|
Name |
Accession |
Description |
Interval |
E-value |
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
1-398 |
1.13e-112 |
|
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: 337.17 E-value: 1.13e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 1 VEFATAFHGILGAGATVVPLNPLLTEEETRRAVQRTGARLRIdaptaralhagasrplspspatedpeaTAVLALSSGTT 80
Cdd:COG0318 60 PEFVVAFLAALRAGAVVVPLNPRLTAEELAYILEDSGARALV---------------------------TALILYTSGTT 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 81 AEPKPVMLSHRALSANIRQTVSALrgnGLDPGWSVLAPLPLSHIYGLNVLLHSSLANGNHVVLMPRFTPRAFARLHAEHR 160
Cdd:COG0318 113 GRPKGVMLTHRNLLANAAAIAAAL---GLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPRFDPERVLELIERER 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 161 IGWSYVAPPIVAALDSEdysADYSAEDFRHTRVMLSGAADLSPDLARRVGERLGVEIIQGYGMTEASPVTHM----MRRG 236
Cdd:COG0318 190 VTVLFGVPTMLARLLRH---PEFARYDLSSLRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTETSPVVTVnpedPGER 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 237 DPLGIGRPVDGTETRIVG-----------GELWVRGPQLCSGYLGAPG----PLVEGWLPTGDLVAPTPDGGLRVTGRTK 301
Cdd:COG0318 267 RPGSVGRPLPGVEVRIVDedgrelppgevGEIVVRGPNVMKGYWNDPEataeAFRDGWLRTGDLGRLDEDGYLYIVGRKK 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 302 EIIKYRGYQVSPAELEEVIAACPGVRDVAVA------RGtlqgeEVPHAFVV----GTAAPAEVHEWVARRVAPYKKVRR 371
Cdd:COG0318 347 DMIISGGENVYPAEVEEVLAAHPGVAEAAVVgvpdekWG-----ERVVAFVVlrpgAELDAEELRAFLRERLARYKVPRR 421
|
410 420
....*....|....*....|....*..
gi 2713532039 372 VTVVESIPRAATGKILRRRLRERAGDA 398
Cdd:COG0318 422 VEFVDELPRTASGKIDRRALRERYAAG 448
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
1-391 |
1.27e-109 |
|
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: 331.12 E-value: 1.27e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 1 VEFATAFHGILGAGATVVPLNPLLTEEETRRAVQRTGARLRIDAPT-----------------ARALHAGASRPLSPSPA 63
Cdd:cd05904 68 IEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFTTAElaeklaslalpvvlldsAEFDSLSFSDLLFEADE 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 64 TEDPEA------TAVLALSSGTTAEPKPVMLSHRALSANIRQTVsALRGNGLDPGWSVLAPLPLSHIYGLNVLLHSSLAN 137
Cdd:cd05904 148 AEPPVVvikqddVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFV-AGEGSNSDSEDVFLCVLPMFHIYGLSSFALGLLRL 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 138 GNHVVLMPRFTPRAFARLHAEHRIGWSYVAPPIVAALDSEDYSADYsaeDFRHTRVMLSGAADLSPDLARRVGERL-GVE 216
Cdd:cd05904 227 GATVVVMPRFDLEELLAAIERYKVTHLPVVPPIVLALVKSPIVDKY---DLSSLRQIMSGAAPLGKELIEAFRAKFpNVD 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 217 IIQGYGMTEASPVTHMM-----RRGDPLGIGRPVDGTETRIVG------------GELWVRGPQLCSGYLGAP-----GP 274
Cdd:cd05904 304 LGQGYGMTESTGVVAMCfapekDRAKYGSVGRLVPNVEAKIVDpetgeslppnqtGELWIRGPSIMKGYLNNPeataaTI 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 275 LVEGWLPTGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAVARGT-LQGEEVPHAFVV----GT 349
Cdd:cd05904 384 DKEGWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPdEEAGEVPMAFVVrkpgSS 463
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2713532039 350 AAPAEVHEWVARRVAPYKKVRRVTVVESIPRAATGKILRRRL 391
Cdd:cd05904 464 LTEDEIMDFVAKQVAPYKKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
2-392 |
3.76e-101 |
|
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: 307.95 E-value: 3.76e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 2 EFATAFHGILGAGATVVPLNPLLTEEETRRAVQRTGARLRIDA-PTARALHAGASRPLSPSPateDPEATAVLALSSGTT 80
Cdd:cd05936 61 QFPIAYFGALKAGAVVVPLNPLYTPRELEHILNDSGAKALIVAvSFTDLLAAGAPLGERVAL---TPEDVAVLQYTSGTT 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 81 AEPKPVMLSHRALSANIRQTVSALrGNGLDPGWSVLAPLPLSHIYGLNVLLHSSLANGNHVVLMPRFTPRAFARLHAEHR 160
Cdd:cd05936 138 GVPKGAMLTHRNLVANALQIKAWL-EDLLEGDDVVLAALPLFHVFGLTVALLLPLALGATIVLIPRFRPIGVLKEIRKHR 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 161 IGWSYVAPPIVAALDSedySADYSAEDFRHTRVMLSGAADLSPDLARRVGERLGVEIIQGYGMTEASPVTHM--MRRGDP 238
Cdd:cd05936 217 VTIFPGVPTMYIALLN---APEFKKRDFSSLRLCISGGAPLPVEVAERFEELTGVPIVEGYGLTETSPVVAVnpLDGPRK 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 239 LG-IGRPVDGTETRIVG-----------GELWVRGPQLCSGYLGAPGP----LVEGWLPTGDLVAPTPDGGLRVTGRTKE 302
Cdd:cd05936 294 PGsIGIPLPGTEVKIVDddgeelppgevGELWVRGPQVMKGYWNRPEEtaeaFVDGWLRTGDIGYMDEDGYFFIVDRKKD 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 303 IIKYRGYQVSPAELEEVIAACPGVRDVAVA------RGtlqgeEVPHAFVV----GTAAPAEVHEWVARRVAPYKKVRRV 372
Cdd:cd05936 374 MIIVGGFNVYPREVEEVLYEHPAVAEAAVVgvpdpySG-----EAVKAFVVlkegASLTEEEIIAFCREQLAGYKVPRQV 448
|
410 420
....*....|....*....|
gi 2713532039 373 TVVESIPRAATGKILRRRLR 392
Cdd:cd05936 449 EFRDELPKSAVGKILRRELR 468
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
1-387 |
3.52e-97 |
|
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: 298.36 E-value: 3.52e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 1 VEFATAFHGILGAGATVVPLNPLLTEEETRRAVQRTGARL----------------------RI---DAPTARALH---- 51
Cdd:cd05911 46 TYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKViftdpdglekvkeaakelgpkdKIivlDDKPDGVLSiedl 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 52 ----AGASRPLSPSPATEDPEATAVLALSSGTTAEPKPVMLSHRALSANIRQTVSALRGNgLDPGWSVLAPLPLSHIYGL 127
Cdd:cd05911 126 lsptLGEEDEDLPPPLKDGKDDTAAILYSSGTTGLPKGVCLSHRNLIANLSQVQTFLYGN-DGSNDVILGFLPLYHIYGL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 128 NVLLHSsLANGNHVVLMPRFTPRAFARLHAEHRIGWSYVAPPIVAALDSedySADYSAEDFRHTRVMLSGAADLSPDLAR 207
Cdd:cd05911 205 FTTLAS-LLNGATVIIMPKFDSELFLDLIEKYKITFLYLVPPIAAALAK---SPLLDKYDLSSLRVILSGGAPLSKELQE 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 208 RVGERLG-VEIIQGYGMTEASPVTHMMRRGDPLG--IGRPVDGTETRIVG------------GELWVRGPQLCSGYLGAP 272
Cdd:cd05911 281 LLAKRFPnATIKQGYGMTETGGILTVNPDGDDKPgsVGRLLPNVEAKIVDddgkdslgpnepGEICVRGPQVMKGYYNNP 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 273 -----GPLVEGWLPTGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAV-----ARGTlqgeEVP 342
Cdd:cd05911 361 eatkeTFDEDGWLHTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVigipdEVSG----ELP 436
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 2713532039 343 HAFVV----GTAAPAEVHEWVARRVAPYKKVR-RVTVVESIPRAATGKIL 387
Cdd:cd05911 437 RAYVVrkpgEKLTEKEVKDYVAKKVASYKQLRgGVVFVDEIPKSASGKIL 486
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
70-387 |
7.03e-81 |
|
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: 251.44 E-value: 7.03e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 70 TAVLALSSGTTAEPKPVMLSHRALSANIRQTVSALrgnGLDPGWSVLAPLPLSHIYGLNVLLhSSLANGNHVVLMPRFTP 149
Cdd:cd04433 2 PALILYTSGTTGKPKGVVLSHRNLLAAAAALAASG---GLTEGDVFLSTLPLFHIGGLFGLL-GALLAGGTVVLLPKFDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 150 RAFARLHAEHRIGWSYVAPPIVAALDSEDYSADYsaeDFRHTRVMLSGAADLSPDLARRVGERLGVEIIQGYGMTEASPV 229
Cdd:cd04433 78 EAALELIEREKVTILLGVPTLLARLLKAPESAGY---DLSSLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 230 THMMRRGDPLG----IGRPVDGTETRIVG-----------GELWVRGPQLCSGYLGAP----GPLVEGWLPTGDLVAPTP 290
Cdd:cd04433 155 VATGPPDDDARkpgsVGRPVPGVEVRIVDpdggelppgeiGELVVRGPSVMKGYWNNPeataAVDEDGWYRTGDLGRLDE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 291 DGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAV-ARGTLQGEEVPHAFVV----GTAAPAEVHEWVARRVAP 365
Cdd:cd04433 235 DGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVvGVPDPEWGERVVAVVVlrpgADLDAEELRAHVRERLAP 314
|
330 340
....*....|....*....|..
gi 2713532039 366 YKKVRRVTVVESIPRAATGKIL 387
Cdd:cd04433 315 YKVPRRVVFVDALPRTASGKID 336
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
2-394 |
5.35e-74 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 239.42 E-value: 5.35e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 2 EFATAFHGILGAGATVVPLNPLLTEEETRRAVQRTGARLRIDA----PTARALHA-------------GASRPLSPS--- 61
Cdd:PRK07656 67 HWVIAALGALKAGAVVVPLNTRYTADEAAYILARGDAKALFVLglflGVDYSATTrlpalehvvicetEEDDPHTEKmkt 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 62 -------------PATEDPEATAVLALSSGTTAEPKPVMLSHRALSANIRQTVSALrgnGLDPGWSVLAPLPLSHIYGLN 128
Cdd:PRK07656 147 ftdflaagdpaerAPEVDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYL---GLTEGDRYLAANPFFHVFGYK 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 129 VLLHSSLANGNHVVLMPRFTPRAFARLHAEHRIGwSYVAPPIV--AALDSEDYSAdysaEDFRHTRVMLSGAADLSPDLA 206
Cdd:PRK07656 224 AGVNAPLMRGATILPLPVFDPDEVFRLIETERIT-VLPGPPTMynSLLQHPDRSA----EDLSSLRLAVTGAASMPVALL 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 207 RRVGERLGVEII-QGYGMTEASPVTHMMRRGD-----PLGIGRPVDGTETRIVG-----------GELWVRGPQLCSGYL 269
Cdd:PRK07656 299 ERFESELGVDIVlTGYGLSEASGVTTFNRLDDdrktvAGTIGTAIAGVENKIVNelgeevpvgevGELLVRGPNVMKGYY 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 270 GAPGPLVE-----GWLPTGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAV-----ARgtlQGe 339
Cdd:PRK07656 379 DDPEATAAaidadGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVigvpdER---LG- 454
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2713532039 340 EVPHAFVV----GTAAPAEVHEWVARRVAPYKKVRRVTVVESIPRAATGKILRRRLRER 394
Cdd:PRK07656 455 EVGKAYVVlkpgAELTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRALREK 513
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
1-394 |
8.62e-74 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 239.50 E-value: 8.62e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 1 VEFATAFHGILGAGATVVPLNPLLTEEETRRAVQRTGARL-----------------------RIDAPTARALHAGASRP 57
Cdd:PLN02246 86 PEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLiitqscyvdklkglaeddgvtvvTIDDPPEGCLHFSELTQ 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 58 LSPSPATE---DPEATAVLALSSGTTAEPKPVMLSHRALSANIRQTVSALRGN-GLDPGWSVLAPLPLSHIYGLNVLLHS 133
Cdd:PLN02246 166 ADENELPEveiSPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVAQQVDGENPNlYFHSDDVILCVLPMFHIYSLNSVLLC 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 134 SLANGNHVVLMPRFTPRAFARLHAEHRIGWSYVAPPIVAALDSEDYSADYsaeDFRHTRVMLSGAADLSPDLARRVGERL 213
Cdd:PLN02246 246 GLRVGAAILIMPKFEIGALLELIQRHKVTIAPFVPPIVLAIAKSPVVEKY---DLSSIRMVLSGAAPLGKELEDAFRAKL 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 214 GVEII-QGYGMTEASPVTHMMR--RGDPLGI-----GRPVDGTETRIVG------------GELWVRGPQLCSGYLGAPG 273
Cdd:PLN02246 323 PNAVLgQGYGMTEAGPVLAMCLafAKEPFPVksgscGTVVRNAELKIVDpetgaslprnqpGEICIRGPQIMKGYLNDPE 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 274 PL-----VEGWLPTGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAV-ARGTLQGEEVPHAFVV 347
Cdd:PLN02246 403 ATantidKDGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVvPMKDEVAGEVPVAFVV 482
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 2713532039 348 GTA----APAEVHEWVARRVAPYKKVRRVTVVESIPRAATGKILRRRLRER 394
Cdd:PLN02246 483 RSNgseiTEDEIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDLRAK 533
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
1-393 |
4.14e-71 |
|
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: 231.05 E-value: 4.14e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 1 VEFATAFHGILGAGATVVPLNPLLTEEETRRAVQRTGARLRI-----DAPTARALH------------------AGASRP 57
Cdd:cd05926 50 LEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVLtpkgeLGPASRAASklglailelaldvgvlirAPSAES 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 58 LSPSPATE---------DPEATAVLALSSGTTAEPKPVMLSHRALSANIRQTVSALRgngLDPGWSVLAPLPLSHIYGLN 128
Cdd:cd05926 130 LSNLLADKknaksegvpLPDDLALILHTSGTTGRPKGVPLTHRNLAASATNITNTYK---LTPDDRTLVVMPLFHVHGLV 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 129 VLLHSSLANGNHVVLMPRFTPRAFARLHAEHRIGWSYVAPPIVAALdSEDYSADYSAEdFRHTRVMLSGAADLSPDLARR 208
Cdd:cd05926 207 ASLLSTLAAGGSVVLPPRFSASTFWPDVRDYNATWYTAVPTIHQIL-LNRPEPNPESP-PPKLRFIRSCSASLPPAVLEA 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 209 VGERLGVEIIQGYGMTEAS------PVTHMMRRgdPLGIGRPVdGTETRIVG-----------GELWVRGPQLCSGYLGA 271
Cdd:cd05926 285 LEATFGAPVLEAYGMTEAAhqmtsnPLPPGPRK--PGSVGKPV-GVEVRILDedgeilppgvvGEICLRGPNVTRGYLNN 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 272 P-----GPLVEGWLPTGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAVAR--GTLQGEEVpHA 344
Cdd:cd05926 362 PeanaeAAFKDGWFRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGvpDEKYGEEV-AA 440
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2713532039 345 FVV----GTAAPAEVHEWVARRVAPYKKVRRVTVVESIPRAATGKILRRRLRE 393
Cdd:cd05926 441 AVVlregASVTEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
2-394 |
4.47e-70 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 229.30 E-value: 4.47e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 2 EFATAFHGILGAGATVVPLNPLLTEEETRRAVQRTGAR--------------LRIDAPTAR---ALHAGASRPLSP---- 60
Cdd:PRK06187 68 EYLEAYFAVPKIGAVLHPINIRLKPEEIAYILNDAEDRvvlvdsefvpllaaILPQLPTVRtviVEGDGPAAPLAPevge 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 61 --------SPATEDPEA----TAVLALSSGTTAEPKPVMLSHRALSANIRQtvsALRGNGLDPGWSVLAPLPLSHIYGLN 128
Cdd:PRK06187 148 yeellaaaSDTFDFPDIdendAAAMLYTSGTTGHPKGVVLSHRNLFLHSLA---VCAWLKLSRDDVYLVIVPMFHVHAWG 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 129 VLLHSsLANGNHVVLMPRFTPRAFARLHAEHRIGWSYVAPPIVAALDSEDYSADYsaeDFRHTRVMLSGAADLSPDLARR 208
Cdd:PRK06187 225 LPYLA-LMAGAKQVIPRRFDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFV---DFSSLRLVIYGGAALPPALLRE 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 209 VGERLGVEIIQGYGMTEASPVTHMMR--RGDPLGI------GRPVDGTETRIVG-------------GELWVRGPQLCSG 267
Cdd:PRK06187 301 FKEKFGIDLVQGYGMTETSPVVSVLPpeDQLPGQWtkrrsaGRPLPGVEARIVDddgdelppdggevGEIIVRGPWLMQG 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 268 YLGAPGP----LVEGWLPTGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAVArgtlqGE---- 339
Cdd:PRK06187 381 YWNRPEAtaetIDGGWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVI-----GVpdek 455
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2713532039 340 --EVPHAFVVG----TAAPAEVHEWVARRVAPYKKVRRVTVVESIPRAATGKILRRRLRER 394
Cdd:PRK06187 456 wgERPVAVVVLkpgaTLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLREQ 516
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
1-388 |
2.29e-69 |
|
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: 225.18 E-value: 2.29e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 1 VEFATAFHGILGAGATVVPLNPLLTEEETRRAVQRTGARLRIDAPtaralhagasrplspspatedpeatAVLALSSGTT 80
Cdd:cd17631 56 PEFLELLFAAARLGAVFVPLNFRLTPPEVAYILADSGAKVLFDDL-------------------------ALLMYTSGTT 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 81 AEPKPVMLSHRALSANirqTVSALRGNGLDPGWSVLAPLPLSHIYGLNVLLHSSLANGNHVVLMPRFTPRAFARLHAEHR 160
Cdd:cd17631 111 GRPKGAMLTHRNLLWN---AVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVILRKFDPETVLDLIERHR 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 161 IGWSYVAPPIVAALDSEDYSADYsaeDFRHTRVMLSGAADLSPDLARRVGERlGVEIIQGYGMTEASPVTHMMRRGDPLG 240
Cdd:cd17631 188 VTSFFLVPTMIQALLQHPRFATT---DLSSLRAVIYGGAPMPERLLRALQAR-GVKFVQGYGMTETSPGVTFLSPEDHRR 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 241 ----IGRPVDGTETRIVG-----------GELWVRGPQLCSGYLGAP----GPLVEGWLPTGDLVAPTPDGGLRVTGRTK 301
Cdd:cd17631 264 klgsAGRPVFFVEVRIVDpdgrevppgevGEIVVRGPHVMAGYWNRPeataAAFRDGWFHTGDLGRLDEDGYLYIVDRKK 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 302 EIIKYRGYQVSPAELEEVIAACPGVRDVAVArgTLQGE---EVPHAFVV----GTAAPAEVHEWVARRVAPYKKVRRVTV 374
Cdd:cd17631 344 DMIISGGENVYPAEVEDVLYEHPAVAEVAVI--GVPDEkwgEAVVAVVVprpgAELDEDELIAHCRERLARYKIPKSVEF 421
|
410
....*....|....
gi 2713532039 375 VESIPRAATGKILR 388
Cdd:cd17631 422 VDALPRNATGKILK 435
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
1-307 |
2.23e-66 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 216.79 E-value: 2.23e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 1 VEFATAFHGILGAGATVVPLNPLLTEEETRRAVQRTGARLRI--DAPTARALHAGASRPLSPS----------------- 61
Cdd:pfam00501 57 PEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSGAKVLItdDALKLEELLEALGKLEVVKlvlvldrdpvlkeeplp 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 62 ------------PATEDPEATAVLALSSGTTAEPKPVMLSHRALSANIRQTVS-ALRGNGLDPGWSVLAPLPLSHIYGLN 128
Cdd:pfam00501 137 eeakpadvppppPPPPDPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRvRPRGFGLGPDDRVLSTLPLFHDFGLS 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 129 VLLHSSLANGNHVVLMPRFTPRAFARLHA---EHRIGWSYVAPPIVAALDSedySADYSAEDFRHTRVMLSGAADLSPDL 205
Cdd:pfam00501 217 LGLLGPLLAGATVVLPPGFPALDPAALLElieRYKVTVLYGVPTLLNMLLE---AGAPKRALLSSLRLVLSGGAPLPPEL 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 206 ARRVGERLGVEIIQGYGMTEASPVTHMMRRGDPLG-----IGRPVDGTETRIV------------GGELWVRGPQLCSGY 268
Cdd:pfam00501 294 ARRFRELFGGALVNGYGLTETTGVVTTPLPLDEDLrslgsVGRPLPGTEVKIVddetgepvppgePGELCVRGPGVMKGY 373
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 2713532039 269 LGAPG-----PLVEGWLPTGDLVAPTPDGGLRVTGRTKEIIKYR 307
Cdd:pfam00501 374 LNDPEltaeaFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
6-394 |
8.34e-62 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 208.70 E-value: 8.34e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 6 AFHGILGAGATVVPLNPLLTEEETRRAVQRTGAR----------------------------------------LRIDAP 45
Cdd:PRK05605 98 AFYAVLRLGAVVVEHNPLYTAHELEHPFEDHGARvaivwdkvaptverlrrttpletivsvnmiaampllqrlaLRLPIP 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 46 TAR----ALHAGASRPLS---------------PSPATEDPEATAVLALSSGTTAEPKPVMLSHRALSANIRQTVSALRG 106
Cdd:PRK05605 178 ALRkaraALTGPAPGTVPwetlvdaaiggdgsdVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAQGKAWVPG 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 107 NGLDPGwSVLAPLPLSHIYGLNVLLHSSLANGNHVVLMPRFTPRAFARLHAEHRIGWSYVAPPIVAALdsedysADYSAE 186
Cdd:PRK05605 258 LGDGPE-RVLAALPMFHAYGLTLCLTLAVSIGGELVLLPAPDIDLILDAMKKHPPTWLPGVPPLYEKI------AEAAEE 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 187 ---DFRHTRVMLSGAADLSPDLARRVGERLGVEIIQGYGMTEASPVThmmrRGDPLG-------IGRPVDGTETRIV--- 253
Cdd:PRK05605 331 rgvDLSGVRNAFSGAMALPVSTVELWEKLTGGLLVEGYGLTETSPII----VGNPMSddrrpgyVGVPFPDTEVRIVdpe 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 254 ----------GGELWVRGPQLCSGYLGAP----GPLVEGWLPTGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEV 319
Cdd:PRK05605 407 dpdetmpdgeEGELLVRGPQVFKGYWNRPeetaKSFLDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEV 486
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 320 IAACPGVRDVAV-----ARGtlqGEEVPHAFVVGTAA---PAEVHEWVARRVAPYKKVRRVTVVESIPRAATGKILRRRL 391
Cdd:PRK05605 487 LREHPGVEDAAVvglprEDG---SEEVVAAVVLEPGAaldPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRREV 563
|
...
gi 2713532039 392 RER 394
Cdd:PRK05605 564 REE 566
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
1-392 |
6.53e-61 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 206.23 E-value: 6.53e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 1 VEFATAFHGILGAGATVVPLNPLLTEEETRRAVQRTGARL------------------------------RIDAPTARAL 50
Cdd:PLN02574 103 VYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLaftspenveklsplgvpvigvpenydfdskRIEFPKFYEL 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 51 HAGASRPLsPSPATEDPEATAVLaLSSGTTAEPKPVMLSHRALSANIRQTVSALRGNGLDPGWS--VLAPLPLSHIYGLN 128
Cdd:PLN02574 183 IKEDFDFV-PKPVIKQDDVAAIM-YSSGTTGASKGVVLTHRNLIAMVELFVRFEASQYEYPGSDnvYLAALPMFHIYGLS 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 129 VLLHSSLANGNHVVLMPRFTPRAFARLHAEHRIGWSYVAPPIVAALDSEDYSAdySAEDFRHTRVMLSGAADLSPDLARR 208
Cdd:PLN02574 261 LFVVGLLSLGSTIVVMRRFDASDMVKVIDRFKVTHFPVVPPILMALTKKAKGV--CGEVLKSLKQVSCGAAPLSGKFIQD 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 209 VGERLG-VEIIQGYGMTEASPV------THMMRRGDPLGIGRPvdGTETRIVG------------GELWVRGPQLCSGYL 269
Cdd:PLN02574 339 FVQTLPhVDFIQGYGMTESTAVgtrgfnTEKLSKYSSVGLLAP--NMQAKVVDwstgcllppgncGELWIQGPGVMKGYL 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 270 GAPGPLV-----EGWLPTGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAVArGTLQGE--EVP 342
Cdd:PLN02574 417 NNPKATQstidkDGWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVT-AVPDKEcgEIP 495
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 2713532039 343 HAFVV---GTA-APAEVHEWVARRVAPYKKVRRVTVVESIPRAATGKILRRRLR 392
Cdd:PLN02574 496 VAFVVrrqGSTlSQEAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELK 549
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
1-391 |
5.34e-59 |
|
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: 197.70 E-value: 5.34e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 1 VEFATAFHGILGAGATVVPLNPLLTEEETRRAVQRTGARLRIdaptaralhagasrplspspATEDPEATAVLALSSGTT 80
Cdd:cd05935 37 PQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAV--------------------VGSELDDLALIPYTSGTT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 81 AEPKPVMLSHRALSANIRQTVsalRGNGLDPGWSVLAPLPLSHIYGLNVLLHSSLANGNHVVLMPRFTPRAFARLHAEHR 160
Cdd:cd05935 97 GLPKGCMHTHFSAAANALQSA---VWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARWDRETALELIEKYK 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 161 IGWSYVAPPIVAALDSedySADYSAEDFRHTRVMLSGAADLSPDLARRVGERLGVEIIQGYGMTEASPVTHMMRRGDP-- 238
Cdd:cd05935 174 VTFWTNIPTMLVDLLA---TPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTETMSQTHTNPPLRPkl 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 239 --LGIgrPVDGTETRIVG------------GELWVRGPQLCSGYLGAPGPLVEGW--------LPTGDLVAPTPDGGLRV 296
Cdd:cd05935 251 qcLGI--P*FGVDARVIDietgrelppnevGEIVVRGPQIFKGYWNRPEETEESFieikgrrfFRTGDLGYMDEEGYFFF 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 297 TGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAVArGTLQGE--EVPHAFVV------GTAAPAEVHEWVARRVAPYKK 368
Cdd:cd05935 329 VDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVI-SVPDERvgEEVKAFIVlrpeyrGKVTEEDIIEWAREQMAAYKY 407
|
410 420
....*....|....*....|...
gi 2713532039 369 VRRVTVVESIPRAATGKILRRRL 391
Cdd:cd05935 408 PREVEFVDELPRSASGKILWRLL 430
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
2-392 |
1.88e-56 |
|
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: 190.97 E-value: 1.88e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 2 EFATAFHGILGAGATVVPLNPLLTEEETRRAVQRTGARLRIDAPtaralhagasrplspspatedpeatAVLALSSGTTA 81
Cdd:cd05934 40 EFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVVDP-------------------------ASILYTSGTTG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 82 EPKPVMLSHRAL--SAnirqtVSALRGNGLDPGWSVLAPLPLSHIYGLNVLLHSSLANGNHVVLMPRFTPRAFARLHAEH 159
Cdd:cd05934 95 PPKGVVITHANLtfAG-----YYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLPRFSASRFWSDVRRY 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 160 RIGWSYVAPPIVAALdsedYSADYSAEDFRHtRVMLSGAADLSPDLARRVGERLGVEIIQGYGMTE-----ASPVTHMMR 234
Cdd:cd05934 170 GATVTNYLGAMLSYL----LAQPPSPDDRAH-RLRAAYGAPNPPELHEEFEERFGVRLLEGYGMTEtivgvIGPRDEPRR 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 235 rgdPLGIGRPVDGTETRIVG-----------GELWVR---GPQLCSGYLGAPGPLVE----GWLPTGDLVAPTPDGGLRV 296
Cdd:cd05934 245 ---PGSIGRPAPGYEVRIVDddgqelpagepGELVIRglrGWGFFKGYYNMPEATAEamrnGWFHTGDLGYRDADGFFYF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 297 TGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAVA--RGTLQGEEVPHAFVV---GTAAPAEVHEWVARRVAPYKKVRR 371
Cdd:cd05934 322 VDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVavPDEVGEDEVKAVVVLrpgETLDPEELFAFCEGQLAYFKVPRY 401
|
410 420
....*....|....*....|.
gi 2713532039 372 VTVVESIPRAATGKILRRRLR 392
Cdd:cd05934 402 IRFVDDLPKTPTEKVAKAQLR 422
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
2-393 |
6.73e-56 |
|
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: 189.81 E-value: 6.73e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 2 EFATAFHGILGAGATVVPLNPLLTEEETRRAVQRTGARLRIDAptaralhagasrplspspatedpeatAVLALSSGTTA 81
Cdd:cd05941 49 EYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDSEPSLVLDP--------------------------ALILYTSGTTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 82 EPKPVMLSHRALSANIRQTVSALRGNGLDpgwSVLAPLPLSHIYGLNVLLHSSLANGNHVVLMPRFTPRAFARLHAEHRI 161
Cdd:cd05941 103 RPKGVVLTHANLAANVRALVDAWRWTEDD---VLLHVLPLHHVHGLVNALLCPLFAGASVEFLPKFDPKEVAISRLMPSI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 162 GWSYVAPPIVAALdSEDYSADYS------AEDFRHTRVMLSGAADLSPDLARRVGERLGVEIIQGYGMTEASPVTHMMRR 235
Cdd:cd05941 180 TVFMGVPTIYTRL-LQYYEAHFTdpqfarAAAAERLRLMVSGSAALPVPTLEEWEAITGHTLLERYGMTEIGMALSNPLD 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 236 GDPLG--IGRPVDGTETRIVG------------GELWVRGPQLCSGYLGAPGPLVE-----GWLPTGDLVAPTPDGGLRV 296
Cdd:cd05941 259 GERRPgtVGMPLPGVQARIVDeetgeplprgevGEIQVRGPSVFKEYWNKPEATKEeftddGWFKTGDLGVVDEDGYYWI 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 297 TGRTK-EIIKYRGYQVSPAELEEVIAACPGVRDVAV--ARGTLQGEEVPhAFVVG-----TAAPAEVHEWVARRVAPYKK 368
Cdd:cd05941 339 LGRSSvDIIKSGGYKVSALEIERVLLAHPGVSECAVigVPDPDWGERVV-AVVVLragaaALSLEELKEWAKQRLAPYKR 417
|
410 420
....*....|....*....|....*
gi 2713532039 369 VRRVTVVESIPRAATGKILRRRLRE 393
Cdd:cd05941 418 PRRLILVDELPRNAMGKVNKKELRK 442
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
49-396 |
3.98e-55 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 190.74 E-value: 3.98e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 49 ALHAGASRPLSPspATEDPEATAVLALSSGTTAEPKPVMLSHRALSANIRQtVSALRGNGLDPGWSVL-APLPLSHIYGL 127
Cdd:PRK05677 190 ALAKGAGQPVTE--ANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQ-CRALMGSNLNEGCEILiAPLPLYHIYAF 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 128 NVLLHSSLANGNHVVLMPrfTPRAFARLHAEHRiGWSYVA-----PPIVAALDSEDYSAdysaEDFRHTRVMLSGAADLS 202
Cdd:PRK05677 267 TFHCMAMMLIGNHNILIS--NPRDLPAMVKELG-KWKFSGfvglnTLFVALCNNEAFRK----LDFSALKLTLSGGMALQ 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 203 PDLARRVGERLGVEIIQGYGMTEASPVTHMMRRGD-PLG-IGRPVDGTETRIVG-----------GELWVRGPQLCSGYL 269
Cdd:PRK05677 340 LATAERWKEVTGCAICEGYGMTETSPVVSVNPSQAiQVGtIGIPVPSTLCKVIDddgnelplgevGELCVKGPQVMKGYW 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 270 GAPGPLVE-----GWLPTGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAvARGT--LQGEEVP 342
Cdd:PRK05677 420 QRPEATDEildsdGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCA-AIGVpdEKSGEAI 498
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2713532039 343 HAFVVGTAAPA----EVHEWVARRVAPYKKVRRVTVVESIPRAATGKILRRRLRERAG 396
Cdd:PRK05677 499 KVFVVVKPGETltkeQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRRELRDEEL 556
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
1-393 |
1.12e-54 |
|
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: 188.89 E-value: 1.12e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 1 VEFATAFHGILGAGATVVPLNPLLTEEE---------------TRRAVQRTGA--------------RLRIDAPTARALH 51
Cdd:cd17642 80 LQFFLPVIAGLFIGVGVAPTNDIYNEREldhslniskptivfcSKKGLQKVLNvqkklkiiktiiilDSKEDYKGYQCLY 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 52 AGASRPLSP--------SPATEDPEATAVLALSSGTTAEPKPVMLSHRALSANIRQTVSALRGNGLDPGWSVLAPLPLSH 123
Cdd:cd17642 160 TFITQNLPPgfneydfkPPSFDRDEQVALIMNSSGSTGLPKGVQLTHKNIVARFSHARDPIFGNQIIPDTAILTVIPFHH 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 124 IYGLNVLLhSSLANGNHVVLMPRFTPRAFARLHAEHRIGWSYVAPPIVAALDSEDYSADYsaeDFRHTRVMLSGAADLSP 203
Cdd:cd17642 240 GFGMFTTL-GYLICGFRVVLMYKFEEELFLRSLQDYKVQSALLVPTLFAFFAKSTLVDKY---DLSNLHEIASGGAPLSK 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 204 DLARRVGERLGVEII-QGYGMTEASPVTHMMRRGD--PLGIGRPVDGTETRIVG------------GELWVRGPQLCSGY 268
Cdd:cd17642 316 EVGEAVAKRFKLPGIrQGYGLTETTSAILITPEGDdkPGAVGKVVPFFYAKVVDldtgktlgpnerGELCVKGPMIMKGY 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 269 LGAPGP-----LVEGWLPTGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAVArGTLQGE--EV 341
Cdd:cd17642 396 VNNPEAtkaliDKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVA-GIPDEDagEL 474
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2713532039 342 PHAFVV----GTAAPAEVHEWVARRVAPYKKVR-RVTVVESIPRAATGKILRRRLRE 393
Cdd:cd17642 475 PAAVVVleagKTMTEKEVMDYVASQVSTAKRLRgGVKFVDEVPKGLTGKIDRRKIRE 531
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
2-395 |
1.94e-53 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 185.93 E-value: 1.94e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 2 EFATAFHGILGAGATVVPLNPLLTEEETRRAVQRTGARLRI------------------------------DAPTARALH 51
Cdd:PRK08314 73 QFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGARVAIvgselapkvapavgnlrlrhvivaqysdylPAEPEIAVP 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 52 AG--ASRPLS-------------------PSPATEDPEATAVLALSSGTTAEPKPVMLSHRALSANIrqtVSALRGNGLD 110
Cdd:PRK08314 153 AWlrAEPPLQalapggvvawkealaaglaPPPHTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANA---VGSVLWSNST 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 111 PGWSVLAPLPLSHIYGLNVLLHSSLANGNHVVLMPRFTPRAFARLHAEHRIG-WSYVAPPIVAALDSedysADYSAEDFR 189
Cdd:PRK08314 230 PESVVLAVLPLFHVTGMVHSMNAPIYAGATVVLMPRWDREAAARLIERYRVThWTNIPTMVVDFLAS----PGLAERDLS 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 190 HTRVMLSGAADLSPDLARRVGERLGVEIIQGYGMTEASPVTHMMRRGDP----LGIgrPVDGTETRIVG----------- 254
Cdd:PRK08314 306 SLRYIGGGGAAMPEAVAERLKELTGLDYVEGYGLTETMAQTHSNPPDRPklqcLGI--PTFGVDARVIDpetleelppge 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 255 -GELWVRGPQLCSGYLGAPGPLVEG--------WLPTGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPG 325
Cdd:PRK08314 384 vGEIVVHGPQVFKGYWNRPEATAEAfieidgkrFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPA 463
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2713532039 326 VRDVAV--ARGTLQGEEVpHAFVV------GTAAPAEVHEWVARRVAPYKKVRRVTVVESIPRAATGKILRRRLRERA 395
Cdd:PRK08314 464 IQEACViaTPDPRRGETV-KAVVVlrpearGKTTEEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQLQEQE 540
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
1-393 |
3.62e-53 |
|
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: 182.58 E-value: 3.62e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 1 VEFATAFHGILGAGATVVPLNPLLTEEETRRAVQRTGARLRIdAPTAralhAGASRPLspspatEDPEATAVLALSSGTT 80
Cdd:cd05903 37 WEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFV-VPER----FRQFDPA------AMPDAVALLLFTSGTT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 81 AEPKPVMLSHRALSANIRQTVSALrgnGLDPGWSVLAPLPLSHIYGLNVLLHSSLANGNHVVLMPRFTPRAFARLHAEHR 160
Cdd:cd05903 106 GEPKGVMHSHNTLSASIRQYAERL---GLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIWDPDKALALMREHG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 161 IGWSYVAPPIVAALDSedySADYSAEDFRHTRVMLSGAADLSPDLARRVGERLGVEIIQGYGMTEASPVTHMMRRGDPLG 240
Cdd:cd05903 183 VTFMMGATPFLTDLLN---AVEEAGEPLSRLRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECPGAVTSITPAPEDR 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 241 I----GRPVDGTETRIV-----------GGELWVRGPQLCSGYLGAP----GPLVEGWLPTGDLVAPTPDGGLRVTGRTK 301
Cdd:cd05903 260 RlytdGRPLPGVEIKVVddtgatlapgvEGELLSRGPSVFLGYLDRPdltaDAAPEGWFRTGDLARLDEDGYLRITGRSK 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 302 EIIKYRGYQVSPAELEEVIAACPGVRDVAV-----ARgtlQGEEVPhAFVVgTAAPA-----EVHEWVAR-RVAPYKKVR 370
Cdd:cd05903 340 DIIIRGGENIPVLEVEDLLLGHPGVIEAAVvalpdER---LGERAC-AVVV-TKSGAlltfdELVAYLDRqGVAKQYWPE 414
|
410 420
....*....|....*....|...
gi 2713532039 371 RVTVVESIPRAATGKILRRRLRE 393
Cdd:cd05903 415 RLVHVDDLPRTPSGKVQKFRLRE 437
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
2-397 |
1.26e-52 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 183.64 E-value: 1.26e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 2 EFATAFHGILGAGATVVPLNPLLTEEETRRAVQRTGARLRIDAPTARALHAGASRPL----------------------- 58
Cdd:PLN02330 92 EYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTNDTNYGKVKGLGLPVivlgeekiegavnwkelleaadr 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 59 -SPSPATEDPEATAVLAL--SSGTTAEPKPVMLSHRALSANIRQTVSALRGNGLDPgWSVLAPLPLSHIYGLNVLLHSSL 135
Cdd:PLN02330 172 aGDTSDNEEILQTDLCALpfSSGTTGISKGVMLTHRNLVANLCSSLFSVGPEMIGQ-VVTLGLIPFFHIYGITGICCATL 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 136 ANGNHVVLMPRFTPRAFARLHAEHRIGWSYVAPPIVAALDSEDYSADYSAEDFRHTRVMlSGAADLSPDLARRVGERL-G 214
Cdd:PLN02330 251 RNKGKVVVMSRFELRTFLNALITQEVSFAPIVPPIILNLVKNPIVEEFDLSKLKLQAIM-TAAAPLAPELLTAFEAKFpG 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 215 VEIIQGYGMTEASPVThmMRRGDP---LGIGR-----------------PVDGTE-TRIVGGELWVRGPQLCSGYLGAPG 273
Cdd:PLN02330 330 VQVQEAYGLTEHSCIT--LTHGDPekgHGIAKknsvgfilpnlevkfidPDTGRSlPKNTPGELCVRSQCVMQGYYNNKE 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 274 PLV-----EGWLPTGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAVArgTLQGE---EVPHAF 345
Cdd:PLN02330 408 ETDrtideDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVV--PLPDEeagEIPAAC 485
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2713532039 346 VV----GTAAPAEVHEWVARRVAPYKKVRRVTVVESIPRAATGKILRRRLRERAGD 397
Cdd:PLN02330 486 VVinpkAKESEEDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKEKMLS 541
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
2-376 |
4.04e-49 |
|
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: 172.39 E-value: 4.04e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 2 EFATAFHGILGAGATVVPLNPLLTEEETRRAVQRTGARLRIdaptaralhagasrplspspaTEDPEATAVLALSSGTTA 81
Cdd:cd05907 42 EWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALF---------------------VEDPDDLATIIYTSGTTG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 82 EPKPVMLSHRALSANIRQTVSALRgngLDPGWSVLAPLPLSHIYGLNVLLHSSLANGNHVVL----------MPRFTPRA 151
Cdd:cd05907 101 RPKGVMLSHRNILSNALALAERLP---ATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFassaetllddLSEVRPTV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 152 FArlhAEHRIgWSYVAPPIVAALDSEDYSADYSAEDFRHTRVMLSGAADLSPDLARRVgERLGVEIIQGYGMTEASPVTH 231
Cdd:cd05907 178 FL---AVPRV-WEKVYAAIKVKAVPGLKRKLFDLAVGGRLRFAASGGAPLPAELLHFF-RALGIPVYEGYGLTETSAVVT 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 232 MMRRGDPLG--IGRPVDGTETRIV-GGELWVRGPQLCSGYLGAPGPLVE-----GWLPTGDLVAPTPDGGLRVTGRTKEI 303
Cdd:cd05907 253 LNPPGDNRIgtVGKPLPGVEVRIAdDGEILVRGPNVMLGYYKNPEATAEaldadGWLHTGDLGEIDEDGFLHITGRKKDL 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 304 IKYR-GYQVSPAELEEVIAACPGVRDVAV------------------ARGTLQGEEVPHAFVVGTAAPAEVHEWVARRV- 363
Cdd:cd05907 333 IITSgGKNISPEPIENALKASPLISQAVVigdgrpflvalivpdpeaLEAWAEEHGIAYTDVAELAANPAVRAEIEAAVe 412
|
410
....*....|....*....
gi 2713532039 364 ------APYKKVRRVTVVE 376
Cdd:cd05907 413 aanarlSRYEQIKKFLLLP 431
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
1-393 |
1.14e-48 |
|
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: 170.22 E-value: 1.14e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 1 VEFATAFHGILGAGATVVPLNPLLTEEETRRAVQRTGARLridaptaralhagasrplspspatedpEATAVLALSSGTT 80
Cdd:cd05912 37 IEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL---------------------------DDIATIMYTSGTT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 81 AEPKPVMLSHRALSANIRQTVSALrgnGLDPGWSVLAPLPLSHIYGLNVLLHSsLANGNHVVLMPRFTPRAFARLHAEHR 160
Cdd:cd05912 90 GKPKGVQQTFGNHWWSAIGSALNL---GLTEDDNWLCALPLFHISGLSILMRS-VIYGMTVYLVDKFDAEQVLHLINSGK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 161 IGWSYVAPPIVAALdSEDYSADYSAedfrHTRVMLSGAADLSPDLARRVGERlGVEIIQGYGMTEA-------SPVTHMM 233
Cdd:cd05912 166 VTIISVVPTMLQRL-LEILGEGYPN----NLRCILLGGGPAPKPLLEQCKEK-GIPVYQSYGMTETcsqivtlSPEDALN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 234 RRGDplgIGRPVDGTETRIVG--------GELWVRGPQLCSGYLGAPGP----LVEGWLPTGDLVAPTPDGGLRVTGRTK 301
Cdd:cd05912 240 KIGS---AGKPLFPVELKIEDdgqppyevGEILLKGPNVTKGYLNRPDAteesFENGWFKTGDIGYLDEEGFLYVLDRRS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 302 EIIKYRGYQVSPAELEEVIAACPGVRDVAVArgtlqGEE------VPHAFVVG--TAAPAEVHEWVARRVAPYKKVRRVT 373
Cdd:cd05912 317 DLIISGGENIYPAEIEEVLLSHPAIKEAGVV-----GIPddkwgqVPVAFVVSerPISEEELIAYCSEKLAKYKVPKKIY 391
|
410 420
....*....|....*....|
gi 2713532039 374 VVESIPRAATGKILRRRLRE 393
Cdd:cd05912 392 FVDELPRTASGKLLRHELKQ 411
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
6-393 |
2.86e-48 |
|
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: 171.27 E-value: 2.86e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 6 AFHGILGAGATVVPLNPLLTEEE--------------TRRAVQRTGARLRIDAPTARALHAGASRPLSPSP--------- 62
Cdd:cd12119 66 LYYAVPGMGAVLHTINPRLFPEQiayiinhaedrvvfVDRDFLPLLEAIAPRLPTVEHVVVMTDDAAMPEPagvgvlaye 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 63 ---ATEDPE---------ATAVLALSSGTTAEPKPVMLSHRALsanIRQTVSALR--GNGLDPGWSVLAPLPLSHIYGLN 128
Cdd:cd12119 146 ellAAESPEydwpdfdenTAAAICYTSGTTGNPKGVVYSHRSL---VLHAMAALLtdGLGLSESDVVLPVVPMFHVNAWG 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 129 VLLHSSLANGNHVVLMPRFTPRAFARLHAEHRIGWSYVAPPIVAALDSEDYSADYsaeDFRHTRVMLSGAADLSPDLARR 208
Cdd:cd12119 223 LPYAAAMVGAKLVLPGPYLDPASLAELIEREGVTFAAGVPTVWQGLLDHLEANGR---DLSSLRRVVIGGSAVPRSLIEA 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 209 VgERLGVEIIQGYGMTEASPVTHMMRRGDPLG-------------IGRPVDGTETRIVG-------------GELWVRGP 262
Cdd:cd12119 300 F-EERGVRVIHAWGMTETSPLGTVARPPSEHSnlsedeqlalrakQGRPVPGVELRIVDddgrelpwdgkavGELQVRGP 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 263 QLCSGYLGAPGP----LVEGWLPTGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAV-ARGTLQ 337
Cdd:cd12119 379 WVTKSYYKNDEEsealTEDGWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAViGVPHPK 458
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 338 GEEVPHAFVV----GTAAPAEVHEWVARRVAPYKKVRRVTVVESIPRAATGKILRRRLRE 393
Cdd:cd12119 459 WGERPLAVVVlkegATVTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
1-391 |
1.30e-47 |
|
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: 168.09 E-value: 1.30e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 1 VEFATAFHGILGAGATVVPLNPLLTEEETRRAVQRTGARLRIDaptaralhagasrplspspateDPEATAVLALSSGTT 80
Cdd:cd05930 48 LEMVVAILAVLKAGAAYVPLDPSYPAERLAYILEDSGAKLVLT----------------------DPDDLAYVIYTSGST 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 81 AEPKPVMLSHRALSANIRQTVSALrgnGLDPGWSVLAPLPLSHIYGLNVLLhSSLANGNHVVLMPRFT---PRAFARLHA 157
Cdd:cd05930 106 GKPKGVMVEHRGLVNLLLWMQEAY---PLTPGDRVLQFTSFSFDVSVWEIF-GALLAGATLVVLPEEVrkdPEALADLLA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 158 EHRIGWSYVAPPIVAALDSEDYSADYSAEDfrhtRVMLSGAAdLSPDLARRVGERL-GVEIIQGYGMTEAS------PVT 230
Cdd:cd05930 182 EEGITVLHLTPSLLRLLLQELELAALPSLR----LVLVGGEA-LPPDLVRRWRELLpGARLVNLYGPTEATvdatyyRVP 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 231 HMMRRGDPLGIGRPVDGTETRIVG-----------GELWVRGPQLCSGYLGAPGPLVEGWLP-----------TGDLVAP 288
Cdd:cd05930 257 PDDEEDGRVPIGRPIPNTRVYVLDenlrpvppgvpGELYIGGAGLARGYLNRPELTAERFVPnpfgpgermyrTGDLVRW 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 289 TPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAV-ARGTLQGEEVPHAFVVGTAAP----AEVHEWVARRV 363
Cdd:cd05930 337 LPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVvAREDGDGEKRLVAYVVPDEGGeldeEELRAHLAERL 416
|
410 420
....*....|....*....|....*...
gi 2713532039 364 APYKKVRRVTVVESIPRAATGKILRRRL 391
Cdd:cd05930 417 PDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
3-400 |
5.00e-47 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 168.19 E-value: 5.00e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 3 FATAFHGILGAGATVVPLNPLLTEEETRRAVQRTGARLRIDAPT-----------------------------------A 47
Cdd:PRK08316 74 YALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAFLVDPAlaptaeaalallpvdtlilslvlggreapggwldfA 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 48 RALHAGASRPLSPSPATEDPeatAVLALSSGTTAEPKPVMLSHRALsanIRQTVSALRGNGLDPGWSVLAPLPLSHIYGL 127
Cdd:PRK08316 154 DWAEAGSVAEPDVELADDDL---AQILYTSGTESLPKGAMLTHRAL---IAEYVSCIVAGDMSADDIPLHALPLYHCAQL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 128 NVLLHSSLANGNHVVLMPRFTPRAFARLHAEHRIGwSYVAPPIV--AALDSedysADYSAEDFRHTRVMLSGAADLSPDL 205
Cdd:PRK08316 228 DVFLGPYLYVGATNVILDAPDPELILRTIEAERIT-SFFAPPTVwiSLLRH----PDFDTRDLSSLRKGYYGASIMPVEV 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 206 ARRVGERL-GVEIIQGYGMTEASPVTHMMRRGDPLG----IGRPVDGTETRIVG-----------GELWVRGPQLCSGYL 269
Cdd:PRK08316 303 LKELRERLpGLRFYNCYGQTEIAPLATVLGPEEHLRrpgsAGRPVLNVETRVVDddgndvapgevGEIVHRSPQLMLGYW 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 270 GAPGPLVE----GWLPTGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAVArgtlqgeEVPH-- 343
Cdd:PRK08316 383 DDPEKTAEafrgGWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVI-------GLPDpk 455
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2713532039 344 ------AFVV----GTAAPAEVHEWVARRVAPYKKVRRVTVVESIPRAATGKILRRRLRERAGDADE 400
Cdd:PRK08316 456 wieavtAVVVpkagATVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKRELRERYAGAFT 522
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
1-392 |
1.35e-46 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 165.93 E-value: 1.35e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 1 VEFATAFHGILGAGATVVPLNPLLTEEETRRAVQRTGARLRIDAPTAralhAGASRPLSP---------SPATEDPEATA 71
Cdd:PRK07787 56 LATVLAVVGALIAGVPVVPVPPDSGVAERRHILADSGAQAWLGPAPD----DPAGLPHVPvrlharswhRYPEPDPDAPA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 72 VLALSSGTTAEPKPVMLSHRALSANIRQTVSALRGNGLDpgwsVLA-PLPLSHIYGLNVLLHSSLANGNHVVLMPRFTPR 150
Cdd:PRK07787 132 LIVYTSGTTGPPKGVVLSRRAIAADLDALAEAWQWTADD----VLVhGLPLFHVHGLVLGVLGPLRIGNRFVHTGRPTPE 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 151 AFARlhAEHRIGWSYVAPPIVAALDSEDYSAdysAEDFRHTRVMLSGAADLSPDLARRVGERLGVEIIQGYGMTEASPVT 230
Cdd:PRK07787 208 AYAQ--ALSEGGTLYFGVPTVWSRIAADPEA---ARALRGARLLVSGSAALPVPVFDRLAALTGHRPVERYGMTETLITL 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 231 HMMRRGD--PLGIGRPVDGTETRIVG-------------GELWVRGPQLCSGYLGAPGPLVE-----GWLPTGDLVAPTP 290
Cdd:PRK07787 283 STRADGErrPGWVGLPLAGVETRLVDedggpvphdgetvGELQVRGPTLFDGYLNRPDATAAaftadGWFRTGDVAVVDP 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 291 DGGLRVTGR-TKEIIKYRGYQVSPAELEEVIAACPGVRDVAVArgtlqGEEVPH------AFVVGT--AAPAEVHEWVAR 361
Cdd:PRK07787 363 DGMHRIVGReSTDLIKSGGYRIGAGEIETALLGHPGVREAAVV-----GVPDDDlgqrivAYVVGAddVAADELIDFVAQ 437
|
410 420 430
....*....|....*....|....*....|.
gi 2713532039 362 RVAPYKKVRRVTVVESIPRAATGKILRRRLR 392
Cdd:PRK07787 438 QLSVHKRPREVRFVDALPRNAMGKVLKKQLL 468
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
31-397 |
3.97e-46 |
|
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: 166.09 E-value: 3.97e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 31 RAVQRTGARLRI-----DAPTARALHAGASRPLSPSPATEDPEATAVLALSSGTTAEPKPVMLSHRALSANIRQTVSALr 105
Cdd:COG1021 142 RELQAEVPSLRHvlvvgDAGEFTSLDALLAAPADLSEPRPDPDDVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEIC- 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 106 gnGLDPGWSVLAPLPLSHIYGLnvllhSS------LANGNHVVLMPRFTP-RAFArLHAEHRIGWSYVAPPIVAA-LDSe 177
Cdd:COG1021 221 --GLDADTVYLAALPAAHNFPL-----SSpgvlgvLYAGGTVVLAPDPSPdTAFP-LIERERVTVTALVPPLALLwLDA- 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 178 dysADYSAEDFRHTRVMLSGAADLSPDLARRVGERLGVEIIQGYGMTEAsPVThMMRRGDPLGI-----GRPV-DGTETR 251
Cdd:COG1021 292 ---AERSRYDLSSLRVLQVGGAKLSPELARRVRPALGCTLQQVFGMAEG-LVN-YTRLDDPEEVilttqGRPIsPDDEVR 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 252 IVG-----------GELWVRGPQLCSGYLGAPG-------PlvEGWLPTGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSP 313
Cdd:COG1021 367 IVDedgnpvppgevGELLTRGPYTIRGYYRAPEhnaraftP--DGFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAA 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 314 AELEEVIAACPGVRDVAVA--RGTLQGEEVpHAFVVGTAAP---AEVHEWVARR-VAPYKKVRRVTVVESIPRAATGKIL 387
Cdd:COG1021 445 EEVENLLLAHPAVHDAAVVamPDEYLGERS-CAFVVPRGEPltlAELRRFLRERgLAAFKLPDRLEFVDALPLTAVGKID 523
|
410
....*....|
gi 2713532039 388 RRRLRERAGD 397
Cdd:COG1021 524 KKALRAALAA 533
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
1-399 |
1.05e-45 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 165.28 E-value: 1.05e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 1 VEFATAFHGILGAGATVVPLNPLLTEEETRRAVQRTGARL-----------------------RIDAPTAR--------- 48
Cdd:COG0365 75 PEAVIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVlitadgglrggkvidlkekvdeaLEELPSLEhvivvgrtg 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 49 ------------ALHAGASRPLSPSP-ATEDPeatAVLALSSGTTAEPKPVMLSHRALSANIRQTVSA---LRGNGL--- 109
Cdd:COG0365 155 advpmegdldwdELLAAASAEFEPEPtDADDP---LFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYvldLKPGDVfwc 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 110 --DPGWsvlaplplshIYGLNVLLHSSLANGNHVVLM---PRF-TPRAFARLHAEHRIGWSYVAPPIVAAL--DSEDYSA 181
Cdd:COG0365 232 taDIGW----------ATGHSYIVYGPLLNGATVVLYegrPDFpDPGRLWELIEKYGVTVFFTAPTAIRALmkAGDEPLK 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 182 DYsaeDFRHTRVMLSGAADLSPDLARRVGERLGVEIIQGYGMTEaspVTHMM---RRGDPL--G-IGRPVDGTETRIV-- 253
Cdd:COG0365 302 KY---DLSSLRLLGSAGEPLNPEVWEWWYEAVGVPIVDGWGQTE---TGGIFisnLPGLPVkpGsMGKPVPGYDVAVVde 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 254 ---------GGELWVRGPQ--LCSGYLGAPG-------PLVEGWLPTGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAE 315
Cdd:COG0365 376 dgnpvppgeEGELVIKGPWpgMFRGYWNDPEryretyfGRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAE 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 316 LEEVIAACPGVRDVAVA------RGtlqgeEVPHAFVV---GTAAP----AEVHEWVARRVAPYKKVRRVTVVESIPRAA 382
Cdd:COG0365 456 IESALVSHPAVAEAAVVgvpdeiRG-----QVVKAFVVlkpGVEPSdelaKELQAHVREELGPYAYPREIEFVDELPKTR 530
|
490
....*....|....*..
gi 2713532039 383 TGKILRRRLRERAGDAD 399
Cdd:COG0365 531 SGKIMRRLLRKIAEGRP 547
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
2-400 |
1.42e-44 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 161.84 E-value: 1.42e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 2 EFATAFHGILGAGATVVPLNPLLTEEETRRAVQRTGARLRIdAPT------------------------------ARALH 51
Cdd:PRK06087 86 EFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFF-APTlfkqtrpvdlilplqnqlpqlqqivgvdklAPATS 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 52 AGA-------SRPLSPSPATEDPEATAVLAlSSGTTAEPKPVMLSHRALSANIRQTVSALRGNGLDpgwSVLAPLPLSHI 124
Cdd:PRK06087 165 SLSlsqiiadYEPLTTAITTHGDELAAVLF-TSGTEGLPKGVMLTHNNILASERAYCARLNLTWQD---VFMMPAPLGHA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 125 YGLNVLLHSSLANGNHVVLMPRFTPRAFARLHAEHRIGWSYVAPPIVAALDSEDYSADYsaeDFRHTRVMLSGAADLSPD 204
Cdd:PRK06087 241 TGFLHGVTAPFLIGARSVLLDIFTPDACLALLEQQRCTCMLGATPFIYDLLNLLEKQPA---DLSALRFFLCGGTTIPKK 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 205 LARRVGERlGVEIIQGYGMTEASPVThMMRRGDPLGI-----GRPVDGTETRIVG-----------GELWVRGPQLCSGY 268
Cdd:PRK06087 318 VARECQQR-GIKLLSVYGSTESSPHA-VVNLDDPLSRfmhtdGYAAAGVEIKVVDearktlppgceGEEASRGPNVFMGY 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 269 LGAPGPLV-----EGWLPTGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAV--ARGTLQGEEV 341
Cdd:PRK06087 396 LDEPELTAraldeEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVvaMPDERLGERS 475
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2713532039 342 PhAFVVGTA-----APAEVHEWVAR-RVAPYKKVRRVTVVESIPRAATGKI--------LRRRLRERAGDADE 400
Cdd:PRK06087 476 C-AYVVLKAphhslTLEEVVAFFSRkRVAKYKYPEHIVVIDKLPRTASGKIqkfllrkdIMRRLTQDVCEEIE 547
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
77-392 |
1.89e-44 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 157.44 E-value: 1.89e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 77 SGTTAEPKPVMLSHRALSANIRQTVSALrgnGLDPGWSVLAPLPLSHIYGLNVLLHSSLANGNHVVLM-PRFTPRAFARL 155
Cdd:cd05917 11 SGTTGSPKGATLTHHNIVNNGYFIGERL---GLTEQDRLCIPVPLFHCFGSVLGVLACLTHGATMVFPsPSFDPLAVLEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 156 HAEHRIGWSYVAPPI-VAALDSEDYSAdysaEDFRHTRVMLSGAADLSPDLARRVGERLGVEIIQ-GYGMTEASPVTHMM 233
Cdd:cd05917 88 IEKEKCTALHGVPTMfIAELEHPDFDK----FDLSSLRTGIMAGAPCPPELMKRVIEVMNMKDVTiAYGMTETSPVSTQT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 234 RRGDPL-----GIGRPVDGTETRIVG------------GELWVRGPQLCSGYLGAPGPLVE-----GWLPTGDLVAPTPD 291
Cdd:cd05917 164 RTDDSIekrvnTVGRIMPHTEAKIVDpeggivppvgvpGELCIRGYSVMKGYWNDPEKTAEaidgdGWLHTGDLAVMDED 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 292 GGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAV-----ARgtlQGEEVPhAFVVGTAAP----AEVHEWVARR 362
Cdd:cd05917 244 GYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVvgvpdER---YGEEVC-AWIRLKEGAelteEDIKAYCKGK 319
|
330 340 350
....*....|....*....|....*....|
gi 2713532039 363 VAPYKKVRRVTVVESIPRAATGKILRRRLR 392
Cdd:cd05917 320 IAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
1-395 |
3.15e-44 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 161.14 E-value: 3.15e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 1 VEFATAFHGILGAGATVVPLNPLLTEEETRRAVQRTGAR----------------------LRIDA------PTA----- 47
Cdd:PRK12492 86 LQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKDSGARalvylnmfgklvqevlpdtgieYLIEAkmgdllPAAkgwlv 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 48 -----------------------RALHAGASRPLSPSPATEDPeaTAVLALSSGTTAEPKPVMLSHRALSANIRQTVSAL 104
Cdd:PRK12492 166 ntvvdkvkkmvpayhlpqavpfkQALRQGRGLSLKPVPVGLDD--IAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACL 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 105 RGNGLD------PGWSVL-APLPLSHIYGLNVLLHSSLANGNHVVLM--PRFTPRAFARLHAehrigWSYVA-----PPI 170
Cdd:PRK12492 244 SQLGPDgqplmkEGQEVMiAPLPLYHIYAFTANCMCMMVSGNHNVLItnPRDIPGFIKELGK-----WRFSAllglnTLF 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 171 VAALDSedysADYSAEDFRHTRVMLSGAADLSPDLARRVGERLGVEIIQGYGMTEASPVTHMMRRGDP--LG-IGRPVDG 247
Cdd:PRK12492 319 VALMDH----PGFKDLDFSALKLTNSGGTALVKATAERWEQLTGCTIVEGYGLTETSPVASTNPYGELarLGtVGIPVPG 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 248 TETRIVG-----------GELWVRGPQLCSGYLGAPGPLV-----EGWLPTGDLVAPTPDGGLRVTGRTKEIIKYRGYQV 311
Cdd:PRK12492 395 TALKVIDddgnelplgerGELCIKGPQVMKGYWQQPEATAealdaEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNV 474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 312 SPAELEEVIAACPGVRDVAV--ARGTLQGEEVpHAFVV---GTAAPAEVHEWVARRVAPYKKVRRVTVVESIPRAATGKI 386
Cdd:PRK12492 475 YPNEIEDVVMAHPKVANCAAigVPDERSGEAV-KLFVVardPGLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKI 553
|
....*....
gi 2713532039 387 LRRRLRERA 395
Cdd:PRK12492 554 LRRELRDIA 562
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
69-395 |
3.22e-44 |
|
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: 155.95 E-value: 3.22e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 69 ATAVLALSSGTTAEPKPVMLSHRALSANIRQTVSALrgnGLDPGWSVLAPLPLSHIYGLNVLLHSSLANGNHVVLMPRft 148
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRL---GFGGGDSWLLSLPLYHVGGLAILVRSLLAGAELVLLERN-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 149 pRAFARLHAEHRIGW-SYVAPPIVAALDSedysaDYSAEDFRHTRVMLSGAADLSPDLARRVGERlGVEIIQGYGMTE-A 226
Cdd:cd17630 76 -QALAEDLAPPGVTHvSLVPTQLQRLLDS-----GQGPAALKSLRAVLLGGAPIPPELLERAADR-GIPLYTTYGMTEtA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 227 SPVTHMMRRGDPLG-IGRPVDGTETRIV-GGELWVRGPQLCSGYLGAPGPLV---EGWLPTGDLVAPTPDGGLRVTGRTK 301
Cdd:cd17630 149 SQVATKRPDGFGRGgVGVLLPGRELRIVeDGEIWVGGASLAMGYLRGQLVPEfneDGWFTTKDLGELHADGRLTVLGRAD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 302 EIIKYRGYQVSPAELEEVIAACPGVRD---VAVARGTLQgeEVPHAFVVG--TAAPAEVHEWVARRVAPYKKVRRVTVVE 376
Cdd:cd17630 229 NMIISGGENIQPEEIEAALAAHPAVRDafvVGVPDEELG--QRPVAVIVGrgPADPAELRAWLKDKLARFKLPKRIYPVP 306
|
330
....*....|....*....
gi 2713532039 377 SIPRAATGKILRRRLRERA 395
Cdd:cd17630 307 ELPRTGGGKVDRRALRAWL 325
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
70-388 |
3.44e-44 |
|
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: 156.12 E-value: 3.44e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 70 TAVLALSSGTTAEPKPVMLSHRalsanirQTVSALRGngldpgWSVLAPL----------PLSHIYGLNVLLHSSLANGN 139
Cdd:cd17638 2 VSDIMFTSGTTGRSKGVMCAHR-------QTLRAAAA------WADCADLteddryliinPFFHTFGYKAGIVACLLTGA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 140 HVVLMPRFTPRAFARLHAEHRIGWSYVAPPIVAALDSEDYSADYsaeDFRHTRVMLSGAADLSPDLARRVGERLGVEII- 218
Cdd:cd17638 69 TVVPVAVFDVDAILEAIERERITVLPGPPTLFQSLLDHPGRKKF---DLSSLRAAVTGAATVPVELVRRMRSELGFETVl 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 219 QGYGMTEASPVThMMRRGDPL-----GIGRPVDGTETRIVG-GELWVRGPQLCSGYLGAPGPLVE-----GWLPTGDLVA 287
Cdd:cd17638 146 TAYGLTEAGVAT-MCRPGDDAetvatTCGRACPGFEVRIADdGEVLVRGYNVMQGYLDDPEATAEaidadGWLHTGDVGE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 288 PTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAVArGTLQGE--EVPHAFVVG----TAAPAEVHEWVAR 361
Cdd:cd17638 225 LDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVI-GVPDERmgEVGKAFVVArpgvTLTEEDVIAWCRE 303
|
330 340
....*....|....*....|....*..
gi 2713532039 362 RVAPYKKVRRVTVVESIPRAATGKILR 388
Cdd:cd17638 304 RLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
1-391 |
4.85e-44 |
|
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 162605 [Multi-domain] Cd Length: 436 Bit Score: 158.38 E-value: 4.85e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 1 VEFATAFHGILGAGATVVPLNPLLTEEETRRAVQRTGARLRIDAP-------TARALH---AGASRPLSPSPATEDpEAT 70
Cdd:TIGR01923 35 IEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDSlleekdfQADSLDrieAAGRYETSLSASFNM-DQI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 71 AVLALSSGTTAEPKPVMLSHRALSANIRQTVSALrgnGLDPGWSVLAPLPLSHIYGLNVLLHSsLANGNHVVLMPRFTpr 150
Cdd:TIGR01923 114 ATLMFTSGTTGKPKAVPHTFRNHYASAVGSKENL---GFTEDDNWLLSLPLYHISGLSILFRW-LIEGATLRIVDKFN-- 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 151 AFARLHAEHRIGWSYVAPPIVAALdsedysADYSAEDFRHTRVMLSGAAdLSPDLARRVGERlGVEIIQGYGMTE-ASPV 229
Cdd:TIGR01923 188 QLLEMIANERVTHISLVPTQLNRL------LDEGGHNENLRKILLGGSA-IPAPLIEEAQQY-GLPIYLSYGMTEtCSQV 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 230 THMMRRGDP--LGIGRPVDGTETRI------VGGELWVRGPQLCSGYLGaPGPLVE-----GWLPTGDLVAPTPDGGLRV 296
Cdd:TIGR01923 260 TTATPEMLHarPDVGRPLAGREIKIkvdnkeGHGEIMVKGANLMKGYLY-QGELTPafeqqGWFNTGDIGELDGEGFLYV 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 297 TGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAVArGTLQGE--EVPHAFVVGTAAP--AEVHEWVARRVAPYKKVRRV 372
Cdd:TIGR01923 339 LGRRDDLIISGGENIYPEEIETVLYQHPGIQEAVVV-PKPDAEwgQVPVAYIVSESDIsqAKLIAYLTEKLAKYKVPIAF 417
|
410
....*....|....*....
gi 2713532039 373 TVVESIPRAATGKILRRRL 391
Cdd:TIGR01923 418 EKLDELPYNASGKILRNQL 436
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
1-392 |
5.01e-44 |
|
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: 159.84 E-value: 5.01e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 1 VEFATAFHGILGAGATVVPLNPLLTEEETRRAVQRTGAR---------------LRIDAPTARAL-HAGASRPLSP---- 60
Cdd:cd05959 65 VDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARvvvvsgelapvlaaaLTKSEHTLVVLiVSGGAGPEAGalll 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 61 -----------SPATEDPEATAVLALSSGTTAEPKPVMLSHralsANIRQTVSALRGN--GLDPGWSVLAPLPLSHIYGL 127
Cdd:cd05959 145 aelvaaeaeqlKPAATHADDPAFWLYSSGSTGRPKGVVHLH----ADIYWTAELYARNvlGIREDDVCFSAAKLFFAYGL 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 128 NVLLHSSLANGNHVVLMP-RFTPRAFARLHAEHRIGWSYVAPPIVAALDSedySADYSAEDFRHTRVMLSGAADLSPDLA 206
Cdd:cd05959 221 GNSLTFPLSVGATTVLMPeRPTPAAVFKRIRRYRPTVFFGVPTLYAAMLA---APNLPSRDLSSLRLCVSAGEALPAEVG 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 207 RRVGERLGVEIIQGYGMTEASPVTHMMRRGD--PLGIGRPVDGTETRIVG-----------GELWVRGPQLCSGYLGAPG 273
Cdd:cd05959 298 ERWKARFGLDILDGIGSTEMLHIFLSNRPGRvrYGTTGKPVPGYEVELRDedggdvadgepGELYVRGPSSATMYWNNRD 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 274 P----LVEGWLPTGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAV-ARGTLQGEEVPHAFVV- 347
Cdd:cd05959 378 KtrdtFQGEWTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVvGVEDEDGLTKPKAFVVl 457
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 2713532039 348 ------GTAAPAEVHEWVARRVAPYKKVRRVTVVESIPRAATGKILRRRLR 392
Cdd:cd05959 458 rpgyedSEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
2-395 |
8.55e-44 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 160.21 E-value: 8.55e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 2 EFATAFHGILGAGATVVPLNPLLTEEETRRAVQRTGARLRI-------------------------------DAPT---- 46
Cdd:PRK06178 95 QFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLaldqlapvveqvraetslrhvivtsladvlpAEPTlplp 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 47 -----ARALHAGASRPLS-------PSPATE-DPEATAVLALSSGTTAEPKPVMLSHRAL--SANIRQTVSALRGNGLdp 111
Cdd:PRK06178 175 dslraPRLAAAGAIDLLPalractaPVPLPPpALDALAALNYTGGTTGMPKGCEHTQRDMvyTAAAAYAVAVVGGEDS-- 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 112 gwSVLAPLPLSHIYGLNVLLHSSLANGNHVVLMPRFTPRAFARLHAEHRIGWSYVAPPIVAALDSEDYSADYSAEDFRHT 191
Cdd:PRK06178 253 --VFLSFLPEFWIAGENFGLLFPLFSGATLVLLARWDAVAFMAAVERYRVTRTVMLVDNAVELMDHPRFAEYDLSSLRQV 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 192 RVMlSGAADLSPDLARRVGERLGVEIIQG-YGMTEaspvTH-------------MMRRGDPLGIGRPVDGTETRIVG--- 254
Cdd:PRK06178 331 RVV-SFVKKLNPDYRQRWRALTGSVLAEAaWGMTE----THtcdtftagfqdddFDLLSQPVFVGLPVPGTEFKICDfet 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 255 ---------GELWVRGPQLCSGYLGAP----GPLVEGWLPTGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIA 321
Cdd:PRK06178 406 gellplgaeGEIVVRTPSLLKGYWNKPeataEALRDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLG 485
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2713532039 322 ACPGVRDVAV-ARGTLQGEEVPHAFVV----GTAAPAEVHEWVARRVAPYkKVRRVTVVESIPRAATGKILRRRLRERA 395
Cdd:PRK06178 486 QHPAVLGSAVvGRPDPDKGQVPVAFVQlkpgADLTAAALQAWCRENMAVY-KVPEIRIVDALPMTATGKVRKQDLQALA 563
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
1-391 |
9.52e-44 |
|
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: 158.52 E-value: 9.52e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 1 VEFATAFHGILGAGATVVPLNPLLTEEETRRAVQRTGARLRIDAPTARALHAG-----------ASRPLSPSPATEDPEA 69
Cdd:cd12117 58 PELVVALLAVLKAGAAYVPLDPELPAERLAFMLADAGAKVLLTDRSLAGRAGGlevavvidealDAGPAGNPAVPVSPDD 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 70 TAVLALSSGTTAEPKPVMLSHRalsaNIRQTVsalrgngLDPGWSVLAPlplshiyGLNVLLHSSLA------------- 136
Cdd:cd12117 138 LAYVMYTSGSTGRPKGVAVTHR----GVVRLV-------KNTNYVTLGP-------DDRVLQTSPLAfdastfeiwgall 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 137 NGNHVVLMPR---FTPRAFARLHAEHRIGWSYVAPPIVAALdsedysADYSAEDFRHTRVMLSGAADLSPDLARRVGERL 213
Cdd:cd12117 200 NGARLVLAPKgtlLDPDALGALIAEEGVTVLWLTAALFNQL------ADEDPECFAGLRELLTGGEVVSPPHVRRVLAAC 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 214 -GVEIIQGYGMTE------ASPVTHMMRRGDPLGIGRPVDGTETRIVG-----------GELWVRGPQLCSGYLGAPGPL 275
Cdd:cd12117 274 pGLRLVNGYGPTEnttfttSHVVTELDEVAGSIPIGRPIANTRVYVLDedgrpvppgvpGELYVGGDGLALGYLNRPALT 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 276 VEGWLP-----------TGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAV-ARGTLQGEEVPH 343
Cdd:cd12117 354 AERFVAdpfgpgerlyrTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVvVREDAGGDKRLV 433
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 2713532039 344 AFVVGTAA--PAEVHEWVARRVAPYKKVRRVTVVESIPRAATGKILRRRL 391
Cdd:cd12117 434 AYVVAEGAldAAELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
1-397 |
1.59e-43 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 158.10 E-value: 1.59e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 1 VEFATAFHGILGAGATVVPLNPLLTEEETRRAVQRTGARLRIDAPTARAL------HAGASRPL-----------SPSPA 63
Cdd:PRK06839 64 LEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTTVLFVEKTFQNMalsmqkVSYVQRVIsitslkeiedrKIDNF 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 64 TEDPE-ATAVLALSSGTTAEPKPVMLSHRALSANIRQTVSALRGNGLDpgwSVLAPLPLSHIYGLNVLLHSSLANGNHVV 142
Cdd:PRK06839 144 VEKNEsASFIICYTSGTTGKPKGAVLTQENMFWNALNNTFAIDLTMHD---RSIVLLPLFHIGGIGLFAFPTLFAGGVII 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 143 LMPRFTPRAFARLHAEHRIGWSYVAPPIVAALDSedySADYSAEDFRHTRVMLSGAADLSPDLARRVGERlGVEIIQGYG 222
Cdd:PRK06839 221 VPRKFEPTKALSMIEKHKVTVVMGVPTIHQALIN---CSKFETTNLQSVRWFYNGGAPCPEELMREFIDR-GFLFGQGFG 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 223 MTEASPVTHMMRRGD----PLGIGRPVDGTETRIVG-----------GELWVRGPQLCSGYLGAPGPLVE----GWLPTG 283
Cdd:PRK06839 297 MTETSPTVFMLSEEDarrkVGSIGKPVLFCDYELIDenknkvevgevGELLIRGPNVMKEYWNRPDATEEtiqdGWLCTG 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 284 DLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAV-ARGTLQGEEVPHAFVV----GTAAPAEVHEW 358
Cdd:PRK06839 377 DLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVvGRQHVKWGEIPIAFIVkkssSVLIEKDVIEH 456
|
410 420 430
....*....|....*....|....*....|....*....
gi 2713532039 359 VARRVAPYKKVRRVTVVESIPRAATGKILRRRLRERAGD 397
Cdd:PRK06839 457 CRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVNQLKS 495
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
1-331 |
2.20e-43 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 159.50 E-value: 2.20e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 1 VEFATAFHGILGAGATVVPLNPLLTEEETRRAVQRTGAR---------------LRIDAPTAR----------------- 48
Cdd:COG1022 76 PEWVIADLAILAAGAVTVPIYPTSSAEEVAYILNDSGAKvlfvedqeqldklleVRDELPSLRhivvldprglrddprll 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 49 ------ALHAGASRP--LSPSPATEDPEATAVLALSSGTTAEPKPVMLSHRALSANIRQTVSALRgngLDPGWSVLAPLP 120
Cdd:COG1022 156 sldellALGREVADPaeLEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLP---LGPGDRTLSFLP 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 121 LSHIYGlNVLLHSSLANGNHVVLMPRFT-----------------PRAFARLHAE-------------------HRIGWS 164
Cdd:COG1022 233 LAHVFE-RTVSYYALAAGATVAFAESPDtlaedlrevkptfmlavPRVWEKVYAGiqakaeeagglkrklfrwaLAVGRR 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 165 YVAppivAALDSEDYSADYSAED-------FR--------HTRVMLSGAADLSPDLAR--RVgerLGVEIIQGYGMTEAS 227
Cdd:COG1022 312 YAR----ARLAGKSPSLLLRLKHaladklvFSklrealggRLRFAVSGGAALGPELARffRA---LGIPVLEGYGLTETS 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 228 PVTHMMRRGDP-LG-IGRPVDGTETRIVG-GELWVRGPQLCSGYLGAPG-----PLVEGWLPTGDLVAPTPDGGLRVTGR 299
Cdd:COG1022 385 PVITVNRPGDNrIGtVGPPLPGVEVKIAEdGEILVRGPNVMKGYYKNPEataeaFDADGWLHTGDIGELDEDGFLRITGR 464
|
410 420 430
....*....|....*....|....*....|....*..
gi 2713532039 300 TKEII-----KYrgyqVSPAELEEVIAACPGVRDVAV 331
Cdd:COG1022 465 KKDLIvtsggKN----VAPQPIENALKASPLIEQAVV 497
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
1-391 |
9.72e-43 |
|
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: 155.90 E-value: 9.72e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 1 VEFATAFHGILGAGATVVPLNPLLTEEetRRAVQ-------------RTGARLRIDAPTARALHAG-ASRPLSPSPATED 66
Cdd:cd17646 59 ADLVVALLAVLKAGAAYLPLDPGYPAD--RLAYMladagpavvlttaDLAARLPAGGDVALLGDEAlAAPPATPPLVPPR 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 67 PEATAVLALSSGTTAEPKPVMLSHRALSANIRQTVSALrgnGLDPGWSVLAPLPLSHIYGLNVLLHSSLANGNHVVLMP- 145
Cdd:cd17646 137 PDNLAYVIYTSGSTGRPKGVMVTHAGIVNRLLWMQDEY---PLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPg 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 146 -RFTPRAFARLHAEHRIGWSYVAPPIVAALDSEDysADYSAEDFRHtrVMLSGAAdLSPDLARRVGERLGVEIIQGYGMT 224
Cdd:cd17646 214 gHRDPAYLAALIREHGVTTCHFVPSMLRVFLAEP--AAGSCASLRR--VFCSGEA-LPPELAARFLALPGAELHNLYGPT 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 225 EAS-PVTHMMRRGD----PLGIGRPVDGTETRI-----------VGGELWVRGPQLCSGYLGAPGPLVEGWLP------- 281
Cdd:cd17646 289 EAAiDVTHWPVRGPaetpSVPIGRPVPNTRLYVlddalrpvpvgVPGELYLGGVQLARGYLGRPALTAERFVPdpfgpgs 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 282 ----TGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAV-ARGTLQGEEVPHAFVVGTAA----- 351
Cdd:cd17646 369 rmyrTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVvARAAPAGAARLVGYVVPAAGaagpd 448
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2713532039 352 PAEVHEWVARRVAPYKKVRRVTVVESIPRAATGKILRRRL 391
Cdd:cd17646 449 TAALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
63-395 |
9.85e-43 |
|
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: 155.95 E-value: 9.85e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 63 ATEDPEATAVLALSSGTTAEPKPVMLSHRALSANIRQTVSALRgngLDPGWSVLAPLPLSHIYGLNVLLHSSLANGNHVV 142
Cdd:cd05909 142 APVQPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFD---PNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVV 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 143 LMPrfTPrafarLHAEHrigwsyVAPPI----VAALDSED-----YSADYSAEDFRHTRVMLSGAADLSPDLARRVGERL 213
Cdd:cd05909 219 FHP--NP-----LDYKK------IPELIydkkATILLGTPtflrgYARAAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKF 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 214 GVEIIQGYGMTEASPVT-----HMMRRgdPLGIGRPVDGTETRIV------------GGELWVRGPQLCSGYLGAPGP-- 274
Cdd:cd05909 286 GIRILEGYGTTECSPVIsvntpQSPNK--EGTVGRPLPGMEVKIVsvetheevpigeGGLLLVRGPNVMLGYLNEPELts 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 275 --LVEGWLPTGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVI-AACPGVRDVAVA--RGTLQGEEVpHAFVVGT 349
Cdd:cd05909 364 faFGDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILsEILPEDNEVAVVsvPDGRKGEKI-VLLTTTT 442
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2713532039 350 AA-PAEVHEWV-ARRVAPYKKVRRVTVVESIPRAATGKILRRRLRERA 395
Cdd:cd05909 443 DTdPSSLNDILkNAGISNLAKPSYIHQVEEIPLLGTGKPDYVTLKALA 490
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
6-400 |
3.26e-42 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 155.96 E-value: 3.26e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 6 AFHGILGAGATVVPLNPLLTEEE-------------------------------------TRRA-------------VQR 35
Cdd:PRK06710 90 GYYGTLLAGGIVVQTNPLYTEREleyqlhdsgakvilcldlvfprvtnvqsatkiehvivTRIAdflpfpknllypfVQK 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 36 TGARLRIDAPTARALHAGASRPLSPSPATE---DPEAT-AVLALSSGTTAEPKPVMLSHRALSANIRQTVSALRgNGLDP 111
Cdd:PRK06710 170 KQSNLVVKVSESETIHLWNSVEKEVNTGVEvpcDPENDlALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLY-NCKEG 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 112 GWSVLAPLPLSHIYGLNVLLHSSLANGNHVVLMPRFTPRAFARLHAEHRIGWSYVAPPIVAALDSEDYSADYsaeDFRHT 191
Cdd:PRK06710 249 EEVVLGVLPFFHVYGMTAVMNLSIMQGYKMVLIPKFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEY---DISSI 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 192 RVMLSGAADLSPDLARRVGERLGVEIIQGYGMTEASPVTH---MMRRGDPLGIGRPVDGTETRIVG------------GE 256
Cdd:PRK06710 326 RACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSPVTHsnfLWEKRVPGSIGVPWPDTEAMIMSletgealppgeiGE 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 257 LWVRGPQLCSGYLGAP----GPLVEGWLPTGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAV- 331
Cdd:PRK06710 406 IVVKGPQIMKGYWNKPeetaAVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTi 485
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2713532039 332 -ARGTLQGEEVpHAFVV---GTAAPAEVHEWVARR-VAPYKKVRRVTVVESIPRAATGKILRRRLRERAGDADE 400
Cdd:PRK06710 486 gVPDPYRGETV-KAFVVlkeGTECSEEELNQFARKyLAAYKVPKVYEFRDELPKTTVGKILRRVLIEEEKRKNE 558
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
1-392 |
3.92e-42 |
|
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: 153.39 E-value: 3.92e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 1 VEFATAFHGILGAGATVVPLNPLLTEEETRRAVQRTGARLRIdaptaralhagasrplspspatEDPEATAVLALSSGTT 80
Cdd:cd05919 46 PELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVV----------------------TSADDIAYLLYSSGTT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 81 AEPKPVMLSHRalsaNIRQTVSALRGN--GLDPGWSVLAPLPLSHIYGLNVLLHSSLANGNHVVLMP-RFTPRAFARLHA 157
Cdd:cd05919 104 GPPKGVMHAHR----DPLLFADAMAREalGLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGASAVLNPgWPTAERVLATLA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 158 EHRIGWSYVAPPIVAALDSedySADYSAEDFRHTRVMLSGAADLSPDLARRVGERLGVEIIQGYGMTEASPVTHMMRRGD 237
Cdd:cd05919 180 RFRPTVLYGVPTFYANLLD---SCAGSPDALRSLRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVGHIFLSNRPGA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 238 --PLGIGRPVDGTETRIVG-----------GELWVRGPQLCSGYLGAP----GPLVEGWLPTGDLVAPTPDGGLRVTGRT 300
Cdd:cd05919 257 wrLGSTGRPVPGYEIRLVDeeghtippgeeGDLLVRGPSAAVGYWNNPeksrATFNGGWYRTGDKFCRDADGWYTHAGRA 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 301 KEIIKYRGYQVSPAELEEVIAACPGVRDVA-VARGTLQGEEVPHAFVVGT--AAPAE-----VHEWVARRVAPYKKVRRV 372
Cdd:cd05919 337 DDMLKVGGQWVSPVEVESLIIQHPAVAEAAvVAVPESTGLSRLTAFVVLKspAAPQEslardIHRHLLERLSAHKVPRRI 416
|
410 420
....*....|....*....|
gi 2713532039 373 TVVESIPRAATGKILRRRLR 392
Cdd:cd05919 417 AFVDELPRTATGKLQRFKLR 436
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
18-392 |
5.61e-42 |
|
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: 153.36 E-value: 5.61e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 18 VPLNPLLTEEETRRAVQRTGARLRIDAPTARAL---------------------HAGASRPLSPSpateDPEATAVLALS 76
Cdd:cd05922 50 VPLNPTLKESVLRYLVADAGGRIVLADAGAADRlrdalpaspdpgtvldadgirAARASAPAHEV----SHEDLALLLYT 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 77 SGTTAEPKPVMLSHRALSANIRQTVSALrgnGLDPGWSVLAPLPLSHIYGLNVLlHSSLANGNHVVLMPRFT-PRAFARL 155
Cdd:cd05922 126 SGSTGSPKLVRLSHQNLLANARSIAEYL---GITADDRALTVLPLSYDYGLSVL-NTHLLRGATLVLTNDGVlDDAFWED 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 156 HAEHRIGWSYVAPPIVAALDSedysADYSAEDFRHTRVMLSGAADLSPDLARRVGERL-GVEIIQGYGMTEASPVTHMM- 233
Cdd:cd05922 202 LREHGATGLAGVPSTYAMLTR----LGFDPAKLPSLRYLTQAGGRLPQETIARLRELLpGAQVYVMYGQTEATRRMTYLp 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 234 --RRGDPLG-IGRPVDGTETRIVG-----------GELWVRGPQLCSGYLGAPGPLVEGWLP-----TGDLVAPTPDGGL 294
Cdd:cd05922 278 peRILEKPGsIGLAIPGGEFEILDddgtptppgepGEIVHRGPNVMKGYWNDPPYRRKEGRGggvlhTGDLARRDEDGFL 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 295 RVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVA-VARGTLQGEEVpHAFVVGTAA--PAEVHEWVARRVAPYKKVRR 371
Cdd:cd05922 358 FIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAaVGLPDPLGEKL-ALFVTAPDKidPKDVLRSLAERLPPYKVPAT 436
|
410 420
....*....|....*....|.
gi 2713532039 372 VTVVESIPRAATGKILRRRLR 392
Cdd:cd05922 437 VRVVDELPLTASGKVDYAALR 457
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
14-394 |
2.07e-41 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 152.04 E-value: 2.07e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 14 GATVVPLNPLLTEEETRRAVQRTGARLRI-DAPTARALHAGASRPLSPSPATEDPEA----------TAVLALSSGTTAE 82
Cdd:PRK03640 76 GAVAVLLNTRLSREELLWQLDDAEVKCLItDDDFEAKLIPGISVKFAELMNGPKEEAeiqeefdldeVATIMYTSGTTGK 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 83 PKPVMLS---HRAlSAnirqTVSALrgN-GL--DPGWsvLAPLPLSHIYGLNVLLHSsLANGNHVVLMPRFTPRAFARLH 156
Cdd:PRK03640 156 PKGVIQTygnHWW-SA----VGSAL--NlGLteDDCW--LAAVPIFHISGLSILMRS-VIYGMRVVLVEKFDAEKINKLL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 157 AEHRIGWSYVAPPIVAALDSEDYSADYSAedfrHTRVMLSGAADLSPDLARRVGERlGVEIIQGYGMTE-ASPV-----T 230
Cdd:PRK03640 226 QTGGVTIISVVSTMLQRLLERLGEGTYPS----SFRCMLLGGGPAPKPLLEQCKEK-GIPVYQSYGMTEtASQIvtlspE 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 231 HMMrrgDPLG-IGRPVDGTETRIV----------GGELWVRGPQLCSGYLGAPGPLVE----GWLPTGDLVAPTPDGGLR 295
Cdd:PRK03640 301 DAL---TKLGsAGKPLFPCELKIEkdgvvvppfeEGEIVVKGPNVTKGYLNREDATREtfqdGWFKTGDIGYLDEEGFLY 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 296 VTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAVArgtlqGEE------VPHAFVV--GTAAPAEVHEWVARRVAPYK 367
Cdd:PRK03640 378 VLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVV-----GVPddkwgqVPVAFVVksGEVTEEELRHFCEEKLAKYK 452
|
410 420
....*....|....*....|....*..
gi 2713532039 368 KVRRVTVVESIPRAATGKILRRRLRER 394
Cdd:PRK03640 453 VPKRFYFVEELPRNASGKLLRHELKQL 479
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
1-331 |
3.86e-41 |
|
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: 150.11 E-value: 3.86e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 1 VEFATAFHGILGAGATVVPLNP------------------LLTEEETRRAVQRTGARLRIDAPTARAlHAGASRPLSPSP 62
Cdd:TIGR01733 36 AELVVAILAVLKAGAAYVPLDPaypaerlafiledagarlLLTDSALASRLAGLVLPVILLDPLELA-ALDDAPAPPPPD 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 63 ATEDPEATAVLALSSGTTAEPKPVMLSHRALSANIRQTVSALrgnGLDPGWSVLAPLPLSH------IYGlnvllhsSLA 136
Cdd:TIGR01733 115 APSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRY---GLDPDDRVLQFASLSFdasveeIFG-------ALL 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 137 NGNHVVLMP----RFTPRAFARLHAEHRIGWSYVAPPIVAALDSEDysadysAEDFRHTRVMLSGAADLSPDLARRVGER 212
Cdd:TIGR01733 185 AGATLVVPPedeeRDDAALLAALIAEHPVTVLNLTPSLLALLAAAL------PPALASLRLVILGGEALTPALVDRWRAR 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 213 LG-VEIIQGYGMTEAS------PVTHMMRRGD-PLGIGRPVDGTETRIVG-----------GELWVRGPQLCSGYLGAP- 272
Cdd:TIGR01733 259 GPgARLINLYGPTETTvwstatLVDPDDAPREsPVPIGRPLANTRLYVLDddlrpvpvgvvGELYIGGPGVARGYLNRPe 338
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2713532039 273 ------------GPLVEGWLPTGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAV 331
Cdd:TIGR01733 339 ltaerfvpdpfaGGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
43-399 |
4.30e-41 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 152.51 E-value: 4.30e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 43 DAPTARALHAgASRPlspspateDPEATAVLALSSGTTAEPKPVMLSHRALSANIRQTVSALrgnGLDPGWSVLAPLPLS 122
Cdd:PRK13295 181 QEPDAPAILA-RLRP--------GPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERL---GLGADDVILMASPMA 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 123 HIYGLNVLLHSSLANGNHVVLMPRFTPRAFARLHAEHRIGWSYVAPPIVAALDSedySADYSAEDFRHTRVMLSGAADLS 202
Cdd:PRK13295 249 HQTGFMYGLMMPVMLGATAVLQDIWDPARAAELIRTEGVTFTMASTPFLTDLTR---AVKESGRPVSSLRTFLCAGAPIP 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 203 PDLARRVGERLGVEIIQGYGMTEASPVThMMRRGDPLGI-----GRPVDGTETRIVG-----------GELWVRGPQLCS 266
Cdd:PRK13295 326 GALVERARAALGAKIVSAWGMTENGAVT-LTKLDDPDERasttdGCPLPGVEVRVVDadgaplpagqiGRLQVRGCSNFG 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 267 GYLGAP---GPLVEGWLPTGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAV-----ARgtlQG 338
Cdd:PRK13295 405 GYLKRPqlnGTDADGWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIvaypdER---LG 481
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2713532039 339 EEVPhAFVV----GTAAPAEVHEWV-ARRVAPYKKVRRVTVVESIPRAATGKILRRRLRERAGDAD 399
Cdd:PRK13295 482 ERAC-AFVVprpgQSLDFEEMVEFLkAQKVAKQYIPERLVVRDALPRTPSGKIQKFRLREMLRGED 546
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
2-392 |
4.53e-41 |
|
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: 150.32 E-value: 4.53e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 2 EFATAFHGILGAGATVVPLNPLLTEEETRRAVQRtgarlridAPTARALHAGASrplspsPATEDpeaTAVLALSSGTTA 81
Cdd:cd05958 48 ELVACWFGIQKAGAIAVATMPLLRPKELAYILDK--------ARITVALCAHAL------TASDD---ICILAFTSGTTG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 82 EPKPVMLSHRALSANIRQ-TVSALRgngLDPGWSVLAPLPLSHIYGLNVLLHSSLANGNHVVLMPRFTPRAFARLHAEHR 160
Cdd:cd05958 111 APKATMHFHRDPLASADRyAVNVLR---LREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEATPDLLLSAIARYK 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 161 IGWSYVAPPIVAALDSedySADYSAEDFRHTRVMLSGAADLSPDLARRVGERLGVEIIQGYGMTEASPVTHMMRRGD--P 238
Cdd:cd05958 188 PTVLFTAPTAYRAMLA---HPDAAGPDLSSLRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEMFHIFISARPGDarP 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 239 LGIGRPVDGTETRIVG-----------GELWVRGPQLCSgYLGAPG---PLVEGWLPTGDLVAPTPDGGLRVTGRTKEII 304
Cdd:cd05958 265 GATGKPVPGYEAKVVDdegnpvpdgtiGRLAVRGPTGCR-YLADKRqrtYVQGGWNITGDTYSRDPDGYFRHQGRSDDMI 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 305 KYRGYQVSPAELEEVIAACPGVRDVAVARGTLQ-GEEVPHAFVV-------GTAAPAEVHEWVARRVAPYKKVRRVTVVE 376
Cdd:cd05958 344 VSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDEsRGVVVKAFVVlrpgvipGPVLARELQDHAKAHIAPYKYPRAIEFVT 423
|
410
....*....|....*.
gi 2713532039 377 SIPRAATGKILRRRLR 392
Cdd:cd05958 424 ELPRTATGKLQRFALR 439
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
13-394 |
1.28e-40 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 150.91 E-value: 1.28e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 13 AGATVVPLNPLLTEEETRRAVQRTGARLRIDAPTA---RALHAGASRP-------LSPSPATED---------------- 66
Cdd:PRK06188 85 AGLRRTALHPLGSLDDHAYVLEDAGISTLIVDPAPfveRALALLARVPslkhvltLGPVPDGVDllaaaakfgpaplvaa 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 67 --PEATAVLALSSGTTAEPKPVMLSHRALSAnirQTVSALRGNGLDPGWSVLAPLPLSHIYGLNVLlhSSLANGNHVVLM 144
Cdd:PRK06188 165 alPPDIAGLAYTGGTTGKPKGVMGTHRSIAT---MAQIQLAEWEWPADPRFLMCTPLSHAGGAFFL--PTLLRGGTVIVL 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 145 PRFTPRAFARLHAEHRIGWSYVAPP-IVAALDSedysADYSAEDFRHTRVMLSGAADLSPDLARRVGERLGVEIIQGYGM 223
Cdd:PRK06188 240 AKFDPAEVLRAIEEQRITATFLVPTmIYALLDH----PDLRTRDLSSLETVYYGASPMSPVRLAEAIERFGPIFAQYYGQ 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 224 TEA-SPVTHMMRR----GDP---LGIGRPVDGTETRIVG-----------GELWVRGPQLCSGYLGAPGPLVE----GWL 280
Cdd:PRK06188 316 TEApMVITYLRKRdhdpDDPkrlTSCGRPTPGLRVALLDedgrevaqgevGEICVRGPLVMDGYWNRPEETAEafrdGWL 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 281 PTGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAVArGTLQ---GEEVpHAFVV----GTAAPA 353
Cdd:PRK06188 396 HTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVI-GVPDekwGEAV-TAVVVlrpgAAVDAA 473
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 2713532039 354 EVHEWVARRVAPYKKVRRVTVVESIPRAATGKILRRRLRER 394
Cdd:PRK06188 474 ELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALRAR 514
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
2-396 |
6.41e-40 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 148.88 E-value: 6.41e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 2 EFATAFHGILGAGATVVPLNPLLTEEETRRAVQRTGARLRI---------DAPTAR----ALHAGASRPLS--------- 59
Cdd:PRK05852 80 EFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLidadgphdrAEPTTRwwplTVNVGGDSGPSggtlsvhld 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 60 ----PSPATEDPEA----TAVLALSSGTTAEPKPVMLSHRALSANIRQTVSALRgngLDPGWSVLAPLPLSHIYGLNVLL 131
Cdd:PRK05852 160 aatePTPATSTPEGlrpdDAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYR---LSPRDATVAVMPLYHGHGLIAAL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 132 HSSLANGNhVVLMP---RFTPRAF-ARLHAEHRIgWsYVAPPIVAALDSEDYSADYSAEDFRHTRVMLSGAADLSPDLAR 207
Cdd:PRK05852 237 LATLASGG-AVLLPargRFSAHTFwDDIKAVGAT-W-YTAVPTIHQILLERAATEPSGRKPAALRFIRSCSAPLTAETAQ 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 208 RVGERLGVEIIQGYGMTEAspvTHMMRRGDPLGIGRPVD------------GTETRIVG-----------GELWVRGPQL 264
Cdd:PRK05852 314 ALQTEFAAPVVCAFGMTEA---THQVTTTQIEGIGQTENpvvstglvgrstGAQIRIVGsdglplpagavGEVWLRGTTV 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 265 CSGYLGAP----GPLVEGWLPTGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAV--ARGTLQG 338
Cdd:PRK05852 391 VRGYLGDPtitaANFTDGWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVfgVPDQLYG 470
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2713532039 339 EEVPHAFVVGTAAPAEVHEWVA---RRVAPYKKVRRVTVVESIPRAATGKILRRRLRERAG 396
Cdd:PRK05852 471 EAVAAVIVPRESAPPTAEELVQfcrERLAAFEIPASFQEASGLPHTAKGSLDRRAVAEQFG 531
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
6-395 |
8.34e-40 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 149.05 E-value: 8.34e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 6 AFHGILGAGATVVPLNPLLTEEETRRAVQRTGA----------------------------------------------- 38
Cdd:PRK08974 90 ALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAkaivivsnfahtlekvvfktpvkhviltrmgdqlstakgtlvnfvvk 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 39 ---RL--RIDAPTA----RALHAGASRP-LSPSPATEDpeaTAVLALSSGTTAEPKPVMLSHRALSANIRQtVSALRGNG 108
Cdd:PRK08974 170 yikRLvpKYHLPDAisfrSALHKGRRMQyVKPELVPED---LAFLQYTGGTTGVAKGAMLTHRNMLANLEQ-AKAAYGPL 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 109 LDPGWS-VLAPLPLSHIYGL--NVLLHSSLANGNHVVLMPRFTPrAFARLHAEHRigwsYVAPPIV-----AALDSEDYS 180
Cdd:PRK08974 246 LHPGKElVVTALPLYHIFALtvNCLLFIELGGQNLLITNPRDIP-GFVKELKKYP----FTAITGVntlfnALLNNEEFQ 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 181 AdysaEDFRHTRVMLSGAADLSPDLARRVGERLGVEIIQGYGMTEASP-VThmmrrGDPL-------GIGRPVDGTETRI 252
Cdd:PRK08974 321 E----LDFSSLKLSVGGGMAVQQAVAERWVKLTGQYLLEGYGLTECSPlVS-----VNPYdldyysgSIGLPVPSTEIKL 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 253 VG-----------GELWVRGPQLCSGYLGAPGP----LVEGWLPTGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELE 317
Cdd:PRK08974 392 VDddgnevppgepGELWVKGPQVMLGYWQRPEAtdevIKDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIE 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 318 EVIAACPGVRDVAvARGT---LQGEEVpHAFVV---GTAAPAEVHEWVARRVAPYKKVRRVTVVESIPRAATGKILRRRL 391
Cdd:PRK08974 472 DVVMLHPKVLEVA-AVGVpseVSGEAV-KIFVVkkdPSLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRREL 549
|
....
gi 2713532039 392 RERA 395
Cdd:PRK08974 550 RDEA 553
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
2-391 |
3.15e-39 |
|
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: 146.32 E-value: 3.15e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 2 EFATAFHGILGAGATVVPLNPLLTEEETRRAVQRTGARLRIdapTARALHAGASRPLSPSPATEDPEaTAVLALSSGTTA 81
Cdd:cd05920 77 EFVVLFFALLRLGAVPVLALPSHRRSELSAFCAHAEAVAYI---VPDRHAGFDHRALARELAESIPE-VALFLLSGGTTG 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 82 EPKPVMLSHRALSANIRQTVSALrgnGLDPGWSVLAPLPLSHIYGLN---VLlhSSLANGNHVVLMPRFTPRAFARLHAE 158
Cdd:cd05920 153 TPKLIPRTHNDYAYNVRASAEVC---GLDQDTVYLAVLPAAHNFPLAcpgVL--GTLLAGGRVVLAPDPSPDAAFPLIER 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 159 HRIGWSYVAPPIVAA-LDSedysADYSAEDFRHTRVMLSGAADLSPDLARRVGERLGVEIIQGYGMTEAspVTHMMRRGD 237
Cdd:cd05920 228 EGVTVTALVPALVSLwLDA----AASRRADLSSLRLLQVGGARLSPALARRVPPVLGCTLQQVFGMAEG--LLNYTRLDD 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 238 PLGI-----GRPVD-GTETRIVG-----------GELWVRGPQLCSGYLGAPGP-----LVEGWLPTGDLVAPTPDGGLR 295
Cdd:cd05920 302 PDEViihtqGRPMSpDDEIRVVDeegnpvppgeeGELLTRGPYTIRGYYRAPEHnarafTPDGFYRTGDLVRRTPDGYLV 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 296 VTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAVAR--GTLQGEEVpHAFVVGTAAP---AEVHEWVARR-VAPYKKV 369
Cdd:cd05920 382 VEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAmpDELLGERS-CAFVVLRDPPpsaAQLRRFLRERgLAAYKLP 460
|
410 420
....*....|....*....|..
gi 2713532039 370 RRVTVVESIPRAATGKILRRRL 391
Cdd:cd05920 461 DRIEFVDSLPLTAVGKIDKKAL 482
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
1-392 |
7.79e-39 |
|
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: 144.02 E-value: 7.79e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 1 VEFATAFHGILGAGATVVPLNPLLTEEETRravqrtgarLRIDAPTARALHAGAsrplspspatEDPeatAVLALSSGTT 80
Cdd:cd05972 36 PELWAVILAVIKLGAVYVPLTTLLGPKDIE---------YRLEAAGAKAIVTDA----------EDP---ALIYFTSGTT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 81 AEPKPVMLSHRALSANIRQTVSALrgnGLDPG---WSVLAPlplSHIYGLNVLLHSSLANGNHVVL--MPRFTPRAFARL 155
Cdd:cd05972 94 GLPKGVLHTHSYPLGHIPTAAYWL---GLRPDdihWNIADP---GWAKGAWSSFFGPWLLGATVFVyeGPRFDAERILEL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 156 HAEHRIGwSYVAPPIV----AALDSEDYsadysaeDFRHTRVMLSGAADLSPDLARRVGERLGVEIIQGYGMTEaSPVTH 231
Cdd:cd05972 168 LERYGVT-SFCGPPTAyrmlIKQDLSSY-------KFSHLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTE-TGLTV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 232 MMRRGDPL---GIGRPVDGTETRIVG-----------GELWVR--GPQLCSGYLGAP----GPLVEGWLPTGDLVAPTPD 291
Cdd:cd05972 239 GNFPDMPVkpgSMGRPTPGYDVAIIDddgrelppgeeGDIAIKlpPPGLFLGYVGDPekteASIRGDYYLTGDRAYRDED 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 292 GGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAVA------RGtlqgeEVPHAFVVGTA-APA------EVHEW 358
Cdd:cd05972 319 GYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVgspdpvRG-----EVVKAFVVLTSgYEPseelaeELQGH 393
|
410 420 430
....*....|....*....|....*....|....
gi 2713532039 359 VARRVAPYKKVRRVTVVESIPRAATGKILRRRLR 392
Cdd:cd05972 394 VKKVLAPYKYPREIEFVEELPKTISGKIRRVELR 427
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
30-395 |
8.12e-39 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 146.04 E-value: 8.12e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 30 RRAVQRTGARLRIDAPTARALHAGASRPLSPSPAtEDPEATAVLALSSGTTAEPKPVMLSHRALSANIRQTVSALrgnGL 109
Cdd:PRK06164 144 DDAADATPAPAPGARVQLFALPDPAPPAAAGERA-ADPDAGALLFTTSGTTSGPKLVLHRQATLLRHARAIARAY---GY 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 110 DPGWSVLAPLPLSHIYGLNVLLhSSLANGNHVVLMPRFTPRAFARLHAEHRIGWSYVAPPIVAAL-DSEDYSADYSaedf 188
Cdd:PRK06164 220 DPGAVLLAALPFCGVFGFSTLL-GALAGGAPLVCEPVFDAARTARALRRHRVTHTFGNDEMLRRIlDTAGERADFP---- 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 189 rhtRVMLSGAADLSP---DLARRVGERlGVEIIQGYGMTEASPVTHMMRRGDP-----LGIGRPVDG-TETRIV------ 253
Cdd:PRK06164 295 ---SARLFGFASFAPalgELAALARAR-GVPLTGLYGSSEVQALVALQPATDPvsvriEGGGRPASPeARVRARdpqdga 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 254 ------GGELWVRGPQLCSGYLGAPGPLVE-----GWLPTGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAA 322
Cdd:PRK06164 371 llpdgeSGEIEIRAPSLMRGYLDNPDATARaltddGYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEA 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 323 CPGVRDVAVARGTLQGEEVPHAFVVGTA----APAEVHEWVARRVAPYKKVRRVTVVESIPRAATG---KILRRRLRERA 395
Cdd:PRK06164 451 LPGVAAAQVVGATRDGKTVPVAFVIPTDgaspDEAGLMAACREALAGFKVPARVQVVEAFPVTESAngaKIQKHRLREMA 530
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
1-392 |
2.70e-38 |
|
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: 144.02 E-value: 2.70e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 1 VEFATAFHGILGAGATVVPLNPLLTEEETRRAVQRTGARLRIDAPTARALHAGASRPLSP---SPATEDPEATAVLALS- 76
Cdd:cd17651 56 AELVVALLAILKAGAAYVPLDPAYPAERLAFMLADAGPVLVLTHPALAGELAVELVAVTLldqPGAAAGADAEPDPALDa 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 77 ---------SGTTAEPKPVMLSHRALsANIRQtvSALRGNGLDPGWSVLAPLPLSHIYGLNVLLhSSLANGNHVVLMP-- 145
Cdd:cd17651 136 ddlayviytSGSTGRPKGVVMPHRSL-ANLVA--WQARASSLGPGARTLQFAGLGFDVSVQEIF-STLCAGATLVLPPee 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 146 -RFTPRAFARLHAEHRIGWSYVAPPIVAALDSEDYSADYSAEDFRHtrVMLSG-AADLSPDLARRVGERLGVEIIQGYGM 223
Cdd:cd17651 212 vRTDPPALAAWLDEQRISRVFLPTVALRALAEHGRPLGVRLAALRY--LLTGGeQLVLTEDLREFCAGLPGLRLHNHYGP 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 224 TEASPVT------HMMRRGDPLGIGRPVDGTETRI-----------VGGELWVRGPQLCSGYLGAPGPLVEGWLP----- 281
Cdd:cd17651 290 TETHVVTalslpgDPAAWPAPPPIGRPIDNTRVYVldaalrpvppgVPGELYIGGAGLARGYLNRPELTAERFVPdpfvp 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 282 ------TGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAV-ARGTLQGEEVPHAFVVGTAA--- 351
Cdd:cd17651 370 garmyrTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVlAREDRPGEKRLVAYVVGDPEapv 449
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2713532039 352 -PAEVHEWVARRVAPYKKVRRVTVVESIPRAATGKILRRRLR 392
Cdd:cd17651 450 dAAELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRALP 491
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
2-399 |
2.04e-37 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 142.20 E-value: 2.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 2 EFATAFHGILGAGATVVPLNPLLTEEETRRAVQRTGARL-------------------------RIDAPTARALHAG-AS 55
Cdd:PRK06155 83 EFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLlvveaallaaleaadpgdlplpavwLLDAPASVSVPAGwST 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 56 RPLSPSPATEDPEA-----TAVLALSSGTTAEPKPVMLSHRALSANIRQTVSALrgnGLDPGWSVLAPLPLSHIYGLNVL 130
Cdd:PRK06155 163 APLPPLDAPAPAAAvqpgdTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDL---EIGADDVLYTTLPLFHTNALNAF 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 131 LhSSLANGNHVVLMPRFTPRAFARLHAEHRIGWSYVAPPIVAALDSEDYSADYSAEdfrHTRVMLSGAadLSPDLARRVG 210
Cdd:PRK06155 240 F-QALLAGATYVLEPRFSASGFWPAVRRHGATVTYLLGAMVSILLSQPARESDRAH---RVRVALGPG--VPAALHAAFR 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 211 ERLGVEIIQGYGMTEASPVTHMMRRGDPLG-IGRPVDGTETRIVG-----------GELWVRGPQ---LCSGYLGAPGPL 275
Cdd:PRK06155 314 ERFGVDLLDGYGSTETNFVIAVTHGSQRPGsMGRLAPGFEARVVDehdqelpdgepGELLLRADEpfaFATGYFGMPEKT 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 276 VEGW----LPTGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAV--ARGTLQGEEVPHAFVV-- 347
Cdd:PRK06155 394 VEAWrnlwFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVfpVPSELGEDEVMAAVVLrd 473
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2713532039 348 GTAA-PAEVHEWVARRVAPYKKVRRVTVVESIPRAATGKILRRRLRERAGDAD 399
Cdd:PRK06155 474 GTALePVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLREQGVTAD 526
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
2-399 |
2.10e-37 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 142.22 E-value: 2.10e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 2 EFATAFHGILGAGATVVPLNPLLTEEETRRAVQRTGARLRIDAPTARALhAGASRPLSPSPAT---------------ED 66
Cdd:PRK07786 79 EFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVVTEAALAPV-ATAVRDIVPLLSTvvvaggssddsvlgyED 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 67 --------------PEATAVLAL-SSGTTAEPKPVMLSHRALSAnirQTVSALRGNGLDPGWSV-LAPLPLSHIYGLNVL 130
Cdd:PRK07786 158 llaeagpahapvdiPNDSPALIMyTSGTTGRPKGAVLTHANLTG---QAMTCLRTNGADINSDVgFVGVPLFHIAGIGSM 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 131 LhSSLANGNHVVLMP--RFTPRAFARLHAEHRIGWSYVAPPIVAALdsedySADYSAE--DFRhTRVMLSGAADLSPDLA 206
Cdd:PRK07786 235 L-PGLLLGAPTVIYPlgAFDPGQLLDVLEAEKVTGIFLVPAQWQAV-----CAEQQARprDLA-LRVLSWGAAPASDTLL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 207 RRVGERL-GVEIIQGYGMTEASPVTHMMRRGDPL----GIGRPVDGTETRIVG-----------GELWVRGPQLCSGYLG 270
Cdd:PRK07786 308 RQMAATFpEAQILAAFGQTEMSPVTCMLLGEDAIrklgSVGKVIPTVAARVVDenmndvpvgevGEIVYRAPTLMSGYWN 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 271 APGPLVE----GWLPTGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAV-ARGTLQGEEVPHAF 345
Cdd:PRK07786 388 NPEATAEafagGWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAViGRADEKWGEVPVAV 467
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2713532039 346 VVGTAAPA-----EVHEWVARRVAPYKKVRRVTVVESIPRAATGKILRRRLRERAGDAD 399
Cdd:PRK07786 468 AAVRNDDAaltleDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTELRERYGACV 526
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
2-388 |
4.10e-37 |
|
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: 140.27 E-value: 4.10e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 2 EFATAFHGILGAGATVVPLNPLLTEEETRRAVQRTGARLRIdaptaralhagasrplspspaTEDPEATAVLALSSGTTA 81
Cdd:cd05914 44 EWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIF---------------------VSDEDDVALINYTSGTTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 82 EPKPVMLSHRALSANIRQTVSALRgngLDPGWSVLAPLPLSHIYGLNVLLHSSLANGNHVVLMPRFTP-----RAFAR-- 154
Cdd:cd05914 103 NSKGVMLTYRNIVSNVDGVKEVVL---LGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDKIPSakiiaLAFAQvt 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 155 --------LHAEHRI-------------GWSYVAPPivaaLDSEDYSADYSA--EDFR-HTRVMLSGAADLSPDLARRVG 210
Cdd:cd05914 180 ptlgvpvpLVIEKIFkmdiipkltlkkfKFKLAKKI----NNRKIRKLAFKKvhEAFGgNIKEFVIGGAKINPDVEEFLR 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 211 ErLGVEIIQGYGMTEASPVTHMMRRGD-PLG-IGRPVDGTETRIVG-------GELWVRGPQLCSGYLGAPGPLVE---- 277
Cdd:cd05914 256 T-IGFPYTIGYGMTETAPIISYSPPNRiRLGsAGKVIDGVEVRIDSpdpatgeGEIIVRGPNVMKGYYKNPEATAEafdk 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 278 -GWLPTGDLVAPTPDGGLRVTGRTKE-IIKYRGYQVSPAELEEVIAACPGV--RDVAVARGTLQGEEVPHA---FVVGTA 350
Cdd:cd05914 335 dGWFHTGDLGKIDAEGYLYIRGRKKEmIVLSSGKNIYPEEIEAKINNMPFVleSLVVVQEKKLVALAYIDPdflDVKALK 414
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2713532039 351 APA-------EVHEWVARRVAPYKKVRRVTVV-ESIPRAATGKILR 388
Cdd:cd05914 415 QRNiidaikwEVRDKVNQKVPNYKKISKVKIVkEEFEKTPKGKIKR 460
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
54-395 |
5.83e-37 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 142.02 E-value: 5.83e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 54 ASRPLSPSPATEDpeATAVLALSSGTTAEPKPVMLSHRALSANirqTVSALRGNGLDPGWSVLAPLPLSHIYGLNVLLHS 133
Cdd:PRK07529 201 GDRLFSGRPIGPD--DVAAYFHTGGTTGMPKLAQHTHGNEVAN---AWLGALLLGLGPGDTVFCGLPLFHVNALLVTGLA 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 134 SLANGNHVVLMP----RfTPRAFAR---LHAEHRIGWSYVAPPIVAAL-----DSEDYSAdysaedfrhTRVMLSGAADL 201
Cdd:PRK07529 276 PLARGAHVVLATpqgyR-GPGVIANfwkIVERYRINFLSGVPTVYAALlqvpvDGHDISS---------LRYALCGAAPL 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 202 SPDLARRVGERLGVEIIQGYGMTEASPVTHMMRRGDPLG---IGRPVDGTETRIVG----------------GELWVRGP 262
Cdd:PRK07529 346 PVEVFRRFEAATGVRIVEGYGLTEATCVSSVNPPDGERRigsVGLRLPYQRVRVVIlddagrylrdcavdevGVLCIAGP 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 263 QLCSGYLGAP---GPLVE-GWLPTGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDV-AVARGTLQ 337
Cdd:PRK07529 426 NVFSGYLEAAhnkGLWLEdGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAaAVGRPDAH 505
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2713532039 338 GEEVPHAFVV----GTAAPAEVHEWVARRVAPYKKV-RRVTVVESIPRAATGKILRRRLRERA 395
Cdd:PRK07529 506 AGELPVAYVQlkpgASATEAELLAFARDHIAERAAVpKHVRILDALPKTAVGKIFKPALRRDA 568
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
1-391 |
2.28e-36 |
|
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: 137.82 E-value: 2.28e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 1 VEFATAFHGILGAGATVVPLNPLLTEEETRRAVQRTGARLRIDaptaralhagasrplspspateDPEATAVLALSSGTT 80
Cdd:cd17643 48 AELIVALLAILKAGGAYVPIDPAYPVERIAFILADSGPSLLLT----------------------DPDDLAYVIYTSGST 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 81 AEPKPVMLSHRALSANIRQTVSALRGNGlDPGWSvlaplpLSHIYGLNVL---LHSSLANGNHVVLMP---RFTPRAFAR 154
Cdd:cd17643 106 GRPKGVVVSHANVLALFAATQRWFGFNE-DDVWT------LFHSYAFDFSvweIWGALLHGGRLVVVPyevARSPEDFAR 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 155 LHAEHRIGWSYVAPPIVAALDSEDYSADYSAEDFRHtrVMLSGAAdLSPDLARRVGERLGV---EIIQGYGMTEASP-VT 230
Cdd:cd17643 179 LLRDEGVTVLNQTPSAFYQLVEAADRDGRDPLALRY--VIFGGEA-LEAAMLRPWAGRFGLdrpQLVNMYGITETTVhVT 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 231 H------MMRRGDPLGIGRPVDGTETRIVG-----------GELWVRGPQLCSGYLGAPGPLVEGWLP------------ 281
Cdd:cd17643 256 FrpldaaDLPAAAASPIGRPLPGLRVYVLDadgrpvppgvvGELYVSGAGVARGYLGRPELTAERFVAnpfggpgsrmyr 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 282 TGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAV-ARGTLQGEEVPHAFVVG----TAAPAEVH 356
Cdd:cd17643 336 TGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAViVREDEPGDTRLVAYVVAddgaAADIAELR 415
|
410 420 430
....*....|....*....|....*....|....*
gi 2713532039 357 EWVARRVAPYKKVRRVTVVESIPRAATGKILRRRL 391
Cdd:cd17643 416 ALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
1-395 |
8.82e-36 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 137.70 E-value: 8.82e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 1 VEFATAFHGILGAGATVVPLNPLLTEEETRRAVQRTGARLRI--------------DAPTARALHAGAS----------- 55
Cdd:PRK08751 87 LQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLVvidnfgttvqqviaDTPVKQVITTGLGdmlgfpkaalv 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 56 -------RPLSPS---------------------PATE-DPEATAVLALSSGTTAEPKPVMLSHRALSANIRQTVSALRG 106
Cdd:PRK08751 167 nfvvkyvKKLVPEyringairfrealalgrkhsmPTLQiEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWLAG 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 107 NG-LDPGWSV-LAPLPLSHIYGL--NVLLHSSLANGNHVVLMPRFTPRAFARLHAEHRIGWSYVAPPIVAALDsedySAD 182
Cdd:PRK08751 247 TGkLEEGCEVvITALPLYHIFALtaNGLVFMKIGGCNHLISNPRDMPGFVKELKKTRFTAFTGVNTLFNGLLN----TPG 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 183 YSAEDFRHTRVMLSGAADLSPDLARRVGERLGVEIIQGYGMTEASPVTHMmrrgDPL-------GIGRPVDGTETRI--- 252
Cdd:PRK08751 323 FDQIDFSSLKMTLGGGMAVQRSVAERWKQVTGLTLVEAYGLTETSPAACI----NPLtlkeyngSIGLPIPSTDACIkdd 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 253 ------VG--GELWVRGPQLCSGYLGAPGPL-----VEGWLPTGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEV 319
Cdd:PRK08751 399 agtvlaIGeiGELCIKGPQVMKGYWKRPEETakvmdADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDV 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 320 IAACPGVRDV-AVARGTLQGEEVPHAFVVgTAAPA----EVHEWVARRVAPYKKVRRVTVVESIPRAATGKILRRRLRER 394
Cdd:PRK08751 479 IAMMPGVLEVaAVGVPDEKSGEIVKVVIV-KKDPAltaeDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRRELRDA 557
|
.
gi 2713532039 395 A 395
Cdd:PRK08751 558 A 558
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
1-394 |
7.77e-35 |
|
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: 135.06 E-value: 7.77e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 1 VEFATAFHGILGAGATVVPLNP---------------------LLTEEETRRAVQRTGARLRIDAPTARALH--AGASRP 57
Cdd:cd05931 59 LDFVAAFLGCLYAGAIAVPLPPptpgrhaerlaailadagprvVLTTAAALAAVRAFAASRPAAGTPRLLVVdlLPDTSA 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 58 LSPSPATEDPEATAVLALSSGTTAEPKPVMLSHRALSANIRQTVSALrgnGLDPGWSVLAPLPLSHIYGLNVLLHSSLAN 137
Cdd:cd05931 139 ADWPPPSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAY---GLDPGDVVVSWLPLYHDMGLIGGLLTPLYS 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 138 GNHVVLMPrftPRAFAR-------LHAEHRIGWSyVAPP-----IVAALDSEDYSADysaeDFRHTRVMLSGAADLSPDL 205
Cdd:cd05931 216 GGPSVLMS---PAAFLRrplrwlrLISRYRATIS-AAPNfaydlCVRRVRDEDLEGL----DLSSWRVALNGAEPVRPAT 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 206 ARRVGER-----LGVEIIQ-GYGMTEASPVTHMMRRGDPLGI----------------------------GRPVDGTETR 251
Cdd:cd05931 288 LRRFAEAfapfgFRPEAFRpSYGLAEATLFVSGGPPGTGPVVlrvdrdalagravavaaddpaarelvscGRPLPDQEVR 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 252 IVG------------GELWVRGPQLCSGYLGAPGPLVE-----------GWLPTGDL--VAptpDGGLRVTGRTKEIIKY 306
Cdd:cd05931 368 IVDpetgrelpdgevGEIWVRGPSVASGYWGRPEATAEtfgalaatdegGWLRTGDLgfLH---DGELYITGRLKDLIIV 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 307 RGYQVSPAELEEVI-AACPGVRDVAVARGTLQGEEVPHAFVV--------GTAAPAEVHEWVARRVAPYK-KVRRVTVVE 376
Cdd:cd05931 445 RGRNHYPQDIEATAeEAHPALRPGCVAAFSVPDDGEERLVVVaevergadPADLAAIAAAIRAAVAREHGvAPADVVLVR 524
|
490 500
....*....|....*....|
gi 2713532039 377 --SIPRAATGKILRRRLRER 394
Cdd:cd05931 525 pgSIPRTSSGKIQRRACRAA 544
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
13-394 |
9.69e-35 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 134.16 E-value: 9.69e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 13 AGATVVPLNPLLTEEETRRAVQRTGARLRI--DAPTAR-------ALHAGASRPLSPSP-ATEDPEATAVLALSSGTTAE 82
Cdd:PRK09088 70 VGAIYVPLNWRLSASELDALLQDAEPRLLLgdDAVAAGrtdvedlAAFIASADALEPADtPSIPPERVSLILFTSGTSGQ 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 83 PKPVMLSHRalsaNIRQT-VSALRGNGLDPGWSVLAPLPLSHIYGLNVLLHSSLANGNHVVLMPRFTPRAFARLHAEHRI 161
Cdd:PRK09088 150 PKGVMLSER----NLQQTaHNFGVLGRVDAHSSFLCDAPMFHIIGLITSVRPVLAVGGSILVSNGFEPKRTLGRLGDPAL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 162 GWS-YVAPPIVAALDSEDYSADYSAedFRH-TRVMLSGAADLSPDLARRVGErlGVEIIQGYGMTEASPVTHM-----MR 234
Cdd:PRK09088 226 GIThYFCVPQMAQAFRAQPGFDAAA--LRHlTALFTGGAPHAAEDILGWLDD--GIPMVDGFGMSEAGTVFGMsvdcdVI 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 235 RGDPLGIGRPVDGTETRIVG-----------GELWVRGPQLCSGYLGAPGPLV-----EGWLPTGDLVAPTPDGGLRVTG 298
Cdd:PRK09088 302 RAKAGAAGIPTPTVQTRVVDdqgndcpagvpGELLLRGPNLSPGYWRRPQATAraftgDGWFRTGDIARRDADGFFWVVD 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 299 RTKEIIKYRGYQVSPAELEEVIAACPGVRDVAV-ARGTLQGEEVPHAFVVGTAA----PAEVHEWVARRVAPYKKVRRVT 373
Cdd:PRK09088 382 RKKDMFISGGENVYPAEIEAVLADHPGIRECAVvGMADAQWGEVGYLAIVPADGapldLERIRSHLSTRLAKYKVPKHLR 461
|
410 420
....*....|....*....|.
gi 2713532039 374 VVESIPRAATGKILRRRLRER 394
Cdd:PRK09088 462 LVDALPRTASGKLQKARLRDA 482
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
43-394 |
1.71e-34 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 130.94 E-value: 1.71e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 43 DAPTARALhAGASRPLSPSpateDPEATAVLAlSSGTTAEPKPVMLSHRALSANIRQTVSALRGngldPGWSVLApLPLS 122
Cdd:PRK07824 16 DERRAALL-RDALRVGEPI----DDDVALVVA-TSGTTGTPKGAMLTAAALTASADATHDRLGG----PGQWLLA-LPAH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 123 HIYGLNVLLHSSLANGNHVVL-MPR-FTPRAFARLHAEHRIGWSY---VAPPIVAALDSEDYSADYSAEDfrhtrVMLSG 197
Cdd:PRK07824 85 HIAGLQVLVRSVIAGSEPVELdVSAgFDPTALPRAVAELGGGRRYtslVPMQLAKALDDPAATAALAELD-----AVLVG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 198 AADLSPDLARRVGErLGVEIIQGYGMTEASpvthmmrrGDPLGIGRPVDGTETRIVGGELWVRGPQLCSGYLGA--PGPL 275
Cdd:PRK07824 160 GGPAPAPVLDAAAA-AGINVVRTYGMSETS--------GGCVYDGVPLDGVRVRVEDGRIALGGPTLAKGYRNPvdPDPF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 276 VE-GWLPTGDLVAPTpDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAVArgtlqgeEVPH--------AFV 346
Cdd:PRK07824 231 AEpGWFRTDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVF-------GLPDdrlgqrvvAAV 302
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 2713532039 347 VGTAAPAEV----HEWVARRVAPYKKVRRVTVVESIPRAATGKILRRRLRER 394
Cdd:PRK07824 303 VGDGGPAPTlealRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVRR 354
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
2-391 |
2.27e-34 |
|
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: 132.37 E-value: 2.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 2 EFATAFHGILGAGATVVPLNPllteeetRRAVQRTGARLRIDAPTAralhagasrplspspATEDPEATAVLALSSGTTA 81
Cdd:cd05945 53 DAIAAFLAALKAGHAYVPLDA-------SSPAERIREILDAAKPAL---------------LIADGDDNAYIIFTSGSTG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 82 EPKPVMLSHRALSANIRQTVSALrgnGLDPGWSVLAPLPLShiYGLNVL-LHSSLANGNHVVLMPR---FTPRAFARLHA 157
Cdd:cd05945 111 RPKGVQISHDNLVSFTNWMLSDF---PLGPGDVFLNQAPFS--FDLSVMdLYPALASGATLVPVPRdatADPKQLFRFLA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 158 EHRIGWSYVAPPIVA-ALDSEDYSADYSAeDFRHtrVMLSGAAdLSPDLARRVGERL-GVEIIQGYGMTEAS-------P 228
Cdd:cd05945 186 EHGITVWVSTPSFAAmCLLSPTFTPESLP-SLRH--FLFCGEV-LPHKTARALQQRFpDARIYNTYGPTEATvavtyieV 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 229 VTHMMRRGDPLGIGRPVDGTETRIV-----------GGELWVRGPQLCSGYLGAPGPLVE--------GWLPTGDLVAPT 289
Cdd:cd05945 262 TPEVLDGYDRLPIGYAKPGAKLVILdedgrpvppgeKGELVISGPSVSKGYLNNPEKTAAaffpdegqRAYRTGDLVRLE 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 290 PDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRD-VAVARGTlqGEEVPH--AFVVGTAA-----PAEVHEWVAR 361
Cdd:cd05945 342 ADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEaVVVPKYK--GEKVTEliAFVVPKPGaeaglTKAIKAELAE 419
|
410 420 430
....*....|....*....|....*....|
gi 2713532039 362 RVAPYKKVRRVTVVESIPRAATGKILRRRL 391
Cdd:cd05945 420 RLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
1-400 |
4.04e-34 |
|
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: 134.60 E-value: 4.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 1 VEFATAFHGILGAGATVVPLNP------------------LLTEEETRRAVQRTGAR-LRIDAPTARAlhAGASRPLSPS 61
Cdd:COG1020 537 LEMVVALLAVLKAGAAYVPLDPaypaerlaymledagarlVLTQSALAARLPELGVPvLALDALALAA--EPATNPPVPV 614
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 62 pateDPEATAVLALSSGTTAEPKPVMLSHRALSANIRQTVSALrgnGLDPGWSVLAPLPLSH------IYGlnvllhsSL 135
Cdd:COG1020 615 ----TPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRY---GLGPGDRVLQFASLSFdasvweIFG-------AL 680
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 136 ANGNHVVLMP---RFTPRAFARLHAEHRIGWSYVAPPIVAALdsedysADYSAEDFRHTRVMLSGAADLSPDLARRVGER 212
Cdd:COG1020 681 LSGATLVLAPpeaRRDPAALAELLARHRVTVLNLTPSLLRAL------LDAAPEALPSLRLVLVGGEALPPELVRRWRAR 754
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 213 L-GVEIIQGYGMTEAS------PVTHMMRRGDPLGIGRPVDGTETRI-----------VGGELWVRGPQLCSGYLGAPGP 274
Cdd:COG1020 755 LpGARLVNLYGPTETTvdstyyEVTPPDADGGSVPIGRPIANTRVYVldahlqpvpvgVPGELYIGGAGLARGYLNRPEL 834
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 275 LVEGWLP------------TGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAV-ARGTLQGEEV 341
Cdd:COG1020 835 TAERFVAdpfgfpgarlyrTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVvAREDAPGDKR 914
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2713532039 342 PHAFVVG----TAAPAEVHEWVARRVAPYKKVRRVTVVESIPRAATGKILRRRLRERAGDADE 400
Cdd:COG1020 915 LVAYVVPeagaAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAAAAAA 977
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
1-392 |
6.85e-34 |
|
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: 131.02 E-value: 6.85e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 1 VEFATAFHGILGAGATVVPLNPLLTEEetrravqrtGARLRIDAPTARALhagasrplspspATEDPEATAVLALSSGTT 80
Cdd:cd05971 42 PECAIAHIAILRSGAIAVPLFALFGPE---------ALEYRLSNSGASAL------------VTDGSDDPALIIYTSGTT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 81 AEPKPVMLSHRALSANIrQTVSALRGNGLDPGWSVLAPLPLSHIYGLNVLLHSSLANGNHVVL--MPRFTPRAFARLHAE 158
Cdd:cd05971 101 GPPKGALHAHRVLLGHL-PGVQFPFNLFPRDGDLYWTPADWAWIGGLLDVLLPSLYFGVPVLAhrMTKFDPKAALDLMSR 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 159 HRIGWSYVaPPIVAALDSEDYsadysaEDFRHTRVML----SGAADLSPDLARRVGERLGVEIIQGYGMTEASPVT---H 231
Cdd:cd05971 180 YGVTTAFL-PPTALKMMRQQG------EQLKHAQVKLraiaTGGESLGEELLGWAREQFGVEVNEFYGQTECNLVIgncS 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 232 MMRRGDPLGIGRPVDGTETRIVG-----------GELWVRGPQLCS--GYLGAPG----PLVEGWLPTGDLVAPTPDGGL 294
Cdd:cd05971 253 ALFPIKPGSMGKPIPGHRVAIVDdngtplppgevGEIAVELPDPVAflGYWNNPSatekKMAGDWLLTGDLGRKDSDGYF 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 295 RVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAVA------RGtlqgeEVPHAFVV-------GTAAPAEVHEWVAR 361
Cdd:cd05971 333 WYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVgipdpiRG-----EIVKAFVVlnpgetpSDALAREIQELVKT 407
|
410 420 430
....*....|....*....|....*....|.
gi 2713532039 362 RVAPYKKVRRVTVVESIPRAATGKILRRRLR 392
Cdd:cd05971 408 RLAAHEYPREIEFVNELPRTATGKIRRRELR 438
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
1-393 |
9.85e-34 |
|
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: 131.50 E-value: 9.85e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 1 VEFATAFHGILGAGATVVPLNPLLTEEETRRAVQRTGARLRI--------------DAPTARALHAgASRPLSP------ 60
Cdd:TIGR02262 66 VDFPIAFLGAIRAGIVPVALNTLLTADDYAYMLEDSRARVVFvsgallpvikaalgKSPHLEHRVV-VGRPEAGevqlae 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 61 ---------SPATEDPEATAVLALSSGTTAEPKPVMLSHralsANIRQTVSALRGN--GLDPGWSVLAPLPLSHIYGLNV 129
Cdd:TIGR02262 145 llateseqfKPAATQADDPAFWLYSSGSTGMPKGVVHTH----SNPYWTAELYARNtlGIREDDVCFSAAKLFFAYGLGN 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 130 LLHSSLANGNHVVLMP-RFTPRAFARLHAEHRIGWSYVAPPIVAALDSEDysaDYSAEDFRHTRVMLSGAADLSPDLARR 208
Cdd:TIGR02262 221 ALTFPMSVGATTVLMGeRPTPDAVFDRLRRHQPTIFYGVPTLYAAMLADP---NLPSEDQVRLRLCTSAGEALPAEVGQR 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 209 VGERLGVEIIQGYGMTEA-----SPVTHMMRRGDPlgiGRPVDGTETRIVG-----------GELWVRGPQLCSGYLGAP 272
Cdd:TIGR02262 298 WQARFGVDIVDGIGSTEMlhiflSNLPGDVRYGTS---GKPVPGYRLRLVGdggqdvadgepGELLISGPSSATMYWNNR 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 273 GP----LVEGWLPTGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAV-ARGTLQGEEVPHAFVV 347
Cdd:TIGR02262 375 AKsrdtFQGEWTRSGDKYVRNDDGSYTYAGRTDDMLKVSGIYVSPFEIESALIQHPAVLEAAVvGVADEDGLIKPKAFVV 454
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 2713532039 348 ----GTAAPAEVHEWVARRVAPYKKVRRVTVVESIPRAATGKILRRRLRE 393
Cdd:TIGR02262 455 lrpgQTALETELKEHVKDRLAPYKYPRWIVFVDDLPKTATGKIQRFKLRE 504
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
43-393 |
2.01e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 131.20 E-value: 2.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 43 DAPTARALHAGASRPLSPSPATEDpeatAVLALSSGTTAEPKPVMLSHRALSANIRQTVSA--LRGNGldpgwSVLAPLP 120
Cdd:PRK07788 186 TDETLDDLIAGSSTAPLPKPPKPG----GIVILTSGTTGTPKGAPRPEPSPLAPLAGLLSRvpFRAGE-----TTLLPAP 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 121 LSHIYGLNVLLhSSLANGNHVVLMPRFTPRAFARLHAEHRIGwSYVAPP-----IVAALdsEDYSADYsaeDFRHTRVML 195
Cdd:PRK07788 257 MFHATGWAHLT-LAMALGSTVVLRRRFDPEATLEDIAKHKAT-ALVVVPvmlsrILDLG--PEVLAKY---DTSSLKIIF 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 196 SGAADLSPDLARRVGERLGVEIIQGYGMTEASPVT----HMMRRgDPLGIGRPVDGTETRI-----------VGGELWVR 260
Cdd:PRK07788 330 VSGSALSPELATRALEAFGPVLYNLYGSTEVAFATiatpEDLAE-APGTVGRPPKGVTVKIldengnevprgVVGRIFVG 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 261 GPQLCSGYLGAPGP-LVEGWLPTGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAVarGTLQGE 339
Cdd:PRK07788 409 NGFPFEGYTDGRDKqIIDGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAV--IGVDDE 486
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2713532039 340 EVPH---AFVV---GTA-APAEVHEWVARRVAPYKKVRRVTVVESIPRAATGKILRRRLRE 393
Cdd:PRK07788 487 EFGQrlrAFVVkapGAAlDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELRE 547
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
9-393 |
2.24e-33 |
|
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: 129.35 E-value: 2.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 9 GILGAGATVVPLNPLLTEEETRRAVQRTGARLRIDAPTaralhagasrplspspatedPEATAVLALSSGTTAEPKPVML 88
Cdd:cd17653 66 AILKAGAAYVPLDAKLPSARIQAILRTSGATLLLTTDS--------------------PDDLAYIIFTSGSTGIPKGVMV 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 89 SHRALSaNIRQTVSALRGNGldPGWSVLAPLPLSHIYGLNVLLhSSLANGNHVVLmprftprafarlhAEHRIGWSYVAP 168
Cdd:cd17653 126 PHRGVL-NYVSQPPARLDVG--PGSRVAQVLSIAFDACIGEIF-STLCNGGTLVL-------------ADPSDPFAHVAR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 169 PIVAALDSEDYSADYSAEDFRHTRVMLSGAADLSPDLARRVGErlGVEIIQGYGMTEASPVTHM--MRRGDPLGIGRPVD 246
Cdd:cd17653 189 TVDALMSTPSILSTLSPQDFPNLKTIFLGGEAVPPSLLDRWSP--GRRLYNAYGPTECTISSTMteLLPGQPVTIGKPIP 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 247 GTETRI-----------VGGELWVRGPQLCSGYLG---------APGPLVEGWL--PTGDLVAPTPDGGLRVTGRTKEII 304
Cdd:cd17653 267 NSTCYIldadlqpvpegVVGEICISGVQVARGYLGnpaltaskfVPDPFWPGSRmyRTGDYGRWTEDGGLEFLGREDNQV 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 305 KYRGYQVSPAELEEVI-AACPGVRDVAVargtLQGEEVPHAFVV-GTAAPAEVHEWVARRVAPYKKVRRVTVVESIPRAA 382
Cdd:cd17653 347 KVRGFRINLEEIEEVVlQSQPEVTQAAA----IVVNGRLVAFVTpETVDVDGLRSELAKHLPSYAVPDRIIALDSFPLTA 422
|
410
....*....|.
gi 2713532039 383 TGKILRRRLRE 393
Cdd:cd17653 423 NGKVDRKALRE 433
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
68-388 |
4.53e-33 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 126.61 E-value: 4.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 68 EATAVLALSSGTTAEPKPVMLSHRALSANIRQTVSAlrgnGLDpgWSV----LAPLPLSHIYGLNVLLHSSLANGNHVVL 143
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKE----GLN--WVVgdvtYLPLPATHIGGLWWILTCLIHGGLCVTG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 144 MPRFTPRAFARLHAEHRIGWSYVAPPIVAALDSEDYSADYSAEDFRHtrVMLSGAADLSPDlaRRVGERLG-VEIIQGYG 222
Cdd:cd17635 75 GENTTYKSLFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRL--IGYGGSRAIAAD--VRFIEATGlTNTAQVYG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 223 MTEASPVTHMMRRGDPLGI---GRPVDGTETRIVG-----------GELWVRGPQLCSGYLGAPGP----LVEGWLPTGD 284
Cdd:cd17635 151 LSETGTALCLPTDDDSIEInavGRPYPGVDVYLAAtdgiagpsasfGTIWIKSPANMLGYWNNPERtaevLIDGWVNTGD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 285 LVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAVAR------GTLQGEEVPHAFVVGTAAPAEVHEW 358
Cdd:cd17635 231 LGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEisdeefGELVGLAVVASAELDENAIRALKHT 310
|
330 340 350
....*....|....*....|....*....|
gi 2713532039 359 VARRVAPYKKVRRVTVVESIPRAATGKILR 388
Cdd:cd17635 311 IRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
74-388 |
6.90e-33 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 125.60 E-value: 6.90e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 74 ALSSGTTAEPKPVMLSHRALSANIRQTVSALRGNGLDpgwSVLAPLPLSHIYGLNVLLhSSLANGNHVVLMPRFTPRAFA 153
Cdd:cd17633 6 GFTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGED---AILAPGPLSHSLFLYGAI-SALYLGGTFIGQRKFNPKSWI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 154 RLHAEHRIGWSYVAPPIVAALDSEDysadysaEDFRHTRVMLSGAADLSPDLARRVGERL-GVEIIQGYGMTEASPVTHM 232
Cdd:cd17633 82 RKINQYNATVIYLVPTMLQALARTL-------EPESKIKSIFSSGQKLFESTKKKLKNIFpKANLIEFYGTSELSFITYN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 233 M--RRGDPLGIGRPVDGTETRI------VGGELWVRGPQLCSGYLGAPGPLVEGWLPTGDLVAPTPDGGLRVTGRTKEII 304
Cdd:cd17633 155 FnqESRPPNSVGRPFPNVEIEIrnadggEIGKIFVKSEMVFSGYVRGGFSNPDGWMSVGDIGYVDEEGYLYLVGRESDMI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 305 KYRGYQVSPAELEEVIAACPGVRDVAV-----ARGTlqgeEVPHAFVVGTAAPA-EVHEWVARRVAPYKKVRRVTVVESI 378
Cdd:cd17633 235 IIGGINIFPTEIESVLKAIPGIEEAIVvgipdARFG----EIAVALYSGDKLTYkQLKRFLKQKLSRYEIPKKIIFVDSL 310
|
330
....*....|
gi 2713532039 379 PRAATGKILR 388
Cdd:cd17633 311 PYTSSGKIAR 320
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
63-395 |
7.81e-33 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 129.51 E-value: 7.81e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 63 ATEDPEATAVLALSSGTTAEPKPVMLSHRALSANIRQTVSALrgnGLDPGWSVLAPLPLSHIYGLNVLLHSSLANGNHVV 142
Cdd:PRK12583 196 ASLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESL---GLTEHDRLCVPVPLYHCFGMVLANLGCMTVGACLV 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 143 L-MPRFTPRAFARLHAEHRIGWSYVAPPI-VAALDSedysADYSAEDFRHTRVMLSGAADLSPDLARRVGERLGV-EIIQ 219
Cdd:PRK12583 273 YpNEAFDPLATLQAVEEERCTALYGVPTMfIAELDH----PQRGNFDLSSLRTGIMAGAPCPIEVMRRVMDEMHMaEVQI 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 220 GYGMTEASPVTHMMRRGDPL-----GIGRPVDGTETRIVG-----------GELWVRGPQLCSGYLGAPGPLVE-----G 278
Cdd:PRK12583 349 AYGMTETSPVSLQTTAADDLerrveTVGRTQPHLEVKVVDpdgatvprgeiGELCTRGYSVMKGYWNNPEATAEsidedG 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 279 WLPTGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAV--ARGTLQGEEVPhAFVV----GTAAP 352
Cdd:PRK12583 429 WMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVfgVPDEKYGEEIV-AWVRlhpgHAASE 507
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2713532039 353 AEVHEWVARRVAPYKKVRRVTVVESIPRAATGKILRRRLRERA 395
Cdd:PRK12583 508 EELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMREIS 550
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
2-393 |
8.52e-33 |
|
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: 128.57 E-value: 8.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 2 EFATAFHGILGAGATVVPLNPLLTEEETRRAVQRTGAR-LRIDAP-TARALHAGASRPLSPSPATEDPEATAvLALSSGT 79
Cdd:cd12118 66 AMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKvLFVDREfEYEDLLAEGDPDFEWIPPADEWDPIA-LNYTSGT 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 80 TAEPKPVMLSHRALSANirqTVSALRGNGLDPGWSVLAPLPLSHIYGLNVLLHSSLANGNHVVLmPRFTPRAFARLHAEH 159
Cdd:cd12118 145 TGRPKGVVYHHRGAYLN---ALANILEWEMKQHPVYLWTLPMFHCNGWCFPWTVAAVGGTNVCL-RKVDAKAIYDLIEKH 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 160 RIGWSYVAPPIVAALDSedySADYSAEDFRHTRVMLSGAADLSPDLARRVgERLGVEIIQGYGMTEAS-PVT-------- 230
Cdd:cd12118 221 KVTHFCGAPTVLNMLAN---APPSDARPLPHRVHVMTAGAPPPAAVLAKM-EELGFDVTHVYGLTETYgPATvcawkpew 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 231 ---------HMMRR-------------GDPLGiGRPV--DGTETrivgGELWVRGPQLCSGYLGAPGPLVE----GWLPT 282
Cdd:cd12118 297 delpteeraRLKARqgvryvgleevdvLDPET-MKPVprDGKTI----GEIVFRGNIVMKGYLKNPEATAEafrgGWFHS 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 283 GDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAV-ARGTLQGEEVPHAFVV----GTAAPAEVHE 357
Cdd:cd12118 372 GDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVvARPDEKWGEVPCAFVElkegAKVTEEEIIA 451
|
410 420 430
....*....|....*....|....*....|....*.
gi 2713532039 358 WVARRVAPYKKVRRVTVVEsIPRAATGKILRRRLRE 393
Cdd:cd12118 452 FCREHLAGFMVPKTVVFGE-LPKTSTGKIQKFVLRD 486
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
78-395 |
1.18e-32 |
|
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: 126.06 E-value: 1.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 78 GTTAEPKPVMLSHralsANIRQTVSALRGNGL-DPGWSVLAPLPLSHIYGLNVLLHSSLANGNHVVLMprfTPRA----- 151
Cdd:cd05944 12 GTTGTPKLAQHTH----SNEVYNAWMLALNSLfDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLA---GPAGyrnpg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 152 ----FARLHAEHRIGWSYVAPPIVAALDSEDYSADYSAedfrhTRVMLSGAADLSPDLARRVGERLGVEIIQGYGMTEAS 227
Cdd:cd05944 85 lfdnFWKLVERYRITSLSTVPTVYAALLQVPVNADISS-----LRFAMSGAAPLPVELRARFEDATGLPVVEGYGLTEAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 228 PVTHMMRRGDPL---GIGRPVDGTETRIVG----------------GELWVRGPQLCSGYLGAPGPLV----EGWLPTGD 284
Cdd:cd05944 160 CLVAVNPPDGPKrpgSVGLRLPYARVRIKVldgvgrllrdcapdevGEICVAGPGVFGGYLYTEGNKNafvaDGWLNTGD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 285 LVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDV-AVARGTLQGEEVPHAFVV----GTAAPAEVHEWV 359
Cdd:cd05944 240 LGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAgAVGQPDAHAGELPVAYVQlkpgAVVEEEELLAWA 319
|
330 340 350
....*....|....*....|....*....|....*..
gi 2713532039 360 ARRVAPYKKV-RRVTVVESIPRAATGKILRRRLRERA 395
Cdd:cd05944 320 RDHVPERAAVpKHIEVLEELPVTAVGKVFKPALRADA 356
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
1-392 |
2.59e-32 |
|
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: 126.71 E-value: 2.59e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 1 VEFATAFHGILGAGATVVPLNPLLTEEETRRAVQRTGARLRIdaptaralhagasrplspspaTEDPEATAVLALSSGTT 80
Cdd:cd17649 48 LEMVVALLAILKAGGAYVPLDPEYPAERLRYMLEDSGAGLLL---------------------THHPRQLAYVIYTSGST 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 81 AEPKPVMLSHRALSANIRQTVSALrgnGLDPGWSVLAPLPLSHIYGLNVLLHSsLANGNHVVLMPR---FTPRAFARLHA 157
Cdd:cd17649 107 GTPKGVAVSHGPLAAHCQATAERY---GLTPGDRELQFASFNFDGAHEQLLPP-LICGACVVLRPDelwASADELAEMVR 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 158 EHRIGWSYVAPPIVAALdsedysadysAEDFRHT--------RVMLSGAADLSPDLARRVGeRLGVEIIQGYGMTEA--S 227
Cdd:cd17649 183 ELGVTVLDLPPAYLQQL----------AEEADRTgdgrppslRLYIFGGEALSPELLRRWL-KAPVRLFNAYGPTEAtvT 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 228 PVTHMMRRGDPLG-----IGRPVDGTETRIVG-----------GELWVRGPQLCSGYLGAPGPLVEGWLP---------- 281
Cdd:cd17649 252 PLVWKCEAGAARAgasmpIGRPLGGRSAYILDadlnpvpvgvtGELYIGGEGLARGYLGRPELTAERFVPdpfgapgsrl 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 282 --TGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAVARGTLQGEEVPHAFVVGTAA------PA 353
Cdd:cd17649 332 yrTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAGGKQLVAYVVLRAAaaqpelRA 411
|
410 420 430
....*....|....*....|....*....|....*....
gi 2713532039 354 EVHEWVARRVAPYKKVRRVTVVESIPRAATGKILRRRLR 392
Cdd:cd17649 412 QLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
49-392 |
3.08e-32 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 127.83 E-value: 3.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 49 ALHAGASRPLSPSPATedPEATAVLALSSGTTAEPKPVMLSHRALSANIRQTV----SALRGNGLDPGWSVLAPLPLSHI 124
Cdd:PRK07059 187 ALAEGARQTFKPVKLG--PDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQMEawlqPAFEKKPRPDQLNFVCALPLYHI 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 125 YGLNVLLHSSLANGNHVVLMPrfTPRAFARLHAEHRiGWSYVAPPIVAALdsedYSA-----DYSAEDFRHTRVMLSGAA 199
Cdd:PRK07059 265 FALTVCGLLGMRTGGRNILIP--NPRDIPGFIKELK-KYQVHIFPAVNTL----YNAllnnpDFDKLDFSKLIVANGGGM 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 200 DLSPDLARRVGERLGVEIIQGYGMTEASPVT--HMMRRGDPLG-IGRPVDGTETRI---------VG--GELWVRGPQLC 265
Cdd:PRK07059 338 AVQRPVAERWLEMTGCPITEGYGLSETSPVAtcNPVDATEFSGtIGLPLPSTEVSIrdddgndlpLGepGEICIRGPQVM 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 266 SGYLGAPGPLV-----EGWLPTGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAvARGTLQGE- 339
Cdd:PRK07059 418 AGYWNRPDETAkvmtaDGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVA-AVGVPDEHs 496
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2713532039 340 -EVPHAFVVG---TAAPAEVHEWVARRVAPYKKVRRVTVVESIPRAATGKILRRRLR 392
Cdd:PRK07059 497 gEAVKLFVVKkdpALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRRELR 553
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
83-388 |
4.14e-32 |
|
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341292 [Multi-domain] Cd Length: 333 Bit Score: 123.92 E-value: 4.14e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 83 PKPVMLSHRALSANIRQTVSALrgnGLDPGWSVLAPLPLSHIYGLNVLLHSSLANGNHVVlMPRFTPRAFARLHAEHRIG 162
Cdd:cd17637 15 PRGAVLSHGNLIAANLQLIHAM---GLTEADVYLNMLPLFHIAGLNLALATFHAGGANVV-MEKFDPAEALELIEEEKVT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 163 WSYVAPPIVAALDSEDYSADYSAEDFRHtrvmLSGAAdlSPDLARRVGERLGVEIIQGYGMTEASPVTHMMR-RGDPLGI 241
Cdd:cd17637 91 LMGSFPPILSNLLDAAEKSGVDLSSLRH----VLGLD--APETIQRFEETTGATFWSLYGQTETSGLVTLSPyRERPGSA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 242 GRPVDGTETRIVG-----------GELWVRGPQLCSGYLGAPG----PLVEGWLPTGDLVAPTPDGGLRVTGRT--KEII 304
Cdd:cd17637 165 GRPGPLVRVRIVDdndrpvpagetGEIVVRGPLVFQGYWNLPEltayTFRNGWHHTGDLGRFDEDGYLWYAGRKpeKELI 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 305 KYRGYQVSPAELEEVIAACPGVRDVAV--ARGTLQGEEVPHAFVVG---TAAPAEVHEWVARRVAPYKKVRRVTVVESIP 379
Cdd:cd17637 245 KPGGENVYPAEVEKVILEHPAIAEVCVigVPDPKWGEGIKAVCVLKpgaTLTADELIEFVGSRIARYKKPRYVVFVEALP 324
|
....*....
gi 2713532039 380 RAATGKILR 388
Cdd:cd17637 325 KTADGSIDR 333
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
1-391 |
4.65e-32 |
|
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: 126.47 E-value: 4.65e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 1 VEFATAFHGILGAGATVVPLNPLLTEEETRRAVQR---TGARLRIDAPTARALHAGASR------------PLSPSPATE 65
Cdd:cd05923 64 VEAVIALLALHRLGAVPALINPRLKAAELAELIERgemTAAVIAVDAQVMDAIFQSGVRvlalsdlvglgePESAGPLIE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 66 D----PEATAVLALSSGTTAEPKPVMLSHRALSANIrQTVSALRGNGLDPGWSVLAPLPLSHIYGLNVLLHSSLANGNHV 141
Cdd:cd05923 144 DpprePEQPAFVFYTSGTTGLPKGAVIPQRAAESRV-LFMSTQAGLRHGRHNVVLGLMPLYHVIGFFAVLVAALALDGTY 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 142 VLMPRFTPRAFARLHAEHRIGWSYVAPPIVAALDSEDYSADYSAEDFRHtrVMLSGAAdlSPD-LARRVGERLGVEIIQG 220
Cdd:cd05923 223 VVVEEFDPADALKLIEQERVTSLFATPTHLDALAAAAEFAGLKLSSLRH--VTFAGAT--MPDaVLERVNQHLPGEKVNI 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 221 YGMTEASPVThMMRRGDPLGIGRPVDGTETRIVG--------------GELWVR--GPQLCSGYLGAP----GPLVEGWL 280
Cdd:cd05923 299 YGTTEAMNSL-YMRDARTGTEMRPGFFSEVRIVRiggspdealangeeGELIVAaaADAAFTGYLNQPeataKKLQDGWY 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 281 PTGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAV--ARGTLQGEEVPhAFVVGTAAPAEVHEW 358
Cdd:cd05923 378 RTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVigVADERWGQSVT-ACVVPREGTLSADEL 456
|
410 420 430
....*....|....*....|....*....|....*..
gi 2713532039 359 ----VARRVAPYKKVRRVTVVESIPRAATGKILRRRL 391
Cdd:cd05923 457 dqfcRASELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
46-397 |
1.08e-31 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 125.76 E-value: 1.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 46 TARALHAGASRPlspsPATEDPEATAVLALSSGTTAEPKPVMLSHRALSANIRQTVSALRgngLDPGWSVLAPLPLSHIY 125
Cdd:PRK07514 138 LEAAAAAPDDFE----TVPRGADDLAAILYTSGTTGRSKGAMLSHGNLLSNALTLVDYWR---FTPDDVLIHALPIFHTH 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 126 GLNVLLHSSLANGNHVVLMPRFTPRAFARL--HAEHRIGwsyVAPPIVAALDSEDYSADYSAedfrHTRVMLSGAADLSP 203
Cdd:PRK07514 211 GLFVATNVALLAGASMIFLPKFDPDAVLALmpRATVMMG---VPTFYTRLLQEPRLTREAAA----HMRLFISGSAPLLA 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 204 DLARRVGERLGVEIIQGYGMTEASPVTHMMRRGDPLG--IGRPVDGTETRIVG------------GELWVRGPQLCSGYL 269
Cdd:PRK07514 284 ETHREFQERTGHAILERYGMTETNMNTSNPYDGERRAgtVGFPLPGVSLRVTDpetgaelppgeiGMIEVKGPNVFKGYW 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 270 GAPGPLVE-----GWLPTGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAVArgtlqgeEVPH- 343
Cdd:PRK07514 364 RMPEKTAEefradGFFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVI-------GVPHp 436
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2713532039 344 -------AFVVGTAA----PAEVHEWVARRVAPYKKVRRVTVVESIPRAATGKILRRRLRERAGD 397
Cdd:PRK07514 437 dfgegvtAVVVPKPGaaldEAAILAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLLREQYAD 501
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
52-386 |
2.64e-31 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 126.23 E-value: 2.64e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 52 AGASRPLSPSPaTEDPEATAVLALSSGTTAEPKPVMLSHRALSANIRQTVSALRGNGLDpgwSVLAPLPLSHIYGLNVLL 131
Cdd:PRK06814 778 LAGRFPLVYFC-NRDPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPED---KVFNALPVFHSFGLTGGL 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 132 HSSLANGNHVVLMPrfTPrafarLHaeHRIgwsyvAPPIVAA-----LDSED-----YSADYSAEDFRHTRVMLSGAADL 201
Cdd:PRK06814 854 VLPLLSGVKVFLYP--SP-----LH--YRI-----IPELIYDtnatiLFGTDtflngYARYAHPYDFRSLRYVFAGAEKV 919
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 202 SPDLARRVGERLGVEIIQGYGMTEASPV----THMMRRgdPLGIGRPVDGTETRIV-------GGELWVRGPQLCSGYLG 270
Cdd:PRK06814 920 KEETRQTWMEKFGIRILEGYGVTETAPVialnTPMHNK--AGTVGRLLPGIEYRLEpvpgideGGRLFVRGPNVMLGYLR 997
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 271 A--PG---PLVEGWLPTGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAAC-PGVRDVAVAR-GTLQGEEVPH 343
Cdd:PRK06814 998 AenPGvlePPADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELwPDALHAAVSIpDARKGERIIL 1077
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 2713532039 344 AFVVGTAAPAEVHEWVARRVAPYKKV-RRVTVVESIPRAATGKI 386
Cdd:PRK06814 1078 LTTASDATRAAFLAHAKAAGASELMVpAEIITIDEIPLLGTGKI 1121
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
1-391 |
7.77e-31 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 125.27 E-value: 7.77e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 1 VEFATAFHGILGAGATVVPLNPLLTEEETRRAVQRTGARL---------RIDAPTA-RALH-AGASRPLSPSPATE---- 65
Cdd:PRK12467 573 IEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLlltqshllaQLPVPAGlRSLClDEPADLLCGYSGHNpeva 652
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 66 -DPEATAVLALSSGTTAEPKPVMLSHRALsANIRQTVSALRGNGLDPGWSVLAPLP--LSHiyglnVLLHSSLANGNHVV 142
Cdd:PRK12467 653 lDPDNLAYVIYTSGSTGQPKGVAISHGAL-ANYVCVIAERLQLAADDSMLMVSTFAfdLGV-----TELFGALASGATLH 726
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 143 LMPR---FTPRAFARLHAEHRIGWSYVAPPIVAALdsedYSADYSAEDFRHTRVMLSGAAdLSPDLARRVGE-RLGVEII 218
Cdd:PRK12467 727 LLPPdcaRDAEAFAALMADQGVTVLKIVPSHLQAL----LQASRVALPRPQRALVCGGEA-LQVDLLARVRAlGPGARLI 801
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 219 QGYGMTEAS-PVTHMMRRGDPLG-----IGRPVDGTETRI-----------VGGELWVRGPQLCSGYLGAPGPLVEGWLP 281
Cdd:PRK12467 802 NHYGPTETTvGVSTYELSDEERDfgnvpIGQPLANLGLYIldhylnpvpvgVVGELYIGGAGLARGYHRRPALTAERFVP 881
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 282 ------------TGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAVARGTLQGEEVPHAFVVgT 349
Cdd:PRK12467 882 dpfgadggrlyrTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQLVAYLV-P 960
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 2713532039 350 AAPAEVHEWVARRVAPYKKVRRV----------TVVESIPRAATGKILRRRL 391
Cdd:PRK12467 961 AAVADGAEHQATRDELKAQLRQVlpdymvpahlLLLDSLPLTPNGKLDRKAL 1012
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
1-391 |
1.04e-30 |
|
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: 121.98 E-value: 1.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 1 VEFATAFHGILGAGATVVPLNPLLTEEETRRAVQRTGARLRIdaptaralhagasrplspspatEDPEATAVLALSSGTT 80
Cdd:cd17652 48 AELVVAILAVLKAGAAYLPLDPAYPAERIAYMLADARPALLL----------------------TTPDNLAYVIYTSGST 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 81 AEPKPVMLSHRALSANIRQTVSALRgngLDPGWSVLAPLPLSHIYGLNVLLhSSLANGNHVVLMPRFT---PRAFARLHA 157
Cdd:cd17652 106 GRPKGVVVTHRGLANLAAAQIAAFD---VGPGSRVLQFASPSFDASVWELL-MALLAGATLVLAPAEEllpGEPLADLLR 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 158 EHRIGWSYVAPPIVAALDSEDYSADysaedfrhtRVMLSGAADLSPDLARR--VGERLgveiIQGYGMTEASPVTHMMR- 234
Cdd:cd17652 182 EHRITHVTLPPAALAALPPDDLPDL---------RTLVVAGEACPAELVDRwaPGRRM----INAYGPTETTVCATMAGp 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 235 --RGDPLGIGRPVDGTETRI-----------VGGELWVRGPQLCSGYLGAPGPLVEGWLP------------TGDLVAPT 289
Cdd:cd17652 249 lpGGGVPPIGRPVPGTRVYVldarlrpvppgVPGELYIAGAGLARGYLNRPGLTAERFVAdpfgapgsrmyrTGDLARWR 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 290 PDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRD-VAVARGTLQGEEVPHAFVVG----TAAPAEVHEWVARRVA 364
Cdd:cd17652 329 ADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEaVVVVRDDRPGDKRLVAYVVPapgaAPTAAELRAHLAERLP 408
|
410 420
....*....|....*....|....*..
gi 2713532039 365 PYKKVRRVTVVESIPRAATGKILRRRL 391
Cdd:cd17652 409 GYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
66-396 |
1.28e-30 |
|
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: 122.08 E-value: 1.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 66 DPEATAVLALSSGTTAEPKPVMLSHRALsanIRQTVSALRGNGLDPGWSVLAPLPLSHIYGLNVLLHSSLANGNHVVLMP 145
Cdd:cd17640 86 DSDDLATIIYTSGTTGNPKGVMLTHANL---LHQIRSLSDIVPPQPGDRFLSILPIWHSYERSAEYFIFACGCSQAYTSI 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 146 RFTPRAFARLHAEHRIG----WSYVAPPIVAALDSEDYSADYSAEDF---RHTRVMLSGAADLsPDLARRVGERLGVEII 218
Cdd:cd17640 163 RTLKDDLKRVKPHYIVSvprlWESLYSGIQKQVSKSSPIKQFLFLFFlsgGIFKFGISGGGAL-PPHVDTFFEAIGIEVL 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 219 QGYGMTEASPVTHMMRRGDPL--GIGRPVDGTETRIVG------------GELWVRGPQLCSGYLGAPGPLVE-----GW 279
Cdd:cd17640 242 NGYGLTETSPVVSARRLKCNVrgSVGRPLPGTEIKIVDpegnvvlppgekGIVWVRGPQVMKGYYKNPEATSKvldsdGW 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 280 LPTGDLVAPTPDGGLRVTGRTKEIIKYR-GYQVSPAELEEVIAACPGVRDVAVArGtlQGEEVPHAFVVGTAapAEVHEW 358
Cdd:cd17640 322 FNTGDLGWLTCGGELVLTGRAKDTIVLSnGENVEPQPIEEALMRSPFIEQIMVV-G--QDQKRLGALIVPNF--EELEKW 396
|
330 340 350
....*....|....*....|....*....|....*...
gi 2713532039 359 VARRVAPYKKVRRVTVVESIPRAATGKILRRRLRERAG 396
Cdd:cd17640 397 AKESGVKLANDRSQLLASKKVLKLYKNEIKDEISNRPG 434
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
50-331 |
4.34e-30 |
|
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: 121.55 E-value: 4.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 50 LHAGASRPLSPSPATedPEATAVLALSSGTTAEPKPVMLSHRALSANIRQTVSAL-RGNGLDPGWSVLAPLPLSHIYGLN 128
Cdd:cd05927 98 EKLGKKNKVPPPPPK--PEDLATICYTSGTTGNPKGVMLTHGNIVSNVAGVFKILeILNKINPTDVYISYLPLAHIFERV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 129 VLlHSSLANGNHV---------------VLMPRF---TPRAFARLHAehRIgWSYVA--PPIVAALdsEDYSADYSAEDF 188
Cdd:cd05927 176 VE-ALFLYHGAKIgfysgdirlllddikALKPTVfpgVPRVLNRIYD--KI-FNKVQakGPLKRKL--FNFALNYKLAEL 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 189 RHT------------------------RVMLSGAADLSPDLARRVGERLGVEIIQGYGMTEASPVTHMMRRGDP-LG-IG 242
Cdd:cd05927 250 RSGvvraspfwdklvfnkikqalggnvRLMLTGSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATLTLPGDTsVGhVG 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 243 RPVDGTETRIV--------------GGELWVRGPQLCSGYLGAPGP-----LVEGWLPTGDLVAPTPDGGLRVTGRTKEI 303
Cdd:cd05927 330 GPLPCAEVKLVdvpemnydakdpnpRGEVCIRGPNVFSGYYKDPEKtaealDEDGWLHTGDIGEWLPNGTLKIIDRKKNI 409
|
330 340
....*....|....*....|....*....
gi 2713532039 304 IKY-RGYQVSPAELEEVIAACPGVRDVAV 331
Cdd:cd05927 410 FKLsQGEYVAPEKIENIYARSPFVAQIFV 438
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
83-384 |
5.04e-30 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 118.17 E-value: 5.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 83 PKPVMLSHRALsanIRQTVSALRGNGLDPGWSVLAPLPLSHIYGLNVLLHSSLANGNHVVlMPRFTPRAFARLHAEHRIG 162
Cdd:cd17636 15 PNGALLSHQAL---LAQALVLAVLQAIDEGTVFLNSGPLFHIGTLMFTLATFHAGGTNVF-VRRVDAEEVLELIEAERCT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 163 WSYVAPPIVAALDSEDYSADYSAEDFRHTRVMlSGAADLSPDLARRVGERLGveiiqGYGMTEAS--PVTHMMRRGDPLG 240
Cdd:cd17636 91 HAFLLPPTIDQIVELNADGLYDLSSLRSSPAA-PEWNDMATVDTSPWGRKPG-----GYGQTEVMglATFAALGGGAIGG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 241 IGRPVDGTETRIVG-----------GELWVRGPQLCSGYLGAPG----PLVEGWLPTGDLVAPTPDGGLRVTGRTKEIIK 305
Cdd:cd17636 165 AGRPSPLVQVRILDedgrevpdgevGEIVARGPTVMAGYWNRPEvnarRTRGGWHHTNDLGRREPDGSLSFVGPKTRMIK 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 306 YRGYQVSPAELEEVIAACPGVRDVAVArgtlqgeEVP--------HAFVV----GTAAPAEVHEWVARRVAPYKKVRRVT 373
Cdd:cd17636 245 SGAENIYPAEVERCLRQHPAVADAAVI-------GVPdprwaqsvKAIVVlkpgASVTEAELIEHCRARIASYKKPKSVE 317
|
330
....*....|.
gi 2713532039 374 VVESIPRAATG 384
Cdd:cd17636 318 FADALPRTAGG 328
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
77-395 |
7.07e-30 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 121.07 E-value: 7.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 77 SGTTAEPKPVMLSHRALSANIRQTVSALRgngLDPGWSVLAPLPLSHIYG--LNVLlhSSLANGNHVVLM-PRFTPRAFA 153
Cdd:PRK08315 208 SGTTGFPKGATLTHRNILNNGYFIGEAMK---LTEEDRLCIPVPLYHCFGmvLGNL--ACVTHGATMVYPgEGFDPLATL 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 154 RLHAEHRIGWSYVAPPI-VAALDSEDYsADYsaeDFRHTR--VMlsgAADLSP-DLARRVGERLGV-EIIQGYGMTEASP 228
Cdd:PRK08315 283 AAVEEERCTALYGVPTMfIAELDHPDF-ARF---DLSSLRtgIM---AGSPCPiEVMKRVIDKMHMsEVTIAYGMTETSP 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 229 VTHMMRRGDPL-----GIGRPVDGTETRIVG------------GELWVRGPQLCSGYLGAPGPLVE-----GWLPTGDLV 286
Cdd:PRK08315 356 VSTQTRTDDPLekrvtTVGRALPHLEVKIVDpetgetvprgeqGELCTRGYSVMKGYWNDPEKTAEaidadGWMHTGDLA 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 287 APTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAV-----ARgtlQGEEVpHAFVV----GTAAPAEVHE 357
Cdd:PRK08315 436 VMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQDVQVvgvpdEK---YGEEV-CAWIIlrpgATLTEEDVRD 511
|
330 340 350
....*....|....*....|....*....|....*...
gi 2713532039 358 WVARRVAPYKKVRRVTVVESIPRAATGKILRRRLRERA 395
Cdd:PRK08315 512 FCRGKIAHYKIPRYIRFVDEFPMTVTGKIQKFKMREMM 549
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
63-395 |
1.17e-29 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 121.57 E-value: 1.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 63 ATEDPEATAVLALSSGTTAEPKPVMLSHRALSANIRQTVSALRGNGLDpgwSVLAPLPLSHIYGLNVLLHSSLANGNHVV 142
Cdd:PRK08633 777 PTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDD---VILSSLPFFHSFGLTVTLWLPLLEGIKVV 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 143 LMPRFT-PRAFARLHAEHR----IGWS-----YVAPPIVaaldsedysadySAEDFRHTRVMLSGAADLSPDLARRVGER 212
Cdd:PRK08633 854 YHPDPTdALGIAKLVAKHRatilLGTPtflrlYLRNKKL------------HPLMFASLRLVVAGAEKLKPEVADAFEEK 921
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 213 LGVEIIQGYGMTEASPVT------HMM-----RRGDPLG-IGRPVDGTETRIV---------GGE---LWVRGPQLCSGY 268
Cdd:PRK08633 922 FGIRILEGYGATETSPVAsvnlpdVLAadfkrQTGSKEGsVGMPLPGVAVRIVdpetfeelpPGEdglILIGGPQVMKGY 1001
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 269 LGAPGPLVE--------GWLPTGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAVARGTL---- 336
Cdd:PRK08633 1002 LGDPEKTAEvikdidgiGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKALGGEEVVFAVTAVpdek 1081
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 337 QGEEVPHAFVVGTAAPAEVHEWVAR-RVAPYKKVRRVTVVESIPRAATGKILRRRLRERA 395
Cdd:PRK08633 1082 KGEKLVVLHTCGAEDVEELKRAIKEsGLPNLWKPSRYFKVEALPLLGSGKLDLKGLKELA 1141
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
6-391 |
1.23e-29 |
|
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: 119.32 E-value: 1.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 6 AFHGILGAGATVVPLNP------------------LLTEEETRravqrtgARLRIDAPTARALHAGASRPLSPSPATEDP 67
Cdd:cd12116 53 AMLAVLKAGAAYVPLDPdypadrlryiledaepalVLTDDALP-------DRLPAGLPVLLLALAAAAAAPAAPRTPVSP 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 68 EATAVLALSSGTTAEPKPVMLSHRALS---ANIRQTVsalrgnGLDPGWSVLAPLPLS-HIYGLNVLLhsSLANGNHVVL 143
Cdd:cd12116 126 DDLAYVIYTSGSTGRPKGVVVSHRNLVnflHSMRERL------GLGPGDRLLAVTTYAfDISLLELLL--PLLAGARVVI 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 144 MPRFT---PRAFARLHAEHRIGWSYVAPPIVAALDSEDYSAdysAEDFRhtrvMLSGAADLSPDLARRVGERLGvEIIQG 220
Cdd:cd12116 198 APRETqrdPEALARLIEAHSITVMQATPATWRMLLDAGWQG---RAGLT----ALCGGEALPPDLAARLLSRVG-SLWNL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 221 YGMTEASPVTHMMRRGDPLG---IGRPVDGTETRI-----------VGGELWVRGPQLCSGYLGAPGPLVEGWLP----- 281
Cdd:cd12116 270 YGPTETTIWSTAARVTAAAGpipIGRPLANTQVYVldaalrpvppgVPGELYIGGDGVAQGYLGRPALTAERFVPdpfag 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 282 -------TGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAVARGTLQGEEVPHAFVVGTAAPA- 353
Cdd:cd12116 350 pgsrlyrTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRRLVAYVVLKAGAAp 429
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 2713532039 354 ---EVHEWVARRVAPYKKVRRVTVVESIPRAATGKILRRRL 391
Cdd:cd12116 430 daaALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
66-393 |
1.26e-29 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 120.20 E-value: 1.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 66 DPEATAVLALSSGTTAEPKPVMLSHRalSANIRQTVSAL-RGNGLDPGWSVLAPLPLSHI--YGLNvllHSSLANGNHVV 142
Cdd:PRK07008 174 DENQASSLCYTSGTTGNPKGALYSHR--STVLHAYGAALpDAMGLSARDAVLPVVPMFHVnaWGLP---YSAPLTGAKLV 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 143 LM-PRFTPRAFARLHAEHRIGWSYVAPPIVAALDSEDYSADYSAEDFRhtRVMLSGAAdLSPDLARRVGERLGVEIIQGY 221
Cdd:PRK07008 249 LPgPDLDGKSLYELIEAERVTFSAGVPTVWLGLLNHMREAGLRFSTLR--RTVIGGSA-CPPAMIRTFEDEYGVEVIHAW 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 222 GMTEASPV--------THMMRRGDP-----LGIGRPVDGTETRIVG-------------GELWVRGPQLCSGYLGAPG-P 274
Cdd:PRK07008 326 GMTEMSPLgtlcklkwKHSQLPLDEqrkllEKQGRVIYGVDMKIVGddgrelpwdgkafGDLQVRGPWVIDRYFRGDAsP 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 275 LVEGWLPTGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVA-VARGTLQGEEVPHAFVV----GT 349
Cdd:PRK07008 406 LVDGWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAAcIACAHPKWDERPLLVVVkrpgAE 485
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 2713532039 350 AAPAEVHEWVARRVAPYKKVRRVTVVESIPRAATGKILRRRLRE 393
Cdd:PRK07008 486 VTREELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLRE 529
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
6-397 |
1.48e-29 |
|
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: 119.18 E-value: 1.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 6 AFHGILGAGATVVPLNPLLTEEETRRAVQRTGARLRIdaptaralhagasrplspspaTEDPEATAVLALSSGTTAEPKP 85
Cdd:cd05918 65 AMLAVLKAGGAFVPLDPSHPLQRLQEILQDTGAKVVL---------------------TSSPSDAAYVIFTSGSTGKPKG 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 86 VMLSHRALSANIRQTVSALrgnGLDPGWSVL--AplplSHIYGLNVL-LHSSLANGNHVVLMPRFTPR-AFARLHAEHRI 161
Cdd:cd05918 124 VVIEHRALSTSALAHGRAL---GLTSESRVLqfA----SYTFDVSILeIFTTLAAGGCLCIPSEEDRLnDLAGFINRLRV 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 162 GWSyVAPPIVAALdsedysadYSAEDFRHTRVMLSGAADLSPDLARRVGERlgVEIIQGYGMTEASPVT---HMMRRGDP 238
Cdd:cd05918 197 TWA-FLTPSVARL--------LDPEDVPSLRTLVLGGEALTQSDVDTWADR--VRLINAYGPAECTIAAtvsPVVPSTDP 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 239 LGIGRPVDGT--------ETRIV--G--GELWVRGPQLCSGYLGAPG------PLVEGWLP------------TGDLVAP 288
Cdd:cd05918 266 RNIGRPLGATcwvvdpdnHDRLVpiGavGELLIEGPILARGYLNDPEktaaafIEDPAWLKqegsgrgrrlyrTGDLVRY 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 289 TPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAVA----RGTLQGEEVPHAFVVG---------------- 348
Cdd:cd05918 346 NPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKEVVVevvkPKDGSSSPQLVAFVVLdgsssgsgdgdslfle 425
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 2713532039 349 -----TAAPAEVHEWVARRVAPYKKVRRVTVVESIPRAATGKILRRRLRERAGD 397
Cdd:cd05918 426 psdefRALVAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRALRELAES 479
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
1-397 |
5.28e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 117.96 E-value: 5.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 1 VEFATAFHGILGAGATVVPLNPLLTEEETRRAVQRTGARL---------RIDAPTARALHAGASRPL----SPSPA-TED 66
Cdd:PRK07638 61 IEFLQLFAGAAMAGWTCVPLDIKWKQDELKERLAISNADMivteryklnDLPDEEGRVIEIDEWKRMiekyLPTYApIEN 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 67 PE-ATAVLALSSGTTAEPKPVMLSHRALSANIRQTVSALrgnGLDPGWSVLAPLPLSH---IYGLNvllhSSLANGNHVV 142
Cdd:PRK07638 141 VQnAPFYMGFTSGSTGKPKAFLRAQQSWLHSFDCNVHDF---HMKREDSVLIAGTLVHslfLYGAI----STLYVGQTVH 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 143 LMPRFTP-RAFARLHAEhRIGWSYVAPPIVAALdsedysadYSAEDFRHTRV-MLSGAADLSPDLARRVGER-LGVEIIQ 219
Cdd:PRK07638 214 LMRKFIPnQVLDKLETE-NISVMYTVPTMLESL--------YKENRVIENKMkIISSGAKWEAEAKEKIKNIfPYAKLYE 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 220 GYGMTEASPVTHMM-----RRgdPLGIGRPVDGTETRIVG-----------GELWVRGPQLCSGYLG----APGPLVEGW 279
Cdd:PRK07638 285 FYGASELSFVTALVdeeseRR--PNSVGRPFHNVQVRICNeageevqkgeiGTVYVKSPQFFMGYIIggvlARELNADGW 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 280 LPTGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAV--ARGTLQGeEVPHAFVVGTAAPAEVHE 357
Cdd:PRK07638 363 MTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVigVPDSYWG-EKPVAIIKGSATKQQLKS 441
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2713532039 358 WVARRVAPYKKVRRVTVVESIPRAATGKILRRRLRERAGD 397
Cdd:PRK07638 442 FCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAKSWIEN 481
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
2-391 |
6.91e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 116.67 E-value: 6.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 2 EFATAFHGILGAGATVVPLNPllteeETRRAVQRtgaRLRIDAPTARALHAGASRPLSPSPaTEDPEATAVLALSSGTTA 81
Cdd:PRK08308 44 DIITLVFFLKEKGASVLPIHP-----DTPKEAAI---RMAKRAGCHGLLYGESDFTKLEAV-NYLAEEPSLLQYSSGTTG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 82 EPKPVMLSHRALSANIRQTVSALRGNgldpgwSVLAPL---PLSHIYGLNVLLHSSLANGNHVVLMPRFTPR-AFARL-- 155
Cdd:PRK08308 115 EPKLIRRSWTEIDREIEAYNEALNCE------QDETPIvacPVTHSYGLICGVLAALTRGSKPVIITNKNPKfALNILrn 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 156 HAEHRIgwsYVAPPIVAALDSedysadYSAEDFRHTRVMLSGAadLSPD-LARRVGERlGVEIIQGYGMTEASPVTHMMR 234
Cdd:PRK08308 189 TPQHIL---YAVPLMLHILGR------LLPGTFQFHAVMTSGT--PLPEaWFYKLRER-TTYMMQQYGCSEAGCVSICPD 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 235 RGDPLGIGRPVDGTETRIVGGElwvrgpqlcsgylGAPGPLV----EGWLPTGDLVAPTPDGGLRVTGRTKEIIKYRGYQ 310
Cdd:PRK08308 257 MKSHLDLGNPLPHVSVSAGSDE-------------NAPEEIVvkmgDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLN 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 311 VSPAELEEVIAACPGVRDVAVARG--TLQGEEVPHAFVV-GTAAPAEVHEWVARRVAPYKKVRRVTVVESIPRAATGKIL 387
Cdd:PRK08308 324 VYPIEVEDVMLRLPGVQEAVVYRGkdPVAGERVKAKVIShEEIDPVQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVS 403
|
....
gi 2713532039 388 RRRL 391
Cdd:PRK08308 404 RKLL 407
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
58-393 |
7.09e-29 |
|
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: 117.48 E-value: 7.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 58 LSPSPATEDPEATAVLALSSGTTAEPKPVMLSHRALSANIRQTVSALRGNGLDPGWSVLAPLPLSHIYGLNVLlHSSLAN 137
Cdd:cd05929 115 GSPETPIEDEAAGWKMLYSGGTTGRPKGIKRGLPGGPPDNDTLMAAALGFGPGADSVYLSPAPLYHAAPFRWS-MTALFM 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 138 GNHVVLMPRFTPRAFARLHAEHRIGWSYVAPPI---VAALdsedYSADYSAEDFRHTRVMLSGAADLSPDLARRVGERLG 214
Cdd:cd05929 194 GGTLVLMEKFDPEEFLRLIERYRVTFAQFVPTMfvrLLKL----PEAVRNAYDLSSLKRVIHAAAPCPPWVKEQWIDWGG 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 215 VEIIQGYGMTEASPVTHMmrRGD-----PLGIGRPVDGtETRIVG-----------GELWVRGPqlcSGYLGAPGPLVE- 277
Cdd:cd05929 270 PIIWEYYGGTEGQGLTII--NGEewlthPGSVGRAVLG-KVHILDedgnevppgeiGEVYFANG---PGFEYTNDPEKTa 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 278 ------GWLPTGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAV--ARGTLQGEEVpHAFV--- 346
Cdd:cd05929 344 aarnegGWSTLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVvgVPDEELGQRV-HAVVqpa 422
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 2713532039 347 ----VGTAAPAEVHEWVARRVAPYKKVRRVTVVESIPRAATGKILRRRLRE 393
Cdd:cd05929 423 pgadAGTALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLRD 473
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
9-395 |
2.14e-28 |
|
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: 115.68 E-value: 2.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 9 GILGAGATVVPLNPLLTEEETRRAVQRTGARLRIDAPTaralhagasrpLSPSPATEDPeatAVLALSSGTTAEPKPVML 88
Cdd:cd05969 44 GIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTEE-----------LYERTDPEDP---TLLHYTSGTTGTPKGVLH 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 89 SHRALsanIRQTVSALRGNGL----------DPGWsvlaplplshIYGLNVLLHSSLANG-NHVVLMPRFTPRAFARLHA 157
Cdd:cd05969 110 VHDAM---IFYYFTGKYVLDLhpddiywctaDPGW----------VTGTVYGIWAPWLNGvTNVVYEGRFDAESWYGIIE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 158 EHRIGWSYVAPPIVAALDSEDysaDYSAE--DFRHTRVMLSGAADLSPDLARRVGERLGVEIIQGYGMTEASPV---THM 232
Cdd:cd05969 177 RVKVTVWYTAPTAIRMLMKEG---DELARkyDLSSLRFIHSVGEPLNPEAIRWGMEVFGVPIHDTWWQTETGSImiaNYP 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 233 MRRGDPLGIGRPVDGTETRIVG-----------GELWVRG--PQLCSGYLGAPG----PLVEGWLPTGDLVAPTPDGGLR 295
Cdd:cd05969 254 CMPIKPGSMGKPLPGVKAAVVDengnelppgtkGILALKPgwPSMFRGIWNDEEryknSFIDGWYLTGDLAYRDEDGYFW 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 296 VTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAV-ARGTLQGEEVPHAFVV-------GTAAPAEVHEWVARRVAPYK 367
Cdd:cd05969 334 FVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGViGKPDPLRGEIIKAFISlkegfepSDELKEEIINFVRQKLGAHV 413
|
410 420
....*....|....*....|....*...
gi 2713532039 368 KVRRVTVVESIPRAATGKILRRRLRERA 395
Cdd:cd05969 414 APREIEFVDNLPKTRSGKIMRRVLKAKE 441
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
9-391 |
9.83e-28 |
|
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: 113.91 E-value: 9.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 9 GILGAGATVVPLNPLLTEEETRRAVQRTGARLRI--------DAPTARALHAGAS---RPLSPSPATEDPEATAVLALSS 77
Cdd:cd12114 56 GILAAGAAYVPVDIDQPAARREAILADAGARLVLtdgpdaqlDVAVFDVLILDLDalaAPAPPPPVDVAPDDLAYVIFTS 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 78 GTTAEPKPVMLSHRALSANIRQTVSALrgnGLDPGWSVLAPLPLSH------IYGLnvllhssLANGNHVVLMP---RFT 148
Cdd:cd12114 136 GSTGTPKGVMISHRAALNTILDINRRF---AVGPDDRVLALSSLSFdlsvydIFGA-------LSAGATLVLPDearRRD 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 149 PRAFARLHAEHRIG-WSYVaPPIVAALDSEDYSADYSAEDFRHtrVMLSGaaDLSP-DLARRVGERL-GVEIIQGYGMTE 225
Cdd:cd12114 206 PAHWAELIERHGVTlWNSV-PALLEMLLDVLEAAQALLPSLRL--VLLSG--DWIPlDLPARLRALApDARLISLGGATE 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 226 AS------PVTHMMRRGDPLGIGRPVDGTETRI-----------VGGELWVRGPQLCSGYLGAPG---------PLVEGW 279
Cdd:cd12114 281 ASiwsiyhPIDEVPPDWRSIPYGRPLANQRYRVldprgrdcpdwVPGELWIGGRGVALGYLGDPEltaarfvthPDGERL 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 280 LPTGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAVARGTLQGEEVPHAFVV-----GTAAPAE 354
Cdd:cd12114 361 YRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDPGGKRLAAFVVpdndgTPIAPDA 440
|
410 420 430
....*....|....*....|....*....|....*..
gi 2713532039 355 VHEWVARRVAPYKKVRRVTVVESIPRAATGKILRRRL 391
Cdd:cd12114 441 LRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
1-391 |
1.14e-27 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 115.82 E-value: 1.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 1 VEFATAFHGILGAGATVVPLNPLLTEEETRRAVQRTGARLRI----DAPTArALHAGASRPLSPSPATE----------- 65
Cdd:PRK12316 572 IEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLsqshLGRKL-PLAAGVQVLDLDRPAAWlegyseenpgt 650
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 66 --DPEATAVLALSSGTTAEPKPVMLSHRALSANIRQTVSALrgnGLDPGWSVLAPLPLShiYGLNV-LLHSSLANGNHVV 142
Cdd:PRK12316 651 elNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAY---GLGVGDTVLQKTPFS--FDVSVwEFFWPLMSGARLV 725
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 143 LMP---RFTPRAFARLHAEHRIGWSYVAPPIVAALDSEDYSADYSAEdfrhTRVMLSGAAdLSPDLARRVGERLGV-EII 218
Cdd:PRK12316 726 VAApgdHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVASCTSL----RRIVCSGEA-LPADAQEQVFAKLPQaGLY 800
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 219 QGYGMTEAS-PVTHMMRR---GDPLGIGRPVDGTETRI-----------VGGELWVRGPQLCSGYLGAPGPLVEGWLP-- 281
Cdd:PRK12316 801 NLYGPTEAAiDVTHWTCVeegGDSVPIGRPIANLACYIldanlepvpvgVLGELYLAGRGLARGYHGRPGLTAERFVPsp 880
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 282 ---------TGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAV-ARGTLQ--GEEVPHAfvVGT 349
Cdd:PRK12316 881 fvagermyrTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVlAVDGKQlvGYVVLES--EGG 958
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2713532039 350 AAPAEVHEWVARRVAPYKKVRRVTVVESIPRAATGKILRRRL 391
Cdd:PRK12316 959 DWREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKAL 1000
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
1-394 |
3.52e-27 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 112.69 E-value: 3.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 1 VEFATAFHGILGAGATVVPLNPLLTEEETRRAVQRTGARLRID----APTARALHAGASRP------------------- 57
Cdd:PRK08276 47 PEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVLIVsaalADTAAELAAELPAGvplllvvagpvpgfrsyee 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 58 -LSPSPAT--EDPEATAVLALSSGTTAEPKPVM--LSHRALSANIRQ-TVSALRGNGLDPGWSVLAPLPLSH----IYGL 127
Cdd:PRK08276 127 aLAAQPDTpiADETAGADMLYSSGTTGRPKGIKrpLPGLDPDEAPGMmLALLGFGMYGGPDSVYLSPAPLYHtaplRFGM 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 128 NVLLHsslanGNHVVLMPRFTPRAFARLHAEHRIGWSYVAPPI-VAALD-SEDYSADYsaeDFRHTRVMLSGAADLSPDL 205
Cdd:PRK08276 207 SALAL-----GGTVVVMEKFDAEEALALIERYRVTHSQLVPTMfVRMLKlPEEVRARY---DVSSLRVAIHAAAPCPVEV 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 206 ARRVGERLGVEIIQGY------GMTEASPVTHMMRRGDplgIGRPVDGtETRIVG-----------GELWVRGPQLCSGY 268
Cdd:PRK08276 279 KRAMIDWWGPIIHEYYasseggGVTVITSEDWLAHPGS---VGKAVLG-EVRILDedgnelppgeiGTVYFEMDGYPFEY 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 269 LGAPGPLVE-----GWLPTGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAV--ARGTLQGEEV 341
Cdd:PRK08276 355 HNDPEKTAAarnphGWVTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVfgVPDEEMGERV 434
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2713532039 342 -----PHAFVVGTAAPA-EVHEWVARRVAPYKKVRRVTVVESIPRAATGKILRRRLRER 394
Cdd:PRK08276 435 kavvqPADGADAGDALAaELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLRDR 493
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
5-391 |
5.46e-27 |
|
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: 111.72 E-value: 5.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 5 TAFHGILGAGATVVPLNPLLTEEETRRAVQRTGARLRIdaptaralhagasrplspspatEDPEATAVLALSSGTTAEPK 84
Cdd:cd17648 53 IAILAVWKAGAAYVPIDPSYPDERIQFILEDTGARVVI----------------------TNSTDLAYAIYTSGTTGKPK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 85 PVMLSHRALsANIRQTVSALRGnGLDPGWSVLAPLPlSHIYGLNV-LLHSSLANGNHVVLMP---RFTPRAFARLHAEHR 160
Cdd:cd17648 111 GVLVEHGSV-VNLRTSLSERYF-GRDNGDEAVLFFS-NYVFDFFVeQMTLALLNGQKLVVPPdemRFDPDRFYAYINREK 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 161 IGWSYVAPPIVAALDsedysadYSAEDfrHTRVMLSGAADLSPDLARRVGERLGVEIIQGYGMTEASpVTHMMRRGDP-- 238
Cdd:cd17648 188 VTYLSGTPSVLQQYD-------LARLP--HLKRVDAAGEEFTAPVFEKLRSRFAGLIINAYGPTETT-VTNHKRFFPGdq 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 239 ---LGIGRPVDGTETRIVG-----------GELWVRGPQLCSGYLGAPGPLVEGWLP-------------------TGDL 285
Cdd:cd17648 258 rfdKSLGRPVRNTKCYVLNdamkrvpvgavGELYLGGDGVARGYLNRPELTAERFLPnpfqteqerargrnarlykTGDL 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 286 VAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAV-AR-GTLQGEEVPHAFVVG--TAAPAEVHE---- 357
Cdd:cd17648 338 VRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVvAKeDASQAQSRIQKYLVGyyLPEPGHVPEsdll 417
|
410 420 430
....*....|....*....|....*....|....*
gi 2713532039 358 -WVARRVAPYKKVRRVTVVESIPRAATGKILRRRL 391
Cdd:cd17648 418 sFLRAKLPRYMVPARLVRLEGIPVTINGKLDVRAL 452
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
13-393 |
7.41e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 111.90 E-value: 7.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 13 AGATVVPLNPLLTEEETRRAVQRTGARL-----RIDAPTARAL-------HAGASRPLSPSPATEDPEATAV-------L 73
Cdd:PRK06145 75 LGAVFLPINYRLAADEVAYILGDAGAKLllvdeEFDAIVALETpkividaAAQADSRRLAQGGLEIPPQAAVaptdlvrL 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 74 ALSSGTTAEPKPVMLSHRALSANIRQTVSALrgnGLDPGWSVLAPLPLSHIYGLNVLLHSSLANGNHVVLMPRFTPRAFA 153
Cdd:PRK06145 155 MYTSGTTDRPKGVMHSYGNLHWKSIDHVIAL---GLTASERLLVVGPLYHVGAFDLPGIAVLWVGGTLRIHREFDPEAVL 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 154 RLHAEHRIGWSYVAPPIVAALDSEDYSADYSAEDFRhtrvMLSGAADLSPDLARRVGERL--GVEIIQGYGMTEASPVTH 231
Cdd:PRK06145 232 AAIERHRLTCAWMAPVMLSRVLTVPDRDRFDLDSLA----WCIGGGEKTPESRIRDFTRVftRARYIDAYGLTETCSGDT 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 232 MMRRG---DPLG-IGRPVDGTETRI-----------VGGELWVRGPQLCSGYLGAP----GPLVEGWLPTGDLVAPTPDG 292
Cdd:PRK06145 308 LMEAGreiEKIGsTGRALAHVEIRIadgagrwlppnMKGEICMRGPKVTKGYWKDPektaEAFYGDWFRSGDVGYLDEEG 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 293 GLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAV--ARGTLQGEEVPHAFVVGTAAP---AEVHEWVARRVAPYK 367
Cdd:PRK06145 388 FLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVigVHDDRWGERITAVVVLNPGATltlEALDRHCRQRLASFK 467
|
410 420
....*....|....*....|....*.
gi 2713532039 368 KVRRVTVVESIPRAATGKILRRRLRE 393
Cdd:PRK06145 468 VPRQLKVRDELPRNPSGKVLKRVLRD 493
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
9-391 |
2.08e-26 |
|
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: 110.10 E-value: 2.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 9 GILGAGATVVPLNPLLTEEetrravqrtgaRLRIDAPTARALHAgasrplspspaTEDPEATAVLALSSGTTAEPKPVML 88
Cdd:cd12115 68 AVLKAGAAYVPLDPAYPPE-----------RLRFILEDAQARLV-----------LTDPDDLAYVIYTSGSTGRPKGVAI 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 89 SHRALSANIRQTVSALRGNGLDpgwSVLAPLPLShiYGLNVL-LHSSLANGNHVVLMPRftprAFARLHAEHRIGWSY-- 165
Cdd:cd12115 126 EHRNAAAFLQWAAAAFSAEELA---GVLASTSIC--FDLSVFeLFGPLATGGKVVLADN----VLALPDLPAAAEVTLin 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 166 -VAPPIVAALDSEDYSADYSAedfrhtrVMLSGAAdLSPDLARRVGERLGVE-IIQGYGMTEASPVT--HMMRRGD--PL 239
Cdd:cd12115 197 tVPSAAAELLRHDALPASVRV-------VNLAGEP-LPRDLVQRLYARLQVErVVNLYGPSEDTTYStvAPVPPGAsgEV 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 240 GIGRPVDGTETRIVG-----------GELWVRGPQLCSGYLGAPGPLVEGWLP-----------TGDLVAPTPDGGLRVT 297
Cdd:cd12115 269 SIGRPLANTQAYVLDralqpvplgvpGELYIGGAGVARGYLGRPGLTAERFLPdpfgpgarlyrTGDLVRWRPDGLLEFL 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 298 GRTKEIIKYRGYQVSPAELEEVIAACPGVRD-VAVARGTLQGEEVPHAFVVGTAA----PAEVHEWVARRVAPYKKVRRV 372
Cdd:cd12115 349 GRADNQVKVRGFRIELGEIEAALRSIPGVREaVVVAIGDAAGERRLVAYIVAEPGaaglVEDLRRHLGTRLPAYMVPSRF 428
|
410
....*....|....*....
gi 2713532039 373 TVVESIPRAATGKILRRRL 391
Cdd:cd12115 429 VRLDALPLTPNGKIDRSAL 447
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
2-393 |
2.97e-26 |
|
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: 110.11 E-value: 2.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 2 EFATAFHGILGAGATVVPLNP------------------LLTEEETRRAVQRTGARLRIDAPTARALHAGASRPLSpspa 63
Cdd:cd17655 59 EMIVGILGILKAGGAYLPIDPdypeeriqyiledsgadiLLTQSHLQPPIAFIGLIDLLDEDTIYHEESENLEPVS---- 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 64 teDPEATAVLALSSGTTAEPKPVMLSHRALSANIrqtvsalrgngldpgWSVLAPLPLSHiyGLNVLLHSS--------- 134
Cdd:cd17655 135 --KSDDLAYVIYTSGSTGKPKGVMIEHRGVVNLV---------------EWANKVIYQGE--HLRVALFASisfdasvte 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 135 ----LANGNHVVLMPRFTPRAFARLHA---EHRIGWSYVAPpivAALDSEDYSADYSAEDFRHtrvMLSGAADLSPDLAR 207
Cdd:cd17655 196 ifasLLSGNTLYIVRKETVLDGQALTQyirQNRITIIDLTP---AHLKLLDAADDSEGLSLKH---LIVGGEALSTELAK 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 208 RVGERLG--VEIIQGYGMTEAS------PVTHMMRRGDPLGIGRPVDGTETRI-----------VGGELWVRGPQLCSGY 268
Cdd:cd17655 270 KIIELFGtnPTITNAYGPTETTvdasiyQYEPETDQQVSVPIGKPLGNTRIYIldqygrpqpvgVAGELYIGGEGVARGY 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 269 LGAP---------GPLVEG--WLPTGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAV-ARGTL 336
Cdd:cd17655 350 LNRPeltaekfvdDPFVPGerMYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVViARKDE 429
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2713532039 337 QGEEVPHAFVVG--TAAPAEVHEWVARRVAPYKKVRRVTVVESIPRAATGKILRRRLRE 393
Cdd:cd17655 430 QGQNYLCAYIVSekELPVAQLREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKALPE 488
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
10-347 |
3.08e-26 |
|
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: 110.25 E-value: 3.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 10 ILGAGATVVPLNPLLTEEETRRAVQRTGARL----RIDAPTARALHAG---ASRPLSPSPA------------------- 63
Cdd:cd05932 51 IWMAGHISVPLYPTLNPDTIRYVLEHSESKAlfvgKLDDWKAMAPGVPeglISISLPPPSAancqyqwddliaqhpplee 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 64 --TEDPEATAVLALSSGTTAEPKPVMLSHRALSANIRQTVSALRGNGLDpgwSVLAPLPLSHIYGLNVLLHSSLANGNHV 141
Cdd:cd05932 131 rpTRFPEQLATLIYTSGTTGQPKGVMLTFGSFAWAAQAGIEHIGTEEND---RMLSYLPLAHVTERVFVEGGSLYGGVLV 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 142 VL----------MPRFTPRAF---ARLHAEHRIGWSYVAP----------PIVAALDSEDYSAdysAEDFRHTRVMLSGA 198
Cdd:cd05932 208 AFaesldtfvedVQRARPTLFfsvPRLWTKFQQGVQDKIPqqklnlllkiPVVNSLVKRKVLK---GLGLDQCRLAGCGS 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 199 ADLSPDLARRVgERLGVEIIQGYGMTEASPVTHMMRRG-DPLG-IGRPVDGTETRIV-GGELWVRGPQLCSGYLGAPGPL 275
Cdd:cd05932 285 APVPPALLEWY-RSLGLNILEAYGMTENFAYSHLNYPGrDKIGtVGNAGPGVEVRISeDGEILVRSPALMMGYYKDPEAT 363
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2713532039 276 VE-----GWLPTGDLVAPTPDGGLRVTGRTKEIIKY-RGYQVSPAELEEVIAACPGVRDVAVargTLQGEEVPHAFVV 347
Cdd:cd05932 364 AEaftadGFLRTGDKGELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKLAEHDRVEMVCV---IGSGLPAPLALVV 438
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
38-393 |
2.58e-25 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 107.48 E-value: 2.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 38 ARLRIDaPTARALHAGA---SRPLSPSPATEDP--EATAVLALSSGTTAEPKPVmlshRALSANIRQTVSAL----RGNG 108
Cdd:PRK12406 118 AAYRIS-PALLTPPAGAidwEGWLAQQEPYDGPpvPQPQSMIYTSGTTGHPKGV----RRAAPTPEQAAAAEqmraLIYG 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 109 LDPGWSVLAPLPLSH----IYGLNvllhsSLANGNHVVLMPRFTPRAFARLHAEHRIGWSYVAPPIVAALDS--EDYSAD 182
Cdd:PRK12406 193 LKPGIRALLTGPLYHsapnAYGLR-----AGRLGGVLVLQPRFDPEELLQLIERHRITHMHMVPTMFIRLLKlpEEVRAK 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 183 YSAEDFRHtrvMLSGAADLSPDLARRVGERLGVEIIQGYGMTEASPVT-----HMMRRgdPLGIGRPVDGTETRIVG--- 254
Cdd:PRK12406 268 YDVSSLRH---VIHAAAPCPADVKRAMIEWWGPVIYEYYGSTESGAVTfatseDALSH--PGTVGKAAPGAELRFVDedg 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 255 --------GELWVRGPQLCS-GYLGAPGPLVE----GWLPTGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIA 321
Cdd:PRK12406 343 rplpqgeiGEIYSRIAGNPDfTYHNKPEKRAEidrgGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLH 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 322 ACPGVRDVAVArGTLQ---GEEV-----PHAFVvgTAAPAEVHEWVARRVAPYKKVRRVTVVESIPRAATGKILRRRLRE 393
Cdd:PRK12406 423 AVPGVHDCAVF-GIPDaefGEALmavvePQPGA--TLDEADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLRD 499
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
47-389 |
6.84e-25 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 106.39 E-value: 6.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 47 ARALHAGASRPLSPSPatedPEATAVLALSSGTTAEPKPVMLSHRALSANIRQTVSALrgnGLDPGWSV-LAPLPLSHIY 125
Cdd:PRK05851 135 ATAAHTNRSASLTPPD----SGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARV---GLDAATDVgCSWLPLYHDM 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 126 GLNVLLHSSLAnGNHVVLMPR--FTPRAFARLHAEHRIGWSYVAPPIVAALDSEDYSADYSAEDFRHTRVMLSGAADLSP 203
Cdd:PRK05851 208 GLAFLLTAALA-GAPLWLAPTtaFSASPFRWLSWLSDSRATLTAAPNFAYNLIGKYARRVSDVDLGALRVALNGGEPVDC 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 204 DLARRVGE---RLGVE---IIQGYGMTEASPVTHMMRRGDPLGI-----------------GRPVDGTETRIVG------ 254
Cdd:PRK05851 287 DGFERFATamaPFGFDagaAAPSYGLAESTCAVTVPVPGIGLRVdevttddgsgarrhavlGNPIPGMEVRISPgdgaag 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 255 ------GELWVRGPQLCSGYLGAPGPLVEGWLPTGDLVAPTpDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRD 328
Cdd:PRK05851 367 vagreiGEIEIRGASMMSGYLGQAPIDPDDWFPTGDLGYLV-DGGLVVCGRAKELITVAGRNIFPTEIERVAAQVRGVRE 445
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 329 VAV-ARGTLQGEEVPHAFV----VGTAAPAEVHEwVARRVAPYKKVRRVTVV----ESIPRAATGKiLRR 389
Cdd:PRK05851 446 GAVvAVGTGEGSARPGLVIaaefRGPDEAGARSE-VVQRVASECGVVPSDVVfvapGSLPRTSSGK-LRR 513
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
48-371 |
8.73e-25 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 106.34 E-value: 8.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 48 RALHAGASRPLSPSPATedPEATAVLALSSGTTAEPKPVMLSHRALSANIRQTVSALRgngLDPGWSVLAPLPLSHIY-- 125
Cdd:PLN02736 203 KLLAQGRSSPQPFRPPK--PEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTK---FYPSDVHISYLPLAHIYer 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 126 -GLNVLLHSSLA----NGNHVVLM--------------PRFTPRAFARLHAEHRIGwsyvappivAALDSEDYSADYSAE 186
Cdd:PLN02736 278 vNQIVMLHYGVAvgfyQGDNLKLMddlaalrptifcsvPRLYNRIYDGITNAVKES---------GGLKERLFNAAYNAK 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 187 dfRHT---------------------------RVMLSGAADLSPDLARRVGERLGVEIIQGYGMTEASPVTHMMRRGDPL 239
Cdd:PLN02736 349 --KQAlengknpspmwdrlvfnkikaklggrvRFMSSGASPLSPDVMEFLRICFGGRVLEGYGMTETSCVISGMDEGDNL 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 240 G--IGRPVDGTETRIVG---------------GELWVRGPQLCSGYLGAPGPLVE-----GWLPTGDLVAPTPDGGLRVT 297
Cdd:PLN02736 427 SghVGSPNPACEVKLVDvpemnytsedqpyprGEICVRGPIIFKGYYKDEVQTREvidedGWLHTGDIGLWLPGGRLKII 506
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2713532039 298 GRTKEIIKY-RGYQVSPAELEEVIAACPGVRDVAVARGTLQgeevphAFVVGTAAPAE--VHEWVARRVAPYKKVRR 371
Cdd:PLN02736 507 DRKKNIFKLaQGEYIAPEKIENVYAKCKFVAQCFVYGDSLN------SSLVAVVVVDPevLKAWAASEGIKYEDLKQ 577
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
54-394 |
1.31e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 105.46 E-value: 1.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 54 ASRPLSPSPATEDpeATAVLALSSGTTAEPKPVMLSHRALSANIRQTVSALRgngLDPGWSVLAP-LPLSHIYGLNVLLH 132
Cdd:PRK07768 140 AADPIDPVETGED--DLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAE---FDVETDVMVSwLPLFHDMGMVGFLT 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 133 SSLANGNHVVLMprfTPRAF-------ARLHAEHRiGWSYVAPPIVAALDSE--DYSADYSAEDFRHTRVMLSGAADLSP 203
Cdd:PRK07768 215 VPMYFGAELVKV---TPMDFlrdpllwAELISKYR-GTMTAAPNFAYALLARrlRRQAKPGAFDLSSLRFALNGAEPIDP 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 204 DLARR---VGERLGVE---IIQGYGMTEASPVTHMMRRGDPL----------------------------GIGRPVDGTE 249
Cdd:PRK07768 291 ADVEDlldAGARFGLRpeaILPAYGMAEATLAVSFSPCGAGLvvdevdadllaalrravpatkgntrrlaTLGPPLPGLE 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 250 TRIVG-----------GELWVRGPQLCSGYL--GAPGPLVE--GWLPTGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPA 314
Cdd:PRK07768 371 VRVVDedgqvlpprgvGVIELRGESVTPGYLtmDGFIPAQDadGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPT 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 315 ELEEVIAACPGVRD---VAVARGTLQGEEvPHAFVVGTAA---PAEVHEW---VARRVAPYKKVRRVTVV----ESIPRA 381
Cdd:PRK07768 451 DIERAAARVEGVRPgnaVAVRLDAGHSRE-GFAVAVESNAfedPAEVRRIrhqVAHEVVAEVGVRPRNVVvlgpGSIPKT 529
|
410
....*....|...
gi 2713532039 382 ATGKILRRRLRER 394
Cdd:PRK07768 530 PSGKLRRANAAEL 542
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
2-391 |
2.37e-24 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 105.81 E-value: 2.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 2 EFATAFHGILGAGATVVPLNPLLTEEETRRAVQRTGARL---------RIDAPTARA---LHAGASRPLSPSPATE---D 66
Cdd:PRK12316 2065 ELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALlltqrhlleRLPLPAGVArlpLDRDAEWADYPDTAPAvqlA 2144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 67 PEATAVLALSSGTTAEPKPVMLSHRALSANIRQTVSALRgngLDPGWSVLAPLPLSHIYGLNVLLHSsLANGNHVVLMP- 145
Cdd:PRK12316 2145 GENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYE---LSPADCELQFMSFSFDGAHEQWFHP-LLNGARVLIRDd 2220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 146 -RFTPRAFARLHAEHRIGWSYVAPPIVAALDSEdysadysAEDFRHT---RVMLSGAADLSPDLARRVGERL-GVEIIQG 220
Cdd:PRK12316 2221 eLWDPEQLYDEMERHGVTILDFPPVYLQQLAEH-------AERDGRPpavRVYCFGGEAVPAASLRLAWEALrPVYLFNG 2293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 221 YGMTEA--SPVTHMMRRGDPLG-----IGRPVDGTETRIVG-----------GELWVRGPQLCSGYLGAPGPLVEGWLP- 281
Cdd:PRK12316 2294 YGPTEAvvTPLLWKCRPQDPCGaayvpIGRALGNRRAYILDadlnllapgmaGELYLGGEGLARGYLNRPGLTAERFVPd 2373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 282 -----------TGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRD-VAVARGTLQGEEVPhAFVVG- 348
Cdd:PRK12316 2374 pfsasgerlyrTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREaVVVAQDGASGKQLV-AYVVPd 2452
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2713532039 349 ---TAAPAEVHEWVARRVAPYKKVRRVTVVESIPRAATGKILRRRL 391
Cdd:PRK12316 2453 daaEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKAL 2498
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
14-394 |
2.90e-24 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 104.46 E-value: 2.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 14 GATVVPLNPLLTEEETRRAVQRTGARLRI--------------DAPTARALHAGASRP-------LSPSPATEDPEATA- 71
Cdd:PRK13382 117 GADILLLNTSFAGPALAEVVTREGVDTVIydeefsatvdralaDCPQATRIVAWTDEDhdltvevLIAAHAGQRPEPTGr 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 72 ---VLALSSGTTAEPKPVMLSHRALSANIRQTVSALRGNGLDPgwSVLAPlPLSHIYGL-NVLLHSSLANGnhVVLMPRF 147
Cdd:PRK13382 197 kgrVILLTSGTTGTPKGARRSGPGGIGTLKAILDRTPWRAEEP--TVIVA-PMFHAWGFsQLVLAASLACT--IVTRRRF 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 148 TPRAFARLHAEHRIGWSYVAPPIVaaldseDYSADYSAEDF-----RHTRVMLSGAADLSPDLARRVGERLGVEIIQGYG 222
Cdd:PRK13382 272 DPEATLDLIDRHRATGLAVVPVMF------DRIMDLPAEVRnrysgRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYN 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 223 MTEASPV---THMMRRGDPLGIGRPVDGTETRIVG-----------GELWVRGPQLCSGYL-GAPGPLVEGWLPTGDLVA 287
Cdd:PRK13382 346 ATEAGMIataTPADLRAAPDTAGRPAEGTEIRILDqdfrevptgevGTIFVRNDTQFDGYTsGSTKDFHDGFMASGDVGY 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 288 PTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAVargtlQGEEVPH------AFVV----GTAAPAEVHE 357
Cdd:PRK13382 426 LDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAV-----IGVDDEQygqrlaAFVVlkpgASATPETLKQ 500
|
410 420 430
....*....|....*....|....*....|....*..
gi 2713532039 358 WVARRVAPYKKVRRVTVVESIPRAATGKILRRRLRER 394
Cdd:PRK13382 501 HVRDNLANYKVPRDIVVLDELPRGATGKILRRELQAR 537
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
13-393 |
3.32e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 104.35 E-value: 3.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 13 AGATVVPLNPLLTEEETRRAVQRTGARLRIdAPTARALHAGASRPLSP----------SPATEDPEATAVLAL------- 75
Cdd:PRK07470 80 LGAVWVPTNFRQTPDEVAYLAEASGARAMI-CHADFPEHAAAVRAASPdlthvvaiggARAGLDYEALVARHLgarvana 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 76 ------------SSGTTAEPKPVMLSHRALSANIRQTVSALRgngldPGWS----VLAPLPLSHIYGLNVLLHssLANGN 139
Cdd:PRK07470 159 avdhddpcwfffTSGTTGRPKAAVLTHGQMAFVITNHLADLM-----PGTTeqdaSLVVAPLSHGAGIHQLCQ--VARGA 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 140 HVVLMP--RFTPRAFARLHAEHRIGWSYVAPPIVAALdSEDYSAD-YSAEDFRHtrVMLSGAADLSPDlARRVGERLGVE 216
Cdd:PRK07470 232 ATVLLPseRFDPAEVWALVERHRVTNLFTVPTILKML-VEHPAVDrYDHSSLRY--VIYAGAPMYRAD-QKRALAKLGKV 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 217 IIQGYGMTEAS-------PVTHMMRRGDPLGIG---RPVDGTETRIVG-----------GELWVRGPQLCSGYLGAP--- 272
Cdd:PRK07470 308 LVQYFGLGEVTgnitvlpPALHDAEDGPDARIGtcgFERTGMEVQIQDdegrelppgetGEICVIGPAVFAGYYNNPean 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 273 -GPLVEGWLPTGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAVArGTLQGE--EVPHAFVV-- 347
Cdd:PRK07470 388 aKAFRDGWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVL-GVPDPVwgEVGVAVCVar 466
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 2713532039 348 --GTAAPAEVHEWVARRVAPYKKVRRVTVVESIPRAATGKILRRRLRE 393
Cdd:PRK07470 467 dgAPVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVRE 514
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
62-392 |
4.66e-24 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 104.34 E-value: 4.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 62 PATEDP---EATAVLALSSGTTAEPKPVMLSHRALSANIRQTV-SALRGNGLDPGwsvLAPLPLSHIYGLNVLLHSSLAN 137
Cdd:PRK06060 136 PGGYEPmggDALAYATYTSGTTGPPKAAIHRHADPLTFVDAMCrKALRLTPEDTG---LCSARMYFAYGLGNSVWFPLAT 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 138 GNHVVLMP-RFTPRAFARLHAEHRIGWSYVAPPIVAALdsedySADYSAEDFRHTRVMLSGAADLSPDLARRVGERLG-V 215
Cdd:PRK06060 213 GGSAVINSaPVTPEAAAILSARFGPSVLYGVPNFFARV-----IDSCSPDSFRSLRCVVSAGEALELGLAERLMEFFGgI 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 216 EIIQGYGMTEASP--VTHMMRRGDPLGIGRPVDGTETRIVG-----------GELWVRGPQLCSGYLGAPGPLVE--GWL 280
Cdd:PRK06060 288 PILDGIGSTEVGQtfVSNRVDEWRLGTLGRVLPPYEIRVVApdgttagpgveGDLWVRGPAIAKGYWNRPDSPVAneGWL 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 281 PTGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAV-------ARGTLQGEEVPH--AFVVGTAA 351
Cdd:PRK06060 368 DTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVvavrestGASTLQAFLVATsgATIDGSVM 447
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2713532039 352 pAEVHEWVARRVAPYKKVRRVTVVESIPRAATGKILRRRLR 392
Cdd:PRK06060 448 -RDLHRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALR 487
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
2-392 |
5.19e-24 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 103.61 E-value: 5.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 2 EFATAFHGILGAGATVVPLNPLLTEEETRRAVQRTGARLRID----APTARALHAGASRPL-------SPSPATED---- 66
Cdd:PRK08008 74 EFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLVTsaqfYPMYRQIQQEDATPLrhicltrVALPADDGvssf 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 67 ------------------PEATAVLALSSGTTAEPKPVMLSHralsANIR--------QTvsALRGNGLdpgwsVLAPLP 120
Cdd:PRK08008 154 tqlkaqqpatlcyapplsTDDTAEILFTSGTTSRPKGVVITH----YNLRfagyysawQC--ALRDDDV-----YLTVMP 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 121 LSHI-YGLNVLLhSSLANGNHVVLMPRFTPRAFARLHAEHRIGWSYVAPPIVAALDSEDYSADysaEDFRHTRVMLSgAA 199
Cdd:PRK08008 223 AFHIdCQCTAAM-AAFSAGATFVLLEKYSARAFWGQVCKYRATITECIPMMIRTLMVQPPSAN---DRQHCLREVMF-YL 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 200 DLSPDLARRVGERLGVEIIQGYGMTEaspvTHMMRRGDPLG-------IGRPVDGTETRIVG-----------GELWVRG 261
Cdd:PRK08008 298 NLSDQEKDAFEERFGVRLLTSYGMTE----TIVGIIGDRPGdkrrwpsIGRPGFCYEAEIRDdhnrplpageiGEICIKG 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 262 ---PQLCSGYLGAPGPLVE-----GWLPTGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAV-- 331
Cdd:PRK08008 374 vpgKTIFKEYYLDPKATAKvleadGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVvg 453
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2713532039 332 ARGTLQGEEVpHAFVV----GTAAPAEVHEWVARRVAPYKKVRRVTVVESIPRAATGKILRRRLR 392
Cdd:PRK08008 454 IKDSIRDEAI-KAFVVlnegETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
56-394 |
6.01e-24 |
|
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: 103.73 E-value: 6.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 56 RPLSPS-PATEDPeatAVLALSSGTTAEPKpvMLSH-------RALSANIRQTVsalRGNGL-----DPGW--SVLAPLP 120
Cdd:cd05970 175 RPTANSyPCGEDI---LLVYFSSGTTGMPK--MVEHdftyplgHIVTAKYWQNV---REGGLhltvaDTGWgkAVWGKIY 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 121 LSHIYGLNVLLHSslangnhvvlMPRFTPRAFARLHAEHRIGwSYVAPP-IVAALDSEDYSaDYSAEDFRHTRVmlSGAA 199
Cdd:cd05970 247 GQWIAGAAVFVYD----------YDKFDPKALLEKLSKYGVT-TFCAPPtIYRFLIREDLS-RYDLSSLRYCTT--AGEA 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 200 dLSPDLARRVGERLGVEIIQGYGMTEASPVTHMM--RRGDPLGIGRPVDGTETRIVG-----------GELWVRGPQ--- 263
Cdd:cd05970 313 -LNPEVFNTFKEKTGIKLMEGFGQTETTLTIATFpwMEPKPGSMGKPAPGYEIDLIDregrsceageeGEIVIRTSKgkp 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 264 --LCSGYLGAPGPLVEGWLP----TGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAVA----- 332
Cdd:cd05970 392 vgLFGGYYKDAEKTAEVWHDgyyhTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTgvpdp 471
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 333 -RGtlqgeEVPHAFVV-------GTAAPAEVHEWVARRVAPYKKVRRVTVVESIPRAATGKILRRRLRER 394
Cdd:cd05970 472 iRG-----QVVKATIVlakgyepSEELKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEIRER 536
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
1-391 |
8.78e-24 |
|
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: 102.55 E-value: 8.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 1 VEFATAFHGILGAGATVVPLNPLLTEEETRRAVQRTGARLridaptaralhagasrplspspATEDPEATAVLALSSGTT 80
Cdd:cd17650 48 LDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLEDSGAKL----------------------LLTQPEDLAYVIYTSGTT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 81 AEPKPVMLSHRalsaNIRQTVSALRGNgldpgwSVLAPLPLSHI----YGLNVL---LHSSLANGNHVVLMP---RFTPR 150
Cdd:cd17650 106 GKPKGVMVEHR----NVAHAAHAWRRE------YELDSFPVRLLqmasFSFDVFagdFARSLLNGGTLVICPdevKLDPA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 151 AFARLHAEHRIGWSYVAPPIVAALDSEDYsadYSAEDFRHTRVMLSGA----ADLSPDLARRVGERLgvEIIQGYGMTEA 226
Cdd:cd17650 176 ALYDLILKSRITLMESTPALIRPVMAYVY---RNGLDLSAMRLLIVGSdgckAQDFKTLAARFGQGM--RIINSYGVTEA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 227 SPVTHMMRRG-DPLG------IGRPVDGTETRI-----------VGGELWVRGPQLCSGYLGAPGPLVEGWLP------- 281
Cdd:cd17650 251 TIDSTYYEEGrDPLGdsanvpIGRPLPNTAMYVlderlqpqpvgVAGELYIGGAGVARGYLNRPELTAERFVEnpfapge 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 282 ----TGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAVA-RGTLQGEEVPHAFVVGTAAP--AE 354
Cdd:cd17650 331 rmyrTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAvREDKGGEARLCAYVVAAATLntAE 410
|
410 420 430
....*....|....*....|....*....|....*..
gi 2713532039 355 VHEWVARRVAPYKKVRRVTVVESIPRAATGKILRRRL 391
Cdd:cd17650 411 LRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
77-400 |
3.32e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 101.56 E-value: 3.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 77 SGTTAEPKPVMLSHR--ALSAnirqtVSALRGNGLDPGWSVLAPLPLSHIYGLNVLLHSSLANGNHVVLMpRFTPRAFAR 154
Cdd:PRK08162 191 SGTTGNPKGVVYHHRgaYLNA-----LSNILAWGMPKHPVYLWTLPMFHCNGWCFPWTVAARAGTNVCLR-KVDPKLIFD 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 155 LHAEHRIGwSYVAPPIVaaldsedYSA-----DYSAEDFRHT-RVMLSGAADLSPDLARrvGERLGVEIIQGYGMTEA-S 227
Cdd:PRK08162 265 LIREHGVT-HYCGAPIV-------LSAlinapAEWRAGIDHPvHAMVAGAAPPAAVIAK--MEEIGFDLTHVYGLTETyG 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 228 PVT------------------HMMRRG------------DPlGIGRPV--DGtETRivgGELWVRGPQLCSGYLGAPGPL 275
Cdd:PRK08162 335 PATvcawqpewdalplderaqLKARQGvryplqegvtvlDP-DTMQPVpaDG-ETI---GEIMFRGNIVMKGYLKNPKAT 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 276 VE----GWLPTGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVA-VARGTLQGEEVPHAFVV--- 347
Cdd:PRK08162 410 EEafagGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAvVAKPDPKWGEVPCAFVElkd 489
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 2713532039 348 -GTAAPAEVHEWVARRVAPYKKVRRVTVVEsIPRAATGKILRRRLRERAGDADE 400
Cdd:PRK08162 490 gASATEEEIIAHCREHLAGFKVPKAVVFGE-LPKTSTGKIQKFVLREQAKSLKA 542
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
2-394 |
4.61e-23 |
|
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: 100.82 E-value: 4.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 2 EFATAFHGILGAGATVVPLNPLLTEEETRRAVQR--------------TGARL--RIDAPTARALHAG--------ASRP 57
Cdd:cd05906 76 DFIPAFWACVLAGFVPAPLTVPPTYDEPNARLRKlrhiwqllgspvvlTDAELvaEFAGLETLSGLPGirvlsieeLLDT 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 58 LSPSPA-TEDPEATAVLALSSGTTAEPKPVMLSHRALSANIRQTVSALRGNGLDPG--WsvlapLPLSHIYGLNVL-LHS 133
Cdd:cd05906 156 AADHDLpQSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFlnW-----VPLDHVGGLVELhLRA 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 134 SLANGNHV------VLMprfTPRAFARLHAEHRIGWSYvAPPIVAAL--DSEDYSADYSAeDFRHTRVMLSGAADLSPDL 205
Cdd:cd05906 231 VYLGCQQVhvpteeILA---DPLRWLDLIDRYRVTITW-APNFAFALlnDLLEEIEDGTW-DLSSLRYLVNAGEAVVAKT 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 206 ARRVGERL---GVE---IIQGYGMTE--------ASPVTHMMRRGDPL-GIGRPVDGTETRIVG-----------GELWV 259
Cdd:cd05906 306 IRRLLRLLepyGLPpdaIRPAFGMTEtcsgviysRSFPTYDHSQALEFvSLGRPIPGVSMRIVDdegqllpegevGRLQV 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 260 RGPQLCSGYLGAPGPLVE-----GWLPTGDLvAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRD--VAVA 332
Cdd:cd05906 386 RGPVVTKGYYNNPEANAEaftedGWFRTGDL-GFLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPsfTAAF 464
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2713532039 333 RGTLQGEEVPHAFVV------GTAAPAEVHEWVARRVAPYKKVRRVTVV----ESIPRAATGKILRRRLRER 394
Cdd:cd05906 465 AVRDPGAETEELAIFfvpeydLQDALSETLRAIRSVVSREVGVSPAYLIplpkEEIPKTSLGKIQRSKLKAA 536
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
64-394 |
5.62e-23 |
|
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: 100.62 E-value: 5.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 64 TEDPEAtavLALSSGTTAEPKpvMLSHRALSANIRQTVSALRGNGL----------DPGW------SVLAPLPLshiyGL 127
Cdd:cd05928 173 SQEPMA---IYFTSGTTGSPK--MAEHSHSSLGLGLKVNGRYWLDLtasdimwntsDTGWiksawsSLFEPWIQ----GA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 128 NVLLHSslangnhvvlMPRFTPRAFARLHAEHRIGwSYVAPPIVAALDSEDysaDYSAEDFRHTRVMLSGAADLSPDLAR 207
Cdd:cd05928 244 CVFVHH----------LPRFDPLVILKTLSSYPIT-TFCGAPTVYRMLVQQ---DLSSYKFPSLQHCVTGGEPLNPEVLE 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 208 RVGERLGVEIIQGYGMTEASpVTHMMRRG---DPLGIGRPVDGTETRIVG-----------GELWVR-GPQ----LCSGY 268
Cdd:cd05928 310 KWKAQTGLDIYEGYGQTETG-LICANFKGmkiKPGSMGKASPPYDVQIIDdngnvlppgteGDIGIRvKPIrpfgLFSGY 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 269 LGAPGPLVEG-----WLpTGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAVA------RGtlq 337
Cdd:cd05928 389 VDNPEKTAATirgdfYL-TGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVsspdpiRG--- 464
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2713532039 338 geEVPHAFVVGTAA---------PAEVHEWVARRVAPYKKVRRVTVVESIPRAATGKILRRRLRER 394
Cdd:cd05928 465 --EVVKAFVVLAPQflshdpeqlTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRDK 528
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
51-331 |
6.00e-23 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 100.64 E-value: 6.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 51 HAGASRPLSPSPAtedPEATAVLALSSGTTAEPKPVMLSHRALsanIRQTVSALRGNGLDPGWSVLAPLPLSHIYGLNVL 130
Cdd:PLN02860 158 RALGTTELDYAWA---PDDAVLICFTSGTTGRPKGVTISHSAL---IVQSLAKIAIVGYGEDDVYLHTAPLCHIGGLSSA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 131 LHSSLANGNHvVLMPRFTPRAFARLHAEHRIGWSYVAPPIVAALDSEDYSADYSAEdFRHTRVMLSGAADLSPDLARRVG 210
Cdd:PLN02860 232 LAMLMVGACH-VLLPKFDAKAALQAIKQHNVTSMITVPAMMADLISLTRKSMTWKV-FPSVRKILNGGGSLSSRLLPDAK 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 211 ERL-GVEIIQGYGMTEASPVTHMMRRGDPLG-------------------------IGRPVDGTETRIVG------GELW 258
Cdd:PLN02860 310 KLFpNAKLFSAYGMTEACSSLTFMTLHDPTLespkqtlqtvnqtksssvhqpqgvcVGKPAPHVELKIGLdessrvGRIL 389
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2713532039 259 VRGPQLCSGYLG----APGPLV-EGWLPTGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAV 331
Cdd:PLN02860 390 TRGPHVMLGYWGqnseTASVLSnDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVV 467
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
60-391 |
6.43e-23 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 100.47 E-value: 6.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 60 PSPATEDPEAtavLALSSGTTAEPKPVMLSHRALSAnirqTVSALRGNGLD-----PGWSVLAPLPLSHIYGL----NVL 130
Cdd:PRK05857 164 ADQGSEDPLA---MIFTSGTTGEPKAVLLANRTFFA----VPDILQKEGLNwvtwvVGETTYSPLPATHIGGLwwilTCL 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 131 LHSSL--ANGNHVVlmprftprAFARLHAEHRIGWSYVAPPIVAALDSEDYSADYSAEDFRHtrVMLSGAADLSPDLarR 208
Cdd:PRK05857 237 MHGGLcvTGGENTT--------SLLEILTTNAVATTCLVPTLLSKLVSELKSANATVPSLRL--VGYGGSRAIAADV--R 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 209 VGERLGVEIIQGYGMTEAS------PV-THMMRRGDPLGIGRPVDGTETRIVG-----------------GELWVRGPQL 264
Cdd:PRK05857 305 FIEATGVRTAQVYGLSETGctalclPTdDGSIVKIEAGAVGRPYPGVDVYLAAtdgigptapgagpsasfGTLWIKSPAN 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 265 CSGYLGAPGP----LVEGWLPTGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAVAR------G 334
Cdd:PRK05857 385 MLGYWNNPERtaevLIDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEipdeefG 464
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2713532039 335 TLQGEEVPHAFVVGTAAPAEVHEWVA----RRVAPYKKVRRVTVVESIPRAATGKILRRRL 391
Cdd:PRK05857 465 ALVGLAVVASAELDESAARALKHTIAarfrRESEPMARPSTIVIVTDIPRTQSGKVMRASL 525
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
3-391 |
1.07e-22 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 99.69 E-value: 1.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 3 FATAFHGILGAGATVVPLNP------------------LLTEEETRRAVQRTG-ARLRIDAPTARALHAGASRPLSPSpa 63
Cdd:PRK13383 98 FVTAVFAVGLLGADVVPISTefrsdalaaalrahhistVVADNEFAERIAGADdAVAVIDPATAGAEESGGRPAVAAP-- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 64 tedpeaTAVLALSSGTTAEPKPVMLSHRaLSANIRQTVSALRGNGLDPGWSVLAPLPLSHIYGLNVLLhSSLANGNHVVL 143
Cdd:PRK13383 176 ------GRIVLLTSGTTGKPKGVPRAPQ-LRSAVGVWVTILDRTRLRTGSRISVAMPMFHGLGLGMLM-LTIALGGTVLT 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 144 MPRFTPRAFARLHAEHRIGwSYVAPPIVAALDSEDYSADYSAEDFRHTRVMLSGAADLSPDLARRVGERLGVEIIQGYGM 223
Cdd:PRK13383 248 HRHFDAEAALAQASLHRAD-AFTAVPVVLARILELPPRVRARNPLPQLRVVMSSGDRLDPTLGQRFMDTYGDILYNGYGS 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 224 TE---ASPVTHMMRRGDPLGIGRPVDGTETRI-----------VGGELWVRGPQLCSGYLGAPG-PLVEGWLPTGDLVAP 288
Cdd:PRK13383 327 TEvgiGALATPADLRDAPETVGKPVAGCPVRIldrnnrpvgprVTGRIFVGGELAGTRYTDGGGkAVVDGMTSTGDMGYL 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 289 TPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAVArgTLQGEEVPH---AFVVGTAA----PAEVHEWVAR 361
Cdd:PRK13383 407 DNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVI--GVPDERFGHrlaAFVVLHPGsgvdAAQLRDYLKD 484
|
410 420 430
....*....|....*....|....*....|
gi 2713532039 362 RVAPYKKVRRVTVVESIPRAATGKILRRRL 391
Cdd:PRK13383 485 RVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
1-395 |
2.12e-22 |
|
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: 98.41 E-value: 2.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 1 VEFATAFHGILGAGATVVPLNPLLTEEETRRAVQRTGA-RLRIDAPTAralhagASRPLspspatedpeataVLALSSGT 79
Cdd:cd05974 36 VELWEAMLAAMKLGAVVIPATTLLTPDDLRDRVDRGGAvYAAVDENTH------ADDPM-------------LLYFTSGT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 80 TAEPKPVMLSHRALSANirqTVSALRGNGLDPG---WSVLAPLPLSHIYGLnvlLHSSLANGNHVVLM--PRFTPRAFAR 154
Cdd:cd05974 97 TSKPKLVEHTHRSYPVG---HLSTMYWIGLKPGdvhWNISSPGWAKHAWSC---FFAPWNAGATVFLFnyARFDAKRVLA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 155 LHAEHRIGwSYVAPPIVAALDSEDYSADYSAEdfrhTRVMLSGAADLSPDLARRVGERLGVEIIQGYGMTEA------SP 228
Cdd:cd05974 171 ALVRYGVT-TLCAPPTVWRMLIQQDLASFDVK----LREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETtalvgnSP 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 229 ----VTHMMRRGDP-------LGIGRPVDGTETRIVGGElwVRGPQLCSGYLGAPGPLVE----GWLPTGDLVAPTPDGG 293
Cdd:cd05974 246 gqpvKAGSMGRPLPgyrvallDPDGAPATEGEVALDLGD--TRPVGLMKGYAGDPDKTAHamrgGYYRTGDIAMRDEDGY 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 294 LRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAVARGTLQGE-EVPHAFVVGTA----APA---EVHEWVARRVAP 365
Cdd:cd05974 324 LTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRlSVPKAFIVLRAgyepSPEtalEIFRFSRERLAP 403
|
410 420 430
....*....|....*....|....*....|
gi 2713532039 366 YKKVRRVTVVEsIPRAATGKILRRRLRERA 395
Cdd:cd05974 404 YKRIRRLEFAE-LPKTISGKIRRVELRRRE 432
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
66-331 |
2.20e-22 |
|
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: 98.83 E-value: 2.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 66 DPEATAVLALSSGTTAEPKPVMLSHRALSANIrQTVSALRGNGLDPGWSVLAPLPLSHIYGLNV---------------- 129
Cdd:cd17639 86 KPDDLACIMYTSGSTGNPKGVMLTHGNLVAGI-AGLGDRVPELLGPDDRYLAYLPLAHIFELAAenvclyrggtigygsp 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 130 --LLHSSLAN--GNHVVLMPRF---TPRAFARL--------------------HA----EHRIGWSYVAP--------PI 170
Cdd:cd17639 165 rtLTDKSKRGckGDLTEFKPTLmvgVPAIWDTIrkgvlaklnpmgglkrtlfwTAyqskLKALKEGPGTPlldelvfkKV 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 171 VAALDSedysadysaedfrHTRVMLSGAADLSPDlARRVGERLGVEIIQGYGMTEASPVTHMMRRGDPL--GIGRPVDGT 248
Cdd:cd17639 245 RAALGG-------------RLRYMLSGGAPLSAD-TQEFLNIVLCPVIQGYGLTETCAGGTVQDPGDLEtgRVGPPLPCC 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 249 ETRIVG--------------GELWVRGPQLCSGYLGAPGPLVE-----GWLPTGDLVAPTPDGGLRVTGRTKEIIKYR-G 308
Cdd:cd17639 311 EIKLVDweeggystdkppprGEILIRGPNVFKGYYKNPEKTKEafdgdGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQnG 390
|
330 340
....*....|....*....|...
gi 2713532039 309 YQVSPAELEEVIAACPGVRDVAV 331
Cdd:cd17639 391 EYIALEKLESIYRSNPLVNNICV 413
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
66-366 |
5.74e-22 |
|
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: 97.88 E-value: 5.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 66 DPEATAVLALSSGTTAEPKPVMLSHRALsanIRQTVSALRGNGLDPGWSVLAPLPLSHIYGLNVLLHSSLANGN------ 139
Cdd:cd17641 156 KGEDVAVLCTTSGTTGKPKLAMLSHGNF---LGHCAAYLAADPLGPGDEYVSVLPLPWIGEQMYSVGQALVCGFivnfpe 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 140 --------------HVVLMPrftPRAFARLHAEHRIGWSYvAPPIVAALDSEDYSADYSAED------------------ 187
Cdd:cd17641 233 epetmmedlreigpTFVLLP---PRVWEGIAADVRARMMD-ATPFKRFMFELGMKLGLRALDrgkrgrpvslwlrlaswl 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 188 --------------FRHTRVMLSGAADLSPDLARRVgERLGVEIIQGYGMTEASPVTHMMRRGD--PLGIGRPVDGTETR 251
Cdd:cd17641 309 adallfrplrdrlgFSRLRSAATGGAALGPDTFRFF-HAIGVPLKQLYGQTELAGAYTVHRDGDvdPDTVGVPFPGTEVR 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 252 IVG-GELWVRGPQLCSGYLGAPGPLVE-----GWLPTGDLVAPTPDGGLRVTGRTKEIIK-YRGYQVSPAELEEVIAACP 324
Cdd:cd17641 388 IDEvGEILVRSPGVFVGYYKNPEATAEdfdedGWLHTGDAGYFKENGHLVVIDRAKDVGTtSDGTRFSPQFIENKLKFSP 467
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2713532039 325 GVRDvAVARGtlQGEEVPHAFVvgTAAPAEVHEWVARRVAPY 366
Cdd:cd17641 468 YIAE-AVVLG--AGRPYLTAFI--CIDYAIVGKWAEQRGIAF 504
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
2-394 |
1.51e-21 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 96.61 E-value: 1.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 2 EFATAFHGILGAGATVVPLnPLLTE--------EETRRAVQRTGARLRI----------DAPTA-RALHAGASRPLSPSP 62
Cdd:PRK09192 86 DFVEAFFACQYAGLVPVPL-PLPMGfggresyiAQLRGMLASAQPAAIItpdellpwvnEATHGnPLLHVLSHAWFKALP 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 63 A------TEDPEATAVLALSSGTTAEPKPVMLSHRALSANIRqtvsALRGNGLD--PGWSVLAPLPLSHIYGLNVLLHSS 134
Cdd:PRK09192 165 EadvalpRPTPDDIAYLQYSSGSTRFPRGVIITHRALMANLR----AISHDGLKvrPGDRCVSWLPFYHDMGLVGFLLTP 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 135 LANGNHVVLMPrftPRAFAR-------LHAEHRIGWSYvAPPI---VAALDSEdySADYSAEDFRHTRVMLSGAADLSPD 204
Cdd:PRK09192 241 VATQLSVDYLP---TRDFARrplqwldLISRNRGTISY-SPPFgyeLCARRVN--SKDLAELDLSCWRVAGIGADMIRPD 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 205 LARRVGERLGV------EIIQGYGMTEASPVTHMMrrgdPLG----------------------------------IGRP 244
Cdd:PRK09192 315 VLHQFAEAFAPagfddkAFMPSYGLAEATLAVSFS----PLGsgivveevdrdrleyqgkavapgaetrrvrtfvnCGKA 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 245 VDGTETRIVG-----------GELWVRGPQLCSGYLGAPGP----LVEGWLPTGDLvAPTPDGGLRVTGRTKEIIKYRGY 309
Cdd:PRK09192 391 LPGHEIEIRNeagmplpervvGHICVRGPSLMSGYFRDEESqdvlAADGWLDTGDL-GYLLDGYLYITGRAKDLIIINGR 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 310 QVSPAELEEVIAACPGVR--DVAVARGTLQGEEVPHAFVVGTAAPAEVHEWVARRVApyKKVRRVTVVE---------SI 378
Cdd:PRK09192 470 NIWPQDIEWIAEQEPELRsgDAAAFSIAQENGEKIVLLVQCRISDEERRGQLIHALA--ALVRSEFGVEaavelvpphSL 547
|
490
....*....|....*.
gi 2713532039 379 PRAATGKILRRRLRER 394
Cdd:PRK09192 548 PRTSSGKLSRAKAKKR 563
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
66-397 |
2.10e-21 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 95.97 E-value: 2.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 66 DPEATAVLALSSGTTAEPKPVMLSHRAlsaNIRQTVSALRGN--GLDPGWSVLAPLPLSHI--YGLNVllhSSLANGNHV 141
Cdd:PRK06018 175 DENTAAGMCYTSGTTGDPKGVLYSHRS---NVLHALMANNGDalGTSAADTMLPVVPLFHAnsWGIAF---SAPSMGTKL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 142 VlMP--RFTPRAFARLHAEHRIGWSYVAPPIVAALDSEDYSADYSAEDFRhtRVMLSGAAdlSPDLARRVGERLGVEIIQ 219
Cdd:PRK06018 249 V-MPgaKLDGASVYELLDTEKVTFTAGVPTVWLMLLQYMEKEGLKLPHLK--MVVCGGSA--MPRSMIKAFEDMGVEVRH 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 220 GYGMTEASPVTHMMRRGDPLG-------------IGRPVDGTETRIVG-------------GELWVRGPQLCSGYLGAPG 273
Cdd:PRK06018 324 AWGMTEMSPLGTLAALKPPFSklpgdarldvlqkQGYPPFGVEMKITDdagkelpwdgktfGRLKVRGPAVAAAYYRVDG 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 274 PLV--EGWLPTGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAVArGTL--QGEEVPHAFVVG- 348
Cdd:PRK06018 404 EILddDGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVI-GVYhpKWDERPLLIVQLk 482
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 2713532039 349 ---TAAPAEVHEWVARRVAPYKKVRRVTVVESIPRAATGKILRRRLRERAGD 397
Cdd:PRK06018 483 pgeTATREEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALREQFKD 534
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
14-367 |
2.73e-21 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 95.32 E-value: 2.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 14 GATVVPLNPLLTEEETRRAVQRTGARLRIDAPTARALHAGASRPLSPSPATE----DPEATAVLALSSGTTAEPKPVMLS 89
Cdd:PRK09029 77 GARVLPLNPQLPQPLLEELLPSLTLDFALVLEGENTFSALTSLHLQLVEGAHavawQPQRLATMTLTSGSTGLPKAAVHT 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 90 HRALSANIRQTVSALRgngLDPGWSVLAPLPLSHIYGLNVL-----------------LHSSLANGNHVVLMPrftpraf 152
Cdd:PRK09029 157 AQAHLASAEGVLSLMP---FTAQDSWLLSLPLFHVSGQGIVwrwlyagatlvvrdkqpLEQALAGCTHASLVP------- 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 153 ARLhaehrigWSYVappivaaldsedysaDYSAEDFRHTRVMLSGAAdLSPDLARRVgERLGVEIIQGYGMTE-ASPVTh 231
Cdd:PRK09029 227 TQL-------WRLL---------------DNRSEPLSLKAVLLGGAA-IPVELTEQA-EQQGIRCWCGYGLTEmASTVC- 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 232 mMRRGDPL-GIGRPVDGTETRIVGGELWVRGPQLCSGYL--GAPGPLV--EGWLPTGDLVAPTpDGGLRVTGRTKEIIKY 306
Cdd:PRK09029 282 -AKRADGLaGVGSPLPGREVKLVDGEIWLRGASLALGYWrqGQLVPLVndEGWFATRDRGEWQ-NGELTILGRLDNLFFS 359
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2713532039 307 RGYQVSPAELEEVIAACPGVRDVAV---------ARgtlqgeevPHAFVV--GTAAPAEVHEWVARRVAPYK 367
Cdd:PRK09029 360 GGEGIQPEEIERVINQHPLVQQVFVvpvadaefgQR--------PVAVVEsdSEAAVVNLAEWLQDKLARFQ 423
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
51-395 |
2.88e-21 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 95.44 E-value: 2.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 51 HAGASRPLSPSPATEdpeaTAVLALSSGTTAEPKPVMLSHRALSANIRQTVSALrgnGLDPGWSVLAPLPLSHIYGLnvl 130
Cdd:PRK10946 169 HPAEDFTATPSPADE----VAFFQLSGGSTGTPKLIPRTHNDYYYSVRRSVEIC---GFTPQTRYLCALPAAHNYPM--- 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 131 lhSS-------LANGNhVVLMPRFTPRAFARLHAEHRIGWSYVAPPIVAALDSEDYSADYSAEdFRHTRVMLSGAADLSP 203
Cdd:PRK10946 239 --SSpgalgvfLAGGT-VVLAPDPSATLCFPLIEKHQVNVTALVPPAVSLWLQAIAEGGSRAQ-LASLKLLQVGGARLSE 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 204 DLARRVGERLGVEIIQGYGMTEAspVTHMMRRGDPLGI-----GRPV-DGTETRIVG-----------GELWVRGPQLCS 266
Cdd:PRK10946 315 TLARRIPAELGCQLQQVFGMAEG--LVNYTRLDDSDERifttqGRPMsPDDEVWVADadgnplpqgevGRLMTRGPYTFR 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 267 GYLGAPGPLV-----EGWLPTGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVA-VA-RGTLQGE 339
Cdd:PRK10946 393 GYYKSPQHNAsafdaNGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAAlVSmEDELMGE 472
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2713532039 340 EvPHAFVVGTAA--PAEVHEWV-ARRVAPYKKVRRVTVVESIPRAATGKILRRRLRERA 395
Cdd:PRK10946 473 K-SCAFLVVKEPlkAVQLRRFLrEQGIAEFKLPDRVECVDSLPLTAVGKVDKKQLRQWL 530
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
73-395 |
5.57e-21 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 94.70 E-value: 5.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 73 LALSSGTTAEPKPVMLSHR-----ALSANIrqtvsalrgngldpGWSV------LAPLPLSHIYGLNVLLHSSLANGNHV 141
Cdd:PLN03102 191 LNYTSGTTADPKGVVISHRgaylsTLSAII--------------GWEMgtcpvyLWTLPMFHCNGWTFTWGTAARGGTSV 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 142 VLMPRFTPRAFARLHAEHRIGWSYVapPIVAALDSEDYSADYSAedfRHTRV-MLSGAADLSPDLARRVgERLGVEIIQG 220
Cdd:PLN03102 257 CMRHVTAPEIYKNIEMHNVTHMCCV--PTVFNILLKGNSLDLSP---RSGPVhVLTGGSPPPAALVKKV-QRLGFQVMHA 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 221 YGMTEAS---------------PVTHMM----RRG-DPLGIGR-PVDGTETR-------IVGGELWVRGPQLCSGYLGAP 272
Cdd:PLN03102 331 YGLTEATgpvlfcewqdewnrlPENQQMelkaRQGvSILGLADvDVKNKETQesvprdgKTMGEIVIKGSSIMKGYLKNP 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 273 GPLVE----GWLPTGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAVAR--GTLQGeEVPHAFV 346
Cdd:PLN03102 411 KATSEafkhGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAmpHPTWG-ETPCAFV 489
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2713532039 347 VGTAAPAEVHEWVARRVAPYKKV--------------RRVTVVESIPRAATGKILRRRLRERA 395
Cdd:PLN03102 490 VLEKGETTKEDRVDKLVTRERDLieycrenlphfmcpRKVVFLQELPKNGNGKILKPKLRDIA 552
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
2-391 |
5.97e-21 |
|
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: 94.16 E-value: 5.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 2 EFATAFHGILGAGATVVPLNPLLTEEETRRAVQRTGARLRIdaptaralhagasrplspspatEDPEATAVLALSSGTTA 81
Cdd:cd17645 60 DMIAAILGVLKAGGAYVPIDPDYPGERIAYMLADSSAKILL----------------------TNPDDLAYVIYTSGSTG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 82 EPKPVMLSHRALsANIRQTVSALRGNGLDPGWSVLAPLPLSHiYGLNVLLHSSLANGNHVVLMP-RFTPRAFARLHAEHR 160
Cdd:cd17645 118 LPKGVMIEHHNL-VNLCEWHRPYFGVTPADKSLVYASFSFDA-SAWEIFPHLTAGAALHVVPSErRLDLDALNDYFNQEG 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 161 IGWSYVAPPIvaaldsedySADYSAEDFRHTRVMLSGAADLspdlarRVGERLGVEIIQGYGMTEASPVTHMMRRGDP-- 238
Cdd:cd17645 196 ITISFLPTGA---------AEQFMQLDNQSLRVLLTGGDKL------KKIERKGYKLVNNYGPTENTVVATSFEIDKPya 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 239 -LGIGRPVDGTETRIVG-----------GELWVRGPQLCSGYLGAP---------GPLVEG--WLPTGDLVAPTPDGGLR 295
Cdd:cd17645 261 nIPIGKPIDNTRVYILDealqlqpigvaGELCIAGEGLARGYLNRPeltaekfivHPFVPGerMYRTGDLAKFLPDGNIE 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 296 VTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAV-ARGTLQGEEVPHAFVVG--TAAPAEVHEWVARRVAPYKKVRRV 372
Cdd:cd17645 341 FLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVlAKEDADGRKYLVAYVTApeEIPHEELREWLKNDLPDYMIPTYF 420
|
410
....*....|....*....
gi 2713532039 373 TVVESIPRAATGKILRRRL 391
Cdd:cd17645 421 VHLKALPLTANGKVDRKAL 439
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
65-394 |
1.33e-20 |
|
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: 93.32 E-value: 1.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 65 EDPEATAVLALSSGTTAEPKPVMLSHRALSANIRQTVSALRGNGLDpgwSVLAPLPLSHIYGLNVL-LHSSLANGNHvVL 143
Cdd:cd05908 103 ELADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKD---RILSWMPLTHDMGLIAFhLAPLIAGMNQ-YL 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 144 MPrftprafARLHAEHRIGWSY-VAPPIVAALDSEDYSADY---------SAE-DFRHTRVMLSGAADLSPDLARRVGER 212
Cdd:cd05908 179 MP-------TRLFIRRPILWLKkASEHKATIVSSPNFGYKYflktlkpekANDwDLSSIRMILNGAEPIDYELCHEFLDH 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 213 LGV------EIIQGYGMTEAS-------------PVTH------------MMRRGDP-----LGIGRPVDGTETRIVG-- 254
Cdd:cd05908 252 MSKyglkrnAILPVYGLAEASvgaslpkaqspfkTITLgrrhvthgepepEVDKKDSecltfVEVGKPIDETDIRICDed 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 255 ---------GELWVRGPQLCSGYLGAPGPLV-----EGWLPTGDLvAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVI 320
Cdd:cd05908 332 nkilpdgyiGHIQIRGKNVTPGYYNNPEATAkvftdDGWLKTGDL-GFIRNGRLVITGREKDIIFVNGQNVYPHDIERIA 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 321 AACPGVRDVAVARGTLQGEEVPHAFVVGTAapaeVHEWVARRVAPYKK-------------VRRVTVVESIPRAATGKIL 387
Cdd:cd05908 411 EELEGVELGRVVACGVNNSNTRNEEIFCFI----EHRKSEDDFYPLGKkikkhlnkrggwqINEVLPIRRIPKTTSGKVK 486
|
....*..
gi 2713532039 388 RRRLRER 394
Cdd:cd05908 487 RYELAQR 493
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
1-391 |
2.20e-20 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 93.69 E-value: 2.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 1 VEFATAFHGILGAGATVVPLNPLLTEEETRRAVQRTGARLRIdapTARALHA-------------------GASRPLSPS 61
Cdd:PRK12467 1635 LEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLL---TQSHLQArlplpdglrslvldqeddwLEGYSDSNP 1711
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 62 PATEDPEATAVLALSSGTTAEPKPVMLSHRALSANIRQTVSALrgnGLDPGWSVLAPLPLSHIYGLNVLLHSsLANGNHV 141
Cdd:PRK12467 1712 AVNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAY---QLSAADVVLQFTSFAFDVSVWELFWP-LINGARL 1787
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 142 VLMPRFT---PRAFARLHAEHRIGWSYVAPPIVAALDSEDysaDYSAEDFRHTRVMLSGAAdLSPDLARRVGERLG-VEI 217
Cdd:PRK12467 1788 VIAPPGAhrdPEQLIQLIERQQVTTLHFVPSMLQQLLQMD---EQVEHPLSLRRVVCGGEA-LEVEALRPWLERLPdTGL 1863
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 218 IQGYGMTEAS-PVTH-MMRRGDPLG-----IGRPVDGTETRI-----------VGGELWVRGPQLCSGYLGAPGPLVEGW 279
Cdd:PRK12467 1864 FNLYGPTETAvDVTHwTCRRKDLEGrdsvpIGQPIANLSTYIldaslnpvpigVAGELYLGGVGLARGYLNRPALTAERF 1943
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 280 LP------------TGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAV-----ARGTL------ 336
Cdd:PRK12467 1944 VAdpfgtvgsrlyrTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVViaqdgANGKQlvayvv 2023
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2713532039 337 -QGEEVPHAFVVGTAAPAEVHEWVARRVAPYKKVRRVTVVESIPRAATGKILRRRL 391
Cdd:PRK12467 2024 pTDPGLVDDDEAQVALRAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKAL 2079
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
1-391 |
3.28e-20 |
|
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: 92.15 E-value: 3.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 1 VEFATAFHGILGAGATVVPLNPLLTEEETRRAVQRTGARL---RIDAPTARALHAGASRPLSPSPATEDPEAT------- 70
Cdd:cd17656 49 AEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRVvltQRHLKSKLSFNKSTILLEDPSISQEDTSNIdyinnsd 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 71 --AVLALSSGTTAEPKPVMLSHRALsANI----RQTVSALRGNGldpgwsVLAPLPLShiygLNVLLH---SSLANGNHV 141
Cdd:cd17656 129 dlLYIIYTSGTTGKPKGVQLEHKNM-VNLlhfeREKTNINFSDK------VLQFATCS----FDVCYQeifSTLLSGGTL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 142 VLMPRFTPRAFARLH---AEHRIGWSYVAPPIVAALDSEDYSADYSAEDFRHtrVMLSGAADLSPDLARRVGERLGVEII 218
Cdd:cd17656 198 YIIREETKRDVEQLFdlvKRHNIEVVFLPVAFLKFIFSEREFINRFPTCVKH--IITAGEQLVITNEFKEMLHEHNVHLH 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 219 QGYGMTEASPVT-HMMRRGDPLG----IGRPVDGTETRI-----------VGGELWVRGPQLCSGYLGAPGPLVEGWLP- 281
Cdd:cd17656 276 NHYGPSETHVVTtYTINPEAEIPelppIGKPISNTWIYIldqeqqlqpqgIVGELYISGASVARGYLNRQELTAEKFFPd 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 282 ----------TGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAV-ARGTLQGEEVPHAFVVG-- 348
Cdd:cd17656 356 pfdpnermyrTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVlDKADDKGEKYLCAYFVMeq 435
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 2713532039 349 TAAPAEVHEWVARRVAPYKKVRRVTVVESIPRAATGKILRRRL 391
Cdd:cd17656 436 ELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
2-392 |
9.52e-20 |
|
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: 90.66 E-value: 9.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 2 EFATAFHGILGAGATVVPLNPLLTEEETRRAVQRTGARLRIdaPTARALHAGASRPLspspatedpeataVLALSSGTTA 81
Cdd:cd05973 37 ELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVV--TDAANRHKLDSDPF-------------VMMFTSGTTG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 82 EPKPVMLSHRALS---ANIRQTVSALRG----NGLDPGWSvlaplplshiYGLNVLLHSSLANGNHVVLMPR-FTPRAFA 153
Cdd:cd05973 102 LPKGVPVPLRALAafgAYLRDAVDLRPEdsfwNAADPGWA----------YGLYYAITGPLALGHPTILLEGgFSVESTW 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 154 RLHAEHRIGwSYVAPPIVAALDSEDYSADYSAEDFRhTRVMLSGAADLSPDLARRVGERLGVEIIQGYGMTE-ASPVTHM 232
Cdd:cd05973 172 RVIERLGVT-NLAGSPTAYRLLMAAGAEVPARPKGR-LRRVSSAGEPLTPEVIRWFDAALGVPIHDHYGQTElGMVLANH 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 233 MRRGDPL---GIGRPVDGTETRI--------VGGELWV------RGPQLC-SGYLGAPGPLVEG-WLPTGDLVAPTPDGG 293
Cdd:cd05973 250 HALEHPVhagSAGRAMPGWRVAVldddgdelGPGEPGRlaidiaNSPLMWfRGYQLPDTPAIDGgYYLTGDTVEFDPDGS 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 294 LRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAV-ARGTLQGEEVPHAFVV-------GTAAPAEVHEWVARRVAP 365
Cdd:cd05973 330 FSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAViGVPDPERTEVVKAFVVlrgghegTPALADELQLHVKKRLSA 409
|
410 420
....*....|....*....|....*..
gi 2713532039 366 YKKVRRVTVVESIPRAATGKILRRRLR 392
Cdd:cd05973 410 HAYPRTIHFVDELPKTPSGKIQRFLLR 436
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
1-391 |
1.10e-19 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 91.64 E-value: 1.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 1 VEFATAFHGILGAGATVVPLNPLLTEEETRRAVQRTGARLRIDAPTARALHAGASRPLSPSPATED------------PE 68
Cdd:PRK10252 519 VFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTADQLPRFADVPDLTSLCYNAPLapqgaaplqlsqPH 598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 69 ATAVLALSSGTTAEPKPVMLSHRALsanirqtVSAL----RGNGLDPGWSVLAPLPLSHIYGLNVLLHSSLANGNHVVLM 144
Cdd:PRK10252 599 HTAYIIFTSGSTGRPKGVMVGQTAI-------VNRLlwmqNHYPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAE 671
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 145 PRF--TPRAFARLHAEHRIGWSYVAPPI----VAALDSEdySADYSAEDFRhtRVMLSGAAdLSPDLARRVGERLGVEII 218
Cdd:PRK10252 672 PEAhrDPLAMQQFFAEYGVTTTHFVPSMlaafVASLTPE--GARQSCASLR--QVFCSGEA-LPADLCREWQQLTGAPLH 746
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 219 QGYGMTEA---------SPVTHMMRRGDPLGIGRPVDGTETRI-----------VGGELWVRGPQLCSGYLGAPGPLVEG 278
Cdd:PRK10252 747 NLYGPTEAavdvswypaFGEELAAVRGSSVPIGYPVWNTGLRIldarmrpvppgVAGDLYLTGIQLAQGYLGRPDLTASR 826
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 279 WLP-----------TGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGV-RDVAVARGTLQGEEVPH--- 343
Cdd:PRK10252 827 FIAdpfapgermyrTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVeQAVTHACVINQAAATGGdar 906
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2713532039 344 ---AFVV-GTAAPAEV---HEWVARRVAPYKKVRRVTVVESIPRAATGKILRRRL 391
Cdd:PRK10252 907 qlvGYLVsQSGLPLDTsalQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKAL 961
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
9-393 |
2.83e-19 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 90.61 E-value: 2.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 9 GILGAGATVVPLNPLLTEEETRRAVQRTGARLRIdapTARALHAGASRPLSPSPATED-------PEATAVLAL------ 75
Cdd:PRK05691 1200 AILKAGGAYVPLDPDYPAERLAYMLADSGVELLL---TQSHLLERLPQAEGVSAIALDslhldswPSQAPGLHLhgdnla 1276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 76 ----SSGTTAEPKPVMLSHRALSANIR--QTVSALRGN---------GLDPG-WSVLAPLplshIYGLNVLLhssLANGN 139
Cdd:PRK05691 1277 yviyTSGSTGQPKGVGNTHAALAERLQwmQATYALDDSdvlmqkapiSFDVSvWECFWPL----ITGCRLVL---AGPGE 1349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 140 HVvlmprfTPRAFARLHAEHRIGWSYVAPPIVAALDSEDYSADYSAedfrhTRVMLSGAADLSPDLARRVGERL-GVEII 218
Cdd:PRK05691 1350 HR------DPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLAAACTS-----LRRLFSGGEALPAELRNRVLQRLpQVQLH 1418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 219 QGYGMTE-ASPVTHMMRR---GDPLGIGRPVDGTETRI-----------VGGELWVRGPQLCSGYLGAPGPLVEGWLP-- 281
Cdd:PRK05691 1419 NRYGPTEtAINVTHWQCQaedGERSPIGRPLGNVLCRVldaelnllppgVAGELCIGGAGLARGYLGRPALTAERFVPdp 1498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 282 ----------TGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAV-ARGTLQGEEVPhAFVVGTA 350
Cdd:PRK05691 1499 lgedgarlyrTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVlVREGAAGAQLV-GYYTGEA 1577
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2713532039 351 APAEVHEWV----ARRVAPYKKVRRVTVVESIPRAATGKILRRRLRE 393
Cdd:PRK05691 1578 GQEAEAERLkaalAAELPEYMVPAQLIRLDQMPLGPSGKLDRRALPE 1624
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
67-333 |
9.25e-19 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 88.23 E-value: 9.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 67 PEATAVLALSSGTTAEPKPVMLSHRALSANIRQ--TVSalrgnGLDPGWSVLAPLPLSHIYGLNVLLHSSLANGNHVVLM 144
Cdd:PRK08043 364 PEDAALILFTSGSEGHPKGVVHSHKSLLANVEQikTIA-----DFTPNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLY 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 145 PrfTPrafarLHaeHRIgwsyvAPPIV------AALDSEDYSADYS----AEDFRHTRVMLSGAADLSPDLARRVGERLG 214
Cdd:PRK08043 439 P--SP-----LH--YRI-----VPELVydrnctVLFGTSTFLGNYArfanPYDFARLRYVVAGAEKLQESTKQLWQDKFG 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 215 VEIIQGYGMTEASPVTH----MMRRgdPLGIGRPVDGTETRIV-------GGELWVRGPQLCSGYL--GAPGPLVE---- 277
Cdd:PRK08043 505 LRILEGYGVTECAPVVSinvpMAAK--PGTVGRILPGMDARLLsvpgieqGGRLQLKGPNIMNGYLrvEKPGVLEVptae 582
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2713532039 278 --------GWLPTGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEV-IAACPGVRDVAVAR 333
Cdd:PRK08043 583 nargemerGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLaLGVSPDKQHATAIK 647
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
1-391 |
3.76e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 87.14 E-value: 3.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 1 VEFATAFHGILGAGATVVPLNPLLTEEETRRAVQRTGARLRIDA-------PTARALHA-----GASRPLSPS-PATE-D 66
Cdd:PRK12467 3156 VEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQahlleqlPAPAGDTAltldrLDLNGYSENnPSTRvM 3235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 67 PEATAVLALSSGTTAEPKPVMLSHRALSANIRQTVSALrgnGLDPGWSVLAPLPLShIYGLNVLLHSSLANGNHVVLMP- 145
Cdd:PRK12467 3236 GENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAY---ELDANDRVLLFMSFS-FDGAQERFLWTLICGGCLVVRDn 3311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 146 -RFTPRAFARLHAEHRIGWSYVAPPIVAALDSEDYSADYSAEDfrhtRVMLSGAAdLSPDLARRVGERLG-VEIIQGYGM 223
Cdd:PRK12467 3312 dLWDPEELWQAIHAHRISIACFPPAYLQQFAEDAGGADCASLD----IYVFGGEA-VPPAAFEQVKRKLKpRGLTNGYGP 3386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 224 TEAS-PVTHMMRRGD------PLGIGRPVDGTETRI-----------VGGELWVRGPQLCSGYLGAPGPLVEGWLP---- 281
Cdd:PRK12467 3387 TEAVvTVTLWKCGGDavceapYAPIGRPVAGRSIYVldgqlnpvpvgVAGELYIGGVGLARGYHQRPSLTAERFVAdpfs 3466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 282 --------TGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAV-ARGTLQGEEVPhAFVVGTAAP 352
Cdd:PRK12467 3467 gsggrlyrTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVlARDGAGGKQLV-AYVVPADPQ 3545
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 2713532039 353 AEVHEWVARRVAP----YKKVRRVTVVESIPRAATGKILRRRL 391
Cdd:PRK12467 3546 GDWRETLRDHLAAslpdYMVPAQLLVLAAMPLGPNGKVDRKAL 3588
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
1-391 |
5.76e-18 |
|
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: 85.18 E-value: 5.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 1 VEFATAFHGILGAGATVVPLNPLLTEEETRRAVQRTGARLRIdaptaralhagasrplspspatEDPEATAVLALSSGTT 80
Cdd:cd17644 61 LEMIIGLLAILKAGGAYVPLDPNYPQERLTYILEDAQISVLL----------------------TQPENLAYVIYTSGST 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 81 AEPKPVMLSHRALsanirqtvsalrgngldpgwsVLAPLPLSHIYGL----NVLLHSSLA-------------NGNHVVL 143
Cdd:cd17644 119 GKPKGVMIEHQSL---------------------VNLSHGLIKEYGItssdRVLQFASIAfdvaaeeiyvtllSGATLVL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 144 MP---RFTPRAFARLHAEHRIG-WSYvaPPIVAALDSEDYSADYSAEDfRHTRVMLSGAADLSPDLARRVGERLG--VEI 217
Cdd:cd17644 178 RPeemRSSLEDFVQYIQQWQLTvLSL--PPAYWHLLVLELLLSTIDLP-SSLRLVIVGGEAVQPELVRQWQKNVGnfIQL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 218 IQGYGMTEASPVTHMMRRGDPLG-------IGRPVDGTETRI-----------VGGELWVRGPQLCSGYLGAPGPLVEGW 279
Cdd:cd17644 255 INVYGPTEATIAATVCRLTQLTErnitsvpIGRPIANTQVYIldenlqpvpvgVPGELHIGGVGLARGYLNRPELTAEKF 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 280 LP-------------TGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAV-ARGTLQGEEVPHAF 345
Cdd:cd17644 335 IShpfnsseserlykTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVViVREDQPGNKRLVAY 414
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 2713532039 346 VVG----TAAPAEVHEWVARRVAPYKKVRRVTVVESIPRAATGKILRRRL 391
Cdd:cd17644 415 IVPhyeeSPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
1-391 |
6.70e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 86.16 E-value: 6.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 1 VEFATAFHGILGAGATVVPLNPLLTEEETRRAVQRTGARLRIDAPTARALHAGASRPLSPSPATED-----------PEA 69
Cdd:PRK12316 3118 LEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQSHLRLPLAQGVQVLDLDRGDENyaeanpairtmPEN 3197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 70 TAVLALSSGTTAEPKPVMLSHRALSANIRQTVSALrgnGLDPGWSVLAPLPLShIYGLNVLLHSSLANGNHVVLMPRFTP 149
Cdd:PRK12316 3198 LAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAY---GLGVGDRVLQFTTFS-FDVFVEELFWPLMSGARVVLAGPEDW 3273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 150 RAFARLHAEHRIGWSYVAPPIVAALdsEDYSADYSAEDFRHTRVMLSGAADLSPDLARRVgeRLGVEIIQGYGMTEASPV 229
Cdd:PRK12316 3274 RDPALLVELINSEGVDVLHAYPSML--QAFLEEEDAHRCTSLKRIVCGGEALPADLQQQV--FAGLPLYNLYGPTEATIT 3349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 230 THMMRRGDP----LGIGRPVDGTETRI-----------VGGELWVRGPQLCSGYLGAPGPLVEGWLP-----------TG 283
Cdd:PRK12316 3350 VTHWQCVEEgkdaVPIGRPIANRACYIldgslepvpvgALGELYLGGEGLARGYHNRPGLTAERFVPdpfvpgerlyrTG 3429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 284 DLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRD---VAVARGTLQGEEVPHAfvVGTAAPAEVHEWVA 360
Cdd:PRK12316 3430 DLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREavvLAVDGRQLVAYVVPED--EAGDLREALKAHLK 3507
|
410 420 430
....*....|....*....|....*....|.
gi 2713532039 361 RRVAPYKKVRRVTVVESIPRAATGKILRRRL 391
Cdd:PRK12316 3508 ASLPEYMVPAHLLFLERMPLTPNGKLDRKAL 3538
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
76-392 |
1.09e-17 |
|
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: 85.06 E-value: 1.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 76 SSGTTAEPKPVmlshralsanirqtvsaLRGNGldpGWSVLAPLPLSHIYGLN-------------VLLHS-----SLAN 137
Cdd:cd05967 238 TSGTTGKPKGV-----------------VRDNG---GHAVALNWSMRNIYGIKpgdvwwaasdvgwVVGHSyivygPLLH 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 138 GNHVVL---MPRFTPR--AFARLHAEHRIGWSYVAPPIVAALDSEDYSADY-SAEDFRHTRVMLSGAADLSPDLARRVGE 211
Cdd:cd05967 298 GATTVLyegKPVGTPDpgAFWRVIEKYQVNALFTAPTAIRAIRKEDPDGKYiKKYDLSSLRTLFLAGERLDPPTLEWAEN 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 212 RLGVEIIQGYGMTEA-SPVTHMMRRGDPLGI-----GRPVDGTETRIVGGELWVRGPQlCSGYLGAPGPLVEGWLP---- 281
Cdd:cd05967 378 TLGVPVIDHWWQTETgWPITANPVGLEPLPIkagspGKPVPGYQVQVLDEDGEPVGPN-ELGNIVIKLPLPPGCLLtlwk 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 282 ------------------TGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAV--ARGTLQGeEV 341
Cdd:cd05967 457 nderfkklylskfpgyydTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVvgVRDELKG-QV 535
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2713532039 342 PHAFVV----GTAAPAEVHE----WVARRVAPYKKVRRVTVVESIPRAATGKILRRRLR 392
Cdd:cd05967 536 PLGLVVlkegVKITAEELEKelvaLVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLR 594
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
47-305 |
1.90e-17 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 84.26 E-value: 1.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 47 ARALHAGASRPLSPSpatEDPEATAVLALSSGTTAEPKPVMLSHRALSANI---RQTVSALRGnGLDPGWSVLAPLPLSH 123
Cdd:PTZ00216 246 AKGHSAGSHHPLNIP---ENNDDLALIMYTSGTTGDPKGVMHTHGSLTAGIlalEDRLNDLIG-PPEEDETYCSYLPLAH 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 124 IYGL---NVLLhsslANGNHVVL-MPRFTPRAFARLH---AEHR----IGWSYV-----------APPI----------- 170
Cdd:PTZ00216 322 IMEFgvtNIFL----ARGALIGFgSPRTLTDTFARPHgdlTEFRpvflIGVPRIfdtikkaveakLPPVgslkrrvfdha 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 171 ----VAALDSEDYSADYSAEDF--------RHTRVMLSGAADLSPDLARRVGERLGVeIIQGYGMTEASPVTHMMRRGD- 237
Cdd:PTZ00216 398 yqsrLRALKEGKDTPYWNEKVFsapravlgGRVRAMLSGGGPLSAATQEFVNVVFGM-VIQGWGLTETVCCGGIQRTGDl 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 238 -PLGIGRPVDGTETRIVG-------------GELWVRGPQLCSGYLGAPGPLVE-----GWLPTGDLVAPTPDGGLRVTG 298
Cdd:PTZ00216 477 ePNAVGQLLKGVEMKLLDteeykhtdtpeprGEILLRGPFLFKGYYKQEELTREvldedGWFHTGDVGSIAANGTLRIIG 556
|
....*..
gi 2713532039 299 RTKEIIK 305
Cdd:PTZ00216 557 RVKALAK 563
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
20-387 |
4.07e-17 |
|
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: 83.01 E-value: 4.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 20 LNPLLTEEETRRAVQRTGARLRIDAPTA---RALHAGASRPLSPSPAteDPEATAVLALSSGTTAEPKPVMLSHRALSAN 96
Cdd:cd17634 183 LNPNVTSVEHVIVLKRTGSDIDWQEGRDlwwRDLIAKASPEHQPEAM--NAEDPLFILYTSGTTGKPKGVLHTTGGYLVY 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 97 IRQTVSALRGNGldPGWSVLAPLPLSHIYGLNVLLHSSLANGNHVVL---MPRF-TPRAFARLHAEHRIGWSYVAPPIVA 172
Cdd:cd17634 261 AATTMKYVFDYG--PGDIYWCTADVGWVTGHSYLLYGPLACGATTLLyegVPNWpTPARMWQVVDKHGVNILYTAPTAIR 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 173 ALDSEDYSAdYSAEDFRHTRVMLSGAADLSPDLARRVGERLGVE---IIQGYGMTEASPVTHMMRRG-DPLGIG---RPV 245
Cdd:cd17634 339 ALMAAGDDA-IEGTDRSSLRILGSVGEPINPEAYEWYWKKIGKEkcpVVDTWWQTETGGFMITPLPGaIELKAGsatRPV 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 246 DGTETRIVGGE------------------------LWVRGPQLCSGYLGApgplVEGWLPTGDLVAPTPDGGLRVTGRTK 301
Cdd:cd17634 418 FGVQPAVVDNEghpqpggtegnlvitdpwpgqtrtLFGDHERFEQTYFST----FKGMYFSGDGARRDEDGYYWITGRSD 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 302 EIIKYRGYQVSPAELEEVIAACPGVRDVAVA--RGTLQGEEvPHAFVV-------GTAAPAEVHEWVARRVAPYKKVRRV 372
Cdd:cd17634 494 DVINVAGHRLGTAEIESVLVAHPKVAEAAVVgiPHAIKGQA-PYAYVVlnhgvepSPELYAELRNWVRKEIGPLATPDVV 572
|
410
....*....|....*
gi 2713532039 373 TVVESIPRAATGKIL 387
Cdd:cd17634 573 HWVDSLPKTRSGKIM 587
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
2-332 |
4.31e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 83.07 E-value: 4.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 2 EFATAFHGILGAGATVVPLnpllTEEETRRAVQRTGARLRIDAPTA--------------RALHAGAS------------ 55
Cdd:PRK05850 71 EYIVAFLGALQAGLIAVPL----SVPQGGAHDERVSAVLRDTSPSVvlttsavvddvteyVAPQPGQSappvievdlldl 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 56 -RPLSPSPATEDPEATAVLALSSGTTAEPKPVMLSHRALSANIRQTVSAL---RGNGLDPGWSVLAPLPLSHIYGLNVLL 131
Cdd:PRK05850 147 dSPRGSDARPRDLPSTAYLQYTSGSTRTPAGVMVSHRNVIANFEQLMSDYfgdTGGVPPPDTTVVSWLPFYHDMGLVLGV 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 132 HSSLANGNHVVLMprfTPRAF----AR---LHAEHRIGWSyVAPPI---VAALDSEDysADYSAEDFRHTRVMLSGAADL 201
Cdd:PRK05850 227 CAPILGGCPAVLT---SPVAFlqrpARwmqLLASNPHAFS-AAPNFafeLAVRKTSD--DDMAGLDLGGVLGIISGSERV 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 202 SPDLARRVGER-----LGVEIIQ-GYGMTEA-----------SPVT-----------HMMRRGDPLG------------I 241
Cdd:PRK05850 301 HPATLKRFADRfapfnLRETAIRpSYGLAEAtvyvatrepgqPPESvrfdyeklsagHAKRCETGGGtplvsygsprspT 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 242 GRPVDGtETRI-----VGGELWVRGPQLCSGYLGAP--------GPLV-------EG-WLPTGDLVAPTpDGGLRVTGRT 300
Cdd:PRK05850 381 VRIVDP-DTCIecpagTVGEIWVHGDNVAAGYWQKPeetertfgATLVdpspgtpEGpWLRTGDLGFIS-EGELFIVGRI 458
|
410 420 430
....*....|....*....|....*....|..
gi 2713532039 301 KEIIKYRGYQVSPAELEEVIAACPGVRDVAVA 332
Cdd:PRK05850 459 KDLLIVDGRNHYPDDIEATIQEITGGRVAAIS 490
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
1-331 |
4.41e-17 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 83.85 E-value: 4.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 1 VEFATAFHGILGAGATVVPLNP-------LLTEEETRRAVQRTGARLRIDAPTARALHA------------GASRPLSPS 61
Cdd:PRK12316 4612 AEMMVGLLAVLKAGGAYVPLDPeyprerlAYMMEDSGAALLLTQSHLLQRLPIPDGLASlaldrdedwegfPAHDPAVRL 4691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 62 pateDPEATAVLALSSGTTAEPKPVMLSHRALSANIrqtVSALRGNGLDPGWSVLAPLPLSHIYGLNVLLHSsLANGNHV 141
Cdd:PRK12316 4692 ----HPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHL---HATGERYELTPDDRVLQFMSFSFDGSHEGLYHP-LINGASV 4763
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 142 VLMP--RFTPRAFARLHAEHRIGwSYVAPPIVAALDSEDYSADysAEDFRHTRVMLSGAAdLSPDLARRVGERLG-VEII 218
Cdd:PRK12316 4764 VIRDdsLWDPERLYAEIHEHRVT-VLVFPPVYLQQLAEHAERD--GEPPSLRVYCFGGEA-VAQASYDLAWRALKpVYLF 4839
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 219 QGYGMTEAS--PVTHMMRRGDPLG-----IGRPVDGTETRI-----------VGGELWVRGPQLCSGYLGAPGPLVEGWL 280
Cdd:PRK12316 4840 NGYGPTETTvtVLLWKARDGDACGaaympIGTPLGNRSGYVldgqlnplpvgVAGELYLGGEGVARGYLERPALTAERFV 4919
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2713532039 281 P------------TGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAV 331
Cdd:PRK12316 4920 PdpfgapggrlyrTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVV 4982
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
52-394 |
9.11e-17 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 82.05 E-value: 9.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 52 AGASRPLSPSPATEDPEATAVLaLSSGTTAEPKPVM--LSHRALSANIRQTVSALRGNGLDPGWSVLAPLPLSHIYGLNV 129
Cdd:PRK13391 139 AEAVAGLPATPIADESLGTDML-YSSGTTGRPKGIKrpLPEQPPDTPLPLTAFLQRLWGFRSDMVYLSPAPLYHSAPQRA 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 130 LLhSSLANGNHVVLMPRFTPRAFARLHAEHRIGWSYVAPPIV--------AALDSEDYSAdysaedfrhTRVMLSGAADL 201
Cdd:PRK13391 218 VM-LVIRLGGTVIVMEHFDAEQYLALIEEYGVTHTQLVPTMFsrmlklpeEVRDKYDLSS---------LEVAIHAAAPC 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 202 SPDLARRVGERLGVEIIQGYGMTEASPVTH------MMRRGDplgIGRPVDGtETRIVG-----------GELWVRGPQL 264
Cdd:PRK13391 288 PPQVKEQMIDWWGPIIHEYYAATEGLGFTAcdseewLAHPGT---VGRAMFG-DLHILDddgaelppgepGTIWFEGGRP 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 265 CSgYLGAPGPLVE------GWLPTGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAV--ARGTL 336
Cdd:PRK13391 364 FE-YLNDPAKTAEarhpdgTWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVfgVPNED 442
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2713532039 337 QGEEVpHAFVV-------GTAAPAEVHEWVARRVAPYKKVRRVTVVESIPRAATGKILRRRLRER 394
Cdd:PRK13391 443 LGEEV-KAVVQpvdgvdpGPALAAELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLRDR 506
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
67-394 |
2.05e-16 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 80.98 E-value: 2.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 67 PEATAV-LALSSGTTAEPKPVMLSHRAL---SANIRQTVSAlrgnGLDPGWSVLAPLPLSHIYGLNVLLHSSLANGNHVV 142
Cdd:PRK05620 179 DETTAAaICYSTGTTGAPKGVVYSHRSLylqSLSLRTTDSL----AVTHGESFLCCVPIYHVLSWGVPLAAFMSGTPLVF 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 143 LMPRFTPRAFARLHAEHRIGWSYVAPPIVAALDSedYSADYSAEDFRHTRVMLSGAAdLSPDLARRVGERLGVEIIQGYG 222
Cdd:PRK05620 255 PGPDLSAPTLAKIIATAMPRVAHGVPTLWIQLMV--HYLKNPPERMSLQEIYVGGSA-VPPILIKAWEERYGVDVVHVWG 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 223 MTEASPVTHMMRrgDPLGI------------GRPVDGTETRIVG------------GELWVRGPQLCSGYLGAPGP---- 274
Cdd:PRK05620 332 MTETSPVGTVAR--PPSGVsgearwayrvsqGRFPASLEYRIVNdgqvmestdrneGEIQVRGNWVTASYYHSPTEeggg 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 275 -----------------LVEGWLPTGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAvargtlq 337
Cdd:PRK05620 410 aastfrgedvedandrfTADGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECA------- 482
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2713532039 338 geevphafVVGTAAPaevhEWVARRVApykkvrrVTVV-ESIPR-AATGKILRRRLRER 394
Cdd:PRK05620 483 --------VIGYPDD----KWGERPLA-------VTVLaPGIEPtRETAERLRDQLRDR 522
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
1-397 |
3.05e-16 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 80.98 E-value: 3.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 1 VEFATAFHGILGAGATVVPLNP-----------------------LLTEEETRRAVQRTGARLRIDAPTARALHAgasrp 57
Cdd:PRK05691 75 PDYVAAFFGCLYAGVIAVPAYPpesarrhhqerllsiiadaeprlLLTVADLRDSLLQMEELAAANAPELLCVDT----- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 58 LSPSPATE------DPEATAVLALSSGTTAEPKPVMLSHRALSAN---IRQTVsalrGNGLDPGWSVLAPLPLSHIYGLN 128
Cdd:PRK05691 150 LDPALAEAwqepalQPDDIAFLQYTSGSTALPKGVQVSHGNLVANeqlIRHGF----GIDLNPDDVIVSWLPLYHDMGLI 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 129 VLLHSSLANGNHVVLM-PR-FTPRAFARLHAEHRIGWSYVAPPIVA-ALDSEDYS-ADYSAEDFRHTRVMLSGAADLSPD 204
Cdd:PRK05691 226 GGLLQPIFSGVPCVLMsPAyFLERPLRWLEAISEYGGTISGGPDFAyRLCSERVSeSALERLDLSRWRVAYSGSEPIRQD 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 205 LARRVGERLGV------EIIQGYGMTEASPVTHMMRRGDP------------------------LGIGRPVDGTETRIVG 254
Cdd:PRK05691 306 SLERFAEKFAAcgfdpdSFFASYGLAEATLFVSGGRRGQGipaleldaealarnraepgtgsvlMSCGRSQPGHAVLIVD 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 255 ------------GELWVRGPQLCSGYLGAPGP----LVE----GWLPTGDLvAPTPDGGLRVTGRTKEIIKYRGYQVSPA 314
Cdd:PRK05691 386 pqslevlgdnrvGEIWASGPSIAHGYWRNPEAsaktFVEhdgrTWLRTGDL-GFLRDGELFVTGRLKDMLIVRGHNLYPQ 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 315 ELEEVIAAC-PGVRD--VAVARGTLQGEEvphafvvGTAAPAEVHEWVARRVAPYK--KVRRVTVVE------------- 376
Cdd:PRK05691 465 DIEKTVEREvEVVRKgrVAAFAVNHQGEE-------GIGIAAEISRSVQKILPPQAliKSIRQAVAEacqeapsvvllln 537
|
490 500
....*....|....*....|...
gi 2713532039 377 --SIPRAATGKILRRRLRERAGD 397
Cdd:PRK05691 538 pgALPKTSSGKLQRSACRLRLAD 560
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
2-398 |
1.44e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 78.18 E-value: 1.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 2 EFATAFHGILGAGATVVPLNPLLTEEETRRAVQRTGARLRI---------------------DAPTARALHAGASRPLsP 60
Cdd:PRK07867 66 EFSLLLGAAALSGIVPVGLNPTRRGAALARDIAHADCQLVLtesahaelldgldpgvrvinvDSPAWADELAAHRDAE-P 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 61 SPATEDPEATAVLALSSGTTAEPKPVMLSHRALSAnirQTVSALRGNGLDPGWSVLAPLPLSHIYGLNVLLHSSLANGNH 140
Cdd:PRK07867 145 PFRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVAS---AGVMLAQRFGLGPDDVCYVSMPLFHSNAVMAGWAVALAAGAS 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 141 VVLMPRFTPRAFarLHAEHRIG---WSYVAPPIVAALDSEDysadySAEDFRHTRVMLSGAADLSPDLARrVGERLGVEI 217
Cdd:PRK07867 222 IALRRKFSASGF--LPDVRRYGatyANYVGKPLSYVLATPE-----RPDDADNPLRIVYGNEGAPGDIAR-FARRFGCVV 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 218 IQGYGMTEASpVTHMMRRGDPLG-IGRPVDGTE------------------TRIVG----GELW-VRGPQLCSGYLGAPG 273
Cdd:PRK07867 294 VDGFGSTEGG-VAITRTPDTPPGaLGPLPPGVAivdpdtgtecppaedadgRLLNAdeaiGELVnTAGPGGFEGYYNDPE 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 274 P----LVEGWLPTGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAV--ARGTLQGEEVPHAFVV 347
Cdd:PRK07867 373 AdaerMRGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVyaVPDPVVGDQVMAALVL 452
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2713532039 348 GTAA---PAEVHEWVARR--VAPYKKVRRVTVVESIPRAATGKILRRRLRERAGDA 398
Cdd:PRK07867 453 APGAkfdPDAFAEFLAAQpdLGPKQWPSYVRVCAELPRTATFKVLKRQLSAEGVDC 508
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
67-332 |
2.17e-15 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 77.78 E-value: 2.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 67 PEATAVLALSSGTTAEPKPVMLSHRALSANIrQTVSALRGNGLDPGWSV-LAPLPLSHIYGLNVLLHSSLANGNHVVLMP 145
Cdd:PRK12582 219 PDTVAKYLFTSGSTGMPKAVINTQRMMCANI-AMQEQLRPREPDPPPPVsLDWMPWNHTMGGNANFNGLLWGGGTLYIDD 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 146 -RFTPRAFAR-LHAEHRIG-WSYVAPPIVAALDSEDYSAD--YSAEDFRHTRVMLSGAADLSPDLARR--------VGER 212
Cdd:PRK12582 298 gKPLPGMFEEtIRNLREISpTVYGNVPAGYAMLAEAMEKDdaLRRSFFKNLRLMAYGGATLSDDLYERmqalavrtTGHR 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 213 lgVEIIQGYGMTEASPV---THMMRRGDPLgIGRPVDGTETRI--VGG--ELWVRGPQLCSGYLGAPGPLV-----EGWL 280
Cdd:PRK12582 378 --IPFYTGYGATETAPTttgTHWDTERVGL-IGLPLPGVELKLapVGDkyEVRVKGPNVTPGYHKDPELTAaafdeEGFY 454
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2713532039 281 PTGD---LVAPT-PDGGLRVTGRTKEIIKY-RGYQVSPAELE-EVIAAC-PGVRDVAVA 332
Cdd:PRK12582 455 RLGDaarFVDPDdPEKGLIFDGRVAEDFKLsTGTWVSVGTLRpDAVAACsPVIHDAVVA 513
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
67-386 |
3.42e-15 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 77.09 E-value: 3.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 67 PEATAVLALSSGTTAEPKPVMLSHRALSANIrQTVSALRGNGLDPGWSVLAPLPLSHIYGLNVLLHSSLANGNHVVL-MP 145
Cdd:cd05921 164 PDTVAKFLFTSGSTGLPKAVINTQRMLCANQ-AMLEQTYPFFGEEPPVLVDWLPWNHTFGGNHNFNLVLYNGGTLYIdDG 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 146 RFTPRAFAR-----------LHAEHRIGWSYvappIVAALDSEDYSAdysAEDFRHTRVMLSGAADLSPDLARR------ 208
Cdd:cd05921 243 KPMPGGFEEtlrnlreisptVYFNVPAGWEM----LVAALEKDEALR---RRFFKRLKLMFYAGAGLSQDVWDRlqalav 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 209 --VGERlgVEIIQGYGMTEASP---VTHMMRRGDPLgIGRPVDGTETRIV--GG--ELWVRGPQLCSGYLGAPGPLV--- 276
Cdd:cd05921 316 atVGER--IPMMAGLGATETAPtatFTHWPTERSGL-IGLPAPGTELKLVpsGGkyEVRVKGPNVTPGYWRQPELTAqaf 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 277 --EGWLPTGDLVAPT----PDGGLRVTGRTKEIIKYR-GYQVS--PAELEEVIAACPGVRDVAVArgTLQGEEV------ 341
Cdd:cd05921 393 deEGFYCLGDAAKLAdpddPAKGLVFDGRVAEDFKLAsGTWVSvgPLRARAVAACAPLVHDAVVA--GEDRAEVgalvfp 470
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2713532039 342 -----------PHAFVVGTAAPAEVHEWVARRVAPYKK--------VRRVTVVESIPRAATGKI 386
Cdd:cd05921 471 dllacrrlvglQEASDAEVLRHAKVRAAFRDRLAALNGeatgsssrIARALLLDEPPSIDKGEI 534
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
64-329 |
5.18e-15 |
|
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341256 [Multi-domain] Cd Length: 596 Bit Score: 76.63 E-value: 5.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 64 TEDPEATAVLALSSGTTAEPKPVMLSHRALSANIRQTVSALRGNGLDPGW-SVLAPLPLSHI------------YGLNVL 130
Cdd:cd05933 146 SQKPNQCCTLIYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLRPATVGQeSVVSYLPLSHIaaqildiwlpikVGGQVY 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 131 ------LHSSLANGNHVVLMPRF--TPRAFARLH-------------------------AEHRIGW---SYVAPPIVAAL 174
Cdd:cd05933 226 faqpdaLKGTLVKTLREVRPTAFmgVPRVWEKIQekmkavgaksgtlkrkiaswakgvgLETNLKLmggESPSPLFYRLA 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 175 DSEDYSADYSAEDFRHTRVMLSGAADLSPDLARRVgerLGVEI--IQGYGMTEASPvTHMMRRGDPLGI---GRPVDGTE 249
Cdd:cd05933 306 KKLVFKKVRKALGLDRCQKFFTGAAPISRETLEFF---LSLNIpiMELYGMSETSG-PHTISNPQAYRLlscGKALPGCK 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 250 TRIVG------GELWVRGPQLCSGYLGAPGPLVE-----GWLPTGDLVAPTPDGGLRVTGRTKEIIKYRGYQ-VSPAELE 317
Cdd:cd05933 382 TKIHNpdadgiGEICFWGRHVFMGYLNMEDKTEEaidedGWLHSGDLGKLDEDGFLYITGRIKELIITAGGEnVPPVPIE 461
|
330
....*....|...
gi 2713532039 318 EVI-AACPGVRDV 329
Cdd:cd05933 462 DAVkKELPIISNA 474
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
76-386 |
5.21e-15 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 76.36 E-value: 5.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 76 SSGTTAEPKPVMLSHRALSANI---RQTVSALRGNGLdpgwsVLAPLPLSHIYGLNVLLhsSLANGNHVVLMP---RFTP 149
Cdd:cd17654 126 TSGTTGTPKIVAVPHKCILPNIqhfRSLFNITSEDIL-----FLTSPLTFDPSVVEIFL--SLSSGATLLIVPtsvKVLP 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 150 RAFAR-LHAEHRIGWSYVAPPIVAALDSEDY-----SADYSaedfrhTRVMLSGAADLSPD--LARRVGERLGVEIIQGY 221
Cdd:cd17654 199 SKLADiLFKRHRITVLQATPTLFRRFGSQSIkstvlSATSS------LRVLALGGEPFPSLviLSSWRGKGNRTRIFNIY 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 222 GMTEAS--PVTHMMRRGD-PLGIGRPVDGTETRI-------VGGELWVRGPQLcSGYLGAPGPLVEG-WLPTGDLVAPTp 290
Cdd:cd17654 273 GITEVScwALAYKVPEEDsPVQLGSPLLGTVIEVrdqngseGTGQVFLGGLNR-VCILDDEVTVPKGtMRATGDFVTVK- 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 291 DGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAVargTLQGEEVPHAFVVGTAAPAEVH-EWVARRVAPYKKV 369
Cdd:cd17654 351 DGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAV---TLSDQQRLIAFIVGESSSSRIHkELQLTLLSSHAIP 427
|
330
....*....|....*..
gi 2713532039 370 RRVTVVESIPRAATGKI 386
Cdd:cd17654 428 DTFVQIDKLPLTSHGKV 444
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
65-385 |
5.56e-15 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 76.39 E-value: 5.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 65 EDPEATAVLALSSGTTAEPKPVMLSHRALSANIRQTVSALRGNGLDPGWSVLAPLplsHIYGLNVLLHSSLANGNHVV-- 142
Cdd:PRK06334 180 KDPEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLPPF---HAYGFNSCTLFPLLSGVPVVfa 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 143 ---LMPR----FTPRAFARLHAEHRIGWSYV---APPIVAALDSEDYsADYSAEDFRHTrvMLSGAADLSPDLARRvger 212
Cdd:PRK06334 257 ynpLYPKkiveMIDEAKVTFLGSTPVFFDYIlktAKKQESCLPSLRF-VVIGGDAFKDS--LYQEALKTFPHIQLR---- 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 213 lgveiiQGYGMTEASPVTHMMRRGDPLG---IGRPVDGTETRIVGGELWV------------RGPQLCSGYLGA-PGPLV 276
Cdd:PRK06334 330 ------QGYGTTECSPVITINTVNSPKHescVGMPIRGMDVLIVSEETKVpvssgetglvltRGTSLFSGYLGEdFGQGF 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 277 -----EGWLPTGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRD----VAVARGTLQGEEVphAFVV 347
Cdd:PRK06334 404 velggETWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEGFGQNAadhaGPLVVCGLPGEKV--RLCL 481
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2713532039 348 GTAAPAEVHE----WVARRVAPYKKVRRVTVVESIPRAATGK 385
Cdd:PRK06334 482 FTTFPTSISEvndiLKNSKTSSILKISYHHQVESIPMLGTGK 523
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
3-386 |
6.07e-15 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 76.46 E-value: 6.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 3 FATAFHGILGAGATVVplnpllteeeTRRAVQRTGARLRIDAPTARALHAGASRPLspspATEDPEATAVLALSSGTTAE 82
Cdd:PRK08180 158 FARALAAVVPADVEVV----------AVRGAVPGRAATPFAALLATPPTAAVDAAH----AAVGPDTIAKFLFTSGSTGL 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 83 PKPVMLSHRALSAN---IRQTVSALRGNG---LDpgWsvlapLPLSHIYGLNVLLHSSLANGNHVVLMP-RFTPRAFARL 155
Cdd:PRK08180 224 PKAVINTHRMLCANqqmLAQTFPFLAEEPpvlVD--W-----LPWNHTFGGNHNLGIVLYNGGTLYIDDgKPTPGGFDET 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 156 HAEHR-----------IGWSYvappIVAALDSEdysADYSAEDFRHTRVMLSGAADLSPDLARR--------VGERlgVE 216
Cdd:PRK08180 297 LRNLReisptvyfnvpKGWEM----LVPALERD---AALRRRFFSRLKLLFYAGAALSQDVWDRldrvaeatCGER--IR 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 217 IIQGYGMTEASPV---TH--MMRRGDplgIGRPVDGTETRIV--GG--ELWVRGPQLCSGYLGAPGPLV-----EGWLPT 282
Cdd:PRK08180 368 MMTGLGMTETAPSatfTTgpLSRAGN---IGLPAPGCEVKLVpvGGklEVRVKGPNVTPGYWRAPELTAeafdeEGYYRS 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 283 GDLVAPT----PDGGLRVTGRTKEIIK-YRGYQVSPAELE-EVIAAC-PGVRDVAVArGTLQGE---------------- 339
Cdd:PRK08180 445 GDAVRFVdpadPERGLMFDGRIAEDFKlSSGTWVSVGPLRaRAVSAGaPLVQDVVIT-GHDRDEigllvfpnldacrrla 523
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2713532039 340 -EVPHAFVVGTAAPAEVHEWVARRVAPYKK--------VRRVTVVESIPRAATGKI 386
Cdd:PRK08180 524 gLLADASLAEVLAHPAVRAAFRERLARLNAqatgsstrVARALLLDEPPSLDAGEI 579
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
27-331 |
1.24e-14 |
|
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: 75.57 E-value: 1.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 27 EETRRAVQRTGARLRIDapTARALHAGASRPLSPSPATEDPEATAVLALSSGTTAEPKPVMLSHRaLSANIRQTVSALRG 106
Cdd:cd17632 184 ESARERLAAVGIPVTTL--TLIAVRGRDLPPAPLFRPEPDDDPLALLIYTSGSTGTPKGAMYTER-LVATFWLKVSSIQD 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 107 NGLDPGwSVLAPLPLSHIYGLNVLLhSSLANGNHVVLMPR-------------------FTPRAFARLHAEHRigwSYVA 167
Cdd:cd17632 261 IRPPAS-ITLNFMPMSHIAGRISLY-GTLARGGTAYFAAAsdmstlfddlalvrptelfLVPRVCDMLFQRYQ---AELD 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 168 PPIVAALDSEDYSADYSAE---DFRHTRVM--LSGAADLSPDLARRVGERLGVEIIQGYGMTEASPVTHMMRRGDPlgig 242
Cdd:cd17632 336 RRSVAGADAETLAERVKAElreRVLGGRLLaaVCGSAPLSAEMKAFMESLLDLDLHDGYGSTEAGAVILDGVIVRP---- 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 243 rPVdgTETRIVG---------------GELWVRGPQLCSGYLGAPGPLVE-----GWLPTGDLVAPT-PDGGLRVTGRTK 301
Cdd:cd17632 412 -PV--LDYKLVDvpelgyfrtdrphprGELLVKTDTLFPGYYKRPEVTAEvfdedGFYRTGDVMAELgPDRLVYVDRRNN 488
|
330 340 350
....*....|....*....|....*....|
gi 2713532039 302 EIIKYRGYQVSPAELEEVIAACPGVRDVAV 331
Cdd:cd17632 489 VLKLSQGEFVTVARLEAVFAASPLVRQIFV 518
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
13-392 |
1.31e-14 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 75.43 E-value: 1.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 13 AGATVVPLNPLLTEEETRRAVQRTGARLRIDAPTARAL--HAGASRPLSPS--------------------PATEDPeAT 70
Cdd:PRK13390 72 SGLYITAINHHLTAPEADYIVGDSGARVLVASAALDGLaaKVGADLPLRLSfggeidgfgsfeaalagagpRLTEQP-CG 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 71 AVLALSSGTTAEPKPVM--LSHRALSANIRQTVSALRG-NGLDPGWSVLAPLPLSHIYGLN--VLLHsslANGNHVVLMP 145
Cdd:PRK13390 151 AVMLYSSGTTGFPKGIQpdLPGRDVDAPGDPIVAIARAfYDISESDIYYSSAPIYHAAPLRwcSMVH---ALGGTVVLAK 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 146 RFTPRAFARLHAEHRIGWSYVAPPIVAALDSEDYSADySAEDFRHTRVMLSGAADLSPDLARRVGERLGVEIIQGYGMTE 225
Cdd:PRK13390 228 RFDAQATLGHVERYRITVTQMVPTMFVRLLKLDADVR-TRYDVSSLRAVIHAAAPCPVDVKHAMIDWLGPIVYEYYSSTE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 226 ASPVThMMRRGD----PLGIGRPV---------DGTET---RIvgGELWVRGPQLCSGYLGAPGPLVEG-------WLPT 282
Cdd:PRK13390 307 AHGMT-FIDSPDwlahPGSVGRSVlgdlhicddDGNELpagRI--GTVYFERDRLPFRYLNDPEKTAAAqhpahpfWTTV 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 283 GDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAV--ARGTLQGEEVPHafVVGTAAPAEVHEWVA 360
Cdd:PRK13390 384 GDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVigVPDPEMGEQVKA--VIQLVEGIRGSDELA 461
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2713532039 361 R--------RVAPYKKVRRVTVVESIPRAATGKILRRRLR 392
Cdd:PRK13390 462 RelidytrsRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
50-331 |
2.41e-14 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 74.85 E-value: 2.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 50 LHAGASRPLSPSPAteDPEATAVLALSSGTTAEPKPVMLSHRALSANIRQTvsALRGNGLDPGWSV----LAPLPLSHIY 125
Cdd:PLN02430 204 LHMGKENPSETNPP--KPLDICTIMYTSGTSGDPKGVVLTHEAVATFVRGV--DLFMEQFEDKMTHddvyLSFLPLAHIL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 126 -----------GLNVLLHSSLANGNHVVLM---PRF---TPRAFARLHA---------------------EHRIGW---- 163
Cdd:PLN02430 280 drmieeyffrkGASVGYYHGDLNALRDDLMelkPTLlagVPRVFERIHEgiqkalqelnprrrlifnalyKYKLAWmnrg 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 164 ---SYVAPpivaaldsedySADYSAedFRHT--------RVMLSGAADLSPDlarrVGERLGVE----IIQGYGMTEASP 228
Cdd:PLN02430 360 yshKKASP-----------MADFLA--FRKVkaklggrlRLLISGGAPLSTE----IEEFLRVTscafVVQGYGLTETLG 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 229 VTHMmrrGDP-----LG-IGRPVDGTETRI----------VG----GELWVRGPQLCSGYLGAPGPLVE----GWLPTGD 284
Cdd:PLN02430 423 PTTL---GFPdemcmLGtVGAPAVYNELRLeevpemgydpLGepprGEICVRGKCLFSGYYKNPELTEEvmkdGWFHTGD 499
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2713532039 285 LVAPTPDGGLRVTGRTKEIIKY-RGYQVSPAELEEVIAACPGVRDVAV 331
Cdd:PLN02430 500 IGEILPNGVLKIIDRKKNLIKLsQGEYVALEYLENVYGQNPIVEDIWV 547
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
78-385 |
9.07e-14 |
|
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: 72.03 E-value: 9.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 78 GTTAEPKPVMLSH---RALSANIRQT----------VSALRGNGLDPGWSVLAPLplshIYGLNVLLHSSLANGNHVVLM 144
Cdd:cd05924 13 GTTGMPKGVMWRQediFRMLMGGADFgtgeftpsedAHKAAAAAAGTVMFPAPPL----MHGTGSWTAFGGLLGGQTVVL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 145 P--RFTPRAFARLHAEHRIGWSYV-----APPIVAALDsedysaDYSAEDFRHTRVMLSGAADLSPD----LARRVGERL 213
Cdd:cd05924 89 PddRFDPEEVWRTIEKHKVTSMTIvgdamARPLIDALR------DAGPYDLSSLFAISSGGALLSPEvkqgLLELVPNIT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 214 GVEII-------QGYGMTEASPV-THMMRRGDPLGIGRPVDGTE-TRIVGGELWV-RGPQLCSGYLGAPG------PLVE 277
Cdd:cd05924 163 LVDAFgssetgfTGSGHSAGSGPeTGPFTRANPDTVVLDDDGRVvPPGSGGVGWIaRRGHIPLGYYGDEAktaetfPEVD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 278 G--WLPTGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAVA--RGTLQGEEVphAFVVGTAAPA 353
Cdd:cd05924 243 GvrYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVgrPDERWGQEV--VAVVQLREGA 320
|
330 340 350
....*....|....*....|....*....|....*..
gi 2713532039 354 -----EVHEWVARRVAPYKKVRRVTVVESIPRAATGK 385
Cdd:cd05924 321 gvdleELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
65-395 |
1.04e-13 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 72.57 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 65 EDPEATAVLALSSGTTAEPKPVMLSHRAlsanirQTVSALRGN---GLDPGWSVLAPLPLSHIYGLNVLLHSSLANGNHV 141
Cdd:PLN02479 192 ADEWQSIALGYTSGTTASPKGVVLHHRG------AYLMALSNAliwGMNEGAVYLWTLPMFHCNGWCFTWTLAALCGTNI 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 142 VLMPRFTP---RAFARLHAEHRIGWSYVAPPIVAALDSEdysadySAEDFRHT-RVMLSGAADlSPDLARRVGERlGVEI 217
Cdd:PLN02479 266 CLRQVTAKaiySAIANYGVTHFCAAPVVLNTIVNAPKSE------TILPLPRVvHVMTAGAAP-PPSVLFAMSEK-GFRV 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 218 IQGYGMTE---------------ASPVTHMMRRGDPLGI---------------GRPV--DGTETrivgGELWVRGPQLC 265
Cdd:PLN02479 338 THTYGLSEtygpstvcawkpewdSLPPEEQARLNARQGVryiglegldvvdtktMKPVpaDGKTM----GEIVMRGNMVM 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 266 SGYLGAPGPLVE----GWLPTGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVA-VARGTLQGEE 340
Cdd:PLN02479 414 KGYLKNPKANEEafanGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASvVARPDERWGE 493
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2713532039 341 VPHAFVV--------GTAAPAEVHEWVARRVAPYKKVRRVTVVESIPRAATGKILRRRLRERA 395
Cdd:PLN02479 494 SPCAFVTlkpgvdksDEAALAEDIMKFCRERLPAYWVPKSVVFGPLPKTATGKIQKHVLRAKA 556
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
78-385 |
3.17e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 71.07 E-value: 3.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 78 GTTAEPKPVMLSH-----------RALSANIRQTVSALRGNGLDPGWSVLAPL-PLSHIYGLNVLLhSSLANGNHVVLMP 145
Cdd:PRK07798 173 GTTGMPKGVMWRQedifrvllggrDFATGEPIEDEEELAKRAAAGPGMRRFPApPLMHGAGQWAAF-AALFSGQTVVLLP 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 146 --RFTPRAFARLHAEHRIGWSYV-----APPIVAALDSEDySADYSAedfrhTRVMLSGAADLSPDLARRVGERL-GVEI 217
Cdd:PRK07798 252 dvRFDADEVWRTIEREKVNVITIvgdamARPLLDALEARG-PYDLSS-----LFAIASGGALFSPSVKEALLELLpNVVL 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 218 IQGYGMTEASPVTHMMRRGDPLGIGRP---------VDGTETRIV----GGELWV-RGPQLCSGYLGAPG------PLVE 277
Cdd:PRK07798 326 TDSIGSSETGFGGSGTVAKGAVHTGGPrftigprtvVLDEDGNPVepgsGEIGWIaRRGHIPLGYYKDPEktaetfPTID 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 278 G--WLPTGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAVA-----RgtlQGEEVphAFVV--- 347
Cdd:PRK07798 406 GvrYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVgvpdeR---WGQEV--VAVVqlr 480
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2713532039 348 --GTAAPAEVHEWVARRVAPYKKVRRVTVVESIPRAATGK 385
Cdd:PRK07798 481 egARPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
2-400 |
3.83e-13 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 70.83 E-value: 3.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 2 EFATAFHGILGAGATVVPLNPLLTEEETRRAVQRTGARLRIDAPTARALHAG---------------------ASRPLSP 60
Cdd:PRK13388 64 EMLFWLAAAALGGYVLVGLNTTRRGAALAADIRRADCQLLVTDAEHRPLLDGldlpgvrvldvdtpayaelvaAAGALTP 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 61 SPATeDPEATAVLALSSGTTAEPKPVMLSHRALsanIRQTVSALRGNGLDPGWSVLAPLPLSHIYGLNVLLHSSLANGNH 140
Cdd:PRK13388 144 HREV-DAMDPFMLIFTSGTTGAPKAVRCSHGRL---AFAGRALTERFGLTRDDVCYVSMPLFHSNAVMAGWAPAVASGAA 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 141 VVLMPRFTPRAFarLHAEHRIG---WSYVAPPIVAALdsedysADYSAEDFRHTRVMLSGAADLSPDLARRVGERLGVEI 217
Cdd:PRK13388 220 VALPAKFSASGF--LDDVRRYGatyFNYVGKPLAYIL------ATPERPDDADNPLRVAFGNEASPRDIAEFSRRFGCQV 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 218 IQGYGMTEASpVTHMMRRGDPLG-IGRPVDGT-----ETRIVG------------------GELWVR-GPQLCSGYLGAP 272
Cdd:PRK13388 292 EDGYGSSEGA-VIVVREPGTPPGsIGRGAPGVaiynpETLTECavarfdahgallnadeaiGELVNTaGAGFFEGYYNNP 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 273 GPLVE----GWLPTGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAV--ARGTLQGEEVPHAFV 346
Cdd:PRK13388 371 EATAErmrhGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVyaVPDERVGDQVMAALV 450
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2713532039 347 V---GTAAPAEVHEWVA------RRVAPykkvRRVTVVESIPRAATGKILRRRLRERAGDADE 400
Cdd:PRK13388 451 LrdgATFDPDAFAAFLAaqpdlgTKAWP----RYVRIAADLPSTATNKVLKRELIAQGWATGD 509
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
278-400 |
3.84e-13 |
|
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: 71.05 E-value: 3.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 278 GWLPTGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAV-ARGTLQGEEVPHAFVV---GTAAP- 352
Cdd:cd05966 469 GYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVvGRPHDIKGEAIYAFVTlkdGEEPSd 548
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2713532039 353 ---AEVHEWVARRVAPYKKVRRVTVVESIPRAATGKILRRRLRERAGDADE 400
Cdd:cd05966 549 elrKELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMRRILRKIAAGEEE 599
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
76-360 |
5.94e-13 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 70.26 E-value: 5.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 76 SSGTTAEPKPVMLSHRALSANIRQTVSALR--GNGLDPGWSVLAPLPLSHIYGlNVLLHSSLANGNHV------------ 141
Cdd:PLN02861 228 TSGTTGEPKGVILTNRAIIAEVLSTDHLLKvtDRVATEEDSYFSYLPLAHVYD-QVIETYCISKGASIgfwqgdirylme 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 142 ---VLMPRF---TPRAFARLHAE---------------HRIGWSYVAPPIVAALDSEDYSADYSAEDFRHT--------R 192
Cdd:PLN02861 307 dvqALKPTIfcgVPRVYDRIYTGimqkissggmlrkklFDFAYNYKLGNLRKGLKQEEASPRLDRLVFDKIkeglggrvR 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 193 VMLSGAADLSpdlaRRVGERLGVE----IIQGYGMTE--ASPVTHMMRRGDPLG-IGRPVDGTETRIVG----------- 254
Cdd:PLN02861 387 LLLSGAAPLP----RHVEEFLRVTscsvLSQGYGLTEscGGCFTSIANVFSMVGtVGVPMTTIEARLESvpemgydalsd 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 255 ---GELWVRGPQLCSGYLGAPG----PLVEGWLPTGDLVAPTPDGGLRVTGRTKEIIKY-RGYQVSPAELEEVIAACPGV 326
Cdd:PLN02861 463 vprGEICLRGNTLFSGYHKRQDlteeVLIDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLsQGEYVAVENLENTYSRCPLI 542
|
330 340 350
....*....|....*....|....*....|....*.
gi 2713532039 327 RDVAVARGTLQgeevphAFVVGTAAPAE--VHEWVA 360
Cdd:PLN02861 543 ASIWVYGNSFE------SFLVAVVVPDRqaLEDWAA 572
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
62-392 |
7.88e-13 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 69.77 E-value: 7.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 62 PATEDPEATAVLALSSGTTAEPKPVMLSHRALSANIRQTVsaLRGNGLDPGWSVLAPLPLSHIYGLNVLLHSSLAnGNHV 141
Cdd:PRK12476 187 PVELDTDDVSHLQYTSGSTRPPVGVEITHRAVGTNLVQMI--LSIDLLDRNTHGVSWLPLYHDMGLSMIGFPAVY-GGHS 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 142 VLMprfTPRAFAR--------LHAEHRIGWSYVAPPivaaldseDYSADYSAE----------DFRHTrVMLSGAADLSP 203
Cdd:PRK12476 264 TLM---SPTAFVRrpqrwikaLSEGSRTGRVVTAAP--------NFAYEWAAQrglpaegddiDLSNV-VLIIGSEPVSI 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 204 DLARRVGERLG------VEIIQGYGMTEAS------------PVTHMMRRGdpLGIGR--PVDGTETRIVG--------- 254
Cdd:PRK12476 332 DAVTTFNKAFApyglprTAFKPSYGIAEATlfvatiapdaepSVVYLDREQ--LGAGRavRVAADAPNAVAhvscgqvar 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 255 --------------------GELWVRGPQLCSGYLGAP------------GPLVEG-----------WLPTGDLvAPTPD 291
Cdd:PRK12476 410 sqwavivdpdtgaelpdgevGEIWLHGDNIGRGYWGRPeetertfgaklqSRLAEGshadgaaddgtWLRTGDL-GVYLD 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 292 GGLRVTGRTKEIIKYRGYQVSPAELEEVIA-ACPGVRDVAVARGTLQGEEVPHAFVV-------GTAAPAEVHE----WV 359
Cdd:PRK12476 489 GELYITGRIADLIVIDGRNHYPQDIEATVAeASPMVRRGYVTAFTVPAEDNERLVIVaeraagtSRADPAPAIDairaAV 568
|
410 420 430
....*....|....*....|....*....|....
gi 2713532039 360 ARRVA-PYKKVRRVTVvESIPRAATGKILRRRLR 392
Cdd:PRK12476 569 SRRHGlAVADVRLVPA-GAIPRTTSGKLARRACR 601
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
53-331 |
1.10e-11 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 66.29 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 53 GASRPLSPS-PATEDpeaTAVLALSSGTTAEPKPVMLSHRalsaNIRQTVSALRG--NGLDPGWSVLAPLPLSHIYGL-- 127
Cdd:PLN02387 237 GKENPVDPDlPSPND---IAVIMYTSGSTGLPKGVMMTHG----NIVATVAGVMTvvPKLGKNDVYLAYLPLAHILELaa 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 128 -NVLLHSSLANG-----------NHV-------------VLM---PRFTPR----------------------AFARLHA 157
Cdd:PLN02387 310 eSVMAAVGAAIGygspltltdtsNKIkkgtkgdasalkpTLMtavPAILDRvrdgvrkkvdakgglakklfdiAYKRRLA 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 158 E-----------HRIGWSY-VAPPIVAALDSedysadysaedfrHTRVMLSGAADLSPDLARRVGERLGVEIIQGYGMTE 225
Cdd:PLN02387 390 AiegswfgawglEKLLWDAlVFKKIRAVLGG-------------RIRFMLSGGAPLSGDTQRFINICLGAPIGQGYGLTE 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 226 ASPVTHMMRRGDP-LG-IGRPVDGTETRIVG---------------GELWVRGPQLCSGYLGAPGPLVE---------GW 279
Cdd:PLN02387 457 TCAGATFSEWDDTsVGrVGPPLPCCYVKLVSweeggylisdkpmprGEIVIGGPSVTLGYFKNQEKTDEvykvdergmRW 536
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2713532039 280 LPTGDLVAPTPDGGLRVTGRTKEIIKYR-GYQVSPAELEEVIAACPGVRDVAV 331
Cdd:PLN02387 537 FYTGDIGQFHPDGCLEIIDRKKDIVKLQhGEYVSLGKVEAALSVSPYVDNIMV 589
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
67-360 |
3.09e-11 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 65.04 E-value: 3.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 67 PEATAVLALSSGTTAEPKPVMLSHRALSANIRQTVSALRG--NGLDPGWSVLAPLPLSHIY------------------- 125
Cdd:PLN02614 222 KSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLKSanAALTVKDVYLSYLPLAHIFdrvieecfiqhgaaigfwr 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 126 GLNVLLHSSLANGNHVVL--MPRFTPRAFARLHAE----------------------HRIGWSYV-APPIVAALDSEDYS 180
Cdd:PLN02614 302 GDVKLLIEDLGELKPTIFcaVPRVLDRVYSGLQKKlsdggflkkfvfdsafsykfgnMKKGQSHVeASPLCDKLVFNKVK 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 181 ADYSAedfrHTRVMLSGAADLSPDLARRVGERLGVEIIQGYGMTEASPVThMMRRGDPLG----IGRPVDGTETRIVG-- 254
Cdd:PLN02614 382 QGLGG----NVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTESCAGT-FVSLPDELDmlgtVGPPVPNVDIRLESvp 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 255 ------------GELWVRGPQLCSGYLG----APGPLVEGWLPTGDLVAPTPDGGLRVTGRTKEIIKY-RGYQVSPAELE 317
Cdd:PLN02614 457 emeydalastprGEICIRGKTLFSGYYKredlTKEVLIDGWLHTGDVGEWQPNGSMKIIDRKKNIFKLsQGEYVAVENIE 536
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2713532039 318 EVIAACPGVRDVAVARGTLQgeevphAFVVGTAAPAE--VHEWVA 360
Cdd:PLN02614 537 NIYGEVQAVDSVWVYGNSFE------SFLVAIANPNQqiLERWAA 575
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
56-393 |
4.49e-11 |
|
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: 64.37 E-value: 4.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 56 RPLSPSPATeDPEAtavLALSSGTTAEPKPVMLSHRALSANIrQTVSALRGNGLDPGWSVLAPLPLSHIYGLNVLLHSSL 135
Cdd:cd05915 145 ADPVRVPER-AACG---MAYTTGTTGLPKGVVYSHRALVLHS-LAASLVDGTALSEKDVVLPVVPMFHVNAWCLPYAATL 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 136 ANGNHVVLMPRFTPRAFARLHAEHRIGWSYVAPPIVAALDSedySADYSAEDFRHTRVMLSGAADlSPDLARRVGERLGV 215
Cdd:cd05915 220 VGAKQVLPGPRLDPASLVELFDGEGVTFTAGVPTVWLALAD---YLESTGHRLKTLRRLVVGGSA-APRSLIARFERMGV 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 216 EIIQGYGMTEAS---------------PVTHMMRRG---------------DPLGIGRPVDGTETRIVGgelwVRGPQLC 265
Cdd:cd05915 296 EVRQGYGLTETSpvvvqnfvkshleslSEEEKLTLKaktglpiplvrlrvaDEEGRPVPKDGKALGEVQ----LKGPWIT 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 266 SGYLG-----APGPLVEGWLPTGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVA-VARGTLQGE 339
Cdd:cd05915 372 GGYYGneeatRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAvVAIPHPKWQ 451
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2713532039 340 EVPHAFVVGTAAPA---EVHEWVARRVAPYKKVRRVTVVES-IPRAATGKILRRRLRE 393
Cdd:cd05915 452 ERPLAVVVPRGEKPtpeELNEHLLKAGFAKWQLPDAYVFAEeIPRTSAGKFLKRALRE 509
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
315-385 |
5.15e-11 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 58.32 E-value: 5.15e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2713532039 315 ELEEVIAACPGVRDVAV--ARGTLQGEeVPHAFVV----GTAAPAEVHEWVARRVAPYKKVRRVTVVESIPRAATGK 385
Cdd:pfam13193 1 EVESALVSHPAVAEAAVvgVPDELKGE-APVAFVVlkpgVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
59-394 |
1.19e-10 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 62.99 E-value: 1.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 59 SPSPATE--DPEATAVLALSSGTTAEPKPVMLSHRALsanIRQTVSALRGNGL----------DPGW------SVLAPLp 120
Cdd:PRK04319 194 SDEFDIEwtDREDGAILHYTSGSTGKPKGVLHVHNAM---LQHYQTGKYVLDLheddvywctaDPGWvtgtsyGIFAPW- 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 121 lshiyglnvllhssLANGNHVVLMPRFTPRAFARLHAEHRIGWSYVAPPIVAALDS--EDYSADYsaeDFRHTRVMLSGA 198
Cdd:PRK04319 270 --------------LNGATNVIDGGRFSPERWYRILEDYKVTVWYTAPTAIRMLMGagDDLVKKY---DLSSLRHILSVG 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 199 ADLSPDLARRVGERLGVEIIQGYGMTE----------ASPVThmmrrgdPLGIGRPVDGTETRIVG-----------GEL 257
Cdd:PRK04319 333 EPLNPEVVRWGMKVFGLPIHDNWWMTEtggimianypAMDIK-------PGSMGKPLPGIEAAIVDdqgnelppnrmGNL 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 258 WVRG--PQLCSGYLGAPGP----LVEGWLPTGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAV 331
Cdd:PRK04319 406 AIKKgwPSMMRGIWNNPEKyesyFAGDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGV 485
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2713532039 332 ------ARGtlqgeEVPHAFVV-------GTAAPAEVHEWVARRVAPYKKVRRVTVVESIPRAATGKILRRRLRER 394
Cdd:PRK04319 486 igkpdpVRG-----EIIKAFVAlrpgyepSEELKEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVLKAW 556
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
9-391 |
1.43e-10 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 63.26 E-value: 1.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 9 GILGAGATVVPLNPLLTEEETRRAVQRTGARL----RIDAPTARAL---HAGASRPL--------SPSPATEDP------ 67
Cdd:PRK05691 3789 GSFKAGAGYLPLDPGLPAQRLQRIIELSRTPVlvcsAACREQARALldeLGCANRPRllvweevqAGEVASHNPgiysgp 3868
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 68 EATAVLALSSGTTAEPKPVMLSHRALSANIRQTVSALRGNGLDpgwsVLAPLPlSHIYGLNV--LLHSSLAnGNHVVLMP 145
Cdd:PRK05691 3869 DNLAYVIYTSGSTGLPKGVMVEQRGMLNNQLSKVPYLALSEAD----VIAQTA-SQSFDISVwqFLAAPLF-GARVEIVP 3942
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 146 R---FTPRAFARLHAEHRIGWSYVAPPIVAALDSEDYSAdysaedFRHTRVMLSGAADLSPDLARRVGERL-GVEIIQGY 221
Cdd:PRK05691 3943 NaiaHDPQGLLAHVQAQGITVLESVPSLIQGMLAEDRQA------LDGLRWMLPTGEAMPPELARQWLQRYpQIGLVNAY 4016
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 222 GMTEAS------PVTHMMRRGDPLGIGRPVDGTETRIVG-----------GELWVRGPQLCSGYLGAPGPLVEGWLP--- 281
Cdd:PRK05691 4017 GPAECSddvaffRVDLASTRGSYLPIGSPTDNNRLYLLDealelvplgavGELCVAGTGVGRGYVGDPLRTALAFVPhpf 4096
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 282 ---------TGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAVARGT------LQGEEVPHAfv 346
Cdd:PRK05691 4097 gapgerlyrTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAVQEgvngkhLVGYLVPHQ-- 4174
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 2713532039 347 vGTAAPAEVHEWVARRVAP----YKKVRRVTVVESIPRAATGKILRRRL 391
Cdd:PRK05691 4175 -TVLAQGALLERIKQRLRAelpdYMVPLHWLWLDRLPLNANGKLDRKAL 4222
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
65-305 |
1.99e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 62.43 E-value: 1.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 65 EDPEATAVLALSSGTTAEPKPVMLSHRalsaNIRQTVSALRGNGLDPGWSV---LAPLPLSHIYGlNVLLHSSL------ 135
Cdd:PTZ00342 301 EDPDFITSIVYTSGTSGKPKGVMLSNK----NLYNTVVPLCKHSIFKKYNPkthLSYLPISHIYE-RVIAYLSFmlggti 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 136 ----------------ANGNHVVLMPRFTPRAFARLHAEhrIGwsyVAPPI-------VAALDSEDYSADYSA--EDFRH 190
Cdd:PTZ00342 376 niwskdinyfskdiynSKGNILAGVPKVFNRIYTNIMTE--IN---NLPPLkrflvkkILSLRKSNNNGGFSKflEGITH 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 191 T------------RVMLSGAADLSPDLARRVGERLGVEIIQGYGMTEAS-PVTHMMRRG-DPLGIGRPVDGT-------- 248
Cdd:PTZ00342 451 IsskikdkvnpnlEVILNGGGKLSPKIAEELSVLLNVNYYQGYGLTETTgPIFVQHADDnNTESIGGPISPNtkykvrtw 530
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2713532039 249 ET-----RIVGGELWVRGPQLCSGYlgapgpLVE-----------GWLPTGDLVAPTPDGGLRVTGRTKEIIK 305
Cdd:PTZ00342 531 ETykatdTLPKGELLIKSDSIFSGY------FLEkeqtknaftedGYFKTGDIVQINKNGSLTFLDRSKGLVK 597
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
66-397 |
3.44e-10 |
|
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: 61.29 E-value: 3.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 66 DPEATAVLALSSGTTAEPKPVMLSHRALSanirqTVSALRGN--GLDPGWSVLAPLPLSHIYGLNVLLHSSLANGNHVVL 143
Cdd:cd05937 85 DPDDPAILIYTSGTTGLPKAAAISWRRTL-----VTSNLLSHdlNLKNGDRTYTCMPLYHGTAAFLGACNCLMSGGTLAL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 144 MPRFTPRAF---ARLHAEHRIgwSYVAPPIVAALdsedySADYSAEDFRHtRVMLSGAADLSPDLARRVGERLGVEII-Q 219
Cdd:cd05937 160 SRKFSASQFwkdVRDSGATII--QYVGELCRYLL-----STPPSPYDRDH-KVRVAWGNGLRPDIWERFRERFNVPEIgE 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 220 GYGMTEASPVTHMMRRGdPLGIG-------------------------------RPVDGTETRIV---GGELWVRGP--- 262
Cdd:cd05937 232 FYAATEGVFALTNHNVG-DFGAGaighhglirrwkfenqvvlvkmdpetddpirDPKTGFCVRAPvgePGEMLGRVPfkn 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 263 -QLCSGYLGAP----GPLVEG-------WLPTGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVA 330
Cdd:cd05937 311 rEAFQGYLHNEdateSKLVRDvfrkgdiYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEAN 390
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2713532039 331 VARGTLQGEE----------VPHAFVVGTAAPAEVHEWVARRVAPYKKVRRVTVVESIPRAATGKILRRRLRERAGD 397
Cdd:cd05937 391 VYGVKVPGHDgragcaaitlEESSAVPTEFTKSLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLRDEGVD 467
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
2-392 |
3.75e-10 |
|
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: 61.74 E-value: 3.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 2 EFATAFHGILGAGATVVPLNPLLTEEETRRAVQRTGARLRIDA-------------PTAR------------ALHAGASR 56
Cdd:cd05968 128 EIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALITAdgftrrgrevnlkEEADkacaqcptvekvVVVRHLGN 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 57 PLSPSP-----------------ATEDPEATAVLALSSGTTAEPKPVMLSHRALSanIRQTVSALRGNGLDPGWSVLAPL 119
Cdd:cd05968 208 DFTPAKgrdlsydeeketagdgaERTESEDPLMIIYTSGTTGKPKGTVHVHAGFP--LKAAQDMYFQFDLKPGDLLTWFT 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 120 PLSHIYGlNVLLHSSLANGNHVVL---MPRF-TPRAFARLHAEHRIGWSYVAPPIVAALDSEDySADYSAEDFRHTRVML 195
Cdd:cd05968 286 DLGWMMG-PWLIFGGLILGATMVLydgAPDHpKADRLWRMVEDHEITHLGLSPTLIRALKPRG-DAPVNAHDLSSLRVLG 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 196 SGAADLSPDLARRVGERLGVE---IIQGYGMTEASP---VTHMMRRGDPLGIGRPVDGTE--------TRIVG--GELWV 259
Cdd:cd05968 364 STGEPWNPEPWNWLFETVGKGrnpIINYSGGTEISGgilGNVLIKPIKPSSFNGPVPGMKadvldesgKPARPevGELVL 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 260 RGP--QLCSG-------YLGAPGPLVEGWLPTGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVA 330
Cdd:cd05968 444 LAPwpGMTRGfwrdedrYLETYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESA 523
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2713532039 331 vARGT---LQGEEvPHAFVV-------GTAAPAEVHEWVARRVAPYKKVRRVTVVESIPRAATGKILRRRLR 392
Cdd:cd05968 524 -AIGVphpVKGEA-IVCFVVlkpgvtpTEALAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIR 593
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
221-396 |
4.60e-10 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 61.16 E-value: 4.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 221 YGMTE-ASPVThMMRRGDPL----GIGRPVDGTETRIVG---GELWVRGPQLCSGYLgapgPLVE---GWLPTGDLVAPT 289
Cdd:PRK07445 261 YGMTEtASQIA-TLKPDDFLagnnSSGQVLPHAQITIPAnqtGNITIQAQSLALGYY----PQILdsqGIFETDDLGYLD 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 290 PDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAVArGTLQGE--EVPHAFVVGTA---APAEVHEWVARRVA 364
Cdd:PRK07445 336 AQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVL-GLPDPHwgEVVTAIYVPKDpsiSLEELKTAIKDQLS 414
|
170 180 190
....*....|....*....|....*....|..
gi 2713532039 365 PYKKVRRVTVVESIPRAATGKILRRRLRERAG 396
Cdd:PRK07445 415 PFKQPKHWIPVPQLPRNPQGKINRQQLQQIAV 446
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
53-398 |
7.79e-10 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 60.60 E-value: 7.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 53 GASRPLSPSPATEDPEATAVLALSSGTTAEPKPVMLSHralSANIRQTVSALRGNGLDPGWSVLAPLPLSHIYGlNVLLH 132
Cdd:PLN03051 104 GSVGGNEYSPVYAPVESVTNILFSSGTTGEPKAIPWTH---LSPLRCASDGWAHMDIQPGDVVCWPTNLGWMMG-PWLLY 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 133 SSLANGNHVVLM---PrfTPRAFARLHAEHRIGWSYVAPPIVAALDSEDySADYSAEDFRHTRV---------------M 194
Cdd:PLN03051 180 SAFLNGATLALYggaP--LGRGFGKFVQDAGVTVLGLVPSIVKAWRHTG-AFAMEGLDWSKLRVfastgeasavddvlwL 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 195 LSGAADLSPDLARRVGERLGVEIIQGYGMTEASP---VTHMMRRG----DPLGIGRPVDGTetriVGGELWVRGPQLCSG 267
Cdd:PLN03051 257 SSVRGYYKPVIEYCGGTELASGYISSTLLQPQAPgafSTASLGTRfvllNDNGVPYPDDQP----CVGEVALAPPMLGAS 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 268 ------------YLGAPGPLVEGwLPT---GDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVI--AACPGVRDVA 330
Cdd:PLN03051 333 drllnadhdkvyYKGMPMYGSKG-MPLrrhGDIMKRTPGGYFCVQGRADDTMNLGGIKTSSVEIERACdrAVAGIAETAA 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 331 VARGTLQGEevPHAFVV-----------GTAAPAEVH----EWVARRVAPYKKVRRVTVVESIPRAATGKILRRRLRERA 395
Cdd:PLN03051 412 VGVAPPDGG--PELLVIflvlgeekkgfDQARPEALQkkfqEAIQTNLNPLFKVSRVKIVPELPRNASNKLLRRVLRDQL 489
|
...
gi 2713532039 396 GDA 398
Cdd:PLN03051 490 KKE 492
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
70-331 |
8.52e-10 |
|
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: 60.06 E-value: 8.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 70 TAVLALSSGTTAEPKPVMLSHRalsanirqtvSALRGNGLDPGWSVLAP-------LPLSHIYGLNVLLHSSLANGNHVV 142
Cdd:cd05940 83 AALYIYTSGTTGLPKAAIISHR----------RAWRGGAFFAGSGGALPsdvlytcLPLYHSTALIVGWSACLASGATLV 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 143 LMPRFTPRAFARLHAEHR------IG--WSYV--APPivaaldsedysadySAEDFRHTRVMLSGAAdLSPDLARRVGER 212
Cdd:cd05940 153 IRKKFSASNFWDDIRKYQatifqyIGelCRYLlnQPP--------------KPTERKHKVRMIFGNG-LRPDIWEEFKER 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 213 LGV-EIIQGYGMTEASpVTHMMRRGDPLGIGR----PVDGTETRIV-----GGELWvRGPqlcSGYL-----GAPGPLV- 276
Cdd:cd05940 218 FGVpRIAEFYAATEGN-SGFINFFGKPGAIGRnpslLRKVAPLALVkydleSGEPI-RDA---EGRCikvprGEPGLLIs 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 277 -----------------------------EGWLPTGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVR 327
Cdd:cd05940 293 rinplepfdgytdpaatekkilrdvfkkgDAWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVE 372
|
....
gi 2713532039 328 DVAV 331
Cdd:cd05940 373 EANV 376
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
10-391 |
4.19e-09 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 58.64 E-value: 4.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 10 ILGAGATVVPLNPLLTEEETRRAVQRTGARLRI-DAPTARA---LHAGASR-------------PLSPSPATEDPEATAV 72
Cdd:PRK05691 2258 ILKAGGAYVPLDPEYPLERLHYMIEDSGIGLLLsDRALFEAlgeLPAGVARwcleddaaalaaySDAPLPFLSLPQHQAY 2337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 73 LALSSGTTAEPKPVMLSHRALSANIRQTVSALrgnGLDPGWSVLaplplsHIYGLNV-----LLHSSLANGNHVVLMPR- 146
Cdd:PRK05691 2338 LIYTSGSTGKPKGVVVSHGEIAMHCQAVIERF---GMRADDCEL------HFYSINFdaaseRLLVPLLCGARVVLRAQg 2408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 147 -FTPRAFARLHAEHRIGWSYVAPPIVAALdsedysADYSA--EDFRHTRVMLSGAADLSPDLARRVGERLGVEII-QGYG 222
Cdd:PRK05691 2409 qWGAEEICQLIREQQVSILGFTPSYGSQL------AQWLAgqGEQLPVRMCITGGEALTGEHLQRIRQAFAPQLFfNAYG 2482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 223 MTE------ASPVTHMMRRGD-PLGIGRPVDGTETRIVG-----------GELWVRGPQLCSGYLGAPGPLVEGWLP--- 281
Cdd:PRK05691 2483 PTEtvvmplACLAPEQLEEGAaSVPIGRVVGARVAYILDadlalvpqgatGELYVGGAGLAQGYHDRPGLTAERFVAdpf 2562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 282 ---------TGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAV-ARGTLQGEEVPHAFVVGTAA 351
Cdd:PRK05691 2563 aadggrlyrTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVlALDTPSGKQLAGYLVSAVAG 2642
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 2713532039 352 PAEVHEWVAR-RVAPYKKVR--------RVTVVESIPRAATGKILRRRL 391
Cdd:PRK05691 2643 QDDEAQAALReALKAHLKQQlpdymvpaHLILLDSLPLTANGKLDRRAL 2691
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
1-392 |
2.32e-08 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 55.89 E-value: 2.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 1 VEFATAFHGILGAGATVVPL---------------------NPLLTEEETRRAVQR------TGARLRIDAPTARALHAG 53
Cdd:PRK07769 90 LDYLIAFFGALYAGRIAVPLfdpaepghvgrlhavlddctpSAILTTTDSAEGVRKffrarpAKERPRVIAVDAVPDEVG 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 54 ASrpLSPSPATEDpeATAVLALSSGTTAEPKPVMLSHRALSANIRQTVSALRGNGLDPG--WsvlapLPLSHIYGLNVLL 131
Cdd:PRK07769 170 AT--WVPPEANED--TIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEGQEGDRGvsW-----LPFFHDMGLITVL 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 132 HSSLAnGNHVVLMprfTPRAFAR---------LHAEHRIGWSYVAPPivaaldseDYSADYSAE-----------DFRHT 191
Cdd:PRK07769 241 LPALL-GHYITFM---SPAAFVRrpgrwirelARKPGGTGGTFSAAP--------NFAFEHAAArglpkdgepplDLSNV 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 192 RVMLSGAADLSPDLARRVGERLG------VEIIQGYGMTEAS------------PVTHMMRrgDPLGIGR--PVDGTETR 251
Cdd:PRK07769 309 KGLLNGSEPVSPASMRKFNEAFApyglppTAIKPSYGMAEATlfvsttpmdeepTVIYVDR--DELNAGRfvEVPADAPN 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 252 IVG-----------------------------GELWVRGPQLCSGYLGAP------------GPLVEG----------WL 280
Cdd:PRK07769 387 AVAqvsagkvgvsewavivdpetaselpdgqiGEIWLHGNNIGTGYWGKPeetaatfqnilkSRLSEShaegapddalWV 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 281 PTGDLVAPTpDGGLRVTGRTKEIIKYRGYQVSPAELE-EVIAACPGVRDVAVARGTLQGEEVPHAFVVGTAA-----PAE 354
Cdd:PRK07769 467 RTGDYGVYF-DGELYITGRVKDLVIIDGRNHYPQDLEyTAQEATKALRTGYVAAFSVPANQLPQVVFDDSHAglkfdPED 545
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2713532039 355 VHEW---VARRVAPYKK---------------------VRRVTVVE--SIPRAATGKILRRRLR 392
Cdd:PRK07769 546 TSEQlviVAERAPGAHKldpqpiaddiraaiavrhgvtVRDVLLVPagSIPRTSSGKIARRACR 609
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
62-397 |
3.90e-08 |
|
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: 55.12 E-value: 3.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 62 PATEDPEATAVLAL--SSGTTAEPKPVMLSHralSANIRQTVSALRGNGLDPGWSVLAPLPLSHIYGLNVLLHSSLANGN 139
Cdd:cd05939 96 PSQDDVNFRDKLFYiyTSGTTGLPKAAVIVH---SRYYRIAAGAYYAFGMRPEDVVYDCLPLYHSAGGIMGVGQALLHGS 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 140 HVVLMPRFTPRAFARLHAEHRIGWSYVAPPIVAALdsedYSADYSAEDFRHtRVMLSGAADLSPDLARRVGERLGV-EII 218
Cdd:cd05939 173 TVVIRKKFSASNFWDDCVKYNCTIVQYIGEICRYL----LAQPPSEEEQKH-NVRLAVGNGLRPQIWEQFVRRFGIpQIG 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 219 QGYGMTE--ASPVTHMMRRGdplGIG---------RPVDGTETRIVGGELwVRGP----QLCSGylGAPGPLV------- 276
Cdd:cd05939 248 EFYGATEgnSSLVNIDNHVG---ACGfnsrilpsvYPIRLIKVDEDTGEL-IRDSdglcIPCQP--GEPGLLVgkiiqnd 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 277 -----EGWLP---------------------TGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVA 330
Cdd:cd05939 322 plrrfDGYVNegatnkkiardvfkkgdsaflSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVV 401
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2713532039 331 VargtlQGEEVPHA-FVVGTAAPAEVHEWV---------ARRVAPYKKVRRVTVVESIPRAATGKILRRRLRERAGD 397
Cdd:cd05939 402 V-----YGVEVPGVeGRAGMAAIVDPERKVdldrfsavlAKSLPPYARPQFIRLLPEVDKTGTFKLQKTDLQKEGYD 473
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
206-392 |
1.02e-07 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 53.80 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 206 ARRVGERLGVEIIQGYGMTEAS-PVTHMMRRGDPLGI-----GRPVDGTETRIV----GGELwvrGPQLcSGYLGAPGPL 275
Cdd:PRK10524 372 ASWISEALGVPVIDNYWQTETGwPILAIARGVEDRPTrlgspGVPMYGYNVKLLnevtGEPC---GPNE-KGVLVIEGPL 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 276 VEGWLPT--GD--------------LVAPTPDGGLR-------VTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAV- 331
Cdd:PRK10524 448 PPGCMQTvwGDddrfvktywslfgrQVYSTFDWGIRdadgyyfILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVv 527
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2713532039 332 -ARGTLQGeEVPHAFVV-----GTAAP-------AEVHEWVARRVAPYKKVRRVTVVESIPRAATGKILRRRLR 392
Cdd:PRK10524 528 gVKDALKG-QVAVAFVVpkdsdSLADRearlaleKEIMALVDSQLGAVARPARVWFVSALPKTRSGKLLRRAIQ 600
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
77-391 |
1.60e-07 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 52.98 E-value: 1.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 77 SGTTAEPKPVMLSHRALsanirqtVS----ALRGNGLDPGWSVLAPLPLShiYGLNVL-LHSSLANGNHVVLMPRFTPRA 151
Cdd:PRK04813 152 SGTTGKPKGVQISHDNL-------VSftnwMLEDFALPEGPQFLNQAPYS--FDLSVMdLYPTLASGGTLVALPKDMTAN 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 152 FARLHAE---HRIG-WsyVAPPIVA--ALDSEDYSADYSAEdfrHTRVMLSGAAdlspdLARRVGERLgVE------IIQ 219
Cdd:PRK04813 223 FKQLFETlpqLPINvW--VSTPSFAdmCLLDPSFNEEHLPN---LTHFLFCGEE-----LPHKTAKKL-LErfpsatIYN 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 220 GYGMTEAS------PVT-HMMRRGDPLGIGRPVDGTETRIVG-----------GELWVRGPQLCSGYLGAPGPL------ 275
Cdd:PRK04813 292 TYGPTEATvavtsiEITdEMLDQYKRLPIGYAKPDSPLLIIDeegtklpdgeqGEIVISGPSVSKGYLNNPEKTaeafft 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 276 VEGwLP---TGDLvAPTPDGGLRVTGRTKEIIKYRGYQVspaELEEV---IAACPGVRdVAVARGTLQGEEVPH--AFVV 347
Cdd:PRK04813 372 FDG-QPayhTGDA-GYLEDGLLFYQGRIDFQIKLNGYRI---ELEEIeqnLRQSSYVE-SAVVVPYNKDHKVQYliAYVV 445
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 2713532039 348 GT--------AAPAEVHEWVARRVAPYKKVRRVTVVESIPRAATGKILRRRL 391
Cdd:PRK04813 446 PKeedferefELTKAIKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
54-395 |
6.57e-07 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 51.44 E-value: 6.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 54 ASRPLSPSPATEDPEATAVLALSSGTTAEPKPVMLSHRALSANIrqtvSALRGN-GLDPGWSVLAPLPLshiyglnVLLH 132
Cdd:PRK09274 160 DGAAAPFPMADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQI----EALREDyGIEPGEIDLPTFPL-------FALF 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 133 SsLANGNHVVLmPRFTPR--AFA---RLHA---EHRIGWSYVAPPIVAALdsedysADYsAEDFRHT-----RVmLSGAA 199
Cdd:PRK09274 229 G-PALGMTSVI-PDMDPTrpATVdpaKLFAaieRYGVTNLFGSPALLERL------GRY-GEANGIKlpslrRV-ISAGA 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 200 DLSPDLARRVGERL--GVEIIQGYGMTEASPV------------THMMRRGDPLGIGRPVDGTETRIVG----------- 254
Cdd:PRK09274 299 PVPIAVIERFRAMLppDAEILTPYGATEALPIssiesreilfatRAATDNGAGICVGRPVDGVEVRIIAisdapipewdd 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 255 ---------GELWVRGPQLCSGYLGAP---------GPLVEGWLPTGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAEL 316
Cdd:PRK09274 379 alrlatgeiGEIVVAGPMVTRSYYNRPeatrlakipDGQGDVWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPC 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 317 EEVIAACPGVRDVAVARGTLQGEEVPhafvvgtaapaevhewvarrvapykkvrrVTVVESIPRAATGK-ILRRRLRERA 395
Cdd:PRK09274 459 ERIFNTHPGVKRSALVGVGVPGAQRP-----------------------------VLCVELEPGVACSKsALYQELRALA 509
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
9-393 |
1.10e-06 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 50.64 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 9 GILGAGATVVplnplltEEETRRAVQRTGARLRIDAP-------------TARALHAGASRPLSPSPATED---PEATAV 72
Cdd:PRK08279 131 NLVDAKHLIV-------GEELVEAFEEARADLARPPRlwvaggdtlddpeGYEDLAAAAAGAPTTNPASRSgvtAKDTAF 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 73 LALSSGTTAEPKPVMLSH-RALsanirqtvSALRG----NGLDPGWSVLAPLPLSHIYGLNVLLHSSLANGNHVVLMPRF 147
Cdd:PRK08279 204 YIYTSGTTGLPKAAVMSHmRWL--------KAMGGfgglLRLTPDDVLYCCLPLYHNTGGTVAWSSVLAAGATLALRRKF 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 148 TPRAFARLHAEHRI-GWSYV---------APPivaaldsedysadySAEDFRHT-RVMLsgAADLSPDLARRVGERLGVE 216
Cdd:PRK08279 276 SASRFWDDVRRYRAtAFQYIgelcryllnQPP--------------KPTDRDHRlRLMI--GNGLRPDIWDEFQQRFGIP 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 217 -IIQGYGMTEASpVTHMMRRGDPLGIGR--PVDGTETRIV----GGELWVRGPQ------------LCSGYLGAPGPLvE 277
Cdd:PRK08279 340 rILEFYAASEGN-VGFINVFNFDGTVGRvpLWLAHPYAIVkydvDTGEPVRDADgrcikvkpgevgLLIGRITDRGPF-D 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 278 G---------------------WLPTGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAVargtl 336
Cdd:PRK08279 418 GytdpeasekkilrdvfkkgdaWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENALSGFPGVEEAVV----- 492
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2713532039 337 QGEEVPH--------AFVVGTAA---PAEVHEWVARRVAPYKKVRRVTVVESIPRAATGKILRRRLRE 393
Cdd:PRK08279 493 YGVEVPGtdgragmaAIVLADGAefdLAALAAHLYERLPAYAVPLFVRLVPELETTGTFKYRKVDLRK 560
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
291-395 |
1.56e-06 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 50.14 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 291 DGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAVA------RGtlqgeEVPHAFVV--GTAAP-----AEVHE 357
Cdd:PRK00174 496 DGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVgrpddiKG-----QGIYAFVTlkGGEEPsdelrKELRN 570
|
90 100 110
....*....|....*....|....*....|....*...
gi 2713532039 358 WVARRVAPYKKVRRVTVVESIPRAATGKILRRRLRERA 395
Cdd:PRK00174 571 WVRKEIGPIAKPDVIQFAPGLPKTRSGKIMRRILRKIA 608
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
192-388 |
5.85e-06 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 48.22 E-value: 5.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 192 RVMLSGAADLSPDLARRVGERLGVEIIQGYGMTEASPVTHMM---RRG-------------DPlGIGRPV-DGTEtrivg 254
Cdd:COG1541 206 KKGIFGGEPWSEEMRKEIEERWGIKAYDIYGLTEVGPGVAYEceaQDGlhiwedhflveiiDP-ETGEPVpEGEE----- 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 255 GELwvrgpqlcsgylgapgplV------EGwLP-----TGDLVAPTPDG---G------LRVTGRTKEIIKYRGYQVSPA 314
Cdd:COG1541 280 GEL------------------VvttltkEA-MPliryrTGDLTRLLPEPcpcGrthpriGRILGRADDMLIIRGVNVFPS 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 315 ELEEVIAACPGVRDVAVARGTLQGEEVPHAFVVGTAAPAEVHEW---VARRVAPYKKVR-RVTVVE--SIPRaATGKILR 388
Cdd:COG1541 341 QIEEVLLRIPEVGPEYQIVVDREGGLDELTVRVELAPGASLEALaeaIAAALKAVLGLRaEVELVEpgSLPR-SEGKAKR 419
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
62-272 |
6.79e-05 |
|
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: 44.76 E-value: 6.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 62 PATEDPeatAVLALSSGTTAEPKPVMLSHRALSANIrqtvSALRGN-GLDPGWSVLAPLPLSHIYGLNVLLHSSLANGNH 140
Cdd:cd05910 82 PKADEP---AAILFTSGSTGTPKGVVYRHGTFAAQI----DALRQLyGIRPGEVDLATFPLFALFGPALGLTSVIPDMDP 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 141 vvLMP-RFTPRAFARLHAEHRIGWSYVAPPIVAALdsedysADYSAED---FRHTRVMLSGAADLSPDLARRVGERL--G 214
Cdd:cd05910 155 --TRPaRADPQKLVGAIRQYGVSIVFGSPALLERV------ARYCAQHgitLPSLRRVLSAGAPVPIALAARLRKMLsdE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 215 VEIIQGYGMTEASPV------------THMMRRGDPLGIGRPVDGTETRIVG--------------------GELWVRGP 262
Cdd:cd05910 227 AEILTPYGATEALPVssigsrellattTAATSGGAGTCVGRPIPGVRVRIIEiddepiaewddtlelprgeiGEITVTGP 306
|
250
....*....|
gi 2713532039 263 QLCSGYLGAP 272
Cdd:cd05910 307 TVTPTYVNRP 316
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
283-394 |
1.05e-04 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 44.30 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 283 GDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEViaaCPGVRD-----VAVARGTLQG--EEVPHAFVVGTAAPAEV 355
Cdd:PLN03052 594 GDIFERTSGGYYRAHGRADDTMNLGGIKVSSVEIERV---CNAADEsvletAAIGVPPPGGgpEQLVIAAVLKDPPGSNP 670
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2713532039 356 ---------HEWVARRVAPYKKVRRVTVVESIPRAATGKILRRRLRER 394
Cdd:PLN03052 671 dlnelkkifNSAIQKKLNPLFKVSAVVIVPSFPRTASNKVMRRVLRQQ 718
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
8-227 |
3.03e-04 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 42.66 E-value: 3.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 8 HGILGAGATVVPLNPLLTE--EETRRAVQRTGARLRIDAPTA---------RALHAGASRPLSPS-PATEDPEATAVLAL 75
Cdd:cd05938 72 HCFRCCGAKVLVVAPELQEavEEVLPALRADGVSVWYLSHTSntegvisllDKVDAASDEPVPASlRAHVTIKSPALYIY 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 76 SSGTTAEPKPVMLSH-RALSANIRQTVSALRGNGLdpgwsVLAPLPLSHIYGLNVLLHSSLANGNHVVLMPRFTPRAFAR 154
Cdd:cd05938 152 TSGTTGLPKAARISHlRVLQCSGFLSLCGVTADDV-----IYITLPLYHSSGFLLGIGGCIELGATCVLKPKFSASQFWD 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 155 LHAEHRIG-WSYVA---------PPivaaldsedysadySAEDfRHTRVMLSGAADLSPDLARRVGERLG-VEIIQGYGM 223
Cdd:cd05938 227 DCRKHNVTvIQYIGellrylcnqPQ--------------SPND-RDHKVRLAIGNGLRADVWREFLRRFGpIRIREFYGS 291
|
....
gi 2713532039 224 TEAS 227
Cdd:cd05938 292 TEGN 295
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
283-387 |
1.09e-03 |
|
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: 41.10 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 283 GDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRD-VAVARGTLQGEEVPHAFVV---GTAAPAEVHEW 358
Cdd:cd05943 489 GDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDsLVVGQEWKDGDERVILFVKlreGVELDDELRKR 568
|
90 100 110
....*....|....*....|....*....|...
gi 2713532039 359 VARRVAPYKKVR----RVTVVESIPRAATGKIL 387
Cdd:cd05943 569 IRSTIRSALSPRhvpaKIIAVPDIPRTLSGKKV 601
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
278-395 |
3.12e-03 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 39.88 E-value: 3.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713532039 278 GWLPTGDLVAPTPDGGLRVTGRTKEIIKYRGYQVSPAELEEVIAACPGVRDVAVA--RGTLQGEEVpHAFVV---GTAAP 352
Cdd:PLN02654 513 GYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVgiEHEVKGQGI-YAFVTlveGVPYS 591
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2713532039 353 AEVHE----WVARRVAPYKKVRRVTVVESIPRAATGKILRRRLRERA 395
Cdd:PLN02654 592 EELRKslilTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKIA 638
|
|
| |
