|
Name |
Accession |
Description |
Interval |
E-value |
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
14-447 |
0e+00 |
|
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: 775.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 14 SYPALSAQAAREPAAFWGPLARDtLVWDTPYHTVWDCDFSTGKIGWFLGGQLNVSVNCLDQHVRKSPESVALIWERDEPG 93
Cdd:cd05966 2 QYKELYKQSIEDPEEFWGEIAKE-LDWFKPWDKVLDWSKGPPFIKWFEGGKLNISYNCLDRHLKERGDKVAIIWEGDEPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 94 TEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVV 173
Cdd:cd05966 81 QSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFAGFSAESLADRINDAQCKLV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 174 ITFNQGLRGGRVVELKKIVDEAVKHCPTVQHVLVAHRTDNKVHM-GDLDVPLEQEMAKEDPVCAPESMGSEDMLFMLYTS 252
Cdd:cd05966 161 ITADGGYRGGKVIPLKEIVDEALEKCPSVEKVLVVKRTGGEVPMtEGRDLWWHDLMAKQSPECEPEWMDSEDPLFILYTS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 253 GSTGMPKGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPVYPNAGRYWET 332
Cdd:cd05966 241 GSTGKPKGVVHTTGGYLLYAATTFKYVFDYHPDDIYWCTADIGWITGHSYIVYGPLANGATTVMFEGTPTYPDPGRYWDI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 333 VERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDSRCTLVDTWWQTETGGICIAP 412
Cdd:cd05966 321 VEKHKVTIFYTAPTAIRALMKFGDEWVKKHDLSSLRVLGSVGEPINPEAWMWYYEVIGKERCPIVDTWWQTETGGIMITP 400
|
410 420 430
....*....|....*....|....*....|....*
gi 91993047 413 RPSEegAEILPAMAMRPFFGIVPVLMDEKGSVVEG 447
Cdd:cd05966 401 LPGA--TPLKPGSATRPFFGIEPAILDEEGNEVEG 433
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
9-451 |
0e+00 |
|
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called acetyl-CoA synthetase and acetyl-activating enzyme. It catalyzes the reaction ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA and belongs to the family of AMP-binding enzymes described by pfam00501.
Pssm-ID: 274022 [Multi-domain] Cd Length: 626 Bit Score: 775.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 9 AAQPGSYPALSAQAAREPAAFWGPLARDTLVWDTPYHTVWDCDFSTgKIGWFLGGQLNVSVNCLDQHVRKSPESVALIWE 88
Cdd:TIGR02188 1 IANLEQYKELYEESIEDPDKFWAKLARELLDWFKPFTKVLDWSFPP-FYKWFVGGELNVSYNCVDRHLEARPDKVAIIWE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 89 RDEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDA 168
Cdd:TIGR02188 80 GDEPGEVRKITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIHSVVFGGFSAEALADRINDA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 169 KCKVVITFNQGLRGGRVVELKKIVDEAVKHCP-TVQHVLVAHRTDNKV-HMGD-LDVPLEQEMAKEDPVCAPESMGSEDM 245
Cdd:TIGR02188 160 GAKLVITADEGLRGGKVIPLKAIVDEALEKCPvSVEHVLVVRRTGNPVvPWVEgRDVWWHDLMAKASAYCEPEPMDSEDP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 246 LFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPVYPN 325
Cdd:TIGR02188 240 LFILYTSGSTGKPKGVLHTTGGYLLYAAMTMKYVFDIKDGDIFWCTADVGWITGHSYIVYGPLANGATTVMFEGVPTYPD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 326 AGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDSRCTLVDTWWQTET 405
Cdd:TIGR02188 320 PGRFWEIIEKHKVTIFYTAPTAIRALMRLGDEWVKKHDLSSLRLLGSVGEPINPEAWMWYYKVVGKERCPIVDTWWQTET 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 91993047 406 GGICIAPRPSeeGAEILPAMAMRPFFGIVPVLMDEKGSVVEGCNVS 451
Cdd:TIGR02188 400 GGIMITPLPG--ATPTKPGSATLPFFGIEPAVVDEEGNPVEGPGEG 443
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
5-447 |
0e+00 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 688.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 5 VAAAAAQPGSYPALSAQAAREPAAFWGPLARDtLVWDTPYHTVWDCDfsTGKIGWFLGGQLNVSVNCLDQHVRKSPESVA 84
Cdd:PRK00174 9 AANALIDMEQYKALYQESVEDPEGFWAEQAKR-LDWFKPFDTVLDWN--APFIKWFEDGELNVSYNCLDRHLKTRGDKVA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 85 LIWERDEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGR 164
Cdd:PRK00174 86 IIWEGDDPGDSRKITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVVFGGFSAEALADR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 165 INDAKCKVVITFNQGLRGGRVVELKKIVDEAVKHCPTVQHVLVAHRTDNKVHMGD-LDVPLEQEMAKEDPVCAPESMGSE 243
Cdd:PRK00174 166 IIDAGAKLVITADEGVRGGKPIPLKANVDEALANCPSVEKVIVVRRTGGDVDWVEgRDLWWHELVAGASDECEPEPMDAE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 244 DMLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPVY 323
Cdd:PRK00174 246 DPLFILYTSGSTGKPKGVLHTTGGYLVYAAMTMKYVFDYKDGDVYWCTADVGWVTGHSYIVYGPLANGATTLMFEGVPNY 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 324 PNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDSRCTLVDTWWQT 403
Cdd:PRK00174 326 PDPGRFWEVIDKHKVTIFYTAPTAIRALMKEGDEHPKKYDLSSLRLLGSVGEPINPEAWEWYYKVVGGERCPIVDTWWQT 405
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 91993047 404 ETGGICIAPRPseeGA-EILPAMAMRPFFGIVPVLMDEKGSVVEG 447
Cdd:PRK00174 406 ETGGIMITPLP---GAtPLKPGSATRPLPGIQPAVVDEEGNPLEG 447
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
59-447 |
0e+00 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 553.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 59 WFLGGQLNVSVNCLDQHVRKSPESVALIWErDEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAA 138
Cdd:COG0365 2 WFVGGRLNIAYNCLDRHAEGRGDKVALIWE-GEDGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 139 MLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFNQGLRGGRVVELKKIVDEAVKHCPTVQHVLVAHRTDNKVHMG 218
Cdd:COG0365 81 MLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGGLRGGKVIDLKEKVDEALEELPSLEHVIVVGRTGADVPME 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 219 DlDVPLEQEMAKEDPVCAPESMGSEDMLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWIT 298
Cdd:COG0365 161 G-DLDWDELLAAASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVLDLKPGDVFWCTADIGWAT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 299 GHSYVVYGPLCNGATSVLFESTPVYPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPIN 378
Cdd:COG0365 240 GHSYIVYGPLLNGATVVLYEGRPDFPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPLKKYDLSSLRLLGSAGEPLN 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 91993047 379 CEAWEWLHRVVGdsrCTLVDTWWQTETGGICIAPRPseeGAEILPAMAMRPFFGIVPVLMDEKGSVVEG 447
Cdd:COG0365 320 PEVWEWWYEAVG---VPIVDGWGQTETGGIFISNLP---GLPVKPGSMGKPVPGYDVAVVDEDGNPVPP 382
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
21-447 |
8.57e-161 |
|
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: 466.67 E-value: 8.57e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 21 QAAREPAAFWGPLARDtLVWDTPYHTVWDCDFSTGK--IGWFLGGQLNVSVNCLDQHVRKSPESVALIWERDEpGTEVR- 97
Cdd:cd17634 7 QSINDPDTFWGEAGKI-LDWITPYQKVKNTSFAPGApsIKWFEDATLNLAANALDRHLRENGDRTAIIYEGDD-TSQSRt 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 98 ITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFN 177
Cdd:cd17634 85 ISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITAD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 178 QGLRGGRVVELKKIVDEAVK-HCPTVQHVLVAHRTDNKVH-MGDLDVPLEQEMAKEDPVCAPESMGSEDMLFMLYTSGST 255
Cdd:cd17634 165 GGVRAGRSVPLKKNVDDALNpNVTSVEHVIVLKRTGSDIDwQEGRDLWWRDLIAKASPEHQPEAMNAEDPLFILYTSGTT 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 256 GMPKGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPVYPNAGRYWETVER 335
Cdd:cd17634 245 GKPKGVLHTTGGYLVYAATTMKYVFDYGPGDIYWCTADVGWVTGHSYLLYGPLACGATTLLYEGVPNWPTPARMWQVVDK 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 336 LKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDSRCTLVDTWWQTETGGICIAPRPs 415
Cdd:cd17634 325 HGVNILYTAPTAIRALMAAGDDAIEGTDRSSLRILGSVGEPINPEAYEWYWKKIGKEKCPVVDTWWQTETGGFMITPLP- 403
|
410 420 430
....*....|....*....|....*....|...
gi 91993047 416 eeGAEILPA-MAMRPFFGIVPVLMDEKGSVVEG 447
Cdd:cd17634 404 --GAIELKAgSATRPVFGVQPAVVDNEGHPQPG 434
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
7-447 |
2.10e-154 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 453.20 E-value: 2.10e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 7 AAAAQPGSYPALSAQAAREPAAFWGPLArDTLVWDTPYHTVWDC----DFSTG--KIGWFLGGQLNVSVNCLDQHVRK-S 79
Cdd:PLN02654 24 ALVSSPQQYMEMYKRSVDDPAGFWSDIA-SQFYWKQKWEGDEVCsenlDVRKGpiSIEWFKGGKTNICYNCLDRNVEAgN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 80 PESVALIWERDEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAE 159
Cdd:PLN02654 103 GDKIAIYWEGNEPGFDASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 160 SLAGRINDAKCKVVITFNQGLRGGRVVELKKIVDEA----------VKHCPTVQHVLVAHRTDNKVHMGDlDVPLEQEMA 229
Cdd:PLN02654 183 SLAQRIVDCKPKVVITCNAVKRGPKTINLKDIVDAAldesakngvsVGICLTYENQLAMKREDTKWQEGR-DVWWQDVVP 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 230 KEDPVCAPESMGSEDMLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLC 309
Cdd:PLN02654 262 NYPTKCEVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMVYTATTFKYAFDYKPTDVYWCTADCGWITGHSYVTYGPML 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 310 NGATSVLFESTPVYPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVV 389
Cdd:PLN02654 342 NGATVLVFEGAPNYPDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDEYVTRHSRKSLRVLGSVGEPINPSAWRWFFNVV 421
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 91993047 390 GDSRCTLVDTWWQTETGGICIAPRPseeGAEIL-PAMAMRPFFGIVPVLMDEKGSVVEG 447
Cdd:PLN02654 422 GDSRCPISDTWWQTETGGFMITPLP---GAWPQkPGSATFPFFGVQPVIVDEKGKEIEG 477
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
15-452 |
3.27e-128 |
|
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: 384.36 E-value: 3.27e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 15 YPALSAQAAREPAAFWGPLARdTLVWDTPYHTVWDCDfSTGKIGWFLGGQLNVSVNCLDQHVRKS-PESVALIWERDEPG 93
Cdd:cd05967 1 YEEVYARSIAEPEAFWAEQAR-LIDWFKPPEKILDNS-NPPFTRWFVGGRLNTCYNALDRHVEAGrGDQIALIYDSPVTG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 94 TEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVV 173
Cdd:cd05967 79 TERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAKELASRIDDAKPKLI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 174 ITFNQGLRGGRVVELKKIVDEAVK---HCPtvQHVLVAHRTDNKVHMGD--LDVPLEQEMAKEDPV-CAPesMGSEDMLF 247
Cdd:cd05967 159 VTASCGIEPGKVVPYKPLLDKALElsgHKP--HHVLVLNRPQVPADLTKpgRDLDWSELLAKAEPVdCVP--VAATDPLY 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 248 MLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPV-YPNA 326
Cdd:cd05967 235 ILYTSGTTGKPKGVVRDNGGHAVALNWSMRNIYGIKPGDVWWAASDVGWVVGHSYIVYGPLLHGATTVLYEGKPVgTPDP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 327 GRYWETVERLKINQFYGAPTAVRLLLKY--GDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGdsrCTLVDTWWQTE 404
Cdd:cd05967 315 GAFWRVIEKYQVNALFTAPTAIRAIRKEdpDGKYIKKYDLSSLRTLFLAGERLDPPTLEWAENTLG---VPVIDHWWQTE 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 91993047 405 TGG------ICIAPRPSEEGAEILPAMAMRpfFGIV-----PVLMDEKGSVVEGCNVSP 452
Cdd:cd05967 392 TGWpitanpVGLEPLPIKAGSPGKPVPGYQ--VQVLdedgePVGPNELGNIVIKLPLPP 448
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
14-440 |
1.84e-120 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 365.04 E-value: 1.84e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 14 SYPALSAQAAREPAAFWGPLARdtLV-WDTPYHTVwdCDFSTGKIG-WFLGGQLNVSVNCLDQHVRKSPESVALIWERDE 91
Cdd:PRK10524 3 SYSEFYQRSIDDPEAFWAEQAR--RIdWQTPFTQV--LDYSNPPFArWFVGGRTNLCHNAVDRHLAKRPEQLALIAVSTE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 92 PGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCK 171
Cdd:PRK10524 79 TDEERTYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIHSVVFGGFASHSLAARIDDAKPV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 172 VVITFNQGLRGGRVVELKKIVDEAV---KHCPtvQHVLVAHR-TDNKVHMGDLDVPLEQEMAK-EDPVCAPESMGSEDML 246
Cdd:PRK10524 159 LIVSADAGSRGGKVVPYKPLLDEAIalaQHKP--RHVLLVDRgLAPMARVAGRDVDYATLRAQhLGARVPVEWLESNEPS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 247 FMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPVYPNA 326
Cdd:PRK10524 237 YILYTSGTTGKPKGVQRDTGGYAVALATSMDTIFGGKAGETFFCASDIGWVVGHSYIVYAPLLAGMATIMYEGLPTRPDA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 327 GRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDSrctLVDTWWQTETG 406
Cdd:PRK10524 317 GIWWRIVEKYKVNRMFSAPTAIRVLKKQDPALLRKHDLSSLRALFLAGEPLDEPTASWISEALGVP---VIDNYWQTETG 393
|
410 420 430
....*....|....*....|....*....|....
gi 91993047 407 GICIAPRPSEEGAEILPAMAMRPFFGIVPVLMDE 440
Cdd:PRK10524 394 WPILAIARGVEDRPTRLGSPGVPMYGYNVKLLNE 427
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
13-447 |
4.37e-110 |
|
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: 337.54 E-value: 4.37e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 13 GSYPALSAQAAREPAAFWGPLARDTLVW--DTPYHTVwdcDFSTGK--IGWFLGGQLNVSVNCLDQHVRKSPESVALIWE 88
Cdd:cd05968 7 PDLEAFLERSAEDNAWFWGEFVKDVGIEwyEPPYQTL---DLSGGKpwAAWFVGGRMNIVEQLLDKWLADTRTRPALRWE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 89 rDEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDA 168
Cdd:cd05968 84 -GEDGTSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 169 KCKVVITFNQGLRGGRVVELKKIVDEAVKHCPTVQHVLVAHRTDNKVHMGDLDvPLEQEMAKEDPVCAPESMGSEDMLFM 248
Cdd:cd05968 163 EAKALITADGFTRRGREVNLKEEADKACAQCPTVEKVVVVRHLGNDFTPAKGR-DLSYDEEKETAGDGAERTESEDPLMI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 249 LYTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGhSYVVYGPLCNGATSVLFESTPVYPNAGR 328
Cdd:cd05968 242 IYTSGTTGKPKGTVHVHAGFPLKAAQDMYFQFDLKPGDLLTWFTDLGWMMG-PWLIFGGLILGATMVLYDGAPDHPKADR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 329 YWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDSRCTLVDTWWQTE-TGG 407
Cdd:cd05968 321 LWRMVEDHEITHLGLSPTLIRALKPRGDAPVNAHDLSSLRVLGSTGEPWNPEPWNWLFETVGKGRNPIINYSGGTEiSGG 400
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 91993047 408 I--CIAPRPseegaeILPAMAMRPFFGIVPVLMDEKGSVVEG 447
Cdd:cd05968 401 IlgNVLIKP------IKPSSFNGPVPGMKADVLDESGKPARP 436
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
59-446 |
1.05e-91 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 288.72 E-value: 1.05e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 59 WFLGGQLNVSVNCLDQHVrKSP--ESVALIWERdePGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAV 136
Cdd:PRK04319 36 WLETGKVNIAYEAIDRHA-DGGrkDKVALRYLD--ASRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELY 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 137 AAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFNQGLRggrvvelKKIVDEavkhCPTVQHVLVahrTDNKVH 216
Cdd:PRK04319 113 FALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLITTPALLE-------RKPADD----LPSLKHVLL---VGEDVE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 217 MGDLDVPLEQEMAKEDPVCAPESMGSEDMLFMLYTSGSTGMPKGIVHTQagyllYAALTH----KLVFDHQPGDIFGCVA 292
Cdd:PRK04319 179 EGPGTLDFNALMEQASDEFDIEWTDREDGAILHYTSGSTGKPKGVLHVH-----NAMLQHyqtgKYVLDLHEDDVYWCTA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 293 DIGWITGHSYVVYGPLCNGATSVLFESTpvyPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGS 372
Cdd:PRK04319 254 DPGWVTGTSYGIFAPWLNGATNVIDGGR---FSPERWYRILEDYKVTVWYTAPTAIRMLMGAGDDLVKKYDLSSLRHILS 330
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 91993047 373 VGEPINCEAWEWLHRVVGdsrCTLVDTWWQTETGGICIAPRPSEegaEILPAMAMRPFFGIVPVLMDEKGSVVE 446
Cdd:PRK04319 331 VGEPLNPEVVRWGMKVFG---LPIHDNWWMTETGGIMIANYPAM---DIKPGSMGKPLPGIEAAIVDDQGNELP 398
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
72-442 |
3.25e-85 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 267.26 E-value: 3.25e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 72 LDQHVRKSPESVALiwerdEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTV 151
Cdd:pfam00501 1 LERQAARTPDKTAL-----EVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 152 IFAGFSAESLAGRINDAKCKVVITFnqglrggrVVELKKIVDEAVKHCPTVQHVLVAHRTDnkvhMGDLDVPLEQEMAKE 231
Cdd:pfam00501 76 LNPRLPAEELAYILEDSGAKVLITD--------DALKLEELLEALGKLEVVKLVLVLDRDP----VLKEEPLPEEAKPAD 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 232 DPVCAPESMGSEDMLFMLYTSGSTGMPKGIVHTQaGYLLYAALTHKLVFDHQ----PGDIFGCVADIGWITGHSYVVYGP 307
Cdd:pfam00501 144 VPPPPPPPPDPDDLAYIIYTSGTTGKPKGVMLTH-RNLVANVLSIKRVRPRGfglgPDDRVLSTLPLFHDFGLSLGLLGP 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 308 LCNGATSVLFESTPVyPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTLGSVGEPINCEAWEWLHR 387
Cdd:pfam00501 223 LLAGATVVLPPGFPA-LDPAALLELIERYKVTVLYGVPTLLNMLLEAGAP--KRALLSSLRLVLSGGAPLPPELARRFRE 299
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 91993047 388 VVGdsrCTLVDTWWQTETGGICIAPRPSEEGAEILPAmAMRPFFGIVPVLMDEKG 442
Cdd:pfam00501 300 LFG---GALVNGYGLTETTGVVTTPLPLDEDLRSLGS-VGRPLPGTEVKIVDDET 350
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
99-446 |
7.25e-72 |
|
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: 233.55 E-value: 7.25e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 99 TYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITfnq 178
Cdd:cd05969 2 TFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLIT--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 179 glrggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvplEQEMAkedpvcapESMGSEDMLFMLYTSGSTGMP 258
Cdd:cd05969 79 ----------------------------------------------TEELY--------ERTDPEDPTLLHYTSGTTGTP 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 259 KGIVHTQAGYLLYAaLTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPvypNAGRYWETVERLKI 338
Cdd:cd05969 105 KGVLHVHDAMIFYY-FTGKYVLDLHPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVVYEGRF---DAESWYGIIERVKV 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 339 NQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGdsrCTLVDTWWQTETGGICIAPRPseeG 418
Cdd:cd05969 181 TVWYTAPTAIRMLMKEGDELARKYDLSSLRFIHSVGEPLNPEAIRWGMEVFG---VPIHDTWWQTETGSIMIANYP---C 254
|
330 340
....*....|....*....|....*...
gi 91993047 419 AEILPAMAMRPFFGIVPVLMDEKGSVVE 446
Cdd:cd05969 255 MPIKPGSMGKPLPGVKAAVVDENGNELP 282
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
99-446 |
2.31e-56 |
|
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: 192.55 E-value: 2.31e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 99 TYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITfnq 178
Cdd:cd05972 2 SFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVT--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 179 glrggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemakedpvcapesmGSEDMLFMLYTSGSTGMP 258
Cdd:cd05972 79 --------------------------------------------------------------DAEDPALIYFTSGTTGLP 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 259 KGIVHTqAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPVYPNagRYWETVERLKI 338
Cdd:cd05972 97 KGVLHT-HSYPLGHIPTAAYWLGLRPDDIHWNIADPGWAKGAWSSFFGPWLLGATVFVYEGPRFDAE--RILELLERYGV 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 339 NQFYGAPTAVRLLLKYGDAwvkKYDRSSLRTLGSVGEPINCEAWEWLHRVVGdsrCTLVDTWWQTETgGICIAPRPseeG 418
Cdd:cd05972 174 TSFCGPPTAYRMLIKQDLS---SYKFSHLRLVVSAGEPLNPEVIEWWRAATG---LPIRDGYGQTET-GLTVGNFP---D 243
|
330 340
....*....|....*....|....*...
gi 91993047 419 AEILPAMAMRPFFGIVPVLMDEKGSVVE 446
Cdd:cd05972 244 MPVKPGSMGRPTPGYDVAIIDDDGRELP 271
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
13-409 |
4.85e-56 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 196.55 E-value: 4.85e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 13 GSYPALSAQAAREPAAFWgplardTLVWD-------TPYHTVWDcdfSTGKIG--WFLGGQLNVSVNCLDQHvrkSPESV 83
Cdd:PRK03584 34 DDYAALWRWSVEDLEAFW------QSVWDffgvigsTPYTVVLA---GRRMPGarWFPGARLNYAENLLRHR---RDDRP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 84 ALIWeRDEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAG 163
Cdd:PRK03584 102 AIIF-RGEDGPRRELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLGAIWSSCSPDFGVQGVLD 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 164 RINDAKCKVVITFNqGLR-GGRVVELKKIVDEAVKHCPTVQHVLVAHRTDNKVHMGDLD--VPLEQEMAK-EDPVCAPES 239
Cdd:PRK03584 181 RFGQIEPKVLIAVD-GYRyGGKAFDRRAKVAELRAALPSLEHVVVVPYLGPAAAAAALPgaLLWEDFLAPaEAAELEFEP 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 240 MGSEDMLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHQPGDIF----GCvadiGWITgHSYVVYGPLCnGATSV 315
Cdd:PRK03584 260 VPFDHPLWILYSSGTTGLPKCIVHGHGGILLEHLKELGLHCDLGPGDRFfwytTC----GWMM-WNWLVSGLLV-GATLV 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 316 LFESTPVYPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDsrct 395
Cdd:PRK03584 334 LYDGSPFYPDPNVLWDLAAEEGVTVFGTSAKYLDACEKAGLVPGETHDLSALRTIGSTGSPLPPEGFDWVYEHVKA---- 409
|
410
....*....|....*.
gi 91993047 396 lvDTWWQTETGG--IC 409
Cdd:PRK03584 410 --DVWLASISGGtdIC 423
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
13-409 |
3.76e-55 |
|
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: 193.64 E-value: 3.76e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 13 GSYPALSAQAAREPAAFWgplardTLVWD---TPYHTVWDCDFSTGKI----GWFLGGQLNVSVNCLdQHvRKSPESVAL 85
Cdd:cd05943 17 ADYAALHRWSVDDPGAFW------AAVWDfsgVRGSKPYDVVVVSGRImpgaRWFPGARLNYAENLL-RH-ADADDPAAI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 86 IweRDEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRI 165
Cdd:cd05943 89 Y--AAEDGERTEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFGVPGVLDRF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 166 NDAKCKVVITFNQGLRGGRVVELKKIVDEAVKHCPTVQHVLVAHRTDNKVHMGDLDVP----LEQEMAKE-DPVCAPESM 240
Cdd:cd05943 167 GQIEPKVLFAVDAYTYNGKRHDVREKVAELVKGLPSLLAVVVVPYTVAAGQPDLSKIAkaltLEDFLATGaAGELEFEPL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 241 GSEDMLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVvyGPLCNGATSVLFEST 320
Cdd:cd05943 247 PFDHPLYILYSSGTTGLPKCIVHGAGGTLLQHLKEHILHCDLRPGDRLFYYTTCGWMMWNWLV--SGLAVGATIVLYDGS 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 321 PVYPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDsrctlvDTW 400
Cdd:cd05943 325 PFYPDTNALWDLADEEGITVFGTSAKYLDALEKAGLKPAETHDLSSLRTILSTGSPLKPESFDYVYDHIKP------DVL 398
|
410
....*....|.
gi 91993047 401 WQTETGG--IC 409
Cdd:cd05943 399 LASISGGtdII 409
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
72-445 |
1.79e-52 |
|
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: 182.70 E-value: 1.79e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 72 LDQHVRKSPESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTV 151
Cdd:COG0318 5 LRRAAARHPDRPALVFG------GRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 152 IFAGFSAESLAGRINDAKCKVVITFnqglrggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemake 231
Cdd:COG0318 79 LNPRLTAEELAYILEDSGARALVTA------------------------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 232 dpvcapesmgsedmlFMLYTSGSTGMPKGIVHTQAGyLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNG 311
Cdd:COG0318 104 ---------------LILYTSGTTGRPKGVMLTHRN-LLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAG 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 312 ATSVLFEStpvyPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGd 391
Cdd:COG0318 168 ATLVLLPR----FDPERVLELIERERVTVLFGVPTMLARLLRHPEF--ARYDLSSLRLVVSGGAPLPPELLERFEERFG- 240
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 91993047 392 srCTLVDTWWQTETGGICIAPRpsEEGAEILPAMAMRPFFGIVPVLMDEKGSVV 445
Cdd:COG0318 241 --VRIVEGYGLTETSPVVTVNP--EDPGERRPGSVGRPLPGVEVRIVDEDGREL 290
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
10-406 |
1.78e-47 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 173.00 E-value: 1.78e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 10 AQPGSYPALSAQAAREPAAFWGPLARDTLVWDTPYHTVwdcdFSTGKI--GWFLGGQLNVSVNCLDQHVrKSP---ESVA 84
Cdd:PTZ00237 5 SDPFDYENDSNYANSNPESFWDEVAKKYVHWDKMYDKV----YSGDEIypDWFKGGELNTCYNVLDIHV-KNPlkrDQDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 85 LIWERDEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGR 164
Cdd:PTZ00237 80 LIYECPYLKKTIKLTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKSLIDR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 165 INDAKCKVVITFNQGLRGGRVVELKKIVDEAV---KHCPTvqHVLVAHRTD-----NKVHMGD-------LDVPLEQEMA 229
Cdd:PTZ00237 160 IETITPKLIITTNYGILNDEIITFTPNLKEAIelsTFKPS--NVITLFRNDitsesDLKKIETiptipntLSWYDEIKKI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 230 KED---PVCAPESMGSEDMLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYvVYG 306
Cdd:PTZ00237 238 KENnqsPFYEYVPVESSHPLYILYTSGTTGNSKAVVRSNGPHLVGLKYYWRSIIEKDIPTVVFSHSSIGWVSFHGF-LYG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 307 PLCNGATSVLFESTPVYPNAGR--YWETVERLKINQFYGAPTAVRLLLKY---GDAWVKKYDRSSLRTLGSVGEPINCEA 381
Cdd:PTZ00237 317 SLSLGNTFVMFEGGIIKNKHIEddLWNTIEKHKVTHTLTLPKTIRYLIKTdpeATIIRSKYDLSNLKEIWCGGEVIEESI 396
|
410 420
....*....|....*....|....*
gi 91993047 382 WEWLHRVVGdSRCTLVdtWWQTETG 406
Cdd:PTZ00237 397 PEYIENKLK-IKSSRG--YGQTEIG 418
|
|
| ac_ac_CoA_syn |
TIGR01217 |
acetoacetyl-CoA synthase; This enzyme catalyzes the first step of the mevalonate pathway of ... |
13-407 |
1.64e-41 |
|
acetoacetyl-CoA synthase; This enzyme catalyzes the first step of the mevalonate pathway of IPP biosynthesis. Most bacteria do not use this pathway, but rather the deoxyxylulose pathway. [Central intermediary metabolism, Other]
Pssm-ID: 273507 [Multi-domain] Cd Length: 652 Bit Score: 156.19 E-value: 1.64e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 13 GSYPALSAQAAREPAAFWGPLARDT-LVWDTPYHTVWDCDFSTGKIgWFLGGQLNVSVNCLdqhvRKSPESVALIWeRDE 91
Cdd:TIGR01217 35 GGYDALHRWSVDELDTFWKAVWEWFdVRFSTPCARVVDDRTMPGAQ-WFPGARLNYAENLL----RAAGTEPALLY-VDE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 92 PGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCK 171
Cdd:TIGR01217 109 THEPAPVTWAELRRQVASLAAALRALGVRPGDRVSGYLPNIPQAVVAMLATASVGAIWSSCSPDFGARGVLDRFQQIEPK 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 172 VVITFNQGLRGGRVVELKKIVDEAVKHCPTVQHVLVahrtdnkvhmgdldVPLEQEMAKEDPVcAPESMGSEDM------ 245
Cdd:TIGR01217 189 LLFTVDGYRYNGKEHDRRDKVAEVRKELPTLRAVVH--------------IPYLGPRETEAPK-IDGALDLEDFtaaaqa 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 246 -------------LFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITgHSYVVYGpLCNGA 312
Cdd:TIGR01217 254 aelvfeqlpfdhpLWILFSSGTTGLPKCIVHSAGGTLVQHLKEHGLHCDLGPGDRLFYYTTTGWMM-WNWLVSG-LATGA 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 313 TSVLFESTPVYPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHrvvgds 392
Cdd:TIGR01217 332 TLVLYDGSPGFPATNVLWDIAERTGATLFGTSAKYVMACRKAGVHPARTHDLSALQCVASTGSPLPPDGFRWVY------ 405
|
410
....*....|....*
gi 91993047 393 RCTLVDTWWQTETGG 407
Cdd:TIGR01217 406 DEIKADVWLASISGG 420
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
94-450 |
1.27e-36 |
|
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: 140.43 E-value: 1.27e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 94 TEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVV 173
Cdd:cd05911 7 TGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 174 ITFNQGLrggrvvelkKIVDEAVKHCPTVQHV-LVAHRTDNKVHMGDLDVPLEQEMAKEDPVCAPEsmGSEDMLFMLYTS 252
Cdd:cd05911 87 FTDPDGL---------EKVKEAAKELGPKDKIiVLDDKPDGVLSIEDLLSPTLGEEDEDLPPPLKD--GKDDTAAILYSS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 253 GSTGMPKGivhtqagyllyAALTHK-LVFDH-----------QPGDIFGCVADIGWITGHSYVVYGPLCnGATSVLFESt 320
Cdd:cd05911 156 GTTGLPKG-----------VCLSHRnLIANLsqvqtflygndGSNDVILGFLPLYHIYGLFTTLASLLN-GATVIIMPK- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 321 pvyPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDawVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVgdSRCTLVDTW 400
Cdd:cd05911 223 ---FDSELFLDLIEKYKITFLYLVPPIAAALAKSPL--LDKYDLSSLRVILSGGAPLSKELQELLAKRF--PNATIKQGY 295
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 91993047 401 WQTETGGICIAPRPSEEGAE----ILPAMAMRpffgivpvLMDEKGSVVEGCNV 450
Cdd:cd05911 296 GMTETGGILTVNPDGDDKPGsvgrLLPNVEAK--------IVDDDGKDSLGPNE 341
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
98-447 |
2.44e-35 |
|
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: 136.11 E-value: 2.44e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 98 ITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITfn 177
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 178 qglrggrvvelkkivDEAVKHcptvqhvlvahrtdnkvhmgDLDvpleqemakedpvcapesmgsEDMLFMLYTSGSTGM 257
Cdd:cd05973 79 ---------------DAANRH--------------------KLD---------------------SDPFVMMFTSGTTGL 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 258 PKGIVHTQAGYLLYAALTHKLVfDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPVYPNAgryWETVERLK 337
Cdd:cd05973 103 PKGVPVPLRALAAFGAYLRDAV-DLRPEDSFWNAADPGWAYGLYYAITGPLALGHPTILLEGGFSVEST---WRVIERLG 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 338 INQFYGAPTAVRLLLKYGDAwVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGdsrCTLVDTWWQTETgGICIA-----P 412
Cdd:cd05973 179 VTNLAGSPTAYRLLMAAGAE-VPARPKGRLRRVSSAGEPLTPEVIRWFDAALG---VPIHDHYGQTEL-GMVLAnhhalE 253
|
330 340 350
....*....|....*....|....*....|....*
gi 91993047 413 RPSEEGAEILPAMAMRpffgiVPVLMDEKGSVVEG 447
Cdd:cd05973 254 HPVHAGSAGRAMPGWR-----VAVLDDDGDELGPG 283
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
244-447 |
1.04e-34 |
|
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: 132.02 E-value: 1.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 244 DMLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHqPGDIFGCVADIGWItGHSYVVYGPLCNGATSVLFEStpvy 323
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLT-EGDVFLSTLPLFHI-GGLFGLLGALLAGGTVVLLPK---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 324 PNAGRYWETVERLKINQFYGAPTAVRLLLKYGDawVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGdsrCTLVDTWWQT 403
Cdd:cd04433 75 FDPEAALELIEREKVTILLGVPTLLARLLKAPE--SAGYDLSSLRALVSGGAPLPPELLERFEEAPG---IKLVNGYGLT 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 91993047 404 ETGGICIAPRPSEEgaEILPAMAMRPFFGIVPVLMDEKGSVVEG 447
Cdd:cd04433 150 ETGGTVATGPPDDD--ARKPGSVGRPVPGVEVRIVDPDGGELPP 191
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
97-447 |
4.39e-34 |
|
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: 133.65 E-value: 4.39e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 97 RITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVitf 176
Cdd:cd05959 29 SLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVV--- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 177 nqglrggrVVE---LKKIVDEAVKHCPTVQHVLVAhrtdnKVHMGDLDVP-LEQEMAKEDPVCAPESMGSEDMLFMLYTS 252
Cdd:cd05959 106 --------VVSgelAPVLAAALTKSEHTLVVLIVS-----GGAGPEAGALlLAELVAAEAEQLKPAATHADDPAFWLYSS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 253 GSTGMPKGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFestPVYPNAGRYWET 332
Cdd:cd05959 173 GSTGRPKGVVHLHADIYWTAELYARNVLGIREDDVCFSAAKLFFAYGLGNSLTFPLSVGATTVLM---PERPTPAAVFKR 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 333 VERLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTLGSVGEPINCEAWE-WLHRVVgdsrCTLVDTWWQTETGGICIA 411
Cdd:cd05959 250 IRRYRPTVFFGVPTLYAAMLAAPNL--PSRDLSSLRLCVSAGEALPAEVGErWKARFG----LDILDGIGSTEMLHIFLS 323
|
330 340 350
....*....|....*....|....*....|....*.
gi 91993047 412 PRPSeegaEILPAMAMRPFFGIVPVLMDEKGSVVEG 447
Cdd:cd05959 324 NRPG----RVRYGTTGKPVPGYEVELRDEDGGDVAD 355
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
64-445 |
4.79e-34 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 133.77 E-value: 4.79e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 64 QLNVSvNCLDQHVRKSPESVALIWERDepgtevRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACA 143
Cdd:PRK06187 5 PLTIG-RILRHGARKHPDKEAVYFDGR------RTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 144 RIGAV-HTV-IFagFSAESLAGRINDAKCKVVItFNQglrggrvvELKKIVDEAVKHCPTVQHVLVAHRTDNKVHmGDLD 221
Cdd:PRK06187 78 KIGAVlHPInIR--LKPEEIAYILNDAEDRVVL-VDS--------EFVPLLAAILPQLPTVRTVIVEGDGPAAPL-APEV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 222 VPLEQEMAKEDPVCAPESMGSEDMLFMLYTSGSTGMPKGIVHtqagyllyaalTHKLVFDHqpgdIFGCVADIGWITGHS 301
Cdd:PRK06187 146 GEYEELLAAASDTFDFPDIDENDAAAMLYTSGTTGHPKGVVL-----------SHRNLFLH----SLAVCAWLKLSRDDV 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 302 YVV-------------YGPLCNGATSVL---FESTPVypnagryWETVERLKINQFYGAPTAVRLLLKYGDAwvKKYDRS 365
Cdd:PRK06187 211 YLVivpmfhvhawglpYLALMAGAKQVIprrFDPENL-------LDLIETERVTFFFAVPTIWQMLLKAPRA--YFVDFS 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 366 SLRTLGSVGEPIN---CEAWEWLHrvvgdsRCTLVDTWWQTETGGICIAPRPSEEGAEILPAM--AMRPFFGIVPVLMDE 440
Cdd:PRK06187 282 SLRLVIYGGAALPpalLREFKEKF------GIDLVQGYGMTETSPVVSVLPPEDQLPGQWTKRrsAGRPLPGVEARIVDD 355
|
....*
gi 91993047 441 KGSVV 445
Cdd:PRK06187 356 DGDEL 360
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
66-446 |
6.06e-33 |
|
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: 130.69 E-value: 6.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 66 NVSVNCLDQHVRKSPESVALIWErDEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARI 145
Cdd:cd05970 17 NFAYDVVDAMAKEYPDKLALVWC-DDAGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 146 GAVHTVIFAGFSAESLAGRINDAKCKVVITFNQGlrggrvvELKKIVDEAVKHCPTVQhVLVahrtdnKVHMGDLD--VP 223
Cdd:cd05970 96 GAIAIPATHQLTAKDIVYRIESADIKMIVAIAED-------NIPEEIEKAAPECPSKP-KLV------WVGDPVPEgwID 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 224 LEQEMAKEDPV----CAPESMGSEDMLFMLYTSGSTGMPKGIVHTQAgYLLYAALTHKLVFDHQPGDIFGCVADIGWITG 299
Cdd:cd05970 162 FRKLIKNASPDferpTANSYPCGEDILLVYFSSGTTGMPKMVEHDFT-YPLGHIVTAKYWQNVREGGLHLTVADTGWGKA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 300 HSYVVYGPLCNGATSVLFESTPVYPNAgrYWETVERLKINQFYGAPTAVRLLLKygdAWVKKYDRSSLRTLGSVGEPINC 379
Cdd:cd05970 241 VWGKIYGQWIAGAAVFVYDYDKFDPKA--LLEKLSKYGVTTFCAPPTIYRFLIR---EDLSRYDLSSLRYCTTAGEALNP 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 91993047 380 EAWEWLHRVVGDSrctLVDTWWQTETgGICIAPRPseeGAEILPAMAMRPFFGIVPVLMDEKGSVVE 446
Cdd:cd05970 316 EVFNTFKEKTGIK---LMEGFGQTET-TLTIATFP---WMEPKPGSMGKPAPGYEIDLIDREGRSCE 375
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
80-445 |
6.49e-33 |
|
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: 129.18 E-value: 6.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 80 PESVALIWERDepgtevRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAE 159
Cdd:cd05930 1 PDAVAVVDGDQ------SLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 160 SLAGRINDAKCKVVITfnqglrggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemakedpvcapes 239
Cdd:cd05930 75 RLAYILEDSGAKLVLT---------------------------------------------------------------- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 240 mGSEDMLFMLYTSGSTGMPKGIVHTQAGyLLYAALTHKLVFDHQPGDIFGCVADIGWItGHSYVVYGPLCNGATSVLFES 319
Cdd:cd05930 91 -DPDDLAYVIYTSGSTGKPKGVMVEHRG-LVNLLLWMQEAYPLTPGDRVLQFTSFSFD-VSVWEIFGALLAGATLVVLPE 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 320 TPVYpNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWvkkyDRSSLRTLGSVGEPINCEAWEWLHRVVgdSRCTLVDT 399
Cdd:cd05930 168 EVRK-DPEALADLLAEEGITVLHLTPSLLRLLLQELELA----ALPSLRLVLVGGEALPPDLVRRWRELL--PGARLVNL 240
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 91993047 400 WWQTETGGICIAPRPSEEGAEILPAMAMRPFFGIVPVLMDEKGSVV 445
Cdd:cd05930 241 YGPTEATVDATYYRVPPDDEEDGRVPIGRPIPNTRVYVLDENLRPV 286
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
66-445 |
1.54e-32 |
|
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: 129.51 E-value: 1.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 66 NVSVNCLDQHVRKS-----PESVALIWERDEpGTEVRITYRELLETTCRLANTL-KRHGVHRGDRVAIYMPVSPLAVAAM 139
Cdd:cd05928 6 NFASDVLDQWADKEkagkrPPNPALWWVNGK-GDEVKWSFRELGSLSRKAANVLsGACGLQRGDRVAVILPRVPEWWLVN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 140 LACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFNqglrggrvvELKKIVDEAVKHCPTVQ-HVLVAHRTDNkvhmG 218
Cdd:cd05928 85 VACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSD---------ELAPEVDSVASECPSLKtKLLVSEKSRD----G 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 219 DLDVPLEQEMAKEDPVCApeSMGSEDMLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWIT 298
Cdd:cd05928 152 WLNFKELLNEASTEHHCV--ETGSQEPMAIYFTSGTTGSPKMAEHSHSSLGLGLKVNGRYWLDLTASDIMWNTSDTGWIK 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 299 GHSYVVYGPLCNGATsVLFESTPVYpNAGRYWETVERLKINQFYGAPTAVRLLLKYGdawVKKYDRSSLRTLGSVGEPIN 378
Cdd:cd05928 230 SAWSSLFEPWIQGAC-VFVHHLPRF-DPLVILKTLSSYPITTFCGAPTVYRMLVQQD---LSSYKFPSLQHCVTGGEPLN 304
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 91993047 379 CEAWE-WLHRVVGDsrctLVDTWWQTETGGICIAPRpseeGAEILPAMAMRPFFGIVPVLMDEKGSVV 445
Cdd:cd05928 305 PEVLEkWKAQTGLD----IYEGYGQTETGLICANFK----GMKIKPGSMGKASPPYDVQIIDDNGNVL 364
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
72-446 |
8.77e-32 |
|
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.
Pssm-ID: 341286 [Multi-domain] Cd Length: 435 Bit Score: 125.80 E-value: 8.77e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 72 LDQHVRKSPESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTV 151
Cdd:cd17631 1 LRRRARRHPDRTALVFG------GRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 152 IFAGFSAESLAGRINDAKCKVVItfnqglrggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemake 231
Cdd:cd17631 75 LNFRLTPPEVAYILADSGAKVLF--------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 232 dpvcapesmgsEDMLFMLYTSGSTGMPKGIVHTQaGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNG 311
Cdd:cd17631 98 -----------DDLALLMYTSGTTGRPKGAMLTH-RNLLWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRG 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 312 ATSVLFEStpvyPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTLGSVGEPinceAWEWLHRVVGD 391
Cdd:cd17631 166 GTVVILRK----FDPETVLDLIERHRVTSFFLVPTMIQALLQHPRF--ATTDLSSLRAVIYGGAP----MPERLLRALQA 235
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 91993047 392 SRCTLVDTWWQTETG-GICIAPRpseEGAEILPAMAMRPFFGIVPVLMDEKGSVVE 446
Cdd:cd17631 236 RGVKFVQGYGMTETSpGVTFLSP---EDHRRKLGSAGRPVFFVEVRIVDPDGREVP 288
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
14-385 |
2.41e-31 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 127.12 E-value: 2.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 14 SYPALSAQAAREPAAFWgplardTLVWDT---PYHT----VWDCDFSTGKIG-WFLGGQLNVSVNCLDQHVRKSPESVAL 85
Cdd:PLN03052 121 SFSEFQRFSVENPEVYW------SIVLDElslVFSVpprcILDTSDESNPGGqWLPGAVLNVAECCLTPKPSKTDDSIAI 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 86 IWeRDEPGTEV---RITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLA 162
Cdd:PLN03052 195 IW-RDEGSDDLpvnRMTLSELRSQVSRVANALDALGFEKGDAIAIDMPMNVHAVIIYLAIILAGCVVVSIADSFAPSEIA 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 163 GRINDAKCKVVITFNQGLRGGRVVELKKIVDEAvkHCPTVQhVLVAHRTDNKVHMGDLDVPLEQEMAKEDPVCAPES--- 239
Cdd:PLN03052 274 TRLKISKAKAIFTQDVIVRGGKSIPLYSRVVEA--KAPKAI-VLPADGKSVRVKLREGDMSWDDFLARANGLRRPDEyka 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 240 --MGSEDMLFMLYTSGSTGMPKGIVHTQAGYLLYAALT--HklvFDHQPGDIFGCVADIGWITGHsYVVYGPLCNGATSV 315
Cdd:PLN03052 351 veQPVEAFTNILFSSGTTGEPKAIPWTQLTPLRAAADAwaH---LDIRKGDIVCWPTNLGWMMGP-WLVYASLLNGATLA 426
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 91993047 316 LFESTPVYPNAGRYwetVERLKINQFYGAPTAVRlllkygdAW-----VKKYDRSSLRTLGSVGEPINCEAWEWL 385
Cdd:PLN03052 427 LYNGSPLGRGFAKF---VQDAKVTMLGTVPSIVK-------TWkntncMAGLDWSSIRCFGSTGEASSVDDYLWL 491
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
72-288 |
1.25e-30 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 124.44 E-value: 1.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 72 LDQHVRKSPESVALIWERDepGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTV 151
Cdd:COG1022 17 LRRRAARFPDRVALREKED--GIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 152 IFAGFSAESLAGRINDAKCKVVITFNQGLrggrvveLKKiVDEAVKHCPTVQHVLVAhrtDNKVHMGDLDV-PLEQEMAK 230
Cdd:COG1022 95 IYPTSSAEEVAYILNDSGAKVLFVEDQEQ-------LDK-LLEVRDELPSLRHIVVL---DPRGLRDDPRLlSLDELLAL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 91993047 231 EDPVCAPE-------SMGSEDMLFMLYTSGSTGMPKGIVHTQAGyLLYAALTHKLVFDHQPGDIF 288
Cdd:COG1022 164 GREVADPAelearraAVKPDDLATIIYTSGTTGRPKGVMLTHRN-LLSNARALLERLPLGPGDRT 227
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
98-446 |
5.56e-30 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 121.03 E-value: 5.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 98 ITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITfn 177
Cdd:cd05919 11 VTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVT-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 178 qglrggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemakedpvcapesmGSEDMLFMLYTSGSTGM 257
Cdd:cd05919 89 ---------------------------------------------------------------SADDIAYLLYSSGTTGP 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 258 PKGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADI--GWITGHSyvVYGPLCNGATSVLFestPVYPNAGRYWETVER 335
Cdd:cd05919 106 PKGVMHAHRDPLLFADAMAREALGLTPGDRVFSSAKMffGYGLGNS--LWFPLAVGASAVLN---PGWPTAERVLATLAR 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 336 LKINQFYGAPTAVRLLLKYGDawVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGdsrCTLVDTWWQTETGGICIAPRPS 415
Cdd:cd05919 181 FRPTVLYGVPTFYANLLDSCA--GSPDALRSLRLCVSAGEALPRGLGERWMEHFG---GPILDGIGATEVGHIFLSNRPG 255
|
330 340 350
....*....|....*....|....*....|.
gi 91993047 416 eegaEILPAMAMRPFFGIVPVLMDEKGSVVE 446
Cdd:cd05919 256 ----AWRLGSTGRPVPGYEIRLVDEEGHTIP 282
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
72-397 |
3.22e-28 |
|
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: 118.42 E-value: 3.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 72 LDQHVRKSPESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTV 151
Cdd:COG1020 482 FEAQAARTPDAVAVVFG------DQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVP 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 152 IFAGFSAESLAGRINDAKCKVVITfnqglrggrvvelkkivdeavkhcptvQHVLVAHRTDNKVHMGDLDVPLEQEMAKE 231
Cdd:COG1020 556 LDPAYPAERLAYMLEDAGARLVLT---------------------------QSALAARLPELGVPVLALDALALAAEPAT 608
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 232 DPVCAPesmGSEDMLFMLYTSGSTGMPKGIVHTQAGYL-LYAALTHKLVFDhqPGDIFGCVADIG-----WitghsyVVY 305
Cdd:COG1020 609 NPPVPV---TPDDLAYVIYTSGSTGRPKGVMVEHRALVnLLAWMQRRYGLG--PGDRVLQFASLSfdasvW------EIF 677
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 306 GPLCNGATSVLFESTPVyPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAwvkkyDRSSLRTLGSVGEPINCEAWEWL 385
Cdd:COG1020 678 GALLSGATLVLAPPEAR-RDPAALAELLARHRVTVLNLTPSLLRALLDAAPE-----ALPSLRLVLVGGEALPPELVRRW 751
|
330
....*....|..
gi 91993047 386 HRVVGDsrCTLV 397
Cdd:COG1020 752 RARLPG--ARLV 761
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
99-423 |
7.02e-26 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 108.89 E-value: 7.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 99 TYRELLETTCRLANTLK-RHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFN 177
Cdd:TIGR01733 1 TYRELDERANRLARHLRaAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 178 QglrggrvvelkkivdeavkHCPTVQHVLVAHrtdnkVHMGDLDVPLEQEMAKEDPVCAPEsmGSEDMLFMLYTSGSTGM 257
Cdd:TIGR01733 81 A-------------------LASRLAGLVLPV-----ILLDPLELAALDDAPAPPPPDAPS--GPDDLAYVIYTSGSTGR 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 258 PKGIVHTQAGyLLYAALTHKLVFDHQPGDIfgcvadigWITGHSYV-------VYGPLCNGATSVLFESTPVYPNAGRYW 330
Cdd:TIGR01733 135 PKGVVVTHRS-LVNLLAWLARRYGLDPDDR--------VLQFASLSfdasveeIFGALLAGATLVVPPEDEERDDAALLA 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 331 ETVERLKINQFYGAPTAVRLLLKygdawVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDSRctLVDTWWQTETGGICI 410
Cdd:TIGR01733 206 ALIAEHPVTVLNLTPSLLALLAA-----ALPPALASLRLVILGGEALTPALVDRWRARGPGAR--LINLYGPTETTVWST 278
|
330
....*....|....*.
gi 91993047 411 A---PRPSEEGAEILP 423
Cdd:TIGR01733 279 AtlvDPDDAPRESPVP 294
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
73-369 |
7.92e-26 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 109.78 E-value: 7.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 73 DQHVRKSPESVALIWerdePGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVI 152
Cdd:PRK13391 4 GIHAQTTPDKPAVIM----ASTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 153 FAGFSAESLAGRINDAKCKVVITFNQGLrggrvvelkKIVDEAVKHCPTVQHVLVAHRTdnkvhmGDLD--VPLEQEMAK 230
Cdd:PRK13391 80 NSHLTPAEAAYIVDDSGARALITSAAKL---------DVARALLKQCPGVRHRLVLDGD------GELEgfVGYAEAVAG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 231 --EDPVcAPESMGSEdmlfMLYTSGSTGMPKGIvhtqagyllYAALTHKLVfDHQPGDIFGCVADIGWITGHSYVVYGPL 308
Cdd:PRK13391 145 lpATPI-ADESLGTD----MLYSSGTTGRPKGI---------KRPLPEQPP-DTPLPLTAFLQRLWGFRSDMVYLSPAPL 209
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 91993047 309 --------CN-----GATSVLFESTpvypNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRT 369
Cdd:PRK13391 210 yhsapqraVMlvirlGGTVIVMEHF----DAEQYLALIEEYGVTHTQLVPTMFSRMLKLPEEVRDKYDLSSLEV 279
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
77-373 |
1.66e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 109.36 E-value: 1.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 77 RKSPESVALIWErdepGTEvrITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGF 156
Cdd:PRK06178 44 RERPQRPAIIFY----GHV--ITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 157 SAESLAGRINDAKCKVVITFNQglrggrvveLKKIVdEAVKHCPTVQHVLVAHRTDNKVHMGDLDVPLEQEMAKED---- 232
Cdd:PRK06178 118 REHELSYELNDAGAEVLLALDQ---------LAPVV-EQVRAETSLRHVIVTSLADVLPAEPTLPLPDSLRAPRLAaaga 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 233 ----------PVCAPESMGSEDMLFML-YTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHS 301
Cdd:PRK06178 188 idllpalracTAPVPLPPPALDALAALnYTGGTTGMPKGCEHTQRDMVYTAAAAYAVAVVGGEDSVFLSFLPEFWIAGEN 267
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 91993047 302 YVVYGPLCNGATSVLFESTpvypNAGRYWETVERLKINQFYGAPTAVRLLLKYGDawVKKYDRSSLRTLGSV 373
Cdd:PRK06178 268 FGLLFPLFSGATLVLLARW----DAVAFMAAVERYRVTRTVMLVDNAVELMDHPR--FAEYDLSSLRQVRVV 333
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
76-368 |
3.98e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 107.71 E-value: 3.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 76 VRKSPESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAG 155
Cdd:PRK08316 21 ARRYPDKTALVFG------DRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 156 FSAESLAGRINDAKCKVVITfNQGLRGgrvvelkkIVDEAVKHCPTVQHVLVAHRTDNKVHMGDLDVpleQEMAKEDPVC 235
Cdd:PRK08316 95 LTGEELAYILDHSGARAFLV-DPALAP--------TAEAALALLPVDTLILSLVLGGREAPGGWLDF---ADWAEAGSVA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 236 APE-SMGSEDMLFMLYTSGSTGMPKGIVHTqagyllYAALTHKLVfdhqpgdifGCVADIGWITG----------HS--- 301
Cdd:PRK08316 163 EPDvELADDDLAQILYTSGTESLPKGAMLT------HRALIAEYV---------SCIVAGDMSADdiplhalplyHCaql 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 91993047 302 YVVYGP-LCNGATSVLFEStpvyPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDawVKKYDRSSLR 368
Cdd:PRK08316 228 DVFLGPyLYVGATNVILDA----PDPELILRTIEAERITSFFAPPTVWISLLRHPD--FDTRDLSSLR 289
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
93-397 |
2.38e-24 |
|
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: 104.82 E-value: 2.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 93 GTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKV 172
Cdd:cd05971 2 GTPEKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 173 VITfnqglrggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemakeDpvcapesmGSEDMLFMLYTS 252
Cdd:cd05971 82 LVT--------------------------------------------------------D--------GSDDPALIIYTS 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 253 GSTGMPKGIVHTQA---GYLLYAALTHKLVfdHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPVYPnaGRY 329
Cdd:cd05971 98 GTTGPPKGALHAHRvllGHLPGVQFPFNLF--PRDGDLYWTPADWAWIGGLLDVLLPSLYFGVPVLAHRMTKFDP--KAA 173
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 91993047 330 WETVERLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTLGSVGEPINCEAWEW--------LHRVVGDSRCTLV 397
Cdd:cd05971 174 LDLMSRYGVTTAFLPPTALKMMRQQGEQ--LKHAQVKLRAIATGGESLGEELLGWareqfgveVNEFYGQTECNLV 247
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
73-316 |
1.03e-23 |
|
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: 103.43 E-value: 1.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 73 DQHVRKSPESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVI 152
Cdd:cd12117 4 EEQAARTPDAVAVVYG------DRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 153 FAGFSAESLAGRINDAKCKVVITfnQGLRGGRVVELKKIVdeavkhcptvqhvlvahrtdnkvhmgDLDVPLEQEMAKED 232
Cdd:cd12117 78 DPELPAERLAFMLADAGAKVLLT--DRSLAGRAGGLEVAV--------------------------VIDEALDAGPAGNP 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 233 PVCApesmGSEDMLFMLYTSGSTGMPKGIVHTQAGYLlyaalthKLVFDH-----QPGDIFGCVADIGWiTGHSYVVYGP 307
Cdd:cd12117 130 AVPV----SPDDLAYVMYTSGSTGRPKGVAVTHRGVV-------RLVKNTnyvtlGPDDRVLQTSPLAF-DASTFEIWGA 197
|
....*....
gi 91993047 308 LCNGATSVL 316
Cdd:cd12117 198 LLNGARLVL 206
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
97-414 |
1.74e-23 |
|
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: 102.99 E-value: 1.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 97 RITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITF 176
Cdd:TIGR02262 30 SLSYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLGAIRAGIVPVALNTLLTADDYAYMLEDSRARVVFVS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 177 NqglrggrvvELKKIVDEAVKHCPTVQHVLVAHRTDNkvhmGDLDvpLEQEMAKEDPVCAPESMGSEDMLFMLYTSGSTG 256
Cdd:TIGR02262 110 G---------ALLPVIKAALGKSPHLEHRVVVGRPEA----GEVQ--LAELLATESEQFKPAATQADDPAFWLYSSGSTG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 257 MPKGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFestPVYPNAGRYWETVERL 336
Cdd:TIGR02262 175 MPKGVVHTHSNPYWTAELYARNTLGIREDDVCFSAAKLFFAYGLGNALTFPMSVGATTVLM---GERPTPDAVFDRLRRH 251
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 91993047 337 KINQFYGAPTAVRLLLkyGDAWVKKYDRSSLRTLGSVGEPINCE-AWEWLHRVVGDsrctLVDTWWQTETGGICIAPRP 414
Cdd:TIGR02262 252 QPTIFYGVPTLYAAML--ADPNLPSEDQVRLRLCTSAGEALPAEvGQRWQARFGVD----IVDGIGSTEMLHIFLSNLP 324
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
72-370 |
5.15e-23 |
|
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: 101.38 E-value: 5.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 72 LDQHVRKSPESVALIwerdepGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVhtV 151
Cdd:COG1021 31 LRRRAERHPDRIAVV------DGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAI--P 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 152 IFAGFS-----AESLAGRInDAKCKVVITFNQGLRggrvveLKKIVDEAVKHCPTVQHVLVAHRTDNKVhmgDLDVPLEQ 226
Cdd:COG1021 103 VFALPAhrraeISHFAEQS-EAVAYIIPDRHRGFD------YRALARELQAEVPSLRHVLVVGDAGEFT---SLDALLAA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 227 EMAKEDPVCAPesmgsEDMLFMLYTSGSTGMPKGIVHTQAGYlLYAALTHKLVFDHQPGDIFGCVADIgwitGHSY---- 302
Cdd:COG1021 173 PADLSEPRPDP-----DDVAFFQLSGGTTGLPKLIPRTHDDY-LYSVRASAEICGLDADTVYLAALPA----AHNFplss 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 91993047 303 -VVYGPLCNGATSVLFEStpvyPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTL 370
Cdd:COG1021 243 pGVLGVLYAGGTVVLAPD----PSPDTAFPLIERERVTVTALVPPLALLWLDAAER--SRYDLSSLRVL 305
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
86-445 |
1.57e-22 |
|
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: 100.01 E-value: 1.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 86 IWERDEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAV-HTvIFAGFSAESLAGR 164
Cdd:cd12119 14 IVSRTHEGEVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVlHT-INPRLFPEQIAYI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 165 INDAKCKVVITFNqglrggrvvELKKIVDEAVKHCPTVQHVLVAhrTDNKVHMGDLDVPL---EQEMAKEDPVCAPESMG 241
Cdd:cd12119 93 INHAEDRVVFVDR---------DFLPLLEAIAPRLPTVEHVVVM--TDDAAMPEPAGVGVlayEELLAAESPEYDWPDFD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 242 SEDMLFMLYTSGSTGMPKGIVHTQAGYLLYA-ALTHKLVFDHQPGDIFGCVADI----GW-------ITGHSYVVYGPLC 309
Cdd:cd12119 162 ENTAAAICYTSGTTGNPKGVVYSHRSLVLHAmAALLTDGLGLSESDVVLPVVPMfhvnAWglpyaaaMVGAKLVLPGPYL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 310 NGATSVlfestpvypnagrywETVERLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTL---GSVGEPINCEAWEWLH 386
Cdd:cd12119 242 DPASLA---------------ELIEREGVTFAAGVPTVWQGLLDHLEA--NGRDLSSLRRVvigGSAVPRSLIEAFEERG 304
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 91993047 387 rvvgdsrctlVDT---WWQTETGGICIAPRP-------SEEGAEILPAMAMRPFFGIVPVLMDEKGSVV 445
Cdd:cd12119 305 ----------VRVihaWGMTETSPLGTVARPpsehsnlSEDEQLALRAKQGRPVPGVELRIVDDDGREL 363
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
80-446 |
3.88e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 98.80 E-value: 3.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 80 PESVALIWeRDEpgtevRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAE 159
Cdd:PRK07798 17 PDRVALVC-GDR-----RLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVED 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 160 SLAGRINDAKCKVVItFNQGLrGGRVVELKkivDEavkhCPTVQHVL-VAHRTDNKVHMGdlDVPLEQEMAKEDPVCAPE 238
Cdd:PRK07798 91 ELRYLLDDSDAVALV-YEREF-APRVAEVL---PR----LPKLRTLVvVEDGSGNDLLPG--AVDYEDALAAGSPERDFG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 239 SmGSEDMLFMLYTSGSTGMPKGIVHTQAGylLYAALTHKLVFDH--QPGDIFGCVADIGWITGHSYVVYGPLCNGAT--- 313
Cdd:PRK07798 160 E-RSPDDLYLLYTGGTTGMPKGVMWRQED--IFRVLLGGRDFATgePIEDEEELAKRAAAGPGMRRFPAPPLMHGAGqwa 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 314 ---------SVLFESTPVYpNAGRYWETVERLKINqfygaptavrLLLKYGDAWVK----------KYDRSSLRTLGSVG 374
Cdd:PRK07798 237 afaalfsgqTVVLLPDVRF-DADEVWRTIEREKVN----------VITIVGDAMARplldaleargPYDLSSLFAIASGG 305
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 91993047 375 EPINCEAWEWLHRVVGDSrcTLVDTWWQTETG--GICIAPRPSEEGAeilpamamRPFFGIVP--VLMDEKGSVVE 446
Cdd:PRK07798 306 ALFSPSVKEALLELLPNV--VLTDSIGSSETGfgGSGTVAKGAVHTG--------GPRFTIGPrtVVLDEDGNPVE 371
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
74-405 |
5.02e-22 |
|
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: 98.18 E-value: 5.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 74 QHVRKSPESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIF 153
Cdd:cd17651 3 RQAARTPDAPALVAE------GRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 154 AGFSAESLAGRINDAKCKVVITfnqglrggrvvelkkivdeavkhcptvqHVLVAHRTDNKVHMGDLDVPLEQEMAKEDP 233
Cdd:cd17651 77 PAYPAERLAFMLADAGPVLVLT----------------------------HPALAGELAVELVAVTLLDQPGAAAGADAE 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 234 VCAPESMGseDMLFMLYTSGSTGMPKGIV--HTQAGYLLYAaltHKLVFDHQPGDIFGCVADIGWITGHSYvVYGPLCNG 311
Cdd:cd17651 129 PDPALDAD--DLAYVIYTSGSTGRPKGVVmpHRSLANLVAW---QARASSLGPGARTLQFAGLGFDVSVQE-IFSTLCAG 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 312 ATSVLfESTPVYPNAGRYWETVERLKINQFYGAPTAVRLLLKygDAWVKKYDRSSLRTLGSVGEPINCEAW--EWLHRVV 389
Cdd:cd17651 203 ATLVL-PPEEVRTDPPALAAWLDEQRISRVFLPTVALRALAE--HGRPLGVRLAALRYLLTGGEQLVLTEDlrEFCAGLP 279
|
330
....*....|....*.
gi 91993047 390 GdsrCTLVDTWWQTET 405
Cdd:cd17651 280 G---LRLHNHYGPTET 292
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
72-405 |
5.30e-22 |
|
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: 98.02 E-value: 5.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 72 LDQHVRKSPESVALIWerdepgTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTV 151
Cdd:cd05936 5 LEEAARRFPDKTALIF------MGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 152 IFAGFSAESLAGRINDAKCKVVI---TFNQGLRGGRVVELKKIVDEavkhcptvqhvlvahrtdnkvhmgdldvpleqem 228
Cdd:cd05936 79 LNPLYTPRELEHILNDSGAKALIvavSFTDLLAAGAPLGERVALTP---------------------------------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 229 akedpvcapesmgsEDMLFMLYTSGSTGMPKGIVHTQaGYLLYAALTHK--LVFDHQPGDIFGCVADIGWITGHSYVVYG 306
Cdd:cd05936 125 --------------EDVAVLQYTSGTTGVPKGAMLTH-RNLVANALQIKawLEDLLEGDDVVLAALPLFHVFGLTVALLL 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 307 PLCNGATSVLFEStpvyPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDawVKKYDRSSLRTLGSVGEPINCEAWEWLH 386
Cdd:cd05936 190 PLALGATIVLIPR----FRPIGVLKEIRKHRVTIFPGVPTMYIALLNAPE--FKKRDFSSLRLCISGGAPLPVEVAERFE 263
|
330
....*....|....*....
gi 91993047 387 RVVGdsrCTLVDTWWQTET 405
Cdd:cd05936 264 ELTG---VPIVEGYGLTET 279
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
129-393 |
6.74e-22 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 97.96 E-value: 6.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 129 MPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFNQGLRGGRVVELKKIVDEAVKHCPTV-----Q 203
Cdd:PLN03051 1 MPMTVDAVIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFTQDVVLRGGRALPLYSKVVEAAPAKAIVlpaagE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 204 HVLVAHRTDNKVHMGDLDVPLEQEMAKEDPVcAPESMGSEDMLFMLYTSGSTGMPKGIVHTQAGyLLYAALTHKLVFDHQ 283
Cdd:PLN03051 81 PVAVPLREQDLSWCDFLGVAAAQGSVGGNEY-SPVYAPVESVTNILFSSGTTGEPKAIPWTHLS-PLRCASDGWAHMDIQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 284 PGDIFGCVADIGWITGhSYVVYGPLCNGATSVLFESTPVYPNAGRYwetVERLKINQFYGAPTAVRLLLKYGDAWVKKYD 363
Cdd:PLN03051 159 PGDVVCWPTNLGWMMG-PWLLYSAFLNGATLALYGGAPLGRGFGKF---VQDAGVTVLGLVPSIVKAWRHTGAFAMEGLD 234
|
250 260 270
....*....|....*....|....*....|
gi 91993047 364 RSSLRTLGSVGEPINCEAWEWLHRVVGDSR 393
Cdd:PLN03051 235 WSKLRVFASTGEASAVDDVLWLSSVRGYYK 264
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
97-377 |
7.97e-22 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 98.11 E-value: 7.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 97 RITYRELLETTCRLANTLKRH-GVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVIT 175
Cdd:PRK08314 35 AISYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGARVAIV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 176 fnqglrggrVVELKKIVDEAVKHCPtVQHVLVAHRTDN-KVHMGD-----LDVPLEQEMAKEDPVCA------------P 237
Cdd:PRK08314 115 ---------GSELAPKVAPAVGNLR-LRHVIVAQYSDYlPAEPEIavpawLRAEPPLQALAPGGVVAwkealaaglappP 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 238 ESMGSEDMLFMLYTSGSTGMPKGIVHTQaGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLF 317
Cdd:PRK08314 185 HTAGPDDLAVLPYTSGTTGVPKGCMHTH-RTVMANAVGSVLWSNSTPESVVLAVLPLFHVTGMVHSMNAPIYAGATVVLM 263
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 91993047 318 -----EStpvypnAGRyweTVERLKINQFYGAPTAVRLLLkyGDAWVKKYDRSSLRTLGSVGEPI 377
Cdd:PRK08314 264 prwdrEA------AAR---LIERYRVTHWTNIPTMVVDFL--ASPGLAERDLSSLRYIGGGGAAM 317
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
80-355 |
1.24e-21 |
|
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: 96.98 E-value: 1.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 80 PESVALiweRDEPGTevrITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAE 159
Cdd:cd12116 1 PDATAV---RDDDRS---LSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPAD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 160 SLAGRINDAKCKVVITfnqglrggrvvelkkivDEAvkhcptvqhvlvahrTDNKVHMGDLDVPLEQEMAKEDPVCAPES 239
Cdd:cd12116 75 RLRYILEDAEPALVLT-----------------DDA---------------LPDRLPAGLPVLLLALAAAAAAPAAPRTP 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 240 MGSEDMLFMLYTSGSTGMPKGIVHTQAGYL-LYAALTHKLVFdhQPGDIFGCVADIGW-ITGHSyvVYGPLCNGATSVLF 317
Cdd:cd12116 123 VSPDDLAYVIYTSGSTGRPKGVVVSHRNLVnFLHSMRERLGL--GPGDRLLAVTTYAFdISLLE--LLLPLLAGARVVIA 198
|
250 260 270
....*....|....*....|....*....|....*...
gi 91993047 318 ESTPVYpNAGRYWETVERLKINQFYGAPTAVRLLLKYG 355
Cdd:cd12116 199 PRETQR-DPEALARLIEAHSITVMQATPATWRMLLDAG 235
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
76-446 |
3.41e-21 |
|
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341267 [Multi-domain] Cd Length: 449 Bit Score: 95.39 E-value: 3.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 76 VRKSPESVALIWERDepgtevRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAG 155
Cdd:cd05945 1 AAANPDRPAVVEGGR------TLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDAS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 156 FSAESLAGRINDAKCKVVITFnqglrggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmGDldvpleqemakedpvc 235
Cdd:cd05945 75 SPAERIREILDAAKPALLIAD-----------------------------------------GD---------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 236 apesmgseDMLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLvFDHQPGDIFGCVADIgwitghS-----YVVYGPLCN 310
Cdd:cd05945 98 --------DNAYIIFTSGSTGRPKGVQISHDNLVSFTNWMLSD-FPLGPGDVFLNQAPF------SfdlsvMDLYPALAS 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 311 GATSVLFESTpVYPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDrsSLRTLGSVGEPINCEAWEWLHRVVG 390
Cdd:cd05945 163 GATLVPVPRD-ATADPKQLFRFLAEHGITVWVSTPSFAAMCLLSPTFTPESLP--SLRHFLFCGEVLPHKTARALQQRFP 239
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 91993047 391 DSRctLVDTWWQTETGGICIAPRPSEE---GAEILPamAMRPFFGIVPVLMDEKGSVVE 446
Cdd:cd05945 240 DAR--IYNTYGPTEATVAVTYIEVTPEvldGYDRLP--IGYAKPGAKLVILDEDGRPVP 294
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
72-266 |
6.33e-21 |
|
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: 95.23 E-value: 6.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 72 LDQHVRKSPESVALIWerdepgTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTV 151
Cdd:TIGR03098 6 LEDAAARLPDATALVH------HDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 152 IFAGFSAESLAGRINDAKCKVVITFNQGLRggrvvelkkIVDEAVKHCPTVQHVLvahRTDNKVHMGDLDVPLE----QE 227
Cdd:TIGR03098 80 INPLLKAEQVAHILADCNVRLLVTSSERLD---------LLHPALPGCHDLRTLI---IVGDPAHASEGHPGEEpaswPK 147
|
170 180 190
....*....|....*....|....*....|....*....
gi 91993047 228 MAKEDPVCAPESMGSEDMLFMLYTSGSTGMPKGIVHTQA 266
Cdd:TIGR03098 148 LLALGDADPPHPVIDSDMAAILYTSGSTGRPKGVVLSHR 186
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
72-406 |
1.05e-20 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 94.73 E-value: 1.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 72 LDQHVRKSPESVALIWERDEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTV 151
Cdd:PRK13295 30 LDACVASCPDKTAVTAVRLGTGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNP 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 152 IFAGFSAESLAGRINDAKCKVVI---TFnqglrggRVVELKKIVDEAVKHCPTVQHVLVAHRTDNKVHMGDLDVPLEQEM 228
Cdd:PRK13295 110 LMPIFRERELSFMLKHAESKVLVvpkTF-------RGFDHAAMARRLRPELPALRHVVVVGGDGADSFEALLITPAWEQE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 229 AKEDPVCAPESMGSEDMLFMLYTSGSTGMPKGIVHTQ----AGYLLYAALthklvFDHQPGDIFGCVADIGWITGHSYVV 304
Cdd:PRK13295 183 PDAPAILARLRPGPDDVTQLIYTSGTTGEPKGVMHTAntlmANIVPYAER-----LGLGADDVILMASPMAHQTGFMYGL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 305 YGPLCNGATSVLFEStpvypnagryWETVERLKINQ-----FYGAPTAvrLLLKYGDAwVKK--YDRSSLRTLGSVGEPI 377
Cdd:PRK13295 258 MMPVMLGATAVLQDI----------WDPARAAELIRtegvtFTMASTP--FLTDLTRA-VKEsgRPVSSLRTFLCAGAPI 324
|
330 340
....*....|....*....|....*....
gi 91993047 378 NCEAWEWLHRVVGdsrCTLVDTWWQTETG 406
Cdd:PRK13295 325 PGALVERARAALG---AKIVSAWGMTENG 350
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
72-368 |
1.09e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 94.59 E-value: 1.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 72 LDQHVRKSPESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTV 151
Cdd:PRK07656 11 LARAARRFGDKEAYVFG------DQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 152 IFAGFSAESLAGRINDAKCKVVITFnQGLRGgrvvelkkiVDEAVKHC-PTVQHVlVAHRTDNKVHMGDLDVPLEQEMAK 230
Cdd:PRK07656 85 LNTRYTADEAAYILARGDAKALFVL-GLFLG---------VDYSATTRlPALEHV-VICETEEDDPHTEKMKTFTDFLAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 231 EDPVCAPESMGSEDMLFMLYTSGSTGMPKGIV--HTQAgYLLYAALTHKLvfDHQPGD----------IFGCVAdiGWIT 298
Cdd:PRK07656 154 GDPAERAPEVDPDDVADILFTSGTTGRPKGAMltHRQL-LSNAADWAEYL--GLTEGDrylaanpffhVFGYKA--GVNA 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 299 ghsyvvygPLCNGATsVLFEstPVYpNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLR 368
Cdd:PRK07656 229 --------PLMRGAT-ILPL--PVF-DPDEVFRLIETERITVLPGPPTMYNSLLQHPDR--SAEDLSSLR 284
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
96-369 |
1.17e-20 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 94.64 E-value: 1.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 96 VRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAgFSAESLAGRINDAKCKVVIT 175
Cdd:PRK07529 57 ETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAGIANPINPL-LEPEQIAELLRAAGAKVLVT 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 176 fnqgLRGGRVVELKKIVDEAVKHCPTVQHVLVAHRTD--------------NKVHMGDLDvpLEQEMAKE--DPVCAPES 239
Cdd:PRK07529 136 ----LGPFPGTDIWQKVAEVLAALPELRTVVEVDLARylpgpkrlavplirRKAHARILD--FDAELARQpgDRLFSGRP 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 240 MGSEDMLFMLYTSGSTGMPKGIVHTQAGyLLYAALTHKLVFDHQPGD----------IFGCVAdigwitghsyVVYGPLC 309
Cdd:PRK07529 210 IGPDDVAAYFHTGGTTGMPKLAQHTHGN-EVANAWLGALLLGLGPGDtvfcglplfhVNALLV----------TGLAPLA 278
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 91993047 310 NGATSVLfeSTPV-YPNAG---RYWETVERLKINQFYGAPTAVRLLLkygDAWVKKYDRSSLRT 369
Cdd:PRK07529 279 RGAHVVL--ATPQgYRGPGviaNFWKIVERYRINFLSGVPTVYAALL---QVPVDGHDISSLRY 337
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
72-273 |
1.26e-20 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 94.56 E-value: 1.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 72 LDQHVRKSPESVALIWERDepgtevRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTV 151
Cdd:PRK08279 43 FEEAAARHPDRPALLFEDQ------SISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVAL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 152 IFAGFSAESLAGRINDAKCKVVITfnqglrGGRVVELkkiVDEAVKHCPTVQHVLVAHRTDNKVHMGDLDVpleQEMAKE 231
Cdd:PRK08279 117 LNTQQRGAVLAHSLNLVDAKHLIV------GEELVEA---FEEARADLARPPRLWVAGGDTLDDPEGYEDL---AAAAAG 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 91993047 232 DPVCAPESMGS---EDMLFMLYTSGSTGMPKGIVHTQAGYLLYAA 273
Cdd:PRK08279 185 APTTNPASRSGvtaKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMG 229
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
74-380 |
1.49e-20 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 94.23 E-value: 1.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 74 QHVRKSPESVALIWERDEPGTEVRITYRELLETTCRLANTLKRHGVhRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIF 153
Cdd:cd05931 1 RRAAARPDRPAYTFLDDEGGREETLTYAELDRRARAIAARLQAVGK-PGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 154 A---GFSAESLAGRINDAKCKVVITfnqglrggrVVELKKIVDEAVKHCPTVQHVLVAHrTDNKvhmgDLDVPleqemak 230
Cdd:cd05931 80 PptpGRHAERLAAILADAGPRVVLT---------TAAALAAVRAFAASRPAAGTPRLLV-VDLL----PDTSA------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 231 eDPVCAPeSMGSEDMLFMLYTSGSTGMPKGIVHTQAGyLLYAALTHKLVFDHQPGDIFG----CVADIGWITGhsyvVYG 306
Cdd:cd05931 139 -ADWPPP-SPDPDDIAYLQYTSGSTGTPKGVVVTHRN-LLANVRQIRRAYGLDPGDVVVswlpLYHDMGLIGG----LLT 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 307 PLCNGATSVLFEstpvyPNA-----GRYWETVERLKInQFYGAPT-AVRLLLKYG-DAWVKKYDRSSLRTLGSVGEPINC 379
Cdd:cd05931 212 PLYSGGPSVLMS-----PAAflrrpLRWLRLISRYRA-TISAAPNfAYDLCVRRVrDEDLEGLDLSSWRVALNGAEPVRP 285
|
.
gi 91993047 380 E 380
Cdd:cd05931 286 A 286
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
80-377 |
2.06e-20 |
|
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: 93.45 E-value: 2.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 80 PESVALIwerdEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAE 159
Cdd:cd05904 19 PSRPALI----DAATGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 160 SLAGRINDAKCKVVITFNQG---LRGG--RVVelkkIVDEAVKHCptvqhvlvAHRTDNKVHMGDLDVPleQEMAKEDPV 234
Cdd:cd05904 95 EIAKQVKDSGAKLAFTTAELaekLASLalPVV----LLDSAEFDS--------LSFSDLLFEADEAEPP--VVVIKQDDV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 235 CApesmgsedmlfMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLV-FDHQPGDIFGCVADIGWITGHSYVVYGPLCNGAT 313
Cdd:cd05904 161 AA-----------LLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEgSNSDSEDVFLCVLPMFHIYGLSSFALGLLRLGAT 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 91993047 314 SVlfestpVYP--NAGRYWETVERLKINQFYGAPTAVRLLLKygDAWVKKYDRSSLRTLGSVGEPI 377
Cdd:cd05904 230 VV------VMPrfDLEELLAAIERYKVTHLPVVPPIVLALVK--SPIVDKYDLSSLRQIMSGAAPL 287
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
72-371 |
3.05e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 90.19 E-value: 3.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 72 LDQHVRKSPESVALIwerDEPGTevrITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTV 151
Cdd:PRK06164 16 LDAHARARPDAVALI---DEDRP---LSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 152 IFAGFSAESLAGRINDAKCKVVItFNQGLRGGRVVELKKIVDEAVKhcPTVQHVLVAHRTDNKVH---MGDLDVPLEQEM 228
Cdd:PRK06164 90 VNTRYRSHEVAHILGRGRARWLV-VWPGFKGIDFAAILAAVPPDAL--PPLRAIAVVDDAADATPapaPGARVQLFALPD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 229 AKEDPVCAPESmGSEDMLFMLY-TSGSTGMPKGIVHTQAGYLLYAALTHKlVFDHQPGDIFGCVADIGWITGHSYVVyGP 307
Cdd:PRK06164 167 PAPPAAAGERA-ADPDAGALLFtTSGTTSGPKLVLHRQATLLRHARAIAR-AYGYDPGAVLLAALPFCGVFGFSTLL-GA 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 91993047 308 LCNGATSVLFestPVYpNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAwvkKYDRSSLRTLG 371
Cdd:PRK06164 244 LAGGAPLVCE---PVF-DAARTARALRRHRVTHTFGNDEMLRRILDTAGE---RADFPSARLFG 300
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
77-421 |
3.58e-18 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 86.88 E-value: 3.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 77 RKSPESVALI----WERDEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVI 152
Cdd:PRK09274 17 QERPDQLAVAvpggRGADGKLAYDELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAVPVLV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 153 FAGFSAESLAGRINDAKCKVVITFNQGLRGGRVVELKKivdEAVKHCPTVqhvlvahrtDNKVHMG--DLDvPLEQEMAK 230
Cdd:PRK09274 97 DPGMGIKNLKQCLAEAQPDAFIGIPKAHLARRLFGWGK---PSVRRLVTV---------GGRLLWGgtTLA-TLLRDGAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 231 EDPVCAPesMGSEDMLFMLYTSGSTGMPKGIVHTQAGYLlyAALTH-KLVFDHQPGDIfgcvaDIgwitgHSY---VVYG 306
Cdd:PRK09274 164 APFPMAD--LAPDDMAAILFTSGSTGTPKGVVYTHGMFE--AQIEAlREDYGIEPGEI-----DL-----PTFplfALFG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 307 PLCnGATSVLFESTPVYP---NAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYdrSSLRTLGSVGEPINCEAWE 383
Cdd:PRK09274 230 PAL-GMTSVIPDMDPTRPatvDPAKLFAAIERYGVTNLFGSPALLERLGRYGEANGIKL--PSLRRVISAGAPVPIAVIE 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 91993047 384 WLHRVVGD--------------------SRCTLVDTWWQTETG-GICIApRPSeEGAEI 421
Cdd:PRK09274 307 RFRAMLPPdaeiltpygatealpissieSREILFATRAATDNGaGICVG-RPV-DGVEV 363
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
93-368 |
4.33e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 86.50 E-value: 4.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 93 GTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKV 172
Cdd:PRK08276 7 PSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 173 VITfnqglrGGRVVELkkiVDEAVKHCPT-VQHVLVAHrtdnkvhmGDLD--VPLEQEMAKEDPV-CAPESMGSEdmlfM 248
Cdd:PRK08276 87 LIV------SAALADT---AAELAAELPAgVPLLLVVA--------GPVPgfRSYEEALAAQPDTpIADETAGAD----M 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 249 LYTSGSTGMPKGIVhtqagyllyAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGA-------------TSV 315
Cdd:PRK08276 146 LYSSGTTGRPKGIK---------RPLPGLDPDEAPGMMLALLGFGMYGGPDSVYLSPAPLYHTAplrfgmsalalggTVV 216
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 91993047 316 LFESTpvypNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLR 368
Cdd:PRK08276 217 VMEKF----DAEEALALIERYRVTHSQLVPTMFVRMLKLPEEVRARYDVSSLR 265
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
80-405 |
9.56e-18 |
|
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341298 [Multi-domain] Cd Length: 450 Bit Score: 85.05 E-value: 9.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 80 PESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAE 159
Cdd:cd17643 1 PEAVAVVDE------DRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 160 SLAGRINDAKCKVVITfnqglrggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemakeDPvcapes 239
Cdd:cd17643 75 RIAFILADSGPSLLLT--------------------------------------------------------DP------ 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 240 mgsEDMLFMLYTSGSTGMPKGIVHTQAGYL-LYAALTHKLVFDHQpgDIfgcvadigWITGHSYV-------VYGPLCNG 311
Cdd:cd17643 93 ---DDLAYVIYTSGSTGRPKGVVVSHANVLaLFAATQRWFGFNED--DV--------WTLFHSYAfdfsvweIWGALLHG 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 312 ATSVLFES----TPVypnagRYWETVERLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLR--TLGsvGEPINCEAWE-W 384
Cdd:cd17643 160 GRLVVVPYevarSPE-----DFARLLRDEGVTVLNQTPSAFYQLVEAADR--DGRDPLALRyvIFG--GEALEAAMLRpW 230
|
330 340
....*....|....*....|.
gi 91993047 385 LHRvVGDSRCTLVDTWWQTET 405
Cdd:cd17643 231 AGR-FGLDRPQLVNMYGITET 250
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
72-267 |
1.19e-17 |
|
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: 85.02 E-value: 1.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 72 LDQHVRKSPESVALIWERdepgteVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTV 151
Cdd:cd17646 4 VAEQAARTPDAPAVVDEG------RTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 152 IFAGFSAESLAGRINDAKCKVVITfNQGLRGGRVVELKKivdeavkhcPTVQHVLVAHRTDnkvhmgdldvpleqemAKE 231
Cdd:cd17646 78 LDPGYPADRLAYMLADAGPAVVLT-TADLAARLPAGGDV---------ALLGDEALAAPPA----------------TPP 131
|
170 180 190
....*....|....*....|....*....|....*.
gi 91993047 232 DPVCAPesmgsEDMLFMLYTSGSTGMPKGIVHTQAG 267
Cdd:cd17646 132 LVPPRP-----DNLAYVIYTSGSTGRPKGVMVTHAG 162
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
95-445 |
1.94e-17 |
|
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: 84.07 E-value: 1.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 95 EVRITYRELLETTCRLANTLKRHGVHR-GDRVAIYMPVSPLAVAAMLACARIGAVhtvifagfsaeslagrindakCKVV 173
Cdd:cd05958 8 EREWTYRDLLALANRIANVLVGELGIVpGNRVLLRGSNSPELVACWFGIQKAGAI---------------------AVAT 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 174 ITFnqgLRGGrvvELKKIVDEAvkhcpTVQHVLVAHRTdnkvhmgdldvpleqemakedpvcapesMGSEDMLFMLYTSG 253
Cdd:cd05958 67 MPL---LRPK---ELAYILDKA-----RITVALCAHAL----------------------------TASDDICILAFTSG 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 254 STGMPKGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTpvypNAGRYWETV 333
Cdd:cd05958 108 TTGAPKATMHFHRDPLASADRYAVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEA----TPDLLLSAI 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 334 ERLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGdsrCTLVDTWWQTETGGICIAPR 413
Cdd:cd05958 184 ARYKPTVLFTAPTAYRAMLAHPDA--AGPDLSSLRKCVSAGEALPAALHRAWKEATG---IPIIDGIGSTEMFHIFISAR 258
|
330 340 350
....*....|....*....|....*....|..
gi 91993047 414 PSeegaEILPAMAMRPFFGIVPVLMDEKGSVV 445
Cdd:cd05958 259 PG----DARPGATGKPVPGYEAKVVDDEGNPV 286
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
80-316 |
4.13e-17 |
|
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: 83.47 E-value: 4.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 80 PESVALIwerdepGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAE 159
Cdd:cd12114 1 PDATAVI------CGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 160 SLAGRINDAKCKVVITfnqglrggrvvelkkiVDEAVKHCPTVQHVLVahrtdnkvhmgDLDVPLEQEMAKEDPVCAPes 239
Cdd:cd12114 75 RREAILADAGARLVLT----------------DGPDAQLDVAVFDVLI-----------LDLDALAAPAPPPPVDVAP-- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 240 mgsEDMLFMLYTSGSTGMPKGIVHTQAGYL-LYAALTHKLVFDhqPGDIFGCVA----DIGwitghSYVVYGPLCNGATS 314
Cdd:cd12114 126 ---DDLAYVIFTSGSTGTPKGVMISHRAALnTILDINRRFAVG--PDDRVLALSslsfDLS-----VYDIFGALSAGATL 195
|
..
gi 91993047 315 VL 316
Cdd:cd12114 196 VL 197
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
97-288 |
4.36e-17 |
|
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: 83.24 E-value: 4.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 97 RITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITf 176
Cdd:cd05939 3 HWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALIF- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 177 nqglrggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgDLDVPLEQEMAKEDPVCAPesMGSEDMLFMLYTSGSTG 256
Cdd:cd05939 82 ------------------------------------------NLLDPLLTQSSTEPPSQDD--VNFRDKLFYIYTSGTTG 117
|
170 180 190
....*....|....*....|....*....|..
gi 91993047 257 MPKGIVHTQAGYLLYAALTHKlVFDHQPGDIF 288
Cdd:cd05939 118 LPKAAVIVHSRYYRIAAGAYY-AFGMRPEDVV 148
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
76-446 |
1.03e-16 |
|
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: 82.17 E-value: 1.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 76 VRKSPESVALIwerdEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAG 155
Cdd:cd05923 11 ASRAPDACAIA----DPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 156 FSAESLAGRI-NDAKCKVVITFNQG------LRGGRVVELKKIVdeavkhcptvqhvlvahrtdnkvhmgDLDVPLEQEM 228
Cdd:cd05923 87 LKAAELAELIeRGEMTAAVIAVDAQvmdaifQSGVRVLALSDLV--------------------------GLGEPESAGP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 229 AKEDPVCAPESMGsedmlFMLYTSGSTGMPKGIVHTQAgyllyAALTHKLVFDHQPGDIFGC------VADIGWITGHSY 302
Cdd:cd05923 141 LIEDPPREPEQPA-----FVFYTSGTTGLPKGAVIPQR-----AAESRVLFMSTQAGLRHGRhnvvlgLMPLYHVIGFFA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 303 VVYGPLCNGATSVLfestPVYPNAGRYWETVERLKINQFYGAPTAVRLLLkyGDAWVKKYDRSSLRTLGSVGEPINCEAW 382
Cdd:cd05923 211 VLVAALALDGTYVV----VEEFDPADALKLIEQERVTSLFATPTHLDALA--AAAEFAGLKLSSLRHVTFAGATMPDAVL 284
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 91993047 383 EWLHRVVGDSRctlVDTWWQTETGGICIAPRPSEEGaeilpamAMRPFFG----IVPVLmdekGSVVE 446
Cdd:cd05923 285 ERVNQHLPGEK---VNIYGTTEAMNSLYMRDARTGT-------EMRPGFFsevrIVRIG----GSPDE 338
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
74-377 |
1.68e-16 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 81.72 E-value: 1.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 74 QHVRKSPESVALIwerDEPGTevRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIF 153
Cdd:PRK06087 31 QTARAMPDKIAVV---DNHGA--SYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 154 AGFSAESLAGRINDAKCKVVIT---FNQGLRGGRVVELKKIVdeavkhcPTVQHVLVAhrtdNKVHMGDLDVPLEQEMAK 230
Cdd:PRK06087 106 PSWREAELVWVLNKCQAKMFFAptlFKQTRPVDLILPLQNQL-------PQLQQIVGV----DKLAPATSSLSLSQIIAD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 231 EDPVCAPESMGSEDMLFMLYTSGSTGMPKGIVHTQAGYLL----YAALTHkLVFDhqpgDIFGCVADIGWITGHSYVVYG 306
Cdd:PRK06087 175 YEPLTTAITTHGDELAAVLFTSGTEGLPKGVMLTHNNILAseraYCARLN-LTWQ----DVFMMPAPLGHATGFLHGVTA 249
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 91993047 307 PLCNGATSVLFESTpvypNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTLGSVGEPI 377
Cdd:PRK06087 250 PFLIGARSVLLDIF----TPDACLALLEQQRCTCMLGATPFIYDLLNLLEK--QPADLSALRFFLCGGTTI 314
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
80-353 |
7.21e-16 |
|
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: 79.66 E-value: 7.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 80 PESVALIwerdEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAE 159
Cdd:cd05926 1 PDAPALV----VPGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 160 SLAGRINDAKCKVVITFNQGL---------RGGRVVELKkiVDEAVKHCPTVQHVLVAHRTDNKVhmgdldvpleqemAK 230
Cdd:cd05926 77 EFEFYLADLGSKLVLTPKGELgpasraaskLGLAILELA--LDVGVLIRAPSAESLSNLLADKKN-------------AK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 231 EDPVCAPesmgsEDMLFMLYTSGSTGMPKGIVHTQAGYLL---YAALTHKLvfdhQPGDIFGCVADIGWITGHSYVVYGP 307
Cdd:cd05926 142 SEGVPLP-----DDLALILHTSGTTGRPKGVPLTHRNLAAsatNITNTYKL----TPDDRTLVVMPLFHVHGLVASLLST 212
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 91993047 308 LCNGATSVLfestPVYPNAGRYWETVERLKINQFYGAPTAVRLLLK 353
Cdd:cd05926 213 LAAGGSVVL----PPRFSASTFWPDVRDYNATWYTAVPTIHQILLN 254
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
99-377 |
1.59e-15 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 78.48 E-value: 1.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 99 TYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITfnq 178
Cdd:PLN02246 52 TYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLIIT--- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 179 glrGGRVVElkKIVDEAvkHCPTVQHVLVAHRTDNKVHMGDLDVPLEQEMAK-----EDPVCAPesmgsedmlfmlYTSG 253
Cdd:PLN02246 129 ---QSCYVD--KLKGLA--EDDGVTVVTIDDPPEGCLHFSELTQADENELPEveispDDVVALP------------YSSG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 254 STGMPKGIVhtqagyllyaaLTHK-LV-------------FDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVL--- 316
Cdd:PLN02246 190 TTGLPKGVM-----------LTHKgLVtsvaqqvdgenpnLYFHSDDVILCVLPMFHIYSLNSVLLCGLRVGAAILImpk 258
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 91993047 317 FEstpvypnAGRYWETVERLKINQFYGAPTAVRLLLKYGDawVKKYDRSSLRTLGSVGEPI 377
Cdd:PLN02246 259 FE-------IGALLELIQRHKVTIAPFVPPIVLAIAKSPV--VEKYDLSSIRMVLSGAAPL 310
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
97-414 |
1.90e-15 |
|
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: 78.10 E-value: 1.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 97 RITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITf 176
Cdd:cd05934 3 RWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 177 nqglrggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemakeDPVCapesmgsedmlfMLYTSGSTG 256
Cdd:cd05934 82 -------------------------------------------------------DPAS------------ILYTSGTTG 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 257 MPKGIVHTQAgYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTpvypNAGRYWETVERL 336
Cdd:cd05934 95 PPKGVVITHA-NLTFAGYYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLPRF----SASRFWSDVRRY 169
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 91993047 337 KINQFYGAPTAVRLLLKygdAWVKKYDRSS-LRTLGsvGEPINCEAWEWLHRVVGdsrCTLVDTWWQTETGGICIAPRP 414
Cdd:cd05934 170 GATVTNYLGAMLSYLLA---QPPSPDDRAHrLRAAY--GAPNPPELHEEFEERFG---VRLLEGYGMTETIVGVIGPRD 240
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
72-405 |
2.24e-15 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 78.28 E-value: 2.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 72 LDQHVRKSPESVALIWERDEpgteVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTV 151
Cdd:PRK12583 24 FDATVARFPDREALVVRHQA----LRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 152 IFAGFSAESLAGRINDAKCKVVITFNqGLRGGRVVElkkIVDEAVKHCPTVQHVLVAH----RTDNKVHMGDLDVP---L 224
Cdd:PRK12583 100 INPAYRASELEYALGQSGVRWVICAD-AFKTSDYHA---MLQELLPGLAEGQPGALACerlpELRGVVSLAPAPPPgflA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 225 EQEMAKEDPVCAPE-------SMGSEDMLFMLYTSGSTGMPKGivhtqagyllyAALTHKLVFDHqpgdifgcvadiGWI 297
Cdd:PRK12583 176 WHELQARGETVSREalaerqaSLDRDDPINIQYTSGTTGFPKG-----------ATLSHHNILNN------------GYF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 298 TGHS---------------YVVYGPLCNGATSVLFESTPVYPN----AGRYWETVERLKINQFYGAPTAVRLLLKYGDaw 358
Cdd:PRK12583 233 VAESlgltehdrlcvpvplYHCFGMVLANLGCMTVGACLVYPNeafdPLATLQAVEEERCTALYGVPTMFIAELDHPQ-- 310
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 91993047 359 VKKYDRSSLRTLGSVGEPinCEAwEWLHRVVGDSRCTLVD-TWWQTET 405
Cdd:PRK12583 311 RGNFDLSSLRTGIMAGAP--CPI-EVMRRVMDEMHMAEVQiAYGMTET 355
|
|
| ACAS_N |
pfam16177 |
Acetyl-coenzyme A synthetase N-terminus; This domain is found at the N-terminus of many ... |
15-71 |
2.53e-15 |
|
Acetyl-coenzyme A synthetase N-terminus; This domain is found at the N-terminus of many acetyl-coenzyme A synthetase enzymes.
Pssm-ID: 465043 [Multi-domain] Cd Length: 55 Bit Score: 69.81 E-value: 2.53e-15
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 91993047 15 YPALSAQAAREPAAFWGPLARDtLVWDTPYHTVWDCDFStGKIGWFLGGQLNVSVNC 71
Cdd:pfam16177 1 YEALYRRSIEDPEGFWGEVAKE-LDWFKPFDKVLDGSNG-PFAKWFVGGKLNVCYNC 55
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
98-320 |
2.57e-15 |
|
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: 77.64 E-value: 2.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 98 ITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITfn 177
Cdd:cd05907 6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFV-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 178 qglrggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemakEDPvcapesmgsEDMLFMLYTSGSTGM 257
Cdd:cd05907 84 -----------------------------------------------------EDP---------DDLATIIYTSGTTGR 101
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 91993047 258 PKGIVHTQAGyLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFEST 320
Cdd:cd05907 102 PKGVMLSHRN-ILSNALALAERLPATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFASSA 163
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
72-390 |
3.96e-15 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 77.62 E-value: 3.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 72 LDQHVRKSPESVALIWERDEpgteVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTV 151
Cdd:PRK05852 22 VEVAATRLPEAPALVVTADR----IAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 152 IFAGFSAESLAGRINDAKCKVVITFNQGLRGGRvvelkkivDEAVKHCPtvqhVLVAHRTDNKVHMGDLDVPLEQEMAKE 231
Cdd:PRK05852 98 LDPALPIAEQRVRSQAAGARVVLIDADGPHDRA--------EPTTRWWP----LTVNVGGDSGPSGGTLSVHLDAATEPT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 232 DPVCAPESMGSEDMLFMlYTSGSTGMPKGIVHTQAGyllYAALTHKLVFDHQPGDIFGCVADIGWITGHSYV--VYGPLC 309
Cdd:PRK05852 166 PATSTPEGLRPDDAMIM-FTGGTTGLPKMVPWTHAN---IASSVRAIITGYRLSPRDATVAVMPLYHGHGLIaaLLATLA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 310 NGATSVLfestpvyPNAGR-----YWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWEW 384
Cdd:PRK05852 242 SGGAVLL-------PARGRfsahtFWDDIKAVGATWYTAVPTIHQILLERAATEPSGRKPAALRFIRSCSAPLTAETAQA 314
|
....*.
gi 91993047 385 LHRVVG 390
Cdd:PRK05852 315 LQTEFA 320
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
97-419 |
4.46e-15 |
|
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: 77.04 E-value: 4.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 97 RITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITf 176
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 177 nqglrggrvvelkkivdeavkhcPTVqhvlvaHRTDNKVHMGDldvpleqemakedpvcapesmgseDMLFMLYTSGSTG 256
Cdd:cd05903 80 -----------------------PER------FRQFDPAAMPD------------------------AVALLLFTSGTTG 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 257 MPKGIVHTqAGYLLYA--ALTHKLVFDhqPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTpvypNAGRYWETVE 334
Cdd:cd05903 107 EPKGVMHS-HNTLSASirQYAERLGLG--PGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIW----DPDKALALMR 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 335 RLKINQFYGAPTAVRLLLKYgdawVKKYDR--SSLRTLGSVGEPINC----EAWEWLHRVVgdsrctlVDTWWQTETGGI 408
Cdd:cd05903 180 EHGVTFMMGATPFLTDLLNA----VEEAGEplSRLRTFVCGGATVPRslarRAAELLGAKV-------CSAYGSTECPGA 248
|
330
....*....|.
gi 91993047 409 CIAPRPSEEGA 419
Cdd:cd05903 249 VTSITPAPEDR 259
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
98-447 |
1.12e-14 |
|
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: 75.68 E-value: 1.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 98 ITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINdakckvvitfn 177
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRVD----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 178 qglRGGRVVelkKIVDEAVKhcptvqhvlvahrtdnkvhmgdldvpleqemakedpvcapesmgSEDMLFMLYTSGSTGM 257
Cdd:cd05974 70 ---RGGAVY---AAVDENTH--------------------------------------------ADDPMLLYFTSGTTSK 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 258 PKGIVHTQAGYLLyAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPVypNAGRYWETVERLK 337
Cdd:cd05974 100 PKLVEHTHRSYPV-GHLSTMYWIGLKPGDVHWNISSPGWAKHAWSCFFAPWNAGATVFLFNYARF--DAKRVLAALVRYG 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 338 INQFYGAPTAVRLLLKYGDAWVkkydRSSLRTLGSVGEPINCEAWEWLHRVVGdsrCTLVDTWWQTETGGIcIAPRPsee 417
Cdd:cd05974 177 VTTLCAPPTVWRMLIQQDLASF----DVKLREVVGAGEPLNPEVIEQVRRAWG---LTIRDGYGQTETTAL-VGNSP--- 245
|
330 340 350
....*....|....*....|....*....|.
gi 91993047 418 GAEILPAMAMRPFFGIVPVLMDEKGS-VVEG 447
Cdd:cd05974 246 GQPVKAGSMGRPLPGYRVALLDPDGApATEG 276
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
80-423 |
1.21e-14 |
|
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341304 [Multi-domain] Cd Length: 450 Bit Score: 75.48 E-value: 1.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 80 PESVALIWErDEpgtevRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAE 159
Cdd:cd17649 1 PDAVALVFG-DQ-----SLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 160 SLAGRINDAKCKVVITfnqglrggrvvelkkivdeavkhcptvQHvlvahrtdnkvhmgdldvpleqemakedpvcaPES 239
Cdd:cd17649 75 RLRYMLEDSGAGLLLT---------------------------HH--------------------------------PRQ 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 240 MGsedmlFMLYTSGSTGMPKGIVHTQagyllyAALTH-----KLVFDHQPGDIFGCVADIGWITGHSYvVYGPLCNGAtS 314
Cdd:cd17649 96 LA-----YVIYTSGSTGTPKGVAVSH------GPLAAhcqatAERYGLTPGDRELQFASFNFDGAHEQ-LLPPLICGA-C 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 315 VLFESTPVYPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAwVKKYDRSSLRTLGSVGEPINCE-AWEWLhrvvgDSR 393
Cdd:cd17649 163 VVLRPDELWASADELAEMVRELGVTVLDLPPAYLQQLAEEADR-TGDGRPPSLRLYIFGGEALSPElLRRWL-----KAP 236
|
330 340 350
....*....|....*....|....*....|...
gi 91993047 394 CTLVDTWWQTE---TGGICIAPRPSEEGAEILP 423
Cdd:cd17649 237 VRLFNAYGPTEatvTPLVWKCEAGAARAGASMP 269
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
78-287 |
1.31e-14 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 75.68 E-value: 1.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 78 KSPESVALiwerdEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFS 157
Cdd:PRK07514 14 ADRDAPFI-----ETPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 158 AESLAGRINDAKCKVVItfnqgLRGGRVVELKKIvdeAVKHcpTVQHV--LVAHRTDnkvhmgdldvPLEQEMAKEDPVC 235
Cdd:PRK07514 89 LAELDYFIGDAEPALVV-----CDPANFAWLSKI---AAAA--GAPHVetLDADGTG----------SLLEAAAAAPDDF 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 91993047 236 APESMGSEDMLFMLYTSGSTGMPKGIVHTQaGYLLYAALTHKLVFDHQPGDI 287
Cdd:PRK07514 149 ETVPRGADDLAAILYTSGTTGRSKGAMLSH-GNLLSNALTLVDYWRFTPDDV 199
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
72-405 |
2.87e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 74.68 E-value: 2.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 72 LDQHVRKSPESVALIWERDEpgtevrITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTV 151
Cdd:PRK06710 30 VEQMASRYPEKKALHFLGKD------ITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 152 IFAGFSAESLAGRINDAKCKVVITFNqgLRGGRVVELKK-------IVDEAVKHCPTVQHVL---VAHRTDNKV------ 215
Cdd:PRK06710 104 TNPLYTERELEYQLHDSGAKVILCLD--LVFPRVTNVQSatkiehvIVTRIADFLPFPKNLLypfVQKKQSNLVvkvses 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 216 HMGDLDVPLEQEM-AKEDPVCAPESmgseDMLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHQPGD--IFGcVA 292
Cdd:PRK06710 182 ETIHLWNSVEKEVnTGVEVPCDPEN----DLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYNCKEGEevVLG-VL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 293 DIGWITGHSYVVYGPLCNGATSVLFestPVYpNAGRYWETVERLKINQFYGAPTAVRLLLKygDAWVKKYDRSSLRTLGS 372
Cdd:PRK06710 257 PFFHVYGMTAVMNLSIMQGYKMVLI---PKF-DMKMVFEAIKKHKVTLFPGAPTIYIALLN--SPLLKEYDISSIRACIS 330
|
330 340 350
....*....|....*....|....*....|...
gi 91993047 373 VGEPINCEAWEWLHRVVGDSrctLVDTWWQTET 405
Cdd:PRK06710 331 GSAPLPVEVQEKFETVTGGK---LVEGYGLTES 360
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
97-377 |
4.05e-14 |
|
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: 74.05 E-value: 4.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 97 RITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITF 176
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 177 NqglrggrvvELkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemakedpvcapesmgsEDMLFMLYTSGSTG 256
Cdd:cd05935 81 S---------EL------------------------------------------------------DDLALIPYTSGTTG 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 257 MPKGIVHTQaGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLF-----ESTPvypnagrywE 331
Cdd:cd05935 98 LPKGCMHTH-FSAAANALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMarwdrETAL---------E 167
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 91993047 332 TVERLKINQFYGAPTAVRLLLkyGDAWVKKYDRSSLRTLGSVGEPI 377
Cdd:cd05935 168 LIEKYKVTFWTNIPTMLVDLL--ATPEFKTRDLSSLKVLTGGGAPM 211
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
69-276 |
7.06e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 73.50 E-value: 7.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 69 VNCLDQHVRKSPESVALiwerDEPGTEvrITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAV 148
Cdd:PRK05605 35 VDLYDNAVARFGDRPAL----DFFGAT--TTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 149 ---HTVIfagFSAESLAGRINDAKCKVVITFN------QGLRGGrvVELKKIVD-EAVKHCPTVQHVLV------AHRTD 212
Cdd:PRK05605 109 vveHNPL---YTAHELEHPFEDHGARVAIVWDkvaptvERLRRT--TPLETIVSvNMIAAMPLLQRLALrlpipaLRKAR 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 91993047 213 NKVHMGDLD-VPLEQ----EMAKEDPVCAPESMGSEDMLFMLYTSGSTGMPKGivhtqagyllyAALTH 276
Cdd:PRK05605 184 AALTGPAPGtVPWETlvdaAIGGDGSDVSHPRPTPDDVALILYTSGTTGKPKG-----------AQLTH 241
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
72-369 |
8.38e-14 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 73.31 E-value: 8.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 72 LDQHVRKSPESVALIwerdEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTV 151
Cdd:PRK08315 22 LDRTAARYPDREALV----YRDQGLRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 152 IFAGFSAESLAGRINDAKCKVVITFNqGLRGGRVVE-LKKIVDEaVKHC----------PTVQHVLvahRTDNKVHMGDL 220
Cdd:PRK08315 98 INPAYRLSELEYALNQSGCKALIAAD-GFKDSDYVAmLYELAPE-LATCepgqlqsarlPELRRVI---FLGDEKHPGML 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 221 DVPLEQEMAKEDPVCAPESMGSE----DMLFMLYTSGSTGMPKGivhtqagyllyAALTHK-------LVFDHQ---PGD 286
Cdd:PRK08315 173 NFDELLALGRAVDDAELAARQATldpdDPINIQYTSGTTGFPKG-----------ATLTHRnilnngyFIGEAMkltEED 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 287 ----------IFGCVadIGwitghsyvVYGPLCNGATSvlfestpVYPNAG----RYWETVERLKINQFYGAPTAVRLLL 352
Cdd:PRK08315 242 rlcipvplyhCFGMV--LG--------NLACVTHGATM-------VYPGEGfdplATLAAVEEERCTALYGVPTMFIAEL 304
|
330
....*....|....*..
gi 91993047 353 KYGDawVKKYDRSSLRT 369
Cdd:PRK08315 305 DHPD--FARFDLSSLRT 319
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
69-266 |
9.33e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 73.27 E-value: 9.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 69 VNCLDQHVRKSPESVALIWERDEpgtevrITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAV 148
Cdd:PRK07786 20 VNQLARHALMQPDAPALRFLGNT------TTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 149 HTVIFAGFSAESLAGRINDAKCKVVITfnqglrGGRVVELKKIVDEAVkhcPTVQHVLVA-HRTDNKVhmgdldVPLEQE 227
Cdd:PRK07786 94 AVPVNFRLTPPEIAFLVSDCGAHVVVT------EAALAPVATAVRDIV---PLLSTVVVAgGSSDDSV------LGYEDL 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 91993047 228 MAKEDPVCAPESMGSEDMLFMLYTSGSTGMPKGIVHTQA 266
Cdd:PRK07786 159 LAEAGPAHAPVDIPNDSPALIMYTSGTTGRPKGAVLTHA 197
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
70-264 |
1.62e-13 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 72.30 E-value: 1.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 70 NCLDQHVRKSPESVALIWERDEpgtevrITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVH 149
Cdd:PRK03640 6 NWLKQRAFLTPDRTAIEFEEKK------VTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 150 TVIFAGFSAESLAGRINDAKCKVVITfnqglrggrvvelkkivDEAVKHcptvqhvlvAHRTDNKVHMGDLdvpleQEMA 229
Cdd:PRK03640 80 VLLNTRLSREELLWQLDDAEVKCLIT-----------------DDDFEA---------KLIPGISVKFAEL-----MNGP 128
|
170 180 190
....*....|....*....|....*....|....*.
gi 91993047 230 KEDPVcaPESMGSEDMLF-MLYTSGSTGMPKGIVHT 264
Cdd:PRK03640 129 KEEAE--IQEEFDLDEVAtIMYTSGTTGKPKGVIQT 162
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
74-388 |
2.07e-13 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 71.80 E-value: 2.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 74 QHVRKSPESVAL-IWERDepgtevrITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVI 152
Cdd:cd05918 7 ERARSQPDAPAVcAWDGS-------LTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 153 FAGFSAESLAGRINDAKCKVVITfnqglrggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemakED 232
Cdd:cd05918 80 DPSHPLQRLQEILQDTGAKVVLT-------------------------------------------------------SS 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 233 PvcapesmgsEDMLFMLYTSGSTGMPKGIVHTQAGYLLyAALTHKLVFDHQPGD--------IFG-CVADIgwitghsyv 303
Cdd:cd05918 105 P---------SDAAYVIFTSGSTGKPKGVVIEHRALST-SALAHGRALGLTSESrvlqfasyTFDvSILEI--------- 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 304 vYGPLCNGAT------SVLFESTPvypnagrywETVERLKINQFYGAPTAVRLLlkygdawvkkyDRS---SLRTLGSVG 374
Cdd:cd05918 166 -FTTLAAGGClcipseEDRLNDLA---------GFINRLRVTWAFLTPSVARLL-----------DPEdvpSLRTLVLGG 224
|
330
....*....|....*
gi 91993047 375 EPINCEAWE-WLHRV 388
Cdd:cd05918 225 EALTQSDVDtWADRV 239
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
80-269 |
2.36e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 71.90 E-value: 2.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 80 PESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAE 159
Cdd:PRK08162 32 PDRPAVIHG------DRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 160 SLAGRINDAKCKVVITFNqglrggrvvELKKIVDEAVKHCPtVQHVLVAHRTDNK----VHMGDLDvpLEQEMAKEDPVC 235
Cdd:PRK08162 106 SIAFMLRHGEAKVLIVDT---------EFAEVAREALALLP-GPKPLVIDVDDPEypggRFIGALD--YEAFLASGDPDF 173
|
170 180 190
....*....|....*....|....*....|....*.
gi 91993047 236 APESMGSE-DMLFMLYTSGSTGMPKGIV-HTQAGYL 269
Cdd:PRK08162 174 AWTLPADEwDAIALNYTSGTTGNPKGVVyHHRGAYL 209
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
76-411 |
4.08e-13 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 71.91 E-value: 4.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 76 VRKSPESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAG 155
Cdd:PRK12316 4561 ARMTPDAVAVVFD------EEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPE 4634
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 156 FSAESLAGRINDAKCKVVITFNQGLRGGRVvelkkivdeavkhcPTVQHVLVAHRTDNKVHMGDLDvPLEQEMAkedpvc 235
Cdd:PRK12316 4635 YPRERLAYMMEDSGAALLLTQSHLLQRLPI--------------PDGLASLALDRDEDWEGFPAHD-PAVRLHP------ 4693
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 236 apesmgsEDMLFMLYTSGSTGMPKGivhtqagyllyAALTHK--LVFDHQPGDIFGCVADIGWITGHSYV-------VYG 306
Cdd:PRK12316 4694 -------DNLAYVIYTSGSTGRPKG-----------VAVSHGslVNHLHATGERYELTPDDRVLQFMSFSfdgshegLYH 4755
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 307 PLCNGAtSVLFESTPVYPNAGRYWETVE-RLKINQFygAPTAVRLLLKyGDAwvKKYDRSSLRTLGSVGEPIN----CEA 381
Cdd:PRK12316 4756 PLINGA-SVVIRDDSLWDPERLYAEIHEhRVTVLVF--PPVYLQQLAE-HAE--RDGEPPSLRVYCFGGEAVAqasyDLA 4829
|
330 340 350
....*....|....*....|....*....|....*
gi 91993047 382 WE-----WLHRVVGDSRCTLVDTWWQTETGGICIA 411
Cdd:PRK12316 4830 WRalkpvYLFNGYGPTETTVTVLLWKARDGDACGA 4864
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
74-447 |
4.13e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 71.11 E-value: 4.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 74 QHVRKSPESVALIwerDEPGTevrITYRELLETTCRLANTLKRHGVHRGDRVAIympvspLA------VAAMLACARIGA 147
Cdd:PRK07788 57 HAARRAPDRAALI---DERGT---LTYAELDEQSNALARGLLALGVRAGDGVAV------LArnhrgfVLALYAAGKVGA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 148 VHTVIFAGFSAESLAGRINDAKCKVVITFNqglrggrvvELKKIVDEAVKHCPTVqHVLVAHrTDNKVHMGDLDVPLEQE 227
Cdd:PRK07788 125 RIILLNTGFSGPQLAEVAAREGVKALVYDD---------EFTDLLSALPPDLGRL-RAWGGN-PDDDEPSGSTDETLDDL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 228 MAKED--PVCAPESMGSedmlFMLYTSGSTGMPKGIVHTQAGYLLYAAlthkLVFDHQP---GDIFGCVADIGWITGHSY 302
Cdd:PRK07788 194 IAGSStaPLPKPPKPGG----IVILTSGTTGTPKGAPRPEPSPLAPLA----GLLSRVPfraGETTLLPAPMFHATGWAH 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 303 VVYGpLCNGATSVL---FestpvypNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINC 379
Cdd:PRK07788 266 LTLA-MALGSTVVLrrrF-------DPEATLEDIAKHKATALVVVPVMLSRILDLGPEVLAKYDTSSLKIIFVSGSALSP 337
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 91993047 380 EAWEWLHRVVGDSRCTLvdtWWQTETGGICIApRPSEegAEILPAMAMRPFFGIVPVLMDEKGSVVEG 447
Cdd:PRK07788 338 ELATRALEAFGPVLYNL---YGSTEVAFATIA-TPED--LAEAPGTVGRPPKGVTVKILDENGNEVPR 399
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
76-378 |
4.64e-13 |
|
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: 70.81 E-value: 4.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 76 VRKSPESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAG 155
Cdd:cd12115 9 AARTPDAIALVCG------DESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 156 FSAESLAGRINDAKCKVVITfnqglrggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemakedpvc 235
Cdd:cd12115 83 YPPERLRFILEDAQARLVLT------------------------------------------------------------ 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 236 apesmGSEDMLFMLYTSGSTGMPKG--IVHTQAGYLLYAALTH-------------KLVFDHQPGDIFgcvadigwitgh 300
Cdd:cd12115 103 -----DPDDLAYVIYTSGSTGRPKGvaIEHRNAAAFLQWAAAAfsaeelagvlastSICFDLSVFELF------------ 165
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 91993047 301 syvvyGPLCNGATSVLFESTPVYPNAGRYWETVerlKINQfygAPTAVRLLLKYGDAwvkkydRSSLRTLGSVGEPIN 378
Cdd:cd12115 166 -----GPLATGGKVVLADNVLALPDLPAAAEVT---LINT---VPSAAAELLRHDAL------PASVRVVNLAGEPLP 226
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
73-406 |
8.87e-13 |
|
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: 69.65 E-value: 8.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 73 DQHVRKSPESVALiwerdePGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVI 152
Cdd:cd17653 4 ERIAAAHPDAVAV------ESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 153 FAGFSAESLAGRINDAKCKVVITFNqglrggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemAKED 232
Cdd:cd17653 78 DAKLPSARIQAILRTSGATLLLTTD---------------------------------------------------SPDD 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 233 PVCApesmgsedmlfmLYTSGSTGMPKGIVHTQAGYLLYAALTHKLvFDHQPGDIFGCVADIGW--ITGhsyVVYGPLCN 310
Cdd:cd17653 107 LAYI------------IFTSGSTGIPKGVMVPHRGVLNYVSQPPAR-LDVGPGSRVAQVLSIAFdaCIG---EIFSTLCN 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 311 GATSVLfeSTPVYPnagryWETVERlKINQFYGAPTavrLLLKYGDAwvkkyDRSSLRTLGSVGEPINCE-AWEWLHRVV 389
Cdd:cd17653 171 GGTLVL--ADPSDP-----FAHVAR-TVDALMSTPS---ILSTLSPQ-----DFPNLKTIFLGGEAVPPSlLDRWSPGRR 234
|
330 340
....*....|....*....|..
gi 91993047 390 -----GDSRCTLVDTWWQTETG 406
Cdd:cd17653 235 lynayGPTECTISSTMTELLPG 256
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
82-318 |
1.02e-12 |
|
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: 70.18 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 82 SVALIWERDEpgtevrITYRELLETTCRLANTLK-RHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAES 160
Cdd:cd17632 58 TLRLLPRFET------ITYAELWERVGAVAAAHDpEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQ 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 161 LAGRINDAKCKVVITFNQGLRGGRvvelkkivdEAVKHCPTVQHVLV-AHRTDNKVHMGDLD------------VPLEQE 227
Cdd:cd17632 132 LAPILAETEPRLLAVSAEHLDLAV---------EAVLEGGTPPRLVVfDHRPEVDAHRAALEsarerlaavgipVTTLTL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 228 MAKED------PVCAPESmgSEDMLFML-YTSGSTGMPKGIVHT--------------QAGYLLYAALTHKLVFDHQPGD 286
Cdd:cd17632 203 IAVRGrdlppaPLFRPEP--DDDPLALLiYTSGSTGTPKGAMYTerlvatfwlkvssiQDIRPPASITLNFMPMSHIAGR 280
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 91993047 287 IfgcvadigwitghsyVVYGPLCNGAT---------SVLFE 318
Cdd:cd17632 281 I---------------SLYGTLARGGTayfaaasdmSTLFD 306
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
94-383 |
1.89e-12 |
|
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: 69.09 E-value: 1.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 94 TEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVV 173
Cdd:cd17642 41 TGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 174 ITFNQGLRggRVVELKKIVdeavkhcPTVQHVLVahrTDNKVHMGDLDVpLEQEMAKEDPVC-------APESMGSEDML 246
Cdd:cd17642 121 FCSKKGLQ--KVLNVQKKL-------KIIKTIII---LDSKEDYKGYQC-LYTFITQNLPPGfneydfkPPSFDRDEQVA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 247 FMLYTSGSTGMPKGIvhtqagyllyaALTHKLV---FDHQPGDIFGC-----VADIGWITGHS----YVVYGPLCNGATS 314
Cdd:cd17642 188 LIMNSSGSTGLPKGV-----------QLTHKNIvarFSHARDPIFGNqiipdTAILTVIPFHHgfgmFTTLGYLICGFRV 256
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 91993047 315 VL---FESTpvypnagRYWETVERLKINQFYGAPTAVRLLLKYgdAWVKKYDRSSLRTLGSVGEPINCEAWE 383
Cdd:cd17642 257 VLmykFEEE-------LFLRSLQDYKVQSALLVPTLFAFFAKS--TLVDKYDLSNLHEIASGGAPLSKEVGE 319
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
70-377 |
3.31e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 68.14 E-value: 3.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 70 NCLDQHVRKSPESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVH 149
Cdd:PRK07470 11 HFLRQAARRFPDRIALVWG------DRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVW 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 150 TVIFAGFSAESLAGRINDAKCKVVI---TFNQGLRGGRVVELK---KIVDEAVKHCPTVQHVLVAHRtDNKVHMGDLDvp 223
Cdd:PRK07470 85 VPTNFRQTPDEVAYLAEASGARAMIchaDFPEHAAAVRAASPDlthVVAIGGARAGLDYEALVARHL-GARVANAAVD-- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 224 leqemaKEDPvcapesmgsedmLFMLYTSGSTGMPKGIV--HTQAGYLlyaaLTHKLVfDHQPGdifgcvadigwITGH- 300
Cdd:PRK07470 162 ------HDDP------------CWFFFTSGTTGRPKAAVltHGQMAFV----ITNHLA-DLMPG-----------TTEQd 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 301 -SYVVyGPL---------CN---GATSVLFESTPVYPNAgrYWETVERLKINQFYGAPTAVRLLLKygDAWVKKYDRSSL 367
Cdd:PRK07470 208 aSLVV-APLshgagihqlCQvarGAATVLLPSERFDPAE--VWALVERHRVTNLFTVPTILKMLVE--HPAVDRYDHSSL 282
|
330
....*....|
gi 91993047 368 RTLGSVGEPI 377
Cdd:PRK07470 283 RYVIYAGAPM 292
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
90-368 |
3.81e-12 |
|
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: 68.13 E-value: 3.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 90 DEPGTEVriTYRELLETTCRLANTLKRhGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAK 169
Cdd:cd05909 2 DTLGTSL--TYRKLLTGAIALARKLAK-MTKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 170 CKVVITFNQ-----GLRGGRVVEL-KKIVD-EAVKhcptvqhvlvahrtdNKVHMGD-LDVPLEQEMAKEDPV----CAP 237
Cdd:cd05909 79 IKTVLTSKQfieklKLHHLFDVEYdARIVYlEDLR---------------AKISKADkCKAFLAGKFPPKWLLrifgVAP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 238 ESmgSEDMLFMLYTSGSTGMPKGIVHTQAGYL--LYAALTHklvFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSV 315
Cdd:cd05909 144 VQ--PDDPAVILFTSGSEGLPKGVVLSHKNLLanVEQITAI---FDPNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVV 218
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 91993047 316 LfestpvYPNAGRYW---ETVERLKINQFYGAPTAVRLLLKYgdawVKKYDRSSLR 368
Cdd:cd05909 219 F------HPNPLDYKkipELIYDKKATILLGTPTFLRGYARA----AHPEDFSSLR 264
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
72-266 |
4.06e-12 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 68.53 E-value: 4.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 72 LDQHVRKSPESVALIWERDEpgtevrITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTV 151
Cdd:PRK10252 464 VAQQAAKTPDAPALADARYQ------FSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLP 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 152 IFAGFSAESLAGRINDAKCKVVITfnqglrggrvvelkkiVDEavkhcptvqhvlVAHRTDNkvhmGDLDVPLEQEMAKE 231
Cdd:PRK10252 538 LDTGYPDDRLKMMLEDARPSLLIT----------------TAD------------QLPRFAD----VPDLTSLCYNAPLA 585
|
170 180 190
....*....|....*....|....*....|....*.
gi 91993047 232 DPVCAPESMGS-EDMLFMLYTSGSTGMPKGIVHTQA 266
Cdd:PRK10252 586 PQGAAPLQLSQpHHTAYIIFTSGSTGRPKGVMVGQT 621
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
95-364 |
4.45e-12 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.
Pssm-ID: 341283 [Multi-domain] Cd Length: 486 Bit Score: 67.71 E-value: 4.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 95 EVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVi 174
Cdd:cd12118 27 DRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVL- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 175 tfnqglrggrvvelkkIVDEavkhcptvqhvlvAHRTDNKVHMGDLDVPLEQemakedpvcaPESmgSEDMLFMLYTSGS 254
Cdd:cd12118 106 ----------------FVDR-------------EFEYEDLLAEGDPDFEWIP----------PAD--EWDPIALNYTSGT 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 255 TGMPKGIVHTQAG-YL--LYAALTHKLvfDHQPG-----DIFGCVadiGWItghsyVVYGPLCNGATSVLFESTpvypNA 326
Cdd:cd12118 145 TGRPKGVVYHHRGaYLnaLANILEWEM--KQHPVylwtlPMFHCN---GWC-----FPWTVAAVGGTNVCLRKV----DA 210
|
250 260 270
....*....|....*....|....*....|....*...
gi 91993047 327 GRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDR 364
Cdd:cd12118 211 KAIYDLIEKHKVTHFCGAPTVLNMLANAPPSDARPLPH 248
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
98-288 |
5.03e-12 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 67.83 E-value: 5.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 98 ITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFN 177
Cdd:PLN02387 107 ITYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICDS 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 178 QglrggrvvELKKIVDEAvKHCPTVQHVLVAHRTDNKVHMGDLDV--------PLEQEMAKEDPVcAPESMGSEDMLFML 249
Cdd:PLN02387 187 K--------QLKKLIDIS-SQLETVKRVIYMDDEGVDSDSSLSGSsnwtvssfSEVEKLGKENPV-DPDLPSPNDIAVIM 256
|
170 180 190
....*....|....*....|....*....|....*....
gi 91993047 250 YTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHQPGDIF 288
Cdd:PLN02387 257 YTSGSTGLPKGVMMTHGNIVATVAGVMTVVPKLGKNDVY 295
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
97-368 |
1.99e-11 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 65.88 E-value: 1.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 97 RITYRELLETTCRLANTLKRHGVHRGDRVAIYM----PVSPLAVAAMlacaRIGAVHTVIFAGFSAESLAGRINDAKCKV 172
Cdd:PRK12406 11 RRSFDELAQRAARAAGGLAALGVRPGDCVALLMrndfAFFEAAYAAM----RLGAYAVPVNWHFKPEEIAYILEDSGARV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 173 VITFNQGLRGgrvveLKKIVDEAVK--HCPTVQHVLVAHRTDN---KVHMGDLDvpLEQEMAKEDPVCAPESMGSEDMLf 247
Cdd:PRK12406 87 LIAHADLLHG-----LASALPAGVTvlSVPTPPEIAAAYRISPallTPPAGAID--WEGWLAQQEPYDGPPVPQPQSMI- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 248 mlYTSGSTGMPKGiVHTQAGYLLYAALTHKLVfdhqpGDIFgcvadiGWITGHSYVVYGPlcngatsvLFESTP-VYP-N 325
Cdd:PRK12406 159 --YTSGTTGHPKG-VRRAAPTPEQAAAAEQMR-----ALIY------GLKPGIRALLTGP--------LYHSAPnAYGlR 216
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 91993047 326 AGRYWET---------------VERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLR 368
Cdd:PRK12406 217 AGRLGGVlvlqprfdpeellqlIERHRITHMHMVPTMFIRLLKLPEEVRAKYDVSSLR 274
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
72-374 |
2.32e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 66.34 E-value: 2.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 72 LDQHVRKSPESVALIWerdepgTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTV 151
Cdd:PRK12467 1580 IEDQAAATPEAVALVF------GEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVP 1653
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 152 IFAGFSAESLAGRINDAKCKVVITfnqglrggrvvelkkivdeavkhcptVQHVLVAHRTDNKVHMGDLDVplEQEMAKE 231
Cdd:PRK12467 1654 LDPEYPRERLAYMIEDSGIELLLT--------------------------QSHLQARLPLPDGLRSLVLDQ--EDDWLEG 1705
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 232 DPVCAPES-MGSEDMLFMLYTSGSTGMPKGivhtqagyllyAALTHKLVFDH--QPGDIFGCVADIGWITGHSYV----- 303
Cdd:PRK12467 1706 YSDSNPAVnLAPQNLAYVIYTSGSTGRPKG-----------AGNRHGALVNRlcATQEAYQLSAADVVLQFTSFAfdvsv 1774
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 304 --VYGPLCNGAtSVLFESTPVYPNAGRYWETVERLKI----------NQF------YGAPTAVRLLLKYGDAWVKKYDRS 365
Cdd:PRK12467 1775 weLFWPLINGA-RLVIAPPGAHRDPEQLIQLIERQQVttlhfvpsmlQQLlqmdeqVEHPLSLRRVVCGGEALEVEALRP 1853
|
....*....
gi 91993047 366 SLRTLGSVG 374
Cdd:PRK12467 1854 WLERLPDTG 1862
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
76-316 |
2.32e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 66.34 E-value: 2.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 76 VRKSPESVALIWERDepgtevRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAG 155
Cdd:PRK12467 522 ARQHPERPALVFGEQ------VLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPE 595
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 156 FSAESLAGRINDAKCKVVITFNQGLR------GGRVVELKKIVDEaVKHCPtvqhvlvAHRTdnkvhmgdlDVPLEqema 229
Cdd:PRK12467 596 YPQDRLAYMLDDSGVRLLLTQSHLLAqlpvpaGLRSLCLDEPADL-LCGYS-------GHNP---------EVALD---- 654
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 230 kedpvcaPESMGsedmlFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLvFDHQPGDIFGCVADIGWITGHsYVVYGPLC 309
Cdd:PRK12467 655 -------PDNLA-----YVIYTSGSTGQPKGVAISHGALANYVCVIAER-LQLAADDSMLMVSTFAFDLGV-TELFGALA 720
|
....*..
gi 91993047 310 NGATSVL 316
Cdd:PRK12467 721 SGATLHL 727
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
107-374 |
2.72e-11 |
|
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: 65.15 E-value: 2.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 107 TCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAgfsaeslagRINDAKCKVVITFNQGLRGGRVV 186
Cdd:cd05922 3 VSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRLGLVFV---------PLNPTLKESVLRYLVADAGGRIV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 187 elkkIVDEAvkhcptvqhvLVAHRTDNKVHMGDLDVPLEQE--MAKEDPVCAPESMGsEDMLFMLYTSGSTGMPKGIV-- 262
Cdd:cd05922 74 ----LADAG----------AADRLRDALPASPDPGTVLDADgiRAARASAPAHEVSH-EDLALLLYTSGSTGSPKLVRls 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 263 HTQagyLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSyVVYGPLCNGATSVLfESTPVYPNAgrYWETVERLKINQFY 342
Cdd:cd05922 139 HQN---LLANARSIAEYLGITADDRALTVLPLSYDYGLS-VLNTHLLRGATLVL-TNDGVLDDA--FWEDLREHGATGLA 211
|
250 260 270
....*....|....*....|....*....|..
gi 91993047 343 GAPTAVRLLLKYGdawVKKYDRSSLRTLGSVG 374
Cdd:cd05922 212 GVPSTYAMLTRLG---FDPAKLPSLRYLTQAG 240
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
80-429 |
2.87e-11 |
|
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: 65.18 E-value: 2.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 80 PESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAE 159
Cdd:cd17650 1 PDAIAVSDA------TRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 160 SLAGRINDAKCKVVITfnqglrggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemakeDPvcapes 239
Cdd:cd17650 75 RLQYMLEDSGAKLLLT--------------------------------------------------------QP------ 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 240 mgsEDMLFMLYTSGSTGMPKGIVHTQAGYL-LYAALTHKLVFDHQPGDIFGcvadigwITGHSYVVYG-----PLCNGAT 313
Cdd:cd17650 93 ---EDLAYVIYTSGTTGKPKGVMVEHRNVAhAAHAWRREYELDSFPVRLLQ-------MASFSFDVFAgdfarSLLNGGT 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 314 SVLFESTPVYpNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTL--GSVGEPIncEAWEWLHRVVGd 391
Cdd:cd17650 163 LVICPDEVKL-DPAALYDLILKSRITLMESTPALIRPVMAYVYR--NGLDLSAMRLLivGSDGCKA--QDFKTLAARFG- 236
|
330 340 350
....*....|....*....|....*....|....*...
gi 91993047 392 SRCTLVDTWWQTETggiCIAPRPSEEGAEILPAMAMRP 429
Cdd:cd17650 237 QGMRIINSYGVTEA---TIDSTYYEEGRDPLGDSANVP 271
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
76-378 |
3.54e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 65.01 E-value: 3.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 76 VRKSPESVALIWerdepgTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAG 155
Cdd:PRK06188 22 LKRYPDRPALVL------GDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 156 FSAESLAGRINDAKCKVVItFNQGLRGGRVVELkkivdeaVKHCPTVQHVLVahrtdnkvhMGDLD--VPLEQEMAKEDP 233
Cdd:PRK06188 96 GSLDDHAYVLEDAGISTLI-VDPAPFVERALAL-------LARVPSLKHVLT---------LGPVPdgVDLLAAAAKFGP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 234 VCAPESMGSEDMLFMLYTSGSTGMPKGIVHTQAGYLLYAALthklvfdhqpgdifgCVADIGWITGHSYVVYGPLCNGAt 313
Cdd:PRK06188 159 APLVAAALPPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQI---------------QLAEWEWPADPRFLMCTPLSHAG- 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 91993047 314 svlfeSTPVYP--------------NAGRYWETVERLKINQFYGAPTAVRLLLKYGDawVKKYDRSSLRTLGSVGEPIN 378
Cdd:PRK06188 223 -----GAFFLPtllrggtvivlakfDPAEVLRAIEEQRITATFLVPTMIYALLDHPD--LRTRDLSSLETVYYGASPMS 294
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
79-261 |
4.93e-11 |
|
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: 64.42 E-value: 4.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 79 SPESVALIWERDEpgtevrITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSA 158
Cdd:cd17656 1 TPDAVAVVFENQK------LTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 159 ESLAGRINDAKCKVVITFNqglrggrvvelkkivdeavkHCPTVQhvlvahrTDNKVHMgdldVPLEQEMAKEDPVCAPE 238
Cdd:cd17656 75 ERRIYIMLDSGVRVVLTQR--------------------HLKSKL-------SFNKSTI----LLEDPSISQEDTSNIDY 123
|
170 180
....*....|....*....|...
gi 91993047 239 SMGSEDMLFMLYTSGSTGMPKGI 261
Cdd:cd17656 124 INNSDDLLYIIYTSGTTGKPKGV 146
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
74-262 |
5.30e-11 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 64.64 E-value: 5.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 74 QHVRKSPESVALiweRDEPGTEvRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIF 153
Cdd:PRK05857 22 EQARQQPEAIAL---RRCDGTS-ALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMAD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 154 AGFSAESLAgRINDAKCKVVITFNqglRGGRVvelkkivdeAVKHCPTVQHVLVAHRTDNKVHMGDLDVPLEQEMAKEDP 233
Cdd:PRK05857 98 GNLPIAAIE-RFCQITDPAAALVA---PGSKM---------ASSAVPEALHSIPVIAVDIAAVTRESEHSLDAASLAGNA 164
|
170 180
....*....|....*....|....*....
gi 91993047 234 vcapeSMGSEDMLFMLYTSGSTGMPKGIV 262
Cdd:PRK05857 165 -----DQGSEDPLAMIFTSGTTGEPKAVL 188
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
73-445 |
5.73e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 65.36 E-value: 5.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 73 DQHVRKSPESVALIWerdepgTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVI 152
Cdd:PRK12316 518 EEQVERTPEAPALAF------GEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPL 591
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 153 FAGFSAESLAGRINDAKCKVVItfnqglrggrvvelkkivdeavkhcpTVQHVLVAHRTDNKVHMGDLDVPLEQEMAKED 232
Cdd:PRK12316 592 DPEYPAERLAYMLEDSGVQLLL--------------------------SQSHLGRKLPLAAGVQVLDLDRPAAWLEGYSE 645
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 233 PvcAPE-SMGSEDMLFMLYTSGSTGMPKGIVHTqagyllYAALTHKLVFDHQP-----GDIFGCVADIGWITGHsYVVYG 306
Cdd:PRK12316 646 E--NPGtELNPENLAYVIYTSGSTGKPKGAGNR------HRALSNRLCWMQQAyglgvGDTVLQKTPFSFDVSV-WEFFW 716
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 307 PLCNGATSVLfESTPVYPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAwvkkYDRSSLRTLGSVGEPInceAWEWLH 386
Cdd:PRK12316 717 PLMSGARLVV-AAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDV----ASCTSLRRIVCSGEAL---PADAQE 788
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 91993047 387 RVVGD-SRCTLVDTWWQTE-TGGICIAPRPSEEGAEILPAmamRPFFGIVPVLMDEKGSVV 445
Cdd:PRK12316 789 QVFAKlPQAGLYNLYGPTEaAIDVTHWTCVEEGGDSVPIG---RPIANLACYILDANLEPV 846
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
98-428 |
7.50e-11 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 64.28 E-value: 7.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 98 ITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITfN 177
Cdd:PRK06060 31 VTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVT-S 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 178 QGLR----GGRVVELKKIVDEAVKHCPTvqhvlvahrtdnkvhmgDLdvpleqemakedpvcapESMGSEDMLFMLYTSG 253
Cdd:PRK06060 110 DALRdrfqPSRVAEAAELMSEAARVAPG-----------------GY-----------------EPMGGDALAYATYTSG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 254 STGMPKGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLfESTPVYPNAGRYWETv 333
Cdd:PRK06060 156 TTGPPKAAIHRHADPLTFVDAMCRKALRLTPEDTGLCSARMYFAYGLGNSVWFPLATGGSAVI-NSAPVTPEAAAILSA- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 334 eRLKINQFYGAPTavrLLLKYGDAWVKKYDRsSLRTLGSVGEPINCEAWEWLHRVVGDsrCTLVDTWWQTETGGICIAP- 412
Cdd:PRK06060 234 -RFGPSVLYGVPN---FFARVIDSCSPDSFR-SLRCVVSAGEALELGLAERLMEFFGG--IPILDGIGSTEVGQTFVSNr 306
|
330 340
....*....|....*....|
gi 91993047 413 ----RPSEEGaEILPAMAMR 428
Cdd:PRK06060 307 vdewRLGTLG-RVLPPYEIR 325
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
76-374 |
1.49e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 63.82 E-value: 1.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 76 VRKSPESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAG 155
Cdd:PRK12316 2013 AARAPEAIAVVFG------DQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPN 2086
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 156 FSAESLAGRINDAKCKVVITfnqglrggrvvelKKIVDEAVKhCPTVQHVLvahrtdnkvhmgDLDVPLEQEmakEDPVC 235
Cdd:PRK12316 2087 YPAERLAYMLEDSGAALLLT-------------QRHLLERLP-LPAGVARL------------PLDRDAEWA---DYPDT 2137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 236 APE-SMGSEDMLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKlVFDHQPGDifgCVADIGWIT--GHSYVVYGPLCNGA 312
Cdd:PRK12316 2138 APAvQLAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGE-RYELSPAD---CELQFMSFSfdGAHEQWFHPLLNGA 2213
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 91993047 313 tSVLFESTPVYpNAGRYWETVER----------LKINQFY------GAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVG 374
Cdd:PRK12316 2214 -RVLIRDDELW-DPEQLYDEMERhgvtildfppVYLQQLAehaerdGRPPAVRVYCFGGEAVPAASLRLAWEALRPVY 2289
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
72-412 |
2.20e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 63.26 E-value: 2.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 72 LDQHVRKSPESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTV 151
Cdd:PRK12467 3101 IEAQVARTPEAPALVFG------DQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVP 3174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 152 IFAGFSAESLAGRINDAKCKVVITfnqglrGGRVVElkkivdeavkHCPTVQHVLVAhrtdnkvhmgDLDVPLEQEMAKE 231
Cdd:PRK12467 3175 LDPEYPRERLAYMIEDSGVKLLLT------QAHLLE----------QLPAPAGDTAL----------TLDRLDLNGYSEN 3228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 232 DPvcAPESMGsEDMLFMLYTSGSTGMPKGI--------VHTQAGYLLYAALTHKLVFDHQPGDIFGCVADigwitghsyv 303
Cdd:PRK12467 3229 NP--STRVMG-ENLAYVIYTSGSTGKPKGVgvrhgalaNHLCWIAEAYELDANDRVLLFMSFSFDGAQER---------- 3295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 304 VYGPLCNGATSVLfestpvypNAGRYW---ETV-----ERLKINQFygAPTAVRLLLKYGDAwvkkYDRSSLRTLGSVGE 375
Cdd:PRK12467 3296 FLWTLICGGCLVV--------RDNDLWdpeELWqaihaHRISIACF--PPAYLQQFAEDAGG----ADCASLDIYVFGGE 3361
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 91993047 376 PINCEAWEWLHRVV---------GDSRCTLVDTWWQTETGGICIAP 412
Cdd:PRK12467 3362 AVPPAAFEQVKRKLkprgltngyGPTEAVVTVTLWKCGGDAVCEAP 3407
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
72-266 |
2.87e-10 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 62.88 E-value: 2.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 72 LDQHVRKSPESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTV 151
Cdd:PRK05691 1137 LNEQARQTPERIALVWD------GGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVP 1210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 152 IFAGFSAESLAGRINDakCKVVITFNQGLRGGRVvelkkivdeavkhcPTVQHVLVahrtdnkvhmgdldVPLEQEMAKE 231
Cdd:PRK05691 1211 LDPDYPAERLAYMLAD--SGVELLLTQSHLLERL--------------PQAEGVSA--------------IALDSLHLDS 1260
|
170 180 190
....*....|....*....|....*....|....*.
gi 91993047 232 DPVCAPE-SMGSEDMLFMLYTSGSTGMPKGIVHTQA 266
Cdd:PRK05691 1261 WPSQAPGlHLHGDNLAYVIYTSGSTGQPKGVGNTHA 1296
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
72-396 |
3.54e-10 |
|
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: 61.96 E-value: 3.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 72 LDQHVRKSPESVALIwerdepGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVhtV 151
Cdd:cd05920 21 LARSAARHPDRIAVV------DGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAV--P 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 152 IFAgfsaeslagrindakckvvitfnqgLRGGRVVELKKIVD--EAVkhcptvqhVLVAHRTdnkvHMGDLDVPLEQEMA 229
Cdd:cd05920 93 VLA-------------------------LPSHRRSELSAFCAhaEAV--------AYIVPDR----HAGFDHRALARELA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 230 KEDPvcapesmgseDMLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLV-FDHQpgDIFGCVADIgwitGHSYV----- 303
Cdd:cd05920 136 ESIP----------EVALFLLSGGTTGTPKLIPRTHNDYAYNVRASAEVCgLDQD--TVYLAVLPA----AHNFPlacpg 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 304 VYGPLCNGATSVLFEStpvyPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAwvKKYDRSSLRTLGSVGEPINCEAWE 383
Cdd:cd05920 200 VLGTLLAGGRVVLAPD----PSPDAAFPLIEREGVTVTALVPALVSLWLDAAAS--RRADLSSLRLLQVGGARLSPALAR 273
|
330
....*....|...
gi 91993047 384 WLHRVVGdsrCTL 396
Cdd:cd05920 274 RVPPVLG---CTL 283
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
76-306 |
4.60e-10 |
|
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341310 [Multi-domain] Cd Length: 490 Bit Score: 61.57 E-value: 4.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 76 VRKSPESVALIWERDEpgtevrITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAG 155
Cdd:cd17655 7 AEKTPDHTAVVFEDQT------LTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 156 FSAESLAGRINDAKCKVVITfnqglrggrvvelkkivDEAVKHcptvqhvlvahrtdNKVHMGDLDVpLEQEMAKEDPV- 234
Cdd:cd17655 81 YPEERIQYILEDSGADILLT-----------------QSHLQP--------------PIAFIGLIDL-LDEDTIYHEESe 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 235 -CAPESmGSEDMLFMLYTSGSTGMPKGIVHTQAG-------------------YLLYAALThklvFDHQPGDIFGCVadi 294
Cdd:cd17655 129 nLEPVS-KSDDLAYVIYTSGSTGKPKGVMIEHRGvvnlvewankviyqgehlrVALFASIS----FDASVTEIFASL--- 200
|
250
....*....|..
gi 91993047 295 gwITGHSYVVYG 306
Cdd:cd17655 201 --LSGNTLYIVR 210
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
95-302 |
8.44e-10 |
|
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: 60.45 E-value: 8.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 95 EVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVI 174
Cdd:cd17640 3 PKRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 175 TFNqglrggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemakedpvcapesmGSEDMLFMLYTSGS 254
Cdd:cd17640 83 VEN---------------------------------------------------------------DSDDLATIIYTSGT 99
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 91993047 255 TGMPKGIVHTQAGyLLYAALTHKLVFDHQPGDIFGCVADIgWitgHSY 302
Cdd:cd17640 100 TGNPKGVMLTHAN-LLHQIRSLSDIVPPQPGDRFLSILPI-W---HSY 142
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
73-272 |
1.50e-09 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 60.08 E-value: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 73 DQHVRKSPESVALIWErDEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVI 152
Cdd:PRK08008 14 DDLADVYGHKTALIFE-SSGGVVRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 153 FAGFSAESLAGRINDAKCKVVITFNQGLRGGRVVELKKivdeavKHCPtvQHVLVAhRTDNKVHMGDLDvpLEQEMAKED 232
Cdd:PRK08008 93 NARLLREESAWILQNSQASLLVTSAQFYPMYRQIQQED------ATPL--RHICLT-RVALPADDGVSS--FTQLKAQQP 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 91993047 233 P-VCAPESMGSEDMLFMLYTSGSTGMPKGIVHTQAGyLLYA 272
Cdd:PRK08008 162 AtLCYAPPLSTDDTAEILFTSGTTSRPKGVVITHYN-LRFA 201
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
89-275 |
1.64e-09 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 59.77 E-value: 1.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 89 RDEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAV-HTVIFAGFsAESLAGRIND 167
Cdd:PRK06018 31 RSVEGPIVRTTYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAIcHTVNPRLF-PEQIAWIINH 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 168 AKCKVVI---TFnqglrggrVVELKKIVDeavkHCPTVQHVLVAhrTDnKVHMGDLDVP----LEQEMAKEDPVCAPESM 240
Cdd:PRK06018 110 AEDRVVItdlTF--------VPILEKIAD----KLPSVERYVVL--TD-AAHMPQTTLKnavaYEEWIAEADGDFAWKTF 174
|
170 180 190
....*....|....*....|....*....|....*
gi 91993047 241 GSEDMLFMLYTSGSTGMPKGIVHTQAGYLLYAALT 275
Cdd:PRK06018 175 DENTAAGMCYTSGTTGDPKGVLYSHRSNVLHALMA 209
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
97-274 |
2.06e-09 |
|
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: 59.29 E-value: 2.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 97 RITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIfagfsaeslagrindakckvvitf 176
Cdd:cd05940 3 ALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALI------------------------ 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 177 NQGLRGgrvvelkkivdEAVKHCPTV---QHVLVahrtdnkvhmgdldvpleqemakedpvcapesmgseDMLFMLYTSG 253
Cdd:cd05940 59 NYNLRG-----------ESLAHCLNVssaKHLVV------------------------------------DAALYIYTSG 91
|
170 180
....*....|....*....|.
gi 91993047 254 STGMPKGIVHTQAGYLLYAAL 274
Cdd:cd05940 92 TTGLPKAAIISHRRAWRGGAF 112
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
75-265 |
3.00e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 59.05 E-value: 3.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 75 HVRKSPESVALIwerdEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFA 154
Cdd:PRK09088 4 HARLQPQRLAAV----DLALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 155 GFSAESLAGRINDAKCKVVITfnqglrggrvvelkkivDEAVKhcptvqhvlvAHRTDnkvhMGDLDVpLEQEMAKEDPV 234
Cdd:PRK09088 80 RLSASELDALLQDAEPRLLLG-----------------DDAVA----------AGRTD----VEDLAA-FIASADALEPA 127
|
170 180 190
....*....|....*....|....*....|.
gi 91993047 235 CAPeSMGSEDMLFMLYTSGSTGMPKGIVHTQ 265
Cdd:PRK09088 128 DTP-SIPPERVSLILFTSGTSGQPKGVMLSE 157
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
69-317 |
3.78e-09 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 58.83 E-value: 3.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 69 VNCLDQHVRKSPESVALIWER---DEPgteVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARI 145
Cdd:PTZ00216 93 VERVEKEVVKDADGKERTMEVthfNET---RYITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQ 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 146 GAVHTVIFAGFSAESLAGRINDAKCKVVITfnqglRGGRVVELKKIVDEAVKHCPTVqhvlvahrtdnkVHMGDLDVPLE 225
Cdd:PTZ00216 170 SMVAATVYANLGEDALAYALRETECKAIVC-----NGKNVPNLLRLMKSGGMPNTTI------------IYLDSLPASVD 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 226 QE----MAKEDPVCAPESMGS----------EDMLFMLYTSGSTGMPKGIVHTQAGylLYA---ALTHKLVfdhqpgDIF 288
Cdd:PTZ00216 233 TEgcrlVAWTDVVAKGHSAGShhplnipennDDLALIMYTSGTTGDPKGVMHTHGS--LTAgilALEDRLN------DLI 304
|
250 260 270
....*....|....*....|....*....|...
gi 91993047 289 GCVADigwitGHSYVVYGPLCN----GATSVLF 317
Cdd:PTZ00216 305 GPPEE-----DETYCSYLPLAHimefGVTNIFL 332
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
108-382 |
5.03e-09 |
|
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: 58.16 E-value: 5.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 108 CRLANTLKRHGVHRG----DRVAIYMPVSPLAvaamlacaRIGAVHTVIFAGFSAESLAGRINDAKCKVVITfnqglrgg 183
Cdd:cd05929 12 FHQRRLLLLDVYSIAlnrnARAAAAEGVWIAD--------GVYIYLINSILTVFAAAAAWKCGACPAYKSSR-------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 184 rvvELKKIVDEAVKHCPTVQHVLVAhrTDNKVHMGDLDVPLEQEMAKEDPVcAPESMGSEdmlfMLYTSGSTGMPKGIvh 263
Cdd:cd05929 76 ---APRAEACAIIEIKAAALVCGLF--TGGGALDGLEDYEAAEGGSPETPI-EDEAAGWK----MLYSGGTTGRPKGI-- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 264 tqagyllyaalthKLVFDHQPGD---IFGCVADIGWITGHSYVVYGPL-------------CNGATSVLFESTpvypNAG 327
Cdd:cd05929 144 -------------KRGLPGGPPDndtLMAAALGFGPGADSVYLSPAPLyhaapfrwsmtalFMGGTLVLMEKF----DPE 206
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 91993047 328 RYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPinCEAW 382
Cdd:cd05929 207 EFLRLIERYRVTFAQFVPTMFVRLLKLPEAVRNAYDLSSLKRVIHAAAP--CPPW 259
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
97-293 |
5.16e-09 |
|
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: 58.07 E-value: 5.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 97 RITYRELLETTCRLANTLKRH-GVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVIT 175
Cdd:cd05938 5 TYTYRDVDRRSNQAARALLAHaGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKVLVV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 176 fnqglrggrVVELKKIVDEAvkhCPTVQ----HVLVAHRTDNKVHMGDLDVPLEQemAKEDPVcaPESMGSE----DMLF 247
Cdd:cd05938 85 ---------APELQEAVEEV---LPALRadgvSVWYLSHTSNTEGVISLLDKVDA--ASDEPV--PASLRAHvtikSPAL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 91993047 248 MLYTSGSTGMPKGIVHTQAGYLLYAALTHklvfdhqpgdIFGCVAD 293
Cdd:cd05938 149 YIYTSGTTGLPKAARISHLRVLQCSGFLS----------LCGVTAD 184
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
98-313 |
6.03e-09 |
|
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: 58.20 E-value: 6.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 98 ITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFN 177
Cdd:cd17641 12 FTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIAED 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 178 QglrgGRVVELKKIVDEAvkhcPTVQHVLVA-------HRTDNKVHMGDLdVPLEQEMAKEDPVCAPESMGS---EDMLF 247
Cdd:cd17641 92 E----EQVDKLLEIADRI----PSVRYVIYCdprgmrkYDDPRLISFEDV-VALGRALDRRDPGLYEREVAAgkgEDVAV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 91993047 248 MLYTSGSTGMPKGIVhTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGAT 313
Cdd:cd17641 163 LCTTSGTTGKPKLAM-LSHGNFLGHCAAYLAADPLGPGDEYVSVLPLPWIGEQMYSVGQALVCGFI 227
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
80-286 |
9.12e-09 |
|
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: 57.26 E-value: 9.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 80 PESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAE 159
Cdd:cd17652 1 PDAPAVVFG------DETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 160 SLAGRINDAKCKVVITFnqglrggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemakedpvcapes 239
Cdd:cd17652 75 RIAYMLADARPALLLTT--------------------------------------------------------------- 91
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 91993047 240 mgSEDMLFMLYTSGSTGMPKGIV--HTQAGYLLYAALTHklvFDHQPGD 286
Cdd:cd17652 92 --PDNLAYVIYTSGSTGRPKGVVvtHRGLANLAAAQIAA---FDVGPGS 135
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
77-284 |
1.72e-08 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 56.69 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 77 RKSPESVALIwerDEPGTevrITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGF 156
Cdd:PRK13382 54 QRCPDRPGLI---DELGT---LTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSF 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 157 SAESLAGRINDAKCKVVItFNQglrggrvvELKKIVDEAVKHCPTVQHVLVAHRTDNKV-HMGDLDVPLEQEmakedpvc 235
Cdd:PRK13382 128 AGPALAEVVTREGVDTVI-YDE--------EFSATVDRALADCPQATRIVAWTDEDHDLtVEVLIAAHAGQR-------- 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 91993047 236 aPESMGSEDMLFMLyTSGSTGMPKGIVHTQAGyllyAALTHKLVFDHQP 284
Cdd:PRK13382 191 -PEPTGRKGRVILL-TSGTTGTPKGARRSGPG----GIGTLKAILDRTP 233
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
73-423 |
2.55e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 56.89 E-value: 2.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 73 DQHVRKSPESVALIWerdepgTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVI 152
Cdd:PRK12316 3064 EEQVERTPDAVALAF------GEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPL 3137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 153 FAGFSAESLAGRINDAKCKVVITfnqglrggrvvelkkivdeavkhcptVQHVLVAHRTDNKVHMGDldvPLEQEMAKED 232
Cdd:PRK12316 3138 DPEYPEERLAYMLEDSGAQLLLS--------------------------QSHLRLPLAQGVQVLDLD---RGDENYAEAN 3188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 233 PvcaPESMGSEDMLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLvFDHQPGDIFGCVADIGWiTGHSYVVYGPLCNGA 312
Cdd:PRK12316 3189 P---AIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQA-YGLGVGDRVLQFTTFSF-DVFVEELFWPLMSGA 3263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 313 TSVLfESTPVYPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAwvkkYDRSSLRTLGSVGepincEAWEWLHRVVGDS 392
Cdd:PRK12316 3264 RVVL-AGPEDWRDPALLVELINSEGVDVLHAYPSMLQAFLEEEDA----HRCTSLKRIVCGG-----EALPADLQQQVFA 3333
|
330 340 350
....*....|....*....|....*....|.
gi 91993047 393 RCTLVDTWWQTETGGICIAPRPSEEGAEILP 423
Cdd:PRK12316 3334 GLPLYNLYGPTEATITVTHWQCVEEGKDAVP 3364
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
71-265 |
2.80e-08 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 56.04 E-value: 2.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 71 CLDQHVRKSPESVALIwERDEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSP----LAVAAMLACARIG 146
Cdd:PRK08180 44 RLVHWAQEAPDRVFLA-ERGADGGWRRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIehalLALAAMYAGVPYA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 147 AVHtvifagfSAESLAGRiNDAKCKVVItfnQGLRGGRVvelkkIVDEAVKHCPTVQHVLVAHR---TDNKVHMGDLDVP 223
Cdd:PRK08180 123 PVS-------PAYSLVSQ-DFGKLRHVL---ELLTPGLV-----FADDGAAFARALAAVVPADVevvAVRGAVPGRAATP 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 91993047 224 LEQEMAKEDPVCAPESM---GSEDMLFMLYTSGSTGMPKGIVHTQ 265
Cdd:PRK08180 187 FAALLATPPTAAVDAAHaavGPDTIAKFLFTSGSTGLPKAVINTH 231
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
73-404 |
5.26e-08 |
|
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341299 [Multi-domain] Cd Length: 465 Bit Score: 54.75 E-value: 5.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 73 DQHVRKSPESVALIWERDEpgtevrITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVI 152
Cdd:cd17644 7 EEQVERTPDAVAVVFEDQQ------LTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 153 FAGFSAESLAGRINDAKCKVVITfnQGlrggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemaked 232
Cdd:cd17644 81 DPNYPQERLTYILEDAQISVLLT--QP----------------------------------------------------- 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 233 pvcapesmgsEDMLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHQPgDIFGCVADIGWITGhSYVVYGPLCNGA 312
Cdd:cd17644 106 ----------ENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGITSS-DRVLQFASIAFDVA-AEEIYVTLLSGA 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 313 TSVLfESTPVYPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDrSSLRTLGSVGEPINCEAWEWLHRVVGDs 392
Cdd:cd17644 174 TLVL-RPEEMRSSLEDFVQYIQQWQLTVLSLPPAYWHLLVLELLLSTIDLP-SSLRLVIVGGEAVQPELVRQWQKNVGN- 250
|
330
....*....|..
gi 91993047 393 RCTLVDTWWQTE 404
Cdd:cd17644 251 FIQLINVYGPTE 262
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
72-265 |
7.10e-08 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 54.48 E-value: 7.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 72 LDQHVRKSPESVALIWERDEpgtevrITYRELLETTCRLANTLK-RHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHT 150
Cdd:PRK06839 8 IEKRAYLHPDRIAIITEEEE------MTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 151 VIFAGFSAESLAGRINDAKCKVVitFNQGLRGGRVVELKKIVdeavkhcpTVQHVlvahrtdnkVHMGDLDVPLEQEMAK 230
Cdd:PRK06839 82 PLNIRLTENELIFQLKDSGTTVL--FVEKTFQNMALSMQKVS--------YVQRV---------ISITSLKEIEDRKIDN 142
|
170 180 190
....*....|....*....|....*....|....*.
gi 91993047 231 EDPvcapesmGSEDMLFML-YTSGSTGMPKGIVHTQ 265
Cdd:PRK06839 143 FVE-------KNESASFIIcYTSGTTGKPKGAVLTQ 171
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
75-308 |
7.76e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 54.51 E-value: 7.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 75 HVRKSPESVALIWERDEpgtevrITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFA 154
Cdd:PRK06145 11 HARRTPDRAALVYRDQE------ISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 155 GFSAESLAGRINDAKCKVVitfnqglrggrvvelkkIVDEAVKHCPTVQH---VLVAHRTDNKVHMGDLDVPleqemake 231
Cdd:PRK06145 85 RLAADEVAYILGDAGAKLL-----------------LVDEEFDAIVALETpkiVIDAAAQADSRRLAQGGLE-------- 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 91993047 232 dpvCAPESMGSEDMLF-MLYTSGSTGMPKGIVHTqagyllYAALTHKlVFDHqpgdifgcVADIGWITGHSYVVYGPL 308
Cdd:PRK06145 140 ---IPPQAAVAPTDLVrLMYTSGTTDRPKGVMHS------YGNLHWK-SIDH--------VIALGLTASERLLVVGPL 199
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
95-339 |
1.11e-07 |
|
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: 53.99 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 95 EVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVI 174
Cdd:cd05914 5 GEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 175 TfnqglrggrvvelkkivdeavkhcptvqhvlvahrTDNkvhmgdldvpleqemakedpvcapesmgsEDMLFMLYTSGS 254
Cdd:cd05914 85 V-----------------------------------SDE-----------------------------DDVALINYTSGT 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 255 TGMPKGIVHTQAG----------YLLYAALTHKLVFdhQP-GDIFGCVADIgwitghsyvVYgPLCNGATSVLFESTP-- 321
Cdd:cd05914 101 TGNSKGVMLTYRNivsnvdgvkeVVLLGKGDKILSI--LPlHHIYPLTFTL---------LL-PLLNGAHVVFLDKIPsa 168
|
250 260
....*....|....*....|....*....
gi 91993047 322 ---------VYPNAG--RYWEtVERLKIN 339
Cdd:cd05914 169 kiialafaqVTPTLGvpVPLV-IEKIFKM 196
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
72-370 |
1.40e-07 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 53.84 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 72 LDQHVRksPESVALIW-ERdepgtevRITYRELLETTCRLANTLKRHGVHRGDRVAIYMP-VSPLAVaAMLACARIGAVh 149
Cdd:PRK10946 31 LTRHAA--SDAIAVICgER-------QFSYRELNQASDNLACSLRRQGIKPGDTALVQLGnVAEFYI-TFFALLKLGVA- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 150 tVIFAGFSAESL-----AGRINDAkckVVItfnqGLRGGRVVELKKIVDEAVKHCPTVQHVLVAHRTdnkvhmGDLDvpL 224
Cdd:PRK10946 100 -PVNALFSHQRSelnayASQIEPA---LLI----ADRQHALFSDDDFLNTLVAEHSSLRVVLLLNDD------GEHS--L 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 225 EQEMAKEDPVCAPESMGSEDMLFMLYTSGSTGMPKGIVHTQAGYlLYAAlthklvfdHQPGDIFGCVADIGWI----TGH 300
Cdd:PRK10946 164 DDAINHPAEDFTATPSPADEVAFFQLSGGSTGTPKLIPRTHNDY-YYSV--------RRSVEICGFTPQTRYLcalpAAH 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 91993047 301 SYVVYGPlcnGATSVLFESTPVY----PNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTL 370
Cdd:PRK10946 235 NYPMSSP---GALGVFLAGGTVVlapdPSATLCFPLIEKHQVNVTALVPPAVSLWLQAIAEGGSRAQLASLKLL 305
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
97-272 |
1.51e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 53.56 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 97 RITYRELLETTCRLANTLKRHGVHRGDRVAIympvspLA------VAAMLACARIGAV-HTV---IFagfsAESLAGRIN 166
Cdd:PRK07008 39 RYTYRDCERRAKQLAQALAALGVEPGDRVGT------LAwngyrhLEAYYGVSGSGAVcHTInprLF----PEQIAYIVN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 167 DAKCKVV---ITFnqglrggrvvelKKIVDEAVKHCPTVQHVLVAhrTDnKVHMGDLDVPL---EQEMAKEDPVCAPESM 240
Cdd:PRK07008 109 HAEDRYVlfdLTF------------LPLVDALAPQCPNVKGWVAM--TD-AAHLPAGSTPLlcyETLVGAQDGDYDWPRF 173
|
170 180 190
....*....|....*....|....*....|..
gi 91993047 241 GSEDMLFMLYTSGSTGMPKGIVHTQAGYLLYA 272
Cdd:PRK07008 174 DENQASSLCYTSGTTGNPKGALYSHRSTVLHA 205
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
98-264 |
1.73e-07 |
|
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: 53.37 E-value: 1.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 98 ITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVItfn 177
Cdd:cd17639 6 MSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECSAIF--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 178 qglrggrvvelkkivdeavkhcptvqhvlvahrTDNKvhmgdldvpleqemaKEDPVCapesmgsedmlfMLYTSGSTGM 257
Cdd:cd17639 83 ---------------------------------TDGK---------------PDDLAC------------IMYTSGSTGN 102
|
....*..
gi 91993047 258 PKGIVHT 264
Cdd:cd17639 103 PKGVMLT 109
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
69-261 |
1.76e-07 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 54.02 E-value: 1.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 69 VNCLDQHVRKSPESVALIWERDEPGTEVRITYRELLETTCRLANTLKRHGVHrGDRVAIYMPVSPLAVAAMLACARIGAV 148
Cdd:PRK05691 12 VQALQRRAAQTPDRLALRFLADDPGEGVVLSYRDLDLRARTIAAALQARASF-GDRAVLLFPSGPDYVAAFFGCLYAGVI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 149 HTVIFAGFSA-----ESLAGRINDAKCKVVITfNQGLRGGrvveLKKIVDEAVKHCPTVQHVlvahrtdnkvhmGDLDVP 223
Cdd:PRK05691 91 AVPAYPPESArrhhqERLLSIIADAEPRLLLT-VADLRDS----LLQMEELAAANAPELLCV------------DTLDPA 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 91993047 224 LEQEMAKedPVCAPesmgsEDMLFMLYTSGSTGMPKGI 261
Cdd:PRK05691 154 LAEAWQE--PALQP-----DDIAFLQYTSGSTALPKGV 184
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
98-277 |
1.84e-07 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 53.49 E-value: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 98 ITYRELLETTCRLANTLKRHGVHRGDRVAIYMP---VSPLAVAAMLacaRIGAVHTVIFAGFSAESLAGRINDAKCKVVI 174
Cdd:PRK07059 49 ITYGELDELSRALAAWLQSRGLAKGARVAIMMPnvlQYPVAIAAVL---RAGYVVVNVNPLYTPRELEHQLKDSGAEAIV 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 175 tfnqglrggrVVE-LKKIVDEAVKHCPtVQHVLVAhrtdnkvHMGDL-----------------DVP---LEQEMAKEDP 233
Cdd:PRK07059 126 ----------VLEnFATTVQQVLAKTA-VKHVVVA-------SMGDLlgfkghivnfvvrrvkkMVPawsLPGHVRFNDA 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 91993047 234 VCA-------PESMGSEDMLFMLYTSGSTGMPKGivhtqagyllyAALTHK 277
Cdd:PRK07059 188 LAEgarqtfkPVKLGPDDVAFLQYTGGTTGVSKG-----------ATLLHR 227
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
95-268 |
1.97e-07 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 53.22 E-value: 1.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 95 EVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVI 174
Cdd:PRK06155 44 GTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 175 TFNQGLRGGRVVELKKIVDEAVkhcptvqhVLVAHRTDNKVHMGDLDVPLEQEMAkedPVCAPESMGSeDMLFMLYTSGS 254
Cdd:PRK06155 124 VEAALLAALEAADPGDLPLPAV--------WLLDAPASVSVPAGWSTAPLPPLDA---PAPAAAVQPG-DTAAILYTSGT 191
|
170
....*....|....
gi 91993047 255 TGMPKGIVHTQAGY 268
Cdd:PRK06155 192 TGPSKGVCCPHAQF 205
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
90-450 |
3.92e-07 |
|
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: 52.28 E-value: 3.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 90 DEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAK 169
Cdd:cd05906 32 DADGSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTVPPTYDEPNARLRKLR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 170 cKVVITFNQGL---RGGRVVELKKIVDEAVkhcptvqhvlvahrtdnkvHMGDLDVPLEQEMAKEDPVCAPESmGSEDML 246
Cdd:cd05906 112 -HIWQLLGSPVvltDAELVAEFAGLETLSG-------------------LPGIRVLSIEELLDTAADHDLPQS-RPDDLA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 247 FMLYTSGSTGMPKGIVHTQAGyLLYAALTHKLVFDHQPGDIFgcvadIGW-----ITGHSYVVYGPLCNGATSVLFESTP 321
Cdd:cd05906 171 LLMLTSGSTGFPKAVPLTHRN-ILARSAGKIQHNGLTPQDVF-----LNWvpldhVGGLVELHLRAVYLGCQQVHVPTEE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 322 VYPNAGRYWETVERLKINQFYgAP----TAVRLLLKYGDAwvKKYDRSSLRTLGSVGEPINCEAWEWLHRVVgdSRCTLV 397
Cdd:cd05906 245 ILADPLRWLDLIDRYRVTITW-APnfafALLNDLLEEIED--GTWDLSSLRYLVNAGEAVVAKTIRRLLRLL--EPYGLP 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 398 DT-----WWQTETGGICI------APRPSEE------GAEIlPAMAMRpffgivpvLMDEKGSVVEGCNV 450
Cdd:cd05906 320 PDairpaFGMTETCSGVIysrsfpTYDHSQAlefvslGRPI-PGVSMR--------IVDDEGQLLPEGEV 380
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
93-345 |
4.67e-07 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 52.15 E-value: 4.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 93 GTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAkcKV 172
Cdd:PLN02861 73 GPYVWLTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHA--EV 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 173 VITFnqglrggrvVELKKI--VDEAVKHCPTVQHVLVAhrtdnkvhMGDLDVPLEQEMAKEDPVCAP----ESMGS---- 242
Cdd:PLN02861 151 SIAF---------VQESKIssILSCLPKCSSNLKTIVS--------FGDVSSEQKEEAEELGVSCFSweefSLMGSldce 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 243 ------EDMLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVFdhqpgdifgcVADIGWITGHSYVVYGPLCNGATSVL 316
Cdd:PLN02861 214 lppkqkTDICTIMYTSGTTGEPKGVILTNRAIIAEVLSTDHLLK----------VTDRVATEEDSYFSYLPLAHVYDQVI 283
|
250 260 270
....*....|....*....|....*....|....*...
gi 91993047 317 fESTPVYPNAG-RYW--------ETVERLKINQFYGAP 345
Cdd:PLN02861 284 -ETYCISKGASiGFWqgdirylmEDVQALKPTIFCGVP 320
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
98-266 |
7.48e-07 |
|
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: 51.45 E-value: 7.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 98 ITYRELLETTCRLANTLKRHGVHR--GDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVIt 175
Cdd:cd05927 6 ISYKEVAERADNIGSALRSLGGKPapASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVF- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 176 FNQGLrggRVVELKKIVDeavkhcptvqhvlvahrtdnkvhmgdldvpleqeMAKEDPVcaPESMGSEDMLF-MLYTSGS 254
Cdd:cd05927 85 CDAGV---KVYSLEEFEK----------------------------------LGKKNKV--PPPPPKPEDLAtICYTSGT 125
|
170
....*....|..
gi 91993047 255 TGMPKGIVHTQA 266
Cdd:cd05927 126 TGNPKGVMLTHG 137
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
91-259 |
9.63e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 51.15 E-value: 9.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 91 EPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIY--MPV--SPLAVAAMLACARIGAVHT----VIFAGFSAESLA 162
Cdd:PRK07768 23 EPDAPVRHTWGEVHERARRIAGGLAAAGVGPGDAVAVLagAPVeiAPTAQGLWMRGASLTMLHQptprTDLAVWAEDTLR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 163 grindakckvVItfnqGLRGGRVVELKKIVDEAVkhcPTVQHVLVAHRTdnkvhMGDLDvpleqemaKEDPVcAPESMGS 242
Cdd:PRK07768 103 ----------VI----GMIGAKAVVVGEPFLAAA---PVLEEKGIRVLT-----VADLL--------AADPI-DPVETGE 151
|
170
....*....|....*..
gi 91993047 243 EDMLFMLYTSGSTGMPK 259
Cdd:PRK07768 152 DDLALMQLTSGSTGSPK 168
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
65-264 |
1.10e-06 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 50.97 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 65 LNVSVNCLDQHVRKSPESVALIWER--DEP-GTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLA 141
Cdd:PLN02430 41 ITTAWDIFSKSVEKYPDNKMLGWRRivDGKvGPYMWKTYKEVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVAMEA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 142 CARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFNQGLRG------GRVVELKKIV-----DEAVKHcPTVQHVLVAHR 210
Cdd:PLN02430 121 CAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVFVQDKKIKEllepdcKSAKRLKAIVsftsvTEEESD-KASQIGVKTYS 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 91993047 211 TDNKVHMGdldvpleqemaKEDP--VCAPESMgseDMLFMLYTSGSTGMPKGIVHT 264
Cdd:PLN02430 200 WIDFLHMG-----------KENPseTNPPKPL---DICTIMYTSGTSGDPKGVVLT 241
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
97-391 |
1.14e-06 |
|
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: 50.54 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 97 RITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVItf 176
Cdd:cd05910 2 RLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAEPDAFI-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 177 nqglrggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdlDVPLEQEMAKedpvcapesmgsedmlfMLYTSGSTG 256
Cdd:cd05910 80 --------------------------------------------GIPKADEPAA-----------------ILFTSGSTG 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 257 MPKGIVHTQAgylLYAALTHKL--VFDHQPGDI----FGCVAdigwitghsyvVYGPLCnGATSVLFESTPVYP---NAG 327
Cdd:cd05910 99 TPKGVVYRHG---TFAAQIDALrqLYGIRPGEVdlatFPLFA-----------LFGPAL-GLTSVIPDMDPTRParaDPQ 163
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 91993047 328 RYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYdrSSLRTLGSVGEPINCEAWEWLHRVVGD 391
Cdd:cd05910 164 KLVGAIRQYGVSIVFGSPALLERVARYCAQHGITL--PSLRRVLSAGAPVPIALAARLRKMLSD 225
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
91-262 |
1.17e-06 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 50.79 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 91 EPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKC 170
Cdd:PLN02614 73 KPGKYVWQTYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEV 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 171 KVVITFNQglrggRVVELKKIVDEAVKHCPTVQHV---------------LVAHRTDNKVHMGD---LDVPLEQEmaked 232
Cdd:PLN02614 153 SIVFVEEK-----KISELFKTCPNSTEYMKTVVSFggvsreqkeeaetfgLVIYAWDEFLKLGEgkqYDLPIKKK----- 222
|
170 180 190
....*....|....*....|....*....|
gi 91993047 233 pvcapesmgsEDMLFMLYTSGSTGMPKGIV 262
Cdd:PLN02614 223 ----------SDICTIMYTSGTTGDPKGVM 242
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
100-265 |
1.54e-06 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 50.39 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 100 YRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHT-----VIFAGFSA--ESLAGRINDAKCKV 172
Cdd:PRK09192 52 YQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVplplpMGFGGRESyiAQLRGMLASAQPAA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 173 VITfnqglrggrVVELKKIVDEAVKHCPTVqhvlvahrtdnkvhmgdLDVPLEQEMAKEDPVCAPESMGSEDMLFMLYTS 252
Cdd:PRK09192 132 IIT---------PDELLPWVNEATHGNPLL-----------------HVLSHAWFKALPEADVALPRPTPDDIAYLQYSS 185
|
170
....*....|...
gi 91993047 253 GSTGMPKGIVHTQ 265
Cdd:PRK09192 186 GSTRFPRGVIITH 198
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
80-175 |
1.72e-06 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 50.09 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 80 PESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGD-RVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSA 158
Cdd:cd17648 1 PDRVAVVYG------DKRLTYRELNERANRLAHYLLSVAEIRPDdLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPD 74
|
90
....*....|....*..
gi 91993047 159 ESLAGRINDAKCKVVIT 175
Cdd:cd17648 75 ERIQFILEDTGARVVIT 91
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
79-269 |
1.84e-06 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 49.87 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 79 SPESVALIwERDEpgtevRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVhtVIFagfsa 158
Cdd:PRK09029 16 RPQAIALR-LNDE-----VLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGAR--VLP----- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 159 eslagrINDAkckvvitFNQGLRGGRVVELkkivdeavkhcpTVQHVLVAHRTDNkvhMGDLDVPLEQEMAKEDPVC-AP 237
Cdd:PRK09029 83 ------LNPQ-------LPQPLLEELLPSL------------TLDFALVLEGENT---FSALTSLHLQLVEGAHAVAwQP 134
|
170 180 190
....*....|....*....|....*....|..
gi 91993047 238 ESMGSedmlfMLYTSGSTGMPKGIVHTQAGYL 269
Cdd:PRK09029 135 QRLAT-----MTLTSGSTGLPKAAVHTAQAHL 161
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
87-414 |
1.84e-06 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 50.17 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 87 WERDEPGTevrITYRELLETTCRLANTLKRH-GVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRI 165
Cdd:PRK05620 31 WGGAEQEQ---TTFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHII 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 166 NDAKCKVVITFNQglrggrvveLKKIVDEAVKHCPTVQHVLVAHRTD---------NKVHMGDLDVPLEQEMAKEDPVCA 236
Cdd:PRK05620 108 NHAEDEVIVADPR---------LAEQLGEILKECPCVRAVVFIGPSDadsaaahmpEGIKVYSYEALLDGRSTVYDWPEL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 237 PESMGSEdmlfMLYTSGSTGMPKGIVHT-QAGYLLYAALTHKLVFDHQPGDIFGCVADI-----------GWITGHSYVV 304
Cdd:PRK05620 179 DETTAAA----ICYSTGTTGAPKGVVYShRSLYLQSLSLRTTDSLAVTHGESFLCCVPIyhvlswgvplaAFMSGTPLVF 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 305 YGPLCNGAT--SVLFESTPvypnagrywetverlkiNQFYGAPTA-VRLLLKYGDawvKKYDRSSLRTL---GSVGEPIN 378
Cdd:PRK05620 255 PGPDLSAPTlaKIIATAMP-----------------RVAHGVPTLwIQLMVHYLK---NPPERMSLQEIyvgGSAVPPIL 314
|
330 340 350
....*....|....*....|....*....|....*.
gi 91993047 379 CEAWEWLHRVvgdsrcTLVDTWWQTETGGICIAPRP 414
Cdd:PRK05620 315 IKAWEERYGV------DVVHVWGMTETSPVGTVARP 344
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
95-353 |
2.62e-06 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 49.63 E-value: 2.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 95 EVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVI 174
Cdd:PLN03102 37 KTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILF 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 175 TFNqglrggrvvELKKIVDEAVKHCPTVQH-----VLVAHRTDNKVHMGDLDVPLEQEMAKEDPvcAPESMGS------- 242
Cdd:PLN03102 117 VDR---------SFEPLAREVLHLLSSEDSnlnlpVIFIHEIDFPKRPSSEELDYECLIQRGEP--TPSLVARmfriqde 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 243 EDMLFMLYTSGSTGMPKGIVHTQAGYLLyAALThkLVFDHQPG---------DIFGCVadiGWItghsyVVYGPLCNGAT 313
Cdd:PLN03102 186 HDPISLNYTSGTTADPKGVVISHRGAYL-STLS--AIIGWEMGtcpvylwtlPMFHCN---GWT-----FTWGTAARGGT 254
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 91993047 314 SVLFEstpvYPNAGRYWETVERLKINQFYGAPTAVRLLLK 353
Cdd:PLN03102 255 SVCMR----HVTAPEIYKNIEMHNVTHMCCVPTVFNILLK 290
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
73-262 |
3.28e-06 |
|
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: 49.09 E-value: 3.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 73 DQHVRKSPESVALIWERDepgtevRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVI 152
Cdd:cd17645 5 EEQVERTPDHVAVVDRGQ------SLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 153 FAGFSAESLAGRINDAKCKVVITfnqglrggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemaked 232
Cdd:cd17645 79 DPDYPGERIAYMLADSSAKILLT--------------------------------------------------------- 101
|
170 180 190
....*....|....*....|....*....|
gi 91993047 233 pvcapesmGSEDMLFMLYTSGSTGMPKGIV 262
Cdd:cd17645 102 --------NPDDLAYVIYTSGSTGLPKGVM 123
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
72-267 |
3.37e-06 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 49.35 E-value: 3.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 72 LDQHVRKSPESVA---LIWERDEPGTEVRITYRELLETTCRLANTLKRHgVHRGDRVAIYMPVSPLAVAAMLACARIGAV 148
Cdd:PRK12476 40 IERNIANVGDTVAyryLDHSHSAAGCAVELTWTQLGVRLRAVGARLQQV-AGPGDRVAILAPQGIDYVAGFFAAIKAGTI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 149 HTVIFA----GfSAESLAGRINDAKCKVVITfnqglrggrvvelkkivDEAVKhcPTVQHVLVAHRTDNKVHMGDLD-VP 223
Cdd:PRK12476 119 AVPLFApelpG-HAERLDTALRDAEPTVVLT-----------------TTAAA--EAVEGFLRNLPRLRRPRVIAIDaIP 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 91993047 224 leqEMAKEDPVCAPesMGSEDMLFMLYTSGSTGMPKG--IVHTQAG 267
Cdd:PRK12476 179 ---DSAGESFVPVE--LDTDDVSHLQYTSGSTRPPVGveITHRAVG 219
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
97-266 |
4.28e-06 |
|
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: 48.83 E-value: 4.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 97 RITYRELLETTCRLANTL-KRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVIt 175
Cdd:cd05941 11 SITYADLVARAARLANRLlALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDSEPSLVL- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 176 fnqglrggrvvelkkivdeavkhcptvqhvlvahrtdnkvhmgdldvpleqemakedpvcapesmgseDMLFMLYTSGST 255
Cdd:cd05941 90 --------------------------------------------------------------------DPALILYTSGTT 101
|
170
....*....|.
gi 91993047 256 GMPKGIVHTQA 266
Cdd:cd05941 102 GRPKGVVLTHA 112
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
242-447 |
4.59e-06 |
|
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: 48.53 E-value: 4.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 242 SEDMLFMLYTSGSTGMPKGIVHTQA---GYLLYAALTHKLVFdhQPGDIFGCVADIGwiTGHSYVVYGPLCNGA------ 312
Cdd:cd05924 2 SADDLYILYTGGTTGMPKGVMWRQEdifRMLMGGADFGTGEF--TPSEDAHKAAAAA--AGTVMFPAPPLMHGTgswtaf 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 313 TSVLFESTPVYP----NAGRYWETVERLKINqfygaptavrLLLKYGDAWVK----------KYDRSSLRTLGSVGEPIN 378
Cdd:cd05924 78 GGLLGGQTVVLPddrfDPEEVWRTIEKHKVT----------SMTIVGDAMARplidalrdagPYDLSSLFAISSGGALLS 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 91993047 379 CEAWEWLHRVVGDSrcTLVDTWWQTETGGICIApRPSEEGAEilpamaMRPFFGIVP--VLMDEKGSVVEG 447
Cdd:cd05924 148 PEVKQGLLELVPNI--TLVDAFGSSETGFTGSG-HSAGSGPE------TGPFTRANPdtVVLDDDGRVVPP 209
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
242-380 |
5.52e-06 |
|
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: 48.25 E-value: 5.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 242 SEDMLFMLYTSGSTGMPKGIVHTQAGyLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGAtSVLFESTP 321
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSN-EVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGA-HVVLAGPA 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 91993047 322 VYPNAGRY---WETVERLKINQFYGAPTAVRLLLKY-GDAwvkkyDRSSLRTLGSVGEPINCE 380
Cdd:cd05944 79 GYRNPGLFdnfWKLVERYRITSLSTVPTVYAALLQVpVNA-----DISSLRFAMSGAAPLPVE 136
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
93-354 |
7.33e-06 |
|
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: 48.23 E-value: 7.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 93 GTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMP------VSPLAVaaMLAcariGAVHTVIFAGFSAESLAGRIN 166
Cdd:cd05932 2 GQVVEFTWGEVADKARRLAAALRALGLEPGSKIALISKncaewfITDLAI--WMA----GHISVPLYPTLNPDTIRYVLE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 167 DAKCKVVITfnqglrgGRV---VELKKIVDEAVKHCPTVQH-VLVAHRT-DNKVHMGDldvPLEqemakEDPVCAPESMG 241
Cdd:cd05932 76 HSESKALFV-------GKLddwKAMAPGVPEGLISISLPPPsAANCQYQwDDLIAQHP---PLE-----ERPTRFPEQLA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 242 SedmlfMLYTSGSTGMPKGIVHTQA--GYLLYAALTHklvFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFES 319
Cdd:cd05932 141 T-----LIYTSGTTGQPKGVMLTFGsfAWAAQAGIEH---IGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAES 212
|
250 260 270
....*....|....*....|....*....|....*
gi 91993047 320 TPVYPnagrywETVERLKINQFYGAPtavRLLLKY 354
Cdd:cd05932 213 LDTFV------EDVQRARPTLFFSVP---RLWTKF 238
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
96-288 |
1.04e-05 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 47.92 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 96 VRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVIT 175
Cdd:PLN02479 44 VRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEVVMV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 176 fNQglrggrvvELKKIVDEAVK---------HCPTVQHVLVAHRTDNKV---HMGDLDVPLEQEMAKEDPVCAPESMGSE 243
Cdd:PLN02479 124 -DQ--------EFFTLAEEALKilaekkkssFKPPLLIVIGDPTCDPKSlqyALGKGAIEYEKFLETGDPEFAWKPPADE 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 91993047 244 -DMLFMLYTSGSTGMPKGIV-HTQAGYLLyaALTHKLVFDHQPGDIF 288
Cdd:PLN02479 195 wQSIALGYTSGTTASPKGVVlHHRGAYLM--ALSNALIWGMNEGAVY 239
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
98-172 |
1.08e-05 |
|
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.
Pssm-ID: 341238 [Multi-domain] Cd Length: 411 Bit Score: 47.34 E-value: 1.08e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 91993047 98 ITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKV 172
Cdd:cd05912 2 YTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL 76
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
95-362 |
1.53e-05 |
|
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: 47.04 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 95 EVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVI 174
Cdd:cd05915 22 VHRTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 175 TFNqglrggrvvELKKIVDEAVKhcptvqhvLVAHRTDNKVHMGDLDvPLEQEMAKEDPVCAPESMGSE-DMLFMLYTSG 253
Cdd:cd05915 102 FDP---------NLLPLVEAIRG--------ELKTVQHFVVMDEKAP-EGYLAYEEALGEEADPVRVPErAACGMAYTTG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 254 STGMPKGIVHTQAG-YLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFEstpvYPNAGRYWET 332
Cdd:cd05915 164 TTGLPKGVVYSHRAlVLHSLAASLVDGTALSEKDVVLPVVPMFHVNAWCLPYAATLVGAKQVLPGP----RLDPASLVEL 239
|
250 260 270
....*....|....*....|....*....|
gi 91993047 333 VERLKINQFYGAPTAVRLLLKYGDAWVKKY 362
Cdd:cd05915 240 FDGEGVTFTAGVPTVWLALADYLESTGHRL 269
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
99-174 |
6.00e-05 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 45.12 E-value: 6.00e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 91993047 99 TYRELLETTCRLANTLK-RHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVI 174
Cdd:cd05937 7 TYSETYDLVLRYAHWLHdDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSRFVI 83
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
99-316 |
1.33e-03 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 41.17 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 99 TYRELLETTCRLANTLKrhGVHRGDR---VAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVIT 175
Cdd:PRK13388 28 TWREVLAEAAARAAALI--ALADPDRplhVGVLLGNTPEMLFWLAAAALGGYVLVGLNTTRRGAALAADIRRADCQLLVT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 176 fnqglrggrvvelkkivDEAvkHCPTVQHVLVAhrtdnKVHMGDLDVPLEQEMAKEDPVCAPES-MGSEDMLFMLYTSGS 254
Cdd:PRK13388 106 -----------------DAE--HRPLLDGLDLP-----GVRVLDVDTPAYAELVAAAGALTPHReVDAMDPFMLIFTSGT 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 91993047 255 TGMPKGIVHTQAGYLLYA-ALTHKlvFDHQPGDIFGCVADIgwitGHSYVVY---GP-LCNGATSVL 316
Cdd:PRK13388 162 TGAPKAVRCSHGRLAFAGrALTER--FGLTRDDVCYVSMPL----FHSNAVMagwAPaVASGAAVAL 222
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
241-269 |
5.43e-03 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 39.38 E-value: 5.43e-03
10 20
....*....|....*....|....*....
gi 91993047 241 GSEDMLFMLYTSGSTGMPKGIVHTQAGYL 269
Cdd:PRK05691 3867 GPDNLAYVIYTSGSTGLPKGVMVEQRGML 3895
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
243-380 |
5.83e-03 |
|
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: 39.01 E-value: 5.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 243 EDMLFMLYTSGSTGMPKGIVHTQagyllyaaltHKLVFdhqpgDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPV 322
Cdd:cd05908 106 DELAFIQFSSGSTGDPKGVMLTH----------ENLVH-----NMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPL 170
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 91993047 323 YPNAGRY-------------W-ETVERLKINQFYGAPTAVRLLLK-YGDAWVKKYDRSSLRTLGSVGEPINCE 380
Cdd:cd05908 171 IAGMNQYlmptrlfirrpilWlKKASEHKATIVSSPNFGYKYFLKtLKPEKANDWDLSSIRMILNGAEPIDYE 243
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
248-368 |
8.06e-03 |
|
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: 38.25 E-value: 8.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 248 MLYTSGSTGMPKGIV--HTQAgYLLYAALthklvfdhqpgdifgcvADIGWIT-GHSYVVYGPLCN------GATSVLFE 318
Cdd:cd17638 5 IMFTSGTTGRSKGVMcaHRQT-LRAAAAW-----------------ADCADLTeDDRYLIINPFFHtfgykaGIVACLLT 66
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 91993047 319 STPVYPNA----GRYWETVERLKINQFYGAPTAVRLLLKYGDawVKKYDRSSLR 368
Cdd:cd17638 67 GATVVPVAvfdvDAILEAIERERITVLPGPPTLFQSLLDHPG--RKKFDLSSLR 118
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
249-408 |
8.33e-03 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 38.49 E-value: 8.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 249 LYTSGSTGMPKGIVHTQaGYLLYAALTHKLVFDHQPGDIFGCVAD-IGW--ITGHSYVVYGPLCNGATSVLFESTPVypn 325
Cdd:PRK12582 226 LFTSGSTGMPKAVINTQ-RMMCANIAMQEQLRPREPDPPPPVSLDwMPWnhTMGGNANFNGLLWGGGTLYIDDGKPL--- 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 326 AGRYWETVERLK-INQ--FYGAPTAVRLL---LKYGDAWVKKYdRSSLRTLGSVGEPINCEAWEWLH----RVVGdSRCT 395
Cdd:PRK12582 302 PGMFEETIRNLReISPtvYGNVPAGYAMLaeaMEKDDALRRSF-FKNLRLMAYGGATLSDDLYERMQalavRTTG-HRIP 379
|
170
....*....|...
gi 91993047 396 LVDTWWQTETGGI 408
Cdd:PRK12582 380 FYTGYGATETAPT 392
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
247-364 |
9.30e-03 |
|
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: 38.08 E-value: 9.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91993047 247 FMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVfdhqpgdifGCVADIGW--------ITGHSYVVYGPLCNGATSVLFE 318
Cdd:cd17630 4 TVILTSGSTGTPKAVVHTAANLLASAAGLHSRL---------GFGGGDSWllslplyhVGGLAILVRSLLAGAELVLLER 74
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 91993047 319 STPVYPNAGRYWETVERLkinqfygAPTAVRLLLKYG--DAWVKKYDR 364
Cdd:cd17630 75 NQALAEDLAPPGVTHVSL-------VPTQLQRLLDSGqgPAALKSLRA 115
|
|
| |
