDIIKT-GGYKVSALEIERHLLAHPSITDVAVIGvpDmtwgQR 513
Cdd:COG1022 430 KNPEATAEAFDADGWLHTGDIGELDEDGFlRITGRKK-DLIVTsGGKNVAPQPIENALKASPLIEQAVVVG--D----GR 502
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 514 --VTAVVALQEGHslshgdLKEWA--RGVlaPYAVPSELL----LVEEIpRNQMGKVNKK 565
Cdd:COG1022 503 pfLAALIVPDFEA------LGEWAeeNGL--PYTSYAELAqdpeVRALI-QEEVDRANAG 553
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
67-567 |
2.83e-75 |
|
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: 245.85 E-value: 2.83e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 67 TYRELYDRSLCLAQEICRlQGCKVGDlqeeRVSFLCSNDVSYVVAQWASWMSGGVAVPLYWKHPEAQLEYFIQDSRSSLV 146
Cdd:cd05935 3 TYLELLEVVKKLASFLSN-KGVRKGD----RVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 147 VVGQEyLERLsplaqrlgvpllpltpavyhgatekpteqpveesgwrdrgAMIFYTSGTTGRPKGALSTHRNLAAVVTGL 226
Cdd:cd05935 78 VVGSE-LDDL----------------------------------------ALIPYTSGTTGLPKGCMHTHFSAAANALQS 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 227 VHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSAQQVWEKFlssEAPQITVFMAVPTVYSKLLdyydk 306
Cdd:cd05935 117 AVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARWDRETALELI---EKYKVTFWTNIPTMLVDLL----- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 307 hfTQPHVQDFvravCKERIRLMVSGSAALPVPLLEKWRSATGHTLLERYGMTE-IGMALSNPLTEARVPgSVGTPLPGVE 385
Cdd:cd05935 189 --ATPEFKTR----DLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTEtMSQTHTNPPLRPKLQ-CLGIP*FGVD 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 386 VRIISEnpqkgspyiihaegnERGTKVTPGfeeKEGELLVRGPSVFREYWDKPEETKSAFTSDG---WFRTGDTAVFKDA 462
Cdd:cd05935 262 ARVIDI---------------ETGRELPPN---EVGEIVVRGPQIFKGYWNRPEETEESFIEIKgrrFFRTGDLGYMDEE 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 463 RYWIRGRTSVDIIKTGGYKVSALEIERHLLAHPSITDVAVIGVPDMTWGQRVTAVVALQEGH--SLSHGDLKEWARGVLA 540
Cdd:cd05935 324 GYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYrgKVTEEDIIEWAREQMA 403
|
490 500
....*....|....*....|....*..
gi 1720427507 541 PYAVPSELLLVEEIPRNQMGKVNKKEL 567
Cdd:cd05935 404 AYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
32-567 |
4.11e-74 |
|
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: 245.22 E-value: 4.11e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 32 LPTTPEAHtdgsVPVFIRALAFGDRIALIDKYG--HHTYRELYDRSLCLAQEICRLQGCKvGDLqeerVSFLCSNDVSYV 109
Cdd:cd05904 1 LPTDLPLD----SVSFLFASAHPSRPALIDAATgrALTYAELERRVRRLAAGLAKRGGRK-GDV----VLLLSPNSIEFP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 110 VAQWASwMSGGVAV----PLYwkhPEAQLEYFIQDSRSSLVVVGQEYLERLSPLAQRLGV---PLLPLTPAVYHGATEKP 182
Cdd:cd05904 72 VAFLAV-LSLGAVVttanPLS---TPAEIAKQVKDSGAKLAFTTAELAEKLASLALPVVLldsAEFDSLSFSDLLFEADE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 183 TEQPVEESGwRDRGAMIFYTSGTTGRPKGALSTHRNLAAVVTGLVHSWAWT--KNDVILHVLPLHHVHGVVNKLLCPLWV 260
Cdd:cd05904 148 AEPPVVVIK-QDDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEGSNsdSEDVFLCVLPMFHIYGLSSFALGLLRL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 261 GATCVMLPEFSAqqvwEKFLSS-EAPQITVFMAVPTVYSKLLDyydkhftQPHVQDFVRAvckeRIRLMVSGSAALPVPL 339
Cdd:cd05904 227 GATVVVMPRFDL----EELLAAiERYKVTHLPVVPPIVLALVK-------SPIVDKYDLS----SLRQIMSGAAPLGKEL 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 340 LEKWRSATGHT-LLERYGMTE---IGMALSNPLTEARVPGSVGTPLPGVEVRIIseNPQKGSPyiihaegnergtkVTPG 415
Cdd:cd05904 292 IEAFRAKFPNVdLGQGYGMTEstgVVAMCFAPEKDRAKYGSVGRLVPNVEAKIV--DPETGES-------------LPPN 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 416 feeKEGELLVRGPSVFREYWDKPEETKSAFTSDGWFRTGDTAVFKDARY-WIRGRTSvDIIKTGGYKVSALEIERHLLAH 494
Cdd:cd05904 357 ---QTGELWIRGPSIMKGYLNNPEATAATIDKEGWLHTGDLCYIDEDGYlFIVDRLK-ELIKYKGFQVAPAELEALLLSH 432
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720427507 495 PSITDVAVIGVPDMTWGQRVTAVVALQEGHSLSHGDLKEWARGVLAPYAVPSELLLVEEIPRNQMGKVNKKEL 567
Cdd:cd05904 433 PEILDAAVIPYPDEEAGEVPMAFVVRKPGSSLTEDEIMDFVAKQVAPYKKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
67-567 |
1.18e-73 |
|
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: 241.90 E-value: 1.18e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 67 TYRELYDRSLCLAQEICRLqGCKVGDlqeeRVSFLCSNDVSYVVAQWASWMSGGVAVPLYWKHPEAQLEYFIQDSRSSLV 146
Cdd:cd05903 3 TYSELDTRADRLAAGLAAL-GVGPGD----VVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 147 VVGQEYLERlsplaqrlgvpllpltpavyhgateKPTEQPveesgwrDRGAMIFYTSGTTGRPKGALSTHRNLAAVVTGL 226
Cdd:cd05903 78 VVPERFRQF-------------------------DPAAMP-------DAVALLLFTSGTTGEPKGVMHSHNTLSASIRQY 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 227 VHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSAQQVWEkFLSSEapQITVFMAVPTVYSKLLDyydk 306
Cdd:cd05903 126 AERLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIWDPDKALA-LMREH--GVTFMMGATPFLTDLLN---- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 307 hftqpHVQDFVRAVCkeRIRLMVSGSAALPVPLLEKWRSATGHTLLERYGMTEIGMALSN--PLTEARVPGSVGTPLPGV 384
Cdd:cd05903 199 -----AVEEAGEPLS--RLRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECPGAVTSitPAPEDRRLYTDGRPLPGV 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 385 EVRIIsenpqkgspyiihaegNERGTKVTPGfeeKEGELLVRGPSVFREYWDKPEETKSAFtSDGWFRTGDTAVFKDARY 464
Cdd:cd05903 272 EIKVV----------------DDTGATLAPG---VEGELLSRGPSVFLGYLDRPDLTADAA-PEGWFRTGDLARLDEDGY 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 465 W-IRGRTSvDIIKTGGYKVSALEIERHLLAHPSITDVAVIGVPDMTWGQRVTAVVALQEGHSLSHGDLKEWARGV-LAPY 542
Cdd:cd05903 332 LrITGRSK-DIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGALLTFDELVAYLDRQgVAKQ 410
|
490 500
....*....|....*....|....*
gi 1720427507 543 AVPSELLLVEEIPRNQMGKVNKKEL 567
Cdd:cd05903 411 YWPERLVHVDDLPRTPSGKVQKFRL 435
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
49-571 |
3.92e-73 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 242.07 E-value: 3.92e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 49 RALAFGDRIALIDKYGHHTYRELYDRSLCLAQEICRLQGCKVGDlqeeRVSFLCSNDVSYVVAQWASWMSGGVAVPLYWK 128
Cdd:PRK06839 11 RAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIYELNVKKGE----RIAILSQNSLEYIVLLFAIAKVECIAVPLNIR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 129 HPEAQLEYFIQDSRSSLVVVGQEYLERLSPLAQRLGV-PLLPLTpavyhGATEKPTEQPVE-ESGWRDRGAMIFYTSGTT 206
Cdd:PRK06839 87 LTENELIFQLKDSGTTVLFVEKTFQNMALSMQKVSYVqRVISIT-----SLKEIEDRKIDNfVEKNESASFIICYTSGTT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 207 GRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVvNKLLCPLWVGATCVMLP-EFSAQQVWEKFlssEAP 285
Cdd:PRK06839 162 GKPKGAVLTQENMFWNALNNTFAIDLTMHDRSIVLLPLFHIGGI-GLFAFPTLFAGGVIIVPrKFEPTKALSMI---EKH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 286 QITVFMAVPTVYSKLLDYYDkhFTQPHVQDfvravckerIRLMVSGSAALPVPLLEKWRSaTGHTLLERYGMTEIGMALS 365
Cdd:PRK06839 238 KVTVVMGVPTIHQALINCSK--FETTNLQS---------VRWFYNGGAPCPEELMREFID-RGFLFGQGFGMTETSPTVF 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 366 NPLTE--ARVPGSVGTPLPGVEVRIISENpqkgspyiihaegnerGTKVTPGfeeKEGELLVRGPSVFREYWDKPEETKS 443
Cdd:PRK06839 306 MLSEEdaRRKVGSIGKPVLFCDYELIDEN----------------KNKVEVG---EVGELLIRGPNVMKEYWNRPDATEE 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 444 AFtSDGWFRTGDTAVF-KDARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSITDVAVIGVPDMTWGQRVTAVVALQE 522
Cdd:PRK06839 367 TI-QDGWLCTGDLARVdEDGFVYIVGRKK-EMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKS 444
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1720427507 523 GHSLSHGDLKEWARGVLAPYAVPSELLLVEEIPRNQMGKVNKKELLKQL 571
Cdd:PRK06839 445 SSVLIEKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVNQL 493
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
33-567 |
7.04e-72 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 239.50 E-value: 7.04e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 33 PTTPEAHTDGSVP-VFIRALA-FGDRIALIDKYGHHTYRELYDRSLCLAQEICRLqGCKVGDlqeeRVSFLCSNDVSYVV 110
Cdd:PRK06188 3 TMADLLHSGATYGhLLVSALKrYPDRPALVLGDTRLTYGQLADRISRYIQAFEAL-GLGTGD----AVALLSLNRPEVLM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 111 AQWASWMSGGVAVPLywkHPEAQLE---YFIQDSR-SSLVVVGQEYLERLSPLAQRlgVP----LLPLTPAVYH----GA 178
Cdd:PRK06188 78 AIGAAQLAGLRRTAL---HPLGSLDdhaYVLEDAGiSTLIVDPAPFVERALALLAR--VPslkhVLTLGPVPDGvdllAA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 179 TEKPTEQPVEESGWRDRGAMIFYTSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVvnKLLCPL 258
Cdd:PRK06188 153 AAKFGPAPLVAAALPPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSHAGGA--FFLPTL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 259 WVGATCVMLPEFSAqqvwEKFLSS-EAPQITVFMAVPTVYSKLLDYYDkhftqPHVQDFvravckERIRLMVSGSAAL-P 336
Cdd:PRK06188 231 LRGGTVIVLAKFDP----AEVLRAiEEQRITATFLVPTMIYALLDHPD-----LRTRDL------SSLETVYYGASPMsP 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 337 VPLLEKWRsATGHTLLERYGMTEIGMALS------NPLTEARVPGSVGTPLPGVEVRIISENpqkgspyiihaeGNErgt 410
Cdd:PRK06188 296 VRLAEAIE-RFGPIFAQYYGQTEAPMVITylrkrdHDPDDPKRLTSCGRPTPGLRVALLDED------------GRE--- 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 411 kVTPGfeeKEGELLVRGPSVFREYWDKPEETKSAFtSDGWFRTGDTAVfKDAR--YWIRGRTSvDIIKTGGYKVSALEIE 488
Cdd:PRK06188 360 -VAQG---EVGEICVRGPLVMDGYWNRPEETAEAF-RDGWLHTGDVAR-EDEDgfYYIVDRKK-DMIVTGGFNVFPREVE 432
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720427507 489 RHLLAHPSITDVAVIGVPDMTWGQRVTAVVALQEGHSLSHGDLKEWARGVLAPYAVPSELLLVEEIPRNQMGKVNKKEL 567
Cdd:PRK06188 433 DVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPGAAVDAAELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKAL 511
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
67-565 |
4.93e-68 |
|
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341233 [Multi-domain] Cd Length: 452 Bit Score: 227.48 E-value: 4.93e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 67 TYRELYDRSLCLAQEIcRLQGCKVGDlqeeRVSFLCSNDVSYVVAQWASWMSGGVAVPLYWKHPEAQLEYFIQDSRSSLV 146
Cdd:cd05907 7 TWAEFAEEVRALAKGL-IALGVEPGD----RVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 147 VVgqeylerlsplaqrlgvpllpltpavyhgatEKPTEQpveesgwrdrgAMIFYTSGTTGRPKGALSTHRNLAAVVTGL 226
Cdd:cd05907 82 FV-------------------------------EDPDDL-----------ATIIYTSGTTGRPKGVMLSHRNILSNALAL 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 227 VHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEfsaqqvwEKFLSSEAPQI--TVFMAVPTVYsklldyy 304
Cdd:cd05907 120 AERLPATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFASS-------AETLLDDLSEVrpTVFLAVPRVW------- 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 305 DKHFTQPHVQD--------FVRAVcKERIRLMVSGSAALPVPLLEKWRSAtGHTLLERYGMTEIGMALSNPLTEARVPGS 376
Cdd:cd05907 186 EKVYAAIKVKAvpglkrklFDLAV-GGRLRFAASGGAPLPAELLHFFRAL-GIPVYEGYGLTETSAVVTLNPPGDNRIGT 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 377 VGTPLPGVEVRIisenpqkgspyiihAEgnergtkvtpgfeekEGELLVRGPSVFREYWDKPEETKSAFTSDGWFRTGDT 456
Cdd:cd05907 264 VGKPLPGVEVRI--------------AD---------------DGEILVRGPNVMLGYYKNPEATAEALDADGWLHTGDL 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 457 AVFK-DARYWIRGRtSVDIIKT-GGYKVSALEIERHLLAHPSITDVAVIGvpDmtwgQR--VTAVVALQEghslshGDLK 532
Cdd:cd05907 315 GEIDeDGFLHITGR-KKDLIITsGGKNISPEPIENALKASPLISQAVVIG--D----GRpfLVALIVPDP------EALE 381
|
490 500 510
....*....|....*....|....*....|....*..
gi 1720427507 533 EWARGVLAPYAVPSELL----LVEEIpRNQMGKVNKK 565
Cdd:cd05907 382 AWAEEHGIAYTDVAELAanpaVRAEI-EAAVEAANAR 417
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
49-571 |
7.72e-68 |
|
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: 229.26 E-value: 7.72e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 49 RALAFGDRIALIDKYGHHTYRELYDRSLCLAQEICRLqGCKVGDlqeeRVSFLCSNDVSYVVAQWASWMSGgvAVPLY-- 126
Cdd:COG1021 34 RAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLAL-GLRPGD----RVVVQLPNVAEFVIVFFALFRAG--AIPVFal 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 127 WKHPEAQLEYFIQDSRSSLVVVGQEYLE-RLSPLAQRL--GVPLLPLTpaVYHGATEKPT------EQPVEESGWR-DRG 196
Cdd:COG1021 107 PAHRRAEISHFAEQSEAVAYIIPDRHRGfDYRALARELqaEVPSLRHV--LVVGDAGEFTsldallAAPADLSEPRpDPD 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 197 AMIFY--TSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHH--------VHGVvnkllcpLWVGATCVM 266
Cdd:COG1021 185 DVAFFqlSGGTTGLPKLIPRTHDDYLYSVRASAEICGLDADTVYLAALPAAHnfplsspgVLGV-------LYAGGTVVL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 267 LPEFSAQQVwekFLSSEAPQITVFMAVPTVYSKLLDYYDKHFTQPhvqdfvravckERIRLMVSGSAALPVPLLEKWRSA 346
Cdd:COG1021 258 APDPSPDTA---FPLIERERVTVTALVPPLALLWLDAAERSRYDL-----------SSLRVLQVGGAKLSPELARRVRPA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 347 TGHTLLERYGMTEiGMALSNPL--TEARVPGSVGTPL-PGVEVRIISEnpqkgspyiihaEGNErgtkVTPGfeeKEGEL 423
Cdd:COG1021 324 LGCTLQQVFGMAE-GLVNYTRLddPEEVILTTQGRPIsPDDEVRIVDE------------DGNP----VPPG---EVGEL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 424 LVRGPSVFREYWDKPEETKSAFTSDGWFRTGDTAVFKDARY-WIRGRtSVDIIKTGGYKVSALEIERHLLAHPSITDVAV 502
Cdd:COG1021 384 LTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYlVVEGR-AKDQINRGGEKIAAEEVENLLLAHPAVHDAAV 462
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720427507 503 IGVPDMTWGQRVTAVVALQeGHSLSHGDLKEW--ARGVlAPYAVPSELLLVEEIPRNQMGKVNKKELLKQL 571
Cdd:COG1021 463 VAMPDEYLGERSCAFVVPR-GEPLTLAELRRFlrERGL-AAFKLPDRLEFVDALPLTAVGKIDKKALRAAL 531
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
67-569 |
1.08e-67 |
|
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: 225.68 E-value: 1.08e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 67 TYRELYDRSLCLAQEICRLqGCKVGDlqeeRVSFLCSNDVSYVVAQWASWMSGGVAVPLYWKHPEAQLEYFIQDSRSSLV 146
Cdd:cd05972 2 SFRELKRESAKAANVLAKL-GLRKGD----RVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 147 VVGQEYLerlsplaqrlgvpllpltpavyhgatekpteqpveesgwrdrgAMIFYTSGTTGRPKGALSTHRNL------A 220
Cdd:cd05972 77 VTDAEDP-------------------------------------------ALIYFTSGTTGLPKGVLHTHSYPlghiptA 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 221 AVVTGL--------VHSWAWTKndvilhvlplhhvhGVVNKLLCPLWVGATCVM--LPEFSAQQVWEKfLSSEapQITVF 290
Cdd:cd05972 114 AYWLGLrpddihwnIADPGWAK--------------GAWSSFFGPWLLGATVFVyeGPRFDAERILEL-LERY--GVTSF 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 291 MAVPTVYsklldyydKHFTQPHVQDFVRavckERIRLMVSGSAALPVPLLEKWRSATGHTLLERYGMTEIGMALSNPLTE 370
Cdd:cd05972 177 CGPPTAY--------RMLIKQDLSSYKF----SHLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDM 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 371 ARVPGSVGTPLPGVEVRIISEnpqkgspyiihaEGNErgtkVTPGfeeKEGELLVR--GPSVFREYWDKPEETKSAFtSD 448
Cdd:cd05972 245 PVKPGSMGRPTPGYDVAIIDD------------DGRE----LPPG---EEGDIAIKlpPPGLFLGYVGDPEKTEASI-RG 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 449 GWFRTGDTAVF-KDARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSITDVAVIGVPDMTWGQRVTAVVALQEGHSLS 527
Cdd:cd05972 305 DYYLTGDRAYRdEDGYFWFVGRAD-DIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPS 383
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1720427507 528 HG---DLKEWARGVLAPYAVPSELLLVEEIPRNQMGKVNKKELLK 569
Cdd:cd05972 384 EElaeELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRVELRD 428
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
65-567 |
9.11e-67 |
|
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: 225.97 E-value: 9.11e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 65 HHTYRELYDRSLCLAQEICRLqGCKVGDlqeeRVSFLCSNDVSYVVAQWASWMSGGVAVPLYWKHPEAQLEYFIQDSRSS 144
Cdd:cd12119 25 RYTYAEVAERARRLANALRRL-GVKPGD----RVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 145 LVVVGQEYLERLSPLAQRL------------GVPLLPLTPAVYHGATEKPTEQPVEEsgWRD----RGAMIFYTSGTTGR 208
Cdd:cd12119 100 VVFVDRDFLPLLEAIAPRLptvehvvvmtddAAMPEPAGVGVLAYEELLAAESPEYD--WPDfdenTAAAICYTSGTTGN 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 209 PKGALSTHRN--LAAVVTGLVHSWAWTKNDVILHVLPLHHVH--GVvnkllcP---LWVGATCV-----MLPEFSAQQVw 276
Cdd:cd12119 178 PKGVVYSHRSlvLHAMAALLTDGLGLSESDVVLPVVPMFHVNawGL------PyaaAMVGAKLVlpgpyLDPASLAELI- 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 277 ekflssEAPQITVFMAVPTVYSKLLDYYDKHftqPHVQDFVRAVckerirlmVSGSAALPVPLLEKWRSAtGHTLLERYG 356
Cdd:cd12119 251 ------EREGVTFAAGVPTVWQGLLDHLEAN---GRDLSSLRRV--------VIGGSAVPRSLIEAFEER-GVRVIHAWG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 357 MTEI-----------GMALSNPLTEARVPGSVGTPLPGVEVRIISENpqkgspyiihaegnergTKVTPGFEEKEGELLV 425
Cdd:cd12119 313 MTETsplgtvarppsEHSNLSEDEQLALRAKQGRPVPGVELRIVDDD-----------------GRELPWDGKAVGELQV 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 426 RGPSVFREYWdKPEETKSAFTSDGWFRTGDTAVFKDARYW-IRGRTSvDIIKTGGYKVSALEIERHLLAHPSITDVAVIG 504
Cdd:cd12119 376 RGPWVTKSYY-KNDEESEALTEDGWLRTGDVATIDEDGYLtITDRSK-DVIKSGGEWISSVELENAIMAHPAVAEAAVIG 453
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720427507 505 VPDMTWGQRVTAVVALQEGHSLSHGDLKEWARGVLAPYAVPSELLLVEEIPRNQMGKVNKKEL 567
Cdd:cd12119 454 VPHPKWGERPLAVVVLKEGATVTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
55-567 |
1.07e-66 |
|
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: 223.56 E-value: 1.07e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 55 DRIALIDKYGHHTYRELYDRSLCLAQeicRLQGCKVGdlQEERVSFLCSNDVSYVVAQWASWMSGGVAVPLYWKHPEAQL 134
Cdd:cd05930 2 DAVAVVDGDQSLTYAELDARANRLAR---YLRERGVG--PGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 135 EYFIQDSRSSLVVVGQEYLerlsplaqrlgvpllpltpavyhgatekpteqpveesgwrdrgAMIFYTSGTTGRPKGALS 214
Cdd:cd05930 77 AYILEDSGAKLVLTDPDDL-------------------------------------------AYVIYTSGSTGKPKGVMV 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 215 THRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVNkLLCPLWVGATCVMLPE---FSAQQVWEKFlssEAPQITVFM 291
Cdd:cd05930 114 EHRGLVNLLLWMQEAYPLTPGDRVLQFTSFSFDVSVWE-IFGALLAGATLVVLPEevrKDPEALADLL---AEEGITVLH 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 292 AVPTVYSKLLDYYDkhftqphvqdfvRAVCKeRIRLMVSGSAALPVPLLEKWRSA-TGHTLLERYGMTEIGMA------L 364
Cdd:cd05930 190 LTPSLLRLLLQELE------------LAALP-SLRLVLVGGEALPPDLVRRWRELlPGARLVNLYGPTEATVDatyyrvP 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 365 SNPLTEARVPgsVGTPLPGVEVRIIsenpqkgspyiihaegNERGTKVTPGfeeKEGELLVRGPSVFREYWDKPEETKSA 444
Cdd:cd05930 257 PDDEEDGRVP--IGRPIPNTRVYVL----------------DENLRPVPPG---VPGELYIGGAGLARGYLNRPELTAER 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 445 FTSDGWF------RTGDTAVFKDAR---YwiRGRTSvDIIKTGGYKVSALEIERHLLAHPSITDVAVIGVPDMTWGQRVT 515
Cdd:cd05930 316 FVPNPFGpgermyRTGDLVRWLPDGnleF--LGRID-DQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLV 392
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1720427507 516 AVVALQEGHSLSHGDLKEWARGVLAPYAVPSELLLVEEIPRNQMGKVNKKEL 567
Cdd:cd05930 393 AYVVPDEGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
67-581 |
7.73e-66 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 224.53 E-value: 7.73e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 67 TYRELYDRSLCLAQEICRLqGCKVGDlqeeRVSFLCSNDVSYVVAQWASWMSGGVAV---PLYwkhPEAQLEYFIQDSRS 143
Cdd:PRK06710 51 TFSVFHDKVKRFANYLQKL-GVEKGD----RVAIMLPNCPQAVIGYYGTLLAGGIVVqtnPLY---TERELEYQLHDSGA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 144 SLVVVGQEYLERLSPLAQRLGVP---------LLPLTPAVYHGATEKPTEQ---PVEESG----W------RDRG----- 196
Cdd:PRK06710 123 KVILCLDLVFPRVTNVQSATKIEhvivtriadFLPFPKNLLYPFVQKKQSNlvvKVSESEtihlWnsvekeVNTGvevpc 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 197 ------AMIFYTSGTTGRPKGALSTHRNLAAVVTGLVHswaWTKN-----DVILHVLPLHHVHGVVNKLLCPLWVGATCV 265
Cdd:PRK06710 203 dpendlALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQ---WLYNckegeEVVLGVLPFFHVYGMTAVMNLSIMQGYKMV 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 266 MLPEFSAQQVWEKFlssEAPQITVFMAVPTVYSKLLDyydkhftQPHVQDFVRAvckeRIRLMVSGSAALPVPLLEKWRS 345
Cdd:PRK06710 280 LIPKFDMKMVFEAI---KKHKVTLFPGAPTIYIALLN-------SPLLKEYDIS----SIRACISGSAPLPVEVQEKFET 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 346 ATGHTLLERYGMTEIG-MALSNPLTEARVPGSVGTPLPGVEVRIISEnpqkgspyiihaegnERGTKVTPGfeeKEGELL 424
Cdd:PRK06710 346 VTGGKLVEGYGLTESSpVTHSNFLWEKRVPGSIGVPWPDTEAMIMSL---------------ETGEALPPG---EIGEIV 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 425 VRGPSVFREYWDKPEETkSAFTSDGWFRTGDTAVF-KDARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSITDVAVI 503
Cdd:PRK06710 408 VKGPQIMKGYWNKPEET-AAVLQDGWLHTGDVGYMdEDGFFYVKDRKK-DMIVASGFNVYPREVEEVLYEHEKVQEVVTI 485
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720427507 504 GVPDMTWGQRVTAVVALQEGHSLSHGDLKEWARGVLAPYAVPSELLLVEEIPRNQMGKVNKKELLKQLYPSGQRSQPG 581
Cdd:PRK06710 486 GVPDPYRGETVKAFVVLKEGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVLIEEEKRKNEDEQTG 563
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
199-567 |
2.25e-64 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 214.45 E-value: 2.25e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 199 IFYTSGTTGRPKGALSTHRNLA--AVVTGlvHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVML-PEFSAQQV 275
Cdd:cd05917 7 IQFTSGTTGSPKGATLTHHNIVnnGYFIG--ERLGLTEQDRLCIPVPLFHCFGSVLGVLACLTHGATMVFPsPSFDPLAV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 276 wekFLSSEAPQITVFMAVPTVYSKLLDYYDKHFTQPHvqdfvravckeRIRLMVSGSAALPVPLLEKWRSATGHT-LLER 354
Cdd:cd05917 85 ---LEAIEKEKCTALHGVPTMFIAELEHPDFDKFDLS-----------SLRTGIMAGAPCPPELMKRVIEVMNMKdVTIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 355 YGMTE----IGMALSNPLTEARVpGSVGTPLPGVEVRIISEnpqkgspyiihaegnerGTKVTPGFEEKeGELLVRGPSV 430
Cdd:cd05917 151 YGMTEtspvSTQTRTDDSIEKRV-NTVGRIMPHTEAKIVDP-----------------EGGIVPPVGVP-GELCIRGYSV 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 431 FREYWDKPEETKSAFTSDGWFRTGDTAVF-KDARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSITDVAVIGVPDMT 509
Cdd:cd05917 212 MKGYWNDPEKTAEAIDGDGWLHTGDLAVMdEDGYCRIVGRIK-DMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDER 290
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720427507 510 WGQRVTAVVALQEGHSLSHGDLKEWARGVLAPYAVPSELLLVEEIPRNQMGKVNKKEL 567
Cdd:cd05917 291 YGEEVCAWIRLKEGAELTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKL 348
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
56-567 |
2.55e-64 |
|
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: 217.33 E-value: 2.55e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 56 RIALIDKYGHHTYRELYDRSLCLAQEICRLqgckvGDLQEERVSFLCSNDVSYVVAQWASWMSGGVAVPLYWKHPEAQLE 135
Cdd:cd05919 1 KTAFYAADRSVTYGQLHDGANRLGSALRNL-----GVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 136 YFIQDSRSSLVVVGQEYLerlsplaqrlgvpllpltpavyhgatekpteqpveesgwrdrgAMIFYTSGTTGRPKGALST 215
Cdd:cd05919 76 YIARDCEARLVVTSADDI-------------------------------------------AYLLYSSGTTGPPKGVMHA 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 216 HRNLAAVVTGL-VHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEF-SAQQVWEKfLSSEAPqiTVFMAV 293
Cdd:cd05919 113 HRDPLLFADAMaREALGLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGASAVLNPGWpTAERVLAT-LARFRP--TVLYGV 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 294 PTVYSKLLDYYDKHftqphvQDFVRAvckerIRLMVSGSAALPVPLLEKWRSATGHTLLERYGMTEIG-MALSNPLTEAR 372
Cdd:cd05919 190 PTFYANLLDSCAGS------PDALRS-----LRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVGhIFLSNRPGAWR 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 373 vPGSVGTPLPGVEVRIIsenpqkgspyiihaegNERGTKVTPGfeeKEGELLVRGPSVFREYWDKPEETKSAFtSDGWFR 452
Cdd:cd05919 259 -LGSTGRPVPGYEIRLV----------------DEEGHTIPPG---EEGDLLVRGPSAAVGYWNNPEKSRATF-NGGWYR 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 453 TGDTAVF-KDARYWIRGRtSVDIIKTGGYKVSALEIERHLLAHPSITDVAVIGVPDMTWGQRVTAVVALQEGHSLSHGDL 531
Cdd:cd05919 318 TGDKFCRdADGWYTHAGR-ADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQESLA 396
|
490 500 510
....*....|....*....|....*....|....*....
gi 1720427507 532 KEWARGV---LAPYAVPSELLLVEEIPRNQMGKVNKKEL 567
Cdd:cd05919 397 RDIHRHLlerLSAHKVPRRIAFVDELPRTATGKLQRFKL 435
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
55-573 |
2.49e-63 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 215.83 E-value: 2.49e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 55 DRIALIDKYGHH--TYRELyDRSLCLAQEICRLQGCKVGDlqeeRVSFLCSNDVSYVVAQWASWMSGGVAVPLYWKHPEA 132
Cdd:PRK09088 10 QRLAAVDLALGRrwTYAEL-DALVGRLAAVLRRRGCVDGE----RLAVLARNSVWLVALHFACARVGAIYVPLNWRLSAS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 133 QLEYFIQDSRSSLVVvGQEYLERLSPLaqrlGVPLLPLTPAV-YHGATEKPTEQPveesgwrDRGAMIFYTSGTTGRPKG 211
Cdd:PRK09088 85 ELDALLQDAEPRLLL-GDDAVAAGRTD----VEDLAAFIASAdALEPADTPSIPP-------ERVSLILFTSGTSGQPKG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 212 ALSTHRNLAAV-----VTGLVhswawTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSAQQVWeKFLSSEAPQ 286
Cdd:PRK09088 153 VMLSERNLQQTahnfgVLGRV-----DAHSSFLCDAPMFHIIGLITSVRPVLAVGGSILVSNGFEPKRTL-GRLGDPALG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 287 ITVFMAVPTVYSKLLDyydkhftQPhvqDFVRAVCKeRIRLMVSGSAALPVPLLEKWRsATGHTLLERYGMTEIGMALSN 366
Cdd:PRK09088 227 ITHYFCVPQMAQAFRA-------QP---GFDAAALR-HLTALFTGGAPHAAEDILGWL-DDGIPMVDGFGMSEAGTVFGM 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 367 PLTEARVP---GSVGTPLPGVEVRIISENpqkgspyiihaegnerGTKVTPGfeeKEGELLVRGPSVFREYWDKPEETKS 443
Cdd:PRK09088 295 SVDCDVIRakaGAAGIPTPTVQTRVVDDQ----------------GNDCPAG---VPGELLLRGPNLSPGYWRRPQATAR 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 444 AFTSDGWFRTGDTAVfKDAR--YWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSITDVAVIGVPDMTWGQRVTAVVALQ 521
Cdd:PRK09088 356 AFTGDGWFRTGDIAR-RDADgfFWVVDRKK-DMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPA 433
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1720427507 522 EGHSLSHGDLKEWARGVLAPYAVPSELLLVEEIPRNQMGKVNKKELLKQLYP 573
Cdd:PRK09088 434 DGAPLDLERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLRDALAA 485
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
54-567 |
1.83e-62 |
|
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ligase, 4-hydroxybenzoate-CoA ligase, 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases.
Pssm-ID: 274059 [Multi-domain] Cd Length: 505 Bit Score: 214.32 E-value: 1.83e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 54 GDRIALIDKYGHHTYRELYDRSLCLAQEICRLqgckvGDLQEERVSFLCSNDVSYVVAQWASWMSGGVAVPLYWKHPEAQ 133
Cdd:TIGR02262 19 GGKTAFIDDISSLSYGELEAQVRRLAAALRRL-----GVKREERVLLLMLDGVDFPIAFLGAIRAGIVPVALNTLLTADD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 134 LEYFIQDSRSSLVVVGQEYLERLSPLAQRLGvpllPLTPAVYHGATEKPTEQPVEESGWR-----------DRGAMIFYT 202
Cdd:TIGR02262 94 YAYMLEDSRARVVFVSGALLPVIKAALGKSP----HLEHRVVVGRPEAGEVQLAELLATEseqfkpaatqaDDPAFWLYS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 203 SGTTGRPKGALSTHRNLAAVV-TGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEF-SAQQVWEKFL 280
Cdd:TIGR02262 170 SGSTGMPKGVVHTHSNPYWTAeLYARNTLGIREDDVCFSAAKLFFAYGLGNALTFPMSVGATTVLMGERpTPDAVFDRLR 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 281 SSeapQITVFMAVPTVYSKLLDYYDkhftqphvqdfVRAVCKERIRLMVSGSAALPVPLLEKWRSATGHTLLERYGMTEI 360
Cdd:TIGR02262 250 RH---QPTIFYGVPTLYAAMLADPN-----------LPSEDQVRLRLCTSAGEALPAEVGQRWQARFGVDIVDGIGSTEM 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 361 G-MALSNPLTEARVpGSVGTPLPGVEVRIIsenpqkgspyiihaegNERGTKVTPGfeeKEGELLVRGPSVFREYWDKPE 439
Cdd:TIGR02262 316 LhIFLSNLPGDVRY-GTSGKPVPGYRLRLV----------------GDGGQDVADG---EPGELLISGPSSATMYWNNRA 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 440 ETKSAFTSdGWFRTGDTAVFK-DARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSITDVAVIGVPDMTWGQRVTAVV 518
Cdd:TIGR02262 376 KSRDTFQG-EWTRSGDKYVRNdDGSYTYAGRTD-DMLKVSGIYVSPFEIESALIQHPAVLEAAVVGVADEDGLIKPKAFV 453
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1720427507 519 ALQEGHSLSHGDLKEWARGVLAPYAVPSELLLVEEIPRNQMGKVNKKEL 567
Cdd:TIGR02262 454 VLRPGQTALETELKEHVKDRLAPYKYPRWIVFVDDLPKTATGKIQRFKL 502
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
53-583 |
1.31e-61 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 212.59 E-value: 1.31e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 53 FGDRIALIDKYGHHTYRELYDRSLCLAQEICRlQGCKVGDlqeeRVSFLCSNDVSYVVAQWASWMSGGVAVPLYWKHPEA 132
Cdd:PRK07470 20 FPDRIALVWGDRSWTWREIDARVDALAAALAA-RGVRKGD----RILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 133 QLEYFIQDSRSSLVVVG---QEYLERLSPLAQRLGVPL--------LPLTPAVYHGATEKPTEQPVEesgwRDRGAMIFY 201
Cdd:PRK07470 95 EVAYLAEASGARAMICHadfPEHAAAVRAASPDLTHVVaiggaragLDYEALVARHLGARVANAAVD----HDDPCWFFF 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 202 TSGTTGRPKGALSTHRNLAAVVT--------GLVHSwawtknDVILHVLPLHHVHGVvnKLLCPLWVGATCVMLP--EFS 271
Cdd:PRK07470 171 TSGTTGRPKAAVLTHGQMAFVITnhladlmpGTTEQ------DASLVVAPLSHGAGI--HQLCQVARGAATVLLPseRFD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 272 AQQVWEKFlssEAPQITVFMAVPTVYsKLL------DYYDkHFTQPHV---------QDFVRAVCKerirlmvsgsaalp 336
Cdd:PRK07470 243 PAEVWALV---ERHRVTNLFTVPTIL-KMLvehpavDRYD-HSSLRYViyagapmyrADQKRALAK-------------- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 337 vpllekwrsaTGHTLLERYGMTEI---------GMALSNPLTEARVpGSVGTPLPGVEVRIIsenpqkgspyiihaegNE 407
Cdd:PRK07470 304 ----------LGKVLVQYFGLGEVtgnitvlppALHDAEDGPDARI-GTCGFERTGMEVQIQ----------------DD 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 408 RGTKVTPGfeeKEGELLVRGPSVFREYWDKPEETKSAFtSDGWFRTGDTAvFKDAR--YWIRGRTSvDIIKTGGYKVSAL 485
Cdd:PRK07470 357 EGRELPPG---ETGEICVIGPAVFAGYYNNPEANAKAF-RDGWFRTGDLG-HLDARgfLYITGRAS-DMYISGGSNVYPR 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 486 EIERHLLAHPSITDVAVIGVPDMTWGQRVTAVVALQEGHSLSHGDLKEWARGVLAPYAVPSELLLVEEIPRNQMGKVNKK 565
Cdd:PRK07470 431 EIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDGAPVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKK 510
|
570
....*....|....*...
gi 1720427507 566 ELLKQLYPSGQRSQPGQG 583
Cdd:PRK07470 511 MVREELEERGLLDLERAP 528
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
49-571 |
1.72e-61 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 210.97 E-value: 1.72e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 49 RALAFGDRIALIDKYGHHTYRELYDRSLCLAQeicRLQgcKVGDLQEERVSFLCSNDVSYVVAQWASWMSGGVAVPLYWK 128
Cdd:PRK03640 11 RAFLTPDRTAIEFEEKKVTFMELHEAVVSVAG---KLA--ALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 129 HPEAQLEYFIQDSRSSLVVVGQEYLERLSPLaQRLGVPLLPltpavyhgatEKPTEQPVEESGWR-DRGAMIFYTSGTTG 207
Cdd:PRK03640 86 LSREELLWQLDDAEVKCLITDDDFEAKLIPG-ISVKFAELM----------NGPKEEAEIQEEFDlDEVATIMYTSGTTG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 208 RPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVvNKLLCPLWVGATCVMLPEFSAQQVWEKFLSSeapQI 287
Cdd:PRK03640 155 KPKGVIQTYGNHWWSAVGSALNLGLTEDDCWLAAVPIFHISGL-SILMRSVIYGMRVVLVEKFDAEKINKLLQTG---GV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 288 TVFMAVPTVYSKLLDYYDKHftqphvqdfvraVCKERIRLMVSGSAALPVPLLEKWRsATGHTLLERYGMTEIG---MAL 364
Cdd:PRK03640 231 TIISVVSTMLQRLLERLGEG------------TYPSSFRCMLLGGGPAPKPLLEQCK-EKGIPVYQSYGMTETAsqiVTL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 365 SNPLTEARVpGSVGTPLPGVEVRIisenpqkgspyiihaegnERGTKVTPGFEEkeGELLVRGPSVFREYWDKPEETKSA 444
Cdd:PRK03640 298 SPEDALTKL-GSAGKPLFPCELKI------------------EKDGVVVPPFEE--GEIVVKGPNVTKGYLNREDATRET 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 445 FtSDGWFRTGDTAVFKDARY-WIRGRTSvDIIKTGGYKVSALEIERHLLAHPSITDVAVIGVPDMTWGQRVTAVVALqeG 523
Cdd:PRK03640 357 F-QDGWFKTGDIGYLDEEGFlYVLDRRS-DLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVK--S 432
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1720427507 524 HSLSHGDLKEWARGVLAPYAVPSELLLVEEIPRNQMGKVNKKELLKQL 571
Cdd:PRK03640 433 GEVTEEELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQLV 480
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
55-567 |
2.12e-61 |
|
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: 210.83 E-value: 2.12e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 55 DRIALIDKYGHH--TYRELYDRSLCLAQEICRLqGCKVGDlqeeRVSFLCSNDVSYVVAQWASWMSGGVAVPLYWKHPEA 132
Cdd:cd05923 16 DACAIADPARGLrlTYSELRARIEAVAARLHAR-GLRPGQ----RVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 133 QLEYFIQ--DSRSSLVVVGQEYLE-------RLSPLAQRLGVPllplTPAVYHGATEKPTEQPvEESGWrdrgamIFYTS 203
Cdd:cd05923 91 ELAELIErgEMTAAVIAVDAQVMDaifqsgvRVLALSDLVGLG----EPESAGPLIEDPPREP-EQPAF------VFYTS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 204 GTTGRPKGALSTHRNLA------AVVTGLVHSwawtKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSAQQVWE 277
Cdd:cd05923 160 GTTGLPKGAVIPQRAAEsrvlfmSTQAGLRHG----RHNVVLGLMPLYHVIGFFAVLVAALALDGTYVVVEEFDPADALK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 278 KFlssEAPQITVFMAVPTVYSKLLdyydkhftqpHVQDFVRAVCKERIRLMVSGsAALPVPLLEKWRSATGHTLLERYGM 357
Cdd:cd05923 236 LI---EQERVTSLFATPTHLDALA----------AAAEFAGLKLSSLRHVTFAG-ATMPDAVLERVNQHLPGEKVNIYGT 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 358 TEIGMALSNPltEARvPGSVGTPLPGVEVRIIsenPQKGSPYIIHAEGnergtkvtpgfeeKEGELLVR--GPSVFREYW 435
Cdd:cd05923 302 TEAMNSLYMR--DAR-TGTEMRPGFFSEVRIV---RIGGSPDEALANG-------------EEGELIVAaaADAAFTGYL 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 436 DKPEETKSAFtSDGWFRTGDTAVFK-DARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSITDVAVIGVPDMTWGQRV 514
Cdd:cd05923 363 NQPEATAKKL-QDGWYRTGDVGYVDpSGDVRILGRVD-DMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSV 440
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1720427507 515 TAVVALQEGhSLSHGDLKEWARGV-LAPYAVPSELLLVEEIPRNQMGKVNKKEL 567
Cdd:cd05923 441 TACVVPREG-TLSADELDQFCRASeLADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
49-571 |
3.13e-61 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 211.92 E-value: 3.13e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 49 RALAFGDRIALIDKYGH-HTYRELYDRSLCLAQEICRlQGCKVGDlqeeRVSFLCSNDVSYVVAQWASWMSGGVAVPLYW 127
Cdd:PRK06087 32 TARAMPDKIAVVDNHGAsYTYSALDHAASRLANWLLA-KGIEPGD----RVAFQLPGWCEFTIIYLACLKVGAVSVPLLP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 128 KHPEAQLEYFIQDSRSSLVVV-----GQEYLERLSPLAQRL-------GV-PLLPLTPAVYHG---ATEKPTEQPVEESG 191
Cdd:PRK06087 107 SWREAELVWVLNKCQAKMFFAptlfkQTRPVDLILPLQNQLpqlqqivGVdKLAPATSSLSLSqiiADYEPLTTAITTHG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 192 wrDRGAMIFYTSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFS 271
Cdd:PRK06087 187 --DELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLDIFT 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 272 AQQVWEKFlssEAPQITVFM-AVPTVYSkLLDYYDKHftQPHVqdfvravckERIRLMVSGSAALPVPLLekwRSATGH- 349
Cdd:PRK06087 265 PDACLALL---EQQRCTCMLgATPFIYD-LLNLLEKQ--PADL---------SALRFFLCGGTTIPKKVA---RECQQRg 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 350 -TLLERYGMTE----IGMALSNPLTeaRVPGSVGTPLPGVEVRIISENPQKgspyiihaegnergtkVTPGfeeKEGELL 424
Cdd:PRK06087 327 iKLLSVYGSTEssphAVVNLDDPLS--RFMHTDGYAAAGVEIKVVDEARKT----------------LPPG---CEGEEA 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 425 VRGPSVFREYWDKPEETKSAFTSDGWFRTGDTAVFKDARYW-IRGRTSvDIIKTGGYKVSALEIERHLLAHPSITDVAVI 503
Cdd:PRK06087 386 SRGPNVFMGYLDEPELTARALDEEGWYYSGDLCRMDEAGYIkITGRKK-DIIVRGGENISSREVEDILLQHPKIHDACVV 464
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 504 GVPDMTWGQRVTAVVALQEG-HSLSHGDLKEW-ARGVLAPYAVPSELLLVEEIPRNQMGKVNKKELLKQL 571
Cdd:PRK06087 465 AMPDERLGERSCAYVVLKAPhHSLTLEEVVAFfSRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRKDI 534
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
198-564 |
6.84e-61 |
|
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341292 [Multi-domain] Cd Length: 333 Bit Score: 204.81 E-value: 6.84e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 198 MIFYTSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVvNKLLCPLWVGATCVMLPEFSAQQVWE 277
Cdd:cd17637 4 VIIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAGL-NLALATFHAGGANVVMEKFDPAEALE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 278 KflsSEAPQITVFMAVPTVYSKLLDYYDKHFTQPhvqDFVRAVckerirlmvsgsAALPVP-LLEKWRSATGHTLLERYG 356
Cdd:cd17637 83 L---IEEEKVTLMGSFPPILSNLLDAAEKSGVDL---SSLRHV------------LGLDAPeTIQRFEETTGATFWSLYG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 357 MTEI-GMALSNPLTEArvPGSVGTPLPGVEVRIISENpqkgspyiihaegnerGTKVTPGfeeKEGELLVRGPSVFREYW 435
Cdd:cd17637 145 QTETsGLVTLSPYRER--PGSAGRPGPLVRVRIVDDN----------------DRPVPAG---ETGEIVVRGPLVFQGYW 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 436 DKPEETKSAFtSDGWFRTGDTAVFKDARY-WIRGRTSV-DIIKTGGYKVSALEIERHLLAHPSITDVAVIGVPDMTWGQR 513
Cdd:cd17637 204 NLPELTAYTF-RNGWHHTGDLGRFDEDGYlWYAGRKPEkELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEG 282
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1720427507 514 VTAVVALQEGHSLSHGDLKEWARGVLAPYAVPSELLLVEEIPRNQMGKVNK 564
Cdd:cd17637 283 IKAVCVLKPGATLTADELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
49-567 |
4.38e-60 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 208.00 E-value: 4.38e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 49 RALAFGDRIALI--DKYG---HHTYRELYdrslclaQEICRL------QGCKVGDlqeeRVSFLCSNDVSYVVAQWASWM 117
Cdd:PRK08008 16 LADVYGHKTALIfeSSGGvvrRYSYLELN-------EEINRTanlfysLGIRKGD----KVALHLDNCPEFIFCWFGLAK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 118 SGGVAVPLYWKHPEAQLEYFIQDSRSSLVVVGQEYLERLSPLAQRLGVPL---------LPLTPAVYHGATEKpTEQPVE 188
Cdd:PRK08008 85 IGAIMVPINARLLREESAWILQNSQASLLVTSAQFYPMYRQIQQEDATPLrhicltrvaLPADDGVSSFTQLK-AQQPAT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 189 ESGWR----DRGAMIFYTSGTTGRPKGALSTHRNLaaVVTGLVHSW--AWTKNDVILHVLPLHHVHGVVNKLLCPLWVGA 262
Cdd:PRK08008 164 LCYAPplstDDTAEILFTSGTTSRPKGVVITHYNL--RFAGYYSAWqcALRDDDVYLTVMPAFHIDCQCTAAMAAFSAGA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 263 TCVMLPEFSAQQVWEKFLSSEApqiTVFMAVPTVYSKLLdyydkhfTQPhVQDFVRAVCkerIRLMVsgsAALPVPLLEK 342
Cdd:PRK08008 242 TFVLLEKYSARAFWGQVCKYRA---TITECIPMMIRTLM-------VQP-PSANDRQHC---LREVM---FYLNLSDQEK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 343 --WRSATGHTLLERYGMTE-IGMALSNPLTEARVPGSVGTPLPGVEVRIISENpqkgspyiihaegnerGTKVTPGfeeK 419
Cdd:PRK08008 305 daFEERFGVRLLTSYGMTEtIVGIIGDRPGDKRRWPSIGRPGFCYEAEIRDDH----------------NRPLPAG---E 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 420 EGELLVRG---PSVFREYWDKPEETKSAFTSDGWFRTGDTAVFKDARYWIRGRTSVDIIKTGGYKVSALEIERHLLAHPS 496
Cdd:PRK08008 366 IGEICIKGvpgKTIFKEYYLDPKATAKVLEADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPK 445
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720427507 497 ITDVAVIGVPDMTWGQRVTAVVALQEGHSLSHGDLKEWARGVLAPYAVPSELLLVEEIPRNQMGKVNKKEL 567
Cdd:PRK08008 446 IQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNL 516
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
145-567 |
1.74e-59 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 209.04 E-value: 1.74e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 145 LVVVGqeyLERLSPLAQRLGVPLL-PLTPAVYHGATEKPTEQPVE--ESGWR---DRGAMIFYTSGTTGRPKGALSTHRN 218
Cdd:PRK07529 161 VVEVD---LARYLPGPKRLAVPLIrRKAHARILDFDAELARQPGDrlFSGRPigpDDVAAYFHTGGTTGMPKLAQHTHGN 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 219 ------LAAVVTGLVHswawtkNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPE--FSAQQVWEKFLS-SEAPQITV 289
Cdd:PRK07529 238 evanawLGALLLGLGP------GDTVFCGLPLFHVNALLVTGLAPLARGAHVVLATPqgYRGPGVIANFWKiVERYRINF 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 290 FMAVPTVYSKLLDyydkhftQPhvqdfVRAVCKERIRLMVSGSAALPVPLLEKWRSATGHTLLERYGMTEiGMALS--NP 367
Cdd:PRK07529 312 LSGVPTVYAALLQ-------VP-----VDGHDISSLRYALCGAAPLPVEVFRRFEAATGVRIVEGYGLTE-ATCVSsvNP 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 368 LTEARVPGSVGTPLPGVEVRIISENPQkgSPYIIHAEGNErgtkvtpgfeekEGELLVRGPSVFREYWDkPEETKSAFTS 447
Cdd:PRK07529 379 PDGERRIGSVGLRLPYQRVRVVILDDA--GRYLRDCAVDE------------VGVLCIAGPNVFSGYLE-AAHNKGLWLE 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 448 DGWFRTGDTA-VFKDARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSITDVAVIGVPDMTWGQRVTAVVALQEGHSL 526
Cdd:PRK07529 444 DGWLNTGDLGrIDADGYFWLTGRAK-DLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYVQLKPGASA 522
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1720427507 527 SHGDLKEWARG-VLAPYAVPSELLLVEEIPRNQMGKVNKKEL 567
Cdd:PRK07529 523 TEAELLAFARDhIAERAAVPKHVRILDALPKTAVGKIFKPAL 564
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
199-564 |
2.05e-59 |
|
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: 200.81 E-value: 2.05e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 199 IFYTSGTTGRPKGALSTHRNlaavVTGLVHSWA----WTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSAQQ 274
Cdd:cd17638 5 IMFTSGTTGRSKGVMCAHRQ----TLRAAAAWAdcadLTEDDRYLIINPFFHTFGYKAGIVACLLTGATVVPVAVFDVDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 275 VWEKFlssEAPQITVFMAVPTVYSKLLDYydkhftqPHVQDFVRAvckeRIRLMVSGSAALPVPLLEKWRSATG-HTLLE 353
Cdd:cd17638 81 ILEAI---ERERITVLPGPPTLFQSLLDH-------PGRKKFDLS----SLRAAVTGAATVPVELVRRMRSELGfETVLT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 354 RYGMTEIGMA-LSNPLTEAR-VPGSVGTPLPGVEVRIisenpqkgspyiihaegnergtkvtpgfeEKEGELLVRGPSVF 431
Cdd:cd17638 147 AYGLTEAGVAtMCRPGDDAEtVATTCGRACPGFEVRI-----------------------------ADDGEVLVRGYNVM 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 432 REYWDKPEETKSAFTSDGWFRTGDTAVFKDARYW-IRGRTSvDIIKTGGYKVSALEIERHLLAHPSITDVAVIGVPDMTW 510
Cdd:cd17638 198 QGYLDDPEATAEAIDADGWLHTGDVGELDERGYLrITDRLK-DMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERM 276
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1720427507 511 GQRVTAVVALQEGHSLSHGDLKEWARGVLAPYAVPSELLLVEEIPRNQMGKVNK 564
Cdd:cd17638 277 GEVGKAFVVARPGVTLTEEDVIAWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
49-567 |
2.18e-59 |
|
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: 205.25 E-value: 2.18e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 49 RALAFGDRIALIDKYGHHTYRELYDRSLCLAqeiCRLQGCKVGdlQEERVSFLCSNDVSYVVAQWASWMSGGVAVPLYWK 128
Cdd:cd05920 24 SAARHPDRIAVVDGDRRLTYRELDRRADRLA---AGLRGLGIR--PGDRVVVQLPNVAEFVVLFFALLRLGAVPVLALPS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 129 HPEAQLEYFIQDSRSSLVVVGQEYlERLSPLAqrLGVPLLPLTPAVyhgatekpteqpveesgwrdrgAMIFYTSGTTGR 208
Cdd:cd05920 99 HRRSELSAFCAHAEAVAYIVPDRH-AGFDHRA--LARELAESIPEV----------------------ALFLLSGGTTGT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 209 PKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHvhgvvN-KLLCP-----LWVGATCVMLPEFSAQQVwekFLSS 282
Cdd:cd05920 154 PKLIPRTHNDYAYNVRASAEVCGLDQDTVYLAVLPAAH-----NfPLACPgvlgtLLAGGRVVLAPDPSPDAA---FPLI 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 283 EAPQITVFMAVPTVYSKLLDYYDKHFTQPhvqdfvravckERIRLMVSGSAALPVPLLEKWRSATGHTLLERYGMTEiGM 362
Cdd:cd05920 226 EREGVTVTALVPALVSLWLDAAASRRADL-----------SSLRLLQVGGARLSPALARRVPPVLGCTLQQVFGMAE-GL 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 363 ----ALSNPltEARVPGSVGTPL-PGVEVRIISEnpqkgspyiihaEGNErgtkVTPGfeeKEGELLVRGPSVFREYWDK 437
Cdd:cd05920 294 lnytRLDDP--DEVIIHTQGRPMsPDDEIRVVDE------------EGNP----VPPG---EEGELLTRGPYTIRGYYRA 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 438 PEETKSAFTSDGWFRTGDTA-VFKDARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSITDVAVIGVPDMTWGQRVTA 516
Cdd:cd05920 353 PEHNARAFTPDGFYRTGDLVrRTPDGYLVVEGRIK-DQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCA 431
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1720427507 517 VVALQeGHSLSHGDLKEWARGV-LAPYAVPSELLLVEEIPRNQMGKVNKKEL 567
Cdd:cd05920 432 FVVLR-DPPPSAAQLRRFLRERgLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
33-567 |
2.26e-59 |
|
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: 205.23 E-value: 2.26e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 33 PTTPEAHTDGSvpvfirALAFGDRIALIdkYGH--HTYRELYDRSLCLAQEICRLqGCKVGDlqeeRVSFLCSNDVSYVV 110
Cdd:cd12118 3 PLTPLSFLERA------AAVYPDRTSIV--YGDrrYTWRQTYDRCRRLASALAAL-GISRGD----TVAVLAPNTPAMYE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 111 AQWASWMSGGVAVPLYWKHPEAQLEYFIQDSRSSLVVVGQEYL-ERLspLAQrlgvpllpltpavyhGATEKPTEQPVEE 189
Cdd:cd12118 70 LHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVLFVDREFEyEDL--LAE---------------GDPDFEWIPPADE 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 190 sgwRDRGAmIFYTSGTTGRPKGALSTHRN--LAAVVTGLvhSWAWTKNDVILHVLPLHHVHGvvnklLCPLW----VGAT 263
Cdd:cd12118 133 ---WDPIA-LNYTSGTTGRPKGVVYHHRGayLNALANIL--EWEMKQHPVYLWTLPMFHCNG-----WCFPWtvaaVGGT 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 264 CVMLPEFSAQQVWEkflSSEAPQITVFMAVPTVYSKLLDYydkhftqphvQDFVRAVCKERIRLMVSGSAAlPVPLLEKw 343
Cdd:cd12118 202 NVCLRKVDAKAIYD---LIEKHKVTHFCGAPTVLNMLANA----------PPSDARPLPHRVHVMTAGAPP-PAAVLAK- 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 344 RSATGHTLLERYGMTEI-GMALSNPLTearvPGSVGTPLPgVEVRIISenpQKGSPYIIHAE---GNERGTKVTPGFEEK 419
Cdd:cd12118 267 MEELGFDVTHVYGLTETyGPATVCAWK----PEWDELPTE-ERARLKA---RQGVRYVGLEEvdvLDPETMKPVPRDGKT 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 420 EGELLVRGPSVFREYWDKPEETKSAFtSDGWFRTGDTAVFK-DARYWIRGRtSVDIIKTGGYKVSALEIERHLLAHPSIT 498
Cdd:cd12118 339 IGEIVFRGNIVMKGYLKNPEATAEAF-RGGWFHSGDLAVIHpDGYIEIKDR-SKDIIISGGENISSVEVEGVLYKHPAVL 416
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720427507 499 DVAVIGVPDMTWGQRVTAVVALQEGHSLSHGDLKEWARGVLAPYAVPSElLLVEEIPRNQMGKVNKKEL 567
Cdd:cd12118 417 EAAVVARPDEKWGEVPCAFVELKEGAKVTEEEIIAFCREHLAGFMVPKT-VVFGELPKTSTGKIQKFVL 484
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
67-567 |
2.13e-58 |
|
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: 200.65 E-value: 2.13e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 67 TYRELYDRSLCLAQeicRLQgcKVGDLQEERVSFLCSNDVSYVVAQWASWMSGGVAVPLYWKHPEAQLEYFIQDSRSSLv 146
Cdd:cd05912 3 TFAELFEEVSRLAE---HLA--ALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 147 vvgqeylerlsplaqrlgvpllpltpavyhgatekpteqpveesgwrDRGAMIFYTSGTTGRPKGALSTHRNLAAVVTGL 226
Cdd:cd05912 77 -----------------------------------------------DDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGS 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 227 VHSWAWTKNDVILHVLPLHHVHGvVNKLLCPLWVGATCVMLPEFSAQQVWEKFLSSEapqITVFMAVPTVYSKLLDYYDK 306
Cdd:cd05912 110 ALNLGLTEDDNWLCALPLFHISG-LSILMRSVIYGMTVYLVDKFDAEQVLHLINSGK---VTIISVVPTMLQRLLEILGE 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 307 HftqphvqdfvravCKERIRLMVSGSAALPVPLLEKWRsATGHTLLERYGMTEIG--MALSNPLTEARVPGSVGTPLPGV 384
Cdd:cd05912 186 G-------------YPNNLRCILLGGGPAPKPLLEQCK-EKGIPVYQSYGMTETCsqIVTLSPEDALNKIGSAGKPLFPV 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 385 EVRIISENpqkgspyiihaegnergtkvtpGFEEKEGELLVRGPSVFREYWDKPEETKSAFtSDGWFRTGDTAVFKDARY 464
Cdd:cd05912 252 ELKIEDDG----------------------QPPYEVGEILLKGPNVTKGYLNRPDATEESF-ENGWFKTGDIGYLDEEGF 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 465 -WIRGRTSvDIIKTGGYKVSALEIERHLLAHPSITDVAVIGVPDMTWGQRVTAVVALQEghSLSHGDLKEWARGVLAPYA 543
Cdd:cd05912 309 lYVLDRRS-DLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSER--PISEEELIAYCSEKLAKYK 385
|
490 500
....*....|....*....|....
gi 1720427507 544 VPSELLLVEEIPRNQMGKVNKKEL 567
Cdd:cd05912 386 VPKKIYFVDELPRTASGKLLRHEL 409
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
56-567 |
7.62e-58 |
|
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: 200.01 E-value: 7.62e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 56 RIALIDKYGHHTYRELydrsLCLAQEICRLQGCKVGDLQEERVSFLCSNDVSYVVAQWASWMSGGVAVPLYWKHPEAQLE 135
Cdd:cd05958 1 RTCLRSPEREWTYRDL----LALANRIANVLVGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 136 YFIQDSRSSLVVVGqeylERLSPlaqrlgvpllpltpavyhgatekpteqpveesgwRDRGAMIFYTSGTTGRPKGALST 215
Cdd:cd05958 77 YILDKARITVALCA----HALTA----------------------------------SDDICILAFTSGTTGAPKATMHF 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 216 HRNLAAVVTGL-VHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSAQQVwekfLSSEAPQ-ITVFMAV 293
Cdd:cd05958 119 HRDPLASADRYaVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEATPDLL----LSAIARYkPTVLFTA 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 294 PTVYSKLLDYYDkhFTQPHVQDfvravckerIRLMVSGSAALPVPLLEKWRSATGHTLLERYGMTE-IGMALSNPLTEAR 372
Cdd:cd05958 195 PTAYRAMLAHPD--AAGPDLSS---------LRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEmFHIFISARPGDAR 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 373 vPGSVGTPLPGVEVRIISEnpqkgspyiihaEGNErgtkVTPGfeeKEGELLVRGPSVFREYWDKPEETksaFTSDGWFR 452
Cdd:cd05958 264 -PGATGKPVPGYEAKVVDD------------EGNP----VPDG---TIGRLAVRGPTGCRYLADKRQRT---YVQGGWNI 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 453 TGDTAVFK-DARYWIRGRtSVDIIKTGGYKVSALEIERHLLAHPSITDVAVIGVPDMTWGQRVTAVVALQEGHSLSH--- 528
Cdd:cd05958 321 TGDTYSRDpDGYFRHQGR-SDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPGPvla 399
|
490 500 510
....*....|....*....|....*....|....*....
gi 1720427507 529 GDLKEWARGVLAPYAVPSELLLVEEIPRNQMGKVNKKEL 567
Cdd:cd05958 400 RELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFAL 438
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
50-570 |
1.70e-57 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 201.54 E-value: 1.70e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 50 ALAFGDRIALIDKYGHHTYRELYDRSLCLAQEICRlQGCKVGDlqeeRVSFLCSNDVSYVVAQWASWMSGGVAVPLYWKH 129
Cdd:PRK07786 27 ALMQPDAPALRFLGNTTTWRELDDRVAALAGALSR-RGVGFGD----RVLILMLNRTEFVESVLAANMLGAIAVPVNFRL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 130 PEAQLEYFIQDSRSSLVVVGqeylERLSPLAQ--RLGVPLLPlTPAVYHGATEK-------------PTEQPVEESgwRD 194
Cdd:PRK07786 102 TPPEIAFLVSDCGAHVVVTE----AALAPVATavRDIVPLLS-TVVVAGGSSDDsvlgyedllaeagPAHAPVDIP--ND 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 195 RGAMIFYTSGTTGRPKGALSTHRNLAA-VVTGLVHSWAWTKNDVILHVLPLHHVHGVVNkLLCPLWVGATCVMLP--EFS 271
Cdd:PRK07786 175 SPALIMYTSGTTGRPKGAVLTHANLTGqAMTCLRTNGADINSDVGFVGVPLFHIAGIGS-MLPGLLLGAPTVIYPlgAFD 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 272 AQQVWEKFlssEAPQITVFMAVPTVYsklldyydkhftqphvqdfvRAVCKE--------RIRLMVSGSAALPVPLLEKW 343
Cdd:PRK07786 254 PGQLLDVL---EAEKVTGIFLVPAQW--------------------QAVCAEqqarprdlALRVLSWGAAPASDTLLRQM 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 344 rSAT--GHTLLERYGMTEIgmalsNPLT-------EARVPGSVGTPLPGVEVRIISENPQKgspyiihaegnergtkVTP 414
Cdd:PRK07786 311 -AATfpEAQILAAFGQTEM-----SPVTcmllgedAIRKLGSVGKVIPTVAARVVDENMND----------------VPV 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 415 GfeeKEGELLVRGPSVFREYWDKPEETKSAFtSDGWFRTGDTAVFKDARY-WIRGRTSvDIIKTGGYKVSALEIERHLLA 493
Cdd:PRK07786 369 G---EVGEIVYRAPTLMSGYWNNPEATAEAF-AGGWFHSGDLVRQDEEGYvWVVDRKK-DMIISGGENIYCAEVENVLAS 443
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720427507 494 HPSITDVAVIGVPDMTWGQRVTAVVALQ-EGHSLSHGDLKEWARGVLAPYAVPSELLLVEEIPRNQMGKVNKKELLKQ 570
Cdd:PRK07786 444 HPDIVEVAVIGRADEKWGEVPVAVAAVRnDDAALTLEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTELRER 521
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
54-567 |
5.69e-57 |
|
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: 198.28 E-value: 5.69e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 54 GDRIALIDKYGHHTYRELYDRSLCLAQeicRLQGCKVGdlQEERVSFLCSNDVSYVVAQWASWMSGGVAVPLYWKHPEAQ 133
Cdd:cd12116 1 PDATAVRDDDRSLSYAELDERANRLAA---RLRARGVG--PGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 134 LEYFIQDSRSSLVVVGQEYLERLSplaqrLGVPLLPLTPAVYHGATEKPTEQPVEesgwrDRGAMIFYTSGTTGRPKGAL 213
Cdd:cd12116 76 LRYILEDAEPALVLTDDALPDRLP-----AGLPVLLLALAAAAAAPAAPRTPVSP-----DDLAYVIYTSGSTGRPKGVV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 214 STHRNLAAVVTGLVHSWAWTKNDVILHVLP-------LhhvhgvvnKLLCPLWVGATCVMLPEFSAQQVwEKFLSS-EAP 285
Cdd:cd12116 146 VSHRNLVNFLHSMRERLGLGPGDRLLAVTTyafdislL--------ELLLPLLAGARVVIAPRETQRDP-EALARLiEAH 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 286 QITVFMAVPTVYSKLLDyydkhfTQPHVQDFVRAVCkerirlmvsGSAALPVPLLEKWRSATGhTLLERYGMTEIGM-AL 364
Cdd:cd12116 217 SITVMQATPATWRMLLD------AGWQGRAGLTALC---------GGEALPPDLAARLLSRVG-SLWNLYGPTETTIwST 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 365 SNPLTEARVPGSVGTPLPGVEVRIIsenpqkgspyiihaegNERGTKVTPGFeekEGELLVRGPSVFREYWDKPEETKSA 444
Cdd:cd12116 281 AARVTAAAGPIPIGRPLANTQVYVL----------------DAALRPVPPGV---PGELYIGGDGVAQGYLGRPALTAER 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 445 FTSDG-------WFRTGDTAVFK-DARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSITDVAVIGVPDMTwGQRVTA 516
Cdd:cd12116 342 FVPDPfagpgsrLYRTGDLVRRRaDGRLEYLGRAD-GQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGG-DRRLVA 419
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1720427507 517 VVALQEGHSLSHGDLKEWARGVLAPYAVPSELLLVEEIPRNQMGKVNKKEL 567
Cdd:cd12116 420 YVVLKAGAAPDAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
55-571 |
1.71e-56 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 199.12 E-value: 1.71e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 55 DRIALIDKYGHH------TYRELYDRSLCLAQEICRLqGCKVGDLqeerVSFLCSNDVSYVVAQWASWMSGGVAVPLYWK 128
Cdd:PRK13295 39 DKTAVTAVRLGTgaprrfTYRELAALVDRVAVGLARL-GVGRGDV----VSCQLPNWWEFTVLYLACSRIGAVLNPLMPI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 129 HPEAQLEYFIQDSRSSLVVVGQEY--------LERLSPLAqrlgvpllpltPAVYH-----GATEKPTEQPVEESGW--- 192
Cdd:PRK13295 114 FRERELSFMLKHAESKVLVVPKTFrgfdhaamARRLRPEL-----------PALRHvvvvgGDGADSFEALLITPAWeqe 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 193 --------RDRG-----AMIFYTSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLW 259
Cdd:PRK13295 183 pdapailaRLRPgpddvTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPMAHQTGFMYGLMMPVM 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 260 VGATCVMlpefsaQQVWEKFLSSEAPQ---ITVFMAvptvysklldyydkhfTQPHVQDFVRAVcKER------IRLMVS 330
Cdd:PRK13295 263 LGATAVL------QDIWDPARAAELIRtegVTFTMA----------------STPFLTDLTRAV-KESgrpvssLRTFLC 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 331 GSAALPVPLLEKWRSATGHTLLERYGMTEIGMALSNPLTEA--RVPGSVGTPLPGVEVRIISENpqkgspyiihaegner 408
Cdd:PRK13295 320 AGAPIPGALVERARAALGAKIVSAWGMTENGAVTLTKLDDPdeRASTTDGCPLPGVEVRVVDAD---------------- 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 409 GTKVTPGfeeKEGELLVRGPSVFREYWDKPEETKSAFtsDGWFRTGDTAvFKDARYWIR--GRTSvDIIKTGGYKVSALE 486
Cdd:PRK13295 384 GAPLPAG---QIGRLQVRGCSNFGGYLKRPQLNGTDA--DGWFDTGDLA-RIDADGYIRisGRSK-DVIIRGGENIPVVE 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 487 IERHLLAHPSITDVAVIGVPDMTWGQRVTAVVALQEGHSLSHGDLKEW--ARGVLAPYaVPSELLLVEEIPRNQMGKVNK 564
Cdd:PRK13295 457 IEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPGQSLDFEEMVEFlkAQKVAKQY-IPERLVVRDALPRTPSGKIQK 535
|
....*..
gi 1720427507 565 KELLKQL 571
Cdd:PRK13295 536 FRLREML 542
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
67-567 |
1.77e-56 |
|
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 162605 [Multi-domain] Cd Length: 436 Bit Score: 196.13 E-value: 1.77e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 67 TYRELYDRSLCLAQEIcRLQGCKVGDlqeeRVSFLCSNDVSYVVAQWASWMSGGVAVPLYWKHPEAQLEYFIQDSRSSLV 146
Cdd:TIGR01923 1 TWQDLDCEAAHLAKAL-KAQGIRSGS----RVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 147 VVGQEYLER--LSPLAQRLGvpllpltpavyhgaTEKPTEQPVEESGWRDRGAMIFYTSGTTGRPKGALSTHRNLAAVVT 224
Cdd:TIGR01923 76 LTDSLLEEKdfQADSLDRIE--------------AAGRYETSLSASFNMDQIATLMFTSGTTGKPKAVPHTFRNHYASAV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 225 GLVHSWAWTKNDVILHVLPLHHVHGVvNKLLCPLWVGATCVMLPEFSaqQVWEKFLSSEapqITVFMAVPTVYSKLLDyy 304
Cdd:TIGR01923 142 GSKENLGFTEDDNWLLSLPLYHISGL-SILFRWLIEGATLRIVDKFN--QLLEMIANER---VTHISLVPTQLNRLLD-- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 305 dkhftqphvqdfvRAVCKERIRLMVSGSAALPVPLLEKWRSaTGHTLLERYGMTEIG---MALSNPLTEARvpGSVGTPL 381
Cdd:TIGR01923 214 -------------EGGHNENLRKILLGGSAIPAPLIEEAQQ-YGLPIYLSYGMTETCsqvTTATPEMLHAR--PDVGRPL 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 382 PGVEVRIISENpqkgspyiihaegnergtkvtpgfEEKEGELLVRGPSVFREYWDkPEETKSAFTSDGWFRTGDTAVFK- 460
Cdd:TIGR01923 278 AGREIKIKVDN------------------------KEGHGEIMVKGANLMKGYLY-QGELTPAFEQQGWFNTGDIGELDg 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 461 DARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSITDVAVIGVPDMTWGQRVTAVVALQEghSLSHGDLKEWARGVLA 540
Cdd:TIGR01923 333 EGFLYVLGRRD-DLIISGGENIYPEEIETVLYQHPGIQEAVVVPKPDAEWGQVPVAYIVSES--DISQAKLIAYLTEKLA 409
|
490 500
....*....|....*....|....*..
gi 1720427507 541 PYAVPSELLLVEEIPRNQMGKVNKKEL 567
Cdd:TIGR01923 410 KYKVPIAFEKLDELPYNASGKILRNQL 436
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
91-575 |
1.51e-55 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 196.26 E-value: 1.51e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 91 GDLQEERVSFLCSNDVSYVVAQWASWMSGGVAVPLYWKHPEAQleyfiQDSRSSLVVVGQEYLERLSPLAQRLG-VPLLP 169
Cdd:PRK05852 64 GLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAE-----QRVRSQAAGARVVLIDADGPHDRAEPtTRWWP 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 170 L-------------TPAVYHGATEKPTEQPVEESGWRDRGAMIFYTSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKND 236
Cdd:PRK05852 139 LtvnvggdsgpsggTLSVHLDAATEPTPATSTPEGLRPDDAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRD 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 237 VILHVLPLHHVHGVVNKLLCPLWVGATcVMLP---EFSAQQVWEKFLSSEApqiTVFMAVPTVYSKLLDyydkhftQPHV 313
Cdd:PRK05852 219 ATVAVMPLYHGHGLIAALLATLASGGA-VLLPargRFSAHTFWDDIKAVGA---TWYTAVPTIHQILLE-------RAAT 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 314 QDFVRAvcKERIRLMVSGSAALPVPLLEKWRSATGHTLLERYGMTEIgmalSNPLTEARVPGSVGTPLPGVEVRIISenp 393
Cdd:PRK05852 288 EPSGRK--PAALRFIRSCSAPLTAETAQALQTEFAAPVVCAFGMTEA----THQVTTTQIEGIGQTENPVVSTGLVG--- 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 394 QKGSPYIIHAEGNerGTKVTPGfeeKEGELLVRGPSVFREYWDKPEETKSAFTsDGWFRTGDT-AVFKDARYWIRGRTSv 472
Cdd:PRK05852 359 RSTGAQIRIVGSD--GLPLPAG---AVGEVWLRGTTVVRGYLGDPTITAANFT-DGWLRTGDLgSLSAAGDLSIRGRIK- 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 473 DIIKTGGYKVSALEIERHLLAHPSITDVAVIGVPDMTWGQRVTAVVALQEGHSLSHGDLKEWARGVLAPYAVPSELLLVE 552
Cdd:PRK05852 432 ELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPRESAPPTAEELVQFCRERLAAFEIPASFQEAS 511
|
490 500
....*....|....*....|...
gi 1720427507 553 EIPRNQMGKVNKKELLKQLYPSG 575
Cdd:PRK05852 512 GLPHTAKGSLDRRAVAEQFGHSV 534
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
32-571 |
2.67e-55 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 196.42 E-value: 2.67e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 32 LPTTPE-AHTDGSVPVFIRALAF--GDRIAlIDKYGHH-TYRELYDRSLCLAqEICRLQGCKVGDlqeeRVSFLCSNDVS 107
Cdd:PRK06178 22 IPREPEyPHGERPLTEYLRAWARerPQRPA-IIFYGHViTYAELDELSDRFA-ALLRQRGVGAGD----RVAVFLPNCPQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 108 YVVAQWASWMSGGVAVPLYWKHPEAQLEYFIQDSRSSLVVVgqeyLERLSPLAQRL-------------------GVPLL 168
Cdd:PRK06178 96 FHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLA----LDQLAPVVEQVraetslrhvivtsladvlpAEPTL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 169 PLtPAVYHGATEKP-------------TEQPVEESGWRDRGAMIFYTSGTTGRPKGALSTHRNL---AAVVTGLVHswAW 232
Cdd:PRK06178 172 PL-PDSLRAPRLAAagaidllpalracTAPVPLPPPALDALAALNYTGGTTGMPKGCEHTQRDMvytAAAAYAVAV--VG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 233 TKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSAQqvwekflsseapqiTVFMAVP----TVYSKLLDYYDKHF 308
Cdd:PRK06178 249 GEDSVFLSFLPEFWIAGENFGLLFPLFSGATLVLLARWDAV--------------AFMAAVEryrvTRTVMLVDNAVELM 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 309 TQPHVQDF-------VRAVckerirlmvSGSAALPVPLLEKWRSATGHTLLE-RYGMTEIGMalSNPLTEA--------- 371
Cdd:PRK06178 315 DHPRFAEYdlsslrqVRVV---------SFVKKLNPDYRQRWRALTGSVLAEaAWGMTETHT--CDTFTAGfqdddfdll 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 372 RVPGSVGTPLPGVEVRIISEnpqkgspyiihaegnERGTKVTPGfeeKEGELLVRGPSVFREYWDKPEETKSAFtSDGWF 451
Cdd:PRK06178 384 SQPVFVGLPVPGTEFKICDF---------------ETGELLPLG---AEGEIVVRTPSLLKGYWNKPEATAEAL-RDGWL 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 452 RTGDTAVFKDA---RYWIRGRtsvDIIKTGGYKVSALEIERHLLAHPSITDVAVIGVPDMTWGQRVTAVVALQEGHSLSH 528
Cdd:PRK06178 445 HTGDIGKIDEQgflHYLGRRK---EMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGADLTA 521
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1720427507 529 GDLKEWARGVLAPYAVPsELLLVEEIPRNQMGKVNKKELLKQL 571
Cdd:PRK06178 522 AALQAWCRENMAVYKVP-EIRIVDALPMTATGKVRKQDLQALA 563
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
65-497 |
1.11e-54 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341240 [Multi-domain] Cd Length: 463 Bit Score: 192.27 E-value: 1.11e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 65 HHTYRELYDRSLCLAQ--EICRLQgckVGDlqeeRVSFLCSNDVSYVVAQWASWMSGGVAVPLYWKHPEAQLEYFIQDSR 142
Cdd:cd05914 7 PLTYKDLADNIAKFALllKINGVG---TGD----RVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 143 SSLVVVGQEylerlsplaqrlgvpllpltpavyhgatekpteqpveesgwrDRGAMIFYTSGTTGRPKGALSTHRNLAAV 222
Cdd:cd05914 80 AKAIFVSDE------------------------------------------DDVALINYTSGTTGNSKGVMLTYRNIVSN 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 223 VTGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSAqqvwEKFLSSEAPQITVFMAVPTVYsKLLD 302
Cdd:cd05914 118 VDGVKEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDKIPS----AKIIALAFAQVTPTLGVPVPL-VIEK 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 303 YYD--------------KHFTQPHVQDFVRAVCKE-------RIRLMVSGSAALPVPLLEKWRSAtGHTLLERYGMTEIG 361
Cdd:cd05914 193 IFKmdiipkltlkkfkfKLAKKINNRKIRKLAFKKvheafggNIKEFVIGGAKINPDVEEFLRTI-GFPYTIGYGMTETA 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 362 MALS-NPLTEARVpGSVGTPLPGVEVRIISENPQKGspyiihaegnergtkvtpgfeekEGELLVRGPSVFREYWDKPEE 440
Cdd:cd05914 272 PIISySPPNRIRL-GSAGKVIDGVEVRIDSPDPATG-----------------------EGEIIVRGPNVMKGYYKNPEA 327
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720427507 441 TKSAFTSDGWFRTGDTAVFKDARY-WIRGRTSVDIIKTGGYKVSALEIERHLLAHPSI 497
Cdd:cd05914 328 TAEAFDKDGWFHTGDLGKIDAEGYlYIRGRKKEMIVLSSGKNIYPEEIEAKINNMPFV 385
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
67-502 |
2.02e-54 |
|
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: 189.78 E-value: 2.02e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 67 TYRELYDRSLCLAQEICRLQGCKVGDlqeeRVSFLCSNDVSYVVAQWASWMSGGVAVPLYWKHPEAQLEYFIQDSRSSLV 146
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGGVGPGD----RVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 147 VVGQEYLERLSPLAQrlgVPLLPLTPAVYHGATEKPTEQPVEESGWRDRgAMIFYTSGTTGRPKGALSTHRNLAAVVTGL 226
Cdd:TIGR01733 77 LTDSALASRLAGLVL---PVILLDPLELAALDDAPAPPPPDAPSGPDDL-AYVIYTSGSTGRPKGVVVTHRSLVNLLAWL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 227 VHSWAWTKNDVILHVLPLHHVHGVVnKLLCPLWVGATCVMLPEfSAQQVWEKFLSS--EAPQITVFMAVPTVYSKLLDyy 304
Cdd:TIGR01733 153 ARRYGLDPDDRVLQFASLSFDASVE-EIFGALLAGATLVVPPE-DEERDDAALLAAliAEHPVTVLNLTPSLLALLAA-- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 305 dkhftqphvqdfVRAVCKERIRLMVSGSAALPVPLLEKWRSATGHT-LLERYGMTE--IG-MALSNPLTEARVPGSV--G 378
Cdd:TIGR01733 229 ------------ALPPALASLRLVILGGEALTPALVDRWRARGPGArLINLYGPTEttVWsTATLVDPDDAPRESPVpiG 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 379 TPLPGVEVriisenpqkgspYIIHAEGNERGTKVTpgfeekeGELLVRGPSVFREYWDKPEETKSAFTSDG--------W 450
Cdd:TIGR01733 297 RPLANTRL------------YVLDDDLRPVPVGVV-------GELYIGGPGVARGYLNRPELTAERFVPDPfaggdgarL 357
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1720427507 451 FRTGDTAVFKDARYW-IRGRTSvDIIKTGGYKVSALEIERHLLAHPSITDVAV 502
Cdd:TIGR01733 358 YRTGDLVRYLPDGNLeFLGRID-DQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
49-567 |
1.02e-53 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 191.51 E-value: 1.02e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 49 RALAFGDRIALIDKYGHHTYRELYDRSLCLAQEIcRLQGCKVGDlqeeRVSFLCSNDVSYV-VAQWASWMsGGVAVPLYW 127
Cdd:PRK06155 30 QAERYPDRPLLVFGGTRWTYAEAARAAAAAAHAL-AAAGVKRGD----RVALMCGNRIEFLdVFLGCAWL-GAIAVPINT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 128 KHPEAQLEYFIQDSRSSLVVVGQEYLERLSPLAQR---------LGVPLLPLTPAVYHGATEKPTEQPVEESGWR--DRG 196
Cdd:PRK06155 104 ALRGPQLEHILRNSGARLLVVEAALLAALEAADPGdlplpavwlLDAPASVSVPAGWSTAPLPPLDAPAPAAAVQpgDTA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 197 AmIFYTSGTTGRPKGALSTH-------RNLAAVVtGLvhswawTKNDVILHVLPLHHVHGVvNKLLCPLWVGATCVMLPE 269
Cdd:PRK06155 184 A-ILYTSGTTGPSKGVCCPHaqfywwgRNSAEDL-EI------GADDVLYTTLPLFHTNAL-NAFFQALLAGATYVLEPR 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 270 FSAQQVWEKFLSSEApqiTVFMAVPTVYSKLLdyydkhfTQPHVQDfvravckERI-RLMVSGSAALPVPLLEKWRSATG 348
Cdd:PRK06155 255 FSASGFWPAVRRHGA---TVTYLLGAMVSILL-------SQPARES-------DRAhRVRVALGPGVPAALHAAFRERFG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 349 HTLLERYGMTEIGMALSNPLTEARvPGSVGTPLPGVEVRIISENpqkgspyiihaegnerGTKVTPGfeeKEGELLVRG- 427
Cdd:PRK06155 318 VDLLDGYGSTETNFVIAVTHGSQR-PGSMGRLAPGFEARVVDEH----------------DQELPDG---EPGELLLRAd 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 428 -PSVFRE-YWDKPEETKSAFtSDGWFRTGDTaVFKDARYWIR--GRTSvDIIKTGGYKVSALEIERHLLAHPSITDVAVI 503
Cdd:PRK06155 378 ePFAFATgYFGMPEKTVEAW-RNLWFHTGDR-VVRDADGWFRfvDRIK-DAIRRRGENISSFEVEQVLLSHPAVAAAAVF 454
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720427507 504 GVPDMTWGQRVTAVVALQEGHSLSHGDLKEWARGVLAPYAVPSELLLVEEIPRNQMGKVNKKEL 567
Cdd:PRK06155 455 PVPSELGEDEVMAAVVLRDGTALEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVL 518
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
66-567 |
3.29e-53 |
|
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: 187.71 E-value: 3.29e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 66 HTYRELYDRSLCLAQEICRLqGCKVGDlqeeRVSFLCSNDVSYVVAQWASWMSGGVAVPLYWKHPEAQLEYFIQDSRSSL 145
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSL-GVGKGD----RVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 146 VVVGQEYLERLSPlaqrlgvpllpltpavyhgatEKPTeqpveesgwrdrgaMIFYTSGTTGRPKGALSTHRNLAAVVTG 225
Cdd:cd05969 76 LITTEELYERTDP---------------------EDPT--------------LLHYTSGTTGTPKGVLHVHDAMIFYYFT 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 226 LVHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLP-EFSAQQvWEKFLSSEapQITVFMAVPTVYSKLLDYY 304
Cdd:cd05969 121 GKYVLDLHPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVVYEgRFDAES-WYGIIERV--KVTVWYTAPTAIRMLMKEG 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 305 DkhftqphvqDFVRAVCKERIRLMVSGSAALPvPLLEKW-RSATGHTLLERYGMTEIG-MALSNPLTEARVPGSVGTPLP 382
Cdd:cd05969 198 D---------ELARKYDLSSLRFIHSVGEPLN-PEAIRWgMEVFGVPIHDTWWQTETGsIMIANYPCMPIKPGSMGKPLP 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 383 GVEVRIISENpqkgspyiihaegnerGTKVTPGfeeKEGELLVRG--PSVFREYWDKPEETKSAFTsDGWFRTGDTAvFK 460
Cdd:cd05969 268 GVKAAVVDEN----------------GNELPPG---TKGILALKPgwPSMFRGIWNDEERYKNSFI-DGWYLTGDLA-YR 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 461 DAR--YWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSITDVAVIGVPDMTWGQRVTAVVALQEGHSLSHG---DLKEWA 535
Cdd:cd05969 327 DEDgyFWFVGRAD-DIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSDElkeEIINFV 405
|
490 500 510
....*....|....*....|....*....|..
gi 1720427507 536 RGVLAPYAVPSELLLVEEIPRNQMGKVNKKEL 567
Cdd:cd05969 406 RQKLGAHVAPREIEFVDNLPKTRSGKIMRRVL 437
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
50-567 |
7.09e-53 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 189.37 E-value: 7.09e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 50 ALAFGDRIALIDKYGHHTYRELYDRSLCLAQEICRLqGCKVGDlqeeRVSFLCSNDVSYVVAQWASWMSGGVAVPLYWKH 129
Cdd:PRK07788 59 ARRAPDRAALIDERGTLTYAELDEQSNALARGLLAL-GVRAGD----GVAVLARNHRGFVLALYAAGKVGARIILLNTGF 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 130 PEAQLEYFIQDSRSSLVVVGQEYLERLSPLAQRLGVpllpltpavYHGATEKPTEQPVEESGWRD--------------- 194
Cdd:PRK07788 134 SGPQLAEVAAREGVKALVYDDEFTDLLSALPPDLGR---------LRAWGGNPDDDEPSGSTDETlddliagsstaplpk 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 195 ---RGAMIFYTSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCpLWVGATCVMLPEFS 271
Cdd:PRK07788 205 ppkPGGIVILTSGTTGTPKGAPRPEPSPLAPLAGLLSRVPFRAGETTLLPAPMFHATGWAHLTLA-MALGSTVVLRRRFD 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 272 AQQVWEkflSSEAPQITVFMAVPTVYSKLLDYYDKHFTQPHVQdfvravckeRIRLMVSGSAALPVPLLEKWRSATGHTL 351
Cdd:PRK07788 284 PEATLE---DIAKHKATALVVVPVMLSRILDLGPEVLAKYDTS---------SLKIIFVSGSALSPELATRALEAFGPVL 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 352 LERYGMTEIGMA-LSNPLTEARVPGSVGTPLPGVEVRIISENpqkgspyiihaegnerGTKVTPGfeeKEGELLVRGPSV 430
Cdd:PRK07788 352 YNLYGSTEVAFAtIATPEDLAEAPGTVGRPPKGVTVKILDEN----------------GNEVPRG---VVGRIFVGNGFP 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 431 FREYWDkpeeTKSAFTSDGWFRTGDTAVFKDARYW-IRGRTSvDIIKTGGYKVSALEIERHLLAHPSITDVAVIGVPDMT 509
Cdd:PRK07788 413 FEGYTD----GRDKQIIDGLLSSGDVGYFDEDGLLfVDGRDD-DMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEE 487
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720427507 510 WGQRVTAVVALQEGHSLSHGDLKEWARGVLAPYAVPSELLLVEEIPRNQMGKVNKKEL 567
Cdd:PRK07788 488 FGQRLRAFVVKAPGAALDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKREL 545
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
65-577 |
7.68e-53 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 188.19 E-value: 7.68e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 65 HHTYRELYDRSLCLAQEIcRLQGCKVGDlqeeRVSFLCSNDVSYVVAQWASWMSGGVAVPLYWKHPEAQLEYFIQDSRSS 144
Cdd:PRK08276 11 VVTYGELEARSNRLAHGL-RALGLREGD----VVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 145 LVVVGQEYLERLSPLAQRL--GVPLLPLTPAVYHGATEKPTE---QPVEESGWRDRGAMIFYTSGTTGRPKG---ALSTH 216
Cdd:PRK08276 86 VLIVSAALADTAAELAAELpaGVPLLLVVAGPVPGFRSYEEAlaaQPDTPIADETAGADMLYSSGTTGRPKGikrPLPGL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 217 RNLAA--VVTGLVHSWAWTKND-VILHVLPLHHV-----HGVVNKLlcplwvGATCVMLPEFSAqqvwEKFLSS-EAPQI 287
Cdd:PRK08276 166 DPDEApgMMLALLGFGMYGGPDsVYLSPAPLYHTaplrfGMSALAL------GGTVVVMEKFDA----EEALALiERYRV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 288 TVFMAVPTVYSKLLdyydkhftqpHVQDFVRAvckeR-----IRLMVSGSAALPVP----LLEKWrsatGHTLLERYGMT 358
Cdd:PRK08276 236 THSQLVPTMFVRML----------KLPEEVRA----RydvssLRVAIHAAAPCPVEvkraMIDWW----GPIIHEYYASS 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 359 E-IGMALSNPLTEARVPGSVGTPLPGvEVRIISENpqkgspyiihaeGNErgtkVTPGfeeKEGELLVRGPSVFREYWDK 437
Cdd:PRK08276 298 EgGGVTVITSEDWLAHPGSVGKAVLG-EVRILDED------------GNE----LPPG---EIGTVYFEMDGYPFEYHND 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 438 PEETKSAFTSDGWFRTGDTAVFKDARY-WIRGRTSvDIIKTGGYKVSALEIERHLLAHPSITDVAVIGVPDMTWGQRVTA 516
Cdd:PRK08276 358 PEKTAAARNPHGWVTVGDVGYLDEDGYlYLTDRKS-DMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKA 436
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720427507 517 VVALQEGHSLS---HGDLKEWARGVLAPYAVPSELLLVEEIPRNQMGKVNKKELLKQLYPSGQR 577
Cdd:PRK08276 437 VVQPADGADAGdalAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLRDRYWEGRQR 500
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
194-567 |
1.65e-52 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 183.45 E-value: 1.65e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 194 DRGAMIFYTSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLP----- 268
Cdd:cd05944 2 DDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLAGpagyr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 269 -EFSAQQVWEKFlssEAPQITVFMAVPTVYSKLLdyydkhfTQPHVQDFvravckERIRLMVSGSAALPVPLLEKWRSAT 347
Cdd:cd05944 82 nPGLFDNFWKLV---ERYRITSLSTVPTVYAALL-------QVPVNADI------SSLRFAMSGAAPLPVELRARFEDAT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 348 GHTLLERYGMTEIGMALS-NPLTEARVPGSVGTPLPGVEVRIISENPQkgSPYIIHAEGNErgtkvtpgfeekEGELLVR 426
Cdd:cd05944 146 GLPVVEGYGLTEATCLVAvNPPDGPKRPGSVGLRLPYARVRIKVLDGV--GRLLRDCAPDE------------VGEICVA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 427 GPSVFREYWDKpEETKSAFTSDGWFRTGDTA-VFKDARYWIRGRtSVDIIKTGGYKVSALEIERHLLAHPSITDVAVIGV 505
Cdd:cd05944 212 GPGVFGGYLYT-EGNKNAFVADGWLNTGDLGrLDADGYLFITGR-AKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQ 289
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720427507 506 PDMTWGQRVTAVVALQEGHSLSHGDLKEWARGVLAPY-AVPSELLLVEEIPRNQMGKVNKKEL 567
Cdd:cd05944 290 PDAHAGELPVAYVQLKPGAVVEEEELLAWARDHVPERaAVPKHIEVLEELPVTAVGKVFKPAL 352
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
195-572 |
1.70e-52 |
|
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: 182.15 E-value: 1.70e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 195 RGAMIFYTSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCpLWVGATCVMLPEFSAqq 274
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLAILVRS-LLAGAELVLLERNQA-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 275 vwekFLSSEAPQITVFMA-VPTVYSKLLDYydkHFTQPHVqdfvravckERIRLMVSGSAALPVPLLEKWrSATGHTLLE 353
Cdd:cd17630 78 ----LAEDLAPPGVTHVSlVPTQLQRLLDS---GQGPAAL---------KSLRAVLLGGAPIPPELLERA-ADRGIPLYT 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 354 RYGMTEIG--MALSNPLTEARvpGSVGTPLPGVEVRIisenpqkgspyiihaegnergtkvtpgfeEKEGELLVRGPSVF 431
Cdd:cd17630 141 TYGMTETAsqVATKRPDGFGR--GGVGVLLPGRELRI-----------------------------VEDGEIWVGGASLA 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 432 REYWDKPEEtkSAFTSDGWFRTGDTAVF-KDARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSITDVAVIGVPDMTW 510
Cdd:cd17630 190 MGYLRGQLV--PEFNEDGWFTTKDLGELhADGRLTVLGRAD-NMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEEL 266
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720427507 511 GQRVTAVVALQEGHslSHGDLKEWARGVLAPYAVPSELLLVEEIPRNQMGKVNKKeLLKQLY 572
Cdd:cd17630 267 GQRPVAVIVGRGPA--DPAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRR-ALRAWL 325
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
55-567 |
2.07e-52 |
|
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: 185.53 E-value: 2.07e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 55 DRIALIDKYGHHTYRELYDRSLCLAQEIcRLQGCKVGDlqeeRVSFLCSNDVSYVVAQWASWMSGGVAVPLYWKHPEAQL 134
Cdd:cd05945 6 DRPAVVEGGRTLTYRELKERADALAAAL-ASLGLDAGD----PVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 135 EYFIQDSRSSLVVvgqeylerlsplaqrlgvpllpltpavyhgATEKPTeqpveesgwrdrgAMIFYTSGTTGRPKGALS 214
Cdd:cd05945 81 REILDAAKPALLI------------------------------ADGDDN-------------AYIIFTSGSTGRPKGVQI 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 215 THRNLAAVVTGLVHSWAWTKNDVILHVLPLH---HVHGvvnkLLCPLWVGATCVMLPEfsAQQVWEKFLSSEAPQ--ITV 289
Cdd:cd05945 118 SHDNLVSFTNWMLSDFPLGPGDVFLNQAPFSfdlSVMD----LYPALASGATLVPVPR--DATADPKQLFRFLAEhgITV 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 290 FMAVPTVYSKLLdyYDKHFTQPHVqdfvravckERIRLMVSGSAALPVPLLEKWRSAT-GHTLLERYGMTEIGMALS--- 365
Cdd:cd05945 192 WVSTPSFAAMCL--LSPTFTPESL---------PSLRHFLFCGEVLPHKTARALQQRFpDARIYNTYGPTEATVAVTyie 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 366 ---NPLTEA-RVPgsVGTPLPGVEVRIIsenpqkgspyiihaegNERGTKVTPGfeeKEGELLVRGPSVFREYWDKPEET 441
Cdd:cd05945 261 vtpEVLDGYdRLP--IGYAKPGAKLVIL----------------DEDGRPVPPG---EKGELVISGPSVSKGYLNNPEKT 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 442 KSAFTSD---GWFRTGDtAVFKDA--RYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSITDVAVIGVPDMTWGQRVTA 516
Cdd:cd05945 320 AAAFFPDegqRAYRTGD-LVRLEAdgLLFYRGRLD-FQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIA 397
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1720427507 517 VVALQEGHSLshGDLKEWA---RGVLAPYAVPSELLLVEEIPRNQMGKVNKKEL 567
Cdd:cd05945 398 FVVPKPGAEA--GLTKAIKaelAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
55-571 |
2.52e-51 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 183.93 E-value: 2.52e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 55 DRIALIDKYGHHTYRELYDRSLCLAQEIcRLQGCKVGDLqeerVSFLCSNDVSYVVAQWASWMSGGVAVPLYWKHPEAQL 134
Cdd:PRK06145 17 DRAALVYRDQEISYAEFHQRILQAAGML-HARGIGQGDV----VALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 135 EYFIQDSRSSLVVVGQEY-----LER----LSPLAQ----RLGVPLLPLTPAvyhgATEKPTEQpveesgwrdrgAMIFY 201
Cdd:PRK06145 92 AYILGDAGAKLLLVDEEFdaivaLETpkivIDAAAQadsrRLAQGGLEIPPQ----AAVAPTDL-----------VRLMY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 202 TSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSAQQVWEkflS 281
Cdd:PRK06145 157 TSGTTDRPKGVMHSYGNLHWKSIDHVIALGLTASERLLVVGPLYHVGAFDLPGIAVLWVGGTLRIHREFDPEAVLA---A 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 282 SEAPQITVFMAVPTVYSKLL-----DYYDKhftqphvqdfvravckERIRLMVSGSAALPVPLLEKWRSA-TGHTLLERY 355
Cdd:PRK06145 234 IERHRLTCAWMAPVMLSRVLtvpdrDRFDL----------------DSLAWCIGGGEKTPESRIRDFTRVfTRARYIDAY 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 356 GMTEI--GMALSNPLTEARVPGSVGTPLPGVEVRIISENpqkgspyiihaegnerGTKVTPGfeeKEGELLVRGPSVFRE 433
Cdd:PRK06145 298 GLTETcsGDTLMEAGREIEKIGSTGRALAHVEIRIADGA----------------GRWLPPN---MKGEICMRGPKVTKG 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 434 YWDKPEETKSAFTsDGWFRTGDTAVFKDARYWIRGRTSVDIIKTGGYKVSALEIERHLLAHPSITDVAVIGVPDMTWGQR 513
Cdd:PRK06145 359 YWKDPEKTAEAFY-GDWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGER 437
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720427507 514 VTAVVALQEGHSLSHGDLKEWARGVLAPYAVPSELLLVEEIPRNQMGKVNKKELLKQL 571
Cdd:PRK06145 438 ITAVVVLNPGATLTLEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLRDEL 495
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
67-567 |
1.14e-50 |
|
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: 180.71 E-value: 1.14e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 67 TYRELYDRSLCLAQEICRLqGCKVGDlqeeRVSFLCSNDVSYVVAQWASWMSGGVAVPLYWKHPEAQLEYFIQDSRSSLV 146
Cdd:cd05971 8 TFKELKTASNRFANVLKEI-GLEKGD----RVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 147 VvgqeylerlsplaqrlgvpllpltpavyhgatekpTEQPVEEsgwrdrgAMIFYTSGTTGRPKGALSTHRNLAAVVTGL 226
Cdd:cd05971 83 V-----------------------------------TDGSDDP-------ALIIYTSGTTGPPKGALHAHRVLLGHLPGV 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 227 VHS----------------WAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSAQQVwekFLSSEAPQITVF 290
Cdd:cd05971 121 QFPfnlfprdgdlywtpadWAWIGGLLDVLLPSLYFGVPVLAHRMTKFDPKAALDLMSRYGVTTA---FLPPTALKMMRQ 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 291 MAVPTvysklldyydKHFtqphvqdfvravcKERIRLMVSGSAALPVPLLEKWRSATGHTLLERYGMTEIGMALSNPLTE 370
Cdd:cd05971 198 QGEQL----------KHA-------------QVKLRAIATGGESLGEELLGWAREQFGVEVNEFYGQTECNLVIGNCSAL 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 371 ARV-PGSVGTPLPGVEVRIISENpqkgspyiihaegnerGTKVTPGfeeKEGELLVRGPS--VFREYWDKPEETKSAFTS 447
Cdd:cd05971 255 FPIkPGSMGKPIPGHRVAIVDDN----------------GTPLPPG---EVGEIAVELPDpvAFLGYWNNPSATEKKMAG 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 448 DgWFRTGDTAVF-KDARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSITDVAVIGVPDMTWGQRVTAVVALQEGHSL 526
Cdd:cd05971 316 D-WLLTGDLGRKdSDGYFWYVGRDD-DVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETP 393
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1720427507 527 SHG---DLKEWARGVLAPYAVPSELLLVEEIPRNQMGKVNKKEL 567
Cdd:cd05971 394 SDAlarEIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRREL 437
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
49-580 |
1.14e-49 |
|
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: 185.83 E-value: 1.14e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 49 RALAFGDRIALIDKYGHHTYRELYDRSLCLAQeicRLQGCKVGdlQEERVSFLCSNDVSYVVAQWASWMSGGVAVPLYWK 128
Cdd:COG1020 485 QAARTPDAVAVVFGDQSLTYAELNARANRLAH---HLRALGVG--PGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPA 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 129 HPEAQLEYFIQDSRSSLVVVGQEYLERLSPLaqrlGVPLLPLTPAVYHGATEKPTEQPVEEsgwrDRGAMIFYTSGTTGR 208
Cdd:COG1020 560 YPAERLAYMLEDAGARLVLTQSALAARLPEL----GVPVLALDALALAAEPATNPPVPVTP----DDLAYVIYTSGSTGR 631
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 209 PKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVNkLLCPLWVGATCVMLPEFSAQ--QVWEKFLSSEapQ 286
Cdd:COG1020 632 PKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFDASVWE-IFGALLSGATLVLAPPEARRdpAALAELLARH--R 708
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 287 ITVFMAVPTVYSKLLDYYDKHFTqphvqdfvravckeRIRLMVSGSAALPVPLLEKWRSATGHT-LLERYGMTE------ 359
Cdd:COG1020 709 VTVLNLTPSLLRALLDAAPEALP--------------SLRLVLVGGEALPPELVRRWRARLPGArLVNLYGPTEttvdst 774
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 360 IGMALSNPLTEARVPgsVGTPLPGVEVRIIsenpqkgspyiihaegNERGTKVTPGFeekEGELLVRGPSVFREYWDKPE 439
Cdd:COG1020 775 YYEVTPPDADGGSVP--IGRPIANTRVYVL----------------DAHLQPVPVGV---PGELYIGGAGLARGYLNRPE 833
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 440 ETKSAFTSDG-------WFRTGDTavfkdARYW----------------IRG-RtsvdiIKTGgykvsalEIERHLLAHP 495
Cdd:COG1020 834 LTAERFVADPfgfpgarLYRTGDL-----ARWLpdgnleflgraddqvkIRGfR-----IELG-------EIEAALLQHP 896
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 496 SITDVAVIGVPDMTWGQRVTAVVALQEGHSLSHGDLKEWARGVLAPYAVPSELLLVEEIPRNQMGKVNKKELLKQLYPSG 575
Cdd:COG1020 897 GVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAAAAA 976
|
....*
gi 1720427507 576 QRSQP 580
Cdd:COG1020 977 AAAAA 981
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
52-564 |
1.46e-49 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 180.35 E-value: 1.46e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 52 AFGDRIALIdkYGHH----TYRELYDRSLCLAQEICRLqGCKVGDlqeeRVSFLCSNDVSYVVAQWASWMSGGVAVPLYW 127
Cdd:PRK12583 30 RFPDREALV--VRHQalryTWRQLADAVDRLARGLLAL-GVQPGD----RVGIWAPNCAEWLLTQFATARIGAILVNINP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 128 KHPEAQLEYFIQDSRSSLVVV-----GQEYLERLSPLAQRL-----------------GVPLLPLTPA----VYH---GA 178
Cdd:PRK12583 103 AYRASELEYALGQSGVRWVICadafkTSDYHAMLQELLPGLaegqpgalacerlpelrGVVSLAPAPPpgflAWHelqAR 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 179 TEKPTEQPVEE---SGWRDRGAMIFYTSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVNKLL 255
Cdd:PRK12583 183 GETVSREALAErqaSLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPVPLYHCFGMVLANL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 256 CPLWVGAtCVMLP--EFSAQQVWEkflSSEAPQITVFMAVPTVYSKLLDYYD-KHFtqphvqDFvravckERIRLMVSGS 332
Cdd:PRK12583 263 GCMTVGA-CLVYPneAFDPLATLQ---AVEEERCTALYGVPTMFIAELDHPQrGNF------DL------SSLRTGIMAG 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 333 AALPVPLLEKwrsatghtLLERYGMTEI----GMALSNPLT---------EARVPgSVGTPLPGVEVRiisenpqkgspy 399
Cdd:PRK12583 327 APCPIEVMRR--------VMDEMHMAEVqiayGMTETSPVSlqttaaddlERRVE-TVGRTQPHLEVK------------ 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 400 IIHAEGNergtKVTPGfeeKEGELLVRGPSVFREYWDKPEETKSAFTSDGWFRTGDTAVFKDARYW-IRGRtSVDIIKTG 478
Cdd:PRK12583 386 VVDPDGA----TVPRG---EIGELCTRGYSVMKGYWNNPEATAESIDEDGWMHTGDLATMDEQGYVrIVGR-SKDMIIRG 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 479 GYKVSALEIERHLLAHPSITDVAVIGVPDMTWGQRVTAVVALQEGHSLSHGDLKEWARGVLAPYAVPSELLLVEEIPRNQ 558
Cdd:PRK12583 458 GENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHPGHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTV 537
|
....*.
gi 1720427507 559 MGKVNK 564
Cdd:PRK12583 538 TGKVQK 543
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
55-570 |
1.49e-49 |
|
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.
Pssm-ID: 211788 [Multi-domain] Cd Length: 517 Bit Score: 179.59 E-value: 1.49e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 55 DRIALIDKYGHHTYRELYDRSLCLAQEICRLqGCKVGdlqeERVSFLCSNDVSYVVAQWASWMSGGVAVPLYWKHPEAQL 134
Cdd:TIGR03098 15 DATALVHHDRTLTYAALSERVLALASGLRGL-GLARG----ERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 135 EYFIQDSRSSLVVVGQEYLERLSP-LAQRLGVPLLPLTPAVYHGATEKPTEQPV-----EESGWRDRG--------AMIF 200
Cdd:TIGR03098 90 AHILADCNVRLLVTSSERLDLLHPaLPGCHDLRTLIIVGDPAHASEGHPGEEPAswpklLALGDADPPhpvidsdmAAIL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 201 YTSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGvVNKLLCPLWVGATCVMLPEFSAQQVWEkfl 280
Cdd:TIGR03098 170 YTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPLSFDYG-FNQLTTAFYVGATVVLHDYLLPRDVLK--- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 281 SSEAPQITVFMAVPTVYSKLLDYYDKHFTQPHvqdfvravckerIRLMVSGSAALPVPLLEKWRSATGHT-LLERYGMTE 359
Cdd:TIGR03098 246 ALEKHGITGLAAVPPLWAQLAQLDWPESAAPS------------LRYLTNSGGAMPRATLSRLRSFLPNArLFLMYGLTE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 360 IGMALSNPLTEA-RVPGSVGTPLPGVEVRIIsenpqkgspyiihaegNERGTKVTPGfeeKEGELLVRGPSVFREYWDKP 438
Cdd:TIGR03098 314 AFRSTYLPPEEVdRRPDSIGKAIPNAEVLVL----------------REDGSECAPG---EEGELVHRGALVAMGYWNDP 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 439 EETKSAFTSDGWFRTG----DTAVFKDARYW--------IRGRTSvDIIKTGGYKVSALEIERHLLAHPSITDVAVIGVP 506
Cdd:TIGR03098 375 EKTAERFRPLPPFPGElhlpELAVWSGDTVRrdeegflyFVGRRD-EMIKTSGYRVSPTEVEEVAYATGLVAEAVAFGVP 453
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720427507 507 DMTWGQRVTAVVALQEGHSLSHGDLKEWARGVLAPYAVPSELLLVEEIPRNQMGKVNKKELLKQ 570
Cdd:TIGR03098 454 DPTLGQAIVLVVTPPGGEELDRAALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKALAKE 517
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
52-561 |
3.26e-49 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 178.93 E-value: 3.26e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 52 AFGDRIALIDKYGHHTYRELYDRSLCLAQEIcRLQGCKVGDlqeeRVSFLCSNDVSYVVAQWASWMSGGVAVPLYWKHPE 131
Cdd:PRK07798 15 AVPDRVALVCGDRRLTYAELEERANRLAHYL-IAQGLGPGD----HVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 132 AQLEYFIQDSRSSLVVVGQEYLERLSPLAQRL-----------GVPLLPLTPAV-YHGA-TEKPTEQPVEESGWRDRgaM 198
Cdd:PRK07798 90 DELRYLLDDSDAVALVYEREFAPRVAEVLPRLpklrtlvvvedGSGNDLLPGAVdYEDAlAAGSPERDFGERSPDDL--Y 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 199 IFYTSGTTGRPKGALSTHRNL-------AAVVTG--------LVHSWAWTKNDVILHVLPLHHVHGVVNKLLCpLWVGAT 263
Cdd:PRK07798 168 LLYTGGTTGMPKGVMWRQEDIfrvllggRDFATGepiedeeeLAKRAAAGPGMRRFPAPPLMHGAGQWAAFAA-LFSGQT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 264 CVMLP--EFSAQQVWEkflSSEAPQITVFMAVPTVYSK-LLDYYDkhftQPHVQDFvravckERIRLMVSGSAALPVPLL 340
Cdd:PRK07798 247 VVLLPdvRFDADEVWR---TIEREKVNVITIVGDAMARpLLDALE----ARGPYDL------SSLFAIASGGALFSPSVK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 341 EKWRSATGH-TLLERYGMTEIG-MALSnplTEARVPGSVGTPL--PGVEVRIISENpqkgspyiihaegnerGTKVTPGf 416
Cdd:PRK07798 314 EALLELLPNvVLTDSIGSSETGfGGSG---TVAKGAVHTGGPRftIGPRTVVLDED----------------GNPVEPG- 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 417 EEKEGeLLVRGPSVFREYWDKPEETKSAF-TSDG--WFRTGDTA-VFKDARYWIRGRTSVdIIKTGGYKVSALEIERHLL 492
Cdd:PRK07798 374 SGEIG-WIARRGHIPLGYYKDPEKTAETFpTIDGvrYAIPGDRArVEADGTITLLGRGSV-CINTGGEKVFPEEVEEALK 451
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720427507 493 AHPSITDVAVIGVPDMTWGQRVTAVVALQEGHSLSHGDLKEWARGVLAPYAVPSELLLVEEIPRNQMGK 561
Cdd:PRK07798 452 AHPDVADALVVGVPDERWGQEVVAVVQLREGARPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
44-567 |
2.09e-48 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 177.17 E-value: 2.09e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 44 VPVFIRALA-FGDRIALIDKYGHHTYRELYDRSLCLAQEICRLQGCKVGDlqeeRVSFLCSNDVSYVVAQWASWMSGGVA 122
Cdd:PRK08974 26 VDMFEQAVArYADQPAFINMGEVMTFRKLEERSRAFAAYLQNGLGLKKGD----RVALMMPNLLQYPIALFGILRAGMIV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 123 V---PLYwkHPEaQLEYFIQDSRSSLVVVGQEY---LERL-------SPLAQRLG---------------------VPLL 168
Cdd:PRK08974 102 VnvnPLY--TPR-ELEHQLNDSGAKAIVIVSNFahtLEKVvfktpvkHVILTRMGdqlstakgtlvnfvvkyikrlVPKY 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 169 PLTPAV-YHGATEKPTE-QPVEESGWRDRGAMIFYTSGTTGRPKGALSTHRNLAAVVtgLVHSWAW-----TKNDVILHV 241
Cdd:PRK08974 179 HLPDAIsFRSALHKGRRmQYVKPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANL--EQAKAAYgpllhPGKELVVTA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 242 LPLHHVHGV-VNKLLCpLWVGATCVM------LPEFSAQQVWEKFlsseapqiTVFMAVPTVYSKLLDyyDKHFTQphvQ 314
Cdd:PRK08974 257 LPLYHIFALtVNCLLF-IELGGQNLLitnprdIPGFVKELKKYPF--------TAITGVNTLFNALLN--NEEFQE---L 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 315 DFvravckERIRLMVSGSAALPVPLLEKWRSATGHTLLERYGMTEIGMALS-NPLTEARVPGSVGTPLPGVEVRIISEnp 393
Cdd:PRK08974 323 DF------SSLKLSVGGGMAVQQAVAERWVKLTGQYLLEGYGLTECSPLVSvNPYDLDYYSGSIGLPVPSTEIKLVDD-- 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 394 qkgspyiihaEGNErgtkVTPGfeeKEGELLVRGPSVFREYWDKPEETKSAFtSDGWFRTGDTAVFkDARYWIR--GRTS 471
Cdd:PRK08974 395 ----------DGNE----VPPG---EPGELWVKGPQVMLGYWQRPEATDEVI-KDGWLATGDIAVM-DEEGFLRivDRKK 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 472 vDIIKTGGYKVSALEIERHLLAHPSITDVAVIGVPDMTWGQRVTAVVALQEgHSLSHGDLKEWARGVLAPYAVPSELLLV 551
Cdd:PRK08974 456 -DMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFVVKKD-PSLTEEELITHCRRHLTGYKVPKLVEFR 533
|
570
....*....|....*.
gi 1720427507 552 EEIPRNQMGKVNKKEL 567
Cdd:PRK08974 534 DELPKSNVGKILRREL 549
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
67-571 |
2.49e-48 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 176.88 E-value: 2.49e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 67 TYRELYDRSLCLAQEICRLQGCKVGDlqeeRVSFLCSNDVSYVVAQWASWMSGGVAV---PLYwkhPEAQLEYFIQDSRS 143
Cdd:PRK05677 51 TYGELYKLSGAFAAWLQQHTDLKPGD----RIAVQLPNVLQYPVAVFGAMRAGLIVVntnPLY---TAREMEHQFNDSGA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 144 SLVVV-------GQEYLER--------------LSPLAQRL----------GVPLLPLTPAV-YHGATEKPTEQPVEE-S 190
Cdd:PRK05677 124 KALVClanmahlAEKVLPKtgvkhvivtevadmLPPLKRLLinavvkhvkkMVPAYHLPQAVkFNDALAKGAGQPVTEaN 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 191 GWRDRGAMIFYTSGTTGRPKGALSTHRNLAAVVT---GLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVML 267
Cdd:PRK05677 204 PQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLqcrALMGSNLNEGCEILIAPLPLYHIYAFTFHCMAMMLIGNHNILI 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 268 PEFSAQQVWEKFLSSEapQITVFMAVPTVYSKLLdyydkhftqpHVQDFvRAVCKERIRLMVSGSAALPVPLLEKWRSAT 347
Cdd:PRK05677 284 SNPRDLPAMVKELGKW--KFSGFVGLNTLFVALC----------NNEAF-RKLDFSALKLTLSGGMALQLATAERWKEVT 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 348 GHTLLERYGMTEIG-MALSNPLtEARVPGSVGTPLPGVEVRIISEnpqkgspyiihaEGNErgtkVTPGfeeKEGELLVR 426
Cdd:PRK05677 351 GCAICEGYGMTETSpVVSVNPS-QAIQVGTIGIPVPSTLCKVIDD------------DGNE----LPLG---EVGELCVK 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 427 GPSVFREYWDKPEETKSAFTSDGWFRTGDTAVFKDARYW-IRGRTSvDIIKTGGYKVSALEIERHLLAHPSITDVAVIGV 505
Cdd:PRK05677 411 GPQVMKGYWQRPEATDEILDSDGWLKTGDIALIQEDGYMrIVDRKK-DMILVSGFNVYPNELEDVLAALPGVLQCAAIGV 489
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 506 PDMTWGQRVTAVVALQEGHSLSHGDLKEWARGVLAPYAVPSELLLVEEIPRNQMGKVNKKEL----LKQL 571
Cdd:PRK05677 490 PDEKSGEAIKVFVVVKPGETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRRELrdeeLKKA 559
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
50-567 |
2.52e-46 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 171.15 E-value: 2.52e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 50 ALAFGDRIALIDKYGH--HTYRELYDRSLCLAQEICRLqGCKVGDlqeeRVSFLCSNDVSYVVAQWASWMSGGVAV---P 124
Cdd:PRK08315 26 AARYPDREALVYRDQGlrWTYREFNEEVDALAKGLLAL-GIEKGD----RVGIWAPNVPEWVLTQFATAKIGAILVtinP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 125 LYWKHpeaQLEYFIQDSRSSLVVV-----GQEYLERLSPLA--------QRLGVPLLP-LTPAVYHGATEKPTEQPVEEs 190
Cdd:PRK08315 101 AYRLS---ELEYALNQSGCKALIAadgfkDSDYVAMLYELApelatcepGQLQSARLPeLRRVIFLGDEKHPGMLNFDE- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 191 gWRDRGAM--------------------IFYTSGTTGRPKGALSTHRNL---AAVVTGLVHswaWTKNDVILHVLPLHHV 247
Cdd:PRK08315 177 -LLALGRAvddaelaarqatldpddpinIQYTSGTTGFPKGATLTHRNIlnnGYFIGEAMK---LTEEDRLCIPVPLYHC 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 248 HGVVNKLLCPLWVGATCV-MLPEFSAQQVWEkflSSEAPQITVFMAVPTVYSKLLDYYD-KHFtqphvqDFvravckERI 325
Cdd:PRK08315 253 FGMVLGNLACVTHGATMVyPGEGFDPLATLA---AVEEERCTALYGVPTMFIAELDHPDfARF------DL------SSL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 326 RLMVSGSAALPVPLLEKwrsatghtLLERYGMTEI----GMALSNPLT---------EARVpGSVGTPLPGVEVRIISEn 392
Cdd:PRK08315 318 RTGIMAGSPCPIEVMKR--------VIDKMHMSEVtiayGMTETSPVStqtrtddplEKRV-TTVGRALPHLEVKIVDP- 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 393 pqkgspyiihaegnERGTKVTPGfeeKEGELLVRGPSVFREYWDKPEETKSAFTSDGWFRTGDTAVFKDARYW-IRGRTS 471
Cdd:PRK08315 388 --------------ETGETVPRG---EQGELCTRGYSVMKGYWNDPEKTAEAIDADGWMHTGDLAVMDEEGYVnIVGRIK 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 472 vDIIKTGGYKVSALEIERHLLAHPSITDVAVIGVPDMTWGQRVTAVVALQEGHSLSHGDLKEWARGVLAPYAVPSELLLV 551
Cdd:PRK08315 451 -DMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGATLTEEDVRDFCRGKIAHYKIPRYIRFV 529
|
570
....*....|....*.
gi 1720427507 552 EEIPRNQMGKVNKKEL 567
Cdd:PRK08315 530 DEFPMTVTGKIQKFKM 545
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
54-568 |
3.33e-46 |
|
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: 168.77 E-value: 3.33e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 54 GDRIALIDKyGHHTYRELYDRslclaqeicrlqgckvgdlqeervsflcsndVSYvvaqwASWMSGGVAVPLYWKHPEAQ 133
Cdd:cd05922 18 GERVVLILP-NRFTYIELSFA-------------------------------VAY-----AGGRLGLVFVPLNPTLKESV 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 134 LEYFIQDSRSSLVVVGQEYLERLsplaqRLGVPLLPLTPAVYhgatekpteqpvEESGWRDRG-------------AMIF 200
Cdd:cd05922 61 LRYLVADAGGRIVLADAGAADRL-----RDALPASPDPGTVL------------DADGIRAARasapahevshedlALLL 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 201 YTSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVvNKLLCPLWVGATCVMLPEFS-AQQVWEKF 279
Cdd:cd05922 124 YTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDRALTVLPLSYDYGL-SVLNTHLLRGATLVLTNDGVlDDAFWEDL 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 280 LSSeapQITVFMAVPTVYSKLLDYYDKHFTQPHvqdfvravckerIRLMVSGSAALPVPLLEKWRSA-TGHTLLERYGMT 358
Cdd:cd05922 203 REH---GATGLAGVPSTYAMLTRLGFDPAKLPS------------LRYLTQAGGRLPQETIARLRELlPGAQVYVMYGQT 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 359 EI--GMALSNPLTEARVPGSVGTPLPGVEVRIIsenpqkgspyiihaegNERGTKVTPGfeeKEGELLVRGPSVFREYWD 436
Cdd:cd05922 268 EAtrRMTYLPPERILEKPGSIGLAIPGGEFEIL----------------DDDGTPTPPG---EPGEIVHRGPNVMKGYWN 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 437 KPEETKSAFTSDGWFRTGDTAVF-KDARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSITDVAVIGVPDmTWGQRVT 515
Cdd:cd05922 329 DPPYRRKEGRGGGVLHTGDLARRdEDGFLFIVGRRD-RMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPD-PLGEKLA 406
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1720427507 516 AVVALQEGHSLShgDLKEWARGVLAPYAVPSELLLVEEIPRNQMGKVNKKELL 568
Cdd:cd05922 407 LFVTAPDKIDPK--DVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
55-567 |
4.01e-46 |
|
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: 168.64 E-value: 4.01e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 55 DRIALIDKYGHHTYRELYDRSLCLAQeicRLQGCKVGdlQEERVSFLCSNDVSYVVAQWASWMSGGVAVPLYWKHPEAQL 134
Cdd:cd17643 2 EAVAVVDEDRRLTYGELDARANRLAR---TLRAEGVG--PGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 135 EYFIQDSRSSLVVVgqeylerlsplaqrlgvpllpltpavyhgatekpteQPveesgwrDRGAMIFYTSGTTGRPKGALS 214
Cdd:cd17643 77 AFILADSGPSLLLT------------------------------------DP-------DDLAYVIYTSGSTGRPKGVVV 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 215 THRNLAAVVTGLVHSWAWTKNDVilhVLPLHH---------VHGvvnkllcPLWVGATCVMLPEF---SAQQVWEkFLSS 282
Cdd:cd17643 114 SHANVLALFAATQRWFGFNEDDV---WTLFHSyafdfsvweIWG-------ALLHGGRLVVVPYEvarSPEDFAR-LLRD 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 283 EapQITVFMAVPTVYSKLLDYYDKHFTQPHvqdfvravckeRIRLMVSGSAALPVPLLEKWRSATGH---TLLERYGMTE 359
Cdd:cd17643 183 E--GVTVLNQTPSAFYQLVEAADRDGRDPL-----------ALRYVIFGGEALEAAMLRPWAGRFGLdrpQLVNMYGITE 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 360 IGMALS-NPLTEARVPGS----VGTPLPGVEVRIISENpqkgspyiihaegnerGTKVTPGfeeKEGELLVRGPSVFREY 434
Cdd:cd17643 250 TTVHVTfRPLDAADLPAAaaspIGRPLPGLRVYVLDAD----------------GRPVPPG---VVGELYVSGAGVARGY 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 435 WDKPEETKSAFTSDGW-------FRTGDTAVFK-DARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSITDVAVIGVP 506
Cdd:cd17643 311 LGRPELTAERFVANPFggpgsrmYRTGDLARRLpDGELEYLGRAD-EQVKIRGFRIELGEIEAALATHPSVRDAAVIVRE 389
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720427507 507 DMTWGQRVTAVVALQEGHSLSHGDLKEWARGVLAPYAVPSELLLVEEIPRNQMGKVNKKEL 567
Cdd:cd17643 390 DEPGDTRLVAYVVADDGAAADIAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
49-567 |
6.37e-46 |
|
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: 168.53 E-value: 6.37e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 49 RALAFGDRIALIDKYGHHTYRELYDRSLCLAQeicRLQGCKVGdlQEERVSFLCSNDVSYVVAQWASWMSGGVAVPLYWK 128
Cdd:cd12117 6 QAARTPDAVAVVYGDRSLTYAELNERANRLAR---RLRAAGVG--PGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 129 HPEAQLEYFIQDSRSSLVVVgqeylerLSPLAQRLGVPLLPLTPAVyHGATEKPTEQPVEESGwrDRGAMIFYTSGTTGR 208
Cdd:cd12117 81 LPAERLAFMLADAGAKVLLT-------DRSLAGRAGGLEVAVVIDE-ALDAGPAGNPAVPVSP--DDLAYVMYTSGSTGR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 209 PKGALSTHRNlaavVTGLVHSWAW---TKNDVILHVLPL------HHVHGvvnkllcPLWVGATCVMLPE---FSAQQVw 276
Cdd:cd12117 151 PKGVAVTHRG----VVRLVKNTNYvtlGPDDRVLQTSPLafdastFEIWG-------ALLNGARLVLAPKgtlLDPDAL- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 277 EKFLssEAPQITVFMAVPTVYSKLLDyydkhftqphvqdfVRAVCKERIRLMVSGSAALPVPLLEKWRSATGH-TLLERY 355
Cdd:cd12117 219 GALI--AEEGVTVLWLTAALFNQLAD--------------EDPECFAGLRELLTGGEVVSPPHVRRVLAACPGlRLVNGY 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 356 GMTE-IGMALSNPLTE-ARVPGSV--GTPLPGVEVRIIsenpqkgspyiihaegNERGTKVTPGfeeKEGELLVRGPSVF 431
Cdd:cd12117 283 GPTEnTTFTTSHVVTElDEVAGSIpiGRPIANTRVYVL----------------DEDGRPVPPG---VPGELYVGGDGLA 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 432 REYWDKPEETKSAFTSDGW------FRTGDTAVFK-DARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSITDVAVIG 504
Cdd:cd12117 344 LGYLNRPALTAERFVADPFgpgerlYRTGDLARWLpDGRLEFLGRID-DQVKIRGFRIELGEIEAALRAHPGVREAVVVV 422
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720427507 505 VPDMTWGQRVTA-VVAlqeGHSLSHGDLKEWARGVLAPYAVPSELLLVEEIPRNQMGKVNKKEL 567
Cdd:cd12117 423 REDAGGDKRLVAyVVA---EGALDAAELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
46-571 |
7.59e-46 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 169.39 E-value: 7.59e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 46 VFIRALAFGDRIALID-KYGH-HTYRELYDRSLCLAQEICRLqGCKVGDlqeeRVSFLCSNDVSYVVAQWASWMSGGV-- 121
Cdd:PLN02246 29 CFERLSEFSDRPCLIDgATGRvYTYADVELLSRRVAAGLHKL-GIRQGD----VVMLLLPNCPEFVLAFLGASRRGAVtt 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 122 -AVPLYwkhPEAQLEYFIQDSRSSLVVVGQEYLERLSPLAQRLGVPLLPLTPAV-----YHGATEKPTEQPVEESGWRDR 195
Cdd:PLN02246 104 tANPFY---TPAEIAKQAKASGAKLIITQSCYVDKLKGLAEDDGVTVVTIDDPPegclhFSELTQADENELPEVEISPDD 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 196 GAMIFYTSGTTGRPKGALSTHRNL----AAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFS 271
Cdd:PLN02246 181 VVALPYSSGTTGLPKGVMLTHKGLvtsvAQQVDGENPNLYFHSDDVILCVLPMFHIYSLNSVLLCGLRVGAAILIMPKFE 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 272 AQQVWEKFlssEAPQITVFMAVPTVY-----SKLLDYYDKhftqphvqdfvravckERIRLMVSGSAALPVPLLEKWRSA 346
Cdd:PLN02246 261 IGALLELI---QRHKVTIAPFVPPIVlaiakSPVVEKYDL----------------SSIRMVLSGAAPLGKELEDAFRAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 347 -TGHTLLERYGMTEIGMALSNPLTEARVP-----GSVGTPLPGVEVRIIseNPQKGS--PYiihaegnergtkvtpgfeE 418
Cdd:PLN02246 322 lPNAVLGQGYGMTEAGPVLAMCLAFAKEPfpvksGSCGTVVRNAELKIV--DPETGAslPR------------------N 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 419 KEGELLVRGPSVFREYWDKPEETKSAFTSDGWFRTGDTA-VFKDARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSI 497
Cdd:PLN02246 382 QPGEICIRGPQIMKGYLNDPEATANTIDKDGWLHTGDIGyIDDDDELFIVDRLK-ELIKYKGFQVAPAELEALLISHPSI 460
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720427507 498 TDVAVIGVPDMTWGQRVTAVVALQEGHSLSHGDLKEWARGVLAPYAVPSELLLVEEIPRNQMGKVNKKELLKQL 571
Cdd:PLN02246 461 ADAAVVPMKDEVAGEVPVAFVVRSNGSEITEDEIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDLRAKL 534
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
67-571 |
3.77e-45 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 168.05 E-value: 3.77e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 67 TYRELYDRSLCLAQEICRLqGCKVGDlqeeRVSFLCSNDVSYVvaQW--ASWMSGGVAVPL-Y-WKHPEAQLEyfIQDSR 142
Cdd:PLN02860 34 TGHEFVDGVLSLAAGLLRL-GLRNGD----VVAIAALNSDLYL--EWllAVACAGGIVAPLnYrWSFEEAKSA--MLLVR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 143 SSLVVVGQE----YLE----RLSPLaqRLGVPLLPLTPAVYHGATEKPTEQPVEESG---------WR-DRGAMIFYTSG 204
Cdd:PLN02860 105 PVMLVTDETcsswYEElqndRLPSL--MWQVFLESPSSSVFIFLNSFLTTEMLKQRAlgtteldyaWApDDAVLICFTSG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 205 TTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVvNKLLCPLWVGATCVMLPEFSAQQVWEKFlssEA 284
Cdd:PLN02860 183 TTGRPKGVTISHSALIVQSLAKIAIVGYGEDDVYLHTAPLCHIGGL-SSALAMLMVGACHVLLPKFDAKAALQAI---KQ 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 285 PQITVFMAVPTVYSKLLDYYDKHFTQPhvqdfvravCKERIRLMVSGSAALPVPLLEKWRSATGHT-LLERYGMTEIGMA 363
Cdd:PLN02860 259 HNVTSMITVPAMMADLISLTRKSMTWK---------VFPSVRKILNGGGSLSSRLLPDAKKLFPNAkLFSAYGMTEACSS 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 364 LS-NPLTEARVPGSVGTPLPGVEVRIISENPQKGS------PyiiHAEgnergTKVTPGFEEKEGELLVRGPSVFREYWD 436
Cdd:PLN02860 330 LTfMTLHDPTLESPKQTLQTVNQTKSSSVHQPQGVcvgkpaP---HVE-----LKIGLDESSRVGRILTRGPHVMLGYWG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 437 KPEETKSAFTSDGWFRTGDTAVFKDA-RYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSITDVAVIGVPDMTWGQRVT 515
Cdd:PLN02860 402 QNSETASVLSNDGWLDTGDIGWIDKAgNLWLIGRSN-DRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVV 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720427507 516 AVVALQEGHSLSHGDLKEWARGV---------------LAPYAVPSELLLVEE-IPRNQMGKVNKKELLKQL 571
Cdd:PLN02860 481 ACVRLRDGWIWSDNEKENAKKNLtlssetlrhhcreknLSRFKIPKLFVQWRKpFPLTTTGKIRRDEVRREV 552
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
49-567 |
3.90e-45 |
|
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341301 [Multi-domain] Cd Length: 488 Bit Score: 166.68 E-value: 3.90e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 49 RALAFGDRIALIDKYGHHTYRELYDRSLCLAQEIcRLQGCKVGDlqeeRVSFLCSNDVSYVVAQWASWMSGGVAVPLYWK 128
Cdd:cd17646 7 QAARTPDAPAVVDEGRTLTYRELDERANRLAHLL-RARGVGPED----RVAVLLPRSADLVVALLAVLKAGAAYLPLDPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 129 HPEAQLEYFIQDSRSSLVVVGqeylerlsPLAQRLGVPLLPLTPAVYHGATEKPTEQPVEESGwRDRGAMIFYTSGTTGR 208
Cdd:cd17646 82 YPADRLAYMLADAGPAVVLTT--------ADLAARLPAGGDVALLGDEALAAPPATPPLVPPR-PDNLAYVIYTSGSTGR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 209 PKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLhhvhGV---VNKLLCPLWVGATCVML-------PEFSAQQVWEK 278
Cdd:cd17646 153 PKGVMVTHAGIVNRLLWMQDEYPLGPGDRVLQKTPL----SFdvsVWELFWPLVAGARLVVArpgghrdPAYLAALIREH 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 279 flsseapQITVFMAVPTVYSKLLDYydkhftqphvqdfVRAVCKERIRLMVSGSAALPVPLLEKWRSATGHTLLERYGMT 358
Cdd:cd17646 229 -------GVTTCHFVPSMLRVFLAE-------------PAAGSCASLRRVFCSGEALPPELAARFLALPGAELHNLYGPT 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 359 EIGMALSNPLTEARVPGS---VGTPLPGVEVRIIsenpqkgspyiihaegNERGTKVTPGFEekeGELLVRGPSVFREYW 435
Cdd:cd17646 289 EAAIDVTHWPVRGPAETPsvpIGRPVPNTRLYVL----------------DDALRPVPVGVP---GELYLGGVQLARGYL 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 436 DKPEETKSAFTSDgWF-------RTGDTAVFK-DARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSITDVAVIGVPD 507
Cdd:cd17646 350 GRPALTAERFVPD-PFgpgsrmyRTGDLARWRpDGALEFLGRSD-DQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAA 427
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720427507 508 MTWGQRVTAVVALQEGHS-LSHGDLKEWARGVLAPYAVPSELLLVEEIPRNQMGKVNKKEL 567
Cdd:cd17646 428 PAGAARLVGYVVPAAGAAgPDTAALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
185-567 |
1.58e-44 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 166.54 E-value: 1.58e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 185 QPVEESgwRDRGAMIFYTSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKND----------VILHVLPLHHVHGVVNKL 254
Cdd:PRK12492 200 KPVPVG--LDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSQLGPDgqplmkegqeVMIAPLPLYHIYAFTANC 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 255 LCPLWVGATCVML------PEFSAQ-QVWekflsseapQITVFMAVPTVYSKLLDYYDkhFTQphvQDFvravckERIRL 327
Cdd:PRK12492 278 MCMMVSGNHNVLItnprdiPGFIKElGKW---------RFSALLGLNTLFVALMDHPG--FKD---LDF------SALKL 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 328 MVSGSAALPVPLLEKWRSATGHTLLERYGMTEIG-MALSNPLTEARVPGSVGTPLPGVEVRIISEnpqkgspyiihaEGN 406
Cdd:PRK12492 338 TNSGGTALVKATAERWEQLTGCTIVEGYGLTETSpVASTNPYGELARLGTVGIPVPGTALKVIDD------------DGN 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 407 ERGtkvtpgFEEKeGELLVRGPSVFREYWDKPEETKSAFTSDGWFRTGDTAVF-KDARYWIRGRTSvDIIKTGGYKVSAL 485
Cdd:PRK12492 406 ELP------LGER-GELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIdPDGFVRIVDRKK-DLIIVSGFNVYPN 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 486 EIERHLLAHPSITDVAVIGVPDMTWGQRVTAVVALQEGhSLSHGDLKEWARGVLAPYAVPSELLLVEEIPRNQMGKVNKK 565
Cdd:PRK12492 478 EIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVVARDP-GLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRR 556
|
..
gi 1720427507 566 EL 567
Cdd:PRK12492 557 EL 558
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
29-567 |
1.94e-44 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 166.17 E-value: 1.94e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 29 HSLLPTTPEAHTDGSVPVFIRALAFGDRiALIDKYGHH--TYRELYDRSLCLAQEICRLQGCKVGDLqeerVSFLCSNDV 106
Cdd:PLN02574 29 HPPVPLPSDPNLDAVSFIFSHHNHNGDT-ALIDSSTGFsiSYSELQPLVKSMAAGLYHVMGVRQGDV----VLLLLPNSV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 107 SYVVAQWASWMSGGVAVPLYWKHPEAQLEYFIQDSRSSLVVVGQEYLERLSPLaqrlGVPLLPLTPAVYH--GATEKPTE 184
Cdd:PLN02574 104 YFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFTSPENVEKLSPL----GVPVIGVPENYDFdsKRIEFPKF 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 185 QPV--EESGW-------RDRGAMIFYTSGTTGRPKGALSTHRNLAAVVTGLV------HSWAWTKNdVILHVLPLHHVHG 249
Cdd:PLN02574 180 YELikEDFDFvpkpvikQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVrfeasqYEYPGSDN-VYLAALPMFHIYG 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 250 VVNKLLCPLWVGATCVMLPEFSAQ---QVWEKFlsseapQITVFMAVPTVYSKLLdyydkHFTQPhvqdfVRAVCKERIR 326
Cdd:PLN02574 259 LSLFVVGLLSLGSTIVVMRRFDASdmvKVIDRF------KVTHFPVVPPILMALT-----KKAKG-----VCGEVLKSLK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 327 LMVSGSAALPVPLLEKWRSATGHT-LLERYGMTE---IGMALSNPlTEARVPGSVGTPLPGVEVRIISEnpqkgspyiih 402
Cdd:PLN02574 323 QVSCGAAPLSGKFIQDFVQTLPHVdFIQGYGMTEstaVGTRGFNT-EKLSKYSSVGLLAPNMQAKVVDW----------- 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 403 aegnERGTKVTPGfeeKEGELLVRGPSVFREYWDKPEETKSAFTSDGWFRTGDTAVF-KDARYWIRGRTSvDIIKTGGYK 481
Cdd:PLN02574 391 ----STGCLLPPG---NCGELWIQGPGVMKGYLNNPKATQSTIDKDGWLRTGDIAYFdEDGYLYIVDRLK-EIIKYKGFQ 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 482 VSALEIERHLLAHPSITDVAVIGVPDMTWGQRVTAVVALQEGHSLSHGDLKEWARGVLAPYAVPSELLLVEEIPRNQMGK 561
Cdd:PLN02574 463 IAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGSTLSQEAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGK 542
|
....*.
gi 1720427507 562 VNKKEL 567
Cdd:PLN02574 543 ILRREL 548
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
197-567 |
6.29e-44 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 164.66 E-value: 6.29e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 197 AMIFYTSGTTGRPKGALSTHRNLAAVVTGlVHSWAWTKN------DVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEF 270
Cdd:PRK08751 211 AFLQYTGGTTGVAKGAMLTHRNLVANMQQ-AHQWLAGTGkleegcEVVITALPLYHIFALTANGLVFMKIGGCNHLISNP 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 271 SAQQVWEKFLssEAPQITVFMAVPTVYSKLLDyyDKHFTQphvQDFvravckERIRLMVSGSAALPVPLLEKWRSATGHT 350
Cdd:PRK08751 290 RDMPGFVKEL--KKTRFTAFTGVNTLFNGLLN--TPGFDQ---IDF------SSLKMTLGGGMAVQRSVAERWKQVTGLT 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 351 LLERYGMTEIG-MALSNPLTEARVPGSVGTPLPGVEVRIISENpqkgspyiihaegnerGTKVTPGfeeKEGELLVRGPS 429
Cdd:PRK08751 357 LVEAYGLTETSpAACINPLTLKEYNGSIGLPIPSTDACIKDDA----------------GTVLAIG---EIGELCIKGPQ 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 430 VFREYWDKPEETKSAFTSDGWFRTGDTAVF-KDARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSITDVAVIGVPDM 508
Cdd:PRK08751 418 VMKGYWKRPEETAKVMDADGWLHTGDIARMdEQGFVYIVDRKK-DMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDE 496
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720427507 509 TWGQrVTAVVALQEGHSLSHGDLKEWARGVLAPYAVPSELLLVEEIPRNQMGKVNKKEL 567
Cdd:PRK08751 497 KSGE-IVKVVIVKKDPALTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRREL 554
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
50-570 |
1.28e-43 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 163.58 E-value: 1.28e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 50 ALAFGDRIALIdkYG--HHTYRELYDRSLCLAQEICRLqGCKVGDlqeeRVSFLCSNDVSYVVAQWASWMSGGVAVPLYW 127
Cdd:PRK08162 28 AEVYPDRPAVI--HGdrRRTWAETYARCRRLASALARR-GIGRGD----TVAVLLPNIPAMVEAHFGVPMAGAVLNTLNT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 128 KHPEAQLEYFIQDSRSSLVVVGQEYLERLSPLAQRLGVPLLPL--------TPAVYHGATE--------KPT---EQPVE 188
Cdd:PRK08162 101 RLDAASIAFMLRHGEAKVLIVDTEFAEVAREALALLPGPKPLVidvddpeyPGGRFIGALDyeaflasgDPDfawTLPAD 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 189 EsgWrDRGAmIFYTSGTTGRPKGALSTHRN--LAAVVTGLvhSWAWTKNDVILHVLPLHHVHGvvnklLCPLW----VGA 262
Cdd:PRK08162 181 E--W-DAIA-LNYTSGTTGNPKGVVYHHRGayLNALSNIL--AWGMPKHPVYLWTLPMFHCNG-----WCFPWtvaaRAG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 263 TCVMLPEFSAQQVWEKFlssEAPQITVFMAVPTVYSKLLdyydkhftqpHVQDFVRAVCKERIRLMVSGsAALPVPLLEK 342
Cdd:PRK08162 250 TNVCLRKVDPKLIFDLI---REHGVTHYCGAPIVLSALI----------NAPAEWRAGIDHPVHAMVAG-AAPPAAVIAK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 343 WRSAtGHTLLERYGMTEI-GMALSN---------PLTE-ARVPGSVGTPLPGVE-VRIIseNPQKGSPyiIHAEGnergt 410
Cdd:PRK08162 316 MEEI-GFDLTHVYGLTETyGPATVCawqpewdalPLDErAQLKARQGVRYPLQEgVTVL--DPDTMQP--VPADG----- 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 411 kvtpgfeEKEGELLVRGPSVFREYWDKPEETKSAFtSDGWFRTGDTAVF-KDARYWIRGRtSVDIIKTGGYKVSALEIER 489
Cdd:PRK08162 386 -------ETIGEIMFRGNIVMKGYLKNPKATEEAF-AGGWFHTGDLAVLhPDGYIKIKDR-SKDIIISGGENISSIEVED 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 490 HLLAHPSITDVAVIGVPDMTWGQRVTAVVALQEGHSLSHGDLKEWARGVLAPYAVPSELLLvEEIPRNQMGKVNKKELLK 569
Cdd:PRK08162 457 VLYRHPAVLVAAVVAKPDPKWGEVPCAFVELKDGASATEEEIIAHCREHLAGFKVPKAVVF-GELPKTSTGKIQKFVLRE 535
|
.
gi 1720427507 570 Q 570
Cdd:PRK08162 536 Q 536
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
55-567 |
1.48e-43 |
|
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: 162.13 E-value: 1.48e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 55 DRIALIDKYGHHTYRELYDRSLCLAQeicRLQGCKVGDlqEERVSFLCSNDVSYVVAQWASWMSGGVAVPLYWKHPEAQL 134
Cdd:cd17651 10 DAPALVAEGRRLTYAELDRRANRLAH---RLRARGVGP--GDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 135 EYFIQDSRSSLVVVGQEylerlspLAQRLGVPLLPLTPAVYHGATEKPTEQPVEESGwRDRGAMIFYTSGTTGRPKGALS 214
Cdd:cd17651 85 AFMLADAGPVLVLTHPA-------LAGELAVELVAVTLLDQPGAAAGADAEPDPALD-ADDLAYVIYTSGSTGRPKGVVM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 215 THRNLA----------AVVTGL-VHSWAWTKNDVILHvlplhhvhgvvnKLLCPLWVGATCVMLPE---FSAQQVWEkFL 280
Cdd:cd17651 157 PHRSLAnlvawqarasSLGPGArTLQFAGLGFDVSVQ------------EIFSTLCAGATLVLPPEevrTDPPALAA-WL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 281 SSEAPQItVFMavPTVYSKLLDYYDKHFTQPHVqdfvravckeRIRLMVSGSAALPV-PLLEKW-RSATGHTLLERYGMT 358
Cdd:cd17651 224 DEQRISR-VFL--PTVALRALAEHGRPLGVRLA----------ALRYLLTGGEQLVLtEDLREFcAGLPGLRLHNHYGPT 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 359 E----IGMALSNPLTEARVPGSVGTPLPGVEVRIIsenpqkgspyiihaegNERGTKVTPGfeeKEGELLVRGPSVFREY 434
Cdd:cd17651 291 EthvvTALSLPGDPAAWPAPPPIGRPIDNTRVYVL----------------DAALRPVPPG---VPGELYIGGAGLARGY 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 435 WDKPEETKSAFTSDGW------FRTGDTAVF-KDARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSITDVAVIGVPD 507
Cdd:cd17651 352 LNRPELTAERFVPDPFvpgarmYRTGDLARWlPDGELEFLGRAD-DQVKIRGFRIELGEIEAALARHPGVREAVVLARED 430
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 508 MTWGQRVTAVVALQEGHSLSHGDLKEWARGVLAPYAVPSELLLVEEIPRNQMGKVNKKEL 567
Cdd:cd17651 431 RPGEKRLVAYVVGDPEAPVDAAELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRAL 490
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
55-567 |
1.52e-43 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 163.01 E-value: 1.52e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 55 DRIALIDKYGHHTYRELYDRSLCLAQEICRLQGCkvgdlQEERVSFLCSNDVSYVVAQWASWMSGGVAVPLYWKHPEAQL 134
Cdd:PRK13382 58 DRPGLIDELGTLTWRELDERSDALAAALQALPIG-----EPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPAL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 135 EYFIQDSRSSLVVVGQEYLERLS------PLAQRLGVPLLPLTPAVYHGATEKPTEQPVEESGwrDRGAMIFYTSGTTGR 208
Cdd:PRK13382 133 AEVVTREGVDTVIYDEEFSATVDraladcPQATRIVAWTDEDHDLTVEVLIAAHAGQRPEPTG--RKGRVILLTSGTTGT 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 209 PKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVNkLLCPLWVGATCVMLPEFSAQQVWEKFLSSEAPQIT 288
Cdd:PRK13382 211 PKGARRSGPGGIGTLKAILDRTPWRAEEPTVIVAPMFHAWGFSQ-LVLAASLACTIVTRRRFDPEATLDLIDRHRATGLA 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 289 VfmaVPTVYSKLLDYYDKhftqphvqdfVRAVCKER-IRLMVSGSAALPVPLLEKWRSATGHTLLERYGMTEIGM-ALSN 366
Cdd:PRK13382 290 V---VPVMFDRIMDLPAE----------VRNRYSGRsLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYNATEAGMiATAT 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 367 PLTEARVPGSVGTPLPGVEVRIISEnpqkgspyiihaEGNErgtkVTPGfeeKEGELLVRGPSVFREYwdKPEETKSafT 446
Cdd:PRK13382 357 PADLRAAPDTAGRPAEGTEIRILDQ------------DFRE----VPTG---EVGTIFVRNDTQFDGY--TSGSTKD--F 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 447 SDGWFRTGDTAVFKDA-RYWIRGRtSVDIIKTGGYKVSALEIERHLLAHPSITDVAVIGVPDMTWGQRVTAVVALQEGHS 525
Cdd:PRK13382 414 HDGFMASGDVGYLDENgRLFVVGR-DDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGAS 492
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1720427507 526 LSHGDLKEWARGVLAPYAVPSELLLVEEIPRNQMGKVNKKEL 567
Cdd:PRK13382 493 ATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRREL 534
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
53-567 |
1.91e-43 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 163.27 E-value: 1.91e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 53 FGDRIALIDKYGHHTYRELYDRSLCLAqeiCRLQ--GCKVGDlqeeRVSFLCSNDVSYVVAQWASWMSGGVAV---PLYW 127
Cdd:PRK07059 36 YADRPAFICMGKAITYGELDELSRALA---AWLQsrGLAKGA----RVAIMMPNVLQYPVAIAAVLRAGYVVVnvnPLYT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 128 KHpeaQLEYFIQDSRSSLVVVgqeyLERLSPLAQR------------------LG----------------VPLLPLTPA 173
Cdd:PRK07059 109 PR---ELEHQLKDSGAEAIVV----LENFATTVQQvlaktavkhvvvasmgdlLGfkghivnfvvrrvkkmVPAWSLPGH 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 174 VYHGAT----EKPTEQPVEESGwrDRGAMIFYTSGTTGRPKGALSTHRNLAAVVTGLvHSW---AWTKND-----VILHV 241
Cdd:PRK07059 182 VRFNDAlaegARQTFKPVKLGP--DDVAFLQYTGGTTGVSKGATLLHRNIVANVLQM-EAWlqpAFEKKPrpdqlNFVCA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 242 LPLHHVHGV-VNKLLcPLWVGATCVMLPEFSAQQVWEKFLSSEapQITVFMAVPTVYSKLLDYYDkhFTQphvQDFvrav 320
Cdd:PRK07059 259 LPLYHIFALtVCGLL-GMRTGGRNILIPNPRDIPGFIKELKKY--QVHIFPAVNTLYNALLNNPD--FDK---LDF---- 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 321 ckERIRLMVSGSAALPVPLLEKWRSATGHTLLERYGMTEIG-MALSNPLTEARVPGSVGTPLPGVEVRIISEnpqkgspy 399
Cdd:PRK07059 327 --SKLIVANGGGMAVQRPVAERWLEMTGCPITEGYGLSETSpVATCNPVDATEFSGTIGLPLPSTEVSIRDD-------- 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 400 iihaEGNErgtkVTPGfeeKEGELLVRGPSVFREYWDKPEETKSAFTSDGWFRTGDTAVFKDarywiRGRTSV-----DI 474
Cdd:PRK07059 397 ----DGND----LPLG---EPGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDE-----RGYTKIvdrkkDM 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 475 IKTGGYKVSALEIERHLLAHPSITDVAVIGVPDMTWGQRVTAVVaLQEGHSLSHGDLKEWARGVLAPYAVPSELLLVEEI 554
Cdd:PRK07059 461 ILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFV-VKKDPALTEEDVKAFCKERLTNYKRPKFVEFRTEL 539
|
570
....*....|...
gi 1720427507 555 PRNQMGKVNKKEL 567
Cdd:PRK07059 540 PKTNVGKILRREL 552
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
33-567 |
3.59e-43 |
|
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341297 [Multi-domain] Cd Length: 532 Bit Score: 161.93 E-value: 3.59e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 33 PTTP-EAHTDGSVPVFI--RALAFGDRIALIDKYG--HHTYRELYDRSLCLAQEICRLqgckvGDLQEERVSFLCSNDVS 107
Cdd:cd17642 7 PFYPlEDGTAGEQLHKAmkRYASVPGTIAFTDAHTgvNYSYAEYLEMSVRLAEALKKY-----GLKQNDRIAVCSENSLQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 108 YVVAQWASWMSGGVAVPLYWKHPEAQLEYFIQDSRSSLVVVGQEYLERLSPLAQRL----GVPLLPLTPAvYHG--ATEK 181
Cdd:cd17642 82 FFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCSKKGLQKVLNVQKKLkiikTIIILDSKED-YKGyqCLYT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 182 PTEQP----------VEESGWRDRG-AMIFYTSGTTGRPKGALSTHRNLAAVVTGL---VHSWAWTKNDVILHVLPLHHV 247
Cdd:cd17642 161 FITQNlppgfneydfKPPSFDRDEQvALIMNSSGSTGLPKGVQLTHKNIVARFSHArdpIFGNQIIPDTAILTVIPFHHG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 248 HGVVNkLLCPLWVGATCVMLPEFSAqqvwEKFLSS-EAPQITVFMAVPTVY-----SKLLDYYDKHftqphvqdfvravc 321
Cdd:cd17642 241 FGMFT-TLGYLICGFRVVLMYKFEE----ELFLRSlQDYKVQSALLVPTLFaffakSTLVDKYDLS-------------- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 322 keriRLMVSGSAALPvplLEKwrsATGHTLLER---------YGMTEIGMA-LSNPLTEARvPGSVGTPLPGVEVRIISE 391
Cdd:cd17642 302 ----NLHEIASGGAP---LSK---EVGEAVAKRfklpgirqgYGLTETTSAiLITPEGDDK-PGAVGKVVPFFYAKVVDL 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 392 NpqkgspyiihaegnergTKVTPGFEEKeGELLVRGPSVFREYWDKPEETKSAFTSDGWFRTGDTAVF-KDARYWIRGRT 470
Cdd:cd17642 371 D-----------------TGKTLGPNER-GELCVKGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYdEDGHFFIVDRL 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 471 SvDIIKTGGYKVSALEIERHLLAHPSITDVAVIGVPDMTWGQRVTAVVALQEGHSLSHGDLKEWargvLAPYAVPSELL- 549
Cdd:cd17642 433 K-SLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLEAGKTMTEKEVMDY----VASQVSTAKRLr 507
|
570 580
....*....|....*....|..
gi 1720427507 550 ----LVEEIPRNQMGKVNKKEL 567
Cdd:cd17642 508 ggvkFVDEVPKGLTGKIDRRKI 529
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
50-567 |
3.62e-43 |
|
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: 160.23 E-value: 3.62e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 50 ALAFGDRiALidkyghhTYRELYDRSLCLAQeicRLQGCKVGdlQEERVSFLCSNDVSYVVAQWASWMSGGVAVPLYWKH 129
Cdd:cd17649 5 ALVFGDQ-SL-------SYAELDARANRLAH---RLRALGVG--PEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 130 PEAQLEYFIQDSRSSLVvvgqeylerlspLAQrlgvpllpltpavyHGATEkpteqpveesgwrdrgAMIFYTSGTTGRP 209
Cdd:cd17649 72 PAERLRYMLEDSGAGLL------------LTH--------------HPRQL----------------AYVIYTSGSTGTP 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 210 KGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHhVHGVVNKLLCPLWVGATCVMLPEFSAQQVWEKFLSSEAPQITV 289
Cdd:cd17649 110 KGVAVSHGPLAAHCQATAERYGLTPGDRELQFASFN-FDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVTV 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 290 fMAVPTVY-SKLLDYYDKHFTQPHVqdfvravckeRIRLMVSGSAALPVPLLEKWRsATGHTLLERYGMTE---IGMALS 365
Cdd:cd17649 189 -LDLPPAYlQQLAEEADRTGDGRPP----------SLRLYIFGGEALSPELLRRWL-KAPVRLFNAYGPTEatvTPLVWK 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 366 NPLTEARVPGSV--GTPLPGVEVRIIsenpqkgspyiihaegNERGTKVTPGfeeKEGELLVRGPSVFREYWDKPEETKS 443
Cdd:cd17649 257 CEAGAARAGASMpiGRPLGGRSAYIL----------------DADLNPVPVG---VTGELYIGGEGLARGYLGRPELTAE 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 444 AFTSDG-------WFRTGDTAVFK-DARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSITDVAVIGVpDMTWGQRVT 515
Cdd:cd17649 318 RFVPDPfgapgsrLYRTGDLARWRdDGVIEYLGRVD-HQVKIRGFRIELGEIEAALLEHPGVREAAVVAL-DGAGGKQLV 395
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1720427507 516 AVVALQEGHSLSHGD--LKEWARGVLAPYAVPSELLLVEEIPRNQMGKVNKKEL 567
Cdd:cd17649 396 AYVVLRAAAAQPELRaqLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKAL 449
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
87-567 |
3.67e-43 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 161.40 E-value: 3.67e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 87 GCKVGDLqeerVSFLCSNDVSYVVAQWASWMSGGVAVPLYWKHPEAQLEYFIQDSRSSlVVVGQEYLerLSPLAQRL--G 164
Cdd:PRK12406 32 GVRPGDC----VALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGAR-VLIAHADL--LHGLASALpaG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 165 VPLLPL-TP----AVYH--GATEKPTEQPVEESGW------------RDRGAMIfYTSGTTGRPKG---ALSTHRNLAAV 222
Cdd:PRK12406 105 VTVLSVpTPpeiaAAYRisPALLTPPAGAIDWEGWlaqqepydgppvPQPQSMI-YTSGTTGHPKGvrrAAPTPEQAAAA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 223 VTGLVHSWAWTKNDVILHVLPLHH----VHGvvnklLCPLWVGATCVMLPEFSAqqvwEKFLSS-EAPQITVFMAVPTVY 297
Cdd:PRK12406 184 EQMRALIYGLKPGIRALLTGPLYHsapnAYG-----LRAGRLGGVLVLQPRFDP----EELLQLiERHRITHMHMVPTMF 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 298 SKLLDYYDKhftqphvqdfVRAVCK-ERIRLMVSGSAALPVP----LLEKWrsatGHTLLERYGMTEIG-MALSNPLTEA 371
Cdd:PRK12406 255 IRLLKLPEE----------VRAKYDvSSLRHVIHAAAPCPADvkraMIEWW----GPVIYEYYGSTESGaVTFATSEDAL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 372 RVPGSVGTPLPGVEVRIISENpqkgspyiihaegnerGTKVTPGfeeKEGELLVRGPSV--FrEYWDKPEEtKSAFTSDG 449
Cdd:PRK12406 321 SHPGTVGKAAPGAELRFVDED----------------GRPLPQG---EIGEIYSRIAGNpdF-TYHNKPEK-RAEIDRGG 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 450 WFRTGDTAVF-KDARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSITDVAVIGVPDMTWGQRVTAVVALQEGHSLSH 528
Cdd:PRK12406 380 FITSGDVGYLdADGYLFLCDRKR-DMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGATLDE 458
|
490 500 510
....*....|....*....|....*....|....*....
gi 1720427507 529 GDLKEWARGVLAPYAVPSELLLVEEIPRNQMGKVNKKEL 567
Cdd:PRK12406 459 ADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRL 497
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
199-570 |
6.97e-43 |
|
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: 161.09 E-value: 6.97e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 199 IFYTSGTTGRPKGALSTHRNLAAVVTGLVHSW-AWTKNDVILHVLPLHHVHGVVNKLLCPlWVGATCVM---LPEFSAQQ 274
Cdd:cd05928 179 IYFTSGTTGSPKMAEHSHSSLGLGLKVNGRYWlDLTASDIMWNTSDTGWIKSAWSSLFEP-WIQGACVFvhhLPRFDPLV 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 275 VWEKFlsSEAPqITVFMAVPTVYSKLLDyydkhftqphvQDFVRAVCKeRIRLMVSGSAALPVPLLEKWRSATGHTLLER 354
Cdd:cd05928 258 ILKTL--SSYP-ITTFCGAPTVYRMLVQ-----------QDLSSYKFP-SLQHCVTGGEPLNPEVLEKWKAQTGLDIYEG 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 355 YGMTEIGMALSNPLTEARVPGSVGTPLPGVEVRIISENpqkgspyiihaegnerGTKVTPGfeeKEGELLVR-GP----S 429
Cdd:cd05928 323 YGQTETGLICANFKGMKIKPGSMGKASPPYDVQIIDDN----------------GNVLPPG---TEGDIGIRvKPirpfG 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 430 VFREYWDKPEETKSAFTSDGWFrTGDTAVF-KDARYWIRGRtSVDIIKTGGYKVSALEIERHLLAHPSITDVAVIGVPDM 508
Cdd:cd05928 384 LFSGYVDNPEKTAATIRGDFYL-TGDRGIMdEDGYFWFMGR-ADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDP 461
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720427507 509 TWGQRVTAVVALQEGHsLSHG------DLKEWARGVLAPYAVPSELLLVEEIPRNQMGKVNKKELLKQ 570
Cdd:cd05928 462 IRGEVVKAFVVLAPQF-LSHDpeqltkELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRDK 528
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
61-504 |
7.25e-43 |
|
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341295 [Multi-domain] Cd Length: 468 Bit Score: 159.83 E-value: 7.25e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 61 DKYGHHTYRELYDRSLCLAqeiCRLQGCKVGdlQEERVSFLCSNDVSYVVAQWASWMSGGVAVPLYWKHPEAQLEYFIQD 140
Cdd:cd17640 1 KPPKRITYKDLYQEILDFA---AGLRSLGVK--AGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 141 SRSSLVVVgqeylerlsplaqrlgvpllpltpavyhgatekpteqpveESGWRDRgAMIFYTSGTTGRPKGALSTHRNLa 220
Cdd:cd17640 76 SESVALVV----------------------------------------ENDSDDL-ATIIYTSGTTGNPKGVMLTHANL- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 221 avVTGLVHSWAWTK---NDVILHVLPLHHVHGVVNKLLCPLWvGATCVmlpeFSAQQVWEKFLSSEAPQitVFMAVPTVY 297
Cdd:cd17640 114 --LHQIRSLSDIVPpqpGDRFLSILPIWHSYERSAEYFIFAC-GCSQA----YTSIRTLKDDLKRVKPH--YIVSVPRLW 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 298 SKLLD-YYDKHFTQPHVQDFV--RAVCKERIRLMVSGSAALPvPLLEKWRSATGHTLLERYGMTEIGMALSNPLTEARVP 374
Cdd:cd17640 185 ESLYSgIQKQVSKSSPIKQFLflFFLSGGIFKFGISGGGALP-PHVDTFFEAIGIEVLNGYGLTETSPVVSARRLKCNVR 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 375 GSVGTPLPGVEVRIISENpqkgspyiihaegnerGTKVTPgFEEKeGELLVRGPSVFREYWDKPEETKSAFTSDGWFRTG 454
Cdd:cd17640 264 GSVGRPLPGTEIKIVDPE----------------GNVVLP-PGEK-GIVWVRGPQVMKGYYKNPEATSKVLDSDGWFNTG 325
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1720427507 455 DTAVF-KDARYWIRGRTSVDIIKTGGYKVSALEIERHLLAHPSITDVAVIG 504
Cdd:cd17640 326 DLGWLtCGGELVLTGRAKDTIVLSNGENVEPQPIEEALMRSPFIEQIMVVG 376
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
198-562 |
1.59e-42 |
|
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: 155.26 E-value: 1.59e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 198 MIFYTSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVvNKLLCPLWVGATCVMLPEFSAQQVWE 277
Cdd:cd17633 4 YIGFTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLFL-YGAISALYLGGTFIGQRKFNPKSWIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 278 KfLSSEapQITVFMAVPTVYSKLLDYYDKHFTqphvqdfvravckerIRLMVSGSAALPVPLLEKWRSATGHT-LLERYG 356
Cdd:cd17633 83 K-INQY--NATVIYLVPTMLQALARTLEPESK---------------IKSIFSSGQKLFESTKKKLKNIFPKAnLIEFYG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 357 MTEIGMALSNPLTEARVPGSVGTPLPGVEVRIISenpqkgspyiihAEGNERGTkvtpgfeekegeLLVRGPSVFREYWD 436
Cdd:cd17633 145 TSELSFITYNFNQESRPPNSVGRPFPNVEIEIRN------------ADGGEIGK------------IFVKSEMVFSGYVR 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 437 KPEETKsaftsDGWFRTGDTAVFKDARY-WIRGRTSvDIIKTGGYKVSALEIERHLLAHPSITDVAVIGVPDMTWGQrvt 515
Cdd:cd17633 201 GGFSNP-----DGWMSVGDIGYVDEEGYlYLVGRES-DMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGE--- 271
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1720427507 516 AVVALQEGHSLSHGDLKEWARGVLAPYAVPSELLLVEEIPRNQMGKV 562
Cdd:cd17633 272 IAVALYSGDKLTYKQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKI 318
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
33-567 |
5.39e-42 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 158.75 E-value: 5.39e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 33 PTTPEAHTDGSVPVFIRALAFG--DRIALIDKYGHHTYRELYDRSLCLAQEICRlQGCKVGDlqeeRVSFLCSNDVSYVV 110
Cdd:PRK06164 1 TPHDAAPRADTLASLLDAHARArpDAVALIDEDRPLSRAELRALVDRLAAWLAA-QGVRRGD----RVAVWLPNCIEWVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 111 AQWASWMSGGVAVPLYWKHPEAQLEYFIQDSRSSLVVV-----GQEYLERLSPLAQRLgVPLLPLTPAVYHGATEKPTEQ 185
Cdd:PRK06164 76 LFLACARLGATVIAVNTRYRSHEVAHILGRGRARWLVVwpgfkGIDFAAILAAVPPDA-LPPLRAIAVVDDAADATPAPA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 186 P------------------VEESGWRDRGAMIFYTSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHV 247
Cdd:PRK06164 155 PgarvqlfalpdpappaaaGERAADPDAGALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 248 HGVvNKLLCPLWVGATCVMLPEFSAQQVWEKFLSSEapqITVFMAVPTVYSKLLDyydkhfTQPHVQDFVRAvckeriRL 327
Cdd:PRK06164 235 FGF-STLLGALAGGAPLVCEPVFDAARTARALRRHR---VTHTFGNDEMLRRILD------TAGERADFPSA------RL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 328 MVSGSAALPVPLLEKWRSATGHTLLERYGMTEI-----GMALSNPLTEARVPGsvGTPL-PGVEVRIIseNPQKGSpyiI 401
Cdd:PRK06164 299 FGFASFAPALGELAALARARGVPLTGLYGSSEVqalvaLQPATDPVSVRIEGG--GRPAsPEARVRAR--DPQDGA---L 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 402 HAEGnergtkvtpgfeeKEGELLVRGPSVFREYWDKPEETKSAFTSDGWFRTGDTAVFK-DARYWIRGRTSvDIIKTGGY 480
Cdd:PRK06164 372 LPDG-------------ESGEIEIRAPSLMRGYLDNPDATARALTDDGYFRTGDLGYTRgDGQFVYQTRMG-DSLRLGGF 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 481 KVSALEIERHLLAHPSITDVAVIGVpDMTWGQRVTAVVALQEGHSLSHGDLKEWARGVLAPYAVPSELLLVEEIPRNQMG 560
Cdd:PRK06164 438 LVNPAEIEHALEALPGVAAAQVVGA-TRDGKTVPVAFVIPTDGASPDEAGLMAACREALAGFKVPARVQVVEAFPVTESA 516
|
570
....*....|
gi 1720427507 561 ---KVNKKEL 567
Cdd:PRK06164 517 ngaKIQKHRL 526
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
55-567 |
5.78e-42 |
|
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: 157.43 E-value: 5.78e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 55 DRIALIDKYGHHTYRELYDRSLCLAQEIcRLQGCKVGDlqeeRVSFLCSNDVSYVVAQWASWMSGGVAVPLYWKHPEAQL 134
Cdd:cd12114 2 DATAVICGDGTLTYGELAERARRVAGAL-KAAGVRPGD----LVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 135 EYFIQDSRSSLVVVGQEYLERLSPLAQRLGVPLLPLTPavyhgatekPTEQPVEESGwRDRGAMIFYTSGTTGRPKGALS 214
Cdd:cd12114 77 EAILADAGARLVLTDGPDAQLDVAVFDVLILDLDALAA---------PAPPPPVDVA-PDDLAYVIFTSGSTGTPKGVMI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 215 THRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVNkLLCPLWVGATCVMLPEFSAQQV--WEKFLSSEapQITVFMA 292
Cdd:cd12114 147 SHRAALNTILDINRRFAVGPDDRVLALSSLSFDLSVYD-IFGALSAGATLVLPDEARRRDPahWAELIERH--GVTLWNS 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 293 VPTVYSKLLDYYDKHFTQPHVQdfvRAVckerirlMVSGSaALPVPLLEKWRSATGH-TLLERYGMTEiGMALSNPLTEA 371
Cdd:cd12114 224 VPALLEMLLDVLEAAQALLPSL---RLV-------LLSGD-WIPLDLPARLRALAPDaRLISLGGATE-ASIWSIYHPID 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 372 RVP---GSV--GTPLPGVEVRIIsenpqkgspyiihaegNERGTKVTPGFeekEGELLVRGPSVFREYWDKPEETKSAFT 446
Cdd:cd12114 292 EVPpdwRSIpyGRPLANQRYRVL----------------DPRGRDCPDWV---PGELWIGGRGVALGYLGDPELTAARFV 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 447 SDG----WFRTGDTavfkdARYW------IRGRtsVDI-IKTGGYKVSALEIERHLLAHPSITDVAVIGVPDMTWGQRVT 515
Cdd:cd12114 353 THPdgerLYRTGDL-----GRYRpdgtleFLGR--RDGqVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDPGGKRLAA 425
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1720427507 516 AVVALQEGHSLSHGDLKEWARGVLAPYAVPSELLLVEEIPRNQMGKVNKKEL 567
Cdd:cd12114 426 FVVPDNDGTPIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
40-567 |
6.39e-42 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 158.24 E-value: 6.39e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 40 TDGSVPVFIRALAFGDRIALIDKYGHHTYRELYDRSLCLAQEICRlQGCKVGdlqeERVSFLCSNDVSYVVAQWASWMSG 119
Cdd:PRK13383 35 TNPYTLLAVTAARWPGRTAIIDDDGALSYRELQRATESLARRLTR-DGVAPG----RAVGVMCRNGRGFVTAVFAVGLLG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 120 GVAVPLYWKHPEAQLEYFIQDSRSSLVVVGQEYLERLSPLAQRLGVpllpLTPAVYhGATEKPTEQPVEESGwrdrgAMI 199
Cdd:PRK13383 110 ADVVPISTEFRSDALAAALRAHHISTVVADNEFAERIAGADDAVAV----IDPATA-GAEESGGRPAVAAPG-----RIV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 200 FYTSGTTGRPKGALSTHRNLAAV---VTGLVHSWAWTKNDVILhVLPLHHVHGVvNKLLCPLWVGATCVMLPEFSAQQVw 276
Cdd:PRK13383 180 LLTSGTTGKPKGVPRAPQLRSAVgvwVTILDRTRLRTGSRISV-AMPMFHGLGL-GMLMLTIALGGTVLTHRHFDAEAA- 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 277 ekFLSSEAPQITVFMAVPTVYSKLLDYYDKhftqphvqdfVRAVCK-ERIRLMVSGSAALPVPLLEKWRSATGHTLLERY 355
Cdd:PRK13383 257 --LAQASLHRADAFTAVPVVLARILELPPR----------VRARNPlPQLRVVMSSGDRLDPTLGQRFMDTYGDILYNGY 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 356 GMTEIGM-ALSNPLTEARVPGSVGTPLPGVEVRIISENpqkgspyiihaeGNERGTKVTpgfeekeGELLVRGPSVFREY 434
Cdd:PRK13383 325 GSTEVGIgALATPADLRDAPETVGKPVAGCPVRILDRN------------NRPVGPRVT-------GRIFVGGELAGTRY 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 435 WDKPEETksafTSDGWFRTGDTAVFKDA-RYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSITDVAVIGVPDMTWGQR 513
Cdd:PRK13383 386 TDGGGKA----VVDGMTSTGDMGYLDNAgRLFIVGRED-DMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHR 460
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1720427507 514 VTAVVALQEGHSLSHGDLKEWARGVLAPYAVPSELLLVEEIPRNQMGKVNKKEL 567
Cdd:PRK13383 461 LAAFVVLHPGSGVDAAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
67-571 |
8.24e-42 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 158.38 E-value: 8.24e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 67 TYRELYDRSLCLAQEICRlQGCKVGDlqeeRVSFLCSNDVSYVVAqWASWMS-GGVAVPLYWK-HPEaQLEYFIQDSRSS 144
Cdd:PRK06018 41 TYAQIHDRALKVSQALDR-DGIKLGD----RVATIAWNTWRHLEA-WYGIMGiGAICHTVNPRlFPE-QIAWIINHAEDR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 145 LVVVGQEYLERLSPLAQRLG-------------VPLLPLTPAVyhgATEKPTEQPVEESGWRD----RGAMIFYTSGTTG 207
Cdd:PRK06018 114 VVITDLTFVPILEKIADKLPsveryvvltdaahMPQTTLKNAV---AYEEWIAEADGDFAWKTfdenTAAGMCYTSGTTG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 208 RPKGALSTHRN--LAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLwVGATCVML-PEFSAQQVWEkFLSSEa 284
Cdd:PRK06018 191 DPKGVLYSHRSnvLHALMANNGDALGTSAADTMLPVVPLFHANSWGIAFSAPS-MGTKLVMPgAKLDGASVYE-LLDTE- 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 285 pQITVFMAVPTVYSKLLDYYDKH-FTQPHvqdfvravckerIRLMVSGSAALPVPLLEKWrSATGHTLLERYGMTE---I 360
Cdd:PRK06018 268 -KVTFTAGVPTVWLMLLQYMEKEgLKLPH------------LKMVVCGGSAMPRSMIKAF-EDMGVEVRHAWGMTEmspL 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 361 GM--ALSNPLTEARVPGSV------GTPLPGVEVRIISEnpqkgspyiihaEGNErgtkvTPGFEEKEGELLVRGPSVFR 432
Cdd:PRK06018 334 GTlaALKPPFSKLPGDARLdvlqkqGYPPFGVEMKITDD------------AGKE-----LPWDGKTFGRLKVRGPAVAA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 433 EYWdkpEETKSAFTSDGWFRTGDTA-VFKDARYWIRGRtSVDIIKTGGYKVSALEIERHLLAHPSITDVAVIGVPDMTWG 511
Cdd:PRK06018 397 AYY---RVDGEILDDDGFFDTGDVAtIDAYGYMRITDR-SKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWD 472
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 512 QRVTAVVALQEGHSLSHGDLKEWARGVLAPYAVPSELLLVEEIPRNQMGKVNKKELLKQL 571
Cdd:PRK06018 473 ERPLLIVQLKPGETATREEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALREQF 532
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
197-564 |
1.86e-41 |
|
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: 152.80 E-value: 1.86e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 197 AMIFYTSGTTGRPKGALSTHRNLAAVVTGLV-HSWAWTKNDVILHVLPLHHVHGVVNKLLCpLWVGATCVMLPEFSAQQV 275
Cdd:cd17635 4 LAVIFTSGTTGEPKAVLLANKTFFAVPDILQkEGLNWVVGDVTYLPLPATHIGGLWWILTC-LIHGGLCVTGGENTTYKS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 276 WEKFLSSEAPQITVFmaVPTVYSKLLDYYdkhftqphvQDFVRAVckERIRLMVSGSaALPVPLLEKWRSATGHT-LLER 354
Cdd:cd17635 83 LFKILTTNAVTTTCL--VPTLLSKLVSEL---------KSANATV--PSLRLIGYGG-SRAIAADVRFIEATGLTnTAQV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 355 YGMTEIGMAL----SNPLTEArvpGSVGTPLPGVEVRIISenpqkgspyiihaegnergTKVTPGFEEKEGELLVRGPSV 430
Cdd:cd17635 149 YGLSETGTALclptDDDSIEI---NAVGRPYPGVDVYLAA-------------------TDGIAGPSASFGTIWIKSPAN 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 431 FREYWDKPEETKSAFTsDGWFRTGDTA-VFKDARYWIRGRTSVDIIKtGGYKVSALEIERHLLAHPSITDVAVIGVPDMT 509
Cdd:cd17635 207 MLGYWNNPERTAEVLI-DGWVNTGDLGeRREDGFLFITGRSSESINC-GGVKIAPDEVERIAEGVSGVQECACYEISDEE 284
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1720427507 510 WGQRV-TAVVALQEGHSLSHGDLKEWARGVLAPYAVPSELLLVEEIPRNQMGKVNK 564
Cdd:cd17635 285 FGELVgLAVVASAELDENAIRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
55-567 |
2.38e-41 |
|
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: 155.10 E-value: 2.38e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 55 DRIALIDKYGHHTYRELYDRSLCLAQeicRLQGCKVGdlQEERVSFLCSNDVSYVVAQWASWMSGGVAVPLYWKHPEAQL 134
Cdd:cd17652 2 DAPAVVFGDETLTYAELNARANRLAR---LLAARGVG--PERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 135 EYFIQDSRSSLVVVgqeylerlsplaqrlgvpllpltpavyhgatekpteQPveesgwrDRGAMIFYTSGTTGRPKGALS 214
Cdd:cd17652 77 AYMLADARPALLLT------------------------------------TP-------DNLAYVIYTSGSTGRPKGVVV 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 215 THRNLAAVVTGLVHSWAWTKNDVILHVLPLHhVHGVVNKLLCPLWVGATCVMLPEFSAQ--QVWEKFLSSEApqITVFMA 292
Cdd:cd17652 114 THRGLANLAAAQIAAFDVGPGSRVLQFASPS-FDASVWELLMALLAGATLVLAPAEELLpgEPLADLLREHR--ITHVTL 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 293 VPTVYSKLldyydkhftqphvqdfvRAVCKERIRLMVSGSAALPVPLLEKWrsATGHTLLERYGMTE--IGMALSNPLTE 370
Cdd:cd17652 191 PPAALAAL-----------------PPDDLPDLRTLVVAGEACPAELVDRW--APGRRMINAYGPTEttVCATMAGPLPG 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 371 ARVPgSVGTPLPGVEVRIISENPQKgspyiihaegnergtkVTPGFEekeGELLVRGPSVFREYWDKPEETKSAFTSDGW 450
Cdd:cd17652 252 GGVP-PIGRPVPGTRVYVLDARLRP----------------VPPGVP---GELYIAGAGLARGYLNRPGLTAERFVADPF 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 451 -------FRTGDTAVFK-DARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSITDVAVIGVPDMTWGQRVTAVVALQE 522
Cdd:cd17652 312 gapgsrmYRTGDLARWRaDGQLEFLGRAD-DQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAP 390
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1720427507 523 GHSLSHGDLKEWARGVLAPYAVPSELLLVEEIPRNQMGKVNKKEL 567
Cdd:cd17652 391 GAAPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
198-556 |
2.80e-41 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 152.07 E-value: 2.80e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 198 MIFYTSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVhGVVNKLLCPLWVGATCVMLPEFSAQQVWE 277
Cdd:cd17636 4 LAIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLNSGPLFHI-GTLMFTLATFHAGGTNVFVRRVDAEEVLE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 278 kFLSSEAPQITvFMAVPTVysklldyydkhftqphvqDFVRAVCKERI----RLMVSGSAALPVPLLEKWRSATGHTLLE 353
Cdd:cd17636 83 -LIEAERCTHA-FLLPPTI------------------DQIVELNADGLydlsSLRSSPAAPEWNDMATVDTSPWGRKPGG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 354 rYGMTEI-GMALSNPLTEARVpGSVGTPLPGVEVRIISEnpqkgspyiihaEGNErgtkVTPGfeeKEGELLVRGPSVFR 432
Cdd:cd17636 143 -YGQTEVmGLATFAALGGGAI-GGAGRPSPLVQVRILDE------------DGRE----VPDG---EVGEIVARGPTVMA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 433 EYWDKPEETkSAFTSDGWFRTGDTavfkdarywirGRTSVD-----------IIKTGGYKVSALEIERHLLAHPSITDVA 501
Cdd:cd17636 202 GYWNRPEVN-ARRTRGGWHHTNDL-----------GRREPDgslsfvgpktrMIKSGAENIYPAEVERCLRQHPAVADAA 269
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1720427507 502 VIGVPDMTWGQRVTAVVALQEGHSLSHGDLKEWARGVLAPYAVPSELLLVEEIPR 556
Cdd:cd17636 270 VIGVPDPRWAQSVKAIVVLKPGASVTEAELIEHCRARIASYKKPKSVEFADALPR 324
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
62-504 |
6.22e-41 |
|
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: 155.32 E-value: 6.22e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 62 KYGHHTYRELYDRSLCLAQEIcRLQGCKVGDlqeeRVSFLCSNDVSYVVAQWASWMSGGVAVPLYWKHPEAQLEYFIQDS 141
Cdd:cd05932 3 QVVEFTWGEVADKARRLAAAL-RALGLEPGS----KIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 142 RSSLVVVGQ--EYLERLSPLAQRLG---VPLLPLTPAVYHGATEKPTEQPVEESGWR--DRGAMIFYTSGTTGRPKGALS 214
Cdd:cd05932 78 ESKALFVGKldDWKAMAPGVPEGLIsisLPPPSAANCQYQWDDLIAQHPPLEERPTRfpEQLATLIYTSGTTGQPKGVML 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 215 THRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATcVMLPE-----------------FSAQQVWE 277
Cdd:cd05932 158 TFGSFAWAAQAGIEHIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVL-VAFAEsldtfvedvqrarptlfFSVPRLWT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 278 KFlsseapQITVFMAVPTvySKLldyyDKHFTQPHVQDFV-RAVCK----ERIRLMVSGSAALPVPLLEKWRSaTGHTLL 352
Cdd:cd05932 237 KF------QQGVQDKIPQ--QKL----NLLLKIPVVNSLVkRKVLKglglDQCRLAGCGSAPVPPALLEWYRS-LGLNIL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 353 ERYGMTEiGMALSN---PLTeaRVPGSVGTPLPGVEVRIisenpqkgspyiihaegnergtkvtpgfeEKEGELLVRGPS 429
Cdd:cd05932 304 EAYGMTE-NFAYSHlnyPGR--DKIGTVGNAGPGVEVRI-----------------------------SEDGEILVRSPA 351
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720427507 430 VFREYWDKPEETKSAFTSDGWFRTGDT-AVFKDARYWIRGRTSvDIIKTG-GYKVSALEIERHLLAHPSITDVAVIG 504
Cdd:cd05932 352 LMMGYYKDPEATAEAFTADGFLRTGDKgELDADGNLTITGRVK-DIFKTSkGKYVAPAPIENKLAEHDRVEMVCVIG 427
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
197-567 |
1.33e-40 |
|
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: 154.03 E-value: 1.33e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 197 AMIFYTSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPE-FSAQQV 275
Cdd:cd05909 150 AVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVVFHPNpLDYKKI 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 276 WEkfLSSEApQITVFMAVPTvyskLLDYYDKhftQPHVQDFvravckERIRLMVSGSAALPVPLLEKWRSATGHTLLERY 355
Cdd:cd05909 230 PE--LIYDK-KATILLGTPT----FLRGYAR---AAHPEDF------SSLRLVVAGAEKLKDTLRQEFQEKFGIRILEGY 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 356 GMTEIG--MALSNPLTeARVPGSVGTPLPGVEVRIISEnpqkgspyiihaEGNErgtkvtPGFEEKEGELLVRGPSVFRE 433
Cdd:cd05909 294 GTTECSpvISVNTPQS-PNKEGTVGRPLPGMEVKIVSV------------ETHE------EVPIGEGGLLLVRGPNVMLG 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 434 YWDKPEETKSAFtSDGWFRTGDTAVFKDARY-WIRGRTSvDIIKTGGYKVSALEIERHLLAH-PSITDVAVIGVPDMTWG 511
Cdd:cd05909 355 YLNEPELTSFAF-GDGWYDTGDIGKIDGEGFlTITGRLS-RFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDGRKG 432
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720427507 512 QRvtaVVALQEGHSLSHGDLKEWARGVLAP-YAVPSELLLVEEIPRNQMGKVNKKEL 567
Cdd:cd05909 433 EK---IVLLTTTTDTDPSSLNDILKNAGISnLAKPSYIHQVEEIPLLGTGKPDYVTL 486
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
49-562 |
1.77e-40 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 154.70 E-value: 1.77e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 49 RALAFGDRIA---LIDKYG---HHTYRELYDRSLCLAQEIcrLQGCKVGDlqeeRVSFLCSNDVSYVVAQWASWMSGGVA 122
Cdd:cd05931 2 RAAARPDRPAytfLDDEGGreeTLTYAELDRRARAIAARL--QAVGKPGD----RVLLLAPPGLDFVAAFLGCLYAGAIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 123 VPLYWKHPEAQLEYF---IQDSRSSLVVVGQEYLERLSPLAQRLGVPLLPLTPAVyhgatekptEQPVEESG--WRDRG- 196
Cdd:cd05931 76 VPLPPPTPGRHAERLaaiLADAGPRVVLTTAAALAAVRAFAASRPAAGTPRLLVV---------DLLPDTSAadWPPPSp 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 197 -----AMIFYTSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFS 271
Cdd:cd05931 147 dpddiAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPSVLMSPAA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 272 aqqvwekflsseapqitvFMAVPTVYSKLLDYYDKHFTQphVQDFVRAVCKERIR-----------LMVSGSAALPVpll 340
Cdd:cd05931 227 ------------------FLRRPLRWLRLISRYRATISA--APNFAYDLCVRRVRdedlegldlssWRVALNGAEPV--- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 341 ekwRSATGHTLLER--------------YGMTE-------------------IGMALSNPLTEARVPG-------SVGTP 380
Cdd:cd05931 284 ---RPATLRRFAEAfapfgfrpeafrpsYGLAEatlfvsggppgtgpvvlrvDRDALAGRAVAVAADDpaarelvSCGRP 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 381 LPGVEVRIIseNPqkgspyiihaegnERGTKVTPGfeeKEGELLVRGPSVFREYWDKPEETKSAF------TSDGWFRTG 454
Cdd:cd05931 361 LPDQEVRIV--DP-------------ETGRELPDG---EVGEIWVRGPSVASGYWGRPEATAETFgalaatDEGGWLRTG 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 455 DTAVFKDARYWIRGRTSvDIIKTGGYKVSALEIERHL-LAHPSI--TDVAVIGVPDmtwGQRVTAVVALQEGHSLSHGDL 531
Cdd:cd05931 423 DLGFLHDGELYITGRLK-DLIIVRGRNHYPQDIEATAeEAHPALrpGCVAAFSVPD---DGEERLVVVAEVERGADPADL 498
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 1720427507 532 KEWARGVLApyAV-------PSELLLVE--EIPRNQMGKV 562
Cdd:cd05931 499 AAIAAAIRA--AVarehgvaPADVVLVRpgSIPRTSSGKI 536
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
193-569 |
2.59e-40 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 154.67 E-value: 2.59e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 193 RDRGAMIFYTSGTTGRPKGALSTHRnlaAVVTglvHsWAWTKndvilHVLPLHH------------VHGVVNKLLCPLWV 260
Cdd:PRK04319 204 REDGAILHYTSGSTGKPKGVLHVHN---AMLQ---H-YQTGK-----YVLDLHEddvywctadpgwVTGTSYGIFAPWLN 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 261 GATCVML-PEFSAQQvWEKFLSSEapQITVFMAVPTVYSKLLDYYDkhftqphvqDFVRAVCKERIRLMVSGSAALPvPL 339
Cdd:PRK04319 272 GATNVIDgGRFSPER-WYRILEDY--KVTVWYTAPTAIRMLMGAGD---------DLVKKYDLSSLRHILSVGEPLN-PE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 340 LEKW-RSATGHTLLERYGMTEIG-MALSNPLTEARVPGSVGTPLPGVEVRIISENPQKGSPYiihaegnergtkvtpgfe 417
Cdd:PRK04319 339 VVRWgMKVFGLPIHDNWWMTETGgIMIANYPAMDIKPGSMGKPLPGIEAAIVDDQGNELPPN------------------ 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 418 eKEGELLVRG--PSVFREYWDKPEETKSAFtSDGWFRTGDTAvFKDAR--YWIRGRTSvDIIKTGGYKVSALEIERHLLA 493
Cdd:PRK04319 401 -RMGNLAIKKgwPSMMRGIWNNPEKYESYF-AGDWYVSGDSA-YMDEDgyFWFQGRVD-DVIKTSGERVGPFEVESKLME 476
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720427507 494 HPSITDVAVIGVPDMTWGQRVTAVVALQEGHSLSH---GDLKEWARGVLAPYAVPSELLLVEEIPRNQMGKVNKKeLLK 569
Cdd:PRK04319 477 HPAVAEAGVIGKPDPVRGEIIKAFVALRPGYEPSEelkEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRR-VLK 554
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
67-455 |
5.01e-40 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.
Pssm-ID: 341250 [Multi-domain] Cd Length: 545 Bit Score: 153.14 E-value: 5.01e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 67 TYRELYDRSLCLAQEICRLQGCKVGDlqeERVSFLCSNDVSYVVAQWASWMSGGVAVPLYwkH---PEAqLEYFIQDSRS 143
Cdd:cd05927 7 SYKEVAERADNIGSALRSLGGKPAPA---SFVGIYSINRPEWIISELACYAYSLVTVPLY--DtlgPEA-IEYILNHAEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 144 SLVVVGQeylerlsplaqrlGVPLLPLTPAVYHGATEK-PTEQPVEESGwrdrgAMIFYTSGTTGRPKGALSTHRNLAAV 222
Cdd:cd05927 81 SIVFCDA-------------GVKVYSLEEFEKLGKKNKvPPPPPKPEDL-----ATICYTSGTTGNPKGVMLTHGNIVSN 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 223 VTGLVHSW----AWTKNDVILHVLPLHHV--HGVVNKLLC-----PLWVGATCVMLPEFSAQQvwekflsseaPqiTVFM 291
Cdd:cd05927 143 VAGVFKILeilnKINPTDVYISYLPLAHIfeRVVEALFLYhgakiGFYSGDIRLLLDDIKALK----------P--TVFP 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 292 AVPTVYSKL----------------------LDYYDKHFTQPHVQ-----DF-----VRAVCKERIRLMVSGSAALPVPL 339
Cdd:cd05927 211 GVPRVLNRIydkifnkvqakgplkrklfnfaLNYKLAELRSGVVRaspfwDKlvfnkIKQALGGNVRLMLTGSAPLSPEV 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 340 LEKWRSATGHTLLERYGMTEI--GMALSNPltEARVPGSVGTPLPGVEVRIISEnPQKGspYiiHAEGNErgtkvtpgfe 417
Cdd:cd05927 291 LEFLRVALGCPVLEGYGQTECtaGATLTLP--GDTSVGHVGGPLPCAEVKLVDV-PEMN--Y--DAKDPN---------- 353
|
410 420 430
....*....|....*....|....*....|....*...
gi 1720427507 418 eKEGELLVRGPSVFREYWDKPEETKSAFTSDGWFRTGD 455
Cdd:cd05927 354 -PRGEVCIRGPNVFSGYYKDPEKTAEALDEDGWLHTGD 390
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
119-567 |
8.66e-40 |
|
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: 152.65 E-value: 8.66e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 119 GGVAVPLYWKHPEAQLEYFIQDSRSSLVVVGQE--YLERLSPLAQRLGVP--LLPLTPAVYHGATE------------KP 182
Cdd:cd05970 96 GAIAIPATHQLTAKDIVYRIESADIKMIVAIAEdnIPEEIEKAAPECPSKpkLVWVGDPVPEGWIDfrkliknaspdfER 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 183 TEQPVEESGwrDRGAMIFYTSGTTGRPKgaLSTHRN---LAAVVTGLVhsWAWTK-NDVILHVLPLHHVHGVVNKLLCPl 258
Cdd:cd05970 176 PTANSYPCG--EDILLVYFSSGTTGMPK--MVEHDFtypLGHIVTAKY--WQNVReGGLHLTVADTGWGKAVWGKIYGQ- 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 259 WVGATCVMLPE---FSAQQVWEKFlssEAPQITVFMAVPTVYSKL----LDYYDKhftqphvqdfvravckERIRLMVSG 331
Cdd:cd05970 249 WIAGAAVFVYDydkFDPKALLEKL---SKYGVTTFCAPPTIYRFLiredLSRYDL----------------SSLRYCTTA 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 332 SAALPVPLLEKWRSATGHTLLERYGMTEIGMALSN-PLTEARvPGSVGTPLPGVEVRIISENpqkgspyiihaegnerGT 410
Cdd:cd05970 310 GEALNPEVFNTFKEKTGIKLMEGFGQTETTLTIATfPWMEPK-PGSMGKPAPGYEIDLIDRE----------------GR 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 411 KVTPGfeeKEGELLVR---GPSV--FREYWDKPEETKSAFtSDGWFRTGDTAVF-KDARYWIRGRTSvDIIKTGGYKVSA 484
Cdd:cd05970 373 SCEAG---EEGEIVIRtskGKPVglFGGYYKDAEKTAEVW-HDGYYHTGDAAWMdEDGYLWFVGRTD-DLIKSSGYRIGP 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 485 LEIERHLLAHPSITDVAVIGVPDMTWGQRVTAVVALQEGHSLSHG---DLKEWARGVLAPYAVPSELLLVEEIPRNQMGK 561
Cdd:cd05970 448 FEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVLAKGYEPSEElkkELQDHVKKVTAPYKYPRIVEFVDELPKTISGK 527
|
....*.
gi 1720427507 562 VNKKEL 567
Cdd:cd05970 528 IRRVEI 533
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
72-568 |
1.46e-39 |
|
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: 150.61 E-value: 1.46e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 72 YDRSLCLAQEICRLQGCKVGDlqeeRVSFLCSNDVSYVVAQWASWMSGGVAVPLYWKHPEAQLEYFIQDSRSSLVVvgqe 151
Cdd:cd05929 23 YSIALNRNARAAAAEGVWIAD----GVYIYLINSILTVFAAAAAWKCGACPAYKSSRAPRAEACAIIEIKAAALVC---- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 152 ylerlsplaqrlGVPLLPLTPAVYHGATEKPTEQPVEESGWRDRGAMIFYTSGTTGRPKGALsthRNLAAVV--TGLVHS 229
Cdd:cd05929 95 ------------GLFTGGGALDGLEDYEAAEGGSPETPIEDEAAGWKMLYSGGTTGRPKGIK---RGLPGGPpdNDTLMA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 230 WA----WTKNDVILHVLPLHHV--HGVVNKllcPLWVGATCVMLPEFSAqqvwEKFLSS-EAPQITVFMAVPTVYSKLLD 302
Cdd:cd05929 160 AAlgfgPGADSVYLSPAPLYHAapFRWSMT---ALFMGGTLVLMEKFDP----EEFLRLiERYRVTFAQFVPTMFVRLLK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 303 YYDKhftQPHVQDFvravckERIRLMVSGSAALPVPLLEKWRSATGHTLLERYGMTE-IGMALSNPLTEARVPGSVGTPL 381
Cdd:cd05929 233 LPEA---VRNAYDL------SSLKRVIHAAAPCPPWVKEQWIDWGGPIIWEYYGGTEgQGLTIINGEEWLTHPGSVGRAV 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 382 PGvEVRIISENpqkgspyiihaeGNErgtkVTPGfeeKEGELLVRGPSVFrEYWDKPEETKSAFTSDGWFRTGDTAVFKD 461
Cdd:cd05929 304 LG-KVHILDED------------GNE----VPPG---EIGEVYFANGPGF-EYTNDPEKTAAARNEGGWSTLGDVGYLDE 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 462 ARYWIRGRTSVDIIKTGGYKVSALEIERHLLAHPSITDVAVIGVPDMTWGQRVTAVVALQEG---HSLSHGDLKEWARGV 538
Cdd:cd05929 363 DGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQPAPGadaGTALAEELIAFLRDR 442
|
490 500 510
....*....|....*....|....*....|
gi 1720427507 539 LAPYAVPSELLLVEEIPRNQMGKVNKKELL 568
Cdd:cd05929 443 LSRYKCPRSIEFVAELPRDDTGKLYRRLLR 472
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
55-579 |
2.40e-39 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 150.31 E-value: 2.40e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 55 DRIALIDKYGHHTYRELYdRSLCLAQEICRLQGCKvgdlqEERVSFLCSNDVSYVVAQWASWMSGGVAVPL--YWKHPEA 132
Cdd:PRK07638 16 NKIAIKENDRVLTYKDWF-ESVCKVANWLNEKESK-----NKTIAILLENRIEFLQLFAGAAMAGWTCVPLdiKWKQDEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 133 QLEYFIqdSRSSLVVVGQEYLERLSPLAQRlgVPLL----PLTPAvyhgatEKPTEQPVEesgwrDRGAMIFY---TSGT 205
Cdd:PRK07638 90 KERLAI--SNADMIVTERYKLNDLPDEEGR--VIEIdewkRMIEK------YLPTYAPIE-----NVQNAPFYmgfTSGS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 206 TGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVH---GVVNKLlcplWVGATCVMLPEFSAQQVWEKfLSS 282
Cdd:PRK07638 155 TGKPKAFLRAQQSWLHSFDCNVHDFHMKREDSVLIAGTLVHSLflyGAISTL----YVGQTVHLMRKFIPNQVLDK-LET 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 283 EapQITVFMAVPTVYSKLLDyydkhftqphvqdfVRAVCKERIRLMVSGsAALPVPLLEKWRSATGH-TLLERYGMTEIG 361
Cdd:PRK07638 230 E--NISVMYTVPTMLESLYK--------------ENRVIENKMKIISSG-AKWEAEAKEKIKNIFPYaKLYEFYGASELS 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 362 -MALSNPLTEARVPGSVGTPLPGVEVRIIsenpqkgspyiihaegNERGTKVTPGfeeKEGELLVRGPSVFREYWDKPEE 440
Cdd:PRK07638 293 fVTALVDEESERRPNSVGRPFHNVQVRIC----------------NEAGEEVQKG---EIGTVYVKSPQFFMGYIIGGVL 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 441 TKSaFTSDGWFRTGDTA-VFKDARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSITDVAVIGVPDMTWGQRVTAVVa 519
Cdd:PRK07638 354 ARE-LNADGWMTVRDVGyEDEEGFIYIVGREK-NMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAII- 430
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 520 lqEGHSLSHgDLKEWARGVLAPYAVPSELLLVEEIPRNQMGKVNKKELLKQLYPSGQRSQ 579
Cdd:PRK07638 431 --KGSATKQ-QLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAKSWIENQEKIYE 487
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
67-571 |
6.55e-39 |
|
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: 150.13 E-value: 6.55e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 67 TYRELYDRSLCLAQEIcRLQGCKVGDlqeeRVSFLCSNDVSYVVAQWASWMSGGVAVPL-------YWKHPEAQLEYFIQ 139
Cdd:cd05906 41 SYQDLLEDARRLAAGL-RQLGLRPGD----SVILQFDDNEDFIPAFWACVLAGFVPAPLtvpptydEPNARLRKLRHIWQ 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 140 DSRSSLVVVGQEYLERLSPLAQRLGVPLLPLTPAVYHGATEKPTEQPVEESgwrDRGAMIFYTSGTTGRPKGALSTHRNL 219
Cdd:cd05906 116 LLGSPVVLTDAELVAEFAGLETLSGLPGIRVLSIEELLDTAADHDLPQSRP---DDLALLMLTSGSTGFPKAVPLTHRNI 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 220 AAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGAtcvmlpefsaQQVwekflsseapqitvfmAVPTVY-- 297
Cdd:cd05906 193 LARSAGKIQHNGLTPQDVFLNWVPLDHVGGLVELHLRAVYLGC----------QQV----------------HVPTEEil 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 298 ---SKLLDYYDKH---------FTQPHVQDFVRAVCKER-----IRLMVSGSAALPVPLLEKWRSatghtLLERY----- 355
Cdd:cd05906 247 adpLRWLDLIDRYrvtitwapnFAFALLNDLLEEIEDGTwdlssLRYLVNAGEAVVAKTIRRLLR-----LLEPYglppd 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 356 ------GMTEI--GMALSNPLTEARVPG-----SVGTPLPGVEVRIISENpqkgspyiihaegnergTKVTPgfEEKEGE 422
Cdd:cd05906 322 airpafGMTETcsGVIYSRSFPTYDHSQalefvSLGRPIPGVSMRIVDDE-----------------GQLLP--EGEVGR 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 423 LLVRGPSVFREYWDKPEETKSAFTSDGWFRTGDTAVFKDARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSITD--V 500
Cdd:cd05906 383 LQVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLGFLDNGNLTITGRTK-DTIIVNGVNYYSHEIEAAVEEVPGVEPsfT 461
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720427507 501 AVIGVPDMTWGQRVTAVV-----ALQEGHSLSHGDLKEWAR---GVLAPYAVPselLLVEEIPRNQMGKVNKKELLKQL 571
Cdd:cd05906 462 AAFAVRDPGAETEELAIFfvpeyDLQDALSETLRAIRSVVSrevGVSPAYLIP---LPKEEIPKTSLGKIQRSKLKAAF 537
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
55-567 |
6.79e-39 |
|
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: 148.23 E-value: 6.79e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 55 DRIALIDKYGHHTYRELYDRSLCLAQEIcRLQGCKvgdlQEERVSFLCSNDVSYVVAQWASWMSGGVAVPLYWKHPEAQL 134
Cdd:cd12115 14 DAIALVCGDESLTYAELNRRANRLAARL-RAAGVG----PESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 135 EYFIQDSRSSLVVVGQEYLerlsplaqrlgvpllpltpavyhgatekpteqpveesgwrdrgAMIFYTSGTTGRPKGALS 214
Cdd:cd12115 89 RFILEDAQARLVLTDPDDL-------------------------------------------AYVIYTSGSTGRPKGVAI 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 215 THRNLAAVVtglvhSWAwtkndviLHVLPLHHVHGV-----------VNKLLCPLWVGATCVMlpefsAQQVWEKFLSSE 283
Cdd:cd12115 126 EHRNAAAFL-----QWA-------AAAFSAEELAGVlastsicfdlsVFELFGPLATGGKVVL-----ADNVLALPDLPA 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 284 APQITVFMAVPTVYSKLLDyydkhftQPHVQDFVRAVCkerirlmVSGSAaLPVPLLEK-WRSATGHTLLERYGMTE--- 359
Cdd:cd12115 189 AAEVTLINTVPSAAAELLR-------HDALPASVRVVN-------LAGEP-LPRDLVQRlYARLQVERVVNLYGPSEdtt 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 360 --IGMALSnplTEARVPGSVGTPLPGVEVriisenpqkgspYIIHAEGNERGTKVTpgfeekeGELLVRGPSVFREYWDK 437
Cdd:cd12115 254 ysTVAPVP---PGASGEVSIGRPLANTQA------------YVLDRALQPVPLGVP-------GELYIGGAGVARGYLGR 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 438 PEETKSAFTSDGW------FRTGDTAVFK-DARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSITDVAVIGVPDMTW 510
Cdd:cd12115 312 PGLTAERFLPDPFgpgarlYRTGDLVRWRpDGLLEFLGRAD-NQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAG 390
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720427507 511 GQRVTAVVALQEGHSLSHGDLKEWARGVLAPYAVPSELLLVEEIPRNQMGKVNKKEL 567
Cdd:cd12115 391 ERRLVAYIVAEPGAAGLVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
66-571 |
8.38e-38 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 146.78 E-value: 8.38e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 66 HTYRELYDRSLCLAQEICRLqGCKVGDlqeeRVSFLCSNDVSYVVAQWASWMSGGVAVPLYWK-HPEaQLEYFIQDSRSS 144
Cdd:PRK07008 40 YTYRDCERRAKQLAQALAAL-GVEPGD----RVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRlFPE-QIAYIVNHAEDR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 145 LVVVGQEYLerlsPLAQRLGvpllPLTPAVYH-----GATEKPTEQ-PV--------EESG---W----RDRGAMIFYTS 203
Cdd:PRK07008 114 YVLFDLTFL----PLVDALA----PQCPNVKGwvamtDAAHLPAGStPLlcyetlvgAQDGdydWprfdENQASSLCYTS 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 204 GTTGRPKGALSTHRN--LAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLwVGATCVML-PEFSAQQVWEKFl 280
Cdd:PRK07008 186 GTTGNPKGALYSHRStvLHAYGAALPDAMGLSARDAVLPVVPMFHVNAWGLPYSAPL-TGAKLVLPgPDLDGKSLYELI- 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 281 ssEAPQITVFMAVPTVYSKLLDYydkhfTQPHVQDFvravckERIRLMVSGSAALPVPLLEKWRSATGHTLLERYGMTEI 360
Cdd:PRK07008 264 --EAERVTFSAGVPTVWLGLLNH-----MREAGLRF------STLRRTVIGGSACPPAMIRTFEDEYGVEVIHAWGMTEM 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 361 ----------GMALSNPLTEAR-VPGSVGTPLPGVEVRIISEN----PQKGSPYiihaegnergtkvtpgfeekeGELLV 425
Cdd:PRK07008 331 splgtlcklkWKHSQLPLDEQRkLLEKQGRVIYGVDMKIVGDDgrelPWDGKAF---------------------GDLQV 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 426 RGPSVFREYWDKPEETksafTSDGWFRTGDTAVF-KDARYWIRGRtSVDIIKTGGYKVSALEIERHLLAHPSITDVAVIG 504
Cdd:PRK07008 390 RGPWVIDRYFRGDASP----LVDGWFPTGDVATIdADGFMQITDR-SKDVIKSGGEWISSIDIENVAVAHPAVAEAACIA 464
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720427507 505 VPDMTWGQRVTAVVALQEGHSLSHGDLKEWARGVLAPYAVPSELLLVEEIPRNQMGKVNKKELLKQL 571
Cdd:PRK07008 465 CAHPKWDERPLLVVVKRPGAEVTREELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLREQF 531
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
50-567 |
2.43e-37 |
|
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: 144.78 E-value: 2.43e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 50 ALAFGDRIAlidkyghhTYRELYDRSLCLAQeICRLQGCKvgdlQEERVSFLCSNDVSYVVAQWASWMSGGVAVPLYWKH 129
Cdd:cd17655 15 AVVFEDQTL--------TYRELNERANQLAR-TLREKGVG----PDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 130 PEAQLEYFIQDSRSSLVVVgQEYLErlSPLAQRlGVPLLPLTPAVYHGATE--KPTEQPveesgwrDRGAMIFYTSGTTG 207
Cdd:cd17655 82 PEERIQYILEDSGADILLT-QSHLQ--PPIAFI-GLIDLLDEDTIYHEESEnlEPVSKS-------DDLAYVIYTSGSTG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 208 RPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLhHVHGVVNKLLCPLWVGATCVMLP--EFSAQQVWEKFLSSEap 285
Cdd:cd17655 151 KPKGVMIEHRGVVNLVEWANKVIYQGEHLRVALFASI-SFDASVTEIFASLLSGNTLYIVRkeTVLDGQALTQYIRQN-- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 286 QITVFMAVPTVYsKLLDYYDKHFTQPhvqdfvravckerIRLMVSGSAALPVPLLEKWRSATGH--TLLERYGMTE---- 359
Cdd:cd17655 228 RITIIDLTPAHL-KLLDAADDSEGLS-------------LKHLIVGGEALSTELAKKIIELFGTnpTITNAYGPTEttvd 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 360 --IGMALSNPLTEARVPgsVGTPLPGVEVRIISEN--PQK-GSPyiihaegnergtkvtpgfeekeGELLVRGPSVFREY 434
Cdd:cd17655 294 asIYQYEPETDQQVSVP--IGKPLGNTRIYILDQYgrPQPvGVA----------------------GELYIGGEGVARGY 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 435 WDKPEETKSAFTSDGW------FRTGDTAVF-KDARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSITDVAVIGVPD 507
Cdd:cd17655 350 LNRPELTAEKFVDDPFvpgermYRTGDLARWlPDGNIEFLGRID-HQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKD 428
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 508 MTWGQRVTAVVALQEghSLSHGDLKEWARGVLAPYAVPSELLLVEEIPRNQMGKVNKKEL 567
Cdd:cd17655 429 EQGQNYLCAYIVSEK--ELPVAQLREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKAL 486
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
38-567 |
2.73e-37 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 144.83 E-value: 2.73e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 38 AHTDGSVPVFIRAlAFGDRIalidkyghhTYRELYDRSLCLAQeICRLQGCKVGDlqeeRVSFLCSNDVSYVVAQWASWM 117
Cdd:PRK13391 7 AQTTPDKPAVIMA-STGEVV---------TYRELDERSNRLAH-LFRSLGLKRGD----HVAIFMENNLRYLEVCWAAER 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 118 SGGVAVPLYWKHPEAQLEYFIQDSRSSLVVVGQEYLERLSPLAQRLGVPLLPLtpaVYHGATEKPTEQPVEE-----SGW 192
Cdd:PRK13391 72 SGLYYTCVNSHLTPAEAAYIVDDSGARALITSAAKLDVARALLKQCPGVRHRL---VLDGDGELEGFVGYAEavaglPAT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 193 R----DRGAMIFYTSGTTGRPKGAL--------STHRNLAAVVTGLvhsWAWTKNDVILHVLPLHHVH-----GVVNKLl 255
Cdd:PRK13391 149 PiadeSLGTDMLYSSGTTGRPKGIKrplpeqppDTPLPLTAFLQRL---WGFRSDMVYLSPAPLYHSApqravMLVIRL- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 256 cplwvGATCVMLPEFSAqqvwEKFLSS-EAPQITVFMAVPTVYSKLL-------DYYDkhftqphVQDFVRAVckerirl 327
Cdd:PRK13391 225 -----GGTVIVMEHFDA----EQYLALiEEYGVTHTQLVPTMFSRMLklpeevrDKYD-------LSSLEVAI------- 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 328 mvsgSAALPVP------LLEKWrsatGHTLLERYGMTE-IGMALSNPLTEARVPGSVGTPLPGVeVRIIsenpqkgspyi 400
Cdd:PRK13391 282 ----HAAAPCPpqvkeqMIDWW----GPIIHEYYAATEgLGFTACDSEEWLAHPGTVGRAMFGD-LHIL----------- 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 401 ihaegNERGTKVTPGfeeKEGELLVRGPSVFrEYWDKPEETKSAFTSDG-WFRTGDTAVFKDARYWIRGRTSVDIIKTGG 479
Cdd:PRK13391 342 -----DDDGAELPPG---EPGTIWFEGGRPF-EYLNDPAKTAEARHPDGtWSTVGDIGYVDEDGYLYLTDRAAFMIISGG 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 480 YKVSALEIERHLLAHPSITDVAVIGVPDMTWGQRVTAVVALQEGHSLS---HGDLKEWARGVLAPYAVPSELLLVEEIPR 556
Cdd:PRK13391 413 VNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDGVDPGpalAAELIAFCRQRLSRQKCPRSIDFEDELPR 492
|
570
....*....|.
gi 1720427507 557 NQMGKVNKKEL 567
Cdd:PRK13391 493 LPTGKLYKRLL 503
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
55-567 |
6.48e-37 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 147.62 E-value: 6.48e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 55 DRIALIDKYGHHTYRELYDRSLCLAQeicRLQGCKVGdlQEERVSFLCSNDVSYVVAQWASWMSGGVAVPLYWKHPEAQL 134
Cdd:PRK12467 527 ERPALVFGEQVLSYAELNRQANRLAH---VLIAAGVG--PDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRL 601
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 135 EYFIQDSRSSLVVvGQEYLERLSPLAQRLGVPLLPLTPAVYHGATEKPTEQPVEEsgwrDRGAMIFYTSGTTGRPKGALS 214
Cdd:PRK12467 602 AYMLDDSGVRLLL-TQSHLLAQLPVPAGLRSLCLDEPADLLCGYSGHNPEVALDP----DNLAYVIYTSGSTGQPKGVAI 676
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 215 THRNLAAVVTGLVHSWAWTKNDVILHVLPLhHVHGVVNKLLCPLWVGATCVMLPEFSAQQVWEKFLSSEAPQITVFMAVP 294
Cdd:PRK12467 677 SHGALANYVCVIAERLQLAADDSMLMVSTF-AFDLGVTELFGALASGATLHLLPPDCARDAEAFAALMADQGVTVLKIVP 755
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 295 TVYSKLLdyydkhftqphvQDFVRAVCKERIRLMVSGSaALPVPLLEKWRS-ATGHTLLERYGMTE--IGMALSNPLTEA 371
Cdd:PRK12467 756 SHLQALL------------QASRVALPRPQRALVCGGE-ALQVDLLARVRAlGPGARLINHYGPTEttVGVSTYELSDEE 822
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 372 RVPGSV--GTPLPGVEVRII--SENPqkgspyiihaegnergtkVTPGFeekEGELLVRGPSVFREYWDKPEETKSAFTS 447
Cdd:PRK12467 823 RDFGNVpiGQPLANLGLYILdhYLNP------------------VPVGV---VGELYIGGAGLARGYHRRPALTAERFVP 881
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 448 DGW-------FRTGDTAVF-KDARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSITDVAVIGVPDMTWGQRVTAVVA 519
Cdd:PRK12467 882 DPFgadggrlYRTGDLARYrADGVIEYLGRMD-HQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQLVAYLVP 960
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1720427507 520 LQEGHSLSHG----DLKEWARGVLAPYAVPSELLLVEEIPRNQMGKVNKKEL 567
Cdd:PRK12467 961 AAVADGAEHQatrdELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKAL 1012
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
67-564 |
1.93e-36 |
|
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: 141.12 E-value: 1.93e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 67 TYRELYDRSLCLAQEICRLqGCKVGDlqeeRVSFLCSNDVSYVVAQWASWMSGGVAVPLYWKHPEAQLEYFIQDSRSSLV 146
Cdd:cd05973 2 TFGELRALSARFANALQEL-GVGPGD----VVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 147 VVGqeylerlspLAQRlgvpllpltpavyhgatEKPTEQPVeesgwrdrgaMIFYTSGTTGRPKGALSTHRNLAAVVTGL 226
Cdd:cd05973 77 VTD---------AANR-----------------HKLDSDPF----------VMMFTSGTTGLPKGVPVPLRALAAFGAYL 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 227 VHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLP-EFSAQQVWEKFlssEAPQITVFMAVPTVYSKLLdyyd 305
Cdd:cd05973 121 RDAVDLRPEDSFWNAADPGWAYGLYYAITGPLALGHPTILLEgGFSVESTWRVI---ERLGVTNLAGSPTAYRLLM---- 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 306 khftqphvQDFVRAVCKERIRLMVSGSAALPV-PLLEKWRSAT-GHTLLERYGMTEIGMALSNPLTEARV--PGSVGTPL 381
Cdd:cd05973 194 --------AAGAEVPARPKGRLRRVSSAGEPLtPEVIRWFDAAlGVPIHDHYGQTELGMVLANHHALEHPvhAGSAGRAM 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 382 PGVEVRIISENpqkgspyiihaegnerGTKVTPGfeeKEGELLV---RGPSV-FREYWDKPEETKSAftsdGWFRTGDTA 457
Cdd:cd05973 266 PGWRVAVLDDD----------------GDELGPG---EPGRLAIdiaNSPLMwFRGYQLPDTPAIDG----GYYLTGDTV 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 458 VFK-DARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSITDVAVIGVPDMTWGQRVTAVVALQEGHSLSHGDLKEWAR 536
Cdd:cd05973 323 EFDpDGSFSFIGRAD-DVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTPALADELQL 401
|
490 500 510
....*....|....*....|....*....|.
gi 1720427507 537 GV---LAPYAVPSELLLVEEIPRNQMGKVNK 564
Cdd:cd05973 402 HVkkrLSAHAYPRTIHFVDELPKTPSGKIQR 432
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
23-569 |
2.03e-36 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 146.26 E-value: 2.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 23 PRRHRGHSLLpttpeAHTDGSVPVFIrALAFGDRialidkygHHTYRELYDRSLCLAQeicRLQGCKVGdlQEERVSFLC 102
Cdd:PRK12316 2000 PRGPGVHQRI-----AEQAARAPEAI-AVVFGDQ--------HLSYAELDSRANRLAH---RLRARGVG--PEVRVAIAA 2060
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 103 SNDVSYVVAQWASWMSGGVAVPLYWKHPEAQLEYFIQDSRSSLVVVGQEYLERLsPLAQrlGVPLLPLTPAVYhgATEKP 182
Cdd:PRK12316 2061 ERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQRHLLERL-PLPA--GVARLPLDRDAE--WADYP 2135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 183 TEQPVEESGwRDRGAMIFYTSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLhHVHGVVNKLLCPLWVGA 262
Cdd:PRK12316 2136 DTAPAVQLA-GENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSF-SFDGAHEQWFHPLLNGA 2213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 263 TCVM------LPEFSAQQVWEKflsseapQITVfMAVPTVYSKLLdyydkhftqphVQDFVRAVCKERIRLMVSGSAALP 336
Cdd:PRK12316 2214 RVLIrddelwDPEQLYDEMERH-------GVTI-LDFPPVYLQQL-----------AEHAERDGRPPAVRVYCFGGEAVP 2274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 337 VPLLEK-WRSATGHTLLERYGMTEIGMALS-------NPLTEARVPgsVGTPLPGVevriisenpqkgSPYIIHAEGNER 408
Cdd:PRK12316 2275 AASLRLaWEALRPVYLFNGYGPTEAVVTPLlwkcrpqDPCGAAYVP--IGRALGNR------------RAYILDADLNLL 2340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 409 GTKVTpgfeekeGELLVRGPSVFREYWDKPEETKSAFTSDGW-------FRTGDTAVFK-DARYWIRGRtsVD-IIKTGG 479
Cdd:PRK12316 2341 APGMA-------GELYLGGEGLARGYLNRPGLTAERFVPDPFsasgerlYRTGDLARYRaDGVVEYLGR--IDhQVKIRG 2411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 480 YKVSALEIERHLLAHPSITDVAVIGVpDMTWGQRVTAVVALQEGHSLSHGDLKEWARGVLAPYAVPSELLLVEEIPRNQM 559
Cdd:PRK12316 2412 FRIELGEIEARLQAHPAVREAVVVAQ-DGASGKQLVAYVVPDDAAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPN 2490
|
570
....*....|
gi 1720427507 560 GKVNKKELLK 569
Cdd:PRK12316 2491 GKLDRKALPK 2500
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
54-562 |
2.18e-36 |
|
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: 143.49 E-value: 2.18e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 54 GDRIALI------DKYGHHTYRELYDRSLCLAQEIcRLQGCKVGDlqeeRVSFLCSNDVSYVVAQWASWMSGGVAVPLYW 127
Cdd:cd17634 67 GDRTAIIyegddtSQSRTISYRELHREVCRFAGTL-LDLGVKKGD----RVAIYMPMIPEAAVAMLACARIGAVHSVIFG 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 128 KHPEAQLEYFIQDSRSSLVVVGQEYLE--RLSPLAQRLGVPLLPLTPAVYHGATEKPTEQPVEESG-----WRDRGA--- 197
Cdd:cd17634 142 GFAPEAVAGRIIDSSSRLLITADGGVRagRSVPLKKNVDDALNPNVTSVEHVIVLKRTGSDIDWQEgrdlwWRDLIAkas 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 198 --------------MIFYTSGTTGRPKGALSTHRNLA-AVVTGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGA 262
Cdd:cd17634 222 pehqpeamnaedplFILYTSGTTGKPKGVLHTTGGYLvYAATTMKYVFDYGPGDIYWCTADVGWVTGHSYLLYGPLACGA 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 263 TCVMlpeFSAQQVWekflsseapqitvfmavPTVySKLLDYYDKH-----FTQPHVqdfVRAVCKE---------RIRLM 328
Cdd:cd17634 302 TTLL---YEGVPNW-----------------PTP-ARMWQVVDKHgvnilYTAPTA---IRALMAAgddaiegtdRSSLR 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 329 VSGSAALPV-PllEKWRSATGHTLLER------YGMTEIGMALSNPL--TEARVPGSVGTPLPGVEVRIIsenpqkgspy 399
Cdd:cd17634 358 ILGSVGEPInP--EAYEWYWKKIGKEKcpvvdtWWQTETGGFMITPLpgAIELKAGSATRPVFGVQPAVV---------- 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 400 iihaegNERGTKVTPGfeeKEGELLVRG--PSVFREYWDKPEETKSAF--TSDGWFRTGDTA-VFKDARYWIRGRtSVDI 474
Cdd:cd17634 426 ------DNEGHPQPGG---TEGNLVITDpwPGQTRTLFGDHERFEQTYfsTFKGMYFSGDGArRDEDGYYWITGR-SDDV 495
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 475 IKTGGYKVSALEIERHLLAHPSITDVAVIGVPDMTWGQRVTAVVALQEGHSLSHG---DLKEWARGVLAPYAVPSELLLV 551
Cdd:cd17634 496 INVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNHGVEPSPElyaELRNWVRKEIGPLATPDVVHWV 575
|
570
....*....|.
gi 1720427507 552 EEIPRNQMGKV 562
Cdd:cd17634 576 DSLPKTRSGKI 586
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
197-571 |
3.78e-36 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 138.64 E-value: 3.78e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 197 AMIFYTSGTTGRPKGALSTHRNLAAVVT------GLVHSWawtkndviLHVLPLHHVHGVvNKLLCPLWVGATCVMLpef 270
Cdd:PRK07824 38 ALVVATSGTTGTPKGAMLTAAALTASADathdrlGGPGQW--------LLALPAHHIAGL-QVLVRSVIAGSEPVEL--- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 271 saqQVWEKFLSSEAPQITVFMAVPTVYSKLLDY-YDKHFTQPHVQDFVRavckeRIRLMVSGSAALPVPLLEKWRSAtGH 349
Cdd:PRK07824 106 ---DVSAGFDPTALPRAVAELGGGRRYTSLVPMqLAKALDDPAATAALA-----ELDAVLVGGGPAPAPVLDAAAAA-GI 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 350 TLLERYGMTEIGmalsnpltearvPGSV--GTPLPGVEVRIIsenpqkgspyiihaegnergtkvtpgfeekEGELLVRG 427
Cdd:PRK07824 177 NVVRTYGMSETS------------GGCVydGVPLDGVRVRVE------------------------------DGRIALGG 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 428 PSVFREYWDKPEEtkSAFTSDGWFRTGDTAVFKDARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSITDVAVIGVPD 507
Cdd:PRK07824 215 PTLAKGYRNPVDP--DPFAEPGWFRTDDLGALDDGVLTVLGRAD-DAISTGGLTVLPQVVEAALATHPAVADCAVFGLPD 291
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720427507 508 MTWGQRVTAVVALQEGHSLSHGDLKEWARGVLAPYAVPSELLLVEEIPRNQMGKVNKKELLKQL 571
Cdd:PRK07824 292 DRLGQRVVAAVVGDGGPAPTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVRRF 355
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
197-536 |
6.95e-35 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.
Pssm-ID: 341294 [Multi-domain] Cd Length: 507 Bit Score: 138.12 E-value: 6.95e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 197 AMIFYTSGTTGRPKGALSTHRNLAAVVTGLVH--SWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPefsaqq 274
Cdd:cd17639 91 ACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDrvPELLGPDDRYLAYLPLAHIFELAAENVCLYRGGTIGYGSP------ 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 275 vweKFLSSE----------APQITVFMAVPTVY--------SKL------------LDYYDKHFTQPHVQD--------F 316
Cdd:cd17639 165 ---RTLTDKskrgckgdltEFKPTLMVGVPAIWdtirkgvlAKLnpmgglkrtlfwTAYQSKLKALKEGPGtplldelvF 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 317 --VRAVCKERIRLMVSGSAALPvPLLEKWRSATGHTLLERYGMTEI--GMALSNPltEARVPGSVGTPLPGVEVRIISEn 392
Cdd:cd17639 242 kkVRAALGGRLRYMLSGGAPLS-ADTQEFLNIVLCPVIQGYGLTETcaGGTVQDP--GDLETGRVGPPLPCCEIKLVDW- 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 393 pqkgspyiihAEGNERGTKVTPgfeekEGELLVRGPSVFREYWDKPEETKSAFTSDGWFRTGDTAVF-KDARYWIRGRTS 471
Cdd:cd17639 318 ----------EEGGYSTDKPPP-----RGEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFhPDGTLKIIDRKK 382
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720427507 472 vDIIKT--GGYkvSALE-IERHLLAHPSITDVAVIGVPDMTwgqRVTAVVALQEGHslshgdLKEWAR 536
Cdd:cd17639 383 -DLVKLqnGEY--IALEkLESIYRSNPLVNNICVYADPDKS---YPVAIVVPNEKH------LTKLAE 438
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
197-571 |
9.72e-35 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 138.38 E-value: 9.72e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 197 AMIFYTSGTTGRPKGALSTHRNLAAVVTGL--VHSWAWTKNDVILHVLPLHHV--HGVvnkllcPL--WVGATCVMLP-- 268
Cdd:PRK05620 184 AAICYSTGTTGAPKGVVYSHRSLYLQSLSLrtTDSLAVTHGESFLCCVPIYHVlsWGV------PLaaFMSGTPLVFPgp 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 269 EFSAQQVwEKFLSSEAPQitVFMAVPTVYSKLLDYYDKHftQPhvqdfvravckERIRL--MVSGSAALPVPLLEKWRSA 346
Cdd:PRK05620 258 DLSAPTL-AKIIATAMPR--VAHGVPTLWIQLMVHYLKN--PP-----------ERMSLqeIYVGGSAVPPILIKAWEER 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 347 TGHTLLERYGMTEIGMAlsnpltearvpGSVGTPLPGV--EVRIISENPQKGSP----YIIHAEGNergtkVTPGFEEKE 420
Cdd:PRK05620 322 YGVDVVHVWGMTETSPV-----------GTVARPPSGVsgEARWAYRVSQGRFPasleYRIVNDGQ-----VMESTDRNE 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 421 GELLVRGPSVFREYWDKP----------------EETKSAFTSDGWFRTGDTA-VFKDARYWIRGRTSvDIIKTGGYKVS 483
Cdd:PRK05620 386 GEIQVRGNWVTASYYHSPteegggaastfrgedvEDANDRFTADGWLRTGDVGsVTRDGFLTIHDRAR-DVIRSGGEWIY 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 484 ALEIERHLLAHPSITDVAVIGVPDMTWGQRVTAVVALQEGHSLSHG---DLKEWARGVLAPYAVPSELLLVEEIPRNQMG 560
Cdd:PRK05620 465 SAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGIEPTREtaeRLRDQLRDRLPNWMLPEYWTFVDEIDKTSVG 544
|
410
....*....|.
gi 1720427507 561 KVNKKELLKQL 571
Cdd:PRK05620 545 KFDKKDLRQHL 555
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
36-581 |
5.43e-34 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 135.91 E-value: 5.43e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 36 PEA----HTDGSvpvfiRALAFGDRIALIDKYGHHTYrelydrslclAQEICrlqgckvgdlQEERVSFLCSNDVSYVVA 111
Cdd:PRK05857 28 PEAialrRCDGT-----SALRYRELVAEVGGLAADLR----------AQSVS----------RGSRVLVISDNGPETYLS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 112 QWASWMSGGVAVPLYWKHPEAQLEYFIQDSRSSLVVVGQEYLERLSPLAQRL-GVPLLPL------TPAVYHGATEKPTE 184
Cdd:PRK05857 83 VLACAKLGAIAVMADGNLPIAAIERFCQITDPAAALVAPGSKMASSAVPEALhSIPVIAVdiaavtRESEHSLDAASLAG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 185 QPveESGWRDRGAMIFyTSGTTGRPKGALSTHRNLAAV-----VTGLvhSWA-WTKNDVILHVLPLHHVHGVVNKLLCpL 258
Cdd:PRK05857 163 NA--DQGSEDPLAMIF-TSGTTGEPKAVLLANRTFFAVpdilqKEGL--NWVtWVVGETTYSPLPATHIGGLWWILTC-L 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 259 WVGATCVMLPEFSAQQVweKFLSSEAPQITVFmaVPTVYSKLLdyYDKHFTqphvqdfvrAVCKERIRLMVSGSA---AL 335
Cdd:PRK05857 237 MHGGLCVTGGENTTSLL--EILTTNAVATTCL--VPTLLSKLV--SELKSA---------NATVPSLRLVGYGGSraiAA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 336 PVPLLEkwrsATGHTLLERYGMTEIG-MALSNPLTEARVP----GSVGTPLPGVEVRIISENpqKGSPyiihaegNERGT 410
Cdd:PRK05857 302 DVRFIE----ATGVRTAQVYGLSETGcTALCLPTDDGSIVkieaGAVGRPYPGVDVYLAATD--GIGP-------TAPGA 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 411 KVTPGFeekeGELLVRGPSVFREYWDKPEETKSAFTsDGWFRTGDTAVFK-DARYWIRGRTSvDIIKTGGYKVSALEIER 489
Cdd:PRK05857 369 GPSASF----GTLWIKSPANMLGYWNNPERTAEVLI-DGWVNTGDLLERReDGFFYIKGRSS-EMIICGGVNIAPDEVDR 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 490 HLLAHPSITDVAVIGVPDMTWGQRV-TAVVALQEGHSLSHGDLKewaRGVLAPY-------AVPSELLLVEEIPRNQMGK 561
Cdd:PRK05857 443 IAEGVSGVREAACYEIPDEEFGALVgLAVVASAELDESAARALK---HTIAARFrresepmARPSTIVIVTDIPRTQSGK 519
|
570 580
....*....|....*....|
gi 1720427507 562 VNKKELLKQLYPSGQRSQPG 581
Cdd:PRK05857 520 VMRASLAAAATADKARVVVR 539
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
49-567 |
5.70e-34 |
|
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: 133.97 E-value: 5.70e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 49 RALAFGDRIALIDKYGHHTYRELYDRSLCLAQEICRLQGCKvGDlqeeRVSFLCSNDVSYVVAQWASWMSGGVAVPLYWK 128
Cdd:cd17653 6 IAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVP-GD----VVPLLSDRSLEMLVAILAILKAGAAYVPLDAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 129 HPEAQLEYFIQDSRSSLVVvgqeylerlsplaqrlgvpllpltpavyhgatekPTEQPveesgwrDRGAMIFYTSGTTGR 208
Cdd:cd17653 81 LPSARIQAILRTSGATLLL----------------------------------TTDSP-------DDLAYIIFTSGSTGI 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 209 PKGALSTHRNLAAVVT---GLVHSwawTKNDVILHVLPLHHVHGVvNKLLCPLWVGATCVmLPEFSAQqvwekfLSSEAP 285
Cdd:cd17653 120 PKGVMVPHRGVLNYVSqppARLDV---GPGSRVAQVLSIAFDACI-GEIFSTLCNGGTLV-LADPSDP------FAHVAR 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 286 QITVFMAVPTVYSKLldyydkhftqpHVQDFvravckERIRLMVSGSAALPVPLLEKWRSatGHTLLERYGMTEIGMALS 365
Cdd:cd17653 189 TVDALMSTPSILSTL-----------SPQDF------PNLKTIFLGGEAVPPSLLDRWSP--GRRLYNAYGPTECTISST 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 366 NPLTEARVPGSVGTPLPGVEVRIISENPQkgspyiihaegnergtkvtPGFEEKEGELLVRGPSVFREYWDKPEETKSAF 445
Cdd:cd17653 250 MTELLPGQPVTIGKPIPNSTCYILDADLQ-------------------PVPEGVVGEICISGVQVARGYLGNPALTASKF 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 446 TSDGW------FRTGDTAVF-KDARYWIRGRTSVDIiKTGGYKVSALEIERHLLA-HPSITDVAVIGVPDmtwgqrvtAV 517
Cdd:cd17653 311 VPDPFwpgsrmYRTGDYGRWtEDGGLEFLGREDNQV-KVRGFRINLEEIEEVVLQsQPEVTQAAAIVVNG--------RL 381
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1720427507 518 VALQEGHSLSHGDLKEWARGVLAPYAVPSELLLVEEIPRNQMGKVNKKEL 567
Cdd:cd17653 382 VAFVTPETVDVDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKAL 431
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
49-567 |
8.23e-34 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 135.19 E-value: 8.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 49 RALAFGDRIALIDKYGHHTYRelydRSLCLAQEICRLQGCKVGDLQEervsflcsNDVSYVVAQWASWMSGGVAVPLYWK 128
Cdd:PRK07867 20 RGLYFEDSFTSWREHIRGSAA----RAAALRARLDPTRPPHVGVLLD--------NTPEFSLLLGAAALSGIVPVGLNPT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 129 HPEAQLEYFIQDSRSSLVVVGQEYLERLSPLAQrlGVPLLPLTPAVYHG--ATEKPTEQPVEESGWRDRgAMIFYTSGTT 206
Cdd:PRK07867 88 RRGAALARDIAHADCQLVLTESAHAELLDGLDP--GVRVINVDSPAWADelAAHRDAEPPFRVADPDDL-FMLIFTSGTS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 207 GRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSAQQvwekFLsseaPQ 286
Cdd:PRK07867 165 GDPKAVRCTHRKVASAGVMLAQRFGLGPDDVCYVSMPLFHSNAVMAGWAVALAAGASIALRRKFSASG----FL----PD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 287 ITVFMAVPTVY-SKLLDYYdkhFTQPHVQDfvravckER---IRLMVsGSAALPVPLlEKWRSATGHTLLERYGMTEIGM 362
Cdd:PRK07867 237 VRRYGATYANYvGKPLSYV---LATPERPD-------DAdnpLRIVY-GNEGAPGDI-ARFARRFGCVVVDGFGSTEGGV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 363 ALSNplTEARVPGSVGTPLPGVEVRiiseNPQKGS---PYIIHAEGNERGTKVTpgfeekeGELL-VRGPSVFREYWDKP 438
Cdd:PRK07867 305 AITR--TPDTPPGALGPLPPGVAIV----DPDTGTecpPAEDADGRLLNADEAI-------GELVnTAGPGGFEGYYNDP 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 439 EETkSAFTSDGWFRTGDTAvFKDAR--YWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSITDVAVIGVPDMTWGQRVTA 516
Cdd:PRK07867 372 EAD-AERMRGGVYWSGDLA-YRDADgyAYFAGRLG-DWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMA 448
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1720427507 517 VVALQEGHSLSHGDLKEW--ARGVLAPYAVPSELLLVEEIPRNQMGKVNKKEL 567
Cdd:PRK07867 449 ALVLAPGAKFDPDAFAEFlaAQPDLGPKQWPSYVRVCAELPRTATFKVLKRQL 501
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
199-563 |
2.67e-33 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 130.58 E-value: 2.67e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 199 IFYTSGTTGRPKGALSTH----------RNLAAVV----TGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATC 264
Cdd:cd05924 8 ILYTGGTTGMPKGVMWRQedifrmlmggADFGTGEftpsEDAHKAAAAAAGTVMFPAPPLMHGTGSWTAFGGLLGGQTVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 265 VMLPEFSAQQVWEkflSSEAPQITVFMAVPTVYSK-LLDYYDKhftqPHVQDFvravckERIRLMVSGSAALPVPLLEKW 343
Cdd:cd05924 88 LPDDRFDPEEVWR---TIEKHKVTSMTIVGDAMARpLIDALRD----AGPYDL------SSLFAISSGGALLSPEVKQGL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 344 RSATGH-TLLERYGMTEIGMALSnpltearvpGSVGTPLPGVEVRIiseNPQKGSPYIihaegNERGTKVTPGfEEKEGE 422
Cdd:cd05924 155 LELVPNiTLVDAFGSSETGFTGS---------GHSAGSGPETGPFT---RANPDTVVL-----DDDGRVVPPG-SGGVGW 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 423 LLVRGpSVFREYWDKPEETKSAF-TSDG--WFRTGDTA-VFKDARYWIRGRTSVdIIKTGGYKVSALEIERHLLAHPSIT 498
Cdd:cd05924 217 IARRG-HIPLGYYGDEAKTAETFpEVDGvrYAVPGDRAtVEADGTVTLLGRGSV-CINTGGEKVFPEEVEEALKSHPAVY 294
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720427507 499 DVAVIGVPDMTWGQRVTAVVALQEGHSLSHGDLKEWARGVLAPYAVPSELLLVEEIPRNQMGKVN 563
Cdd:cd05924 295 DVLVVGRPDERWGQEVVAVVQLREGAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGKAD 359
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
67-567 |
4.15e-33 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 132.83 E-value: 4.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 67 TYRELYDRSLCLAQeICRLQGCKVGDLqeerVSFLCSNDVSYVVAQWASWMSG--GVAVPLYWKHPEAqlEYFIQDSRSS 144
Cdd:PRK13390 26 SYRQLDDDSAALAR-VLYDAGLRTGDV----VALLSDNSPEALVVLWAALRSGlyITAINHHLTAPEA--DYIVGDSGAR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 145 LVVVGQEylerLSPLAQRLGVPLlPLT-------------PAVYHGATEKPTEQPVeesgwrdrGAMIFYTSGTTGRPKG 211
Cdd:PRK13390 99 VLVASAA----LDGLAAKVGADL-PLRlsfggeidgfgsfEAALAGAGPRLTEQPC--------GAVMLYSSGTTGFPKG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 212 ALST--HRN-------LAAVVTGLvhsWAWTKNDVILHVLPLHHVH-----GVVNKLlcplwvGATCVMLPEFSAQQVW- 276
Cdd:PRK13390 166 IQPDlpGRDvdapgdpIVAIARAF---YDISESDIYYSSAPIYHAAplrwcSMVHAL------GGTVVLAKRFDAQATLg 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 277 --EKFlsseapQITVFMAVPTVYSKLLDYYDKHFTQPHVQDfvravckerIRLMVSGSAALPVPLLEKWRSATGHTLLER 354
Cdd:PRK13390 237 hvERY------RITVTQMVPTMFVRLLKLDADVRTRYDVSS---------LRAVIHAAAPCPVDVKHAMIDWLGPIVYEY 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 355 YGMTEI-GMALSNPLTEARVPGSVGTPLpgvevriisenpqKGSPYIIHAEGNE--RGTKVTPGFEekegellvRGPSVF 431
Cdd:PRK13390 302 YSSTEAhGMTFIDSPDWLAHPGSVGRSV-------------LGDLHICDDDGNElpAGRIGTVYFE--------RDRLPF 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 432 ReYWDKPEETKSAF--TSDGWFRTGDTAVFKDARY-WIRGRTSVDIIkTGGYKVSALEIERHLLAHPSITDVAVIGVPDM 508
Cdd:PRK13390 361 R-YLNDPEKTAAAQhpAHPFWTTVGDLGSVDEDGYlYLADRKSFMII-SGGVNIYPQETENALTMHPAVHDVAVIGVPDP 438
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720427507 509 TWGQRVTAVVALQEGHSLSHG---DLKEWARGVLAPYAVPSELLLVEEIPRNQMGKVNKKEL 567
Cdd:PRK13390 439 EMGEQVKAVIQLVEGIRGSDElarELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLL 500
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
50-567 |
5.71e-33 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 135.67 E-value: 5.71e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 50 ALAFGDRialidkygHHTYRELYDRSLCLAQEICRLqgckvGDLQEERVSFLCSNDVSYVVAQWASWMSGGVAVPLYWKH 129
Cdd:PRK12467 1592 ALVFGEQ--------ELTYGELNRRANRLAHRLIAL-----GVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEY 1658
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 130 PEAQLEYFIQDSRSSLVVVGQEYLERLsPLAQrlGVPLLPLTPAVYHGATEKPTEQPVEESGwrDRGAMIFYTSGTTGRP 209
Cdd:PRK12467 1659 PRERLAYMIEDSGIELLLTQSHLQARL-PLPD--GLRSLVLDQEDDWLEGYSDSNPAVNLAP--QNLAYVIYTSGSTGRP 1733
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 210 KGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPlHHVHGVVNKLLCPLWVGATCVMLPeFSAQQVWEKFLSS-EAPQIT 288
Cdd:PRK12467 1734 KGAGNRHGALVNRLCATQEAYQLSAADVVLQFTS-FAFDVSVWELFWPLINGARLVIAP-PGAHRDPEQLIQLiERQQVT 1811
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 289 VFMAVPTVYSKLLDyYDKHFTQPhvqdfvravckERIRLMVSGSAALPVPLLEKWRSATGHT-LLERYGMTEIGM----- 362
Cdd:PRK12467 1812 TLHFVPSMLQQLLQ-MDEQVEHP-----------LSLRRVVCGGEALEVEALRPWLERLPDTgLFNLYGPTETAVdvthw 1879
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 363 ALSNPLTEARVPGSVGTPLPGVevriisenpqkgSPYIIHAEGNERGTKVTpgfeekeGELLVRGPSVFREYWDKPEETK 442
Cdd:PRK12467 1880 TCRRKDLEGRDSVPIGQPIANL------------STYILDASLNPVPIGVA-------GELYLGGVGLARGYLNRPALTA 1940
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 443 SAFTSDGW-------FRTGDTavfkdARYwiRGRTSVDI-------IKTGGYKVSALEIERHLLAHPSITDVAVIGVPDM 508
Cdd:PRK12467 1941 ERFVADPFgtvgsrlYRTGDL-----ARY--RADGVIEYlgridhqVKIRGFRIELGEIEARLREQGGVREAVVIAQDGA 2013
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720427507 509 TWGQRVTAVVALQEG-------HSLSHGDLKEWARGVLAPYAVPSELLLVEEIPRNQMGKVNKKEL 567
Cdd:PRK12467 2014 NGKQLVAYVVPTDPGlvdddeaQVALRAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKAL 2079
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
50-583 |
2.49e-32 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 133.54 E-value: 2.49e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 50 ALAFGDRIAlidkyghhTYRELYDRSLCLAQeicRLQGCKVGdlQEERVSFLCSNDVSYVVAQWASWMSGGVAVPLYWKH 129
Cdd:PRK12316 529 ALAFGEETL--------DYAELNRRANRLAH---ALIERGVG--PDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEY 595
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 130 PEAQLEYFIQDSRSSLVVvGQEYLERLSPLAQRLGVPLLPLTPAVYHGATEKPTEQPVEEsgwrDRGAMIFYTSGTTGRP 209
Cdd:PRK12316 596 PAERLAYMLEDSGVQLLL-SQSHLGRKLPLAAGVQVLDLDRPAAWLEGYSEENPGTELNP----ENLAYVIYTSGSTGKP 670
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 210 KGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVnKLLCPLWVGATCVMLPE---FSAQQVWEkflSSEAPQ 286
Cdd:PRK12316 671 KGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVW-EFFWPLMSGARLVVAAPgdhRDPAKLVE---LINREG 746
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 287 ITVFMAVPTVYSKLLdyydkhftqphvQDFVRAVCKErIRLMVSGSAALPVPLLEK--WRSATGHtLLERYGMTE--IGM 362
Cdd:PRK12316 747 VDTLHFVPSMLQAFL------------QDEDVASCTS-LRRIVCSGEALPADAQEQvfAKLPQAG-LYNLYGPTEaaIDV 812
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 363 ALSNPLTEARVPGSVGTPLPGVevriisenpqkgSPYIIHAEGNERGTKVTpgfeekeGELLVRGPSVFREYWDKPEETK 442
Cdd:PRK12316 813 THWTCVEEGGDSVPIGRPIANL------------ACYILDANLEPVPVGVL-------GELYLAGRGLARGYHGRPGLTA 873
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 443 SAFTSDGW------FRTGDTAVFK-DARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSITDVAVIGVPdmtwGQRVT 515
Cdd:PRK12316 874 ERFVPSPFvagermYRTGDLARYRaDGVIEYAGRID-HQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GKQLV 948
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720427507 516 AVVALQEGHSLSHGDLKEWARGVLAPYAVPSELLLVEEIPRNQMGKVNKKELlkqlyPSGQRSQPGQG 583
Cdd:PRK12316 949 GYVVLESEGGDWREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKAL-----PAPEASVAQQG 1011
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
49-567 |
5.69e-32 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 132.39 E-value: 5.69e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 49 RALAFGDRIALIDKYGHHTYRELYDRSLCLAQeicRLQGCKVGdlQEERVSFLCSNDVSYVVAQWASWMSGGVAVPLYWK 128
Cdd:PRK12316 4560 RARMTPDAVAVVFDEEKLTYAELNRRANRLAH---ALIARGVG--PEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPE 4634
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 129 HPEAQLEYFIQDSRSSLVVVGQEYLERLsPLAQrlGVPLLPLTPA-VYHGATEKPTEQPVEEsgwrDRGAMIFYTSGTTG 207
Cdd:PRK12316 4635 YPRERLAYMMEDSGAALLLTQSHLLQRL-PIPD--GLASLALDRDeDWEGFPAHDPAVRLHP----DNLAYVIYTSGSTG 4707
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 208 RPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLhHVHGVVNKLLCPLWVGATCVM------LPEFSAQQVWEKfls 281
Cdd:PRK12316 4708 RPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSF-SFDGSHEGLYHPLINGASVVIrddslwDPERLYAEIHEH--- 4783
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 282 seapQITVFMAVPTVYSKLLdyydkhftqphvQDFVRAVCKERIRLMVSGSAALPVPLLEK-WRSATGHTLLERYGMTEi 360
Cdd:PRK12316 4784 ----RVTVLVFPPVYLQQLA------------EHAERDGEPPSLRVYCFGGEAVAQASYDLaWRALKPVYLFNGYGPTE- 4846
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 361 gmALSNPLTEARVPGS--------VGTPLPGVevriisenpqkgSPYIIHAEGNERGTKVTpgfeekeGELLVRGPSVFR 432
Cdd:PRK12316 4847 --TTVTVLLWKARDGDacgaaympIGTPLGNR------------SGYVLDGQLNPLPVGVA-------GELYLGGEGVAR 4905
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 433 EYWDKPEETKSAFTSDGW-------FRTGDTAVFK-DARYWIRGRtsVD-IIKTGGYKVSALEIERHLLAHPSITDVAVI 503
Cdd:PRK12316 4906 GYLERPALTAERFVPDPFgapggrlYRTGDLARYRaDGVIDYLGR--VDhQVKIRGFRIELGEIEARLREHPAVREAVVI 4983
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720427507 504 GVPDMTWGQRV-------TAVVALQEGHSLSHGDLKEWARGVLAPYAVPSELLLVEEIPRNQMGKVNKKEL 567
Cdd:PRK12316 4984 AQEGAVGKQLVgyvvpqdPALADADEAQAELRDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKAL 5054
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
53-567 |
6.29e-32 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 130.14 E-value: 6.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 53 FGDRIALIDKYGHHTYRELYDRSLCLAQEICRLQGCKvgdlqEERVSFLCSNDVSYVVAQWASWMSGGVAVPLYWKHPEA 132
Cdd:PLN03102 27 YPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNITK-----NDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 133 QLEYFIQDSRSSLVVVGQEYlerlSPLAQRLgVPLLPLTPAVYH---------GATEKPTEQPVEESGWRDRG------- 196
Cdd:PLN03102 102 SIAAILRHAKPKILFVDRSF----EPLAREV-LHLLSSEDSNLNlpvifiheiDFPKRPSSEELDYECLIQRGeptpslv 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 197 AMIF------------YTSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGvvnkllcplWV---- 260
Cdd:PLN03102 177 ARMFriqdehdpislnYTSGTTADPKGVVISHRGAYLSTLSAIIGWEMGTCPVYLWTLPMFHCNG---------WTftwg 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 261 ----GATCVMLPEFSAQQVWEKFlssEAPQITVFMAVPTVYSKLL--DYYDKHFTQPHVQdfvravckerirlMVSGSAA 334
Cdd:PLN03102 248 taarGGTSVCMRHVTAPEIYKNI---EMHNVTHMCCVPTVFNILLkgNSLDLSPRSGPVH-------------VLTGGSP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 335 LPVPLLEKWRSaTGHTLLERYGMTE-IGMALSNPLTEA--RVPgsvgtplpgvEVRIISENPQKGSPYIIHAEGNERGTK 411
Cdd:PLN03102 312 PPAALVKKVQR-LGFQVMHAYGLTEaTGPVLFCEWQDEwnRLP----------ENQQMELKARQGVSILGLADVDVKNKE 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 412 V---TPGFEEKEGELLVRGPSVFREYWDKPEETKSAFtSDGWFRTGDTAVFK-DARYWIRGRtSVDIIKTGGYKVSALEI 487
Cdd:PLN03102 381 TqesVPRDGKTMGEIVIKGSSIMKGYLKNPKATSEAF-KHGWLNTGDVGVIHpDGHVEIKDR-SKDIIISGGENISSVEV 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 488 ERHLLAHPSITDVAVIGVPDMTWGQRVTAVVALQEGHS----------LSHGDLKEWARGVLAPYAVPSELLLVEEIPRN 557
Cdd:PLN03102 459 ENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETtkedrvdklvTRERDLIEYCRENLPHFMCPRKVVFLQELPKN 538
|
570
....*....|
gi 1720427507 558 QMGKVNKKEL 567
Cdd:PLN03102 539 GNGKILKPKL 548
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
67-570 |
1.45e-31 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 130.15 E-value: 1.45e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 67 TYRELYDRSLCLAqEICRLQGCKVGDlqeeRVsFLCSNDVSYVVAQWASWMSGGVAVplYWKHPEAQLEYFI---QDSRS 143
Cdd:PRK06060 32 THGQIHDGAARLG-EVLRNRGLSSGD----RV-LLCLPDSPDLVQLLLACLARGVMA--FLANPELHRDDHAlaaRNTEP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 144 SLVVVGQEYLERLSPLAQRLGVPLLPltpavyHGATEKPTE-QPVeeSGwrDRGAMIFYTSGTTGRPKGALSTHRNLAAV 222
Cdd:PRK06060 104 ALVVTSDALRDRFQPSRVAEAAELMS------EAARVAPGGyEPM--GG--DALAYATYTSGTTGPPKAAIHRHADPLTF 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 223 VTGLV-HSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSAQQVWEKFLSSEAPqiTVFMAVPTVYSKLL 301
Cdd:PRK06060 174 VDAMCrKALRLTPEDTGLCSARMYFAYGLGNSVWFPLATGGSAVINSAPVTPEAAAILSARFGP--SVLYGVPNFFARVI 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 302 DYYDKhftqphvqDFVRAVckeriRLMVSGSAALPVPLLEKWRSATGHT-LLERYGMTEIGMA-LSNPLTEARvPGSVGT 379
Cdd:PRK06060 252 DSCSP--------DSFRSL-----RCVVSAGEALELGLAERLMEFFGGIpILDGIGSTEVGQTfVSNRVDEWR-LGTLGR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 380 PLPGVEVRIISENpqkgspyiihaegnerGTKVTPGFEekeGELLVRGPSVFREYWDKPEetkSAFTSDGWFRTGDTAVF 459
Cdd:PRK06060 318 VLPPYEIRVVAPD----------------GTTAGPGVE---GDLWVRGPAIAKGYWNRPD---SPVANEGWLDTRDRVCI 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 460 KDARYWIRGRTSVDIIKTGGYKVSALEIERHLLAHPSITDVAVIGVPDMTWGQRVTAVVALQEGHSLSHGDLKEWARGV- 538
Cdd:PRK06060 376 DSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGATIDGSVMRDLHRGLl 455
|
490 500 510
....*....|....*....|....*....|....
gi 1720427507 539 --LAPYAVPSELLLVEEIPRNQMGKVNKKELLKQ 570
Cdd:PRK06060 456 nrLSAFKVPHRFAVVDRLPRTPNGKLVRGALRKQ 489
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
145-570 |
2.65e-31 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 127.84 E-value: 2.65e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 145 LVVVGQEYLERLSPLAQRlGVPLLPLTPAVYHGATEKPTE-QPVEESGWRDRGAMIFyTSGTTGRPKGALSTHRNLAAVV 223
Cdd:PRK13388 102 LLVTDAEHRPLLDGLDLP-GVRVLDVDTPAYAELVAAAGAlTPHREVDAMDPFMLIF-TSGTTGAPKAVRCSHGRLAFAG 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 224 TGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSAQqvweKFLsseaPQITVFMAVPTVY-SKLLD 302
Cdd:PRK13388 180 RALTERFGLTRDDVCYVSMPLFHSNAVMAGWAPAVASGAAVALPAKFSAS----GFL----DDVRRYGATYFNYvGKPLA 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 303 YYDKHFTQPHVQD--FVRAVckerirlmvsGSAALPVPLlEKWRSATGHTLLERYGMTEIGMALSNPltEARVPGSVGTP 380
Cdd:PRK13388 252 YILATPERPDDADnpLRVAF----------GNEASPRDI-AEFSRRFGCQVEDGYGSSEGAVIVVRE--PGTPPGSIGRG 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 381 LPGVEVRiiseNPQKGSPYIIhAEGNERGTKVTPgfEEKEGELLVR-GPSVFREYWDKPEETKSAFtSDGWFRTGDTAvF 459
Cdd:PRK13388 319 APGVAIY----NPETLTECAV-ARFDAHGALLNA--DEAIGELVNTaGAGFFEGYYNNPEATAERM-RHGMYWSGDLA-Y 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 460 KDARYWI--RGRTSvDIIKTGGYKVSALEIERHLLAHPSITDVAVIGVPDMTWGQRVTAVVALQEGHSLSHGDLKEW--A 535
Cdd:PRK13388 390 RDADGWIyfAGRTA-DWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVMAALVLRDGATFDPDAFAAFlaA 468
|
410 420 430
....*....|....*....|....*....|....*
gi 1720427507 536 RGVLAPYAVPSELLLVEEIPRNQMGKVNKKELLKQ 570
Cdd:PRK13388 469 QPDLGTKAWPRYVRIAADLPSTATNKVLKRELIAQ 503
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
55-567 |
2.23e-30 |
|
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: 124.08 E-value: 2.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 55 DRIALIDKYGHHTYRELYDRSLCLAQeicRLQGCKVGDlqEERVSFLCSNDVSYVVAQWASWMSGGVAVPLYWKHPEAQL 134
Cdd:cd17644 15 DAVAVVFEDQQLTYEELNTKANQLAH---YLQSLGVKS--ESLVGICVERSLEMIIGLLAILKAGGAYVPLDPNYPQERL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 135 EYFIQDSRSSLVVVGQEYLerlsplaqrlgvpllpltpavyhgatekpteqpveesgwrdrgAMIFYTSGTTGRPKGALS 214
Cdd:cd17644 90 TYILEDAQISVLLTQPENL-------------------------------------------AYVIYTSGSTGKPKGVMI 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 215 THRNLAAVVTGLVHSWAWTKNDVILHVLPLhhVHGVVNKLLCPLWV-GATCVMLPE---FSAQQVWEKflsSEAPQITVF 290
Cdd:cd17644 127 EHQSLVNLSHGLIKEYGITSSDRVLQFASI--AFDVAAEEIYVTLLsGATLVLRPEemrSSLEDFVQY---IQQWQLTVL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 291 mAVPTVYSKLLdyydkhftqphVQDFVRAVCK--ERIRLMVSGSAALPVPLLEKWRSATGH--TLLERYGMTEIGMA--- 363
Cdd:cd17644 202 -SLPPAYWHLL-----------VLELLLSTIDlpSSLRLVIVGGEAVQPELVRQWQKNVGNfiQLINVYGPTEATIAatv 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 364 --LSNPLTEARVPGSVGTPLPGVEVRIISENPQKgspyiihaegnergtkVTPGFEekeGELLVRGPSVFREYWDKPEET 441
Cdd:cd17644 270 crLTQLTERNITSVPIGRPIANTQVYILDENLQP----------------VPVGVP---GELHIGGVGLARGYLNRPELT 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 442 KSAFTSDGW--------FRTGDTAVF-KDARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSITDVAVIGVPDMTWGQ 512
Cdd:cd17644 331 AEKFISHPFnsseserlYKTGDLARYlPDGNIEYLGRID-NQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNK 409
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1720427507 513 RVTAVVALQEGHSLSHGDLKEWARGVLAPYAVPSELLLVEEIPRNQMGKVNKKEL 567
Cdd:cd17644 410 RLVAYIVPHYEESPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
55-567 |
2.60e-30 |
|
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: 123.73 E-value: 2.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 55 DRIALIDKYGHHTYRELYDRSLCLAQeicRLQGCKVGdlQEERVSFLCSNDVSYVVAQWASWMSGGVAVPLYWKHPEAQL 134
Cdd:cd17650 2 DAIAVSDATRQLTYRELNERANQLAR---TLRGLGVA--PGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 135 EYFIQDSrsslvvvgqeylerlsplaqrlGVPLLPLTPavyhgatekpteqpveesgwrDRGAMIFYTSGTTGRPKGALS 214
Cdd:cd17650 77 QYMLEDS----------------------GAKLLLTQP---------------------EDLAYVIYTSGTTGKPKGVMV 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 215 THRNLAAVvtglVHSWawtKNDVILHVLPLHHVHGV-------VNKLLCPLWVGATCVMLPE---FSAQQVWEKFLSSEa 284
Cdd:cd17650 114 EHRNVAHA----AHAW---RREYELDSFPVRLLQMAsfsfdvfAGDFARSLLNGGTLVICPDevkLDPAALYDLILKSR- 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 285 pqITVFMAVPTVYSKLLDYYDKHFTQPhvqdfvravckERIRLMVSGS----AALPVPLLEKWRSATghTLLERYGMTEI 360
Cdd:cd17650 186 --ITLMESTPALIRPVMAYVYRNGLDL-----------SAMRLLIVGSdgckAQDFKTLAARFGQGM--RIINSYGVTEA 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 361 GMALS------NPLTEAR-VPgsVGTPLPGVEVRIISE--NPQKGSPYiihaegnergtkvtpgfeekeGELLVRGPSVF 431
Cdd:cd17650 251 TIDSTyyeegrDPLGDSAnVP--IGRPLPNTAMYVLDErlQPQPVGVA---------------------GELYIGGAGVA 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 432 REYWDKPEETKSAFTSDGW------FRTGDTAVFK-DARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSITDVAVIG 504
Cdd:cd17650 308 RGYLNRPELTAERFVENPFapgermYRTGDLARWRaDGNVELLGRVD-HQVKIRGFRIELGEIESQLARHPAIDEAVVAV 386
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720427507 505 VPDMTWGQRVTA-VVAlqeGHSLSHGDLKEWARGVLAPYAVPSELLLVEEIPRNQMGKVNKKEL 567
Cdd:cd17650 387 REDKGGEARLCAyVVA---AATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
194-571 |
7.87e-30 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 125.42 E-value: 7.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 194 DRGAMIFYTSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLP----- 268
Cdd:PRK08633 782 DDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLPFFHSFGLTVTLWLPLLEGIKVVYHPdptda 861
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 269 EFSAQQVwEKFlsseapQITVFMAVPTvyskLLDYYDKHfTQPHVQDFvravckERIRLMVSGSAALPVPLLEKWRSATG 348
Cdd:PRK08633 862 LGIAKLV-AKH------RATILLGTPT----FLRLYLRN-KKLHPLMF------ASLRLVVAGAEKLKPEVADAFEEKFG 923
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 349 HTLLERYGMTEIG--MALSNPLTEAR--------VPGSVGTPLPGVEVRIIseNPqkgspyiihaegnERGTKVTPGfee 418
Cdd:PRK08633 924 IRILEGYGATETSpvASVNLPDVLAAdfkrqtgsKEGSVGMPLPGVAVRIV--DP-------------ETFEELPPG--- 985
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 419 KEGELLVRGPSVFREYWDKPEETKSAFT---SDGWFRTGDTAVF-KDARYWIRGRTSvDIIKTGGYKVS--ALEIERHLL 492
Cdd:PRK08633 986 EDGLILIGGPQVMKGYLGDPEKTAEVIKdidGIGWYVTGDKGHLdEDGFLTITDRYS-RFAKIGGEMVPlgAVEEELAKA 1064
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 493 AHPSITDVAVIGVPDMTWGQRVTAVVALQEghsLSHGDLKE-WARGVLAPYAVPSELLLVEEIPRNQMGKVNKKeLLKQL 571
Cdd:PRK08633 1065 LGGEEVVFAVTAVPDEKKGEKLVVLHTCGA---EDVEELKRaIKESGLPNLWKPSRYFKVEALPLLGSGKLDLK-GLKEL 1140
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
201-570 |
1.70e-29 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 122.78 E-value: 1.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 201 YTSGTTGRPKGALSTHRNLAAvvtGLVHSWAWTKNDVI-----LHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSAQQV 275
Cdd:PLN02330 191 FSSGTTGISKGVMLTHRNLVA---NLCSSLFSVGPEMIgqvvtLGLIPFFHIYGITGICCATLRNKGKVVVMSRFELRTF 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 276 WEKFLSSEapqITVFMAVPTVYSKLLdyydkhfTQPHVQDFvrAVCKERIRLMVSGSAALPVPLLEKWRSA-TGHTLLER 354
Cdd:PLN02330 268 LNALITQE---VSFAPIVPPIILNLV-------KNPIVEEF--DLSKLKLQAIMTAAAPLAPELLTAFEAKfPGVQVQEA 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 355 YGMTE---IGMALSNPLTEARVP--GSVGTPLPGVEVRIIseNPQKGSPYiihaegnergTKVTPGfeekegELLVRGPS 429
Cdd:PLN02330 336 YGLTEhscITLTHGDPEKGHGIAkkNSVGFILPNLEVKFI--DPDTGRSL----------PKNTPG------ELCVRSQC 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 430 VFREYWDKPEETKSAFTSDGWFRTGDTA-VFKDARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSITDVAVIGVPDM 508
Cdd:PLN02330 398 VMQGYYNNKEETDRTIDEDGWLHTGDIGyIDDDGDIFIVDRIK-ELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDE 476
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720427507 509 TWGQRVTAVVALQEGHSLSHGDLKEWARGVLAPYAVPSELLLVEEIPRNQMGKVNKKeLLKQ 570
Cdd:PLN02330 477 EAGEIPAACVVINPKAKESEEDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRR-LLKE 537
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
54-562 |
2.05e-29 |
|
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: 123.05 E-value: 2.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 54 GDRIALI------DKYGHHTYRELYdrslclaQEICRL------QGCKVGDlqeeRVSFLCSNDVSYVVAQWASWMSGGV 121
Cdd:cd05966 67 GDKVAIIwegdepDQSRTITYRELL-------REVCRFanvlksLGVKKGD----RVAIYMPMIPELVIAMLACARIGAV 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 122 avplywkH--------PEAqLEYFIQDSRSSLVVVGQEYL--ERLSPL-------------------AQRLGVPLlPLTP 172
Cdd:cd05966 136 -------HsvvfagfsAES-LADRINDAQCKLVITADGGYrgGKVIPLkeivdealekcpsvekvlvVKRTGGEV-PMTE 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 173 AV---YHGATEK-PTEQPVEesgWRDRGAMIF--YTSGTTGRPKGALSThrnlaavvTG--LVHSWAWTKNdvilhVLPL 244
Cdd:cd05966 207 GRdlwWHDLMAKqSPECEPE---WMDSEDPLFilYTSGSTGKPKGVVHT--------TGgyLLYAATTFKY-----VFDY 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 245 H----------------HVHGVVNKLLCplwvGATCVML------PEFSaqQVWEKFlssEAPQITVFMAVPTVYSKLLD 302
Cdd:cd05966 271 HpddiywctadigwitgHSYIVYGPLAN----GATTVMFegtptyPDPG--RYWDIV---EKHKVTIFYTAPTAIRALMK 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 303 YYDKHftqPHVQDfvravckeRIRLMVSGSAALPV-PllEKWRSATGHTLLER------YGMTEIGMALSNPL---TEAR 372
Cdd:cd05966 342 FGDEW---VKKHD--------LSSLRVLGSVGEPInP--EAWMWYYEVIGKERcpivdtWWQTETGGIMITPLpgaTPLK 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 373 vPGSVGTPLPGVEvriisenpqkgsPYIIHAEGNERGTkvtpgfeEKEGELLVRG--PSVFREYWDKPEETKSAFTSD-- 448
Cdd:cd05966 409 -PGSATRPFFGIE------------PAILDEEGNEVEG-------EVEGYLVIKRpwPGMARTIYGDHERYEDTYFSKfp 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 449 GWFRTGDTAVF-KDARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSITDVAVIGVPDMTWGQRVTAVVALQEGHSLS 527
Cdd:cd05966 469 GYYFTGDGARRdEDGYYWITGRVD-DVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPS 547
|
570 580 590
....*....|....*....|....*....|....*...
gi 1720427507 528 H---GDLKEWARGVLAPYAVPSELLLVEEIPRNQMGKV 562
Cdd:cd05966 548 DelrKELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKI 585
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
130-506 |
2.20e-29 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 122.31 E-value: 2.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 130 PEAQLEYFI----QDSRSSLVVVGQeyleRLSPLAQRLGVPLLPLTPAVYHGATEKPTEQpveesgwrdrgAMIFYTSGT 205
Cdd:PRK09274 121 PKAHLARRLfgwgKPSVRRLVTVGG----RLLWGGTTLATLLRDGAAAPFPMADLAPDDM-----------AAILFTSGS 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 206 TGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVnkllcplwVGATCVmLPEFSA--------QQVW- 276
Cdd:PRK09274 186 TGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDLPTFPLFALFGPA--------LGMTSV-IPDMDPtrpatvdpAKLFa 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 277 --EKFlsseapQITVFMAVPTVYSKLLDYydkhftqphvqdfvravCKER------IRLMVSGSAALPVPLLEKWRSATG 348
Cdd:PRK09274 257 aiERY------GVTNLFGSPALLERLGRY-----------------GEANgiklpsLRRVISAGAPVPIAVIERFRAMLP 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 349 HT--LLERYGMTE------IGM-ALSNPLTEARVPGS---VGTPLPGVEVRII--SENPqkgspyIIHAEGNERgtkVTP 414
Cdd:PRK09274 314 PDaeILTPYGATEalpissIESrEILFATRAATDNGAgicVGRPVDGVEVRIIaiSDAP------IPEWDDALR---LAT 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 415 GfeeKEGELLVRGPSVFREYWDKPEETKSAFTSDG----WFRTGDTAVFKD-ARYWIRGRTSvDIIKTGGYKVSALEIER 489
Cdd:PRK09274 385 G---EIGEIVVAGPMVTRSYYNRPEATRLAKIPDGqgdvWHRMGDLGYLDAqGRLWFCGRKA-HRVETAGGTLYTIPCER 460
|
410
....*....|....*..
gi 1720427507 490 HLLAHPSITDVAVIGVP 506
Cdd:PRK09274 461 IFNTHPGVKRSALVGVG 477
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
50-567 |
6.02e-29 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 121.10 E-value: 6.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 50 ALAFGDRIALIDKYGHHTYRELYDRSLCLAQEICRlQGCKVGDLqeerVSFLCSNDVSYVVAQWASWMSGGVAVPLYWKH 129
Cdd:PLN02479 30 AVVHPTRKSVVHGSVRYTWAQTYQRCRRLASALAK-RSIGPGST----VAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 130 PEAQLEYFIQDSRSSLVVVGQEYL----ERLSPLAQRLG----VPLL-----------PLTPAVYHGATE--KPTEQPVE 188
Cdd:PLN02479 105 NAPTIAFLLEHSKSEVVMVDQEFFtlaeEALKILAEKKKssfkPPLLivigdptcdpkSLQYALGKGAIEyeKFLETGDP 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 189 ESGWR---DRGAMIF--YTSGTTGRPKGALSTHRnlAAVVTGLVHSWAWTKND--VILHVLPLHHVHGvvnklLCPLWVG 261
Cdd:PLN02479 185 EFAWKppaDEWQSIAlgYTSGTTASPKGVVLHHR--GAYLMALSNALIWGMNEgaVYLWTLPMFHCNG-----WCFTWTL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 262 A----TCVMLPEFSAQQVWEKFLSSeapQITVFMAVPTVYSKLLDY--YDKHFTQPHVqdfvravckerIRLMVSGSAal 335
Cdd:PLN02479 258 AalcgTNICLRQVTAKAIYSAIANY---GVTHFCAAPVVLNTIVNApkSETILPLPRV-----------VHVMTAGAA-- 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 336 PVPLLEKWRSATGHTLLERYGMTEIgmalSNPLTE-ARVPGSVGTPlPGVEVRIiseNPQKGSPYiIHAEG----NERGT 410
Cdd:PLN02479 322 PPPSVLFAMSEKGFRVTHTYGLSET----YGPSTVcAWKPEWDSLP-PEEQARL---NARQGVRY-IGLEGldvvDTKTM 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 411 KVTPGFEEKEGELLVRGPSVFREYWDKPEETKSAFtSDGWFRTGDTAV-FKDARYWIRGRtSVDIIKTGGYKVSALEIER 489
Cdd:PLN02479 393 KPVPADGKTMGEIVMRGNMVMKGYLKNPKANEEAF-ANGWFHSGDLGVkHPDGYIEIKDR-SKDIIISGGENISSLEVEN 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 490 HLLAHPSITDVAVIGVPDMTWGQRVTAVVALQEGHSLSH-----GDLKEWARGVLAPYAVPSELLLvEEIPRNQMGKVNK 564
Cdd:PLN02479 471 VVYTHPAVLEASVVARPDERWGESPCAFVTLKPGVDKSDeaalaEDIMKFCRERLPAYWVPKSVVF-GPLPKTATGKIQK 549
|
...
gi 1720427507 565 KEL 567
Cdd:PLN02479 550 HVL 552
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
67-504 |
2.48e-28 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 119.45 E-value: 2.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 67 TYRELYDRSLCLAQEICRLqGCKVGDlqeeRVSFLCSNDVSYVVAQWASWMSGGVAVPLYWKHPEAQLEYFIQDSRSSLV 146
Cdd:cd17641 13 TWADYADRVRAFALGLLAL-GVGRGD----VVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 147 VVG-QEYLERLSPLAQRL------------GV-----PLLPLTPAVYHGATEKPTEQP--VEESGWRDRG---AMIFYTS 203
Cdd:cd17641 88 IAEdEEQVDKLLEIADRIpsvryviycdprGMrkyddPRLISFEDVVALGRALDRRDPglYEREVAAGKGedvAVLCTTS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 204 GTTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGaTCVMLPE-------------- 269
Cdd:cd17641 168 GTTGKPKLAMLSHGNFLGHCAAYLAADPLGPGDEYVSVLPLPWIGEQMYSVGQALVCG-FIVNFPEepetmmedlreigp 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 270 ---FSAQQVWEKFLS------SEAPQITVFM--AVPTVYSKLLDYyDKHFTQPHVQDFVRAVCKERI------------- 325
Cdd:cd17641 247 tfvLLPPRVWEGIAAdvrarmMDATPFKRFMfeLGMKLGLRALDR-GKRGRPVSLWLRLASWLADALlfrplrdrlgfsr 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 326 -RLMVSGSAALPvPLLEKWRSATGHTLLERYGMTEI-GMALSNPLTEARvPGSVGTPLPGVEVRIIsenpqkgspyiiha 403
Cdd:cd17641 326 lRSAATGGAALG-PDTFRFFHAIGVPLKQLYGQTELaGAYTVHRDGDVD-PDTVGVPFPGTEVRID-------------- 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 404 egnergtkvtpgfeeKEGELLVRGPSVFREYWDKPEETKSAFTSDGWFRTGDTAVFKDARYW-IRGRTSvDIIKTG-GYK 481
Cdd:cd17641 390 ---------------EVGEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLvVIDRAK-DVGTTSdGTR 453
|
490 500
....*....|....*....|...
gi 1720427507 482 VSALEIERHLLAHPSITDVAVIG 504
Cdd:cd17641 454 FSPQFIENKLKFSPYIAEAVVLG 476
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
202-569 |
3.44e-28 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 117.79 E-value: 3.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 202 TSGTTGRPKGALSTHRNLAAVVTGL--------VHSwawtkndviLHVLPLHHVHGVVnKLLCPLWVGATCVMLPefsaq 273
Cdd:PRK07445 128 TGGSSGQIRFAIHTWETLTASVQGFqryfqlqqVNS---------FCVLPLYHVSGLM-QFMRSFLTGGKLVILP----- 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 274 qvWEKFLSSEAPQITV---FMA-VPTVYSKLLdyydkhftQPHVQ---DFvRAVckerirlMVSGSAALPvPLLEKWRSA 346
Cdd:PRK07445 193 --YKRLKSGQELPPNPsdfFLSlVPTQLQRLL--------QLRPQwlaQF-RTI-------LLGGAPAWP-SLLEQARQL 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 347 tGHTLLERYGMTEIGMALSNPLTEARVPG--SVGTPLPGVEVRIisENPQKGspyIIHaegnergtkvtpgfeekegell 424
Cdd:PRK07445 254 -QLRLAPTYGMTETASQIATLKPDDFLAGnnSSGQVLPHAQITI--PANQTG---NIT---------------------- 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 425 VRGPSVFREYWdkPEetksAFTSDGWFRTGDTAVF-KDARYWIRGRTSVDIIkTGGYKVSALEIERHLLAHPSITDVAVI 503
Cdd:PRK07445 306 IQAQSLALGYY--PQ----ILDSQGIFETDDLGYLdAQGYLHILGRNSQKII-TGGENVYPAEVEAAILATGLVQDVCVL 378
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720427507 504 GVPDMTWGQRVTAVVALQEGhSLSHGDLKEWARGVLAPYAVPSELLLVEEIPRNQMGKVNKKELLK 569
Cdd:PRK07445 379 GLPDPHWGEVVTAIYVPKDP-SISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQ 443
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
49-574 |
4.77e-28 |
|
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: 117.64 E-value: 4.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 49 RALAFGDRIALIDKYGHHTYRELYDRSLCLAQEICRL---QGCKVGdlqeerVSFlcsnDVS--YVVAQWASWMSGGVAV 123
Cdd:cd05918 8 RARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLgvgPGVFVP------LCF----EKSkwAVVAMLAVLKAGGAFV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 124 PLYWKHPEAQLEYFIQDSRSSLVVvgqeylerlsplaqrlgvpllpltpavyhgatekpTEQPveesgwrDRGAMIFYTS 203
Cdd:cd05918 78 PLDPSHPLQRLQEILQDTGAKVVL-----------------------------------TSSP-------SDAAYVIFTS 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 204 GTTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLplHHVHGV-VNKLLCPLWVGAT-CVM--------LPEFSAQ 273
Cdd:cd05918 116 GSTGKPKGVVIEHRALSTSALAHGRALGLTSESRVLQFA--SYTFDVsILEIFTTLAAGGClCIPseedrlndLAGFINR 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 274 QvwekflsseapQITVFMAVPTVySKLLDyydkhftqPhvQDFVRavckerIRLMVSGSAALPVPLLEKWrsATGHTLLE 353
Cdd:cd05918 194 L-----------RVTWAFLTPSV-ARLLD--------P--EDVPS------LRTLVLGGEALTQSDVDTW--ADRVRLIN 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 354 RYGMTE--IGMALSNPLTEARvPGSVGTPLPGVevriisenpqkgsPYIIHAEGNERgtKVTPGFEekeGELLVRGPSVF 431
Cdd:cd05918 244 AYGPAEctIAATVSPVVPSTD-PRNIGRPLGAT-------------CWVVDPDNHDR--LVPIGAV---GELLIEGPILA 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 432 REYWDKPEETKSAFTSD-GW------------FRTGD--------TAVF---KDARYWIRG-RtsVDIiktggykvsaLE 486
Cdd:cd05918 305 RGYLNDPEKTAAAFIEDpAWlkqegsgrgrrlYRTGDlvrynpdgSLEYvgrKDTQVKIRGqR--VEL----------GE 372
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 487 IERHLLAHPSITDVAVIGV---PDMTWGQRVTAVVALQEGHSLSHG-----------------DLKEWARGVLAPYAVPS 546
Cdd:cd05918 373 IEHHLRQSLPGAKEVVVEVvkpKDGSSSPQLVAFVVLDGSSSGSGDgdslflepsdefralvaELRSKLRQRLPSYMVPS 452
|
570 580
....*....|....*....|....*...
gi 1720427507 547 ELLLVEEIPRNQMGKVNKKeLLKQLYPS 574
Cdd:cd05918 453 VFLPLSHLPLTASGKIDRR-ALRELAES 479
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
55-567 |
4.87e-28 |
|
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: 117.58 E-value: 4.87e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 55 DRIALIDKYGHHTYRELYDRSLCLAQEIcRLQGCKvgdlQEERVSFLCSNDVSYVVAQWASWMSGGVAVPLYWKHPEAQL 134
Cdd:cd17656 3 DAVAVVFENQKLTYRELNERSNQLARFL-REKGVK----KDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 135 EYFIQDSRSSlVVVGQEYLErlSPLAQRlGVPLLPLTPAVYHGATEKpteqpVEESGWRDRGAMIFYTSGTTGRPKGALS 214
Cdd:cd17656 78 IYIMLDSGVR-VVLTQRHLK--SKLSFN-KSTILLEDPSISQEDTSN-----IDYINNSDDLLYIIYTSGTTGKPKGVQL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 215 THRNLAAVVT-GLVHSWAWTKNDVILHVLPLHHV--HGVVNKLLcplwVGATCVMLPEFSAQQVWE--KFLSSEAPQITV 289
Cdd:cd17656 149 EHKNMVNLLHfEREKTNINFSDKVLQFATCSFDVcyQEIFSTLL----SGGTLYIIREETKRDVEQlfDLVKRHNIEVVF 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 290 FmavPTVYSKLLdYYDKHFtqphVQDFVRAVcKERI----RLMVSGsaalpvPLLEKWRSATGHtLLERYGMTE---IGM 362
Cdd:cd17656 225 L---PVAFLKFI-FSEREF----INRFPTCV-KHIItageQLVITN------EFKEMLHEHNVH-LHNHYGPSEthvVTT 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 363 ALSNPLTEARVPGSVGTPLPGVEVRIISENPQ---KGSPyiihaegnergtkvtpgfeekeGELLVRGPSVFREYWDKPE 439
Cdd:cd17656 289 YTINPEAEIPELPPIGKPISNTWIYILDQEQQlqpQGIV----------------------GELYISGASVARGYLNRQE 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 440 ETKSAFTSDGW------FRTGDTAVF-KDARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSITDVAVIGVPDMTWGQ 512
Cdd:cd17656 347 LTAEKFFPDPFdpnermYRTGDLARYlPDGNIEFLGRAD-HQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEK 425
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1720427507 513 RVTA-VVALQEghsLSHGDLKEWARGVLAPYAVPSELLLVEEIPRNQMGKVNKKEL 567
Cdd:cd17656 426 YLCAyFVMEQE---LNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
145-455 |
6.66e-28 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 118.66 E-value: 6.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 145 LVVVGQEYlERLSPLAQRLGVPLLPLTPAVYHG-ATEKPTEQPVEESGwrdrgAMIFYTSGTTGRPKGALSTHRNLAAVV 223
Cdd:PLN02736 177 IVVVGGAD-EPLPSLPSGTGVEIVTYSKLLAQGrSSPQPFRPPKPEDV-----ATICYTSGTTGTPKGVVLTHGNLIANV 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 224 TGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCpLWVGATCvmlpEFSAQQVWEKFLSSEAPQITVFMAVPTVYSKLLD- 302
Cdd:PLN02736 251 AGSSLSTKFYPSDVHISYLPLAHIYERVNQIVM-LHYGVAV----GFYQGDNLKLMDDLAALRPTIFCSVPRLYNRIYDg 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 303 -------------------YYDK-----HFTQPH------VQDFVRAVCKERIRLMVSGSAALPVPLLEKWRSATGHTLL 352
Cdd:PLN02736 326 itnavkesgglkerlfnaaYNAKkqaleNGKNPSpmwdrlVFNKIKAKLGGRVRFMSSGASPLSPDVMEFLRICFGGRVL 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 353 ERYGMTEIGMALSNPLTEARVPGSVGTPLPGVEVRIIS----ENPQKGSPYiihaegnergtkvtpgfeeKEGELLVRGP 428
Cdd:PLN02736 406 EGYGMTETSCVISGMDEGDNLSGHVGSPNPACEVKLVDvpemNYTSEDQPY-------------------PRGEICVRGP 466
|
330 340
....*....|....*....|....*..
gi 1720427507 429 SVFREYWDKPEETKSAFTSDGWFRTGD 455
Cdd:PLN02736 467 IIFKGYYKDEVQTREVIDEDGWLHTGD 493
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
49-567 |
1.06e-27 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 119.29 E-value: 1.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 49 RALAFGDRIALIDKYGHHTYRELYDRSLCLAQeicRLQGCKVGdlQEERVSFLCSNDVSYVVAQWASWMSGGVAVPLYWK 128
Cdd:PRK12316 3066 QVERTPDAVALAFGEQRLSYAELNRRANRLAH---RLIERGVG--PDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPE 3140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 129 HPEAQLEYFIQDSRSsLVVVGQEYLErlspLAQRLGVPLLPLTPAVYHGATEKPTEQPVEESGwrdrgAMIFYTSGTTGR 208
Cdd:PRK12316 3141 YPEERLAYMLEDSGA-QLLLSQSHLR----LPLAQGVQVLDLDRGDENYAEANPAIRTMPENL-----AYVIYTSGSTGK 3210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 209 PKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLhHVHGVVNKLLCPLWVGATCVMlpefSAQQVWEKFLSSEAPQIT 288
Cdd:PRK12316 3211 PKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTF-SFDVFVEELFWPLMSGARVVL----AGPEDWRDPALLVELINS 3285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 289 VFMAVPTVYSKLLdyyDKHFTQPHVQDFVravckeRIRLMVSGSAALPVPLLEKWRSatGHTLLERYGMTE--IGMALSN 366
Cdd:PRK12316 3286 EGVDVLHAYPSML---QAFLEEEDAHRCT------SLKRIVCGGEALPADLQQQVFA--GLPLYNLYGPTEatITVTHWQ 3354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 367 PLTEARVPGSVGTPLPGVEVRIISENpqkgspyiihaegnergtkVTPGFEEKEGELLVRGPSVFREYWDKPEETKSAFT 446
Cdd:PRK12316 3355 CVEEGKDAVPIGRPIANRACYILDGS-------------------LEPVPVGALGELYLGGEGLARGYHNRPGLTAERFV 3415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 447 SDGW------FRTGDTAVFKDARYWIRGRTSVDIIKTGGYKVSALEIERHLLAHPSITDVAVIGVPdmtwGQRVTAVVAL 520
Cdd:PRK12316 3416 PDPFvpgerlYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAVD----GRQLVAYVVP 3491
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1720427507 521 QEGHSLSHGDLKEWARGVLAPYAVPSELLLVEEIPRNQMGKVNKKEL 567
Cdd:PRK12316 3492 EDEAGDLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKAL 3538
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
58-583 |
1.40e-26 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 115.53 E-value: 1.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 58 ALIDKYGHHTYRELYDRSLCLAQEIcRLQGCKVGDlqeeRVSFLCSNDVSYVVAQWASWMSGGVAVPLYWKHPEAQLEYF 137
Cdd:PRK10252 476 ALADARYQFSYREMREQVVALANLL-RERGVKPGD----SVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMM 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 138 IQDSRSSLVVVGQEYLERLSPLAqrLGVPLLPLTPAVYHGATEKPTEQPveesgwrDRGAMIFYTSGTTGRPKGALSTHR 217
Cdd:PRK10252 551 LEDARPSLLITTADQLPRFADVP--DLTSLCYNAPLAPQGAAPLQLSQP-------HHTAYIIFTSGSTGRPKGVMVGQT 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 218 nlaAVVTGLV---HSWAWTKNDVILHVLPL-HHVHgvVNKLLCPLWVGATCVML-PEFSAQQVW-EKFLSSEApqITVFM 291
Cdd:PRK10252 622 ---AIVNRLLwmqNHYPLTADDVVLQKTPCsFDVS--VWEFFWPFIAGAKLVMAePEAHRDPLAmQQFFAEYG--VTTTH 694
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 292 AVPTVYSKlldyydkhFTQPHVQDFVRAVCKERIRLMVSGSaALPVPLLEKWRSATGHTLLERYGMTEIGMALS----NP 367
Cdd:PRK10252 695 FVPSMLAA--------FVASLTPEGARQSCASLRQVFCSGE-ALPADLCREWQQLTGAPLHNLYGPTEAAVDVSwypaFG 765
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 368 LTEARVPGS---VGTPLPGVEVRIIsenpqkgspyiihaegNERGTKVTPGFeekEGELLVRGPSVFREYWDKPEETKSA 444
Cdd:PRK10252 766 EELAAVRGSsvpIGYPVWNTGLRIL----------------DARMRPVPPGV---AGDLYLTGIQLAQGYLGRPDLTASR 826
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 445 FTSDGW------FRTGDTAVFKD---ARYWirGRtSVDIIKTGGYKVSALEIERHLLAHPSITDVA----VIGVPDMTWG 511
Cdd:PRK10252 827 FIADPFapgermYRTGDVARWLDdgaVEYL--GR-SDDQLKIRGQRIELGEIDRAMQALPDVEQAVthacVINQAAATGG 903
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720427507 512 ---QRVTAVVAlQEGHSLSHGDLKEWARGVLAPYAVPSELLLVEEIPRNQMGKVNKKELLKqlyPSGQRSQPGQG 583
Cdd:PRK10252 904 darQLVGYLVS-QSGLPLDTSALQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKALPL---PELKAQVPGRA 974
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
67-562 |
2.63e-26 |
|
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: 113.35 E-value: 2.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 67 TYRELYDRSLCLAQEICRLqGCKVGDlqeeRVSFLCSNDVSYVVAQWASWMSGGVAVPLYWKHPEAQLEYFIQDSRSSLV 146
Cdd:cd05968 93 TYGELLYEVKRLANGLRAL-GVGKGD----RVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKAL 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 147 VVGQEYLER---LSPLA------------------QRLGVPLLPlTPAVYHGATEKPTEQPVE-ESGWRDRGAMIFYTSG 204
Cdd:cd05968 168 ITADGFTRRgreVNLKEeadkacaqcptvekvvvvRHLGNDFTP-AKGRDLSYDEEKETAGDGaERTESEDPLMIIYTSG 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 205 TTGRPKGALSTHRNL---AAVvtGLVHSWAWTKNDVILHVLPLHHVHGVVnKLLCPLWVGATCVM---LPEF-SAQQVWE 277
Cdd:cd05968 247 TTGKPKGTVHVHAGFplkAAQ--DMYFQFDLKPGDLLTWFTDLGWMMGPW-LIFGGLILGATMVLydgAPDHpKADRLWR 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 278 kflSSEAPQITVFMAVPTVYSKLldyydkhftQPHVQDFVRAvcKERIRLMVSGSAALPVPLlEKWRSATGHTLLERY-- 355
Cdd:cd05968 324 ---MVEDHEITHLGLSPTLIRAL---------KPRGDAPVNA--HDLSSLRVLGSTGEPWNP-EPWNWLFETVGKGRNpi 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 356 ----GMTEI-GMALSNPLTEARVPGSVGTPLPGVEVRIIsenpqkgspyiihaegNERGTKVTPgfeeKEGELLVRGP-- 428
Cdd:cd05968 389 inysGGTEIsGGILGNVLIKPIKPSSFNGPVPGMKADVL----------------DESGKPARP----EVGELVLLAPwp 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 429 SVFREYWDKPEETKSAFTS--DGWFRTGDTAVFKDARYW-IRGRtSVDIIKTGGYKVSALEIERHLLAHPSITDVAVIGV 505
Cdd:cd05968 449 GMTRGFWRDEDRYLETYWSrfDNVWVHGDFAYYDEEGYFyILGR-SDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGV 527
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 506 PDMTWGQRVTAVVALQEGHSLSHGDLKEWARGV---LAPYAVPSELLLVEEIPRNQMGKV 562
Cdd:cd05968 528 PHPVKGEAIVCFVVLKPGVTPTEALAEELMERVadeLGKPLSPERILFVKDLPKTRNAKV 587
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
67-570 |
1.10e-25 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 110.21 E-value: 1.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 67 TYRELYDRSLCLAQEICRLQGCKVGDLqeerVSFLCSNDVSYVVAQWASWMSGGVAVPLYWKHPEAQLEYFIQDSRSSLV 146
Cdd:cd05937 7 TYSETYDLVLRYAHWLHDDLGVQAGDF----VAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSRFV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 147 VVGQEYLerlsplaqrlgvpllpltpavyhgatekpteqpveesgwrdrgAMIFYTSGTTGRPKGALSTHRNLAAVVTGL 226
Cdd:cd05937 83 IVDPDDP-------------------------------------------AILIYTSGTTGLPKAAAISWRRTLVTSNLL 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 227 VHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSAQQVWEKFLSSEApqiTVFMAVPTVYSKLLDY--- 303
Cdd:cd05937 120 SHDLNLKNGDRTYTCMPLYHGTAAFLGACNCLMSGGTLALSRKFSASQFWKDVRDSGA---TIIQYVGELCRYLLSTpps 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 304 -YDKhftqphvqdfvravcKERIRlMVSGSAALPvPLLEKWRsatghtllERYGMTEIG---------MALSNPLTEARV 373
Cdd:cd05937 197 pYDR---------------DHKVR-VAWGNGLRP-DIWERFR--------ERFNVPEIGefyaategvFALTNHNVGDFG 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 374 PGSVGtpLPGVEVRIISEN--------PQKGSPYiihaEGNERGTKVTPGFEEkEGELLVRGP----SVFREYWDKPEET 441
Cdd:cd05937 252 AGAIG--HHGLIRRWKFENqvvlvkmdPETDDPI----RDPKTGFCVRAPVGE-PGEMLGRVPfknrEAFQGYLHNEDAT 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 442 KSAFTS------DGWFRTGDtAVFKDA--RYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSITDVAVIGV--PDMTwG 511
Cdd:cd05937 325 ESKLVRdvfrkgDIYFRTGD-LLRQDAdgRWYFLDRLG-DTFRWKSENVSTTEVADVLGAHPDIAEANVYGVkvPGHD-G 401
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720427507 512 QRVTAVVALQEGHS----LSHGDLKEWARGVLAPYAVPSELLLVEEIPRNQMGKVNKKELLKQ 570
Cdd:cd05937 402 RAGCAAITLEESSAvpteFTKSLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLRDE 464
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
49-580 |
1.20e-25 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 111.50 E-value: 1.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 49 RALAFGDRIALIDKYGHHTYRELYDRslclAQEICRL---QGCKVGDLqeerVSFLCSNDVSYVVAqWASWMSGGVAVPL 125
Cdd:PRK08279 46 AAARHPDRPALLFEDQSISYAELNAR----ANRYAHWaaaRGVGKGDV----VALLMENRPEYLAA-WLGLAKLGAVVAL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 126 YWKHPEAQ-LEYFIQDSRSSLVVVGQEYLERLSPLAQ--RLGVPLLPLTPAVYHG----------ATEKPTEQPVEESG- 191
Cdd:PRK08279 117 LNTQQRGAvLAHSLNLVDAKHLIVGEELVEAFEEARAdlARPPRLWVAGGDTLDDpegyedlaaaAAGAPTTNPASRSGv 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 192 -WRDRgAMIFYTSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEF 270
Cdd:PRK08279 197 tAKDT-AFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDVLYCCLPLYHNTGGTVAWSSVLAAGATLALRRKF 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 271 SAQQVWEKFlssEAPQITVFMAVPTVYSKLLDYYDKHFTQPHvqdfvravckeRIRLMVsgSAALPVPLLEKWRSATG-H 349
Cdd:PRK08279 276 SASRFWDDV---RRYRATAFQYIGELCRYLLNQPPKPTDRDH-----------RLRLMI--GNGLRPDIWDEFQQRFGiP 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 350 TLLERYGMTEIGMALSNPLTearVPGSVG-TPLPGVE-VRIISENPQKGSPyIIHAEGneRGTKVTPGfeekE-GELLV- 425
Cdd:PRK08279 340 RILEFYAASEGNVGFINVFN---FDGTVGrVPLWLAHpYAIVKYDVDTGEP-VRDADG--RCIKVKPG----EvGLLIGr 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 426 ---RGPsvFREYWDkPEETKS-----AFT-SDGWFRTGDTAVFKDARYWirgrTSVDII------KtgGYKVSALEIERH 490
Cdd:PRK08279 410 itdRGP--FDGYTD-PEASEKkilrdVFKkGDAWFNTGDLMRDDGFGHA----QFVDRLgdtfrwK--GENVATTEVENA 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 491 LLAHPSITDVAVIGV--PDMTwGQRVTAVVALQEGHSLshgDLKEWARGV---LAPYAVPSELLLVEEIPRNQMGKVNKK 565
Cdd:PRK08279 481 LSGFPGVEEAVVYGVevPGTD-GRAGMAAIVLADGAEF---DLAALAAHLyerLPAYAVPLFVRLVPELETTGTFKYRKV 556
|
570
....*....|....*
gi 1720427507 566 ELLKQLYPSGQRSQP 580
Cdd:PRK08279 557 DLRKEGFDPSKVDDP 571
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
50-567 |
6.34e-25 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 110.64 E-value: 6.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 50 ALAFGDRIAlidkyghhTYRELYDRSLCLAQeicRLQGCKVGdlQEERVSFLCSNDVSYVVAQWASWMSGGVAVPLYWKH 129
Cdd:PRK12467 3113 ALVFGDQQL--------SYAELNRRANRLAH---RLIAIGVG--PDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEY 3179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 130 PEAQLEYFIQDSRSSLVVVGQEYLERLSPLAQRLGVPLLPLTPAVYHGATEKPTEQPveesgwrDRGAMIFYTSGTTGRP 209
Cdd:PRK12467 3180 PRERLAYMIEDSGVKLLLTQAHLLEQLPAPAGDTALTLDRLDLNGYSENNPSTRVMG-------ENLAYVIYTSGSTGKP 3252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 210 KGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHhVHGVVNKLLCPLWVGATCVMLP--EFSAQQVWEKFLsseAPQI 287
Cdd:PRK12467 3253 KGVGVRHGALANHLCWIAEAYELDANDRVLLFMSFS-FDGAQERFLWTLICGGCLVVRDndLWDPEELWQAIH---AHRI 3328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 288 TVFMAVPTvysklldyydkhFTQPHVQDFVRAVCKeRIRLMVSGSAALPVPLLEKWRSATGHT-LLERYGMTEigmALSN 366
Cdd:PRK12467 3329 SIACFPPA------------YLQQFAEDAGGADCA-SLDIYVFGGEAVPPAAFEQVKRKLKPRgLTNGYGPTE---AVVT 3392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 367 PL----TEARVPGS----VGTPLPGVevriisenpqkgSPYIIHAEGNERGTKVTpgfeekeGELLVRGPSVFREYWDKP 438
Cdd:PRK12467 3393 VTlwkcGGDAVCEApyapIGRPVAGR------------SIYVLDGQLNPVPVGVA-------GELYIGGVGLARGYHQRP 3453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 439 EETKSAFTSDGW-------FRTGDTAVFK-DARYWIRGRtsVD-IIKTGGYKVSALEIERHLLAHPSITDVAVIGVPDMT 509
Cdd:PRK12467 3454 SLTAERFVADPFsgsggrlYRTGDLARYRaDGVIEYLGR--IDhQVKIRGFRIELGEIEARLLQHPSVREAVVLARDGAG 3531
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720427507 510 WGQRVTAVVALQEGhslshGDLKEWARGVLAP----YAVPSELLLVEEIPRNQMGKVNKKEL 567
Cdd:PRK12467 3532 GKQLVAYVVPADPQ-----GDWRETLRDHLAAslpdYMVPAQLLVLAAMPLGPNGKVDRKAL 3588
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
62-576 |
1.32e-24 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 107.57 E-value: 1.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 62 KYGHHTYRELYDRSLCLAQEIcRLQGCKVGDlqeeRVSFLCSNDVSYVVAQWASWMSGGVAVPlywkhpeaqleyfiqds 141
Cdd:cd05908 12 KEKFVSYRHLREEALGYLGAL-QELGIKPGQ----EVVFQITHNNKFLYLFWACLLGGMIAVP----------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 142 rsslVVVG--QEYLERLSPLAQRLGVPLLPltpavyhgATEKPTEQpveesgWRDRGAMIFYTSGTTGRPKGALSTHRNL 219
Cdd:cd05908 70 ----VSIGsnEEHKLKLNKVWNTLKNPYLI--------TEEEVLCE------LADELAFIQFSSGSTGDPKGVMLTHENL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 220 AAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLP--EFSAQQV-WEKFLSSEAPQITvfmAVPTV 296
Cdd:cd05908 132 VHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMPtrLFIRRPIlWLKKASEHKATIV---SSPNF 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 297 YSKlldYYDKHFTQPHVQDfvraVCKERIRLMVSGSAALPVPLLEKWRSATGHTLLER------YGMTEIGMALSNP--- 367
Cdd:cd05908 209 GYK---YFLKTLKPEKAND----WDLSSIRMILNGAEPIDYELCHEFLDHMSKYGLKRnailpvYGLAEASVGASLPkaq 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 368 -------------LTEARVPG------------SVGTPLPGVEVRIISE-NPQKGSPYIIHAEgnERGTKVTPGfeekeg 421
Cdd:cd05908 282 spfktitlgrrhvTHGEPEPEvdkkdsecltfvEVGKPIDETDIRICDEdNKILPDGYIGHIQ--IRGKNVTPG------ 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 422 ellvrgpsvfreYWDKPEETKSAFTSDGWFRTGDTAVFKDARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSIT--D 499
Cdd:cd05908 354 ------------YYNNPEATAKVFTDDGWLKTGDLGFIRNGRLVITGREK-DIIFVNGQNVYPHDIERIAEELEGVElgR 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 500 VAVIGVPDMTWGQRVTAVVALqegHSLSHGDLKEWARGV------LAPYAVpSELLLVEEIPRNQMGKVNKKElLKQLYP 573
Cdd:cd05908 421 VVACGVNNSNTRNEEIFCFIE---HRKSEDDFYPLGKKIkkhlnkRGGWQI-NEVLPIRRIPKTTSGKVKRYE-LAQRYQ 495
|
...
gi 1720427507 574 SGQ 576
Cdd:cd05908 496 SGE 498
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
199-569 |
1.43e-24 |
|
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: 108.17 E-value: 1.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 199 IFYTSGTTGRPKG----------ALS-THRNLAAVVTGlvHSWaWTKNDVILHVLPLHHVHGvvnkllcPLWVGATCVM- 266
Cdd:cd05967 235 ILYTSGTTGKPKGvvrdngghavALNwSMRNIYGIKPG--DVW-WAASDVGWVVGHSYIVYG-------PLLHGATTVLy 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 267 --LPEFS--AQQVW---EKFlsseapQITVFMAVPTVYSKLldyydkHFTQPHvQDFVRAVCKERIRLMVSGSAALPVPL 339
Cdd:cd05967 305 egKPVGTpdPGAFWrviEKY------QVNALFTAPTAIRAI------RKEDPD-GKYIKKYDLSSLRTLFLAGERLDPPT 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 340 LEKWRSATGHTLLERYGMTEIGMALS-NPLTEARVP---GSVGTPLPGVEVRIISENpqkgspyiihaegnerGTKVTPG 415
Cdd:cd05967 372 LEWAENTLGVPVIDHWWQTETGWPITaNPVGLEPLPikaGSPGKPVPGYQVQVLDED----------------GEPVGPN 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 416 feeKEGELLVRGP---SVFREYWDKPEETKSAF--TSDGWFRTGDTAVFKDARY-WIRGRTSvDIIKTGGYKVSALEIER 489
Cdd:cd05967 436 ---ELGNIVIKLPlppGCLLTLWKNDERFKKLYlsKFPGYYDTGDAGYKDEDGYlFIMGRTD-DVINVAGHRLSTGEMEE 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 490 HLLAHPSITDVAVIGVPDMTWGQRVTAVVALQEGHSLSHGDLKE----WARGVLAPYAVPSELLLVEEIPRNQMGKVNKK 565
Cdd:cd05967 512 SVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEGVKITAEELEKelvaLVREQIGPVAAFRLVIFVKRLPKTRSGKILRR 591
|
....
gi 1720427507 566 ELLK 569
Cdd:cd05967 592 TLRK 595
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
67-469 |
2.09e-24 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 107.75 E-value: 2.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 67 TYRELYDRSLCLAQEICRL---QGCKVGDLQEERVSFLCSndvsyvvaQWASWMSGGVAVPLYWKHPEAQLEYFIQDSRS 143
Cdd:PTZ00216 123 TYAELWERIVNFGRGLAELgltKGSNVAIYEETRWEWLAS--------IYGIWSQSMVAATVYANLGEDALAYALRETEC 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 144 SLVVVGQE--------------------YLERLSPLAQRLGVPLLPLTPAVYHGATEKPTEqPVEESGWRDRGAMIFYTS 203
Cdd:PTZ00216 195 KAIVCNGKnvpnllrlmksggmpnttiiYLDSLPASVDTEGCRLVAWTDVVAKGHSAGSHH-PLNIPENNDDLALIMYTS 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 204 GTTGRPKGALSTHRNLAAVVTGLVHSWawtkNDVI---------LHVLPLHHV--HGVVNKLL---CPLWVGAT------ 263
Cdd:PTZ00216 274 GTTGDPKGVMHTHGSLTAGILALEDRL----NDLIgppeedetyCSYLPLAHImeFGVTNIFLargALIGFGSPrtltdt 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 264 ----CVMLPEFSaqqvwekflsseaPqiTVFMAVPTVY--------SKL----------------------LDYYDKHFT 309
Cdd:PTZ00216 350 farpHGDLTEFR-------------P--VFLIGVPRIFdtikkaveAKLppvgslkrrvfdhayqsrlralKEGKDTPYW 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 310 QPHVQDFVRAVCKERIRLMVSGSAALPVPLLEKWRSATGhTLLERYGMTEI----GMALSNPLTearvPGSVGTPLPGVE 385
Cdd:PTZ00216 415 NEKVFSAPRAVLGGRVRAMLSGGGPLSAATQEFVNVVFG-MVIQGWGLTETvccgGIQRTGDLE----PNAVGQLLKGVE 489
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 386 VRIISENPQKgspyiiHAEgnergtkvTPgfeEKEGELLVRGPSVFREYWDKPEETKSAFTSDGWFRTGDTAVF-KDARY 464
Cdd:PTZ00216 490 MKLLDTEEYK------HTD--------TP---EPRGEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIaANGTL 552
|
....*
gi 1720427507 465 WIRGR 469
Cdd:PTZ00216 553 RIIGR 557
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
50-567 |
2.80e-24 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 108.72 E-value: 2.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 50 ALAFGDRIALIDKYGHHTYRELYDRSLCLAQeicRLQGCKVGdlQEERVSFLCSNDVSYVVAQWASWMSGGVAVPLYWKH 129
Cdd:PRK05691 1141 ARQTPERIALVWDGGSLDYAELHAQANRLAH---YLRDKGVG--PDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDY 1215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 130 PEAQLEYFIQDSRSSLVVVGQEYLERLSPLAQRLGVPLLPLTPAVYhgatekPTEQP-VEESGwrDRGAMIFYTSGTTGR 208
Cdd:PRK05691 1216 PAERLAYMLADSGVELLLTQSHLLERLPQAEGVSAIALDSLHLDSW------PSQAPgLHLHG--DNLAYVIYTSGSTGQ 1287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 209 PKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLhHVHGVVNKLLCPLWVGATCVML-------PEFSAQQVwekfls 281
Cdd:PRK05691 1288 PKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPI-SFDVSVWECFWPLITGCRLVLAgpgehrdPQRIAELV------ 1360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 282 sEAPQITVFmavptvysklldyydkHFTQPHVQDFVR----AVCKeRIRLMVSGSAALPVPLLEKWRSA-TGHTLLERYG 356
Cdd:PRK05691 1361 -QQYGVTTL----------------HFVPPLLQLFIDeplaAACT-SLRRLFSGGEALPAELRNRVLQRlPQVQLHNRYG 1422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 357 MTEIGMALSNPLTEA----RVPgsVGTPLPGVEVRIISenpqkgspyiihAEGNErgtkVTPGFeekEGELLVRGPSVFR 432
Cdd:PRK05691 1423 PTETAINVTHWQCQAedgeRSP--IGRPLGNVLCRVLD------------AELNL----LPPGV---AGELCIGGAGLAR 1481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 433 EYWDKPEETKSAFTSDGW-------FRTGDTAVFK-DARYWIRGRTSVDiIKTGGYKVSALEIERHLLAHPSITDVAVIg 504
Cdd:PRK05691 1482 GYLGRPALTAERFVPDPLgedgarlYRTGDRARWNaDGALEYLGRLDQQ-VKLRGFRVEPEEIQARLLAQPGVAQAAVL- 1559
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720427507 505 VPDMTWGQRVTAVVALQEGHSLSHGDLKEWARGVLAPYAVPSELLLVEEIPRNQMGKVNKKEL 567
Cdd:PRK05691 1560 VREGAAGAQLVGYYTGEAGQEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRAL 1622
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
67-455 |
3.30e-24 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 106.77 E-value: 3.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 67 TYRELYDRSLCLAQEICRLQGCKVGDlqeeRVSFLCSNDVSYVVAQWASWMSGGVAVPLYWKHPEAQLEYFIQDSRSSLV 146
Cdd:cd17632 69 TYAELWERVGAVAAAHDPEQPVRPGD----FVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 147 VVGQEYLerlsPLAQRL------------------------------------GVPLLPLTPAVYHGATEKPTEQPVEES 190
Cdd:cd17632 145 AVSAEHL----DLAVEAvleggtpprlvvfdhrpevdahraalesarerlaavGIPVTTLTLIAVRGRDLPPAPLFRPEP 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 191 GwRDRGAMIFYTSGTTGRPKGALSTHRNLAAvvtglvhswAWTKND----------VILHVLPLHHVHGvVNKLLCPLWV 260
Cdd:cd17632 221 D-DDPLALLIYTSGSTGTPKGAMYTERLVAT---------FWLKVSsiqdirppasITLNFMPMSHIAG-RISLYGTLAR 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 261 GATCVMLPEFSAQQVWEKFlsSEAPQITVFMaVPTVYSKLLDYY----DKHFTQPHVQDF----VRAVCKERI---RLM- 328
Cdd:cd17632 290 GGTAYFAAASDMSTLFDDL--ALVRPTELFL-VPRVCDMLFQRYqaelDRRSVAGADAETlaerVKAELRERVlggRLLa 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 329 -VSGSAALPVPLLEKWRSATGHTLLERYGMTEIGMALSNpltearvpGSVGTPlPGVEVRIIsENPQKG-----SPYiih 402
Cdd:cd17632 367 aVCGSAPLSAEMKAFMESLLDLDLHDGYGSTEAGAVILD--------GVIVRP-PVLDYKLV-DVPELGyfrtdRPH--- 433
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1720427507 403 aegnergtkvtpgfeeKEGELLVRGPSVFREYWDKPEETKSAFTSDGWFRTGD 455
Cdd:cd17632 434 ----------------PRGELLVKTDTLFPGYYKRPEVTAEVFDEDGFYRTGD 470
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
183-567 |
7.15e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 104.35 E-value: 7.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 183 TEQPVEESGWRD--RGAMIFYTSGTTGRPK----GALSTHRNLAAVVTglvhswAWTKNDVILHVL--PLHHVHGVVNKL 254
Cdd:PRK08308 88 SDFTKLEAVNYLaeEPSLLQYSSGTTGEPKlirrSWTEIDREIEAYNE------ALNCEQDETPIVacPVTHSYGLICGV 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 255 LCPLWVGATCVML----PEFSAQQVwekflsSEAPQITVFmAVPTVYSKLldyydKHFTQPHVQDFvravckeriRLMVS 330
Cdd:PRK08308 162 LAALTRGSKPVIItnknPKFALNIL------RNTPQHILY-AVPLMLHIL-----GRLLPGTFQFH---------AVMTS 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 331 GsAALPVPLLEKWRSATGHtLLERYGMTEIG-MALSNPLTEarvPGSVGTPLPGVEVRIiSENPQKGSPYIIHAEGNERG 409
Cdd:PRK08308 221 G-TPLPEAWFYKLRERTTY-MMQQYGCSEAGcVSICPDMKS---HLDLGNPLPHVSVSA-GSDENAPEEIVVKMGDKEIF 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 410 TKvTPGFEEKEGELlvrgpsVFREYWDkpeetksaftsdgwfrtgdtavfkdarywirgrtsvDIIKTGGYKVSALEIER 489
Cdd:PRK08308 295 TK-DLGYKSERGTL------HFMGRMD------------------------------------DVINVSGLNVYPIEVED 331
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720427507 490 HLLAHPSITDVAVIGVPDMTWGQRVTAVVALQegHSLSHGDLKEWARGVLAPYAVPSELLLVEEIPRNQMGKVNKKEL 567
Cdd:PRK08308 332 VMLRLPGVQEAVVYRGKDPVAGERVKAKVISH--EEIDPVQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLL 407
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
178-504 |
9.54e-24 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 105.51 E-value: 9.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 178 ATEKPTEQpVEESGWR---DRGAMIFYTSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVL---PLHHVHGVv 251
Cdd:PRK12582 202 AATPPTAA-VAAAIAAitpDTVAKYLFTSGSTGMPKAVINTQRMMCANIAMQEQLRPREPDPPPPVSLdwmPWNHTMGG- 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 252 NKLLCP-LWVGATCVM-----LPEFSAQQVweKFLSSEAPqiTVFMAVPTVYSKLLDYYDKhftqphvQDFVRAVCKERI 325
Cdd:PRK12582 280 NANFNGlLWGGGTLYIddgkpLPGMFEETI--RNLREISP--TVYGNVPAGYAMLAEAMEK-------DDALRRSFFKNL 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 326 RLMVSGSAALPVPLLEKWR----SATGH--TLLERYGMTEIGMALSNPLTEARVPGSVGTPLPGVEVRIISenpqKGSPY 399
Cdd:PRK12582 349 RLMAYGGATLSDDLYERMQalavRTTGHriPFYTGYGATETAPTTTGTHWDTERVGLIGLPLPGVELKLAP----VGDKY 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 400 iihaegnergtkvtpgfeekegELLVRGPSVFREYWDKPEETKSAFTSDGWFRTGDTAVFKDARYWIR-----GRTSVDI 474
Cdd:PRK12582 425 ----------------------EVRVKGPNVTPGYHKDPELTAAAFDEEGFYRLGDAARFVDPDDPEKglifdGRVAEDF 482
|
330 340 350
....*....|....*....|....*....|..
gi 1720427507 475 IKTGGYKVSALEIERHLLA--HPSITDVAVIG 504
Cdd:PRK12582 483 KLSTGTWVSVGTLRPDAVAacSPVIHDAVVAG 514
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
160-567 |
1.31e-23 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 103.80 E-value: 1.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 160 AQRLGVPLLP----LTPAVYHGATE--KPTEQPVEESGWRDRGAMIFYTSGTTGRPKGALSTHRNLAAvvtGLVHSWAWT 233
Cdd:cd05974 45 AMKLGAVVIPattlLTPDDLRDRVDrgGAVYAAVDENTHADDPMLLYFTSGTTSKPKLVEHTHRSYPV---GHLSTMYWI 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 234 ---KNDVILHVLPLHHVHGVVNKLLCPLWVGATCVML--PEFSAQQVWEKFlssEAPQITVFMAVPTVYSKLLDyydkhf 308
Cdd:cd05974 122 glkPGDVHWNISSPGWAKHAWSCFFAPWNAGATVFLFnyARFDAKRVLAAL---VRYGVTTLCAPPTVWRMLIQ------ 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 309 tqphvQDFVRAvcKERIRLMVSGSAALPVPLLEKWRSATGHTLLERYGMTEIGMALSNPLTEARVPGSVGTPLPGVEVRI 388
Cdd:cd05974 193 -----QDLASF--DVKLREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVGNSPGQPVKAGSMGRPLPGYRVAL 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 389 ISenpqkgspyiihAEGNErgtkvtpgfeEKEGELLV-----RGPSVFREYWDKPEETKSAFtSDGWFRTGDTAVF-KDA 462
Cdd:cd05974 266 LD------------PDGAP----------ATEGEVALdlgdtRPVGLMKGYAGDPDKTAHAM-RGGYYRTGDIAMRdEDG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 463 RYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSITDVAVIGVPDMTWGQRVTAVVALQEGHSLSHG---DLKEWARGVL 539
Cdd:cd05974 323 YLTYVGRAD-DVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGYEPSPEtalEIFRFSRERL 401
|
410 420
....*....|....*....|....*...
gi 1720427507 540 APYAVPSELLLVeEIPRNQMGKVNKKEL 567
Cdd:cd05974 402 APYKRIRRLEFA-ELPKTISGKIRRVEL 428
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
61-504 |
2.47e-23 |
|
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: 104.36 E-value: 2.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 61 DKYGHHTYRELYDRslclaqeiCRLQG---CKVGDLQEERVSFLCSNDVSYVVAQWASWMSGGVAVPLYWKH-PEAqLEY 136
Cdd:cd05933 4 DKWHTLTYKEYYEA--------CRQAAkafLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNsPEA-CQY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 137 FIQDSRSSLVVVG-----------QEYLERLSPLAQrLGVPLLPLTPAVY------HGATEKPTEQ--PVEESGWRDRGA 197
Cdd:cd05933 75 VAETSEANILVVEnqkqlqkilqiQDKLPHLKAIIQ-YKEPLKEKEPNLYswdefmELGRSIPDEQldAIISSQKPNQCC 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 198 MIFYTSGTTGRPKGALSTHRNL----AAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGAtCVMLPEFSAQ 273
Cdd:cd05933 154 TLIYTSGTTGMPKGVMLSHDNItwtaKAASQHMDLRPATVGQESVVSYLPLSHIAAQILDIWLPIKVGG-QVYFAQPDAL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 274 QvWEKFLSSEAPQITVFMAVPTVYSKLLDYYDKHFTQP-----HVQDFVRAV-CKERIRLMVSGSaalPVPL-------- 339
Cdd:cd05933 233 K-GTLVKTLREVRPTAFMGVPRVWEKIQEKMKAVGAKSgtlkrKIASWAKGVgLETNLKLMGGES---PSPLfyrlakkl 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 340 -LEKWRSATG----HTLL----------------------ERYGMTEIGMA--LSNPltEARVPGSVGTPLPGVEVRIIS 390
Cdd:cd05933 309 vFKKVRKALGldrcQKFFtgaapisretlefflslnipimELYGMSETSGPhtISNP--QAYRLLSCGKALPGCKTKIHN 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 391 ENpqkgspyiihAEGNergtkvtpgfeekeGELLVRGPSVFREYWDKPEETKSAFTSDGWFRTGDTAVFKDARY-WIRGR 469
Cdd:cd05933 387 PD----------ADGI--------------GEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFlYITGR 442
|
490 500 510
....*....|....*....|....*....|....*.
gi 1720427507 470 TSVDIIKTGGYKVSALEIERHLLAH-PSITDVAVIG 504
Cdd:cd05933 443 IKELIITAGGENVPPVPIEDAVKKElPIISNAMLIG 478
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
55-567 |
5.37e-23 |
|
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.
Pssm-ID: 341300 [Multi-domain] Cd Length: 440 Bit Score: 101.86 E-value: 5.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 55 DRIALIDKYGHHTYRELYDRSLCLAQeicRLQGCKVGdlQEERVSFLCSNDVSYVVAQWASWMSGGVAVPLYWKHPEAQL 134
Cdd:cd17645 13 DHVAVVDRGQSLTYKQLNEKANQLAR---HLRGKGVK--PDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGERI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 135 EYFIQDSRSSLVVVGQEYLerlsplaqrlgvpllpltpavyhgatekpteqpveesgwrdrgAMIFYTSGTTGRPKGALS 214
Cdd:cd17645 88 AYMLADSSAKILLTNPDDL-------------------------------------------AYVIYTSGSTGLPKGVMI 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 215 THRNLAAVVTGLVHSWAWTKNDVILhVLPLHHVHGVVNKLLCPLWVGATCVMLPEfsaqqvwEKFLSSEapqitvfmavp 294
Cdd:cd17645 125 EHHNLVNLCEWHRPYFGVTPADKSL-VYASFSFDASAWEIFPHLTAGAALHVVPS-------ERRLDLD----------- 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 295 tvysKLLDYYDKH-----FTQPHVQDFVRAVCKERIRLMVSGSAALPVpLLEKwrsatGHTLLERYGMTEIG-MALSNPL 368
Cdd:cd17645 186 ----ALNDYFNQEgitisFLPTGAAEQFMQLDNQSLRVLLTGGDKLKK-IERK-----GYKLVNNYGPTENTvVATSFEI 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 369 TEARVPGSVGTPLPGVEVRIISEnpqkgspyiihaegnerGTKVTPgfEEKEGELLVRGPSVFREYWDKPEETKSAFTSD 448
Cdd:cd17645 256 DKPYANIPIGKPIDNTRVYILDE-----------------ALQLQP--IGVAGELCIAGEGLARGYLNRPELTAEKFIVH 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 449 GW------FRTGDTAVF-KDARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSITDVAVIGVPDMTWGQRVTAVVALQ 521
Cdd:cd17645 317 PFvpgermYRTGDLAKFlPDGNIEFLGRLD-QQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTAP 395
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1720427507 522 EghSLSHGDLKEWARGVLAPYAVPSELLLVEEIPRNQMGKVNKKEL 567
Cdd:cd17645 396 E--EIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
197-463 |
1.97e-22 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 101.49 E-value: 1.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 197 AMIFYTSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKND--VILHVLPLHHVHGVVNKLLCPLWVGATCVM-----LPE 269
Cdd:PRK08180 212 AKFLFTSGSTGLPKAVINTHRMLCANQQMLAQTFPFLAEEppVLVDWLPWNHTFGGNHNLGIVLYNGGTLYIddgkpTPG 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 270 FSAQQVweKFLSSEAPqiTVFMAVPTVYSKLLDYYDKhftqphvQDFVRAVCKERIRLMVSGSAALPVPLLEKWRSATGH 349
Cdd:PRK08180 292 GFDETL--RNLREISP--TVYFNVPKGWEMLVPALER-------DAALRRRFFSRLKLLFYAGAALSQDVWDRLDRVAEA 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 350 TLLER------YGMTEIGMALSNPLTEARVPGSVGTPLPGVEVRIIsenpqkgsPYiihaegnerGTKVtpgfeekegEL 423
Cdd:PRK08180 361 TCGERirmmtgLGMTETAPSATFTTGPLSRAGNIGLPAPGCEVKLV--------PV---------GGKL---------EV 414
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1720427507 424 LVRGPSVFREYWDKPEETKSAFTSDGWFRTGDTAVFKDAR 463
Cdd:PRK08180 415 RVKGPNVTPGYWRAPELTAEAFDEEGYYRSGDAVRFVDPA 454
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
67-570 |
6.62e-22 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 98.58 E-value: 6.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 67 TYRELYDRSLCLAQEIcRLQGCKVGDLqeerVSFLCSNDVSYVVAQWASWMSGGVAvplywkhpeAQLEYFIqdsrsslv 146
Cdd:cd05940 5 TYAELDAMANRYARWL-KSLGLKPGDV----VALFMENRPEYVLLWLGLVKIGAVA---------ALINYNL-------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 147 vvgqeyleRLSPLAQRLGVP---LLPLTPAVYhgatekpteqpveesgwrdrgamiFYTSGTTGRPKGALSTHRNLAAVV 223
Cdd:cd05940 63 --------RGESLAHCLNVSsakHLVVDAALY------------------------IYTSGTTGLPKAAIISHRRAWRGG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 224 TGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSAQQVWEKFLsseAPQITVFMAVPTVYSKLLDy 303
Cdd:cd05940 111 AFFAGSGGALPSDVLYTCLPLYHSTALIVGWSACLASGATLVIRKKFSASNFWDDIR---KYQATIFQYIGELCRYLLN- 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 304 ydkhfTQPHVQDFvravcKERIRlMVSGSAALPvpllEKWRSATGH----TLLERYGMTEIGMALSNpltEARVPGSVG- 378
Cdd:cd05940 187 -----QPPKPTER-----KHKVR-MIFGNGLRP----DIWEEFKERfgvpRIAEFYAATEGNSGFIN---FFGKPGAIGr 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 379 ---TPLPGVEVRIISENPQKGSPyIIHAEGneRGTKVTPGfeeKEGELLVR--GPSVFREYWDKPEETKSAFTS-----D 448
Cdd:cd05940 249 npsLLRKVAPLALVKYDLESGEP-IRDAEG--RCIKVPRG---EPGLLISRinPLEPFDGYTDPAATEKKILRDvfkkgD 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 449 GWFRTGDTAVFKDARYW-IRGRTSvDIIKTGGYKVSALEIERHLLAHPSITDVAVIGV--PDmTWGQRVTAVVALQEGHS 525
Cdd:cd05940 323 AWFNTGDLMRLDGEGFWyFVDRLG-DTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVqvPG-TDGRAGMAAIVLQPNEE 400
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1720427507 526 LshgDLKEWARGV---LAPYAVPSELLLVEEIPRNQMGKVNKKELLKQ 570
Cdd:cd05940 401 F---DLSALAAHLeknLPGYARPLFLRLQPEMEITGTFKQQKVDLRNE 445
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
55-462 |
1.15e-21 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 99.04 E-value: 1.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 55 DRIALIDKYGHH-----TYRELYDRSLCLAQEICRLqgckvgDLQEER-VSFLCSNDVSYVVAQWASwMSGGVAV----P 124
Cdd:cd05921 10 DRTWLAEREGNGgwrrvTYAEALRQVRAIAQGLLDL------GLSAERpLLILSGNSIEHALMALAA-MYAGVPAapvsP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 125 LY--WKHPEAQLEYFIQdsrssLVVVGQEYLERLSPLAQRLGVPLLPLTPAVY---HGATEKPT------EQPVEESGWR 193
Cdd:cd05921 83 AYslMSQDLAKLKHLFE-----LLKPGLVFAQDAAPFARALAAIFPLGTPLVVsrnAVAGRGAIsfaelaATPPTAAVDA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 194 DRGAM-------IFYTSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKND--VILHVLPLHHVHGVVNKLLCPLWVGATC 264
Cdd:cd05921 158 AFAAVgpdtvakFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEppVLVDWLPWNHTFGGNHNFNLVLYNGGTL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 265 VM-----LPEFSAQQVweKFLSSEAPqiTVFMAVPTVYSKLLDYYDKhftqphvQDFVRAVCKERIRLMVSGSAALPVPL 339
Cdd:cd05921 238 YIddgkpMPGGFEETL--RNLREISP--TVYFNVPAGWEMLVAALEK-------DEALRRRFFKRLKLMFYAGAGLSQDV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 340 LEKWR----SATGH--TLLERYGMTEIGMALSNPLTEARVPGSVGTPLPGVEVRIISenpqKGSPYiihaEGNERGTKVT 413
Cdd:cd05921 307 WDRLQalavATVGEriPMMAGLGATETAPTATFTHWPTERSGLIGLPAPGTELKLVP----SGGKY----EVRVKGPNVT 378
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1720427507 414 PGfeekegellvrgpsvfreYWDKPEETKSAFTSDGWFRTGDTAVFKDA 462
Cdd:cd05921 379 PG------------------YWRQPELTAQAFDEEGFYCLGDAAKLADP 409
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
55-567 |
2.39e-21 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 97.09 E-value: 2.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 55 DRIALIDKYGHHTYRELYDRSLCLAQEICrlqgcKVGDLQ-EERVSFLCSNDVSYVVAQWASWMSGGVAVPLYWKHPEAQ 133
Cdd:cd17648 2 DRVAVVYGDKRLTYRELNERANRLAHYLL-----SVAEIRpDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDER 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 134 LEYFIQDSRSSLVVVGQEYLerlsplaqrlgvpllpltpavyhgatekpteqpveesgwrdrgAMIFYTSGTTGRPKGAL 213
Cdd:cd17648 77 IQFILEDTGARVVITNSTDL-------------------------------------------AYAIYTSGTTGKPKGVL 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 214 STHRNLAAVVTGLVHSWAWTKND--VIL----HVLPLHhvhgvVNKLLCPLWVGATCVMLPEfSAQQVWEKFLS-SEAPQ 286
Cdd:cd17648 114 VEHGSVVNLRTSLSERYFGRDNGdeAVLffsnYVFDFF-----VEQMTLALLNGQKLVVPPD-EMRFDPDRFYAyINREK 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 287 ITVFMAVPTVysklLDYYDkHFTQPHVQdfvravckeriRLMVSGSaALPVPLLEKWRSATGHTLLERYGMTEIGM-ALS 365
Cdd:cd17648 188 VTYLSGTPSV----LQQYD-LARLPHLK-----------RVDAAGE-EFTAPVFEKLRSRFAGLIINAYGPTETTVtNHK 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 366 NP-LTEARVPGSVGTPLPGVEVRIISENPQkgsPYIIHAegnergtkvtpgfeekEGELLVRGPSVFREYWDKPEETKSA 444
Cdd:cd17648 251 RFfPGDQRFDKSLGRPVRNTKCYVLNDAMK---RVPVGA----------------VGELYLGGDGVARGYLNRPELTAER 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 445 FTSDGW--------------FRTGDTAVFK-DARYWIRGRTSVDiIKTGGYKVSALEIERHLLAHPSITDVAVIGVPDMT 509
Cdd:cd17648 312 FLPNPFqteqerargrnarlYKTGDLVRWLpSGELEYLGRNDFQ-VKIRGQRIEPGEVEAALASYPGVRECAVVAKEDAS 390
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720427507 510 WGQ--RVTAVVA--LQEGHSLSHGDLKEWARGVLAPYAVPSELLLVEEIPRNQMGKVNKKEL 567
Cdd:cd17648 391 QAQsrIQKYLVGyyLPEPGHVPESDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKLDVRAL 452
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
67-455 |
2.99e-21 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 97.99 E-value: 2.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 67 TYRELYDRSLCLAQEIcRLQGCKVGDlqeeRVSFLCSNDVSYVVAQWASWMSGGVAVPLYWKHPEAQLEYFIQDSRSSLV 146
Cdd:PLN02861 79 TYKEVYDAAIRIGSAI-RSRGVNPGD----RCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSIA 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 147 VVgQEylerlSPLAQRLGVplLP-----LTPAVYHGATEKPTEQPVEESG-----WRDRGAM-----------------I 199
Cdd:PLN02861 154 FV-QE-----SKISSILSC--LPkcssnLKTIVSFGDVSSEQKEEAEELGvscfsWEEFSLMgsldcelppkqktdictI 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 200 FYTSGTTGRPKGALSTHRNLAAVVTGLVH-----SWAWTKNDVILHVLPLHHVHGVVNKLLCpLWVGATCvmlpefsaqQ 274
Cdd:PLN02861 226 MYTSGTTGEPKGVILTNRAIIAEVLSTDHllkvtDRVATEEDSYFSYLPLAHVYDQVIETYC-ISKGASI---------G 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 275 VWE---KFLSSEAPQI--TVFMAVPTVYSKL--------------------------LDYYDKHFTQ----PHVQDFVRA 319
Cdd:PLN02861 296 FWQgdiRYLMEDVQALkpTIFCGVPRVYDRIytgimqkissggmlrkklfdfaynykLGNLRKGLKQeeasPRLDRLVFD 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 320 VCKE----RIRLMVSGSAALPVPLLEKWRSATGHTLLERYGMTE-IGMALSNPLTEARVPGSVGTPLPGVEVRIISEnPQ 394
Cdd:PLN02861 376 KIKEglggRVRLLLSGAAPLPRHVEEFLRVTSCSVLSQGYGLTEsCGGCFTSIANVFSMVGTVGVPMTTIEARLESV-PE 454
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720427507 395 KGSPYIIHAegnergtkvtpgfeeKEGELLVRGPSVFREYWDKPEETKSAFtSDGWFRTGD 455
Cdd:PLN02861 455 MGYDALSDV---------------PRGEICLRGNTLFSGYHKRQDLTEEVL-IDGWFHTGD 499
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
199-561 |
6.60e-21 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 96.75 E-value: 6.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 199 IFYTSGTTGRPKG-----------ALSTHRNL------------AAV--VTGlvHSWAwtkndvilhvlplhhVHGvvnk 253
Cdd:PRK00174 250 ILYTSGSTGKPKGvlhttggylvyAAMTMKYVfdykdgdvywctADVgwVTG--HSYI---------------VYG---- 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 254 llcPLWVGATCVML---PEFSAQ----QVWEKFlsseapQITVFMAVPTVYSKLLDYYDkhftqphvqDFVRAVCKERIR 326
Cdd:PRK00174 309 ---PLANGATTLMFegvPNYPDPgrfwEVIDKH------KVTIFYTAPTAIRALMKEGD---------EHPKKYDLSSLR 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 327 LMvsGSAALPV-PllEKWR---SATGHtllER------YGMTEIGMALSNPLTEAR--VPGSVGTPLPGVEvriisenpq 394
Cdd:PRK00174 371 LL--GSVGEPInP--EAWEwyyKVVGG---ERcpivdtWWQTETGGIMITPLPGATplKPGSATRPLPGIQ--------- 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 395 kgsPYIIHAEGNErgtkvTPGfeEKEGELLVRG--PSVFREYWDKPEETKSAFTSD--GWFRTGDTAVF-KDARYWIRGR 469
Cdd:PRK00174 435 ---PAVVDEEGNP-----LEG--GEGGNLVIKDpwPGMMRTIYGDHERFVKTYFSTfkGMYFTGDGARRdEDGYYWITGR 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 470 TSvDIIKTGGYKVSALEIERHLLAHPSITDVAVIGVPDMTWGQRVTAVVALQEGHSLS---HGDLKEWARGVLAPYAVPS 546
Cdd:PRK00174 505 VD-DVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEEPSdelRKELRNWVRKEIGPIAKPD 583
|
410
....*....|....*
gi 1720427507 547 ELLLVEEIPRNQMGK 561
Cdd:PRK00174 584 VIQFAPGLPKTRSGK 598
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
49-567 |
9.31e-21 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 97.55 E-value: 9.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 49 RALAFGDRIALIDKYGHHTYRELYDRSLCLAQEIcRLQGckVGdlQEERVSFLCSNDVSYVVAQWASWMSGGVAVPLYWK 128
Cdd:PRK05691 2197 QAARTPQAPALTFAGQTLSYAELDARANRLARAL-RERG--VG--PQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPE 2271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 129 HPEAQLEYFIQDSRSSLVVVGQEYLERLSPLAQRLG-------VPLLPLTPAVYHGATEKPTEQpveesgwrdrgAMIFY 201
Cdd:PRK05691 2272 YPLERLHYMIEDSGIGLLLSDRALFEALGELPAGVArwcleddAAALAAYSDAPLPFLSLPQHQ-----------AYLIY 2340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 202 TSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLhHVHGVVNKLLCPLWVGATCVMlpefSAQQVW--EKF 279
Cdd:PRK05691 2341 TSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDCELHFYSI-NFDAASERLLVPLLCGARVVL----RAQGQWgaEEI 2415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 280 LS-SEAPQITVFMAVPTVYSKLLDYYDKHFTQPHVqdfvravckeriRLMVSGSAALPVPLLEKWRSATGHTLL-ERYGM 357
Cdd:PRK05691 2416 CQlIREQQVSILGFTPSYGSQLAQWLAGQGEQLPV------------RMCITGGEALTGEHLQRIRQAFAPQLFfNAYGP 2483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 358 TE-IGMALSNPLTEARVPGSVGTPLPgvevRIISENpqkgSPYIIHAEgnergtkVTPGFEEKEGELLVRGPSVFREYWD 436
Cdd:PRK05691 2484 TEtVVMPLACLAPEQLEEGAASVPIG----RVVGAR----VAYILDAD-------LALVPQGATGELYVGGAGLAQGYHD 2548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 437 KPEETKSAFTSDGW-------FRTGDTAVFKD---ARYWIRGRTSVdiiKTGGYKVSALEIERHLLAHPSITDVAVIGVP 506
Cdd:PRK05691 2549 RPGLTAERFVADPFaadggrlYRTGDLVRLRAdglVEYVGRIDHQV---KIRGFRIELGEIESRLLEHPAVREAVVLALD 2625
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720427507 507 DMTWGQRVTAVVALQEGHSLSHGD-----LKEWARGVLAPYAVPSELLLVEEIPRNQMGKVNKKEL 567
Cdd:PRK05691 2626 TPSGKQLAGYLVSAVAGQDDEAQAalreaLKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRAL 2691
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
50-569 |
5.56e-20 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 93.26 E-value: 5.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 50 ALAFGDRialidKYG--HHTYRELYDRSLCLAQEICRLqgckvGDLQEERVSFLCSNDVSYVVAQWASWMSGGVAVPLYW 127
Cdd:cd05915 12 EVVSRLH-----TGEvhRTTYAEVYQRARRLMGGLRAL-----GVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 128 KHPEAQLEYFIQDSRSSLVVVGQEYL----ERLSPLAQRLGVPLLPLTPAVYHG--ATEKPTEQPVEESGWRDRGAMIFy 201
Cdd:cd05915 82 RLSPKEIAYILNHAEDKVLLFDPNLLplveAIRGELKTVQHFVVMDEKAPEGYLayEEALGEEADPVRVPERAACGMAY- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 202 TSGTTGRPKGALSTHRN--LAAVVTGLVHSWAWTKNDVILHVLPLHHVHGvvnklLCPLWV----GATCVMLPEFSAQQV 275
Cdd:cd05915 161 TTGTTGLPKGVVYSHRAlvLHSLAASLVDGTALSEKDVVLPVVPMFHVNA-----WCLPYAatlvGAKQVLPGPRLDPAS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 276 WekFLSSEAPQITVFMAVPTVYSKLLDyydkhftqphVQDFVRAVCKERIRLMVSGSAalPVPLLEKWRSATGHTLLERY 355
Cdd:cd05915 236 L--VELFDGEGVTFTAGVPTVWLALAD----------YLESTGHRLKTLRRLVVGGSA--APRSLIARFERMGVEVRQGY 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 356 GMTEI---GMA-LSNPLTEArvpgsvgtpLPgvEVRIISENPQKGSPYIIHAEGNERGTKVTPGFEEKEGELL-VRGPSV 430
Cdd:cd05915 302 GLTETspvVVQnFVKSHLES---------LS--EEEKLTLKAKTGLPIPLVRLRVADEEGRPVPKDGKALGEVqLKGPWI 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 431 FREYWDKPEETKSAFTSDGWFRTGDTAVFKDARYWIRGRTSVDIIKTGGYKVSALEIERHLLAHPSITDVAVIGVPDMTW 510
Cdd:cd05915 371 TGGYYGNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKW 450
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720427507 511 GQRVTAVVALQEGHSLSHGDLKEWARGVLAPYAVPSELLLVEEIPRNQMGKVNKKELLK 569
Cdd:cd05915 451 QERPLAVVVPRGEKPTPEELNEHLLKAGFAKWQLPDAYVFAEEIPRTSAGKFLKRALRE 509
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
62-455 |
7.57e-20 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 93.55 E-value: 7.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 62 KYGHHTYRELYDRSLCLAQEicrLQGCKVGDlqEERVSFLCSNDVSYVVAQWASWMSGGVAVPLYWKHPEAQLEYFIQDS 141
Cdd:PLN02614 76 KYVWQTYQEVYDIVIKLGNS---LRSVGVKD--EAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHS 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 142 RSSLVVVGQEyleRLSPLAQRLGVPLLPLTPAVYHGATEKPTEQPVEESG-----WRDRGAM------------------ 198
Cdd:PLN02614 151 EVSIVFVEEK---KISELFKTCPNSTEYMKTVVSFGGVSREQKEEAETFGlviyaWDEFLKLgegkqydlpikkksdict 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 199 IFYTSGTTGRPKGALSTHRNLAAVVTGLVH-----SWAWTKNDVILHVLPLHHVHGVVNKLlCPLWVGAtcvmlpefsAQ 273
Cdd:PLN02614 228 IMYTSGTTGDPKGVMISNESIVTLIAGVIRllksaNAALTVKDVYLSYLPLAHIFDRVIEE-CFIQHGA---------AI 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 274 QVWE---KFLSSEAPQI--TVFMAVPTV----YS----KLLD-------YYDKHFT---------QPHVQ------DFVR 318
Cdd:PLN02614 298 GFWRgdvKLLIEDLGELkpTIFCAVPRVldrvYSglqkKLSDggflkkfVFDSAFSykfgnmkkgQSHVEasplcdKLVF 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 319 AVCKE----RIRLMVSGSAALPVPLLEKWRSATGHTLLERYGMTE--IGMALSNPlTEARVPGSVGTPLPGVEVRIISEn 392
Cdd:PLN02614 378 NKVKQglggNVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTEscAGTFVSLP-DELDMLGTVGPPVPNVDIRLESV- 455
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720427507 393 pqkgspyiihAEGNERGTKVTPgfeekEGELLVRGPSVFREYWDKPEETKSAFTsDGWFRTGD 455
Cdd:PLN02614 456 ----------PEMEYDALASTP-----RGEICIRGKTLFSGYYKREDLTKEVLI-DGWLHTGD 502
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
68-576 |
1.17e-19 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 92.76 E-value: 1.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 68 YRELYDRSLCLAQEICRLqGCKVGDlqeeRVSFLCSNDVSYVVAQWASWMSGGVAVPL-----------YwkhpEAQLEY 136
Cdd:PRK09192 52 YQTLRARAEAGARRLLAL-GLKPGD----RVALIAETDGDFVEAFFACQYAGLVPVPLplpmgfggresY----IAQLRG 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 137 FIQDSRSSLVVVGQEYLERLSPLAQRLGvPLLPLTPAVYH----GATEKPTEQPveesgwrDRGAMIFYTSGTTGRPKGA 212
Cdd:PRK09192 123 MLASAQPAAIITPDELLPWVNEATHGNP-LLHVLSHAWFKalpeADVALPRPTP-------DDIAYLQYSSGSTRFPRGV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 213 LSTHRNLAAVVTGLVH------------SWawtkndvilhvLPLHHVHGVVNKLLCPLwvgatcvmlpefsAQQVWEKFL 280
Cdd:PRK09192 195 IITHRALMANLRAISHdglkvrpgdrcvSW-----------LPFYHDMGLVGFLLTPV-------------ATQLSVDYL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 281 SSEApqitvFMAVPTVYSKLLDyyDKHFTQPHVQDFVRAVCKERIRlmVSGSAALPvplLEKWRSA----------TGHT 350
Cdd:PRK09192 251 PTRD-----FARRPLQWLDLIS--RNRGTISYSPPFGYELCARRVN--SKDLAELD---LSCWRVAgigadmirpdVLHQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 351 LLER--------------YGMTEIGMALS-NPLTE-----------------ARVPGS----------VGTPLPGVEVRI 388
Cdd:PRK09192 319 FAEAfapagfddkafmpsYGLAEATLAVSfSPLGSgivveevdrdrleyqgkAVAPGAetrrvrtfvnCGKALPGHEIEI 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 389 ISENPQkgspyiihaegnergtkVTPgfEEKEGELLVRGPSVFREYWDKpEETKSAFTSDGWFRTGDTAVFKDARYWIRG 468
Cdd:PRK09192 399 RNEAGM-----------------PLP--ERVVGHICVRGPSLMSGYFRD-EESQDVLAADGWLDTGDLGYLLDGYLYITG 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 469 RTSvDIIKTGGYKVSALEIERHLLAHPSIT--DVAVIGVPDMTwGQRVTAVVALQEGHSLSHGDLKEWARGVL-APYAVP 545
Cdd:PRK09192 459 RAK-DLIIINGRNIWPQDIEWIAEQEPELRsgDAAAFSIAQEN-GEKIVLLVQCRISDEERRGQLIHALAALVrSEFGVE 536
|
570 580 590
....*....|....*....|....*....|...
gi 1720427507 546 SELLLV--EEIPRNQMGKVNKKElLKQLYPSGQ 576
Cdd:PRK09192 537 AAVELVppHSLPRTSSGKLSRAK-AKKRYLSGA 568
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
197-563 |
1.17e-19 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 93.49 E-value: 1.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 197 AMIFYTSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPE-FSAQQV 275
Cdd:PRK06814 796 AVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPEDKVFNALPVFHSFGLTGGLVLPLLSGVKVFLYPSpLHYRII 875
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 276 WEKFLSSEApqiTVFMAVPTvyskLLDYYDKHftqPHVQDFvravckERIRLMVSGSAALPVPLLEKWRSATGHTLLERY 355
Cdd:PRK06814 876 PELIYDTNA---TILFGTDT----FLNGYARY---AHPYDF------RSLRYVFAGAEKVKEETRQTWMEKFGIRILEGY 939
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 356 GMTEIG--MALSNPLteARVPGSVGTPLPGVEVRIisenpqkgspyiihaegnergTKVtPGFEEKeGELLVRGPSVFRE 433
Cdd:PRK06814 940 GVTETApvIALNTPM--HNKAGTVGRLLPGIEYRL---------------------EPV-PGIDEG-GRLFVRGPNVMLG 994
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 434 YW--DKP---EETKsaftsDGWFRTGDTAVFKDARY-WIRGRTSvDIIKTGGYKVSALEIERHLLAHPSITDVAVIGVPD 507
Cdd:PRK06814 995 YLraENPgvlEPPA-----DGWYDTGDIVTIDEEGFiTIKGRAK-RFAKIAGEMISLAAVEELAAELWPDALHAAVSIPD 1068
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720427507 508 MTWGQRvtaVVALQEGHSLSHGDLKEWARGVLAP-YAVPSELLLVEEIPRNQMGKVN 563
Cdd:PRK06814 1069 ARKGER---IILLTTASDATRAAFLAHAKAAGASeLMVPAEIITIDEIPLLGTGKID 1122
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
199-569 |
2.79e-19 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 91.11 E-value: 2.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 199 IFYTSGTTGRPKGALSTHRNLAAVVtglvhSWAWTKNDVI-----------------------------LHVLPlhhvHG 249
Cdd:PRK04813 148 IIFTSGTTGKPKGVQISHDNLVSFT-----NWMLEDFALPegpqflnqapysfdlsvmdlyptlasggtLVALP----KD 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 250 VVN--KLL------CPL--WVgAT------CVMLPEFSAQQVwekflsseaPQITVFMavptvysklldyydkhftqphv 313
Cdd:PRK04813 219 MTAnfKQLfetlpqLPInvWV-STpsfadmCLLDPSFNEEHL---------PNLTHFL---------------------- 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 314 qdFvravCKErirlmvsgsaALPVpllekwrsATGHTLLER---------YGMTEIGMALSN-PLTEA------RVPgsV 377
Cdd:PRK04813 267 --F----CGE----------ELPH--------KTAKKLLERfpsatiyntYGPTEATVAVTSiEITDEmldqykRLP--I 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 378 GTPLPGVEVRIISENpqkgspyiihaegnerGTKVTPGfeeKEGELLVRGPSVFREYWDKPEETKSAF-TSDGW--FRTG 454
Cdd:PRK04813 321 GYAKPDSPLLIIDEE----------------GTKLPDG---EQGEIVISGPSVSKGYLNNPEKTAEAFfTFDGQpaYHTG 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 455 DTAVFKDARYWIRGRtsVDI-IKTGGYKVSALEIERHLLAHPSItDVAVIgVPDMTwGQRVT---AVVALQEGH-----S 525
Cdd:PRK04813 382 DAGYLEDGLLFYQGR--IDFqIKLNGYRIELEEIEQNLRQSSYV-ESAVV-VPYNK-DHKVQyliAYVVPKEEDferefE 456
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1720427507 526 LSHG---DLKEwargVLAPYAVPSELLLVEEIPRNQMGKVNKKELLK 569
Cdd:PRK04813 457 LTKAikkELKE----RLMEYMIPRKFIYRDSLPLTPNGKIDRKALIE 499
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
55-571 |
3.58e-19 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 90.82 E-value: 3.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 55 DRIALIDKYGHHTYRELYDRSLCLAQEICRlQGCKVGD---LQeervsflCSNDVSYVVAQWASWMSGGVAVPLYWKHPE 131
Cdd:PRK10946 38 DAIAVICGERQFSYRELNQASDNLACSLRR-QGIKPGDtalVQ-------LGNVAEFYITFFALLKLGVAPVNALFSHQR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 132 AQLEYFIQDSRSSLVVV--------GQEYLERLSPLAQRLGVPLL-------PLTPAVYHGATE-KPTEQPVEESGWrdr 195
Cdd:PRK10946 110 SELNAYASQIEPALLIAdrqhalfsDDDFLNTLVAEHSSLRVVLLlnddgehSLDDAINHPAEDfTATPSPADEVAF--- 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 196 gamiFYTSG-TTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHH--------VHGVvnkllcpLWVGATCVM 266
Cdd:PRK10946 187 ----FQLSGgSTGTPKLIPRTHNDYYYSVRRSVEICGFTPQTRYLCALPAAHnypmsspgALGV-------FLAGGTVVL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 267 LPEFSAQQVwekFLSSEAPQITVFMAVPTVYSKLLdyydKHFTQPHVQDFVRAvckerIRLMVSGSAALPVPLLEKWRSA 346
Cdd:PRK10946 256 APDPSATLC---FPLIEKHQVNVTALVPPAVSLWL----QAIAEGGSRAQLAS-----LKLLQVGGARLSETLARRIPAE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 347 TGHTLLERYGMTEiGM----ALSNPltEARVPGSVGTPL-PGVEVRIISEnpqkgspyiihaEGNErgtkVTPGfeeKEG 421
Cdd:PRK10946 324 LGCQLQQVFGMAE-GLvnytRLDDS--DERIFTTQGRPMsPDDEVWVADA------------DGNP----LPQG---EVG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 422 ELLVRGPSVFREYWDKPEETKSAFTSDGWFRTGDTaVFKDARYWIR--GRTSvDIIKTGGYKVSALEIERHLLAHPSITD 499
Cdd:PRK10946 382 RLMTRGPYTFRGYYKSPQHNASAFDANGFYCSGDL-VSIDPDGYITvvGREK-DQINRGGEKIAAEEIENLLLRHPAVIH 459
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720427507 500 VAVIGVPDMTWGQRVTAVVALQEghSLSHGDLKEWAR--GVlAPYAVPSELLLVEEIPRNQMGKVNKKELLKQL 571
Cdd:PRK10946 460 AALVSMEDELMGEKSCAFLVVKE--PLKAVQLRRFLReqGI-AEFKLPDRVECVDSLPLTAVGKVDKKQLRQWL 530
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
486-561 |
7.63e-19 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 81.05 E-value: 7.63e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720427507 486 EIERHLLAHPSITDVAVIGVPDMTWGQRVTAVVALQEGHSLSHGDLKEWARGVLAPYAVPSELLLVEEIPRNQMGK 561
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
194-542 |
9.77e-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: 341236 [Multi-domain] Cd Length: 457 Bit Score: 89.06 E-value: 9.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 194 DRGAMIFYTSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVnkllcplwVGATCV---MLPEF 270
Cdd:cd05910 85 DEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEVDLATFPLFALFGPA--------LGLTSVipdMDPTR 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 271 SAQQVWEKFLSS-EAPQITVFMAVPTVYSKLLDYYDKH-FTQPHVqdfvravckeriRLMVSGSAALPVPLLEKWRSATG 348
Cdd:cd05910 157 PARADPQKLVGAiRQYGVSIVFGSPALLERVARYCAQHgITLPSL------------RRVLSAGAPVPIALAARLRKMLS 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 349 HT--LLERYGMTE---IGMALSNPLTEARVPGS-------VGTPLPGVEVRIISENPQKgspyiIHAEGNERgtKVTPGf 416
Cdd:cd05910 225 DEaeILTPYGATEalpVSSIGSRELLATTTAATsggagtcVGRPIPGVRVRIIEIDDEP-----IAEWDDTL--ELPRG- 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 417 eeKEGELLVRGPSVFREYWDKPEETKSAFTSDG----WFRTGDTAVFKDA-RYWIRGRTSVDIIKTGGyKVSALEIERHL 491
Cdd:cd05910 297 --EIGEITVTGPTVTPTYVNRPVATALAKIDDNsegfWHRMGDLGYLDDEgRLWFCGRKAHRVITTGG-TLYTEPVERVF 373
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1720427507 492 LAHPSITDVAVIGVpDMTWGQRVTAVVALQEGHSLSHGDLKEWARGVLAPY 542
Cdd:cd05910 374 NTHPGVRRSALVGV-GKPGCQLPVLCVEPLPGTITPRARLEQELRALAKDY 423
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
182-569 |
1.22e-18 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 89.57 E-value: 1.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 182 PTEQPVEesgWRDRGAMIF--YTSGTTGRPKGALSTHRN-LAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCPL 258
Cdd:PLN02654 264 PTKCEVE---WVDAEDPLFllYTSGSTGKPKGVLHTTGGyMVYTATTFKYAFDYKPTDVYWCTADCGWITGHSYVTYGPM 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 259 WVGATCVML---PEF-SAQQVWE---KFlsseapQITVFMAVPTVYSKLLDYYDKHFTQphvqdfvravcKERIRLMVSG 331
Cdd:PLN02654 341 LNGATVLVFegaPNYpDSGRCWDivdKY------KVTIFYTAPTLVRSLMRDGDEYVTR-----------HSRKSLRVLG 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 332 SAALPV-PLLEKW-RSATGHT---LLERYGMTEIGMALSNPLTEA--RVPGSVGTPLPGVEVRIISENPQKgspyiihAE 404
Cdd:PLN02654 404 SVGEPInPSAWRWfFNVVGDSrcpISDTWWQTETGGFMITPLPGAwpQKPGSATFPFFGVQPVIVDEKGKE-------IE 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 405 GnergtkvtpgfeEKEGELLVRG--PSVFRE-YWDKPEETKSAFTS-DGWFRTGD-TAVFKDARYWIRGRTSvDIIKTGG 479
Cdd:PLN02654 477 G------------ECSGYLCVKKswPGAFRTlYGDHERYETTYFKPfAGYYFSGDgCSRDKDGYYWLTGRVD-DVINVSG 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 480 YKVSALEIERHLLAHPSITDVAVIGVPDMTWGQRVTAVVALQEGHSLSHgDLKE----WARGVLAPYAVPSELLLVEEIP 555
Cdd:PLN02654 544 HRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQGIYAFVTLVEGVPYSE-ELRKslilTVRNQIGAFAAPDKIHWAPGLP 622
|
410
....*....|....
gi 1720427507 556 RNQMGKVNKKELLK 569
Cdd:PLN02654 623 KTRSGKIMRRILRK 636
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
49-489 |
1.35e-18 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 90.61 E-value: 1.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 49 RALAFGDRIAL---IDKYGHH---TYRELYDRSLCLAQEICRLQGckVGDlqeeRVSFLCSNDVSYVVAQWASWMSGGVA 122
Cdd:PRK05691 18 RAAQTPDRLALrflADDPGEGvvlSYRDLDLRARTIAAALQARAS--FGD----RAVLLFPSGPDYVAAFFGCLYAGVIA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 123 VPLY-----WKHPEAQLEYFIQDSRSSLVVVGQEYLERLSPLAQRLGVPLLPLTpAVyhgatekPTEQPVEESGWR---- 193
Cdd:PRK05691 92 VPAYppesaRRHHQERLLSIIADAEPRLLLTVADLRDSLLQMEELAAANAPELL-CV-------DTLDPALAEAWQepal 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 194 --DRGAMIFYTSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKN--DVILHVLPLHHVHGVVNKLLCPLWVGATCVMLpe 269
Cdd:PRK05691 164 qpDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGIDLNpdDVIVSWLPLYHDMGLIGGLLQPIFSGVPCVLM-- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 270 fsaqqvwekflsseAPQitVFMAVPTVYSKLLDYYDKhfTQPHVQDFVRAVCKERIrlmvsGSAALPVPLLEKWRSA--- 346
Cdd:PRK05691 242 --------------SPA--YFLERPLRWLEAISEYGG--TISGGPDFAYRLCSERV-----SESALERLDLSRWRVAysg 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 347 ---------------------TGHTLLERYGMTEIGMALSN-------PLTE------AR---VPG------SVGTPLPG 383
Cdd:PRK05691 299 sepirqdslerfaekfaacgfDPDSFFASYGLAEATLFVSGgrrgqgiPALEldaealARnraEPGtgsvlmSCGRSQPG 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 384 VEVRIISENPQKGSPyiihaegnergtkvtpgfEEKEGELLVRGPSVFREYWDKPEETKSAFTS-DG--WFRTGDTAVFK 460
Cdd:PRK05691 379 HAVLIVDPQSLEVLG------------------DNRVGEIWASGPSIAHGYWRNPEASAKTFVEhDGrtWLRTGDLGFLR 440
|
490 500
....*....|....*....|....*....
gi 1720427507 461 DARYWIRGRTSvDIIKTGGYKVSALEIER 489
Cdd:PRK05691 441 DGELFVTGRLK-DMLIVRGHNLYPQDIEK 468
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
49-489 |
2.13e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 88.51 E-value: 2.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 49 RALAFGDRIALIdkygHHTYRELYDRSLCLAQeicRLQGCKVGdlQEERVSFLCSNDVSYVVAQWASWMSGGVAVPLYWK 128
Cdd:PRK07768 17 RGMVTGEPDAPV----RHTWGEVHERARRIAG---GLAAAGVG--PGDAVAVLAGAPVEIAPTAQGLWMRGASLTMLHQP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 129 HPEAQLEYFIQDSR-------SSLVVVGQEYLErLSPLAQRLGVPLLPLTPAVyhgATEKPTEQPVEEsgwrDRGAMIFY 201
Cdd:PRK07768 88 TPRTDLAVWAEDTLrvigmigAKAVVVGEPFLA-AAPVLEEKGIRVLTVADLL---AADPIDPVETGE----DDLALMQL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 202 TSGTTGRPKGALSTHRNLAAVVTGLVHSWAWT-KNDVILHVLPLHHVHGVVNKLLCPLWVGATCVmlpefsaqqvwekfl 280
Cdd:PRK07768 160 TSGSTGSPKAVQITHGNLYANAEAMFVAAEFDvETDVMVSWLPLFHDMGMVGFLTVPMYFGAELV--------------- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 281 sseapQITV--FMAVPTVYSKLLDYYDKHFTQ-PhvqDFVRAVCKER--------------IRLMVSGSAALPVPLLEKW 343
Cdd:PRK07768 225 -----KVTPmdFLRDPLLWAELISKYRGTMTAaP---NFAYALLARRlrrqakpgafdlssLRFALNGAEPIDPADVEDL 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 344 RSATG------HTLLERYGMTEIGMALSNP--------------LTEAR---VPG---------SVGTPLPGVEVRIISE 391
Cdd:PRK07768 297 LDAGArfglrpEAILPAYGMAEATLAVSFSpcgaglvvdevdadLLAALrraVPAtkgntrrlaTLGPPLPGLEVRVVDE 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 392 NPQkgspyiihaegnergtkVTPgfEEKEGELLVRGPSVFREYwDKPEETKSAFTSDGWFRTGDTAVFKDA-RYWIRGRT 470
Cdd:PRK07768 377 DGQ-----------------VLP--PRGVGVIELRGESVTPGY-LTMDGFIPAQDADGWLDTGDLGYLTEEgEVVVCGRV 436
|
490
....*....|....*....
gi 1720427507 471 SvDIIKTGGYKVSALEIER 489
Cdd:PRK07768 437 K-DVIIMAGRNIYPTDIER 454
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
194-555 |
3.40e-18 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 88.61 E-value: 3.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 194 DRGAMIFYTSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLP----- 268
Cdd:PRK08043 365 EDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPsplhy 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 269 EFSAQQVWEKflsseapQITVFMAVPTvyskLLDYYDKhFTQPHvqDFVRavckerIRLMVSGSAALPVPLLEKWRSATG 348
Cdd:PRK08043 445 RIVPELVYDR-------NCTVLFGTST----FLGNYAR-FANPY--DFAR------LRYVVAGAEKLQESTKQLWQDKFG 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 349 HTLLERYGMTEIGMALSNPLTEARVPGSVGTPLPGVEVRIISenpqkgspyiihaegnergtkvTPGFEEKeGELLVRGP 428
Cdd:PRK08043 505 LRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLS----------------------VPGIEQG-GRLQLKGP 561
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 429 SVFREYW--DKPE--ETKSAFTSDG-----WFRTGDTAVFKDARY-WIRGRTSvDIIKTGGYKVSaLEIERHL--LAHPS 496
Cdd:PRK08043 562 NIMNGYLrvEKPGvlEVPTAENARGemergWYDTGDIVRFDEQGFvQIQGRAK-RFAKIAGEMVS-LEMVEQLalGVSPD 639
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 497 ITDVAVIgVPDMTWGQrvtAVVALQEGHSLSHGDLKEWARGVLAP-YAVPSELLLVEEIP 555
Cdd:PRK08043 640 KQHATAI-KSDASKGE---ALVLFTTDSELTREKLQQYAREHGVPeLAVPRDIRYLKQLP 695
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
63-579 |
3.61e-18 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 88.33 E-value: 3.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 63 YGHHTYRELYDRSLCLAQEIcRLQGCKVGdlqeERVSFLCSNDVSYVVAQWASWMSGGVAVPLY-----------WKHPE 131
Cdd:PLN02430 74 YMWKTYKEVYEEVLQIGSAL-RASGAEPG----SRVGIYGSNCPQWIVAMEACAAHSLICVPLYdtlgpgavdyiVDHAE 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 132 AQLeYFIQD--------------SRSSLVVVGQEYLERLSPLAQRLGVPLLPLTPAVYHGaTEKPTE----QPVEEsgwr 193
Cdd:PLN02430 149 IDF-VFVQDkkikellepdcksaKRLKAIVSFTSVTEEESDKASQIGVKTYSWIDFLHMG-KENPSEtnppKPLDI---- 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 194 drgAMIFYTSGTTGRPKGALSTHRNLAAVVTGL-----VHSWAWTKNDVILHVLPLHHV-------------------HG 249
Cdd:PLN02430 223 ---CTIMYTSGTSGDPKGVVLTHEAVATFVRGVdlfmeQFEDKMTHDDVYLSFLPLAHIldrmieeyffrkgasvgyyHG 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 250 VVNKL------LCP-LWVGATCVMlpefsaQQVWE---KFLSSEAP-QITVFMAVptvYSKLLDYYDKHFTQPHVQDF-- 316
Cdd:PLN02430 300 DLNALrddlmeLKPtLLAGVPRVF------ERIHEgiqKALQELNPrRRLIFNAL---YKYKLAWMNRGYSHKKASPMad 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 317 ------VRAVCKERIRLMVSGSAALPVPLLEKWRSATGHTLLERYGMTEI--GMALSNPlTEARVPGSVGTPLPGVEVRi 388
Cdd:PLN02430 371 flafrkVKAKLGGRLRLLISGGAPLSTEIEEFLRVTSCAFVVQGYGLTETlgPTTLGFP-DEMCMLGTVGAPAVYNELR- 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 389 ISENPQKGspyiihaegnergtkVTPGFEEKEGELLVRGPSVFREYWDKPEETKSAFtSDGWFRTGDTA-VFKDARYWIR 467
Cdd:PLN02430 449 LEEVPEMG---------------YDPLGEPPRGEICVRGKCLFSGYYKNPELTEEVM-KDGWFHTGDIGeILPNGVLKII 512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 468 GRTSvDIIKTGGYKVSALE-IERHLLAHPSITDVAVIGvpdMTWGQRVTAVVALQEghslshGDLKEWAR--GVLAPYav 544
Cdd:PLN02430 513 DRKK-NLIKLSQGEYVALEyLENVYGQNPIVEDIWVYG---DSFKSMLVAVVVPNE------ENTNKWAKdnGFTGSF-- 580
|
570 580 590
....*....|....*....|....*....|....*
gi 1720427507 545 pSELLLVEEIprnqmgkvnKKELLKQLYPSGQRSQ 579
Cdd:PLN02430 581 -EELCSLPEL---------KEHILSELKSTAEKNK 605
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
67-545 |
4.68e-18 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 87.35 E-value: 4.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 67 TYRELYDRSLCLAQEICRLQGCKVGDLqeerVSFLCSNDVSYVVAqWASWMSGGVAVPLYWKHPEAQ-LEYFIQDSRSSL 145
Cdd:cd05938 7 TYRDVDRRSNQAARALLAHAGLRPGDT----VALLLGNEPAFLWI-WLGLAKLGCPVAFLNTNIRSKsLLHCFRCCGAKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 146 VVVG---QEYLERLSPLAQRLGVPLLPLTPAVYH-----------GATEKPT-EQPVEESGWRDRgAMIFYTSGTTGRPK 210
Cdd:cd05938 82 LVVApelQEAVEEVLPALRADGVSVWYLSHTSNTegvislldkvdAASDEPVpASLRAHVTIKSP-ALYIYTSGTTGLPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 211 GALSTHRNLAAVvTGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSAQQVWEKFLSSEapqITVF 290
Cdd:cd05938 161 AARISHLRVLQC-SGFLSLCGVTADDVIYITLPLYHSSGFLLGIGGCIELGATCVLKPKFSASQFWDDCRKHN---VTVI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 291 MAVptvySKLLDYYDKHFTQPHVQDfvravckERIRLMVsGSAALPvpllEKWRSAT---GHT-LLERYGMTEIGMALSN 366
Cdd:cd05938 237 QYI----GELLRYLCNQPQSPNDRD-------HKVRLAI-GNGLRA----DVWREFLrrfGPIrIREFYGSTEGNIGFFN 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 367 pltEARVPGSVG---------TPLpgvevRIISENPQKGSPyIIHAEGneRGTKVTPGfeekEGELLV---RGPSVFREY 434
Cdd:cd05938 301 ---YTGKIGAVGrvsylykllFPF-----ELIKFDVEKEEP-VRDAQG--FCIPVAKG----EPGLLVakiTQQSPFLGY 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 435 WDKPEETKSAF------TSDGWFRTGDTAV--------FKDarywirgRTSvDIIKTGGYKVSALEIERHLLAHPSITDV 500
Cdd:cd05938 366 AGDKEQTEKKLlrdvfkKGDVYFNTGDLLVqdqqnflyFHD-------RVG-DTFRWKGENVATTEVADVLGLLDFLQEV 437
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1720427507 501 AVIGVPDMTWGQRV-TAVVALQEGHSLSHGDLKEWARGVLAPYAVP 545
Cdd:cd05938 438 NVYGVTVPGHEGRIgMAAVKLKPGHEFDGKKLYQHVREYLPAYARP 483
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
187-549 |
1.21e-17 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 85.69 E-value: 1.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 187 VEESGWR-DRGAMIFYTSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGvvnklLCPLW----VG 261
Cdd:PRK09029 127 AHAVAWQpQRLATMTLTSGSTGLPKAAVHTAQAHLASAEGVLSLMPFTAQDSWLLSLPLFHVSG-----QGIVWrwlyAG 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 262 ATCVmLPEFsaqqvwEKFLSSEApQITVFMAVPTVYSKLLDYYDKHFTQPHVqdfvravckerirLMvsGSAALPVPL-- 339
Cdd:PRK09029 202 ATLV-VRDK------QPLEQALA-GCTHASLVPTQLWRLLDNRSEPLSLKAV-------------LL--GGAAIPVELte 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 340 -LEKW--RSATGhtllerYGMTEigMAlsNPLTEARVPGS--VGTPLPGVEVRIIsenpqkgspyiihaegnergtkvtp 414
Cdd:PRK09029 259 qAEQQgiRCWCG------YGLTE--MA--STVCAKRADGLagVGSPLPGREVKLV------------------------- 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 415 gfeekEGELLVRGPSVFREYWdKPEETKSAFTSDGWFRTGDTAVFKDARYWIRGRTSVDIIkTGGYKVSALEIERHLLAH 494
Cdd:PRK09029 304 -----DGEIWLRGASLALGYW-RQGQLVPLVNDEGWFATRDRGEWQNGELTILGRLDNLFF-SGGEGIQPEEIERVINQH 376
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720427507 495 PSITDVAVIGVPDMTWGQRVTAVVALQEGHSLShgDLKEWARGVLA----P---YAVPSELL 549
Cdd:PRK09029 377 PLVQQVFVVPVADAEFGQRPVAVVESDSEAAVV--NLAEWLQDKLArfqqPvayYLLPPELK 436
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
115-579 |
6.64e-16 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 81.75 E-value: 6.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 115 SWMSGGVAVPLYWKHPEAQLEYFIQDSRSSLVVVGQEYLERLSPLAQRLGV---PLLPLTPAVYHGATekPTEQPVEESG 191
Cdd:PRK05691 3790 SFKAGAGYLPLDPGLPAQRLQRIIELSRTPVLVCSAACREQARALLDELGCanrPRLLVWEEVQAGEV--ASHNPGIYSG 3867
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 192 wRDRGAMIFYTSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWvGATCVMLPEFS 271
Cdd:PRK05691 3868 -PDNLAYVIYTSGSTGLPKGVMVEQRGMLNNQLSKVPYLALSEADVIAQTASQSFDISVWQFLAAPLF-GARVEIVPNAI 3945
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 272 AQQVWEKFLSSEAPQITVFMAVPTVYSKLLdyydkhfTQPHVQdfvravcKERIRLMVSGSAALPVPLLEKWrsatghtl 351
Cdd:PRK05691 3946 AHDPQGLLAHVQAQGITVLESVPSLIQGML-------AEDRQA-------LDGLRWMLPTGEAMPPELARQW-------- 4003
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 352 LERYgmTEIGmaLSNPLTEARVPGSV-----------GTPLPgvevriisenpqKGSP------YIIhaegNERGTKVTP 414
Cdd:PRK05691 4004 LQRY--PQIG--LVNAYGPAECSDDVaffrvdlastrGSYLP------------IGSPtdnnrlYLL----DEALELVPL 4063
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 415 GfeeKEGELLVRGPSVFREYWDKPEETKSAFTSDGW-------FRTGDTA-VFKDARYWIRGRtsVD-IIKTGGYKVSAL 485
Cdd:PRK05691 4064 G---AVGELCVAGTGVGRGYVGDPLRTALAFVPHPFgapgerlYRTGDLArRRSDGVLEYVGR--IDhQVKIRGYRIELG 4138
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 486 EIERHLLAHPSITDVAViGVPDMTWGQRVTAVVALQEGhSLSHGDL----KEWARGVLAPYAVPSELLLVEEIPRNQMGK 561
Cdd:PRK05691 4139 EIEARLHEQAEVREAAV-AVQEGVNGKHLVGYLVPHQT-VLAQGALleriKQRLRAELPDYMVPLHWLWLDRLPLNANGK 4216
|
490
....*....|....*...
gi 1720427507 562 VNKKElLKQLYPSGQRSQ 579
Cdd:PRK05691 4217 LDRKA-LPALDIGQLQSQ 4233
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
84-469 |
1.59e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 79.77 E-value: 1.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 84 RLQGC-KVGDlqeeRVSFLCSNDVSYVVAQWASWMSGGVAVPLYwkHPEA-----QLEYFIQDSRSSLVVVGQEYLE--- 154
Cdd:PRK07769 71 RLQQVtKPGD----RVAILAPQNLDYLIAFFGALYAGRIAVPLF--DPAEpghvgRLHAVLDDCTPSAILTTTDSAEgvr 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 155 ---RLSPLAQRLGVPLLPLTP-AVyhGATEKPTEQPveesgwRDRGAMIFYTSGTTGRPKGALSTHRNLAAVVTGLVHSW 230
Cdd:PRK07769 145 kffRARPAKERPRVIAVDAVPdEV--GATWVPPEAN------EDTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDAL 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 231 AWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSAQQV--WEKFLSSEAPQIT-VFMAVPtvysklldyydkH 307
Cdd:PRK07769 217 EGQEGDRGVSWLPFFHDMGLITVLLPALLGHYITFMSPAAFVRRPgrWIRELARKPGGTGgTFSAAP------------N 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 308 FTQPHVQdfVRAVCKE--------RIRLMVSGSAALPVPLLEKWRSATGHTLLER------YGMTEIGMALSNPL--TEA 371
Cdd:PRK07769 285 FAFEHAA--ARGLPKDgeppldlsNVKGLLNGSEPVSPASMRKFNEAFAPYGLPPtaikpsYGMAEATLFVSTTPmdEEP 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 372 RVPGSVGTPLPG---VEVRIISEN--PQKGSPYIIHAE-----GNERGTKVTPGfeeKEGELLVRGPSVFREYWDKPEET 441
Cdd:PRK07769 363 TVIYVDRDELNAgrfVEVPADAPNavAQVSAGKVGVSEwavivDPETASELPDG---QIGEIWLHGNNIGTGYWGKPEET 439
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1720427507 442 KSAF---------------TSDG--WFRTGDTAVFKDARYWIRGR 469
Cdd:PRK07769 440 AATFqnilksrlseshaegAPDDalWVRTGDYGVYFDGELYITGR 484
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
197-567 |
3.88e-15 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 77.90 E-value: 3.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 197 AMIFYTSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCpLWVGATCVMLPEfSAQQVW 276
Cdd:cd17654 121 AYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFNITSEDILFLTSPLTFDPSVVEIFLS-LSSGATLLIVPT-SVKVLP 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 277 EKFLSS--EAPQITVFMAVPTVYsklldyydKHFTQPHVQDFVRAVCKErIRLMVSGSAALPVP-LLEKWRSATGHT-LL 352
Cdd:cd17654 199 SKLADIlfKRHRITVLQATPTLF--------RRFGSQSIKSTVLSATSS-LRVLALGGEPFPSLvILSSWRGKGNRTrIF 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 353 ERYGMTEIGM-ALSNPLTEARVPGSVGTPLPG--VEVRIISENPQKGspyiihaegnergtkvtpgfeEKEGELLVRGpS 429
Cdd:cd17654 270 NIYGITEVSCwALAYKVPEEDSPVQLGSPLLGtvIEVRDQNGSEGTG---------------------QVFLGGLNRV-C 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 430 VFREYWDKPEETksaftsdgWFRTGDTAVFKDARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSITDVAVigvpdmT 509
Cdd:cd17654 328 ILDDEVTVPKGT--------MRATGDFVTVKDGELFFLGRKD-SQIKRRGKRINLDLIQQVIESCLGVESCAV------T 392
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 510 W--GQRVTAVVALQEGHSLSHGDLKewaRGVLAPYAVPSELLLVEEIPRNQMGKVNKKEL 567
Cdd:cd17654 393 LsdQQRLIAFIVGESSSSRIHKELQ---LTLLSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
65-572 |
2.06e-14 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 75.92 E-value: 2.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 65 HHTYRELydrsLCLAQEICRL---QGCKVGDLqeerVSFLCSNDVSYVvAQWASWMSGGVAVPLY---WKHPeaQLEYFI 138
Cdd:cd05939 3 HWTFREL----NEYSNKVANFfqaQGYRSGDV----VALFMENRLEFV-ALWLGLAKIGVETALInsnLRLE--SLLHCI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 139 QDSRSSLVVVgqeylerlsplaqRLGVPLLPLTPavyhgaTEKPTEQPVeesGWRDRGAMIfYTSGTTGRPKGALSTHRN 218
Cdd:cd05939 72 TVSKAKALIF-------------NLLDPLLTQSS------TEPPSQDDV---NFRDKLFYI-YTSGTTGLPKAAVIVHSR 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 219 LAAVVTGLVHSWAWTKNDVILHVLPLHH----VHGVVNKLLcplwVGATCVMLPEFSAQQVWEKFLSSEApqiTVFMAVP 294
Cdd:cd05939 129 YYRIAAGAYYAFGMRPEDVVYDCLPLYHsaggIMGVGQALL----HGSTVVIRKKFSASNFWDDCVKYNC---TIVQYIG 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 295 TVYSKLLdyydkhfTQPHVQDfvraVCKERIRLMVsGSAALPvpllEKWRSATGH----TLLERYGMTEIGMALSNPLTE 370
Cdd:cd05939 202 EICRYLL-------AQPPSEE----EQKHNVRLAV-GNGLRP----QIWEQFVRRfgipQIGEFYGATEGNSSLVNIDNH 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 371 ARVPGSVGTPLPGV-EVRIISENPQKGSP------YIIHAEGNERGTKVtpgfeekeGELLVRGPSV-FREYWDKPEETK 442
Cdd:cd05939 266 VGACGFNSRILPSVyPIRLIKVDEDTGELirdsdgLCIPCQPGEPGLLV--------GKIIQNDPLRrFDGYVNEGATNK 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 443 ----SAFTS-DGWFRTGDTAVFKDARY-WIRGRTSvDIIKTGGYKVSALEIERHLLAHPSITDVAVIGV--PDMTWGQRV 514
Cdd:cd05939 338 kiarDVFKKgDSAFLSGDVLVMDELGYlYFKDRTG-DTFRWKGENVSTTEVEGILSNVLGLEDVVVYGVevPGVEGRAGM 416
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720427507 515 TAVVALQEGHSLSHgdLKEWARGVLAPYAVPSELLLVEEIPRNQMGKVNKKELLKQLY 572
Cdd:cd05939 417 AAIVDPERKVDLDR--FSAVLAKSLPPYARPQFIRLLPEVDKTGTFKLQKTDLQKEGY 472
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
62-574 |
2.48e-14 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 76.31 E-value: 2.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 62 KYGHHTYRELYDRSLCLAQEICRLqgckvGDLQEERVSFLCSNDVSYVVAQWASWMSGGVAVPLYWKHPEAQLEYFIQDS 141
Cdd:PLN02387 103 EYEWITYGQVFERVCNFASGLVAL-----GHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNET 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 142 RSSLVVVGQEYLERLSPLAQRL------------GVPLLPLTPAVYHGATEKPTEqpVEESGWRDRG----------AMI 199
Cdd:PLN02387 178 EVTTVICDSKQLKKLIDISSQLetvkrviymddeGVDSDSSLSGSSNWTVSSFSE--VEKLGKENPVdpdlpspndiAVI 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 200 FYTSGTTGRPKGALSTHRNLAAVVTGLVHSW-AWTKNDVILHVLPLHHVhgvvnkllcpLWVGATCVMLPEFSA------ 272
Cdd:PLN02387 256 MYTSGSTGLPKGVMMTHGNIVATVAGVMTVVpKLGKNDVYLAYLPLAHI----------LELAAESVMAAVGAAigygsp 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 273 ------QQVWEKFLSSEAPQI--TVFMAVPTVY------------------SKLLD--YY----------------DKHF 308
Cdd:PLN02387 326 ltltdtSNKIKKGTKGDASALkpTLMTAVPAILdrvrdgvrkkvdakgglaKKLFDiaYKrrlaaiegswfgawglEKLL 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 309 TQPHVQDFVRAVCKERIRLMVSGSAALPVPLLEKWRSATGHTLLERYGMTEI--GMALSNPltEARVPGSVGTPLPGVEV 386
Cdd:PLN02387 406 WDALVFKKIRAVLGGRIRFMLSGGAPLSGDTQRFINICLGAPIGQGYGLTETcaGATFSEW--DDTSVGRVGPPLPCCYV 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 387 RIISenpqkgspyiiHAEGNERGT-KVTPgfeekEGELLVRGPSVFREYWDKPEETKSAFTSDG----WFRTGDTAVFK- 460
Cdd:PLN02387 484 KLVS-----------WEEGGYLISdKPMP-----RGEIVIGGPSVTLGYFKNQEKTDEVYKVDErgmrWFYTGDIGQFHp 547
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 461 DARYWIRGRTSvDIIKT--GGYkVSALEIERHLLAHPSITDVAVIGVPDMTWGqrVTAVVAlqeghslSHGDLKEWARGV 538
Cdd:PLN02387 548 DGCLEIIDRKK-DIVKLqhGEY-VSLGKVEAALSVSPYVDNIMVHADPFHSYC--VALVVP-------SQQALEKWAKKA 616
|
570 580 590
....*....|....*....|....*....|....*.
gi 1720427507 539 LAPYAVPSELllveeiprnqmgkVNKKELLKQLYPS 574
Cdd:PLN02387 617 GIDYSNFAEL-------------CEKEEAVKEVQQS 639
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
197-494 |
9.70e-14 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 74.08 E-value: 9.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 197 AMIFYTSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVmlpeFSAQQVW 276
Cdd:PRK06334 186 AVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLPPFHAYGFNSCTLFPLLSGVPVV----FAYNPLY 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 277 EKFLSS--EAPQITVFMAVPTVYSKLLDYYDKHFTqphvqdfvravCKERIRLMVSGSAALPVPLLEKWRSATGH-TLLE 353
Cdd:PRK06334 262 PKKIVEmiDEAKVTFLGSTPVFFDYILKTAKKQES-----------CLPSLRFVVIGGDAFKDSLYQEALKTFPHiQLRQ 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 354 RYGMTEIGMALS-NPLTEARVPGSVGTPLPGVEVRIISEnpqkgspyiihaegnERGTKVTPGfeeKEGELLVRGPSVFR 432
Cdd:PRK06334 331 GYGTTECSPVITiNTVNSPKHESCVGMPIRGMDVLIVSE---------------ETKVPVSSG---ETGLVLTRGTSLFS 392
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720427507 433 EYW-DKPEETKSAFTSDGWFRTGDTA-VFKDARYWIRGRTSvDIIKTGGYKVSALEIERHLLAH 494
Cdd:PRK06334 393 GYLgEDFGQGFVELGGETWYVTGDLGyVDRHGELFLKGRLS-RFVKIGAEMVSLEALESILMEG 455
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
186-571 |
8.07e-12 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 67.84 E-value: 8.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 186 PVEESgwrdRGAMIFYTSGTTGRPKGALsthRNLAAVVTGLVHSWAWTKNDVILHVLPLHH------VHGVVNKLLCplw 259
Cdd:PTZ00237 250 PVESS----HPLYILYTSGTTGNSKAVV---RSNGPHLVGLKYYWRSIIEKDIPTVVFSHSsigwvsFHGFLYGSLS--- 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 260 VGATCVML------PEFSAQQVWEKFlssEAPQITVFMAVPTVYSKLLDyydkhfTQPHVQDFVRAVCKERIRLMVSGSA 333
Cdd:PTZ00237 320 LGNTFVMFeggiikNKHIEDDLWNTI---EKHKVTHTLTLPKTIRYLIK------TDPEATIIRSKYDLSNLKEIWCGGE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 334 ALPVPLLEKWRSATGHTLLERYGMTEIGMALSNPLTEARVP-GSVGTPLPGVEVRIISEnpqkgspyiihaEGNERGtkv 412
Cdd:PTZ00237 391 VIEESIPEYIENKLKIKSSRGYGQTEIGITYLYCYGHINIPyNATGVPSIFIKPSILSE------------DGKELN--- 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 413 tpgfEEKEGEL---LVRGPSVFREYWDKPEETKSAFTS-DGWFRTGDTAvFKDAR--YWIRGRtSVDIIKTGGYKVSALE 486
Cdd:PTZ00237 456 ----VNEIGEVafkLPMPPSFATTFYKNDEKFKQLFSKfPGYYNSGDLG-FKDENgyYTIVSR-SDDQIKISGNKVQLNT 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 487 IERHLLAHPSITDVAVIGVPDMTWGQRVTAVVALQEGHSLSHGDLKEWARGV-------LAPYAVPSELLLVEEIPRNQM 559
Cdd:PTZ00237 530 IETSILKHPLVLECCSIGIYDPDCYNVPIGLLVLKQDQSNQSIDLNKLKNEInniitqdIESLAVLRKIIIVNQLPKTKT 609
|
410
....*....|..
gi 1720427507 560 GKVNKKELLKQL 571
Cdd:PTZ00237 610 GKIPRQIISKFL 621
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
96-469 |
3.19e-11 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 65.92 E-value: 3.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 96 ERVSFLCSNDVSYVVAQWASWMSGGVAVPLYwkHPEAQ-----LEYFIQDSRSSLVVVGQ-------EYLERLSplaqRL 163
Cdd:PRK12476 93 DRVAILAPQGIDYVAGFFAAIKAGTIAVPLF--APELPghaerLDTALRDAEPTVVLTTTaaaeaveGFLRNLP----RL 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 164 GVPLLPLTPAVYHGATEKPTEQPVEEsgwrDRGAMIFYTSGTTGRPKGALSTHRnlaAVVTGLV-------------HSW 230
Cdd:PRK12476 167 RRPRVIAIDAIPDSAGESFVPVELDT----DDVSHLQYTSGSTRPPVGVEITHR---AVGTNLVqmilsidlldrntHGV 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 231 AWtkndvilhvLPLHHVHGVVNKLLCPLWVGATCVMLP-EFSAQ-QVWEKFLSSEAPQITVFMAVPtvysklldyydkhf 308
Cdd:PRK12476 240 SW---------LPLYHDMGLSMIGFPAVYGGHSTLMSPtAFVRRpQRWIKALSEGSRTGRVVTAAP-------------- 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 309 tqphvqDFVRAVCKER--------IRL----MVSGSAALPVPLLEKWRSATGHTLLER------YGMTEIGMALSN--PL 368
Cdd:PRK12476 297 ------NFAYEWAAQRglpaegddIDLsnvvLIIGSEPVSIDAVTTFNKAFAPYGLPRtafkpsYGIAEATLFVATiaPD 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 369 TEARVPGSVGTPL-PGVEVRIISENPQkGSPYII--HAEGNERGTKVTPGFEEKE-----GELLVRGPSVFREYWDKPEE 440
Cdd:PRK12476 371 AEPSVVYLDREQLgAGRAVRVAADAPN-AVAHVScgQVARSQWAVIVDPDTGAELpdgevGEIWLHGDNIGRGYWGRPEE 449
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1720427507 441 TKSAF------------------TSDGWFRTGDTAVFKDARYWIRGR 469
Cdd:PRK12476 450 TERTFgaklqsrlaegshadgaaDDGTWLRTGDLGVYLDGELYITGR 496
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
199-562 |
4.01e-11 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 65.74 E-value: 4.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 199 IFYTSGTTGRPKG----------ALSThrNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGvvnkllcPLWVGATCVM-- 266
Cdd:PRK10524 238 ILYTSGTTGKPKGvqrdtggyavALAT--SMDTIFGGKAGETFFCASDIGWVVGHSYIVYA-------PLLAGMATIMye 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 267 -LPEFSAQQVWEKFLssEAPQITVFMAVPTVYsKLLDYYDKHFTQPHVQDFVRAvckerirLMVSGSaalpvPLLE---K 342
Cdd:PRK10524 309 gLPTRPDAGIWWRIV--EKYKVNRMFSAPTAI-RVLKKQDPALLRKHDLSSLRA-------LFLAGE-----PLDEptaS 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 343 WRS-ATGHTLLERYGMTEIG---MALSNPLtEARVP--GSVGTPLPGVEVRIISENPqkgspyiihaegnerGTKVTPGf 416
Cdd:PRK10524 374 WISeALGVPVIDNYWQTETGwpiLAIARGV-EDRPTrlGSPGVPMYGYNVKLLNEVT---------------GEPCGPN- 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 417 eEKeGELLVRGP-------SVFReywDKPEETKSAFTSDG--WFRTGDTAVF-KDARYWIRGRTSvDIIKTGGYKVSALE 486
Cdd:PRK10524 437 -EK-GVLVIEGPlppgcmqTVWG---DDDRFVKTYWSLFGrqVYSTFDWGIRdADGYYFILGRTD-DVINVAGHRLGTRE 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 487 IERHLLAHPSITDVAVIGVPDMTWGQRVTAVVALQEGHSLSH--------GDLKEWARGVLAPYAVPSELLLVEEIPRNQ 558
Cdd:PRK10524 511 IEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSDSLADrearlaleKEIMALVDSQLGAVARPARVWFVSALPKTR 590
|
....
gi 1720427507 559 MGKV 562
Cdd:PRK10524 591 SGKL 594
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
67-469 |
8.13e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 61.50 E-value: 8.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 67 TYRELYDRSLCLAQEICRLqgCKVGDlqeeRVSFLCSNDVSYVVAQWASWMSGGVAVPLywkhPEAQleYFIQDSRSSLV 146
Cdd:PRK05850 37 TWSQLYRRTLNVAEELRRH--GSTGD----RAVILAPQGLEYIVAFLGALQAGLIAVPL----SVPQ--GGAHDERVSAV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 147 --------------VVGQ--EYLER--LSPLAQRLGVPLLPL-TPAvyhgatekpteQPVEESGWRDRGAMIFYTSGTTG 207
Cdd:PRK05850 105 lrdtspsvvlttsaVVDDvtEYVAPqpGQSAPPVIEVDLLDLdSPR-----------GSDARPRDLPSTAYLQYTSGSTR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 208 RPKGALSTHRNLAAVVTGLVHSW------AWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVmlpefsaqqvwekFLS 281
Cdd:PRK05850 174 TPAGVMVSHRNVIANFEQLMSDYfgdtggVPPPDTTVVSWLPFYHDMGLVLGVCAPILGGCPAV-------------LTS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 282 SEApqitvFMAVPTVYSKLLDYYDKHFTQPHVQDFVRAVCKER-----------IRLMVSGSaalpvpllEKWRSATGHT 350
Cdd:PRK05850 241 PVA-----FLQRPARWMQLLASNPHAFSAAPNFAFELAVRKTSdddmagldlggVLGIISGS--------ERVHPATLKR 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 351 LLER---YGMTEIGMALSNPLTEARVpgSVGTPLPGVEVRIISENPQKGSPYiiHAE--GNERGTKVT------------ 413
Cdd:PRK05850 308 FADRfapFNLRETAIRPSYGLAEATV--YVATREPGQPPESVRFDYEKLSAG--HAKrcETGGGTPLVsygsprsptvri 383
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720427507 414 ----------PGfeeKEGELLVRGPSVFREYWDKPEETKSAF----------TSDG-WFRTGDTAVFKDARYWIRGR 469
Cdd:PRK05850 384 vdpdtciecpAG---TVGEIWVHGDNVAAGYWQKPEETERTFgatlvdpspgTPEGpWLRTGDLGFISEGELFIVGR 457
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
199-455 |
2.92e-09 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 60.12 E-value: 2.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 199 IFYTSGTTGRPKGALSTHRNLAAVVTGLV-HSWAWTKN-DVILHVLPLHHVHGVVNKLLCpLWVGATCvmlpefsaqQVW 276
Cdd:PTZ00342 309 IVYTSGTSGKPKGVMLSNKNLYNTVVPLCkHSIFKKYNpKTHLSYLPISHIYERVIAYLS-FMLGGTI---------NIW 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 277 EKFLSSEAPQI-----TVFMAVPTVYSKLldyYDKHFTQ-----PHVQDFVRAV-------------------------C 321
Cdd:PTZ00342 379 SKDINYFSKDIynskgNILAGVPKVFNRI---YTNIMTEinnlpPLKRFLVKKIlslrksnnnggfskflegithisskI 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 322 KERI----RLMVSGSAALPVPLLEKWRSATGHTLLERYGMTEIGMALSNPLTEARVPGSVGTPL-PGVEVRIISENPQKG 396
Cdd:PTZ00342 456 KDKVnpnlEVILNGGGKLSPKIAEELSVLLNVNYYQGYGLTETTGPIFVQHADDNNTESIGGPIsPNTKYKVRTWETYKA 535
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720427507 397 spyiihaegnergTKVTPgfeekEGELLVRGPSVFREYWDKPEETKSAFTSDGWFRTGD 455
Cdd:PTZ00342 536 -------------TDTLP-----KGELLIKSDSIFSGYFLEKEQTKNAFTEDGYFKTGD 576
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
106-571 |
3.85e-09 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 59.39 E-value: 3.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 106 VSYVVAQWASWMSGGV----------AVPLYWKHpeAQLEYFIQDSRSSLVVVGqEYLERLSPLAQrlGVPLLPLTPAvy 175
Cdd:PRK05851 65 VELVAAIQGAWLAGAAvsilpgpvrgADDGRWAD--ATLTRFAGIGVRTVLSHG-SHLERLRAVDS--SVTVHDLATA-- 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 176 hGATEKPTEQPVEESGwrdRGAMIFYTSGTTGRPKGALSTHRNLAAVVTGLV-HSWAWTKNDVILHVLPLHHVHGVVNkL 254
Cdd:PRK05851 138 -AHTNRSASLTPPDSG---GPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNaRVGLDAATDVGCSWLPLYHDMGLAF-L 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 255 LCPLWVGATCVMLPE--FSAQQV-WEKFLSSEAPQITvfmAVPTV-YSKLLDYYDKhftqphvqdfVRAVCKERIRLMVS 330
Cdd:PRK05851 213 LTAALAGAPLWLAPTtaFSASPFrWLSWLSDSRATLT---AAPNFaYNLIGKYARR----------VSDVDLGALRVALN 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 331 GSAALPVPLLEKWRSATGH------TLLERYGMTEIGMALSNPltearVPGS--------------------VGTPLPGV 384
Cdd:PRK05851 280 GGEPVDCDGFERFATAMAPfgfdagAAAPSYGLAESTCAVTVP-----VPGIglrvdevttddgsgarrhavLGNPIPGM 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 385 EVRIiseNPQKGSpyiihAEGNERGTkvtpgfeekeGELLVRGPSVFREYWDKPeetksAFTSDGWFRTGDTAVFKDARY 464
Cdd:PRK05851 355 EVRI---SPGDGA-----AGVAGREI----------GEIEIRGASMMSGYLGQA-----PIDPDDWFPTGDLGYLVDGGL 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 465 WIRGRTSvDIIKTGGYKVSALEIERHLLAHPSITDVAVIGVPDMTWGQRVTAVVALQEGHSLSHGDLKEWARGVLAPYA- 543
Cdd:PRK05851 412 VVCGRAK-ELITVAGRNIFPTEIERVAAQVRGVREGAVVAVGTGEGSARPGLVIAAEFRGPDEAGARSEVVQRVASECGv 490
|
490 500 510
....*....|....*....|....*....|
gi 1720427507 544 VPSELLLVE--EIPRNQMGKVNKKELLKQL 571
Cdd:PRK05851 491 VPSDVVFVApgSLPRTSSGKLRRLAVKRSL 520
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
452-578 |
2.29e-04 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 44.30 E-value: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 452 RTGDtaVFK---DARYWIRGRTSvDIIKTGGYKVSALEIERHL-LAHPSITDVAVIGVPDMTWGQRVTAVVALQEGHSLS 527
Cdd:PLN03052 592 RHGD--IFErtsGGYYRAHGRAD-DTMNLGGIKVSSVEIERVCnAADESVLETAAIGVPPPGGGPEQLVIAAVLKDPPGS 668
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720427507 528 HGDLKEWARGV-------LAPYAVPSELLLVEEIPRNQMGKVNKKELLKQLYPSGQRS 578
Cdd:PLN03052 669 NPDLNELKKIFnsaiqkkLNPLFKVSAVVIVPSFPRTASNKVMRRVLRQQLAQELSRS 726
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
199-571 |
2.94e-04 |
|
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: 43.80 E-value: 2.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 199 IFYTSGTTGRPKGalsthrnlaavvtgLVHSWAWTkndvILHVLPLHHVHGVV-----------------NKLLCPLWVG 261
Cdd:cd05943 254 ILYSSGTTGLPKC--------------IVHGAGGT----LLQHLKEHILHCDLrpgdrlfyyttcgwmmwNWLVSGLAVG 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 262 ATCVML---PEFSAQQVWEKFLSSEapQITVFMAVPtvysKLLDYYDKHFTQPHvqdfvRAVCKERIRLMVSGSAALPVP 338
Cdd:cd05943 316 ATIVLYdgsPFYPDTNALWDLADEE--GITVFGTSA----KYLDALEKAGLKPA-----ETHDLSSLRTILSTGSPLKPE 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 339 LLEKWRSATGHTLL--ERYGMTEI--GMALSNPLTEARvPGSVGTPLPGVEVRIISENpqkgspyiihaegnerGTKVTp 414
Cdd:cd05943 385 SFDYVYDHIKPDVLlaSISGGTDIisCFVGGNPLLPVY-RGEIQCRGLGMAVEAFDEE----------------GKPVW- 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 415 gfEEKeGELLVRG--PSVFREYWDKPEETK--SAF--TSDGWFRTGDTAVF-KDARYWIRGRtSVDIIKTGGYKVSALEI 487
Cdd:cd05943 447 --GEK-GELVCTKpfPSMPVGFWNDPDGSRyrAAYfaKYPGVWAHGDWIEItPRGGVVILGR-SDGTLNPGGVRIGTAEI 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 488 ERHLLAHPSITDVAVIGVPDMTWGQRVTAVVALQEGHSLSHgDLKEWARGV----LAPYAVPSELLLVEEIPRNQMGKvn 563
Cdd:cd05943 523 YRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLREGVELDD-ELRKRIRSTirsaLSPRHVPAKIIAVPDIPRTLSGK-- 599
|
....*....
gi 1720427507 564 KKELL-KQL 571
Cdd:cd05943 600 KVEVAvKKI 608
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
452-571 |
1.94e-03 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 40.95 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427507 452 RTGDTAVFKDARYWIRGRTSVDIIKTGGYKVSALEIERHLL-AHPSITDVAVIGVPDMTWGQRVTAVVA----LQEGHSL 526
Cdd:PLN03051 360 RHGDIMKRTPGGYFCVQGRADDTMNLGGIKTSSVEIERACDrAVAGIAETAAVGVAPPDGGPELLVIFLvlgeEKKGFDQ 439
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1720427507 527 SHG-DLK----EWARGVLAPYAVPSELLLVEEIPRNQMGKVNKKELLKQL 571
Cdd:PLN03051 440 ARPeALQkkfqEAIQTNLNPLFKVSRVKIVPELPRNASNKLLRRVLRDQL 489
|
|
| |
