|
Name |
Accession |
Description |
Interval |
E-value |
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
75-659 |
3.69e-176 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 513.51 E-value: 3.69e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 75 KWFIGGKLNIYNNCIERNiARGLGSKVCVCYEHESGKKRAITFWQLKLLVDTIASAMKAHGIGKGDFVGMCMPISIDSIA 154
Cdd:COG0365 1 RWFVGGRLNIAYNCLDRH-AEGRGDKVALIWEGEDGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 155 VMFACFKIGAVCMqmapTTSTD-GTKDIVDHVRIARAKMFFMADSYSYGGKNFTL-EKIHQGVSDIFSVRHIVVFENDAP 232
Cdd:COG0365 80 AMLACARIGAVHS----PVFPGfGAEALADRIEDAEAKVLITADGGLRGGKVIDLkEKVDEALEELPSLEHVIVVGRTGA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 233 HSPFSPFVFgkkemrsvfWDDFCKQgKSTIARTERCNAEDVALMLFSSGTTrekGKkPKRILHTHGGVLAQICKEVGFGF 312
Cdd:COG0365 156 DVPMEGDLD---------WDELLAA-ASAEFEPEPTDADDPLFILYTSGTT---GK-PKGVVHTHGGYLVHAATTAKYVL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 313 DCKEDDVFYWMTNFGWMMAPWEIV-GALHFGATLVCFEGAPSYPKPDRIFGIIERYKVSIFGSTPGFIAGLRKNHIS-GD 390
Cdd:COG0365 222 DLKPGDVFWCTADIGWATGHSYIVyGPLLNGATVVLYEGRPDFPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEpLK 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 391 DFNLSSLRILGSTGSILFSENWEWFFSVFGkgkCPINNIIGGTEMLGCFAQNLPNIPCKIGSVGVFALGMGGDIFNEKGE 470
Cdd:COG0365 302 KYDLSSLRLLGSAGEPLNPEVWEWWYEAVG---VPIVDGWGQTETGGIFISNLPGLPVKPGSMGKPVPGYDVAVVDEDGN 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 471 SVRR-ETGRVVCTHPFPSMTRGFYADEEGYQETYFSAFRGVWAHGDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIES 549
Cdd:COG0365 379 PVPPgEEGELVIKGPWPGMFRGYWNDPERYRETYFGRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIES 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 550 ALIGFRAaefrVMEAIAVGIPDKNSENKIICFVILEGQDRLTETDEAALRSVVADIVNPQAKPERIFAIKELPRNAAAKV 629
Cdd:COG0365 459 ALVSHPA----VAEAAVVGVPDEIRGQVVKAFVVLKPGVEPSDELAKELQAHVREELGPYAYPREIEFVDELPKTRSGKI 534
|
570 580 590
....*....|....*....|....*....|
gi 1277171962 630 PYKAISRVFCDRYVIAQTRVVNPQALEEIA 659
Cdd:COG0365 535 MRRLLRKIAEGRPLGDTSTLEDPEALDEIK 564
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
24-652 |
2.50e-142 |
|
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: 428.45 E-value: 2.50e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 24 MQRYEISSWQELLE-ASNDIEWFWPRAMEFLGVRWFTPYAKLYDDTEGISHTKWFIGGKLNIYNNCIERNIaRGLGSKVC 102
Cdd:cd05968 1 MASLGIPDLEAFLErSAEDNAWFWGEFVKDVGIEWYEPPYQTLDLSGGKPWAAWFVGGRMNIVEQLLDKWL-ADTRTRPA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 103 VCYEHESGKKRAITFWQLKLLVDTIASAMKAHGIGKGDFVGMCMPISIDSIAVMFACFKIGAVcmqMAPTTSTDGTKDIV 182
Cdd:cd05968 80 LRWEGEDGTSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGI---VVPIFSGFGKEAAA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 183 DHVRIARAKMFFMADSYSYGGKNFTL-EKIHQGVSDIFSVRHIVVFENDAPHSPFSPFvfgkkemRSVFWDDFCKqgkST 261
Cdd:cd05968 157 TRLQDAEAKALITADGFTRRGREVNLkEEADKACAQCPTVEKVVVVRHLGNDFTPAKG-------RDLSYDEEKE---TA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 262 IARTERCNAEDVALMLFSSGTTrekgKKPKRILHTHGGVLAQICKEVGFGFDCKEDDVFYWMTNFGWMMAPWEIVGALHF 341
Cdd:cd05968 227 GDGAERTESEDPLMIIYTSGTT----GKPKGTVHVHAGFPLKAAQDMYFQFDLKPGDLLTWFTDLGWMMGPWLIFGGLIL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 342 GATLVCFEGAPSYPKPDRIFGIIERYKVSIFGSTPGFIAGLRKnhiSGDDF----NLSSLRILGSTGSILFSENWEWFFS 417
Cdd:cd05968 303 GATMVLYDGAPDHPKADRLWRMVEDHEITHLGLSPTLIRALKP---RGDAPvnahDLSSLRVLGSTGEPWNPEPWNWLFE 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 418 VFGKGKCPINNIIGGTEMLGCFAQNLPNIPCKIGSVGVFALGMGGDIFNEKGESVRRETGRVVCTHPFPSMTRGFYADEE 497
Cdd:cd05968 380 TVGKGRNPIINYSGGTEISGGILGNVLIKPIKPSSFNGPVPGMKADVLDESGKPARPEVGELVLLAPWPGMTRGFWRDED 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 498 GYQETYFSAFRGVWAHGDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIESALIgfraAEFRVMEAIAVGIPDKNSENK 577
Cdd:cd05968 460 RYLETYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLN----AHPAVLESAAIGVPHPVKGEA 535
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1277171962 578 IICFVILEGQDRLTETDEAALRSVVADIVNPQAKPERIFAIKELPRNAAAKVPYKAISRVFCDRYVIAQTRVVNP 652
Cdd:cd05968 536 IVCFVVLKPGVTPTEALAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIRAAYLGKELGDLSSLENP 610
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
7-659 |
4.42e-129 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 395.70 E-value: 4.42e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 7 IWEPNEYFLNESRVARFMQRYE------ISSWQELLEAS-NDIEWFWPRAMEFLGVRWFTPYAKLYDDTEgISHTKWFIG 79
Cdd:PRK03584 5 LWTPSAERIAASRMTAFIRWLAarrglsFDDYAALWRWSvEDLEAFWQSVWDFFGVIGSTPYTVVLAGRR-MPGARWFPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 80 GKLNIynnciERNIAR-GLGSKVCVCYEHESGKKRAITFWQLKLLVDTIASAMKAHGIGKGDFVGMCMPISIDSIAVMFA 158
Cdd:PRK03584 84 ARLNY-----AENLLRhRRDDRPAIIFRGEDGPRRELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 159 CFKIGAV---CmqmapttSTD-GTKDIVDHVRIARAKMFFMADSYSYGGKNF-TLEKIHQGVSDIFSVRHIVVFENDAPH 233
Cdd:PRK03584 159 TASLGAIwssC-------SPDfGVQGVLDRFGQIEPKVLIAVDGYRYGGKAFdRRAKVAELRAALPSLEHVVVVPYLGPA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 234 SPFSPFVfgkkemRSVFWDDFCKQGKSTIARTERCNAEDVALMLFSSGTTrekGKkPKRILHTHGGVLAQICKEVGFGFD 313
Cdd:PRK03584 232 AAAAALP------GALLWEDFLAPAEAAELEFEPVPFDHPLWILYSSGTT---GL-PKCIVHGHGGILLEHLKELGLHCD 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 314 CKEDDVFYWMTNFGWMMAPWeIVGALHFGATLVCFEGAPSYPKPDRIFGIIERYKVSIFGSTPGFIAGLRKNHIS-GDDF 392
Cdd:PRK03584 302 LGPGDRFFWYTTCGWMMWNW-LVSGLLVGATLVLYDGSPFYPDPNVLWDLAAEEGVTVFGTSAKYLDACEKAGLVpGETH 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 393 NLSSLRILGSTGSILFSENWEWFFSVFGKGKCpINNIIGGTEMLGCFAQNLPNIPCKIGSVGVFALGMGGDIFNEKGESV 472
Cdd:PRK03584 381 DLSALRTIGSTGSPLPPEGFDWVYEHVKADVW-LASISGGTDICSCFVGGNPLLPVYRGEIQCRGLGMAVEAWDEDGRPV 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 473 RRETGRVVCTHPFPSMTRGFYADEEG--YQETYFSAFRGVWAHGDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIesa 550
Cdd:PRK03584 460 VGEVGELVCTKPFPSMPLGFWNDPDGsrYRDAYFDTFPGVWRHGDWIEITEHGGVVIYGRSDATLNRGGVRIGTAEI--- 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 551 ligFRAAEF--RVMEAIAVGIPDKNSENKIICFVIL-EGQDrLTETDEAALRSVVADIVNPQAKPERIFAIKELPRNAAA 627
Cdd:PRK03584 537 ---YRQVEAlpEVLDSLVIGQEWPDGDVRMPLFVVLaEGVT-LDDALRARIRTTIRTNLSPRHVPDKIIAVPDIPRTLSG 612
|
650 660 670
....*....|....*....|....*....|....*
gi 1277171962 628 KVPYKAISRVFCDR---YVIAQTRVVNPQALEEIA 659
Cdd:PRK03584 613 KKVELPVKKLLHGRpvkKAVNRDALANPEALDWFA 647
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
20-656 |
1.10e-128 |
|
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: 393.95 E-value: 1.10e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 20 VARFMQR------YEISSWQELLEAS-NDIEWFWPRAMEFLGVRWFTPYAKLYDDTEGISHTKWFIGGKLNIYNNCIERN 92
Cdd:cd05943 1 MDAFRRWvnarhgLSLADYAALHRWSvDDPGAFWAAVWDFSGVRGSKPYDVVVVSGRIMPGARWFPGARLNYAENLLRHA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 93 IARGLgskvCVCYEHESGKKRAITFWQLKLLVDTIASAMKAHGIGKGDFVGMCMPISIDSIAVMFACFKIGAVCMQMAPT 172
Cdd:cd05943 81 DADDP----AAIYAAEDGERTEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 173 TstdGTKDIVDHVRIARAKMFFMADSYSYGGKNFT-LEKIHQGVSDIFSVRHIVVF-------ENDAPHSPfspfvfgkk 244
Cdd:cd05943 157 F---GVPGVLDRFGQIEPKVLFAVDAYTYNGKRHDvREKVAELVKGLPSLLAVVVVpytvaagQPDLSKIA--------- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 245 emRSVFWDDFCKQGKSTIARTERCNAEDVALMLFSSGTTrekgKKPKRILHTHGGVLAQICKEVGFGFDCKEDDVFYWMT 324
Cdd:cd05943 225 --KALTLEDFLATGAAGELEFEPLPFDHPLYILYSSGTT----GLPKCIVHGAGGTLLQHLKEHILHCDLRPGDRLFYYT 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 325 NFGWMMAPWeIVGALHFGATLVCFEGAPSYPKPDRIFGIIERYKVSIFGSTPGFIAGLRKNHIS-GDDFNLSSLRILGST 403
Cdd:cd05943 299 TCGWMMWNW-LVSGLAVGATIVLYDGSPFYPDTNALWDLADEEGITVFGTSAKYLDALEKAGLKpAETHDLSSLRTILST 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 404 GSILFSENWEWFFSVFGKGkCPINNIIGGTEMLGCFAQNLPNIPCKIGSVGVFALGMGGDIFNEKGESVRRETGRVVCTH 483
Cdd:cd05943 378 GSPLKPESFDYVYDHIKPD-VLLASISGGTDIISCFVGGNPLLPVYRGEIQCRGLGMAVEAFDEEGKPVWGEKGELVCTK 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 484 PFPSMTRGFYADEEG--YQETYFSAFRGVWAHGDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIESALIGFraaeFRV 561
Cdd:cd05943 457 PFPSMPVGFWNDPDGsrYRAAYFAKYPGVWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKI----PEV 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 562 MEAIAVGIPDKNSENKIICFVILEGQDRLTETDEAALRSVVADIVNPQAKPERIFAIKELPRNAAAKVPYKAISRVFCDR 641
Cdd:cd05943 533 EDSLVVGQEWKDGDERVILFVKLREGVELDDELRKRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGKKVEVAVKKIIAGR 612
|
650
....*....|....*
gi 1277171962 642 YVIAQTRVVNPQALE 656
Cdd:cd05943 613 PVKNAGALANPESLD 627
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
38-629 |
6.14e-116 |
|
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: 359.58 E-value: 6.14e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 38 ASNDIEWFWPRAMEFLGVRWFTPYAKLYDDTEGISHTKWFIGGKLNIYNNCIERNIARGlGSKVCVCYEHESGKK-RAIT 116
Cdd:cd17634 8 SINDPDTFWGEAGKILDWITPYQKVKNTSFAPGAPSIKWFEDATLNLAANALDRHLREN-GDRTAIIYEGDDTSQsRTIS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 117 FWQLKLLVDTIASAMKAHGIGKGDFVGMCMPISIDSIAVMFACFKIGAVcmqMAPTTSTDGTKDIVDHVRIARAKMFFMA 196
Cdd:cd17634 87 YRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAV---HSVIFGGFAPEAVAGRIIDSSSRLLITA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 197 DSYSYGGKNFTLEKIhqgVSDIF-----SVRHIVVFenDAPHSPFspfvfGKKEMRSVFWDDFCKQgKSTIARTERCNAE 271
Cdd:cd17634 164 DGGVRAGRSVPLKKN---VDDALnpnvtSVEHVIVL--KRTGSDI-----DWQEGRDLWWRDLIAK-ASPEHQPEAMNAE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 272 DVALMLFSSGTTrekgKKPKRILHTHGGVLAQICKEVGFGFDCKEDDVFYWMTNFGWMMA-PWEIVGALHFGATLVCFEG 350
Cdd:cd17634 233 DPLFILYTSGTT----GKPKGVLHTTGGYLVYAATTMKYVFDYGPGDIYWCTADVGWVTGhSYLLYGPLACGATTLLYEG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 351 APSYPKPDRIFGIIERYKVSIFGSTPGFIAGLRKnhiSGDD----FNLSSLRILGSTGSILFSENWEWFFSVFGKGKCPI 426
Cdd:cd17634 309 VPNWPTPARMWQVVDKHGVNILYTAPTAIRALMA---AGDDaiegTDRSSLRILGSVGEPINPEAYEWYWKKIGKEKCPV 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 427 NNIIGGTEMLGCFAQNLPN-IPCKIGSVGVFALGMGGDIFNEKGESVRRET-GRVVCTHPFPSMTRGFYADEEGYQETYF 504
Cdd:cd17634 386 VDTWWQTETGGFMITPLPGaIELKAGSATRPVFGVQPAVVDNEGHPQPGGTeGNLVITDPWPGQTRTLFGDHERFEQTYF 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 505 SAFRGVWAHGDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIESALigfrAAEFRVMEAIAVGIPDKNSENKIICFVIL 584
Cdd:cd17634 466 STFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVL----VAHPKVAEAAVVGIPHAIKGQAPYAYVVL 541
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 1277171962 585 EGQDRLTETDEAALRSVVADIVNPQAKPERIFAIKELPRNAAAKV 629
Cdd:cd17634 542 NHGVEPSPELYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
31-629 |
9.44e-116 |
|
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: 359.57 E-value: 9.44e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 31 SWQELLEAS-NDIEWFW-PRAMEFlgvRWFTPYAKLYDDTEGISHTKWFIGGKLNIYNNCIERNIARgLGSKVCVCYEHE 108
Cdd:cd05966 2 QYKELYKQSiEDPEEFWgEIAKEL---DWFKPWDKVLDWSKGPPFIKWFEGGKLNISYNCLDRHLKE-RGDKVAIIWEGD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 109 SG-KKRAITFWQLKLLVDTIASAMKAHGIGKGDFVGMCMPISIDSIAVMFACFKIGAVCMQMAPTTSTDGTKD-IVDhvr 186
Cdd:cd05966 78 EPdQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFAGFSAESLADrIND--- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 187 iARAKMFFMADSYSYGGKNFTLEKI-HQGVSDIFSVRHIVVFENDAPHSPFspfvfgkKEMRSVFWDDFCKqGKSTIART 265
Cdd:cd05966 155 -AQCKLVITADGGYRGGKVIPLKEIvDEALEKCPSVEKVLVVKRTGGEVPM-------TEGRDLWWHDLMA-KQSPECEP 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 266 ERCNAEDVALMLFSSGTTrekGKkPKRILHTHGGVL---AQICKEVgfgFDCKEDDVFYWMTNFGWMMAPWEIV-GALHF 341
Cdd:cd05966 226 EWMDSEDPLFILYTSGST---GK-PKGVVHTTGGYLlyaATTFKYV---FDYHPDDIYWCTADIGWITGHSYIVyGPLAN 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 342 GATLVCFEGAPSYPKPDRIFGIIERYKVSIFGSTPGFIAGLRKnhiSGDDF----NLSSLRILGSTGSILFSENWEWFFS 417
Cdd:cd05966 299 GATTVMFEGTPTYPDPGRYWDIVEKHKVTIFYTAPTAIRALMK---FGDEWvkkhDLSSLRVLGSVGEPINPEAWMWYYE 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 418 VFGKGKCPINNIIGGTEMLGCFAQNLPN-IPCKIGSVGVFALGMGGDIFNEKGESVRRETGRVVC-THPFPSMTRGFYAD 495
Cdd:cd05966 376 VIGKERCPIVDTWWQTETGGIMITPLPGaTPLKPGSATRPFFGIEPAILDEEGNEVEGEVEGYLViKRPWPGMARTIYGD 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 496 EEGYQETYFSAFRGVWAHGDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIESALIgfraAEFRVMEAIAVGIPDKNSE 575
Cdd:cd05966 456 HERYEDTYFSKFPGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALV----AHPAVAEAAVVGRPHDIKG 531
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 1277171962 576 NKIICFVILEGQDRLTETDEAALRSVVADIVNPQAKPERIFAIKELPRNAAAKV 629
Cdd:cd05966 532 EAIYAFVTLKDGEEPSDELRKELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKI 585
|
|
| ac_ac_CoA_syn |
TIGR01217 |
acetoacetyl-CoA synthase; This enzyme catalyzes the first step of the mevalonate pathway of ... |
4-656 |
1.85e-101 |
|
acetoacetyl-CoA synthase; This enzyme catalyzes the first step of the mevalonate pathway of IPP biosynthesis. Most bacteria do not use this pathway, but rather the deoxyxylulose pathway. [Central intermediary metabolism, Other]
Pssm-ID: 273507 [Multi-domain] Cd Length: 652 Bit Score: 323.76 E-value: 1.85e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 4 EKYIWEPNEYFLNESRVARFM----QRYEIS--SWQELLEAS-NDIEWFWPRAMEFLGVRWFTPYAKLYDDTEGIShTKW 76
Cdd:TIGR01217 3 PQPLWQPDAQRIAQARMTRFQawagEHHGAAegGYDALHRWSvDELDTFWKAVWEWFDVRFSTPCARVVDDRTMPG-AQW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 77 FIGGKLNIYNNCIerniaRGLGSKVCVCYEHESGKKRAITFWQLKLLVDTIASAMKAHGIGKGDFVGMCMPISIDSIAVM 156
Cdd:TIGR01217 82 FPGARLNYAENLL-----RAAGTEPALLYVDETHEPAPVTWAELRRQVASLAAALRALGVRPGDRVSGYLPNIPQAVVAM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 157 FACFKIGAVCMQMAPTTstdGTKDIVDHVRIARAKMFFMADSYSYGGKNF-TLEKIHQGVSDIFSVRHIVVFENDAPHSP 235
Cdd:TIGR01217 157 LATASVGAIWSSCSPDF---GARGVLDRFQQIEPKLLFTVDGYRYNGKEHdRRDKVAEVRKELPTLRAVVHIPYLGPRET 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 236 FSPFVFGkkemrSVFWDDFCKQGKSTIARTERCNAEDVALMLFSSGTTrekgKKPKRILHTHGGVLAQICKEVGFGFDCK 315
Cdd:TIGR01217 234 EAPKIDG-----ALDLEDFTAAAQAAELVFEQLPFDHPLWILFSSGTT----GLPKCIVHSAGGTLVQHLKEHGLHCDLG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 316 EDDVFYWMTNFGWMMAPWeIVGALHFGATLVCFEGAPSYPKPDRIFGIIERYKVSIFGSTPGFIAGLRKNHIS-GDDFNL 394
Cdd:TIGR01217 305 PGDRLFYYTTTGWMMWNW-LVSGLATGATLVLYDGSPGFPATNVLWDIAERTGATLFGTSAKYVMACRKAGVHpARTHDL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 395 SSLRILGSTGSILFSENWEWFFSVFgKGKCPINNIIGGTEMLGCFAQNLPNIPCKIGSVGVFALGMGGDIFNEKGESVRR 474
Cdd:TIGR01217 384 SALQCVASTGSPLPPDGFRWVYDEI-KADVWLASISGGTDICSCFAGANPTLPVHIGEIQAPGLGTAVQSWDPEGKPVTG 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 475 ETGRVVCTHPFPSMTRGFYADEEG--YQETYFSAFRGVWAHGDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIESALI 552
Cdd:TIGR01217 463 EVGELVCTNPMPSMPIRFWNDPDGskYRDAYFDTYPGVWRHGDWITLTPRGGIVIHGRSDSTLNPQGVRMGSAEIYNAVE 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 553 GFRaaefRVMEAIAVGIPDKNSENKIICFVILEGQDRLTETDEAALRSVVADIVNPQAKPERIFAIKELPRNAAAKVPYK 632
Cdd:TIGR01217 543 RLD----EVRESLCIGQEQPDGGYRVVLFVHLAPGATLDDALLDRIKRTIRAGLSPRHVPDEIIEVPGIPHTLTGKRVEV 618
|
650 660
....*....|....*....|....
gi 1277171962 633 AISRVFCDRYVIAQTRVVNPQALE 656
Cdd:TIGR01217 619 AVKRVLQGTPVDNPGAIDNPELLD 642
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
37-622 |
1.96e-98 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 315.16 E-value: 1.96e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 37 EASNDIEWFWPRAMEFLgvRWFTPYAKLYDDteGISHTKWFIGGKLNIYNNCIERNIARGlGSKVCVCYEHESGKK-RAI 115
Cdd:PRK00174 25 ESVEDPEGFWAEQAKRL--DWFKPFDTVLDW--NAPFIKWFEDGELNVSYNCLDRHLKTR-GDKVAIIWEGDDPGDsRKI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 116 TFWQLKLLVDTIASAMKAHGIGKGDFVGMCMPISIDSIAVMFACFKIGAVcmqmapTT------STDGTKD-IVDhvriA 188
Cdd:PRK00174 100 TYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAV------HSvvfggfSAEALADrIID----A 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 189 RAKMFFMADSYSYGGKNFTLEKI-HQGVSDIFSVRHIVVFE---NDAPHspfspfvfgkKEMRSVFWDDFCKqGKSTIAR 264
Cdd:PRK00174 170 GAKLVITADEGVRGGKPIPLKANvDEALANCPSVEKVIVVRrtgGDVDW----------VEGRDLWWHELVA-GASDECE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 265 TERCNAEDVALMLFSSGTTrekGKkPKRILHTHGGVLAQIC---KEVgfgFDCKEDDVfYWMT-NFGWMMAPWEIV-GAL 339
Cdd:PRK00174 239 PEPMDAEDPLFILYTSGST---GK-PKGVLHTTGGYLVYAAmtmKYV---FDYKDGDV-YWCTaDVGWVTGHSYIVyGPL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 340 HFGATLVCFEGAPSYPKPDRIFGIIERYKVSIFGSTPGFIAGLRKnhiSGDDF----NLSSLRILGSTGSILFSENWEWF 415
Cdd:PRK00174 311 ANGATTLMFEGVPNYPDPGRFWEVIDKHKVTIFYTAPTAIRALMK---EGDEHpkkyDLSSLRLLGSVGEPINPEAWEWY 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 416 FSVFGKGKCPINNIIGGTEMLGCFAQNLPN-IPCKIGSV-----GVFAlgmggDIFNEKGESVRRET-GRVVCTHPFPSM 488
Cdd:PRK00174 388 YKVVGGERCPIVDTWWQTETGGIMITPLPGaTPLKPGSAtrplpGIQP-----AVVDEEGNPLEGGEgGNLVIKDPWPGM 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 489 TRGFYADEEGYQETYFSAFRGVWAHGDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIESALIGFRAaefrVMEAIAVG 568
Cdd:PRK00174 463 MRTIYGDHERFVKTYFSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPK----VAEAAVVG 538
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 1277171962 569 IPDKNSENKIICFVILEGQDRLTETDEAALRSVVADIVNPQAKPERIFAIKELP 622
Cdd:PRK00174 539 RPDDIKGQGIYAFVTLKGGEEPSDELRKELRNWVRKEIGPIAKPDVIQFAPGLP 592
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
2-629 |
1.66e-78 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 263.30 E-value: 1.66e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 2 ADEKYIWEPNEYFLNESRVARFMQryeissWQELLEAS-NDIEWFWPR-AMEFLGVRWFTP---YAKLYDDTEGISHTKW 76
Cdd:PLN02654 8 SEENDLVFPSKDFSAQALVSSPQQ------YMEMYKRSvDDPAGFWSDiASQFYWKQKWEGdevCSENLDVRKGPISIEW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 77 FIGGKLNIYNNCIERNIARGLGSKVCVCYE-HESGKKRAITFWQLKLLVDTIASAMKAHGIGKGDFVGMCMPISIDSIAV 155
Cdd:PLN02654 82 FKGGKTNICYNCLDRNVEAGNGDKIAIYWEgNEPGFDASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 156 MFACFKIGAV-CMQMAPTTSTDGTKDIVDhvriARAKMFFMADSYSYGGKNFTLEKI-----HQGVSDIFSVRHIVVFEN 229
Cdd:PLN02654 162 MLACARIGAVhSVVFAGFSAESLAQRIVD----CKPKVVITCNAVKRGPKTINLKDIvdaalDESAKNGVSVGICLTYEN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 230 D-APHSPFSPFvfgkKEMRSVFWDDFCKQgKSTIARTERCNAEDVALMLFSSGTTrekgKKPKRILHTHGGVLAQICKEV 308
Cdd:PLN02654 238 QlAMKREDTKW----QEGRDVWWQDVVPN-YPTKCEVEWVDAEDPLFLLYTSGST----GKPKGVLHTTGGYMVYTATTF 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 309 GFGFDCKEDDVFYWMTNFGWMMA-PWEIVGALHFGATLVCFEGAPSYPKPDRIFGIIERYKVSIFGSTPGFIAGLRKnhi 387
Cdd:PLN02654 309 KYAFDYKPTDVYWCTADCGWITGhSYVTYGPMLNGATVLVFEGAPNYPDSGRCWDIVDKYKVTIFYTAPTLVRSLMR--- 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 388 SGDDF----NLSSLRILGSTGSILFSENWEWFFSVFGKGKCPINNIIGGTEMLGCFAQNLPNI-PCKIGSVGVFALGMGG 462
Cdd:PLN02654 386 DGDEYvtrhSRKSLRVLGSVGEPINPSAWRWFFNVVGDSRCPISDTWWQTETGGFMITPLPGAwPQKPGSATFPFFGVQP 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 463 DIFNEKGESVRRETGRVVCTH-PFPSMTRGFYADEEGYQETYFSAFRGVWAHGDFAEMDEDGFVFMRGRSDDIINKNGIK 541
Cdd:PLN02654 466 VIVDEKGKEIEGECSGYLCVKkSWPGAFRTLYGDHERYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHR 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 542 FSPANIESALIgfraAEFRVMEAIAVGIPDKNSENKIICFVILEGQDRLTETDEAALRSVVADIVNPQAKPERIFAIKEL 621
Cdd:PLN02654 546 IGTAEVESALV----SHPQCAEAAVVGIEHEVKGQGIYAFVTLVEGVPYSEELRKSLILTVRNQIGAFAAPDKIHWAPGL 621
|
....*...
gi 1277171962 622 PRNAAAKV 629
Cdd:PLN02654 622 PKTRSGKI 629
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
38-658 |
1.03e-70 |
|
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: 241.07 E-value: 1.03e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 38 ASNDIEWFWPRAMEflGVRWFTPYAKLYDDTEGIShTKWFIGGKLNIYNNCIERNIARGLGSKVCVCYEH-ESGKKRAIT 116
Cdd:cd05967 8 SIAEPEAFWAEQAR--LIDWFKPPEKILDNSNPPF-TRWFVGGRLNTCYNALDRHVEAGRGDQIALIYDSpVTGTERTYT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 117 FWQLKLLVDTIASAMKAHGIGKGDFVGMCMPISIDSIAVMFACFKIGAVCMQM-----APTTSTDgtkdiVDHvriARAK 191
Cdd:cd05967 85 YAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVfggfaAKELASR-----IDD---AKPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 192 MFFMADSYSYGGKNFTLEKI-HQGVSD-IFSVRHIVVFenDAPHSPFSPFVFGkkemRSVFWDDFCKQgkstiARTERC- 268
Cdd:cd05967 157 LIVTASCGIEPGKVVPYKPLlDKALELsGHKPHHVLVL--NRPQVPADLTKPG----RDLDWSELLAK-----AEPVDCv 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 269 --NAEDVALMLFSSGTTrekgKKPKRILHTHGGVLAQICKEVGFGFDCKEDDVFYWMTNFGWMMAPWEIV-GALHFGATL 345
Cdd:cd05967 226 pvAATDPLYILYTSGTT----GKPKGVVRDNGGHAVALNWSMRNIYGIKPGDVWWAASDVGWVVGHSYIVyGPLLHGATT 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 346 VCFEGAP-SYPKPDRIFGIIERYKVSIFGSTPGFIAGLRKNHISGD---DFNLSSLRILGSTGSILFSENWEWFFSVFGK 421
Cdd:cd05967 302 VLYEGKPvGTPDPGAFWRVIEKYQVNALFTAPTAIRAIRKEDPDGKyikKYDLSSLRTLFLAGERLDPPTLEWAENTLGV 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 422 gkcPINNIIGGTEMLGCFAQN---LPNIPCKIGSVGVFALGMGGDIFNEKGESVR-RETGRVVCTHPF-PSMTRGFYADE 496
Cdd:cd05967 382 ---PVIDHWWQTETGWPITANpvgLEPLPIKAGSPGKPVPGYQVQVLDEDGEPVGpNELGNIVIKLPLpPGCLLTLWKND 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 497 EGYQETYFSAFRGVWAHGDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIESALIGFRAaefrVMEAIAVGIPDKNSEN 576
Cdd:cd05967 459 ERFKKLYLSKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPA----VAECAVVGVRDELKGQ 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 577 KIICFVILEGQDRLTETD-EAALRSVVADIVNPQAKPERIFAIKELPRNAAAKVPYKAIsRVFCD--RYVIAQTrVVNPQ 653
Cdd:cd05967 535 VPLGLVVLKEGVKITAEElEKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTL-RKIADgeDYTIPST-IEDPS 612
|
....*
gi 1277171962 654 ALEEI 658
Cdd:cd05967 613 VLDEI 617
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
113-634 |
4.61e-61 |
|
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: 210.82 E-value: 4.61e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 113 RAITFWQLKLLVDTIASAMKAHGIGKGDFVGMCMPISIDSIAVMFACFKIGAVCMQMAPTTSTDGTKDIVDHvriARAKM 192
Cdd:COG0318 23 RRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEELAYILED---SGARA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 193 FFmadsysyggknftlekihqgvsdifsvrhivvfendaphspfspfvfgkkemrsvfwddfckqgkstiartercnaed 272
Cdd:COG0318 100 LV------------------------------------------------------------------------------ 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 273 VALMLFSSGTTRekgkKPKRILHTHGGVLA---QICKEVGFGfdckEDDVFYWMT----NFGWMMAPWeivGALHFGATL 345
Cdd:COG0318 102 TALILYTSGTTG----RPKGVMLTHRNLLAnaaAIAAALGLT----PGDVVLVALplfhVFGLTVGLL---APLLAGATL 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 346 VCfegaPSYPKPDRIFGIIERYKVSIFGSTPGFIAGLRkNHISGDDFNLSSLRILGSTGSILFSENWEWFFSVFGkgkCP 425
Cdd:COG0318 171 VL----LPRFDPERVLELIERERVTVLFGVPTMLARLL-RHPEFARYDLSSLRLVVSGGAPLPPELLERFEERFG---VR 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 426 INNIIGGTEMLGCFAQNLPNI-PCKIGSVGVFALGMGGDIFNEKGESV-RRETGRVVCTHPfpSMTRGFYADEEGYQEty 503
Cdd:COG0318 243 IVEGYGLTETSPVVTVNPEDPgERRPGSVGRPLPGVEVRIVDEDGRELpPGEVGEIVVRGP--NVMKGYWNDPEATAE-- 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 504 fsAFRGVWAH-GDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIESALigfrAAEFRVMEAIAVGIPDKNSENKIICFV 582
Cdd:COG0318 319 --AFRDGWLRtGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVL----AAHPGVAEAAVVGVPDEKWGERVVAFV 392
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1277171962 583 ILEGQDRLtetDEAALRSVVADIVNPQAKPERIFAIKELPRNAAAKVPYKAI 634
Cdd:COG0318 393 VLRPGAEL---DAEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRAL 441
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
272-629 |
1.04e-58 |
|
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: 200.97 E-value: 1.04e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 272 DVALMLFSSGTTrekgKKPKRILHTHGGVLAQICKeVGFGFDCKEDDVFYWMTNFGWMMAPWEIVGALHFGATLVCFEGa 351
Cdd:cd04433 1 DPALILYTSGTT----GKPKGVVLSHRNLLAAAAA-LAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPK- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 352 psyPKPDRIFGIIERYKVSIFGSTPGFIAGLRKnHISGDDFNLSSLRILGSTGSILFSENWEWFFSVFGkgkCPINNIIG 431
Cdd:cd04433 75 ---FDPEAALELIEREKVTILLGVPTLLARLLK-APESAGYDLSSLRALVSGGAPLPPELLERFEEAPG---IKLVNGYG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 432 GTEMLGCFAQNLP-NIPCKIGSVGVFALGMGGDIFNEKGESVR-RETGRVVCTHPfpSMTRGFYADEEgyqETYFSAFRG 509
Cdd:cd04433 148 LTETGGTVATGPPdDDARKPGSVGRPVPGVEVRIVDPDGGELPpGEIGELVVRGP--SVMKGYWNNPE---ATAAVDEDG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 510 VWAHGDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIESALIGFRAaefrVMEAIAVGIPDKNSENKIICFVILEGQDR 589
Cdd:cd04433 223 WYRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPG----VAEAAVVGVPDPEWGERVVAVVVLRPGAD 298
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1277171962 590 LtetDEAALRSVVADIVNPQAKPERIFAIKELPRNAAAKV 629
Cdd:cd04433 299 L---DAEELRAHVRERLAPYKVPRRVVFVDALPRTASGKI 335
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
94-536 |
1.90e-57 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 200.23 E-value: 1.90e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 94 ARGLGSKVCVcyehESGKKRAITFWQLKLLVDTIASAMKAHGIGKGDFVGMCMPISIDSIAVMFACFKIGAVCMQMAPTT 173
Cdd:pfam00501 5 AARTPDKTAL----EVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 174 STDGTKDIVDHvriARAKMFFMADsysyggkNFTLEKIHQGVSDIFSVRHIVVFENDAPhspfspfvfgkKEMRSVFWDD 253
Cdd:pfam00501 81 PAEELAYILED---SGAKVLITDD-------ALKLEELLEALGKLEVVKLVLVLDRDPV-----------LKEEPLPEEA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 254 FCKqgKSTIARTERCNAEDVALMLFSSGTTrekGkKPKRILHTHGGVLAQI-----CKEVGFGFDckEDDVFYWMTNFGW 328
Cdd:pfam00501 140 KPA--DVPPPPPPPPDPDDLAYIIYTSGTT---G-KPKGVMLTHRNLVANVlsikrVRPRGFGLG--PDDRVLSTLPLFH 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 329 MMA-PWEIVGALHFGATLVCFEGAPSyPKPDRIFGIIERYKVSIFGSTPGFIAGLRkNHISGDDFNLSSLRILGSTGSIL 407
Cdd:pfam00501 212 DFGlSLGLLGPLLAGATVVLPPGFPA-LDPAALLELIERYKVTVLYGVPTLLNMLL-EAGAPKRALLSSLRLVLSGGAPL 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 408 FSENWEWFFSVFGkgkCPINNIIGGTEMLGCFAQNLPNIPC--KIGSVGVFALGMGGDIFNEK-GESVRR-ETGRVVCTH 483
Cdd:pfam00501 290 PPELARRFRELFG---GALVNGYGLTETTGVVTTPLPLDEDlrSLGSVGRPLPGTEVKIVDDEtGEPVPPgEPGELCVRG 366
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1277171962 484 pfPSMTRGFYADEEGYQETYFSafrGVWAH-GDFAEMDEDGFVFMRGRSDDIIN 536
Cdd:pfam00501 367 --PGVMKGYLNDPELTAEAFDE---DGWYRtGDLGRRDEDGYLEIVGRKKDQIK 415
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
116-629 |
7.05e-52 |
|
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: 185.23 E-value: 7.05e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 116 TFWQLKLLVDTIASAMKAHGIGKGDFVGMCMPISIDSIAVMFACFKIGAVcmqMAPTTSTDGTKDIVDHVRIARAKMffm 195
Cdd:cd05972 2 SFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAV---YVPLTTLLGPKDIEYRLEAAGAKA--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 196 adsysyggknftlekihqgvsdifsvrhIVvfendaphspfspfvfgkkemrsvfwddfckqgkstiarterCNAEDVAL 275
Cdd:cd05972 76 ----------------------------IV------------------------------------------TDAEDPAL 85
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 276 MLFSSGTTrekgKKPKRILHTHGGVLAQIcKEVGFGFDCKEDDVFYWMTNFGWMMAPW-EIVGALHFGATLVCFEGAPSy 354
Cdd:cd05972 86 IYFTSGTT----GLPKGVLHTHSYPLGHI-PTAAYWLGLRPDDIHWNIADPGWAKGAWsSFFGPWLLGATVFVYEGPRF- 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 355 pKPDRIFGIIERYKVSIFGSTPGFIAGLRKNHISGddFNLSSLRILGSTGSILFSENWEWFFSVFGKgkcPINNIIGGTE 434
Cdd:cd05972 160 -DAERILELLERYGVTSFCGPPTAYRMLIKQDLSS--YKFSHLRLVVSAGEPLNPEVIEWWRAATGL---PIRDGYGQTE 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 435 ---MLGcfaqNLPNIPCKIGSVGVFALGMGGDIFNEKGESVRR-ETGRVVCTHPFPSMTRGFYADEEGYQETyfsaFRGV 510
Cdd:cd05972 234 tglTVG----NFPDMPVKPGSMGRPTPGYDVAIIDDDGRELPPgEEGDIAIKLPPPGLFLGYVGDPEKTEAS----IRGD 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 511 WAH-GDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIESALIGFRAaefrVMEAIAVGIPDKNSENKIICFVIL----E 585
Cdd:cd05972 306 YYLtGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPA----VAEAAVVGSPDPVRGEVVKAFVVLtsgyE 381
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1277171962 586 GQDRLTETdeaaLRSVVADIVNPQAKPERIFAIKELPRNAAAKV 629
Cdd:cd05972 382 PSEELAEE----LQGHVKKVLAPYKYPREIEFVEELPKTISGKI 421
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
116-629 |
1.17e-50 |
|
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: 182.32 E-value: 1.17e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 116 TFWQLKLLVDTIASAMKAHGIGKGDFVGMCMPISIDSIAVMFACFKIGAVcmqMAPTTSTDGTKDIVDHVRIARAKMFFm 195
Cdd:cd05969 2 TFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAV---ICPLFSAFGPEAIRDRLENSEAKVLI- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 196 adsysyggknfTLEKIHqgvsdifsvrhivvfendaphspfspfvfgkkemrsvfwddfckqgkstiartERCNAEDVAL 275
Cdd:cd05969 78 -----------TTEELY-----------------------------------------------------ERTDPEDPTL 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 276 MLFSSGTTrekgKKPKRILHTHGGVLAQ--ICKEVgfgFDCKEDDVFYWMTNFGW-------MMAPWeivgaLHfGATLV 346
Cdd:cd05969 94 LHYTSGTT----GTPKGVLHVHDAMIFYyfTGKYV---LDLHPDDIYWCTADPGWvtgtvygIWAPW-----LN-GVTNV 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 347 CFEGAPSypkPDRIFGIIERYKVSIFGSTPGFIAGLRKnhiSGDD----FNLSSLRILGSTGSILFSENWEWFFSVFGKg 422
Cdd:cd05969 161 VYEGRFD---AESWYGIIERVKVTVWYTAPTAIRMLMK---EGDElarkYDLSSLRFIHSVGEPLNPEAIRWGMEVFGV- 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 423 kcPINNIIGGTEMLGCFAQNLPNIPCKIGSVGVFALGMGGDIFNEKGESVRRETGRVVCTHP-FPSMTRGFYADEEGYQE 501
Cdd:cd05969 234 --PIHDTWWQTETGSIMIANYPCMPIKPGSMGKPLPGVKAAVVDENGNELPPGTKGILALKPgWPSMFRGIWNDEERYKN 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 502 TYFSafrGVWAHGDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIESALIGFRAaefrVMEAIAVGIPDKNSENKIICF 581
Cdd:cd05969 312 SFID---GWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPA----VAEAGVIGKPDPLRGEIIKAF 384
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1277171962 582 VILEGQDRLTETDEAALRSVVADIVNPQAKPERIFAIKELPRNAAAKV 629
Cdd:cd05969 385 ISLKEGFEPSDELKEEIINFVRQKLGAHVAPREIEFVDNLPKTRSGKI 432
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
113-629 |
4.47e-50 |
|
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: 181.64 E-value: 4.47e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 113 RAITFWQLKLLVDTIASAMKAHGIGKGDFVGMCMPISIDSIAVMFACFKIGAVCMqMAPTTSTDGTkdIVDHVRIARAKM 192
Cdd:cd05911 9 KELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFS-AANPIYTADE--LAHQLKISKPKV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 193 FFMAdsysyggkNFTLEKIHQGVSDIFSVRHIVVFeNDAPHSPFSPfvfgkkemrSVFWDDFCKQGKSTIARTERCNAED 272
Cdd:cd05911 86 IFTD--------PDGLEKVKEAAKELGPKDKIIVL-DDKPDGVLSI---------EDLLSPTLGEEDEDLPPPLKDGKDD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 273 VALMLFSSGTTrekGkKPKRILHTHGGVLAQICKEVGFGFDCKE-DDVFYWMTNFGWMMAPWEIVGALHFGATLV---CF 348
Cdd:cd05911 148 TAAILYSSGTT---G-LPKGVCLSHRNLIANLSQVQTFLYGNDGsNDVILGFLPLYHIYGLFTTLASLLNGATVIimpKF 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 349 EgapsypkPDRIFGIIERYKVSIFGSTPGFIAGLRKNHISgDDFNLSSLRILGSTGSILFSENWEWFFSVFgkGKCPINN 428
Cdd:cd05911 224 D-------SELFLDLIEKYKITFLYLVPPIAAALAKSPLL-DKYDLSSLRVILSGGAPLSKELQELLAKRF--PNATIKQ 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 429 IIGGTEMLGCFAQNlPNIPCKIGSVGVFALGMGGDIFNEKGESV--RRETGRvVCTHpFPSMTRGFYADEEGYQETYFSa 506
Cdd:cd05911 294 GYGMTETGGILTVN-PDGDDKPGSVGRLLPNVEAKIVDDDGKDSlgPNEPGE-ICVR-GPQVMKGYYNNPEATKETFDE- 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 507 frGVWAH-GDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIESALigfraAEF-RVMEAIAVGIPDKNSENKIICFVIL 584
Cdd:cd05911 370 --DGWLHtGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVL-----LEHpGVADAAVIGIPDEVSGELPRAYVVR 442
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1277171962 585 EGQDRLTETDeaalrsvVADIVNPQ---AKPER--IFAIKELPRNAAAKV 629
Cdd:cd05911 443 KPGEKLTEKE-------VKDYVAKKvasYKQLRggVVFVDEIPKSASGKI 485
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
76-592 |
5.24e-49 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 180.48 E-value: 5.24e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 76 WFIGGKLNIYNNCIERNIARGLGSKVCVCYEHESGKkRAITFWQLKLLVDTIASAMKAHGIGKGDFVGMCMPISIDSIAV 155
Cdd:PRK04319 36 WLETGKVNIAYEAIDRHADGGRKDKVALRYLDASRK-EKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 156 MFACFKIGAVcmqMAPTTSTDGTKDIVDHVRIARAKMFFMADSysyggknfTLEKIhqGVSDIFSVRHIVVFENDAPHSP 235
Cdd:PRK04319 115 LLGALKNGAI---VGPLFEAFMEEAVRDRLEDSEAKVLITTPA--------LLERK--PADDLPSLKHVLLVGEDVEEGP 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 236 fsPFVFGKKEMRSVfwddfckqgkSTIARTERCNAEDVALMLFSSGTTrekgKKPKRILHTHGGVLA--QICKEVgfgFD 313
Cdd:PRK04319 182 --GTLDFNALMEQA----------SDEFDIEWTDREDGAILHYTSGST----GKPKGVLHVHNAMLQhyQTGKYV---LD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 314 CKEDDVfYWMT-NFGW-------MMAPWeivgaLHfGATLVCFEGAPSypkPDRIFGIIERYKVSIFGSTPGFIAGLRKn 385
Cdd:PRK04319 243 LHEDDV-YWCTaDPGWvtgtsygIFAPW-----LN-GATNVIDGGRFS---PERWYRILEDYKVTVWYTAPTAIRMLMG- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 386 hiSGDD----FNLSSLRILGSTGSILFSENWEWFFSVFGKgkcPINNIIGGTEMLGCFAQNLPNIPCKIGSVGVFALGMG 461
Cdd:PRK04319 312 --AGDDlvkkYDLSSLRHILSVGEPLNPEVVRWGMKVFGL---PIHDNWWMTETGGIMIANYPAMDIKPGSMGKPLPGIE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 462 GDIFNEKGESVRR-ETGRVVCTHPFPSMTRGFYADEEGYQetyfSAFRGVW-AHGDFAEMDEDGFVFMRGRSDDIINKNG 539
Cdd:PRK04319 387 AAIVDDQGNELPPnRMGNLAIKKGWPSMMRGIWNNPEKYE----SYFAGDWyVSGDSAYMDEDGYFWFQGRVDDVIKTSG 462
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1277171962 540 IKFSPANIESALIGFRAaefrVMEAIAVGIPDKNSENKIICFVIL----EGQDRLTE 592
Cdd:PRK04319 463 ERVGPFEVESKLMEHPA----VAEAGVIGKPDPVRGEIIKAFVALrpgyEPSEELKE 515
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
40-658 |
3.73e-45 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 170.51 E-value: 3.73e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 40 NDIEWFWprAMEFLGVRWFTPYAKLYDDtegiSH---TKWFIGGKLNIYNNCIERNIARGLGSKVCVCYEHESGKKRAIT 116
Cdd:PRK10524 13 DDPEAFW--AEQARRIDWQTPFTQVLDY----SNppfARWFVGGRTNLCHNAVDRHLAKRPEQLALIAVSTETDEERTYT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 117 FWQLKLLVDTIASAMKAHGIGKGDFVGMCMPISIDSIAVMFACFKIGAV-CMQMAPTTSTDGTKDIVDhvriARAKMFFM 195
Cdd:PRK10524 87 FRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIhSVVFGGFASHSLAARIDD----AKPVLIVS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 196 ADSYSYGG-----KNFTLEKIHQGVSDIFSVrhIVVFENDAPhspfspfvFGKKEMRSVFWDDFCKQGKSTIARTERCNA 270
Cdd:PRK10524 163 ADAGSRGGkvvpyKPLLDEAIALAQHKPRHV--LLVDRGLAP--------MARVAGRDVDYATLRAQHLGARVPVEWLES 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 271 EDVALMLFSSGTTrekgKKPKRILHTHGG---VLAQICKEVgfgFDCKEDDVFYWMTNFGWMMAPWEIV-GALHFGATLV 346
Cdd:PRK10524 233 NEPSYILYTSGTT----GKPKGVQRDTGGyavALATSMDTI---FGGKAGETFFCASDIGWVVGHSYIVyAPLLAGMATI 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 347 CFEGAPSYPKPDRIFGIIERYKVSIFGSTPGFIAGLRK-------NHisgddfNLSSLRILGSTGSILFSENWEWFFSVF 419
Cdd:PRK10524 306 MYEGLPTRPDAGIWWRIVEKYKVNRMFSAPTAIRVLKKqdpallrKH------DLSSLRALFLAGEPLDEPTASWISEAL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 420 GKgkcPINNIIGGTE----MLGcFAQNLPNIPCKIGSVGVFALGMGGDIFNEK-GESVR-RETGRVVCTHPFPSmtrGF- 492
Cdd:PRK10524 380 GV---PVIDNYWQTEtgwpILA-IARGVEDRPTRLGSPGVPMYGYNVKLLNEVtGEPCGpNEKGVLVIEGPLPP---GCm 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 493 ---YADEEGYQETYFSAF-RGVWAHGDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIESALigfrAAEFRVMEAIAVG 568
Cdd:PRK10524 453 qtvWGDDDRFVKTYWSLFgRQVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESI----SSHPAVAEVAVVG 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 569 IPDKNSENKIICFVILEGQDRLTETD-----EAALRSVVADIVNPQAKPERIFAIKELPRNAAAKVPYKAISRVFCDRYV 643
Cdd:PRK10524 529 VKDALKGQVAVAFVVPKDSDSLADREarlalEKEIMALVDSQLGAVARPARVWFVSALPKTRSGKLLRRAIQAIAEGRDP 608
|
650
....*....|....*
gi 1277171962 644 IAQTRVVNPQALEEI 658
Cdd:PRK10524 609 GDLTTIEDPAALQQI 623
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
100-637 |
2.97e-44 |
|
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: 166.52 E-value: 2.97e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 100 KVCVCYEHESGKKRAITFWQLKLLVDTIASAMKAHGIGKGDFVGMCMPISIDSIAVMFACFKIGAVCMqmaPTTSTDGTK 179
Cdd:cd05970 33 KLALVWCDDAGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAI---PATHQLTAK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 180 DIVDHVRIARAKMFFMADsysygGKNFTlEKIHQGVSDIFSVRHIVVFENDAPHSpfspfvfgkkemrsvfWDDF---CK 256
Cdd:cd05970 110 DIVYRIESADIKMIVAIA-----EDNIP-EEIEKAAPECPSKPKLVWVGDPVPEG----------------WIDFrklIK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 257 QGKSTIAR----TERCNaEDVALMLFSSGTTREkgkkPKRILHTHGGVLAQICKeVGFGFDCKEDDVFYWMTNFGWMMAP 332
Cdd:cd05970 168 NASPDFERptanSYPCG-EDILLVYFSSGTTGM----PKMVEHDFTYPLGHIVT-AKYWQNVREGGLHLTVADTGWGKAV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 333 W-EIVGALHFGATLVCFEgapsYPK--PDRIFGIIERYKVSIFGSTPGFIAGLRKNHISgdDFNLSSLRILGSTGSILFS 409
Cdd:cd05970 242 WgKIYGQWIAGAAVFVYD----YDKfdPKALLEKLSKYGVTTFCAPPTIYRFLIREDLS--RYDLSSLRYCTTAGEALNP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 410 ENWEWFFSVFGkgkCPINNIIGGTEMLGCFAqNLPNIPCKIGSVGVFALGMGGDIFNEKGESVRR-ETGRVVCT----HP 484
Cdd:cd05970 316 EVFNTFKEKTG---IKLMEGFGQTETTLTIA-TFPWMEPKPGSMGKPAPGYEIDLIDREGRSCEAgEEGEIVIRtskgKP 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 485 FpSMTRGFYADEEGYQETYFSafrGVWAHGDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIESALIGFRAaefrVMEA 564
Cdd:cd05970 392 V-GLFGGYYKDAEKTAEVWHD---GYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPA----VLEC 463
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1277171962 565 IAVGIPDKNSENKIICFVILEGQDRLTETDEAALRSVVADIVNPQAKPERIFAIKELPRNAAAKvpykaISRV 637
Cdd:cd05970 464 AVTGVPDPIRGQVVKATIVLAKGYEPSEELKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGK-----IRRV 531
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
146-629 |
7.64e-44 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 164.60 E-value: 7.64e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 146 MPISIDSIAVMFACFKIGAVCMQMAPTTSTdgtKDIVDHVRIARAKMFFMADSYSYGGKNFTLekiHQGVSDIFSVRHIV 225
Cdd:PLN03051 1 MPMTVDAVIIYLAIVLAGCVVVSVADSFSA---KEIATRLDISGAKGVFTQDVVLRGGRALPL---YSKVVEAAPAKAIV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 226 VFENDAPHSPfspfvfgKKEMRSVFWDDFCKQGKSTIARTER------CNAEDVALMLFSSGTTREkgkkPKRILHTHgg 299
Cdd:PLN03051 75 LPAAGEPVAV-------PLREQDLSWCDFLGVAAAQGSVGGNeyspvyAPVESVTNILFSSGTTGE----PKAIPWTH-- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 300 vLAQI-CKEVGFGF-DCKEDDVFYWMTNFGWMMAPWEIVGALHFGATLVCFEGAPSypkpDRIFG-IIERYKVSIFGSTP 376
Cdd:PLN03051 142 -LSPLrCASDGWAHmDIQPGDVVCWPTNLGWMMGPWLLYSAFLNGATLALYGGAPL----GRGFGkFVQDAGVTVLGLVP 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 377 GFIAGLRK-NHISGDDFNLSSLRILGSTGSILFSENWEWFFSVFGKGKcPINNIIGGTEMLGCFAQNLPNIPCKIGSVGV 455
Cdd:PLN03051 217 SIVKAWRHtGAFAMEGLDWSKLRVFASTGEASAVDDVLWLSSVRGYYK-PVIEYCGGTELASGYISSTLLQPQAPGAFST 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 456 FALGMGGDIFNEKGESVRRE---TGRVVCTHPF-PSMTRGFYADeegYQETYF-----SAFRG--VWAHGDFAEMDEDGF 524
Cdd:PLN03051 296 ASLGTRFVLLNDNGVPYPDDqpcVGEVALAPPMlGASDRLLNAD---HDKVYYkgmpmYGSKGmpLRRHGDIMKRTPGGY 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 525 VFMRGRSDDIINKNGIKFSPANIESALIgfrAAEFRVMEAIAVGIPDKNSENKIICFVILEGQDRLT--ETDEAALRSVV 602
Cdd:PLN03051 373 FCVQGRADDTMNLGGIKTSSVEIERACD---RAVAGIAETAAVGVAPPDGGPELLVIFLVLGEEKKGfdQARPEALQKKF 449
|
490 500 510
....*....|....*....|....*....|.
gi 1277171962 603 ADIV----NPQAKPERIFAIKELPRNAAAKV 629
Cdd:PLN03051 450 QEAIqtnlNPLFKVSRVKIVPELPRNASNKL 480
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
8-629 |
9.42e-43 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 164.87 E-value: 9.42e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 8 WEPNEYFLNESRVARFMQRY-----------EISSWQELLEASND-IEWFWPRAMEFLGVRWFTPYAKLYDDTEGISHT- 74
Cdd:PLN03052 87 WFPSPEIAKLTNLGRLLEARgkellgskykdPISSFSEFQRFSVEnPEVYWSIVLDELSLVFSVPPRCILDTSDESNPGg 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 75 KWFIGGKLNIYNNCIERNIARGLGSkVCVCYEHESGKK---RAITFWQLKLLVDTIASAMKAHGIGKGDFVGMCMPISID 151
Cdd:PLN03052 167 QWLPGAVLNVAECCLTPKPSKTDDS-IAIIWRDEGSDDlpvNRMTLSELRSQVSRVANALDALGFEKGDAIAIDMPMNVH 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 152 SIAVMFACFKIGAVCMQMAPTTSTdgtKDIVDHVRIARAKMFFMADSYSYGGKNFTLekiHQGVSDIFSVRHIVVfenda 231
Cdd:PLN03052 246 AVIIYLAIILAGCVVVSIADSFAP---SEIATRLKISKAKAIFTQDVIVRGGKSIPL---YSRVVEAKAPKAIVL----- 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 232 PHSPFSPFVfgkkEMRS--VFWDDFCKQGKsTIARTERCNA-----EDVALMLFSSGTTREkgkkPKRILHTHggvLAQI 304
Cdd:PLN03052 315 PADGKSVRV----KLREgdMSWDDFLARAN-GLRRPDEYKAveqpvEAFTNILFSSGTTGE----PKAIPWTQ---LTPL 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 305 -CKEVGFG-FDCKEDDVFYWMTNFGWMMAPWEIVGALHFGATLVCFEGAPSypkpDRIFG-IIERYKVSIFGSTPGfIAG 381
Cdd:PLN03052 383 rAAADAWAhLDIRKGDIVCWPTNLGWMMGPWLVYASLLNGATLALYNGSPL----GRGFAkFVQDAKVTMLGTVPS-IVK 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 382 LRKNHISGDDFNLSSLRILGSTGSILFSENWEWFFSvfGKGKCPINNIIGGTEMLGCFAQNLPNIPCKIGSVGVFALGMG 461
Cdd:PLN03052 458 TWKNTNCMAGLDWSSIRCFGSTGEASSVDDYLWLMS--RAGYKPIIEYCGGTELGGGFVTGSLLQPQAFAAFSTPAMGCK 535
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 462 GDIFNEKGESVRRE---TGRVV-CTHPFPSMTRGFYADeegYQETYFSA---FRG--VWAHGDFAEMDEDGFVFMRGRSD 532
Cdd:PLN03052 536 LFILDDSGNPYPDDapcTGELAlFPLMFGASSTLLNAD---HYKVYFKGmpvFNGkiLRRHGDIFERTSGGYYRAHGRAD 612
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 533 DIINKNGIKFSPANIESALigfRAAEFRVMEAIAVGIPDKNS--ENKIIcFVILEGQDRLTETDEA---ALRSVVADIVN 607
Cdd:PLN03052 613 DTMNLGGIKVSSVEIERVC---NAADESVLETAAIGVPPPGGgpEQLVI-AAVLKDPPGSNPDLNElkkIFNSAIQKKLN 688
|
650 660
....*....|....*....|..
gi 1277171962 608 PQAKPERIFAIKELPRNAAAKV 629
Cdd:PLN03052 689 PLFKVSAVVIVPSFPRTASNKV 710
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
112-629 |
1.11e-42 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 161.51 E-value: 1.11e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 112 KRAITFWQLKLLVDTIASAMKAHGIGKGDFVGMCMPISIDSIAVMFACFKIGAVcmqMAPTT---STDGTKDIVDHvriA 188
Cdd:PRK06187 29 GRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAV---LHPINirlKPEEIAYILND---A 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 189 RAKMFFmADSysyggknfTLEKIHQGVSDIF-SVRHIVVfENDAPHSPFSPFVFGKKEMRSVFWDDFCkqgksTIARTER 267
Cdd:PRK06187 103 EDRVVL-VDS--------EFVPLLAAILPQLpTVRTVIV-EGDGPAAPLAPEVGEYEELLAAASDTFD-----FPDIDEN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 268 cnaeDVALMLFSSGTTrekGKkPKRILHTHGGVL---AQICKEVGFGfdckEDDVFYWMT------NFGWMMApweivgA 338
Cdd:PRK06187 168 ----DAAAMLYTSGTT---GH-PKGVVLSHRNLFlhsLAVCAWLKLS----RDDVYLVIVpmfhvhAWGLPYL------A 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 339 LHFGATLVcfegapsYPK---PDRIFGIIERYKVSIFGSTPGFIAG-LRKNHISGDDFnlSSLRILGSTGSILFSENWEW 414
Cdd:PRK06187 230 LMAGAKQV-------IPRrfdPENLLDLIETERVTFFFAVPTIWQMlLKAPRAYFVDF--SSLRLVIYGGAALPPALLRE 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 415 FFSVFGkgkCPINNIIGGTEM--LGCFAQ---NLPNIPCKIGSVGVFALGMGGDIFNEKGESVRRETGRV--VCTHPfPS 487
Cdd:PRK06187 301 FKEKFG---IDLVQGYGMTETspVVSVLPpedQLPGQWTKRRSAGRPLPGVEARIVDDDGDELPPDGGEVgeIIVRG-PW 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 488 MTRGFYADEEGYQETyfsaFRGVWAH-GDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIESALIGFRAaefrVMEAIA 566
Cdd:PRK06187 377 LMQGYWNRPEATAET----IDGGWLHtGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPA----VAEVAV 448
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1277171962 567 VGIPDKNSENKIICFVIL-EGQdrltETDEAALRSVVADIVNPQAKPERIFAIKELPRNAAAKV 629
Cdd:PRK06187 449 IGVPDEKWGERPVAVVVLkPGA----TLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKI 508
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
91-629 |
6.85e-40 |
|
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: 153.29 E-value: 6.85e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 91 RNIARGLGSKVCVCYEHESgkkraITFWQLKLLVDTIASAMKAHGIGKGDFVGMCMPISIDSIAVMFACFKIGAVCMQMA 170
Cdd:cd05959 11 LNLNEGRGDKTAFIDDAGS-----LTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 171 PTTSTDgtkdivDHVriarakmFFMADSYSYGGknFTLEKIHQ-----GVSDIFSVRHIVVFENDAPHSPFSpfvfgkke 245
Cdd:cd05959 86 TLLTPD------DYA-------YYLEDSRARVV--VVSGELAPvlaaaLTKSEHTLVVLIVSGGAGPEAGAL-------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 246 MRSVFWDDFCKQGKStiARTercNAEDVALMLFSSGTTrekgKKPKRILHTH-----------GGVLAqickevgfgfdC 314
Cdd:cd05959 143 LLAELVAAEAEQLKP--AAT---HADDPAFWLYSSGST----GRPKGVVHLHadiywtaelyaRNVLG-----------I 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 315 KEDDVF---------YWMTNfgwmmapwEIVGALHFGATLVCFegaPSYPKPDRIFGIIERYKVSIFGSTPGFIAGLRKN 385
Cdd:cd05959 203 REDDVCfsaaklffaYGLGN--------SLTFPLSVGATTVLM---PERPTPAAVFKRIRRYRPTVFFGVPTLYAAMLAA 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 386 HISGDDfNLSSLRILGSTGSILFSENWEWFFSVFGkgkCPINNIIGGTEMLGCFAQNLPNiPCKIGSVGVFALGMGGDIF 465
Cdd:cd05959 272 PNLPSR-DLSSLRLCVSAGEALPAEVGERWKARFG---LDILDGIGSTEMLHIFLSNRPG-RVRYGTTGKPVPGYEVELR 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 466 NEKGESVRR-ETGRVVCTHPfpSMTRGFYADEEGYQETyfsaFRGVWAH-GDFAEMDEDGFVFMRGRSDDIINKNGIKFS 543
Cdd:cd05959 347 DEDGGDVADgEPGELYVRGP--SSATMYWNNRDKTRDT----FQGEWTRtGDKYVRDDDGFYTYAGRADDMLKVSGIWVS 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 544 PANIESALIGFRAaefrVMEAIAVGIPDKNSENKIICFVILEGQDRLTETDEAALRSVVADIVNPQAKPERIFAIKELPR 623
Cdd:cd05959 421 PFEVESALVQHPA----VLEAAVVGVEDEDGLTKPKAFVVLRPGYEDSEALEEELKEFVKDRLAPYKYPRWIVFVDELPK 496
|
....*.
gi 1277171962 624 NAAAKV 629
Cdd:cd05959 497 TATGKI 502
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
113-629 |
2.56e-38 |
|
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: 147.61 E-value: 2.56e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 113 RAITFWQLKLLVDTIASAMKAHGIGKGDFVGMCMPISIDSIAVMFACFKIGAVCMQMAPTTSTDgtkdivDHVRIARakm 192
Cdd:cd05919 9 RSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPD------DYAYIAR--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 193 ffmadsysyggknftlekihqgvsdifsvrhivvfendaphspfspfvfgkkemrsvfwddfckqgkSTIARTERCNAED 272
Cdd:cd05919 80 -------------------------------------------------------------------DCEARLVVTSADD 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 273 VALMLFSSGTTrekgKKPKRILHTHGGVL--AQ-ICKEVgfgFDCKEDDVFYWMTN--FGW-----MMAPWEIvgalhfG 342
Cdd:cd05919 93 IAYLLYSSGTT----GPPKGVMHAHRDPLlfADaMAREA---LGLTPGDRVFSSAKmfFGYglgnsLWFPLAV------G 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 343 ATLVCFEGAPSypkPDRIFGIIERYKVSIFGSTPGFIAGLRKN-HISGDDFnlSSLRILGSTGSILFSENWEWFFSVFGk 421
Cdd:cd05919 160 ASAVLNPGWPT---AERVLATLARFRPTVLYGVPTFYANLLDScAGSPDAL--RSLRLCVSAGEALPRGLGERWMEHFG- 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 422 gkCPINNIIGGTEMLGCFAQNLPNiPCKIGSVGVFALGMGGDIFNEKGESVrrETGRV-VCTHPFPSMTRGFYADEEGYQ 500
Cdd:cd05919 234 --GPILDGIGATEVGHIFLSNRPG-AWRLGSTGRPVPGYEIRLVDEEGHTI--PPGEEgDLLVRGPSAAVGYWNNPEKSR 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 501 ETyfsaFRGVW-AHGDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIESALIGFRAaefrVMEAIAVGIPDKNSENKII 579
Cdd:cd05919 309 AT----FNGGWyRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPA----VAEAAVVAVPESTGLSRLT 380
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1277171962 580 CFVILEGQDRLTETDEAALRSVVADIVNPQAKPERIFAIKELPRNAAAKV 629
Cdd:cd05919 381 AFVVLKSPAAPQESLARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKL 430
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
109-629 |
6.17e-38 |
|
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: 146.94 E-value: 6.17e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 109 SGKKRAITFWQLKLLVDTIASAMKAHGIGKGDFVGMCMPISIDSIAVMFACFKIGAVCMQMAPTtstdgtkdivdhvria 188
Cdd:cd05936 19 IFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPL---------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 189 rakmffmadsysYGGKnftlEKIHQ----GVSDIFSVrhivvfendaphspfspfvfgkkemrsVFWDDFCKQGKSTIAR 264
Cdd:cd05936 83 ------------YTPR----ELEHIlndsGAKALIVA---------------------------VSFTDLLAAGAPLGER 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 265 TERcNAEDVALMLFSSGTTrekGKkPKRILHTHGGVLA--QICKEVgFGFDCKEDDVF-----YWMTnFGWMMApweIVG 337
Cdd:cd05936 120 VAL-TPEDVAVLQYTSGTT---GV-PKGAMLTHRNLVAnaLQIKAW-LEDLLEGDDVVlaalpLFHV-FGLTVA---LLL 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 338 ALHFGATLVCFegaPSyPKPDRIFGIIERYKVSIFGSTPGFIAGLrKNHISGDDFNLSSLRILGSTGSILFSENWEWFFS 417
Cdd:cd05936 190 PLALGATIVLI---PR-FRPIGVLKEIRKHRVTIFPGVPTMYIAL-LNAPEFKKRDFSSLRLCISGGAPLPVEVAERFEE 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 418 VFGkgkCPINNIIGGTEM--LGCFaqNLPNIPCKIGSVGVFALGMGGDIFNEKGESV-RRETGRVVCTHPfpSMTRGFYA 494
Cdd:cd05936 265 LTG---VPIVEGYGLTETspVVAV--NPLDGPRKPGSIGIPLPGTEVKIVDDDGEELpPGEVGELWVRGP--QVMKGYWN 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 495 DEEGYQETyfsaFRGVWAH-GDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIESALIGFRAaefrVMEAIAVGIPDKN 573
Cdd:cd05936 338 RPEETAEA----FVDGWLRtGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPA----VAEAAVVGVPDPY 409
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1277171962 574 SENKIICFVILEGQDRLTETDEAA-LRSVVADIvnpqaK-PERIFAIKELPRNAAAKV 629
Cdd:cd05936 410 SGEAVKAFVVLKEGASLTEEEIIAfCREQLAGY-----KvPRQVEFRDELPKSAVGKI 462
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
89-629 |
3.16e-36 |
|
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: 141.59 E-value: 3.16e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 89 IERNIARGlGSKVCVCYEHESgkkraITFWQLKLLVDTIASAMKAHGIGKGDFVGMCMPISIDSIAVMFACFKIGAVCMQ 168
Cdd:cd17631 1 LRRRARRH-PDRTALVFGGRS-----LTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 169 MAPTTSTDGTKDIVDHvriARAKMFFmadsysyggknftlekihqgvsdifsvrhivvfendaphspfspfvfgkkemrs 248
Cdd:cd17631 75 LNFRLTPPEVAYILAD---SGAKVLF------------------------------------------------------ 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 249 vfwddfckqgkstiartercnaEDVALMLFSSGTTrekgKKPKRILHTHGGVLAQiCKEVGFGFDCKEDDVFYW---MTN 325
Cdd:cd17631 98 ----------------------DDLALLMYTSGTT----GRPKGAMLTHRNLLWN-AVNALAALDLGPDDVLLVvapLFH 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 326 FGWMMAPWeiVGALHFGATLVCFEGapsyPKPDRIFGIIERYKVSIFGSTPGFIAGLRkNHISGDDFNLSSLRILGSTGS 405
Cdd:cd17631 151 IGGLGVFT--LPTLLRGGTVVILRK----FDPETVLDLIERHRVTSFFLVPTMIQALL-QHPRFATTDLSSLRAVIYGGA 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 406 I----LFSEnwewfFSVFGkgkCPINNIIGGTEM--LGCF-----AQNlpnipcKIGSVGVFALGMGGDIFNEKGESVR- 473
Cdd:cd17631 224 PmperLLRA-----LQARG---VKFVQGYGMTETspGVTFlspedHRR------KLGSAGRPVFFVEVRIVDPDGREVPp 289
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 474 RETGRVVCTHpfPSMTRGFYADEEgyqETYfSAFRGVWAH-GDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIESALI 552
Cdd:cd17631 290 GEVGEIVVRG--PHVMAGYWNRPE---ATA-AAFRDGWFHtGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLY 363
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1277171962 553 GFRAaefrVMEAIAVGIPDKNSENKIICFVILEGQDRLTETDEAA-LRSVVADIvnpqAKPERIFAIKELPRNAAAKV 629
Cdd:cd17631 364 EHPA----VAEVAVIGVPDEKWGEAVVAVVVPRPGAELDEDELIAhCRERLARY----KIPKSVEFVDALPRNATGKI 433
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
270-629 |
2.14e-33 |
|
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: 133.37 E-value: 2.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 270 AEDVALMLFSSGTTrekgKKPKRILHTHGGVLAqICKevGFGFDC---KEDDVFYWMTNF-------GWMMAPWeivgal 339
Cdd:cd05958 96 SDDICILAFTSGTT----GAPKATMHFHRDPLA-SAD--RYAVNVlrlREDDRFVGSPPLaftfglgGVLLFPF------ 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 340 HFGATLVCFEGApsypKPDRIFGIIERYKVSIFGSTP-GFIAGLRKNHISGDDfnLSSLRILGSTGSILFSENWEWFFSV 418
Cdd:cd05958 163 GVGASGVLLEEA----TPDLLLSAIARYKPTVLFTAPtAYRAMLAHPDAAGPD--LSSLRKCVSAGEALPAALHRAWKEA 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 419 FGkgkCPINNIIGGTEMLGCFAQNLPNiPCKIGSVGVFALGMGGDIFNEKGESVRR-ETGRVVCTHPfpsmtRGFYADEE 497
Cdd:cd05958 237 TG---IPIIDGIGSTEMFHIFISARPG-DARPGATGKPVPGYEAKVVDDEGNPVPDgTIGRLAVRGP-----TGCRYLAD 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 498 GYQETYFsafRGVW-AHGDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIESALIGFRAaefrVMEAIAVGIPDKNSEN 576
Cdd:cd05958 308 KRQRTYV---QGGWnITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPA----VAECAVVGHPDESRGV 380
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1277171962 577 KIICFVILEGQDRLTETDEAALRSVVADIVNPQAKPERIFAIKELPRNAAAKV 629
Cdd:cd05958 381 VVKAFVVLRPGVIPGPVLARELQDHAKAHIAPYKYPRAIEFVTELPRTATGKL 433
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
115-629 |
6.91e-33 |
|
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: 131.87 E-value: 6.91e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 115 ITFWQLKLLVDTIASAMKAHGIGKGDFVGMCMPISIDSIAVMFACFKIGAVcmqMAPTTSTDGTKDIVDHVRIARAkmff 194
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAV---YQPLFTAFGPKAIEHRLRTSGA---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 195 madsysyggknftlekihqgvsdifsvrHIVVFENDAPHSPfspfvfgkkemrsvfwddfckqgkstiartercnAEDVA 274
Cdd:cd05973 74 ----------------------------RLVVTDAANRHKL----------------------------------DSDPF 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 275 LMLFSSGTTrekgKKPKRILHTHGGVLAqICKEVGFGFDCKEDDVFYWMTNFGWMMAPW-EIVGALHFGATLVCFEGAPS 353
Cdd:cd05973 92 VMMFTSGTT----GLPKGVPVPLRALAA-FGAYLRDAVDLRPEDSFWNAADPGWAYGLYyAITGPLALGHPTILLEGGFS 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 354 ypkPDRIFGIIERYKVSIFGSTPGFIAGLRKNHISGDDFNLSSLRILGSTGSILFSENWEWFFSVFGkgkCPINNIIGGT 433
Cdd:cd05973 167 ---VESTWRVIERLGVTNLAGSPTAYRLLMAAGAEVPARPKGRLRRVSSAGEPLTPEVIRWFDAALG---VPIHDHYGQT 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 434 EmLGCFAQN--LPNIPCKIGSVGVFALGMGGDIFNEKG-ESVRRETGRV-VCTHPFPSMTRGfyadeeGYQETYFSAFRG 509
Cdd:cd05973 241 E-LGMVLANhhALEHPVHAGSAGRAMPGWRVAVLDDDGdELGPGEPGRLaIDIANSPLMWFR------GYQLPDTPAIDG 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 510 VW-AHGDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIESALIGFRAaefrVMEAIAVGIPDKNSENKIICFVILEGQD 588
Cdd:cd05973 314 GYyLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPA----VAEAAVIGVPDPERTEVVKAFVVLRGGH 389
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1277171962 589 RLTETDEAALRSVVADIVNPQAKPERIFAIKELPRNAAAKV 629
Cdd:cd05973 390 EGTPALADELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKI 430
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
114-629 |
1.03e-31 |
|
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: 128.27 E-value: 1.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 114 AITFWQLKLLVDTIASAMKAHGIGKGDFVGMCMPISIDSIAVMFACFKIGAVCmqmAPTTSTDGTKDIVDHVRIARAKMF 193
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVT---NPILPFFREHELAFILRRAKAKVF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 194 FMadsysyggknftlekihqgvsdifsvrhivvfendaphspfsPFVFGKKemrsvfwdDFCKQGkstiartercnaEDV 273
Cdd:cd05903 78 VV------------------------------------------PERFRQF--------DPAAMP------------DAV 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 274 ALMLFSSGTTREkgkkPKRILHTHGGVLAQICKEV---GFGfdckEDDVFywmtnfgWMMAPW-EIVGALHfGATLVCFE 349
Cdd:cd05903 96 ALLLFTSGTTGE----PKGVMHSHNTLSASIRQYAerlGLG----PGDVF-------LVASPMaHQTGFVY-GFTLPLLL 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 350 GAPSYPK----PDRIFGIIERYKVSIFGSTPGFIAGLrKNHISGDDFNLSSLRILGSTGS----ILFSENWEWF----FS 417
Cdd:cd05903 160 GAPVVLQdiwdPDKALALMREHGVTFMMGATPFLTDL-LNAVEEAGEPLSRLRTFVCGGAtvprSLARRAAELLgakvCS 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 418 VFGKGKCPinNIIGGTE------MLGCFAQNLPNIPCKIGSVGVFALGMGgdifnEKGESVRREtgrvvcthpfPSMTRG 491
Cdd:cd05903 239 AYGSTECP--GAVTSITpapedrRLYTDGRPLPGVEIKVVDDTGATLAPG-----VEGELLSRG----------PSVFLG 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 492 FYADEEgyqeTYFSAFRGVWAH-GDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIESALIGFRAaefrVMEAIAVGIP 570
Cdd:cd05903 302 YLDRPD----LTADAAPEGWFRtGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPG----VIEAAVVALP 373
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1277171962 571 DKNSENKIICFVILEGQDRLTETDEAA--LRSVVADivnpQAKPERIFAIKELPRNAAAKV 629
Cdd:cd05903 374 DERLGERACAVVVTKSGALLTFDELVAylDRQGVAK----QYWPERLVHVDDLPRTPSGKV 430
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
114-635 |
1.35e-31 |
|
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: 128.97 E-value: 1.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 114 AITFWQLKLLVDTIASAMKAHGIGKGDFVGMCMPISIDSIAVMFACFKIGAVCMQMAPTTstdgTKDIVDhvriarakmF 193
Cdd:cd05926 14 ALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAY----KKAEFE---------F 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 194 FMADSysygGKNFTLEKIHQGVSDIFSVRHIVVFENDAPHSPFSPFVFGKKEMRSvfwddFCKQGKSTIARTERCNAEDV 273
Cdd:cd05926 81 YLADL----GSKLVLTPKGELGPASRAASKLGLAILELALDVGVLIRAPSAESLS-----NLLADKKNAKSEGVPLPDDL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 274 ALMLFSSGTTrekgKKPKRILHTHGGVLAQ---ICKEVGFGFDckeDDVFYWMTNF---GwmmapwEIVGALhfgATLVC 347
Cdd:cd05926 152 ALILHTSGTT----GRPKGVPLTHRNLAASatnITNTYKLTPD---DRTLVVMPLFhvhG------LVASLL---STLAA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 348 fEGAPSYP---KPDRIFGIIERYKVSIFGSTPGFIAGLRKNHISGDDFNLSSLRILGSTGSILFSENWEWFFSVFGkgkC 424
Cdd:cd05926 216 -GGSVVLPprfSASTFWPDVRDYNATWYTAVPTIHQILLNRPEPNPESPPPKLRFIRSCSASLPPAVLEALEATFG---A 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 425 PINNIIGGTE----MlgcFAQNLPNIPCKIGSVGvFALGMGGDIFNEKGESVRR-ETGRVVCTHPfpSMTRGFYADEEGY 499
Cdd:cd05926 292 PVLEAYGMTEaahqM---TSNPLPPGPRKPGSVG-KPVGVEVRILDEDGEILPPgVVGEICLRGP--NVTRGYLNNPEAN 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 500 QEtyfSAFRGVWAH-GDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIESALIGFRAaefrVMEAIAVGIPDKNSENKI 578
Cdd:cd05926 366 AE---AAFKDGWFRtGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPA----VLEAVAFGVPDEKYGEEV 438
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1277171962 579 ICFVILEGQdrlTETDEAALRSVVADIVNPQAKPERIFAIKELPRNAAAKVPYKAIS 635
Cdd:cd05926 439 AAAVVLREG---ASVTEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVA 492
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
116-629 |
4.09e-31 |
|
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: 126.78 E-value: 4.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 116 TFWQLKLLVDTIASAMKAHGIGKGDFVGMCMPISIDSIAVMFACFKIGAVCMQMAPTTSTDGTKdivdhvriarakmFFM 195
Cdd:cd05971 8 TFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALE-------------YRL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 196 ADSysyggknftlekihqgvsdifSVRHIVVFENDAPhspfspfvfgkkemrsvfwddfckqgkstiartercnaedvAL 275
Cdd:cd05971 75 SNS---------------------GASALVTDGSDDP-----------------------------------------AL 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 276 MLFSSGTTrekgKKPKRILHTHGGVLAQIcKEVGFGFDC--KEDDVFYWMTNFGWMMAPWEI-VGALHFGATLVCFEGAP 352
Cdd:cd05971 93 IIYTSGTT----GPPKGALHAHRVLLGHL-PGVQFPFNLfpRDGDLYWTPADWAWIGGLLDVlLPSLYFGVPVLAHRMTK 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 353 SypKPDRIFGIIERYKVSIFGSTPGFIAGLRKNHISGDDFNLSsLRILGSTGSILFSENWEWFFSVFGkgkCPINNIIGG 432
Cdd:cd05971 168 F--DPKAALDLMSRYGVTTAFLPPTALKMMRQQGEQLKHAQVK-LRAIATGGESLGEELLGWAREQFG---VEVNEFYGQ 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 433 TEMLGCFAQNLPNIPCKIGSVGVFALGMGGDIFNEKGESV-RRETGRVVCTHPFPSMTRGFYADEEGYQETyfsaFRGVW 511
Cdd:cd05971 242 TECNLVIGNCSALFPIKPGSMGKPIPGHRVAIVDDNGTPLpPGEVGEIAVELPDPVAFLGYWNNPSATEKK----MAGDW 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 512 -AHGDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIESALIGFRAaefrVMEAIAVGIPDKNSENKIICFVIL----EG 586
Cdd:cd05971 318 lLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPA----VLMAAVVGIPDPIRGEIVKAFVVLnpgeTP 393
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1277171962 587 QDRLTEtdeaALRSVVADIVNPQAKPERIFAIKELPRNAAAKV 629
Cdd:cd05971 394 SDALAR----EIQELVKTRLAAHEYPREIEFVNELPRTATGKI 432
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
113-629 |
1.02e-30 |
|
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: 126.58 E-value: 1.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 113 RAITFWQLKLLVDTIASAMKAHGIGKGDFVGMCMPISIDSIAVMFACFKIGAVCMQMAPTTSTDgtkDIVDHVRIARAKM 192
Cdd:cd05904 31 RALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPA---EIAKQVKDSGAKL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 193 FFMADSYsyggknftLEKIHQgvsdiFSVRHIVVfendaphspfspfvfGKKEMRSVFWDDFCKQGKSTIARTERCNAED 272
Cdd:cd05904 108 AFTTAEL--------AEKLAS-----LALPVVLL---------------DSAEFDSLSFSDLLFEADEAEPPVVVIKQDD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 273 VALMLFSSGTTrekGkKPKRILHTHGGVLAQICKEV-GFGFDCKEDDV------FYWMTNFGWMMapweiVGALHFGATL 345
Cdd:cd05904 160 VAALLYSSGTT---G-RSKGVMLTHRNLIAMVAQFVaGEGSNSDSEDVflcvlpMFHIYGLSSFA-----LGLLRLGATV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 346 VcfegapSYPKPD--RIFGIIERYKVSIFGSTPGFIAGLRKNHIsGDDFNLSSLRILGSTGSILFSENWEWFFSVFgkGK 423
Cdd:cd05904 231 V------VMPRFDleELLAAIERYKVTHLPVVPPIVLALVKSPI-VDKYDLSSLRQIMSGAAPLGKELIEAFRAKF--PN 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 424 CPINNIIGGTEMLGCFAQNLPNI--PCKIGSVGVFALGMGGDIFN-EKGESV-RRETGRvVCTHPfPSMTRGFYADEEGY 499
Cdd:cd05904 302 VDLGQGYGMTESTGVVAMCFAPEkdRAKYGSVGRLVPNVEAKIVDpETGESLpPNQTGE-LWIRG-PSIMKGYLNNPEAT 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 500 QETYFSafRGvWAH-GDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIESALIGFRAaefrVMEAIAVGIPDKNSENKI 578
Cdd:cd05904 380 AATIDK--EG-WLHtGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPE----ILDAAVIPYPDEEAGEVP 452
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1277171962 579 ICFVILEGQDRLTETDeaaLRSVVADIVNPQAKPERIFAIKELPRNAAAKV 629
Cdd:cd05904 453 MAFVVRKPGSSLTEDE---IMDFVAKQVAPYKKVRKVAFVDAIPKSPSGKI 500
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
121-637 |
5.13e-29 |
|
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: 121.28 E-value: 5.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 121 KLLVDTIASAMKAHGIGK-GDFVGMCMPISIDSIAVMFACFKIGAVCMQMAPTTSTDGTKDIVDHVRIAR---AKMFfma 196
Cdd:cd05909 12 KLLTGAIALARKLAKMTKeGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTvltSKQF--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 197 dsysyggknftLEKI-HQGVSDIFSVRHIVVFENDAPHSPFSPFVFGKKEMRSVFWDDFCKQGKSTIartercNAEDVAL 275
Cdd:cd05909 89 -----------IEKLkLHHLFDVEYDARIVYLEDLRAKISKADKCKAFLAGKFPPKWLLRIFGVAPV------QPDDPAV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 276 MLFSSGTTREkgkkPKRILHTHGGVLAQI--CKEVgfgFDCKEDDVF---------YWMTNFGWMmapweivgALHFGAT 344
Cdd:cd05909 152 ILFTSGSEGL----PKGVVLSHKNLLANVeqITAI---FDPNPEDVVfgalpffhsFGLTGCLWL--------PLLSGIK 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 345 LVCfegAPSYPKPDRIFGIIERYKVSIFGSTPGFIAGLRKNhISGDDFnlSSLRILGSTGSILFSENWEWFFSVFGKgkc 424
Cdd:cd05909 217 VVF---HPNPLDYKKIPELIYDKKATILLGTPTFLRGYARA-AHPEDF--SSLRLVVAGAEKLKDTLRQEFQEKFGI--- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 425 PINNIIGGTEMLGCFAQNLPNIPCKIGSVGVFALGMGGDIFNEKG--ESVRRETGRVVCTHpfPSMTRGFYADEEGYQEt 502
Cdd:cd05909 288 RILEGYGTTECSPVISVNTPQSPNKEGTVGRPLPGMEVKIVSVETheEVPIGEGGLLLVRG--PNVMLGYLNEPELTSF- 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 503 yfsAFRGVW-AHGDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIESALIGFRAAEFRVmeaIAVGIPDKNSENKIICF 581
Cdd:cd05909 365 ---AFGDGWyDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEILPEDNEV---AVVSVPDGRKGEKIVLL 438
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1277171962 582 VILEGQDRLTETDeaALRSvvADIVNpQAKPERIFAIKELPRNAAAKVPYKAISRV 637
Cdd:cd05909 439 TTTTDTDPSSLND--ILKN--AGISN-LAKPSYIHQVEEIPLLGTGKPDYVTLKAL 489
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
38-636 |
1.06e-28 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 121.77 E-value: 1.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 38 ASNDIEWFWPRAMEFLgVRWFTPYAKLYDDTEgiSHTKWFIGGKLNIYNNCIERNIARGLG-SKVCVCYEHESGKKRA-I 115
Cdd:PTZ00237 17 ANSNPESFWDEVAKKY-VHWDKMYDKVYSGDE--IYPDWFKGGELNTCYNVLDIHVKNPLKrDQDALIYECPYLKKTIkL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 116 TFWQLKLLVDTIASAMKAHGIGKGDFVGMCMPISIDSIAVMFACFKIGAvcmqmAPTTSTDG--TKDIVDHVRIARAKMF 193
Cdd:PTZ00237 94 TYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGA-----THCVLFDGysVKSLIDRIETITPKLI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 194 FmadSYSYGGKN-----FT---LEKIHQGVsdiFSVRH-IVVFENDAPHSPFSPFVFGKKEM-RSVFWDDFCKQGKSTia 263
Cdd:PTZ00237 169 I---TTNYGILNdeiitFTpnlKEAIELST---FKPSNvITLFRNDITSESDLKKIETIPTIpNTLSWYDEIKKIKEN-- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 264 rTERCNAEDVAL-------MLFSSGTTrekgKKPKRILHTHGGVLAQICKEVGFGFDCKEDDVFYWMTNFGWMMAPWEIV 336
Cdd:PTZ00237 241 -NQSPFYEYVPVesshplyILYTSGTT----GNSKAVVRSNGPHLVGLKYYWRSIIEKDIPTVVFSHSSIGWVSFHGFLY 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 337 GALHFGATLVCFEGAPSYPK--PDRIFGIIERYKVSIFGSTPGFIAGLRKNHISGDD----FNLSSLRILGSTGSILFSE 410
Cdd:PTZ00237 316 GSLSLGNTFVMFEGGIIKNKhiEDDLWNTIEKHKVTHTLTLPKTIRYLIKTDPEATIirskYDLSNLKEIWCGGEVIEES 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 411 NWEWFFSvfgKGKCPINNIIGGTEMlGC---FAQNLPNIPCKigSVGVFALGMGGDIFNEKGESV-RRETGRVVCTHPFP 486
Cdd:PTZ00237 396 IPEYIEN---KLKIKSSRGYGQTEI-GItylYCYGHINIPYN--ATGVPSIFIKPSILSEDGKELnVNEIGEVAFKLPMP 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 487 -SMTRGFYADEEGYQETyFSAFRGVWAHGDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIESALIGFRAaefrVMEAI 565
Cdd:PTZ00237 470 pSFATTFYKNDEKFKQL-FSKFPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPL----VLECC 544
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1277171962 566 AVGIPDKNSENKIICFVILEGQDRLTETDEAALRSVVADIV----NPQAKPERIFAIKELPRNAAAKVPYKAISR 636
Cdd:PTZ00237 545 SIGIYDPDCYNVPIGLLVLKQDQSNQSIDLNKLKNEINNIItqdiESLAVLRKIIIVNQLPKTKTGKIPRQIISK 619
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
91-629 |
4.84e-28 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 118.47 E-value: 4.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 91 RNIARGLGSKVCVCYEHESgkkraITFWQLKLLVDTIASAMKAHGIGKGDFVGMCMPISIDSIAVMFACFKIGAVCMQMA 170
Cdd:PRK07656 12 ARAARRFGDKEAYVFGDQR-----LTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 171 PTTSTDGTKDIvdhVRIARAKMFFMADSYsyggknftLEKIHQGVSDIFSVRHIVVFENDAPHSPFSPFvfgkkemrsVF 250
Cdd:PRK07656 87 TRYTADEAAYI---LARGDAKALFVLGLF--------LGVDYSATTRLPALEHVVICETEEDDPHTEKM---------KT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 251 WDDFCKQGKSTiARTERCNAEDVALMLFSSGTTrekGkKPKRILHTHGGVL---AQICKEVGFgfdcKEDDVfYWMTN-- 325
Cdd:PRK07656 147 FTDFLAAGDPA-ERAPEVDPDDVADILFTSGTT---G-RPKGAMLTHRQLLsnaADWAEYLGL----TEGDR-YLAANpf 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 326 ---FGWMMApweIVGALHFGATLVcfegapSYPK--PDRIFGIIERYKVSIFGSTPGFIAGLRkNHISGDDFNLSSLRIL 400
Cdd:PRK07656 217 fhvFGYKAG---VNAPLMRGATIL------PLPVfdPDEVFRLIETERITVLPGPPTMYNSLL-QHPDRSAEDLSSLRLA 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 401 GSTGSILFSENWEWFFSVFGkgkcpINNIIGG---TEM--LGCFaqNLPNIPCKI--GSVGVFALGMGGDIFNEKGESVR 473
Cdd:PRK07656 287 VTGAASMPVALLERFESELG-----VDIVLTGyglSEAsgVTTF--NRLDDDRKTvaGTIGTAIAGVENKIVNELGEEVP 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 474 R-ETGRVVCTHpfPSMTRGFYADEEGYQEtyfsAFRGV-WAH-GDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIESA 550
Cdd:PRK07656 360 VgEVGELLVRG--PNVMKGYYDDPEATAA----AIDADgWLHtGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEV 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 551 LIGFRAaefrVMEAIAVGIPDKNSENKIICFVILEGQDRLTETDEAAL-RSVVADIVNPQAkperIFAIKELPRNAAAKV 629
Cdd:PRK07656 434 LYEHPA----VAEAAVIGVPDERLGEVGKAYVVLKPGAELTEEELIAYcREHLAKYKVPRS----IEFLDELPKNATGKV 505
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
112-629 |
1.88e-27 |
|
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: 116.78 E-value: 1.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 112 KRAITFWQLKLLVDTIASAMKAHGIGKGDFVGMCMPISIDSIAVMFACFKIGAV-CMQMAPTTSTDgtkdiVDH-VRIAR 189
Cdd:COG1021 48 ERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAIpVFALPAHRRAE-----ISHfAEQSE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 190 AKMFFMADSYsyGGKNF--TLEKIHQGVSdifSVRHIVVFENDAPHSPfspfvfgkkemrsvfWDDFCKQGKStiARTER 267
Cdd:COG1021 123 AVAYIIPDRH--RGFDYraLARELQAEVP---SLRHVLVVGDAGEFTS---------------LDALLAAPAD--LSEPR 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 268 CNAEDVALMLFSSGTTrekGkKPKRILHTHGGVL------AQICkevgfGFDckEDDVF---------YWMTNFGwmmap 332
Cdd:COG1021 181 PDPDDVAFFQLSGGTT---G-LPKLIPRTHDDYLysvrasAEIC-----GLD--ADTVYlaalpaahnFPLSSPG----- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 333 weIVGALHFGATLVCfegAPSyPKPDRIFGIIERYKVSIFGSTPGfIAGLRKNHISGDDFNLSSLRILGSTGSILFSENW 412
Cdd:COG1021 245 --VLGVLYAGGTVVL---APD-PSPDTAFPLIERERVTVTALVPP-LALLWLDAAERSRYDLSSLRVLQVGGAKLSPELA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 413 EwffSVfgkgkcpinniiggTEMLGCFAQNlpnipckigsvgVFalGMG--------------------------GD--- 463
Cdd:COG1021 318 R---RV--------------RPALGCTLQQ------------VF--GMAeglvnytrlddpeevilttqgrpispDDevr 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 464 IFNEKGESVRR-ETGRVVCTHPFpsmT-RGFYADEEgYQETYFSA---FRGvwahGDFAEMDEDGFVFMRGRSDDIINKN 538
Cdd:COG1021 367 IVDEDGNPVPPgEVGELLTRGPY---TiRGYYRAPE-HNARAFTPdgfYRT----GDLVRRTPDGYLVVEGRAKDQINRG 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 539 GIKFSPANIESALIGFRAaefrVMEAIAVGIPDKNSENKIICFVILEGQDRLTETDEAALRSV-VADIvnpqaK-PERIF 616
Cdd:COG1021 439 GEKIAAEEVENLLLAHPA----VHDAAVVAMPDEYLGERSCAFVVPRGEPLTLAELRRFLRERgLAAF-----KlPDRLE 509
|
570
....*....|...
gi 1277171962 617 AIKELPRNAAAKV 629
Cdd:COG1021 510 FVDALPLTAVGKI 522
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
113-633 |
7.06e-24 |
|
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: 104.92 E-value: 7.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 113 RAITFWQLKLLVDTIASAMKAHGIGKGDFVGMCMPISIDSIAVMFACFKIGAVCMQMAPTTSTDgtkdivdhvRIArakm 192
Cdd:cd05930 11 QSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAE---------RLA---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 193 FFMADSysyggknftlekihqgvsdifSVRHIVVfendaphspfspfvfgkkemrsvfwddfckqgkstiartercNAED 272
Cdd:cd05930 78 YILEDS---------------------GAKLVLT------------------------------------------DPDD 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 273 VALMLFSSGTTrekGKkPKRILHTHGGVLAQIcKEVGFGFDCKEDDVFYWMTNFGWMMAPWEIVGALHFGATLVCFEGAP 352
Cdd:cd05930 95 LAYVIYTSGST---GK-PKGVMVEHRGLVNLL-LWMQEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEV 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 353 SYPkPDRIFGIIERYKVSIFGSTPGFIAGLrknHISGDDFNLSSLRILGSTGSILFSENWEWFFSVFGKGKcpINNIIGG 432
Cdd:cd05930 170 RKD-PEALADLLAEEGITVLHLTPSLLRLL---LQELELAALPSLRLVLVGGEALPPDLVRRWRELLPGAR--LVNLYGP 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 433 TE------MLGCFAQN-----------LPNI----------PCKIGSVGVFALGmggdifnekGESVRR-------ETGR 478
Cdd:cd05930 244 TEatvdatYYRVPPDDeedgrvpigrpIPNTrvyvldenlrPVPPGVPGELYIG---------GAGLARgylnrpeLTAE 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 479 VVCTHPFPSMTRgFYAdeegyqeTyfsafrgvwahGDFAEMDEDG-FVFMrGRSDDIINKNGIKFSPANIESALIGFRAa 557
Cdd:cd05930 315 RFVPNPFGPGER-MYR-------T-----------GDLVRWLPDGnLEFL-GRIDDQVKIRGYRIELGEIEAALLAHPG- 373
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1277171962 558 efrVMEAIAVGIPDKNSENKIICFVILEGQDrltETDEAALRSVVADIVNPQAKPERIFAIKELPRNAAAKVPYKA 633
Cdd:cd05930 374 ---VREAAVVAREDGDGEKRLVAYVVPDEGG---ELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKA 443
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
116-629 |
1.03e-23 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 105.60 E-value: 1.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 116 TFWQLKLLVDTIASAMKAHGIGKGDFVGMCMPISIDSIAVMFACFKIGAVcmqMAPTTSTDGTKDIVDHVRIARAKMFFM 195
Cdd:PRK06087 51 TYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAV---SVPLLPSWREAELVWVLNKCQAKMFFA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 196 ADSYSyggKNFTLEKIHQGVSDIFSVRHIVVFENDAPHSPfspfvfgkkemrSVFWDDFCKQGKsTIARTERCNAEDVAL 275
Cdd:PRK06087 128 PTLFK---QTRPVDLILPLQNQLPQLQQIVGVDKLAPATS------------SLSLSQIIADYE-PLTTAITTHGDELAA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 276 MLFSSGTTrekgKKPKRILHTHGGVLAQ---ICKEVGFgfdcKEDDVFywmtnfgWMMAPWEIVGALHFGATLVCFEGAP 352
Cdd:PRK06087 192 VLFTSGTE----GLPKGVMLTHNNILASeraYCARLNL----TWQDVF-------MMPAPLGHATGFLHGVTAPFLIGAR 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 353 SYP----KPDRIFGIIERYKVS-IFGSTPgFIAGLRkNHISGDDFNLSSLR--------------------------ILG 401
Cdd:PRK06087 257 SVLldifTPDACLALLEQQRCTcMLGATP-FIYDLL-NLLEKQPADLSALRfflcggttipkkvarecqqrgikllsVYG 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 402 STGSILFS-----ENWEWFFSVFGKGkcpinniIGGTEmLGCFAQNLPNIPCkiGSVG--------VFalgMGgdIFNEK 468
Cdd:PRK06087 335 STESSPHAvvnldDPLSRFMHTDGYA-------AAGVE-IKVVDEARKTLPP--GCEGeeasrgpnVF---MG--YLDEP 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 469 gesvrRETGRVVcthpfpsmtrgfyaDEEGYqetYFSafrgvwahGDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIE 548
Cdd:PRK06087 400 -----ELTARAL--------------DEEGW---YYS--------GDLCRMDEAGYIKITGRKKDIIVRGGENISSREVE 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 549 SALIGFRaaefRVMEAIAVGIPDKNSENKIICFVILEGQDRlTETDEAALRSVVADIVNPQAKPERIFAIKELPRNAAAK 628
Cdd:PRK06087 450 DILLQHP----KIHDACVVAMPDERLGERSCAYVVLKAPHH-SLTLEEVVAFFSRKRVAKYKYPEHIVVIDKLPRTASGK 524
|
.
gi 1277171962 629 V 629
Cdd:PRK06087 525 I 525
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
113-634 |
1.24e-23 |
|
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: 104.25 E-value: 1.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 113 RAITFWQLKLLVDTIASAMKAHGIGKGDFVGMCMPISIDSIAVMFACFKIGAVCMQMAPTTSTDGTKDIVDhvrIARAKM 192
Cdd:cd05945 15 RTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIREILD---AAKPAL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 193 FFMADSysyggknftlekihqgvsdifsvrhivvfendaphspfspfvfgkkemrsvfwddfckqgkstiartercnaeD 272
Cdd:cd05945 92 LIADGD-------------------------------------------------------------------------D 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 273 VALMLFSSGTTrekGKkPKRILHTHGGVLAQICKEVGFgFDCKEDDVFYWMTNFGWMMAPWEIVGALHFGATLVCFegap 352
Cdd:cd05945 99 NAYIIFTSGST---GR-PKGVQISHDNLVSFTNWMLSD-FPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPV---- 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 353 syPK-----PDRIFGIIERYKVSIFGSTPGFIAGLRKNhisgDDFN---LSSLRilgstgSILFS---------ENWEWF 415
Cdd:cd05945 170 --PRdatadPKQLFRFLAEHGITVWVSTPSFAAMCLLS----PTFTpesLPSLR------HFLFCgevlphktaRALQQR 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 416 FSvfgkgKCPINNIIGGTE-MLGCFAQNLPN-IPCKIGSVGV-FAL-GMGGDIFNEKGESVRR-ETGRVVCTHPfpSMTR 490
Cdd:cd05945 238 FP-----DARIYNTYGPTEaTVAVTYIEVTPeVLDGYDRLPIgYAKpGAKLVILDEDGRPVPPgEKGELVISGP--SVSK 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 491 GFYADEEGYQETYFSaFRGVWAH--GDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIESALigfRAAEFrVMEAIAVG 568
Cdd:cd05945 311 GYLNNPEKTAAAFFP-DEGQRAYrtGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAAL---RQVPG-VKEAVVVP 385
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1277171962 569 IPDKNSENKIICFVILEGQDrlTETDEAALRSVVADIVNPQAKPERIFAIKELPRNAAAKVPYKAI 634
Cdd:cd05945 386 KYKGEKVTELIAFVVPKPGA--EAGLTKAIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
91-629 |
3.86e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 103.47 E-value: 3.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 91 RNIARGLGSKVCVCYEHesgkkRAITFWQLKLLVDTIASAMKAHGIGKGDFVGMCMPISIDSIAVMFACFKIGAVcmqMA 170
Cdd:PRK08316 18 RRSARRYPDKTALVFGD-----RSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAV---HV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 171 PTTSTDGTKD---IVDHvriARAKMFFmADSYSYGgknfTLEKIHQGVSDIFSVRHIVVFENDAPHSpfspfvfgkkemr 247
Cdd:PRK08316 90 PVNFMLTGEElayILDH---SGARAFL-VDPALAP----TAEAALALLPVDTLILSLVLGGREAPGG------------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 248 svfWDDFCK--QGKSTIARTERCNAEDVALMLFSSGTTrekgKKPKRILHTHGGVLAQIckeVGFGFDC--KEDDVF--- 320
Cdd:PRK08316 149 ---WLDFADwaEAGSVAEPDVELADDDLAQILYTSGTE----SLPKGAMLTHRALIAEY---VSCIVAGdmSADDIPlha 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 321 ---Y---WMTNFgwmMAPWeivgaLHFGATLVCFEGapsyPKPDRIFGIIERYKVSIFGSTPG-FIAGLRknHISGDDFN 393
Cdd:PRK08316 219 lplYhcaQLDVF---LGPY-----LYVGATNVILDA----PDPELILRTIEAERITSFFAPPTvWISLLR--HPDFDTRD 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 394 LSSLRILGSTGSILFSENWE---------WFFSVFGKGK-CPINNIIGGTEMLGcfaqnlpnipcKIGSVGVFALGMGGD 463
Cdd:PRK08316 285 LSSLRKGYYGASIMPVEVLKelrerlpglRFYNCYGQTEiAPLATVLGPEEHLR-----------RPGSAGRPVLNVETR 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 464 IFNEKGESVRR-ETGRVVctHPFPSMTRGFYADEEGYQEtyfsAFRGVWAH-GDFAEMDEDGFVFMRGRSDDIINKNGIK 541
Cdd:PRK08316 354 VVDDDGNDVAPgEVGEIV--HRSPQLMLGYWDDPEKTAE----AFRGGWFHsGDLGVMDEEGYITVVDRKKDMIKTGGEN 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 542 FSPANIESALIGFRAaefrVMEAIAVGIPDKNSENKIICFVILEGQDRLTetdEAALRSVVADIVNPQAKPERIFAIKEL 621
Cdd:PRK08316 428 VASREVEEALYTHPA----VAEVAVIGLPDPKWIEAVTAVVVPKAGATVT---EDELIAHCRARLAGFKVPKRVIFVDEL 500
|
....*...
gi 1277171962 622 PRNAAAKV 629
Cdd:PRK08316 501 PRNPSGKI 508
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
103-629 |
1.32e-22 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 102.05 E-value: 1.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 103 VCYEHESGKKRAITFWQLKLLVDTIASAMKAHGIGKGDFVGMCMPISIDSIAVMFACFKIGAVCMQMAPTTSTDGTKDIV 182
Cdd:PRK13295 44 TAVRLGTGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFML 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 183 DHvriARAKMFFMADSYsyggKNFTLEKIHQGV-SDIFSVRHIVVFENDAPHSpFSPFVFGKKemrsvfWDDfcKQGKST 261
Cdd:PRK13295 124 KH---AESKVLVVPKTF----RGFDHAAMARRLrPELPALRHVVVVGGDGADS-FEALLITPA------WEQ--EPDAPA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 262 IARTERCNAEDVALMLFSSGTTREkgkkPKRILHTHGGVLAQICKEVGfGFDCKEDDVFYW------MTNFGW-MMAPwe 334
Cdd:PRK13295 188 ILARLRPGPDDVTQLIYTSGTTGE----PKGVMHTANTLMANIVPYAE-RLGLGADDVILMaspmahQTGFMYgLMMP-- 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 335 ivgaLHFGATLVCFEgapsYPKPDRIFGIIERYKVSI-FGSTPgFIAGLrKNHISGDDFNLSSLRILGSTGS----ILFS 409
Cdd:PRK13295 261 ----VMLGATAVLQD----IWDPARAAELIRTEGVTFtMASTP-FLTDL-TRAVKESGRPVSSLRTFLCAGApipgALVE 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 410 ENWEwffsVFGKgkcpinNIIGGTEMLGCFAQNL--PNIPCK--IGSVGVFALGMGGDIFNEKGESVRR-ETGRVVCTHP 484
Cdd:PRK13295 331 RARA----ALGA------KIVSAWGMTENGAVTLtkLDDPDEraSTTDGCPLPGVEVRVVDADGAPLPAgQIGRLQVRGC 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 485 F--------PSMTRgfyADEEGYQETyfsafrgvwahGDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIESALigFRA 556
Cdd:PRK13295 401 SnfggylkrPQLNG---TDADGWFDT-----------GDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALL--YRH 464
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1277171962 557 AEfrVMEAIAVGIPDKNSENKIICFVILE-GQdrlTETDEAALRSVVADIVNPQAKPERIFAIKELPRNAAAKV 629
Cdd:PRK13295 465 PA--IAQVAIVAYPDERLGERACAFVVPRpGQ---SLDFEEMVEFLKAQKVAKQYIPERLVVRDALPRTPSGKI 533
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
113-629 |
1.61e-22 |
|
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: 100.83 E-value: 1.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 113 RAITFWQLKLLVDTIASAMKAHGIGKGDFVGMCMPISIDSIAVMFACFKIGAVCMQMAPTTSTDGTKDIVDHvriARAKM 192
Cdd:cd05934 2 RRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDH---SGAQL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 193 ffmadsysyggknftlekihqgvsdifsvrhIVVfendaphspfspfvfgkkemrsvfwddfckqgkstiartercnaeD 272
Cdd:cd05934 79 -------------------------------VVV---------------------------------------------D 82
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 273 VALMLFSSGTTrekgKKPKRILHTH------GGVLAQickevgfGFDCKEDDVFYWMTNFGWMMA-PWEIVGALHFGATL 345
Cdd:cd05934 83 PASILYTSGTT----GPPKGVVITHanltfaGYYSAR-------RFGLGEDDVYLTVLPLFHINAqAVSVLAALSVGATL 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 346 VCfegAPSYpKPDRIFGIIERYKVSIFGSTPGFIAGLRKNHISGDDfNLSSLRILGSTGSIlfSENWEWFFSVFGkgkCP 425
Cdd:cd05934 152 VL---LPRF-SASRFWSDVRRYGATVTNYLGAMLSYLLAQPPSPDD-RAHRLRAAYGAPNP--PELHEEFEERFG---VR 221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 426 INNIIGGTEMLGCFAQNLPNiPCKIGSVGVFALGMGGDIFNEKGESVRR-ETGR-VVCTHPFPSMTRGFYADEEGYQEty 503
Cdd:cd05934 222 LLEGYGMTETIVGVIGPRDE-PRRPGSIGRPAPGYEVRIVDDDGQELPAgEPGElVIRGLRGWGFFKGYYNMPEATAE-- 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 504 fsAFRGVWAH-GDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIESALIGFRAaefrVMEAIAVGIPDKNSENKIICFV 582
Cdd:cd05934 299 --AMRNGWFHtGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPA----VREAAVVAVPDEVGEDEVKAVV 372
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1277171962 583 ILEGQDRLTETD-EAALRSVVAdivnPQAKPERIFAIKELPRNAAAKV 629
Cdd:cd05934 373 VLRPGETLDPEElFAFCEGQLA----YFKVPRYIRFVDDLPKTPTEKV 416
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
106-568 |
2.63e-22 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 101.72 E-value: 2.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 106 EHESGKKRAITFWQLKLLVDTIASAMKAHGIGKGDFVGMCMPISIDSIAVMFACFKIGAVCMQMAPTTSTDGTKDIVDHv 185
Cdd:COG1022 32 EKEDGIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVPIYPTSSAEEVAYILND- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 186 riARAKMFFMADSysyggknFTLEKIHQGVSDIFSVRHIVVFENDAPHSPFspfvfgkkemRSVFWDDFCKQGKSTI--- 262
Cdd:COG1022 111 --SGAKVLFVEDQ-------EQLDKLLEVRDELPSLRHIVVLDPRGLRDDP----------RLLSLDELLALGREVAdpa 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 263 ---ARTERCNAEDVALMLFSSGTTrekGkKPKRILHTHGGVLAQI--CKEVgfgFDCKEDDVFY------WMtnFGWMMA 331
Cdd:COG1022 172 eleARRAAVKPDDLATIIYTSGTT---G-RPKGVMLTHRNLLSNAraLLER---LPLGPGDRTLsflplaHV--FERTVS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 332 pweiVGALHFGATLVCFEG-----------APSY----PkpdRIF-----GIIER------YKVSIF------------- 372
Cdd:COG1022 243 ----YYALAAGATVAFAESpdtlaedlrevKPTFmlavP---RVWekvyaGIQAKaeeaggLKRKLFrwalavgrryara 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 373 ---GSTPGFiaGLRKNHISGDDFNLSSLR-ILGS------TGSILFSENWEWFFSVFGkgkcpInNII---GGTEMLGCF 439
Cdd:COG1022 316 rlaGKSPSL--LLRLKHALADKLVFSKLReALGGrlrfavSGGAALGPELARFFRALG-----I-PVLegyGLTETSPVI 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 440 AQNLPNIPcKIGSVGVFALGMggdifnekgeSVRR-ETGRVVCTHpfPSMTRGFYADEEGYQETyFSAfRGvWAH-GDFA 517
Cdd:COG1022 388 TVNRPGDN-RIGTVGPPLPGV----------EVKIaEDGEILVRG--PNVMKGYYKNPEATAEA-FDA-DG-WLHtGDIG 451
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1277171962 518 EMDEDGFVFMRGRSDDII-NKNGIKFSPANIESALIGFRAAEfrvmEAIAVG 568
Cdd:COG1022 452 ELDEDGFLRITGRKKDLIvTSGGKNVAPQPIENALKASPLIE----QAVVVG 499
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
272-629 |
1.11e-21 |
|
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: 97.17 E-value: 1.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 272 DVALMLFSSGTTrekgKKPKRILHTHGGVLAQiCKEVGFGFDCKEDDV-FYWMTNFGWMMAPWEIVGALHFGATLVcFEG 350
Cdd:cd05944 3 DVAAYFHTGGTT----GTPKLAQHTHSNEVYN-AWMLALNSLFDPDDVlLCGLPLFHVNGSVVTLLTPLASGAHVV-LAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 351 APSYPKP---DRIFGIIERYKVSIFGSTPGFIAGLRKNHISGDdfnLSSLRILGSTGSILFSEnwewFFSVF-GKGKCPI 426
Cdd:cd05944 77 PAGYRNPglfDNFWKLVERYRITSLSTVPTVYAALLQVPVNAD---ISSLRFAMSGAAPLPVE----LRARFeDATGLPV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 427 NNIIGGTEMLGCFAQNLPNIPCKIGSVGVFALGMGGDIFNEKGES--VRR----ETGRVVCTHP--FPSMTrgfyadeeg 498
Cdd:cd05944 150 VEGYGLTEATCLVAVNPPDGPKRPGSVGLRLPYARVRIKVLDGVGrlLRDcapdEVGEICVAGPgvFGGYL--------- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 499 YQETYFSAF-RGVWAH-GDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIESALIGFRAAEFrvmeAIAVGIPDKNSEN 576
Cdd:cd05944 221 YTEGNKNAFvADGWLNtGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAF----AGAVGQPDAHAGE 296
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1277171962 577 KIICFVILEgqdRLTETDEAALRSVVADIVNPQAK-PERIFAIKELPRNAAAKV 629
Cdd:cd05944 297 LPVAYVQLK---PGAVVEEEELLAWARDHVPERAAvPKHIEVLEELPVTAVGKV 347
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
115-629 |
2.89e-21 |
|
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: 96.78 E-value: 2.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 115 ITFWQLKLLVDTIASAMKAHGIGKGDFVGMCMPISIDSIAVMFACFKIGAVCMQMAPTTSTdgtkdivdhvriaRAKMFF 194
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKE-------------RELEYI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 195 MADSYSyggknftlekihqgvsdifsvrhivvfendaphspfspfvfgkkemrsvfwddfckqgKSTIARTERcnaEDVA 274
Cdd:cd05935 69 LNDSGA----------------------------------------------------------KVAVVGSEL---DDLA 87
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 275 LMLFSSGTTrekgKKPKRILHTHGGVLAQ-ICKEVGFGFDCKEDDV----FYWMTNF-GWMMAPweivgaLHFGATLVCF 348
Cdd:cd05935 88 LIPYTSGTT----GLPKGCMHTHFSAAANaLQSAVWTGLTPSDVILaclpLFHVTGFvGSLNTA------VYVGGTYVLM 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 349 egapSYPKPDRIFGIIERYKVSIFGSTPGFIAGLRkNHISGDDFNLSSLRILGSTGSILFSENWEWFFSVFGkgkCPINN 428
Cdd:cd05935 158 ----ARWDRETALELIEKYKVTFWTNIPTMLVDLL-ATPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTG---LRFVE 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 429 IIGGTEMLGCFAQNLPNIPcKIGSVGVFALGMGGDIFN-EKGESVR-RETGRVVCTHPfpSMTRGFYADEEGYQETYFSA 506
Cdd:cd05935 230 GYGLTETMSQTHTNPPLRP-KLQCLGIP*FGVDARVIDiETGRELPpNEVGEIVVRGP--QIFKGYWNRPEETEESFIEI 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 507 -----FRGvwahGDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIESALIGFRAaefrVMEAIAVGIPDKNSENKIICF 581
Cdd:cd05935 307 kgrrfFRT----GDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPA----I*EVCVISVPDERVGEEVKAF 378
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1277171962 582 VILEGQDRLTETDEAALRSVVADIVNPQAKPERIFaIKELPRNAAAKV 629
Cdd:cd05935 379 IVLRPEYRGKVTEEDIIEWAREQMAAYKYPREVEF-VDELPRSASGKI 425
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
116-629 |
7.24e-20 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 93.68 E-value: 7.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 116 TFWQLKLLVDTIASAMKAHGIGKGDFVGMCMPISIDSIAVMFACFKIGAVCMQMAPTTSTDGTKDIVDHvriARAKMFFM 195
Cdd:PRK12583 47 TWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQ---SGVRWVIC 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 196 ADSYSYGGKNFTLEKIHQGVS----------DIFSVRHIVVFE-NDAPHSpfspfvfgkkemrsVFWDDFCKQGKSTI-- 262
Cdd:PRK12583 124 ADAFKTSDYHAMLQELLPGLAegqpgalaceRLPELRGVVSLApAPPPGF--------------LAWHELQARGETVSre 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 263 ---ARTERCNAEDVALMLFSSGTTrekgKKPKRILHTHGGVL---AQICKEVGFGfdckEDDV------FYWMtnFGWMM 330
Cdd:PRK12583 190 alaERQASLDRDDPINIQYTSGTT----GFPKGATLSHHNILnngYFVAESLGLT----EHDRlcvpvpLYHC--FGMVL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 331 ApweIVGALHFGATLVcfegapsYP----KPDRIFGIIERYK-VSIFGSTPGFIAGLrkNHISGDDFNLSSLR---ILGS 402
Cdd:PRK12583 260 A---NLGCMTVGACLV-------YPneafDPLATLQAVEEERcTALYGVPTMFIAEL--DHPQRGNFDLSSLRtgiMAGA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 403 TGSIlfsenwEWFFSVFGKGKCPINNI-IGGTEMLGCFAQNLPN--IPCKIGSVGVFALGMGGDIFNEKGESVRR-ETGR 478
Cdd:PRK12583 328 PCPI------EVMRRVMDEMHMAEVQIaYGMTETSPVSLQTTAAddLERRVETVGRTQPHLEVKVVDPDGATVPRgEIGE 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 479 VvCTHPFPSMtRGFYADEEGYQEtyfSAFRGVWAH-GDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIESALIGFRAa 557
Cdd:PRK12583 402 L-CTRGYSVM-KGYWNNPEATAE---SIDEDGWMHtGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPA- 475
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1277171962 558 efrVMEAIAVGIPDKNSENKIICFVILEGQDRLTETDeaaLRSVVADIVNPQAKPERIFAIKELPRNAAAKV 629
Cdd:PRK12583 476 ---VADVQVFGVPDEKYGEEIVAWVRLHPGHAASEEE---LREFCKARIAHFKVPRYFRFVDEFPMTVTGKV 541
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
105-638 |
1.17e-19 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 93.48 E-value: 1.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 105 YEHESGKKRA---ITFWQLKLLVDTIASAMKAHGIGKGDFVGMCMPISIDSIAVMFACFKIGAVCmQMAPTTSTDgtkDI 181
Cdd:PRK07529 46 FLLDADPLDRpetWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAGIAN-PINPLLEPE---QI 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 182 VDHVRIARAKM------FFMADsysyggknfTLEKIHQGVSDIFSVRHIV-VFENDA---PHSPFSPFVFGKKEMRSVFW 251
Cdd:PRK07529 122 AELLRAAGAKVlvtlgpFPGTD---------IWQKVAEVLAALPELRTVVeVDLARYlpgPKRLAVPLIRRKAHARILDF 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 252 DDFCKQGKSTIARTER-CNAEDVALMLFSSGTTrekGKkPKRILHTHGGVLAQiCKEVGFGFDCKEDDV-------FYWM 323
Cdd:PRK07529 193 DAELARQPGDRLFSGRpIGPDDVAAYFHTGGTT---GM-PKLAQHTHGNEVAN-AWLGALLLGLGPGDTvfcglplFHVN 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 324 TNFGWMMAPweivgaLHFGATLVcFEGAPSYPKP---DRIFGIIERYKVSIFGSTPGFIAGLRKNHISGDDfnLSSLRIL 400
Cdd:PRK07529 268 ALLVTGLAP------LARGAHVV-LATPQGYRGPgviANFWKIVERYRINFLSGVPTVYAALLQVPVDGHD--ISSLRYA 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 401 GSTGSILFSENWEWFFSVFGkgkCPINNIIGGTEMLGCFAQNLPNIPCKIGSVG---------VFALGMGGDIFNEkgeS 471
Cdd:PRK07529 339 LCGAAPLPVEVFRRFEAATG---VRIVEGYGLTEATCVSSVNPPDGERRIGSVGlrlpyqrvrVVILDDAGRYLRD---C 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 472 VRRETGRVVCTHP--FPSMTR-----GFYADEeGYQETyfsafrgvwahGDFAEMDEDGFVFMRGRSDDIINKNGIKFSP 544
Cdd:PRK07529 413 AVDEVGVLCIAGPnvFSGYLEaahnkGLWLED-GWLNT-----------GDLGRIDADGYFWLTGRAKDLIIRGGHNIDP 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 545 ANIESALIGFRAaefrVMEAIAVGIPDKNSENKIICFVIL-EGqdrlTETDEAALRSVVAD-IVNPQAKPERIFAIKELP 622
Cdd:PRK07529 481 AAIEEALLRHPA----VALAAAVGRPDAHAGELPVAYVQLkPG----ASATEAELLAFARDhIAERAAVPKHVRILDALP 552
|
570 580
....*....|....*....|..
gi 1277171962 623 RNAAAKvPYK------AISRVF 638
Cdd:PRK07529 553 KTAVGK-IFKpalrrdAIRRVL 573
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
94-634 |
2.44e-19 |
|
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: 91.62 E-value: 2.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 94 ARGLGSKVCVCyehesGKKRAITFWQLKLLVDTIASAMKAHGIGKGDFVGMCMPISIDSIAVMFACFKIGAVCMQMAPTT 173
Cdd:cd05920 25 AARHPDRIAVV-----DGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVLALPSH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 174 STdgtKDIVDHVRIARAKMFFMADSysyggknftlekihqgvsdifsvrhivvfendapHSPFSPfvfgkkemrsvfwdd 253
Cdd:cd05920 100 RR---SELSAFCAHAEAVAYIVPDR----------------------------------HAGFDH--------------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 254 fckqgkSTIARTERCNAEDVALMLFSSGTTrekgKKPKRILHTHGGVL------AQICkevgfGFDckEDDVfYWMTN-- 325
Cdd:cd05920 128 ------RALARELAESIPEVALFLLSGGTT----GTPKLIPRTHNDYAynvrasAEVC-----GLD--QDTV-YLAVLpa 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 326 -FGWMMAPWEIVGALHFGATLVCfegAPSyPKPDRIFGIIERYKVSIFGSTPGfIAGLRKNHISGDDFNLSSLRILGSTG 404
Cdd:cd05920 190 aHNFPLACPGVLGTLLAGGRVVL---APD-PSPDAAFPLIEREGVTVTALVPA-LVSLWLDAAASRRADLSSLRLLQVGG 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 405 SILFSENWEWFFSVFGkgkCPINNIIGGTEMLGCF------------AQNLPNIPckigsvgvfalgmgGD---IFNEKG 469
Cdd:cd05920 265 ARLSPALARRVPPVLG---CTLQQVFGMAEGLLNYtrlddpdeviihTQGRPMSP--------------DDeirVVDEEG 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 470 ESVRR-ETGRVVCTHPFpsMTRGFYADEEgYQETYFSAfRGVWAHGDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIE 548
Cdd:cd05920 328 NPVPPgEEGELLTRGPY--TIRGYYRAPE-HNARAFTP-DGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVE 403
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 549 SALIGFRAaefrVMEAIAVGIPDKNSENKIICFVILEGQdrltETDEAALRSVVADIVNPQAK-PERIFAIKELPRNAAA 627
Cdd:cd05920 404 NLLLRHPA----VHDAAVVAMPDELLGERSCAFVVLRDP----PPSAAQLRRFLRERGLAAYKlPDRIEFVDSLPLTAVG 475
|
....*..
gi 1277171962 628 KVPYKAI 634
Cdd:cd05920 476 KIDKKAL 482
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
132-629 |
2.62e-19 |
|
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: 91.76 E-value: 2.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 132 KAHGIGKGDFVGMCMPISIDSIAVMFACFKIGAVCMqmaPTTSTDGTKDIVDHVRIARAKMFFMADSYSYGGKNFTLEki 211
Cdd:cd05928 60 GACGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFI---PGTIQLTAKDILYRLQASKAKCIVTSDELAPEVDSVASE-- 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 212 hqgvSDIFSVRHIVvfendAPHSPFSPFVFgKKEMRSVFWDDFCKQGKStiartercnaEDVALMLFSSGTTrekgKKPK 291
Cdd:cd05928 135 ----CPSLKTKLLV-----SEKSRDGWLNF-KELLNEASTEHHCVETGS----------QEPMAIYFTSGTT----GSPK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 292 RILHTHGGVLAQICKEVGFGFDCKEDDVFYWMTNFGW-------MMAPWeIVGALHFGATLVCFEgapsypkPDRIFGII 364
Cdd:cd05928 191 MAEHSHSSLGLGLKVNGRYWLDLTASDIMWNTSDTGWiksawssLFEPW-IQGACVFVHHLPRFD-------PLVILKTL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 365 ERYKVSIFGSTPGFIAGLRKNHISGDDFnlSSLRILGSTGSILFSENWEWFFSVFGkgkCPINNIIGGTEMlGCFAQNLP 444
Cdd:cd05928 263 SSYPITTFCGAPTVYRMLVQQDLSSYKF--PSLQHCVTGGEPLNPEVLEKWKAQTG---LDIYEGYGQTET-GLICANFK 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 445 NIPCKIGSVGVFALGMGGDIFNEKGESVRRETG-----RVVCTHPFpsmtrGFYADEEGYQETYFSAFRG-VWAHGDFAE 518
Cdd:cd05928 337 GMKIKPGSMGKASPPYDVQIIDDNGNVLPPGTEgdigiRVKPIRPF-----GLFSGYVDNPEKTAATIRGdFYLTGDRGI 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 519 MDEDGFVFMRGRSDDIINKNGIKFSPANIESALIGFRAaefrVMEAIAVGIPDKNSENKIICFVILEGQ------DRLTE 592
Cdd:cd05928 412 MDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPA----VVESAVVSSPDPIRGEVVKAFVVLAPQflshdpEQLTK 487
|
490 500 510
....*....|....*....|....*....|....*..
gi 1277171962 593 TDEAALRSVVAdivnPQAKPERIFAIKELPRNAAAKV 629
Cdd:cd05928 488 ELQQHVKSVTA----PYKYPRKVEFVQELPKTVTGKI 520
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
271-629 |
2.93e-19 |
|
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: 89.63 E-value: 2.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 271 EDVALMLFSSGTTREkgkkPKRILHTHGGVLAQICKEVGFGFDCKEDDVFYWMTNFGWMMAPWEIVGALHFGATLVCFEG 350
Cdd:cd17635 1 EDPLAVIFTSGTTGE----PKAVLLANKTFFAVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 351 APSYPKpdrIFGIIERYKVSIFGSTP---GFIAGLRKNHISgddfNLSSLRILGSTGSILF---SENWEWFfsvfgkGKC 424
Cdd:cd17635 77 NTTYKS---LFKILTTNAVTTTCLVPtllSKLVSELKSANA----TVPSLRLIGYGGSRAIaadVRFIEAT------GLT 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 425 PINNIIGGTEMLGCFAQNLPNIPCKIGSVGVFALGMGGDIFNEKG-ESVRRETGRVVCTHPfpSMTRGFYADEEGYQETY 503
Cdd:cd17635 144 NTAQVYGLSETGTALCLPTDDDSIEINAVGRPYPGVDVYLAATDGiAGPSASFGTIWIKSP--ANMLGYWNNPERTAEVL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 504 FsafrGVWAH-GDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIESALIGFRAaefrVMEAIAVGIPDKNSENKIICFV 582
Cdd:cd17635 222 I----DGWVNtGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSG----VQECACYEISDEEFGELVGLAV 293
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1277171962 583 ILEGQDrltetDEAALRSVVADI---VNPQAKPERIFAIKELPRNAAAKV 629
Cdd:cd17635 294 VASAEL-----DENAIRALKHTIrreLEPYARPSTIVIVTDIPRTQSGKV 338
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
114-638 |
3.85e-19 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 91.44 E-value: 3.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 114 AITFWQLKLLVDTIASAM-KAHGIGKGDFVGMCMPISIDSIAVMFACFKIGAVCMQMAPTTSTdgtKDIVDHVRIARAKM 192
Cdd:PLN02574 66 SISYSELQPLVKSMAAGLyHVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSL---GEIKKRVVDCSVGL 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 193 FFMADSysyggknfTLEKIHQ-GVSdIFSVRHIVVFENDAPHspFSPFvfgkkemRSVFWDDFCKQGKSTIartercNAE 271
Cdd:PLN02574 143 AFTSPE--------NVEKLSPlGVP-VIGVPENYDFDSKRIE--FPKF-------YELIKEDFDFVPKPVI------KQD 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 272 DVALMLFSSGTT-REKGkkpkrILHTHGGVLAQICKEVGFGFDCKE----DDVF---------YWMTNFgwmmapweIVG 337
Cdd:PLN02574 199 DVAAIMYSSGTTgASKG-----VVLTHRNLIAMVELFVRFEASQYEypgsDNVYlaalpmfhiYGLSLF--------VVG 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 338 ALHFGATLVCFEgapSYPKPDRIfGIIERYKVSIFGSTPGFIAGLRKNHISGDDFNLSSLRILGSTGSILFSENWEWFFS 417
Cdd:PLN02574 266 LLSLGSTIVVMR---RFDASDMV-KVIDRFKVTHFPVVPPILMALTKKAKGVCGEVLKSLKQVSCGAAPLSGKFIQDFVQ 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 418 VFgkgkcPINNIIGGTEM-----LGCFAQNLPNIPcKIGSVGVFALGMGGDIFNEKGESVRRETGRVVCTHPFPSMTRGF 492
Cdd:PLN02574 342 TL-----PHVDFIQGYGMtestaVGTRGFNTEKLS-KYSSVGLLAPNMQAKVVDWSTGCLLPPGNCGELWIQGPGVMKGY 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 493 YADEEGyqeTYFSAFRGVWAH-GDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIESALIgfraAEFRVMEAIAVGIPD 571
Cdd:PLN02574 416 LNNPKA---TQSTIDKDGWLRtGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLI----SHPEIIDAAVTAVPD 488
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1277171962 572 KNSENKIICFVILEGQDRLTETdeaALRSVVADIVNPQAKPERIFAIKELPRNAAAKVPYKAISRVF 638
Cdd:PLN02574 489 KECGEIPVAFVVRRQGSTLSQE---AVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELKRSL 552
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
271-634 |
8.72e-19 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 89.81 E-value: 8.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 271 EDVALMLFSSGTTrekgKKPKRILHTHGGVL--AQICKEVgfgFDCKEDDVFYWMTNFGWMMAPWEIVGALHFGATLVCf 348
Cdd:cd05922 117 EDLALLLYTSGST----GSPKLVRLSHQNLLanARSIAEY---LGITADDRALTVLPLSYDYGLSVLNTHLLRGATLVL- 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 349 egAPSYPKPDRIFGIIERYKVSIFGSTPGFIAGLRKnhISGDDFNLSSLRILGSTGSILFSENWEWFFSVFGKGKcpINN 428
Cdd:cd05922 189 --TNDGVLDDAFWEDLREHGATGLAGVPSTYAMLTR--LGFDPAKLPSLRYLTQAGGRLPQETIARLRELLPGAQ--VYV 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 429 IIGGTEmlgCFAQN--LP--NIPCKIGSVGVFALGMGGDIFNEKG-ESVRRETGRVVCTHPFPSMTrgfYADEEGYqETY 503
Cdd:cd05922 263 MYGQTE---ATRRMtyLPpeRILEKPGSIGLAIPGGEFEILDDDGtPTPPGEPGEIVHRGPNVMKG---YWNDPPY-RRK 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 504 FSAFRGVWAHGDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIESALigfrAAEFRVMEAIAVGIPDKNSEnKIICFVI 583
Cdd:cd05922 336 EGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAA----RSIGLIIEAAAVGLPDPLGE-KLALFVT 410
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1277171962 584 LEGQDrltetDEAALRSVVADIVNPQAKPERIFAIKELPRNAAAKVPYKAI 634
Cdd:cd05922 411 APDKI-----DPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAAL 456
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
133-400 |
1.86e-18 |
|
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: 88.09 E-value: 1.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 133 AHGIGKGDFVGMCMPISIDSIAVMFACFKIGAVCMQMAPTTSTDgtkdivdhvRIArakmFFMADSysyggknftlekih 212
Cdd:TIGR01733 19 AGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAE---------RLA----FILEDA-------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 213 qgvsdifSVRHIVVfenDAPHSPFSPFVFGKKEMRSVFWDDFCKQGKSTIARTERCNAEDVALMLFSSGTTrekGKkPKR 292
Cdd:TIGR01733 72 -------GARLLLT---DSALASRLAGLVLPVILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGST---GR-PKG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 293 ILHTHGGVLAQICKEVGFgFDCKEDDVFYWMTNFGWMMAPWEIVGALHFGATLVCFEGAPSYPKPDRIFGIIERYKVSIF 372
Cdd:TIGR01733 138 VVVTHRSLVNLLAWLARR-YGLDPDDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLAALIAEHPVTVL 216
|
250 260
....*....|....*....|....*...
gi 1277171962 373 GSTPGFIAGLrknhISGDDFNLSSLRIL 400
Cdd:TIGR01733 217 NLTPSLLALL----AAALPPALASLRLV 240
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
94-634 |
4.24e-18 |
|
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: 88.07 E-value: 4.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 94 ARGLGSKVCVCYEHESGKKRAiTFWQLKLLVDTIASAMKAHGIGKGDFVGMCMPISIDSIAVMFACFKIGAVCMQMAPTT 173
Cdd:cd12119 6 ARLHGDREIVSRTHEGEVHRY-TYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 174 STDGTKDIVDHvriARAKMFFMADSYSYggknfTLEKIhqgVSDIFSVRHIVVFENDAPHSPFSPfvfgkkeMRSVFWDD 253
Cdd:cd12119 85 FPEQIAYIINH---AEDRVVFVDRDFLP-----LLEAI---APRLPTVEHVVVMTDDAAMPEPAG-------VGVLAYEE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 254 FCKQGkSTIARTERCNAEDVALMLFSSGTTrekGKkPK------R--ILHTHGGVLAQickevgfGFDCKEDDVFYWMTN 325
Cdd:cd12119 147 LLAAE-SPEYDWPDFDENTAAAICYTSGTT---GN-PKgvvyshRslVLHAMAALLTD-------GLGLSESDVVLPVVP 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 326 F----GWMMApweiVGALHFGATLVcFEGApsYPKPDRIFGIIERYKVSIFGSTPGFIAGLRkNHISGDDFNLSSLRILG 401
Cdd:cd12119 215 MfhvnAWGLP----YAAAMVGAKLV-LPGP--YLDPASLAELIEREGVTFAAGVPTVWQGLL-DHLEANGRDLSSLRRVV 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 402 STGSILFSENWEWFFSvfgKGkCPINNIIGGTEM--LGCFAQ------NLP-----NIPCKIGsvgVFALGMGGDIFNEK 468
Cdd:cd12119 287 IGGSAVPRSLIEAFEE---RG-VRVIHAWGMTETspLGTVARppsehsNLSedeqlALRAKQG---RPVPGVELRIVDDD 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 469 GESVRR---ETGRVVCTHPFpsMTRGFYADEEGYQETyfsaFRGVWAH-GDFAEMDEDGFVFMRGRSDDIINKNGIKFSP 544
Cdd:cd12119 360 GRELPWdgkAVGELQVRGPW--VTKSYYKNDEESEAL----TEDGWLRtGDVATIDEDGYLTITDRSKDVIKSGGEWISS 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 545 ANIESALIGFRAaefrVMEAIAVGIPD-KNSENKIICFVILEGQDrlteTDEAALRSVVADIVNPQAKPERIFAIKELPR 623
Cdd:cd12119 434 VELENAIMAHPA----VAEAAVIGVPHpKWGERPLAVVVLKEGAT----VTAEELLEFLADKVAKWWLPDDVVFVDEIPK 505
|
570
....*....|.
gi 1277171962 624 NAAAKVPYKAI 634
Cdd:cd12119 506 TSTGKIDKKAL 516
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
113-571 |
4.64e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 88.09 E-value: 4.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 113 RAITFWQLKLLVDTIASAMKAH-GIGKGDFVGMCMPISIDSIAVMFACFKIGAVCMQMAPTTSTDGTKDIV-DhvriARA 190
Cdd:PRK08314 34 RAISYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVtD----SGA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 191 KMFFMADSYsyggknftLEKIHQGVSDIfSVRHIVV------FENDAPHSP-----FSPFVFGKKEMRSVFWDDFCKQGK 259
Cdd:PRK08314 110 RVAIVGSEL--------APKVAPAVGNL-RLRHVIVaqysdyLPAEPEIAVpawlrAEPPLQALAPGGVVAWKEALAAGL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 260 STIARTERcnAEDVALMLFSSGTTrekgKKPKRILHTHGGVLAQIckeVGFG--FDCKEDDV------FYWMTNF-GWMM 330
Cdd:PRK08314 181 APPPHTAG--PDDLAVLPYTSGTT----GVPKGCMHTHRTVMANA---VGSVlwSNSTPESVvlavlpLFHVTGMvHSMN 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 331 APweivgaLHFGATLVCFegapsyPKPDRIFG--IIERYKVSIFGSTPGFIAGLRKN-HIsgDDFNLSSLRILGSTGSIL 407
Cdd:PRK08314 252 AP------IYAGATVVLM------PRWDREAAarLIERYRVTHWTNIPTMVVDFLASpGL--AERDLSSLRYIGGGGAAM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 408 FSENWEWFFSVFGkgkcpINNI--IGGTEMLGCFAQNLPNIPcKIGSVGVFALGMGGDIFN-EKGESV-RRETGRVVcTH 483
Cdd:PRK08314 318 PEAVAERLKELTG-----LDYVegYGLTETMAQTHSNPPDRP-KLQCLGIPTFGVDARVIDpETLEELpPGEVGEIV-VH 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 484 PfPSMTRGFYADEEGYQETYFSA-----FRGvwahGDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIESALIGFRAae 558
Cdd:PRK08314 391 G-PQVFKGYWNRPEATAEAFIEIdgkrfFRT----GDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPA-- 463
|
490
....*....|...
gi 1277171962 559 frVMEAIAVGIPD 571
Cdd:PRK08314 464 --IQEACVIATPD 474
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
113-634 |
1.73e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 86.24 E-value: 1.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 113 RAITFWQLKLLVDTIASAMKAHGIGKGDFVGMCMPISIDSIAVMFACFKIGAVCMQMAPTTSTdgtKDIVDHVRIARAKM 192
Cdd:PRK06710 48 KDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTE---RELEYQLHDSGAKV 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 193 FFMADsysyggknFTLEKIhQGVSDIFSVRHIVVfENDAPHSPFS-----PFVFGKKEMRSV---------FWDDFCKQG 258
Cdd:PRK06710 125 ILCLD--------LVFPRV-TNVQSATKIEHVIV-TRIADFLPFPknllyPFVQKKQSNLVVkvsesetihLWNSVEKEV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 259 KSTIARTerCNAE-DVALMLFSSGTTrekgKKPKRILHTHGGVLAQICKEVGFGFDCKEDD-----VFYWMTNFGwMMAP 332
Cdd:PRK06710 195 NTGVEVP--CDPEnDLALLQYTGGTT----GFPKGVMLTHKNLVSNTLMGVQWLYNCKEGEevvlgVLPFFHVYG-MTAV 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 333 WEIVGALHFGATLVcfegapsyPKPDR--IFGIIERYKVSIFGSTPG-FIAGLRKNHISgdDFNLSSLRILGSTGSILFS 409
Cdd:PRK06710 268 MNLSIMQGYKMVLI--------PKFDMkmVFEAIKKHKVTLFPGAPTiYIALLNSPLLK--EYDISSIRACISGSAPLPV 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 410 ENWEWFFSVFGkGKcpINNIIGGTEMLGCFAQNL---PNIPckiGSVGVFALGMGGDIFN-EKGESVRR-ETGRVVCTHP 484
Cdd:PRK06710 338 EVQEKFETVTG-GK--LVEGYGLTESSPVTHSNFlweKRVP---GSIGVPWPDTEAMIMSlETGEALPPgEIGEIVVKGP 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 485 fpSMTRGFYADEEgyqETYfSAFRGVWAH-GDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIESALIGFRaaefRVME 563
Cdd:PRK06710 412 --QIMKGYWNKPE---ETA-AVLQDGWLHtGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHE----KVQE 481
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1277171962 564 AIAVGIPDKNSENKIICFVIL-EGQDRLTETDEAALRSVVADIVNPQAKPERifaiKELPRNAAAKVPYKAI 634
Cdd:PRK06710 482 VVTIGVPDPYRGETVKAFVVLkEGTECSEEELNQFARKYLAAYKVPKVYEFR----DELPKTTVGKILRRVL 549
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
113-634 |
1.89e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 85.86 E-value: 1.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 113 RAITFWQLKLLVDTIASAMKAHGIGKGDFVGMCMPISIDSIAVMFACFKIGAVcmqMAPT------------TSTDGTK- 179
Cdd:PRK07470 31 RSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAV---WVPTnfrqtpdevaylAEASGARa 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 180 -----DIVDHVRIARAKMFFMADSYSYGGKNFTLekihqgvsdifSVRHIVVFENDAPHSPfspfvfgkkemrsvfwddf 254
Cdd:PRK07470 108 michaDFPEHAAAVRAASPDLTHVVAIGGARAGL-----------DYEALVARHLGARVAN------------------- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 255 ckqgkstiARTERcnaEDVALMLFSSGTTrekgKKPKRILHTHGG----VLAQICKEVGfgfDCKEDDVfywmtnfGWMM 330
Cdd:PRK07470 158 --------AAVDH---DDPCWFFFTSGTT----GRPKAAVLTHGQmafvITNHLADLMP---GTTEQDA-------SLVV 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 331 APWEIVGALHF------GATLVCFegaPSYP-KPDRIFGIIERYKVSIFGSTPGfIAGLRKNHISGDDFNLSSLRILGST 403
Cdd:PRK07470 213 APLSHGAGIHQlcqvarGAATVLL---PSERfDPAEVWALVERHRVTNLFTVPT-ILKMLVEHPAVDRYDHSSLRYVIYA 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 404 GSILFSENWEWFFSVFGKgkcPINNIIGGTEMLGC---------FAQNLPNIpcKIGSVGVFALGMGGDIFNEKGESVRR 474
Cdd:PRK07470 289 GAPMYRADQKRALAKLGK---VLVQYFGLGEVTGNitvlppalhDAEDGPDA--RIGTCGFERTGMEVQIQDDEGRELPP 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 475 -ETGRV-VCThpfPSMTRGFYADEEGYQEtyfsAFRGVWAH-GDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIESAL 551
Cdd:PRK07470 364 gETGEIcVIG---PAVFAGYYNNPEANAK----AFRDGWFRtGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKL 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 552 IGFRAaefrVMEAIAVGIPD-KNSENKIICFVILEGQDrlteTDEAALRSVVADIVNPQAKPERIFAIKELPRNAAAKVP 630
Cdd:PRK07470 437 LTHPA----VSEVAVLGVPDpVWGEVGVAVCVARDGAP----VDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKIT 508
|
....
gi 1277171962 631 YKAI 634
Cdd:PRK07470 509 KKMV 512
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
113-629 |
2.86e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 85.48 E-value: 2.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 113 RAITFWQLKLLVDTIASAMKAHGIGKGDFVGMCMPISIDSIAVMFACFKIGAVCMQMAPTTStdgTKDIVDHVRIARAKM 192
Cdd:PRK06178 57 HVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFR---EHELSYELNDAGAEV 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 193 FFMADsysyggknfTLEKIHQGVSDIFSVRHIVV-----FENDAPHSPFSPFVFGKKEMRSVFWDDFCKQGKSTI-ARTE 266
Cdd:PRK06178 134 LLALD---------QLAPVVEQVRAETSLRHVIVtsladVLPAEPTLPLPDSLRAPRLAAAGAIDLLPALRACTApVPLP 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 267 RCNAEDVALMLFSSGTTrekgKKPKRILHTHGGVLAQICKEVGFGFDCKEDDVF------YWMT--NFGwMMAPweivga 338
Cdd:PRK06178 205 PPALDALAALNYTGGTT----GMPKGCEHTQRDMVYTAAAAYAVAVVGGEDSVFlsflpeFWIAgeNFG-LLFP------ 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 339 LHFGATLVCFegapSYPKPDRIFGIIERYKVSI-FGSTPGFIAGLrkNHISGDDFNLSSLRILGS--------------- 402
Cdd:PRK06178 274 LFSGATLVLL----ARWDAVAFMAAVERYRVTRtVMLVDNAVELM--DHPRFAEYDLSSLRQVRVvsfvkklnpdyrqrw 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 403 ---TGSILFSENWewffsvfgkgkcpinniiGGTEMLGCfaqnlpnipckigsvGVFALGMGGDIFNEKGESV------- 472
Cdd:PRK06178 348 ralTGSVLAEAAW------------------GMTETHTC---------------DTFTAGFQDDDFDLLSQPVfvglpvp 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 473 -------RRETGRVVcthPF----------PSMTRGFYADEEGYQEtyfsAFRGVWAH-GDFAEMDEDGFVFMRGRSDDI 534
Cdd:PRK06178 395 gtefkicDFETGELL---PLgaegeivvrtPSLLKGYWNKPEATAE----ALRDGWLHtGDIGKIDEQGFLHYLGRRKEM 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 535 INKNGIKFSPANIEsALIGFRAAefrVMEAIAVGIPDKNSENKIICFVIL-EGQDrlteTDEAALRSVVADIVNPQAKPE 613
Cdd:PRK06178 468 LKVNGMSVFPSEVE-ALLGQHPA---VLGSAVVGRPDPDKGQVPVAFVQLkPGAD----LTAAALQAWCRENMAVYKVPE 539
|
570
....*....|....*.
gi 1277171962 614 rIFAIKELPRNAAAKV 629
Cdd:PRK06178 540 -IRIVDALPMTATGKV 554
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
113-632 |
6.68e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 84.17 E-value: 6.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 113 RAITFWQLKLLVDTIASAMKAHGIGKGDFVGMCMPISIDSIAVMFACFKIGAVcmqmaP-TTSTDGTKDIVDHV-RIARA 190
Cdd:PRK07798 27 RRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAV-----PvNVNYRYVEDELRYLlDDSDA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 191 KMFFMADSYSyggknftlEKIHQGVSDIFSVRHIVVFENDAPHSPFSPfvfgkkemrSVFWDDFCKQGKSTIARTERCnA 270
Cdd:PRK07798 102 VALVYEREFA--------PRVAEVLPRLPKLRTLVVVEDGSGNDLLPG---------AVDYEDALAAGSPERDFGERS-P 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 271 EDVaLMLFSSGTTrekGKkPKRILHTHGGVLaqickEVGFG---FDC------KEDDVFYWMTNFG--WMMAP------- 332
Cdd:PRK07798 164 DDL-YLLYTGGTT---GM-PKGVMWRQEDIF-----RVLLGgrdFATgepiedEEELAKRAAAGPGmrRFPAPplmhgag 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 333 -WEIVGALHFGATLVcFEGAPSYpKPDRIFGIIERYKVSIFgstpgFIAG------LRKNHISGDDFNLSSLRILGSTGS 405
Cdd:PRK07798 234 qWAAFAALFSGQTVV-LLPDVRF-DADEVWRTIEREKVNVI-----TIVGdamarpLLDALEARGPYDLSSLFAIASGGA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 406 ILFSENWEWFFSVFgkgkcP---INNIIGGTE----MLGCFAQNLPNipckiGSVGVFALGMGGDIFNEKGESVR---RE 475
Cdd:PRK07798 307 LFSPSVKEALLELL-----PnvvLTDSIGSSEtgfgGSGTVAKGAVH-----TGGPRFTIGPRTVVLDEDGNPVEpgsGE 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 476 TGRVVCTHPFPSmtrGFYADEEGYQETYFSaFRGV-WA-HGDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIESALIG 553
Cdd:PRK07798 377 IGWIARRGHIPL---GYYKDPEKTAETFPT-IDGVrYAiPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKA 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 554 FRAaefrVMEAIAVGIPDKNSENKIICFVIL-EGqdrlTETDEAALRSVVADIVNPQAKPERIFAIKELPRNAAAKVPYK 632
Cdd:PRK07798 453 HPD----VADALVVGVPDERWGQEVVAVVQLrEG----ARPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGKADYR 524
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
127-634 |
8.13e-17 |
|
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: 84.12 E-value: 8.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 127 IASAMKAHGIGKGDFVGMCMPISIDSIAVMFACFKIGAVcmqMAPTTSTDGTKDIVDHVRIARAKMFFMAdsysyggKNf 206
Cdd:cd17642 57 LAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVG---VAPTNDIYNERELDHSLNISKPTIVFCS-------KK- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 207 TLEKIHQGVSDIFSVRHIVVFENDAPHSpfspfvfGKKEMRSVFWDDFCKQGKSTIARTERCNA-EDVALMLFSSGTTre 285
Cdd:cd17642 126 GLQKVLNVQKKLKIIKTIIILDSKEDYK-------GYQCLYTFITQNLPPGFNEYDFKPPSFDRdEQVALIMNSSGST-- 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 286 kgKKPKRILHTHGGVLAQI--CKEVGFGFDCKED----DVFYWMTNFGWMMapweIVGALHFGATLVCFegapsYPKPDR 359
Cdd:cd17642 197 --GLPKGVQLTHKNIVARFshARDPIFGNQIIPDtailTVIPFHHGFGMFT----TLGYLICGFRVVLM-----YKFEEE 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 360 IF-GIIERYKVSIFGSTPGFIAGLRKNHISgDDFNLSSLRILGSTGSILFSENWEwffSVFGKGKCP-INNIIGGTE-ML 436
Cdd:cd17642 266 LFlRSLQDYKVQSALLVPTLFAFFAKSTLV-DKYDLSNLHEIASGGAPLSKEVGE---AVAKRFKLPgIRQGYGLTEtTS 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 437 GCFAQnlPNIPCKIGSVGVFALGMGGDIF----------NEKGEsvrretgrvVCTHPfPSMTRGFYADEEGYQETyfsA 506
Cdd:cd17642 342 AILIT--PEGDDKPGAVGKVVPFFYAKVVdldtgktlgpNERGE---------LCVKG-PMIMKGYVNNPEATKAL---I 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 507 FRGVWAH-GDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIESALIgfraAEFRVMEAIAVGIPDKNSENKIICFVILE 585
Cdd:cd17642 407 DKDGWLHsGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILL----QHPKIFDAGVAGIPDEDAGELPAAVVVLE 482
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1277171962 586 GQDRLTETDeaalrsvVADIVNPQAKPER------IFaIKELPRNAAAKVPYKAI 634
Cdd:cd17642 483 AGKTMTEKE-------VMDYVASQVSTAKrlrggvKF-VDEVPKGLTGKIDRRKI 529
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
120-634 |
4.66e-16 |
|
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: 81.27 E-value: 4.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 120 LKLLVDTIASAMKAH-----GIGKGDFVGMCMPISIDSIAVMFACFKIGAVCMQMAPTTSTDGTKDIVDHVRIARAKMFF 194
Cdd:cd05929 18 LLLDVYSIALNRNARaaaaeGVWIADGVYIYLINSILTVFAAAAAWKCGACPAYKSSRAPRAEACAIIEIKAAALVCGLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 195 MADSysyggknftlekIHQGVSDIFSVrhivvfENDAPHSPFSPFVFGkkemrsvfWDdfckqgkstiartercnaedva 274
Cdd:cd05929 98 TGGG------------ALDGLEDYEAA------EGGSPETPIEDEAAG--------WK---------------------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 275 lMLFSSGTTrekgKKPKRILHTHGGVL----AQICKEVGFGFDckEDDVF------YWMTNFGWMMapweivGALHFGAT 344
Cdd:cd05929 130 -MLYSGGTT----GRPKGIKRGLPGGPpdndTLMAAALGFGPG--ADSVYlspaplYHAAPFRWSM------TALFMGGT 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 345 LVCFEGApsypKPDRIFGIIERYKVSIFGSTPG-FIAGLRKNHISGDDFNLSSLRILGSTG---SILFSENW-EWFFSVf 419
Cdd:cd05929 197 LVLMEKF----DPEEFLRLIERYRVTFAQFVPTmFVRLLKLPEAVRNAYDLSSLKRVIHAAapcPPWVKEQWiDWGGPI- 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 420 gkgkcpINNIIGGTEMLG---CFAQNLPNIPckiGSVGVFALGmGGDIFNEKGESV-RRETGRVVCTHPFPsmtrgfYAD 495
Cdd:cd05929 272 ------IWEYYGGTEGQGltiINGEEWLTHP---GSVGRAVLG-KVHILDEDGNEVpPGEIGEVYFANGPG------FEY 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 496 EEGYQETYFSAFRGVWAH-GDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIESALIgfraAEFRVMEAIAVGIPDKNS 574
Cdd:cd05929 336 TNDPEKTAAARNEGGWSTlGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALI----AHPKVLDAAVVGVPDEEL 411
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 575 ENKIICFVILEGQDRLTETDEAALRSVVADIVNPQAKPERIFAIKELPRNAAAKVPYKAI 634
Cdd:cd05929 412 GQRVHAVVQPAPGADAGTALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLL 471
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
110-627 |
5.56e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 81.33 E-value: 5.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 110 GKKRAITFWQLKLLVDTIASAMKAHGIGKGDFVGMCMPISIDSIAVMFACFKIGAVCmqMAPTTSTDgTKDIVDHVRIAR 189
Cdd:PRK06164 31 DEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATV--IAVNTRYR-SHEVAHILGRGR 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 190 AKMFFMADSYsyggKNFTLEKIHQGVSD--IFSVRHIVVFENDAPHSPfSPFVFGKkemRSVFwdDFCKQGKSTIARTER 267
Cdd:PRK06164 108 ARWLVVWPGF----KGIDFAAILAAVPPdaLPPLRAIAVVDDAADATP-APAPGAR---VQLF--ALPDPAPPAAAGERA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 268 CNAEDVALMLFSSGTTrekgKKPKRILHTHGGVL--AQICKEVgFGFDckEDDVFYWMT----NFGWMMApweiVGALHF 341
Cdd:PRK06164 178 ADPDAGALLFTTSGTT----SGPKLVLHRQATLLrhARAIARA-YGYD--PGAVLLAALpfcgVFGFSTL----LGALAG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 342 GATLVC---FEGAPSypkpdriFGIIERYKVS-IFGSTPGFIAGLRKNHISGDdfnLSSLRILGSTGsilFSENWEWFFS 417
Cdd:PRK06164 247 GAPLVCepvFDAART-------ARALRRHRVThTFGNDEMLRRILDTAGERAD---FPSARLFGFAS---FAPALGELAA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 418 VFGKGKCPINNIIGGTEMLGCFAQNLPNIPckigsVGVFALGMGGDIFNEKGESVRRETGRVVCTH--------PFPSMT 489
Cdd:PRK06164 314 LARARGVPLTGLYGSSEVQALVALQPATDP-----VSVRIEGGGRPASPEARVRARDPQDGALLPDgesgeieiRAPSLM 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 490 RGFYADEEGYQEtyfsAFR--GVWAHGDFAEMDEDG-FVFMrGRSDDIINKNGIKFSPANIESALIGFRAaefrVMEAIA 566
Cdd:PRK06164 389 RGYLDNPDATAR----ALTddGYFRTGDLGYTRGDGqFVYQ-TRMGDSLRLGGFLVNPAEIEHALEALPG----VAAAQV 459
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1277171962 567 VGIpDKNSENKIICFVILEGQdrlTETDEAALRSVVADIVNPQAKPERIFAIKELPRNAAA 627
Cdd:PRK06164 460 VGA-TRDGKTVPVAFVIPTDG---ASPDEAGLMAACREALAGFKVPARVQVVEAFPVTESA 516
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
253-629 |
9.05e-16 |
|
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: 79.92 E-value: 9.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 253 DFCKQGKSTIARTERCNAEDVALML-FSSGTTrekgKKPKRILHTHG----GVLAQIckevgFGFDCKEDDVFYWMTNFG 327
Cdd:cd05974 66 DRVDRGGAVYAAVDENTHADDPMLLyFTSGTT----SKPKLVEHTHRsypvGHLSTM-----YWIGLKPGDVHWNISSPG 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 328 WMMAPWEIVGA-LHFGATLVCFegapSYPK--PDRIFGIIERYKVSIFGSTPGFIAGLRKNHISGDDfnlSSLRILGSTG 404
Cdd:cd05974 137 WAKHAWSCFFApWNAGATVFLF----NYARfdAKRVLAALVRYGVTTLCAPPTVWRMLIQQDLASFD---VKLREVVGAG 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 405 SILFSENWEWFFSVFGKgkcPINNIIGGTEMlGCFAQNLPNIPCKIGSVGVFALGMGGDIFNEKGESVRRetGRVVC--- 481
Cdd:cd05974 210 EPLNPEVIEQVRRAWGL---TIRDGYGQTET-TALVGNSPGQPVKAGSMGRPLPGYRVALLDPDGAPATE--GEVALdlg 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 482 -THPFPSMTrGFYADEEGYQETYFSAFrgvWAHGDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIESALIGFRAaefr 560
Cdd:cd05974 284 dTRPVGLMK-GYAGDPDKTAHAMRGGY---YRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPA---- 355
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 561 VMEAIAVGIPDKNSENKIICFVIL-EGQDRLTETDEAALRSvVADIVNPQAKPERIfAIKELPRNAAAKV 629
Cdd:cd05974 356 VAEAAVVPSPDPVRLSVPKAFIVLrAGYEPSPETALEIFRF-SRERLAPYKRIRRL-EFAELPKTISGKI 423
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
271-629 |
2.36e-15 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 78.09 E-value: 2.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 271 EDVALMLFSSGTTrekgKKPKRILHTHGGVLA---------------QICKEVGFgFDCkeddvfywmtnFGWMMApweI 335
Cdd:cd05917 2 DDVINIQFTSGTT----GSPKGATLTHHNIVNngyfigerlglteqdRLCIPVPL-FHC-----------FGSVLG---V 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 336 VGALHFGATLVCfeGAPSYpKPDRIFGIIERYKVSIFGSTPG-FIAGLrkNHISGDDFNLSSLR--ILGstGSILFSENW 412
Cdd:cd05917 63 LACLTHGATMVF--PSPSF-DPLAVLEAIEKEKCTALHGVPTmFIAEL--EHPDFDKFDLSSLRtgIMA--GAPCPPELM 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 413 EWFFSVFGKGKCPInnIIGGTEMLGCFAQNLPN--IPCKIGSVG-----VFA--LGMGGDI---FNEKGEsvrretgrvV 480
Cdd:cd05917 136 KRVIEVMNMKDVTI--AYGMTETSPVSTQTRTDdsIEKRVNTVGrimphTEAkiVDPEGGIvppVGVPGE---------L 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 481 CTHPFPSMtRGFYADEEGYQETyfsAFRGVWAH-GDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIESaligFRAAEF 559
Cdd:cd05917 205 CIRGYSVM-KGYWNDPEKTAEA---IDGDGWLHtGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEE----FLHTHP 276
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1277171962 560 RVMEAIAVGIPDKNSENKIICFVILEGQDRLTETD-EAALRSVVADivnpQAKPERIFAIKELPRNAAAKV 629
Cdd:cd05917 277 KVSDVQVVGVPDERYGEEVCAWIRLKEGAELTEEDiKAYCKGKIAH----YKVPRYVFFVDEFPLTVSGKI 343
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
115-629 |
4.06e-15 |
|
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: 78.32 E-value: 4.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 115 ITFWQLKLLVDTIASAMKAHGIGKGDFVGMCMPISIDSIAVMFACFKIGAVCMQMAPTTSTDGTKDIvdhvrIARAKMff 194
Cdd:cd05923 29 LTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAEL-----IERGEM-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 195 madsysyggknftlekihqgvsdifsvrHIVVFENDAPHSPFSPFVFGKKEMRSVFWDD--FCKQGKSTIARTerCNAED 272
Cdd:cd05923 102 ----------------------------TAAVIAVDAQVMDAIFQSGVRVLALSDLVGLgePESAGPLIEDPP--REPEQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 273 VALMLFSSGTT-REKGKK-PKRilHTHGGVLAqICKEVGFGFDcKEDDVFYWMTNFGWMMAPWEIVGALHFGATLVcfeg 350
Cdd:cd05923 152 PAFVFYTSGTTgLPKGAViPQR--AAESRVLF-MSTQAGLRHG-RHNVVLGLMPLYHVIGFFAVLVAALALDGTYV---- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 351 APSYPKPDRIFGIIERYKVSIFGSTPGFIAGLrKNHISGDDFNLSSLRILGSTGSILFSENWEwffSVFGKGKCPINNII 430
Cdd:cd05923 224 VVEEFDPADALKLIEQERVTSLFATPTHLDAL-AAAAEFAGLKLSSLRHVTFAGATMPDAVLE---RVNQHLPGEKVNIY 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 431 GGTE-MLGCFAQNLP---------NIPCKIGSVG---VFALGMGgdifnEKGESVRRETGRVVCTHPFpsmtRGFYADEE 497
Cdd:cd05923 300 GTTEaMNSLYMRDARtgtemrpgfFSEVRIVRIGgspDEALANG-----EEGELIVAAAADAAFTGYL----NQPEATAK 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 498 GYQEtyfsafrGVWAHGDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIESALigfrAAEFRVMEAIAVGIPDKNSENK 577
Cdd:cd05923 371 KLQD-------GWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVL----SRHPGVTEVVVIGVADERWGQS 439
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1277171962 578 IICFVIL-EGQDRLTETDEAALRSVVADIvnpqAKPERIFAIKELPRNAAAKV 629
Cdd:cd05923 440 VTACVVPrEGTLSADELDQFCRASELADF----KRPRRYFFLDELPKNAMNKV 488
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
113-633 |
5.48e-15 |
|
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: 78.01 E-value: 5.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 113 RAITFWQLKLLVDTIASAMKAHGIGKGDFVGMCMPISIDSIAVMFACFKIGAVCMQMAPTTSTDgtkdivdhvRIArakm 192
Cdd:cd12117 21 RSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAE---------RLA---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 193 FFMADSysyggknftlekihqGVSDIFSVRHivvfendaphspfSPFVFGKKEMRSVFWDDFCKQGKSTIARteRCNAED 272
Cdd:cd12117 88 FMLADA---------------GAKVLLTDRS-------------LAGRAGGLEVAVVIDEALDAGPAGNPAV--PVSPDD 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 273 VALMLFSSGTTrekGKkPKRILHTHGGVLAqICKEVGFGfDCKEDDVFYWMTNFGWMMAPWEIVGALHFGATLVcfeGAP 352
Cdd:cd12117 138 LAYVMYTSGST---GR-PKGVAVTHRGVVR-LVKNTNYV-TLGPDDRVLQTSPLAFDASTFEIWGALLNGARLV---LAP 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 353 SYP--KPDRIFGIIERYKVS-IFGSTPGF----------IAGLRKNHISGDDFNLSS----------LRIL---GSTGSI 406
Cdd:cd12117 209 KGTllDPDALGALIAEEGVTvLWLTAALFnqladedpecFAGLRELLTGGEVVSPPHvrrvlaacpgLRLVngyGPTENT 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 407 LFSEnwewFFSV----FGKGKCPINNIIGGTEmlgCFAQNLPNIPCKIGSVG-VFALGMGgdifNEKGESVRRE-TGRVV 480
Cdd:cd12117 289 TFTT----SHVVteldEVAGSIPIGRPIANTR---VYVLDEDGRPVPPGVPGeLYVGGDG----LALGYLNRPAlTAERF 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 481 CTHPFPSMTRgfyadeegyqetyfsAFRGvwahGDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIESALigfRAAEfR 560
Cdd:cd12117 358 VADPFGPGER---------------LYRT----GDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAAL---RAHP-G 414
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1277171962 561 VMEAIAVGIPDKNSENKIICFVILEGqdrltETDEAALRSVVADIVNPQAKPERIFAIKELPRNAAAKVPYKA 633
Cdd:cd12117 415 VREAVVVVREDAGGDKRLVAYVVAEG-----ALDAAELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRA 482
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
276-629 |
9.52e-15 |
|
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: 75.90 E-value: 9.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 276 MLFSSGTTrekgKKPKRILHTHGGVLAQickevgfgFDCKEDDvFYwMTNFGWMMAP---------WEIVGALHFGATLV 346
Cdd:cd17633 5 IGFTSGTT----GLPKAYYRSERSWIES--------FVCNEDL-FN-ISGEDAILAPgplshslflYGAISALYLGGTFI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 347 CFEGApsypKPDRIFGIIERYKVSIFGSTPGFIAGLRKNhisgdDFNLSSLRILGSTGSILFSENWEWFFSVFgkgkcPI 426
Cdd:cd17633 71 GQRKF----NPKSWIRKINQYNATVIYLVPTMLQALART-----LEPESKIKSIFSSGQKLFESTKKKLKNIF-----PK 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 427 NNIIG--GTEMLGCFAQNLPNIPCKIGSVGVFALGMGGDIFNEKGesvrRETGRVVCTHPfpsMTRGFYADEEGYQETYF 504
Cdd:cd17633 137 ANLIEfyGTSELSFITYNFNQESRPPNSVGRPFPNVEIEIRNADG----GEIGKIFVKSE---MVFSGYVRGGFSNPDGW 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 505 SAFrgvwahGDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIESALIGFRAAEfrvmEAIAVGIPDKNSeNKIICFVIl 584
Cdd:cd17633 210 MSV------GDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIE----EAIVVGIPDARF-GEIAVALY- 277
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1277171962 585 EGqDRLTETDeaaLRSVVADIVNPQAKPERIFAIKELPRNAAAKV 629
Cdd:cd17633 278 SG-DKLTYKQ---LKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKI 318
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
259-636 |
2.06e-14 |
|
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341308 [Multi-domain] Cd Length: 433 Bit Score: 75.81 E-value: 2.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 259 KSTIARTERCN-------AEDVALMLFSSGTTrekgKKPKRILHTHGGVL------------------AQICkevGFGFD 313
Cdd:cd17653 86 IQAILRTSGATlllttdsPDDLAYIIFTSGST----GIPKGVMVPHRGVLnyvsqpparldvgpgsrvAQVL---SIAFD 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 314 CkeddvfywmtnfgwmmAPWEIVGALHFGATLVCFEgaPSYPKPDRIfgiierYKVSIFGSTPGFIAGLRKnhisgDDF- 392
Cdd:cd17653 159 A----------------CIGEIFSTLCNGGTLVLAD--PSDPFAHVA------RTVDALMSTPSILSTLSP-----QDFp 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 393 NLSSLRILGSTGSILFSENWewffsvfGKGKCpINNIIGGTE--MLGCFAQNLPNIPCKIGS----VGVFALGMGgdifn 466
Cdd:cd17653 210 NLKTIFLGGEAVPPSLLDRW-------SPGRR-LYNAYGPTEctISSTMTELLPGQPVTIGKpipnSTCYILDAD----- 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 467 eKGESVRRETGRVVCTHPfpSMTRGFYADEEGYQETYFSAFRG----VWAHGDFAEMDEDGFVFMRGRSDDIINKNGIKF 542
Cdd:cd17653 277 -LQPVPEGVVGEICISGV--QVARGYLGNPALTASKFVPDPFWpgsrMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRI 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 543 SPANIESALIGFRAaefRVMEAIAVgipdkNSENKIICFVILEGqdrlteTDEAALRSVVADIVNPQAKPERIFAIKELP 622
Cdd:cd17653 354 NLEEIEEVVLQSQP---EVTQAAAI-----VVNGRLVAFVTPET------VDVDGLRSELAKHLPSYAVPDRIIALDSFP 419
|
410
....*....|....
gi 1277171962 623 RNAAAKVPYKAISR 636
Cdd:cd17653 420 LTANGKVDRKALRE 433
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
124-568 |
2.48e-14 |
|
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: 75.71 E-value: 2.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 124 VDTIASAMKAHGIGKGDFVGMCMPISIDSIAVMFACFKIGAVCMQMAPTTSTDGTKDIVDHvriARAKMFFmadsysygg 203
Cdd:cd05907 15 VRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILND---SEAKALF--------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 204 knftlekihqgVSDifsvrhivvfendaphspfspfvfgkkemrsvfwddfckqgkstiartercnAEDVALMLFSSGTT 283
Cdd:cd05907 83 -----------VED----------------------------------------------------PDDLATIIYTSGTT 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 284 rekGKkPKRILHTHGGVLAQiCKEVGFGFDCKEDDVFYWM----TNFGWMMApweIVGALHFGATLVCFEGApsypkpDR 359
Cdd:cd05907 100 ---GR-PKGVMLSHRNILSN-ALALAERLPATEGDRHLSFlplaHVFERRAG---LYVPLLAGARIYFASSA------ET 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 360 IFGIIERYKVSIFGSTPGF----IAGLRKNHISGDDFNLSSLRILGS-----TGSILFSENWEWFFSVFGkgkCPINNII 430
Cdd:cd05907 166 LLDDLSEVRPTVFLAVPRVwekvYAAIKVKAVPGLKRKLFDLAVGGRlrfaaSGGAPLPAELLHFFRALG---IPVYEGY 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 431 GGTEMLGCFAQNLPNIPcKIGSVGVFALGMGGDIfNEKGEsvrretgrvVCTHPfPSMTRGFYADEEgyqETYFSAFRGV 510
Cdd:cd05907 243 GLTETSAVVTLNPPGDN-RIGTVGKPLPGVEVRI-ADDGE---------ILVRG-PNVMLGYYKNPE---ATAEALDADG 307
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 511 WAH-GDFAEMDEDGFVFMRGRSDD-IINKNGIKFSPANIESALIGFRAaefrVMEAIAVG 568
Cdd:cd05907 308 WLHtGDLGEIDEDGFLHITGRKKDlIITSGGKNISPEPIENALKASPL----ISQAVVIG 363
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
268-603 |
3.13e-14 |
|
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: 75.78 E-value: 3.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 268 CNAEDVALMLFSSGTTrekgKKPKRILHTHGGVLA-QICKEVGFGFDckEDDVFY-WMtnfgwmmaPWEIVGAL---HFG 342
Cdd:cd05906 164 SRPDDLALLMLTSGST----GFPKAVPLTHRNILArSAGKIQHNGLT--PQDVFLnWV--------PLDHVGGLvelHLR 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 343 AT-LVC--FEGAPSY--PKPDRIFGIIERYKVSI-FGstPGFIAGLRKNH---ISGDDFNLSSLRILGSTGSILFSENWE 413
Cdd:cd05906 230 AVyLGCqqVHVPTEEilADPLRWLDLIDRYRVTItWA--PNFAFALLNDLleeIEDGTWDLSSLRYLVNAGEAVVAKTIR 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 414 WFFSVFGKGKCPINNII---GGTEM-------LGCFAQNLPNIPcKIGSVGVFALGMGGDIFNEKGESV-RRETGRV-VC 481
Cdd:cd05906 308 RLLRLLEPYGLPPDAIRpafGMTETcsgviysRSFPTYDHSQAL-EFVSLGRPIPGVSMRIVDDEGQLLpEGEVGRLqVR 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 482 ThpfPSMTRGFYADEEGYQEtyfsAFR--GVWAHGDFAEMDeDGFVFMRGRSDDIINKNGIKFSPANIESAL-------I 552
Cdd:cd05906 387 G---PVVTKGYYNNPEANAE----AFTedGWFRTGDLGFLD-NGNLTITGRTKDTIIVNGVNYYSHEIEAAVeevpgveP 458
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1277171962 553 GFRAaefrvmeAIAVGIPDKNSENKIICFVILEG-QDRLTETDEaALRSVVA 603
Cdd:cd05906 459 SFTA-------AFAVRDPGAETEELAIFFVPEYDlQDALSETLR-AIRSVVS 502
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
449-629 |
9.90e-14 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 73.84 E-value: 9.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 449 KIGSVGVFALGMGGDIFNEKGESVRRETGRVVCTHPfpSMTRGFYADEEGYQEtyfsAFRGVWAH-GDFAEMDEDGFVFM 527
Cdd:PRK03640 305 KLGSAGKPLFPCELKIEKDGVVVPPFEEGEIVVKGP--NVTKGYLNREDATRE----TFQDGWFKtGDIGYLDEEGFLYV 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 528 RGRSDDIINKNGIKFSPANIESALIGFRAaefrVMEAIAVGIPDKNSENKIICFVILEgqdrlTETDEAALRSVVADIVN 607
Cdd:PRK03640 379 LDRRSDLIISGGENIYPAEIEEVLLSHPG----VAEAGVVGVPDDKWGQVPVAFVVKS-----GEVTEEELRHFCEEKLA 449
|
170 180
....*....|....*....|..
gi 1277171962 608 PQAKPERIFAIKELPRNAAAKV 629
Cdd:PRK03640 450 KYKVPKRFYFVEELPRNASGKL 471
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
113-404 |
1.14e-13 |
|
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: 74.89 E-value: 1.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 113 RAITFWQLKLLVDTIASAMKAHGIGKGDFVGMCMPISIDSIAVMFACFKIGAVCMQMAPTTSTDgtkdivdhvRIArakm 192
Cdd:COG1020 500 QSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAE---------RLA---- 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 193 fFM-ADSysyggknftlekihqgvsdifSVRHIVVFENDAPHSPfspfvfgKKEMRSVFWDDFCKQGKSTIARTERCNAE 271
Cdd:COG1020 567 -YMlEDA---------------------GARLVLTQSALAARLP-------ELGVPVLALDALALAAEPATNPPVPVTPD 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 272 DVALMLFSSGTTrekGKkPKRILHTHGGV---LAQICKEVGFGfdckEDDVFYWMTNFGWMMAPWEIVGALHFGATLVCF 348
Cdd:COG1020 618 DLAYVIYTSGST---GR-PKGVMVEHRALvnlLAWMQRRYGLG----PGDRVLQFASLSFDASVWEIFGALLSGATLVLA 689
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1277171962 349 --EGAPSypkPDRIFGIIERYKVSIFGSTPGFIAGLRKNHISGddfnLSSLRILGSTG 404
Cdd:COG1020 690 ppEARRD---PAALAELLARHRVTVLNLTPSLLRALLDAAPEA----LPSLRLVLVGG 740
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
272-634 |
1.37e-13 |
|
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.
Pssm-ID: 341264 [Multi-domain] Cd Length: 442 Bit Score: 73.48 E-value: 1.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 272 DVALMLFSSGTTrekgKKPKRILHTHGGVLAQI---CKEVGFgfdcKEDDVFYwmtnfgwMMAPWE--------IVGALH 340
Cdd:cd05941 90 DPALILYTSGTT----GRPKGVVLTHANLAANVralVDAWRW----TEDDVLL-------HVLPLHhvhglvnaLLCPLF 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 341 FGATLVCFegapsyPKPDRIFGIIERYK--VSIFGSTPGF----IAGLRKNHISGDDFN---LSSLRILGSTGSILFSEN 411
Cdd:cd05941 155 AGASVEFL------PKFDPKEVAISRLMpsITVFMGVPTIytrlLQYYEAHFTDPQFARaaaAERLRLMVSGSAALPVPT 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 412 WEWFFSVFGkgkcpiNNII---GGTEmlgcFAQNLPN------IPckiGSVGvFALgmggdifneKGESVR---RETGRV 479
Cdd:cd05941 229 LEEWEAITG------HTLLeryGMTE----IGMALSNpldgerRP---GTVG-MPL---------PGVQARivdEETGEP 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 480 VCTHPF-------PSMTRGFYADEEGYQEtyfsAFR--GVWAHGDFAEMDEDGFVFMRGR-SDDIINKNGIKFSPANIES 549
Cdd:cd05941 286 LPRGEVgeiqvrgPSVFKEYWNKPEATKE----EFTddGWFKTGDLGVVDEDGYYWILGRsSVDIIKSGGYKVSALEIER 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 550 ALIGFRAaefrVMEAIAVGIPDKNSENKIICFVILEGQdrLTETDEAALRSVVADIVNPQAKPERIFAIKELPRNAAAKV 629
Cdd:cd05941 362 VLLAHPG----VSECAVIGVPDPDWGERVVAVVVLRAG--AAALSLEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKV 435
|
....*
gi 1277171962 630 PYKAI 634
Cdd:cd05941 436 NKKEL 440
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
357-641 |
2.65e-13 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 72.59 E-value: 2.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 357 PDRIFGIIERYKVSIFGSTPGFIAGLRkNHISGDDFNLSSLRilgstgsilfsenweWFFSvfGKGKCPINNIIGGTEML 436
Cdd:PRK06839 227 PTKALSMIEKHKVTVVMGVPTIHQALI-NCSKFETTNLQSVR---------------WFYN--GGAPCPEELMREFIDRG 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 437 GCFAQNL------PNI--------PCKIGSVGVFALGMGGDIFNEKGESVRR-ETGRVVCTHPfpSMTRGFYADEEGYQE 501
Cdd:PRK06839 289 FLFGQGFgmtetsPTVfmlseedaRRKVGSIGKPVLFCDYELIDENKNKVEVgEVGELLIRGP--NVMKEYWNRPDATEE 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 502 TyfsaFRGVWAH-GDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIESALIGFRAaefrVMEAIAVGIPDKNSENKIIC 580
Cdd:PRK06839 367 T----IQDGWLCtGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSD----VYEVAVVGRQHVKWGEIPIA 438
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1277171962 581 FVILEGQDRLTETDeaaLRSVVADIVNPQAKPERIFAIKELPRNAAAKVPYKAISRVFCDR 641
Cdd:PRK06839 439 FIVKKSSSVLIEKD---VIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVNQLKSR 496
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
88-629 |
5.33e-13 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 71.94 E-value: 5.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 88 CIERniARGLGSKVCVCyEHESGkkRAITFWQLKLLVDTIASAMKAHGIGKGDFVGMCMPISIDSIAVMFACFKIGAVCM 167
Cdd:PLN02246 29 CFER--LSEFSDRPCLI-DGATG--RVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 168 QMAP-TTSTDgtkdIVDHVRIARAKMFFMADSYsyggknftLEKihqgVSDIFSVRHIVVFENDAPhspfspfvfgkKEM 246
Cdd:PLN02246 104 TANPfYTPAE----IAKQAKASGAKLIITQSCY--------VDK----LKGLAEDDGVTVVTIDDP-----------PEG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 247 RSVFWDDFckQGKSTIARTERCNAEDVALMLFSSGTTrekgKKPKRILHTHGGVLAQICKEV-----GFGFdcKEDDV-- 319
Cdd:PLN02246 157 CLHFSELT--QADENELPEVEISPDDVVALPYSSGTT----GLPKGVMLTHKGLVTSVAQQVdgenpNLYF--HSDDVil 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 320 -----FYWMTNFGWMMApweivgALHFGATLVCFegapsyPKPD--RIFGIIERYKVSIFGSTPGFIAGLRKNHISgDDF 392
Cdd:PLN02246 229 cvlpmFHIYSLNSVLLC------GLRVGAAILIM------PKFEigALLELIQRHKVTIAPFVPPIVLAIAKSPVV-EKY 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 393 NLSSLRILGSTGSILFSENWEWFFS-----VFGKGkcpinniIGGTE------MLGCFAQNlPnIPCKIGSVGVFALGMG 461
Cdd:PLN02246 296 DLSSIRMVLSGAAPLGKELEDAFRAklpnaVLGQG-------YGMTEagpvlaMCLAFAKE-P-FPVKSGSCGTVVRNAE 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 462 GDIFN-EKGESVRRETGRVVCTHPfPSMTRGFYADEEGYQETyfsAFRGVWAH-GDFAEMDEDGFVFMRGRSDDIINKNG 539
Cdd:PLN02246 367 LKIVDpETGASLPRNQPGEICIRG-PQIMKGYLNDPEATANT---IDKDGWLHtGDIGYIDDDDELFIVDRLKELIKYKG 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 540 IKFSPANIESALIgfraAEFRVMEAIAVGIPDKNSENKIICFVILEGQDRLTETDeaaLRSVVADIVNPQAKPERIFAIK 619
Cdd:PLN02246 443 FQVAPAELEALLI----SHPSIADAAVVPMKDEVAGEVPVAFVVRSNGSEITEDE---IKQFVAKQVVFYKRIHKVFFVD 515
|
570
....*....|
gi 1277171962 620 ELPRNAAAKV 629
Cdd:PLN02246 516 SIPKAPSGKI 525
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
94-642 |
1.20e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 70.69 E-value: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 94 ARGLGSKVCVCYEHESgkkraITFWQLKLLVDTIASAMKAHGIGKGDFVGMCMPISIDSIAVMFACFKIGAVCMQMAPTT 173
Cdd:PRK06145 12 ARRTPDRAALVYRDQE-----ISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 174 STDGTKDIVDHvriARAKMFFMADSY----SYGGKNFTLEKIHQGVSDIFSvrhivvfendAPHSPFSPfvfgkkeMRSV 249
Cdd:PRK06145 87 AADEVAYILGD---AGAKLLLVDEEFdaivALETPKIVIDAAAQADSRRLA----------QGGLEIPP-------QAAV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 250 FWDDFCKqgkstiartercnaedvalMLFSSGTTrekgKKPKRILHTHGGV-LAQICKEVGFGFDcKEDDVFywmtnfgw 328
Cdd:PRK06145 147 APTDLVR-------------------LMYTSGTT----DRPKGVMHSYGNLhWKSIDHVIALGLT-ASERLL-------- 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 329 MMAPWEIVGALHFGATLVCFEGA----PSYPKPDRIFGIIERYKVsifgsTPGFIAGLRKNHI----SGDDFNLSSLRIL 400
Cdd:PRK06145 195 VVGPLYHVGAFDLPGIAVLWVGGtlriHREFDPEAVLAAIERHRL-----TCAWMAPVMLSRVltvpDRDRFDLDSLAWC 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 401 GSTGSILFSENWEWFFSVFGKGKcpINNIIGGTEMLG--CFAQNLPNIPcKIGSVGVFALGMGGDIFNEKGESVRRETGR 478
Cdd:PRK06145 270 IGGGEKTPESRIRDFTRVFTRAR--YIDAYGLTETCSgdTLMEAGREIE-KIGSTGRALAHVEIRIADGAGRWLPPNMKG 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 479 VVCTHPfPSMTRGFYADEEGYQEtyfsAFRGVWAH-GDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIESALigFRAA 557
Cdd:PRK06145 347 EICMRG-PKVTKGYWKDPEKTAE----AFYGDWFRsGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVI--YELP 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 558 EfrVMEAIAVGIPDKNSENKIICFVIL-EGQ----DRLTETDEAALRSVvadivnpqAKPERIFAIKELPRNAAAKVpyk 632
Cdd:PRK06145 420 E--VAEAAVIGVHDDRWGERITAVVVLnPGAtltlEALDRHCRQRLASF--------KVPRQLKVRDELPRNPSGKV--- 486
|
570
....*....|
gi 1277171962 633 aISRVFCDRY 642
Cdd:PRK06145 487 -LKRVLRDEL 495
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
115-629 |
1.70e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 70.34 E-value: 1.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 115 ITFWQLKLLVDTIASAMKAHGIGKGDFVGMCMPISIDSIAVMFACFKIGAVCMQMAPTTSTDGTKDIvdhvrIAR--AKM 192
Cdd:PRK07788 75 LTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQLAEV-----AARegVKA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 193 FFMADSYSYggknfTLEKIHQGVSDIFSVrhIVVFENDAPHSPFSPFVfgkkemrsvfwDDFCKQGKSTIARTERCNAed 272
Cdd:PRK07788 150 LVYDDEFTD-----LLSALPPDLGRLRAW--GGNPDDDEPSGSTDETL-----------DDLIAGSSTAPLPKPPKPG-- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 273 vALMLFSSGTTrekGKkPKRILHTHG---GVLAQICKEVGFgfdcKEDDVFYwMTN--F-GWMMAPWEIvgALHFGATLV 346
Cdd:PRK07788 210 -GIVILTSGTT---GT-PKGAPRPEPsplAPLAGLLSRVPF----RAGETTL-LPApmFhATGWAHLTL--AMALGSTVV 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 347 C---FegapsypKPDRIFGIIERYKVSIFGSTPGF---IAGLRKNHISgdDFNLSSLRILGSTGSILFSENWEWFFSVFG 420
Cdd:PRK07788 278 LrrrF-------DPEATLEDIAKHKATALVVVPVMlsrILDLGPEVLA--KYDTSSLKIIFVSGSALSPELATRALEAFG 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 421 KGKCpinNIIGGTEMlgCFA-----QNLPNIPckiGSVGVFALGMGGDIFNEKGESVRR-ETGRVVCTHPFPsmtrgF-- 492
Cdd:PRK07788 349 PVLY---NLYGSTEV--AFAtiatpEDLAEAP---GTVGRPPKGVTVKILDENGNEVPRgVVGRIFVGNGFP-----Feg 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 493 YADEEGYQETyfsafRGVWAHGDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIESALIGFRAaefrVMEAIAVGIPDK 572
Cdd:PRK07788 416 YTDGRDKQII-----DGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPD----VVEAAVIGVDDE 486
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1277171962 573 NSENKIICFVILEGQDRLTETD-EAALRSVVADIVNPQakpERIFaIKELPRNAAAKV 629
Cdd:PRK07788 487 EFGQRLRAFVVKAPGAALDEDAiKDYVRDNLARYKVPR---DVVF-LDELPRNPTGKV 540
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
394-635 |
2.13e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 70.03 E-value: 2.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 394 LSSLRILGSTGSILFSENWEWFFSVFGKgkcPINNIIGGTEM-LGCFAQ--NLPNIPckiGSVGVFALGMGGDIFNEKGE 470
Cdd:PRK13383 291 LPQLRVVMSSGDRLDPTLGQRFMDTYGD---ILYNGYGSTEVgIGALATpaDLRDAP---ETVGKPVAGCPVRILDRNNR 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 471 SV-RRETGRVVCTHPFPSmTRgfYADEEGYqetyfSAFRGVWAHGDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIES 549
Cdd:PRK13383 365 PVgPRVTGRIFVGGELAG-TR--YTDGGGK-----AVVDGMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVEN 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 550 ALigfrAAEFRVMEAIAVGIPDKNSENKIICFVILE-GQDrlteTDEAALRSVVADIVNPQAKPERIFAIKELPRNAAAK 628
Cdd:PRK13383 437 AL----AAHPAVADNAVIGVPDERFGHRLAAFVVLHpGSG----VDAAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGK 508
|
....*..
gi 1277171962 629 VPYKAIS 635
Cdd:PRK13383 509 VLRKELP 515
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
113-633 |
3.05e-12 |
|
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: 69.29 E-value: 3.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 113 RAITFWQLKLLVDTIASAMKAHGIGKGDFVGMCMPISIDSIAVMFACFKIGAVCMQMAPTTSTDgtkdivdhvRIArakm 192
Cdd:cd17651 19 RRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAE---------RLA---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 193 FFMADSysyggkNFTLEKIHQGVSDIFSVRHIVVFENDAPHSPfspfvfgkkemrsvfwddfckqGKSTIARTERCNAED 272
Cdd:cd17651 86 FMLADA------GPVLVLTHPALAGELAVELVAVTLLDQPGAA----------------------AGADAEPDPALDADD 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 273 VALMLFSSGTTrekgKKPKRILHTHGGVLAQICKEVGFGFDCKEDDVFYWMTnFGWMMAPWEIVGALHFGATLVcFEGAP 352
Cdd:cd17651 138 LAYVIYTSGST----GRPKGVVMPHRSLANLVAWQARASSLGPGARTLQFAG-LGFDVSVQEIFSTLCAGATLV-LPPEE 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 353 SYPKPDRIFGIIERYKVSI-FGSTPgfIAGLRKNHISGDDFNLSSLRILGSTGS--ILFSENWEWFFsvfGKGKCPINNI 429
Cdd:cd17651 212 VRTDPPALAAWLDEQRISRvFLPTV--ALRALAEHGRPLGVRLAALRYLLTGGEqlVLTEDLREFCA---GLPGLRLHNH 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 430 IGGTEMLGCFAQNLPNIPCK----------IGSVGVFAL---------GMGGDIFnEKGESVRRE-TGRvvcthpfPSMT 489
Cdd:cd17651 287 YGPTETHVVTALSLPGDPAAwpapppigrpIDNTRVYVLdaalrpvppGVPGELY-IGGAGLARGyLNR-------PELT 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 490 RgfyadeEGYQETYFSAFRGVWAHGDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIESALigfrAAEFRVMEAIAVGI 569
Cdd:cd17651 359 A------ERFVPDPFVPGARMYRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAAL----ARHPGVREAVVLAR 428
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1277171962 570 PDKNSENKIICFVILEGQDRLtetDEAALRSVVADIVNPQAKPERIFAIKELPRNAAAKVPYKA 633
Cdd:cd17651 429 EDRPGEKRLVAYVVGDPEAPV---DAAELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRA 489
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
449-629 |
4.22e-12 |
|
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: 68.53 E-value: 4.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 449 KIGSVGVFALGMggDIFNEKGESVRRETGRVVCTHPfpSMTRGFYADEEGYQETyfsaFRGVWAH-GDFAEMDEDGFVFM 527
Cdd:cd05912 240 KIGSAGKPLFPV--ELKIEDDGQPPYEVGEILLKGP--NVTKGYLNRPDATEES----FENGWFKtGDIGYLDEEGFLYV 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 528 RGRSDDIINKNGIKFSPANIESALIGFRAaefrVMEAIAVGIPDKNSENKIICFVILEGqdrltETDEAALRSVVADIVN 607
Cdd:cd05912 312 LDRRSDLIISGGENIYPAEIEEVLLSHPA----IKEAGVVGIPDDKWGQVPVAFVVSER-----PISEEELIAYCSEKLA 382
|
170 180
....*....|....*....|..
gi 1277171962 608 PQAKPERIFAIKELPRNAAAKV 629
Cdd:cd05912 383 KYKVPKKIYFVDELPRTASGKL 404
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
271-632 |
5.06e-12 |
|
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: 67.79 E-value: 5.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 271 EDVALMLFSSGTTrekgKKPKRILHTHG---GVLAQickevGFGFDCKEDDVFYWM-------TNFGWMMAP-------- 332
Cdd:cd05924 3 ADDLYILYTGGTT----GMPKGVMWRQEdifRMLMG-----GADFGTGEFTPSEDAhkaaaaaAGTVMFPAPplmhgtgs 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 333 WEIVGALHFGATLVcfegAPSYP-KPDRIFGIIERYKV---SIFGSTpgFIAGLRKNHISGDDFNLSSLRILGSTGSILF 408
Cdd:cd05924 74 WTAFGGLLGGQTVV----LPDDRfDPEEVWRTIEKHKVtsmTIVGDA--MARPLIDALRDAGPYDLSSLFAISSGGALLS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 409 SENWEWFFSVfgKGKCPINNIIGGTE--MLGcFAQNLPNIPckigSVGVFALGMGGDIfnekgesVRRETGRVVcTHPFP 486
Cdd:cd05924 148 PEVKQGLLEL--VPNITLVDAFGSSEtgFTG-SGHSAGSGP----ETGPFTRANPDTV-------VLDDDGRVV-PPGSG 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 487 SMTR---------GFYADEEGYQETYFSAfRGV-WA-HGDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIESALigfr 555
Cdd:cd05924 213 GVGWiarrghiplGYYGDEAKTAETFPEV-DGVrYAvPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEAL---- 287
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1277171962 556 AAEFRVMEAIAVGIPDKNSENKIICFVILEGQdrlTETDEAALRSVVADIVNPQAKPERIFAIKELPRNAAAKVPYK 632
Cdd:cd05924 288 KSHPAVYDVLVVGRPDERWGQEVVAVVQLREG---AGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGKADYR 361
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
113-629 |
5.13e-12 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 68.87 E-value: 5.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 113 RAITFWQLKLLVDTIASAMKAHGIGKGDFVGMCMPISIDSIAVMFACFKIGAVCMQMAPT-TSTDGTKDIVDHvriaRAK 191
Cdd:PRK05605 56 ATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVEHNPLyTAHELEHPFEDH----GAR 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 192 MFFMADSYSYggknfTLEKIHQGVSdifsVRHIVVFE-----------------------NDAPHSPFSPFVFGKKEMRS 248
Cdd:PRK05605 132 VAIVWDKVAP-----TVERLRRTTP----LETIVSVNmiaampllqrlalrlpipalrkaRAALTGPAPGTVPWETLVDA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 249 VFwddfckQGKSTIARTERCNAEDVALMLFSSGTTrekgKKPKRILHTHGGVLAQI------CKEVGFGfdckeDDVF-- 320
Cdd:PRK05605 203 AI------GGDGSDVSHPRPTPDDVALILYTSGTT----GKPKGAQLTHRNLFANAaqgkawVPGLGDG-----PERVla 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 321 -------YWMTnfgwmmapweIVGAL--HFGATLVCFegaPSyPKPDRIFGIIERYKVSIFGSTPGF---IAGLRKNHis 388
Cdd:PRK05605 268 alpmfhaYGLT----------LCLTLavSIGGELVLL---PA-PDIDLILDAMKKHPPTWLPGVPPLyekIAEAAEER-- 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 389 gdDFNLSSLRILGSTGSIL---FSENWE-----WFFSVFGKGKC-PI--NNIIGGTEMLGCFAQNLPNIPCKIGSVGVFA 457
Cdd:PRK05605 332 --GVDLSGVRNAFSGAMALpvsTVELWEkltggLLVEGYGLTETsPIivGNPMSDDRRPGYVGVPFPDTEVRIVDPEDPD 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 458 LGMGGDifnEKGESVRRetGrvvcthpfPSMTRGFYADEEGYQEtyfsAFRGVWAH-GDFAEMDEDGFVFMRGRSDDIIN 536
Cdd:PRK05605 410 ETMPDG---EEGELLVR--G--------PQVFKGYWNRPEETAK----SFLDGWFRtGDVVVMEEDGFIRIVDRIKELII 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 537 KNGIKFSPANIESALIGFRAaefrVMEAIAVGIP-DKNSENKIICFVILEGqdrlTETDEAALRSVVADIVNPQAKPERI 615
Cdd:PRK05605 473 TGGFNVYPAEVEEVLREHPG----VEDAAVVGLPrEDGSEEVVAAVVLEPG----AALDPEGLRAYCREHLTRYKVPRRF 544
|
570
....*....|....
gi 1277171962 616 FAIKELPRNAAAKV 629
Cdd:PRK05605 545 YHVDELPRDQLGKV 558
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
113-629 |
7.57e-12 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 68.27 E-value: 7.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 113 RAITFWQLKLLVDTIASAMKAHGIGKGDFVGMCMPISIDSIAVMFACFKIGA----VCMQMAPTtstdgtkDIVDHVRIA 188
Cdd:PRK07786 41 NTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAiavpVNFRLTPP-------EIAFLVSDC 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 189 RAKMFFMADSysyggknftLEKIHQGVSDIFSVRHIVVFENDAPHSPfspfVFGkkemrsvfWDDFckqgkstIARTERC 268
Cdd:PRK07786 114 GAHVVVTEAA---------LAPVATAVRDIVPLLSTVVVAGGSSDDS----VLG--------YEDL-------LAEAGPA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 269 NA-----EDV-ALMLFSSGTTrekgKKPKRILHTHGGVLAQICKEV-GFGFDcKEDDVFYWMTNFGWMMAPWEIVGALHF 341
Cdd:PRK07786 166 HApvdipNDSpALIMYTSGTT----GRPKGAVLTHANLTGQAMTCLrTNGAD-INSDVGFVGVPLFHIAGIGSMLPGLLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 342 GATLVCfegapsYP----KPDRIFGIIERYKV-SIFGSTPGFIAGLRKNHISGDDFnlsSLRILG-----STGSILfSEN 411
Cdd:PRK07786 241 GAPTVI------YPlgafDPGQLLDVLEAEKVtGIFLVPAQWQAVCAEQQARPRDL---ALRVLSwgaapASDTLL-RQM 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 412 WEWF-----FSVFGKGK-CPINNIIGGTEMLGcfaqnlpnipcKIGSVGVFALGMGGDIFNEKGESVRR-ETGRVVctHP 484
Cdd:PRK07786 311 AATFpeaqiLAAFGQTEmSPVTCMLLGEDAIR-----------KLGSVGKVIPTVAARVVDENMNDVPVgEVGEIV--YR 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 485 FPSMTRGFYADEEGYQEtyfsAFRGVWAH-GDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIESALigfrAAEFRVME 563
Cdd:PRK07786 378 APTLMSGYWNNPEATAE----AFAGGWFHsGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVL----ASHPDIVE 449
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1277171962 564 AIAVGIPD-KNSENKIICFVILEGQDRLTETDeaaLRSVVADIVNPQAKPERIFAIKELPRNAAAKV 629
Cdd:PRK07786 450 VAVIGRADeKWGEVPVAVAAVRNDDAALTLED---LAEFLTDRLARYKHPKALEIVDALPRNPAGKV 513
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
190-629 |
3.56e-11 |
|
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: 65.96 E-value: 3.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 190 AKMFFMADSYSYG-GKNFTLEKIHQGVSDIFSVRHIV----VFENDAPHSPFSP--------FVFGKKEMRSVFWDDF-C 255
Cdd:cd17654 20 ADLAEKISNLSNFlRKKFQTEERAIGLRCDRGTESPVailaILFLGAAYAPIDPaspeqrslTVMKKCHVSYLLQNKElD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 256 KQGKSTIARTERCN---AEDVALMLFSSGTTrekgKKPKRILHTHGGVLAQIckeVGFG--FDCKEDDVfYWMTNFgWMM 330
Cdd:cd17654 100 NAPLSFTPEHRHFNirtDECLAYVIHTSGTT----GTPKIVAVPHKCILPNI---QHFRslFNITSEDI-LFLTSP-LTF 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 331 APW--EIVGALHFGATLVCfeGAPSYPKPDRIFGII--ERYKVSIFGSTPGFIAGLRKNHISgdDFNLS---SLRILGST 403
Cdd:cd17654 171 DPSvvEIFLSLSSGATLLI--VPTSVKVLPSKLADIlfKRHRITVLQATPTLFRRFGSQSIK--STVLSatsSLRVLALG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 404 GSILFS----ENWEwffsvfGKG-KCPINNIIGGTEmLGCFAQ----NLPNIPCKIGSvgvfalgmggDIFNEKGESVRR 474
Cdd:cd17654 247 GEPFPSlvilSSWR------GKGnRTRIFNIYGITE-VSCWALaykvPEEDSPVQLGS----------PLLGTVIEVRDQ 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 475 ETGRVVCTHPFPSMTRGFYADEegYQETYFSAFRgvwAHGDFAEMdEDGFVFMRGRSDDIINKNGIKfspanIESALIGF 554
Cdd:cd17654 310 NGSEGTGQVFLGGLNRVCILDD--EVTVPKGTMR---ATGDFVTV-KDGELFFLGRKDSQIKRRGKR-----INLDLIQQ 378
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1277171962 555 RAAEFRVMEAIAVGIPDKnseNKIICFVILEGQDRLTEtdeaalRSVVADIVNPQAKPERIFAIKELPRNAAAKV 629
Cdd:cd17654 379 VIESCLGVESCAVTLSDQ---QRLIAFIVGESSSSRIH------KELQLTLLSSHAIPDTFVQIDKLPLTSHGKV 444
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
113-634 |
7.65e-11 |
|
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: 64.64 E-value: 7.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 113 RAITFWQLKLLVDTIASAMKAHGIGKGDFVGMCMPISIDSIAVMFACFKIGAVCMQMAPTTSTDgtkdivdhvRIArakm 192
Cdd:cd17643 11 RRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVE---------RIA---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 193 FFMADSysyggknftlekihqgvsdifSVRHIVVfendaphspfspfvfgkkemrsvfwddfckqgkstiartercNAED 272
Cdd:cd17643 78 FILADS---------------------GPSLLLT------------------------------------------DPDD 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 273 VALMLFSSGTTrekgKKPKRILHTHGGVLAQI-CKEVGFGFDckEDDVFYWMTNFGWMMAPWEIVGALHFGATLVCFEGA 351
Cdd:cd17643 95 LAYVIYTSGST----GRPKGVVVSHANVLALFaATQRWFGFN--EDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYE 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 352 PSYPkPDRIFGIIERYKVSIFGSTP----GFIAGLRKNHIsgddfNLSSLR--ILGstGSILFSENWEWFFSVFGKGKCP 425
Cdd:cd17643 169 VARS-PEDFARLLRDEGVTVLNQTPsafyQLVEAADRDGR-----DPLALRyvIFG--GEALEAAMLRPWAGRFGLDRPQ 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 426 INNIIGGTE-----------MLGCFAQNLPNIPCKIGSVGVFAL---------GMGGDIFNEkGESVRR-------ETGR 478
Cdd:cd17643 241 LVNMYGITEttvhvtfrpldAADLPAAAASPIGRPLPGLRVYVLdadgrpvppGVVGELYVS-GAGVARgylgrpeLTAE 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 479 VVCTHPFPSMTRGFYADeegyqetyfsafrgvwahGDFAEMDEDG-FVFMrGRSDDIINKNGIKFSPANIESALIGFRAa 557
Cdd:cd17643 320 RFVANPFGGPGSRMYRT------------------GDLARRLPDGeLEYL-GRADEQVKIRGFRIELGEIEAALATHPS- 379
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1277171962 558 efrVMEAIAVGIPDKNSENKIICFVILEGQdrlTETDEAALRSVVADIVNPQAKPERIFAIKELPRNAAAKVPYKAI 634
Cdd:cd17643 380 ---VRDAAVIVREDEPGDTRLVAYVVADDG---AAADIAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
431-634 |
1.01e-10 |
|
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: 63.50 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 431 GGTEMLGCFAQNLPNIPCKiGSVGVFALGMGGDIFNE-----KGESVRRETGRVVCTHPFpsmtrgfyaDEEGYQETyfs 505
Cdd:cd17630 143 GMTETASQVATKRPDGFGR-GGVGVLLPGRELRIVEDgeiwvGGASLAMGYLRGQLVPEF---------NEDGWFTT--- 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 506 afrgvwahGDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIESALigfrAAEFRVMEAIAVGIPDKNSENKIICFVILE 585
Cdd:cd17630 210 --------KDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAAL----AAHPAVRDAFVVGVPDEELGQRPVAVIVGR 277
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1277171962 586 GqdrltETDEAALRSVVADIVNPQAKPERIFAIKELPRNAAAKVPYKAI 634
Cdd:cd17630 278 G-----PADPAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRAL 321
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
514-636 |
1.31e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 64.24 E-value: 1.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 514 GDFAEMDEDGFVFMRGR-SDDIINKNGIKFSPANIESALIGFRAaefrVMEAIAVGIPDKNSENKIICFVIlegqdRLTE 592
Cdd:PRK07787 355 GDVAVVDPDGMHRIVGReSTDLIKSGGYRIGAGEIETALLGHPG----VREAAVVGVPDDDLGQRIVAYVV-----GADD 425
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1277171962 593 TDEAALRSVVADIVNPQAKPERIFAIKELPRNAAAKVPYKAISR 636
Cdd:PRK07787 426 VAADELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLLS 469
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
94-632 |
1.41e-10 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 64.32 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 94 ARGLGSKVCVCYEHESGKKRAITFWQLKLLVDTIASAMKAHGIGKGDFVGMCMPISIDSIAVMFACFKIGAVCMQMAPTT 173
Cdd:PRK08008 17 ADVYGHKTALIFESSGGVVRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 174 STDGTKDIVDHvriARAKMFFMADSYS--YggknftlEKIHQgvSDIFSVRHIVVFENDAPhspfspfvfgkKEMRSVFW 251
Cdd:PRK08008 97 LREESAWILQN---SQASLLVTSAQFYpmY-------RQIQQ--EDATPLRHICLTRVALP-----------ADDGVSSF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 252 DDFCKQGKSTIARTERCNAEDVALMLFSSGTTrekgKKPKRILHTHGGVLaqickevgFG-----FDC--KEDDVFywMT 324
Cdd:PRK08008 154 TQLKAQQPATLCYAPPLSTDDTAEILFTSGTT----SRPKGVVITHYNLR--------FAgyysaWQCalRDDDVY--LT 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 325 nfgwMMAPWEI-------VGALHFGATLVCFEgapSYpKPDRIFGIIERYKVSIFGSTPGFIAGLRKNHISGDDFNlSSL 397
Cdd:PRK08008 220 ----VMPAFHIdcqctaaMAAFSAGATFVLLE---KY-SARAFWGQVCKYRATITECIPMMIRTLMVQPPSANDRQ-HCL 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 398 RilgstgSILF-----SENWEWFFSVFGkgkCPINNIIGGTEMLGCFAQNLPNIPCKIGSVGVFALGMGGDIFNEKGESV 472
Cdd:PRK08008 291 R------EVMFylnlsDQEKDAFEERFG---VRLLTSYGMTETIVGIIGDRPGDKRRWPSIGRPGFCYEAEIRDDHNRPL 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 473 -RRETGRVvCTHPFPSMT--RGFYADEEGYQETyFSAfrGVWAH-GDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIE 548
Cdd:PRK08008 362 pAGEIGEI-CIKGVPGKTifKEYYLDPKATAKV-LEA--DGWLHtGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELE 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 549 SALigfrAAEFRVMEAIAVGIPDKNSENKIICFVILEGQDRLTEtdEAALRSVVADIvnpqAK---PERIFAIKELPRNA 625
Cdd:PRK08008 438 NII----ATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSE--EEFFAFCEQNM----AKfkvPSYLEIRKDLPRNC 507
|
....*..
gi 1277171962 626 AAKVPYK 632
Cdd:PRK08008 508 SGKIIKK 514
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
269-637 |
2.65e-10 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 63.79 E-value: 2.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 269 NAEDVALMLFSSGTTREkgkkPKRILHTHGGVLAQIcKEVGFGFDCKEDDVfywmtnfgwmmapweIVGAL---H-FGAT 344
Cdd:PRK08633 780 KPDDTATIIFSSGSEGE----PKGVMLSHHNILSNI-EQISDVFNLRNDDV---------------ILSSLpffHsFGLT 839
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 345 ----LVCFEGAPS--YPKPDRIFGI---IERYKVSIFGSTPGFI-AGLRKNHISGDDFnlSSLRILGSTGSILFSENWEW 414
Cdd:PRK08633 840 vtlwLPLLEGIKVvyHPDPTDALGIaklVAKHRATILLGTPTFLrLYLRNKKLHPLMF--ASLRLVVAGAEKLKPEVADA 917
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 415 FFSVFGKgkcPINNIIGGTEMLGCFAQNLPNI---------PCKIGSVGVFALGMGGDIFN-EKGESVR-RETGRVVCTH 483
Cdd:PRK08633 918 FEEKFGI---RILEGYGATETSPVASVNLPDVlaadfkrqtGSKEGSVGMPLPGVAVRIVDpETFEELPpGEDGLILIGG 994
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 484 pfPSMTRGFYADEEGYQETYFSAFRGVW-AHGDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIESALIGFRAAEfrVM 562
Cdd:PRK08633 995 --PQVMKGYLGDPEKTAEVIKDIDGIGWyVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKALGGE--EV 1070
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1277171962 563 EAIAVGIPDKNSENKIICFVilegqdRLTETDEAALRSVVADI-VNPQAKPERIFAIKELPRNAAAKVPYKAISRV 637
Cdd:PRK08633 1071 VFAVTAVPDEKKGEKLVVLH------TCGAEDVEELKRAIKESgLPNLWKPSRYFKVEALPLLGSGKLDLKGLKEL 1140
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
95-436 |
3.40e-10 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 62.99 E-value: 3.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 95 RGLGSKVCVCYEHesgkkraITFWQLKLLVDTIASAMKAHGIGKGDFVgMCM-PISIDSIAVMFACFKIGAVCMQMAPTT 173
Cdd:PRK09274 29 GGRGADGKLAYDE-------LSFAELDARSDAIAHGLNAAGIGRGMRA-VLMvTPSLEFFALTFALFKAGAVPVLVDPGM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 174 STDGTKDIVDHVR------IARAkmffmadsysyggknftlekihQGVSDIF-----SVRHIVVFEndaphspfspfvfg 242
Cdd:PRK09274 101 GIKNLKQCLAEAQpdafigIPKA----------------------HLARRLFgwgkpSVRRLVTVG-------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 243 kkemRSVFWddfckqGKSTIARTERCNA-----------EDVALMLFSSGTTrekGkKPKRILHTHGGVLAQIckEVgfg 311
Cdd:PRK09274 145 ----GRLLW------GGTTLATLLRDGAaapfpmadlapDDMAAILFTSGST---G-TPKGVVYTHGMFEAQI--EA--- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 312 fdCKEDdvfywmtnfgWMMAPWEI------VGALH---FGATLVCFEGAPSYP---KPDRIFGIIERYKVS-IFGStPGF 378
Cdd:PRK09274 206 --LRED----------YGIEPGEIdlptfpLFALFgpaLGMTSVIPDMDPTRPatvDPAKLFAAIERYGVTnLFGS-PAL 272
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1277171962 379 I-----AGLRKNHisgddfNLSSLRILGSTGSILFSENWEWFFSVFGKGkCPINNIIGGTEML 436
Cdd:PRK09274 273 LerlgrYGEANGI------KLPSLRRVISAGAPVPIAVIERFRAMLPPD-AEILTPYGATEAL 328
|
|
| ACAS_N |
pfam16177 |
Acetyl-coenzyme A synthetase N-terminus; This domain is found at the N-terminus of many ... |
33-88 |
3.68e-10 |
|
Acetyl-coenzyme A synthetase N-terminus; This domain is found at the N-terminus of many acetyl-coenzyme A synthetase enzymes.
Pssm-ID: 465043 [Multi-domain] Cd Length: 55 Bit Score: 55.94 E-value: 3.68e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1277171962 33 QELLEAS-NDIEWFWPRAMEFLgvRWFTPYAKLYDDTEGIsHTKWFIGGKLNIYNNC 88
Cdd:pfam16177 2 EALYRRSiEDPEGFWGEVAKEL--DWFKPFDKVLDGSNGP-FAKWFVGGKLNVCYNC 55
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
272-651 |
6.17e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 61.93 E-value: 6.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 272 DVALMLFSSGTTrekgKKPKRILHTHGGV--LAQICkevgfgfdckeddvfywMTNFGW-------MMAPWEIVGALHF- 341
Cdd:PRK06188 169 DIAGLAYTGGTT----GKPKGVMGTHRSIatMAQIQ-----------------LAEWEWpadprflMCTPLSHAGGAFFl 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 342 -----GATLVCFEGApsypKPDRIFGIIERYKVSIFGSTPGFIAGLRkNHISGDDFNLSSLRIL--GST----------- 403
Cdd:PRK06188 228 ptllrGGTVIVLAKF----DPAEVLRAIEEQRITATFLVPTMIYALL-DHPDLRTRDLSSLETVyyGASpmspvrlaeai 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 404 ---GSIlfsenwewFFSVFGKGKCPINNIIGGTEmlgcfaQNLPNIPCKIGSVGVFALGMGGDIFNEKGESVrrETGRV- 479
Cdd:PRK06188 303 erfGPI--------FAQYYGQTEAPMVITYLRKR------DHDPDDPKRLTSCGRPTPGLRVALLDEDGREV--AQGEVg 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 480 -VCTHPfPSMTRGFYADEEGYQETyfsaFRGVWAH-GDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIESALigfraA 557
Cdd:PRK06188 367 eICVRG-PLVMDGYWNRPEETAEA----FRDGWLHtGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVL-----A 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 558 EFRVMEAIAV-GIPD-KNSENKIICFVILEGQDRltetDEAALRSVVADIVNPQAKPERIFAIKELPRNAAAKVPYKAIS 635
Cdd:PRK06188 437 EHPAVAQVAViGVPDeKWGEAVTAVVVLRPGAAV----DAAELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALR 512
|
410
....*....|....*.
gi 1277171962 636 rvfcDRYVIAQTRVVN 651
Cdd:PRK06188 513 ----ARYWEGRGRAVG 524
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
272-629 |
1.47e-09 |
|
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: 60.21 E-value: 1.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 272 DVALMLFSSGTTrekgKKPKRILHTHGGVLaQICKEVGFGFDCKEDDVFY----WMTNFGWMMApweIVGALHFGATLV- 346
Cdd:cd17638 1 DVSDIMFTSGTT----GRSKGVMCAHRQTL-RAAAAWADCADLTEDDRYLiinpFFHTFGYKAG---IVACLLTGATVVp 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 347 --CFEgapsypkPDRIFGIIERYKVSIFGSTPGFIAGLRkNHISGDDFNLSSLRilgstgsilfsenwewfFSVFGKGKC 424
Cdd:cd17638 73 vaVFD-------VDAILEAIERERITVLPGPPTLFQSLL-DHPGRKKFDLSSLR-----------------AAVTGAATV 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 425 PINNIIGGTEMLGcfaqnLPNIPCKIG--SVGVFALGMGGDIFnekgESVRRETGR------VVCTHPF------PSMTR 490
Cdd:cd17638 128 PVELVRRMRSELG-----FETVLTAYGltEAGVATMCRPGDDA----ETVATTCGRacpgfeVRIADDGevlvrgYNVMQ 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 491 GFYADEEGYQETYFSafRGvWAH-GDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIESALigfrAAEFRVMEAIAVGI 569
Cdd:cd17638 199 GYLDDPEATAEAIDA--DG-WLHtGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGAL----AEHPGVAQVAVIGV 271
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1277171962 570 PDKNSENKIICFVILEGQDRLTETDEAAL-RSVVADIVNPQAkperIFAIKELPRNAAAKV 629
Cdd:cd17638 272 PDERMGEVGKAFVVARPGVTLTEEDVIAWcRERLANYKVPRF----VRFLDELPRNASGKV 328
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
487-629 |
2.19e-09 |
|
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: 60.39 E-value: 2.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 487 SMTRGFYADEEGYQEtyfsAFRGVWAH-GDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIESALIGFRAaefrVMEAI 565
Cdd:cd12118 348 IVMKGYLKNPEATAE----AFRGGWFHsGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPA----VLEAA 419
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1277171962 566 AVGIPDKNSENKIICFVIL-EGQDRLTETDEAALRSVVADIVNPqakpeRIFAIKELPRNAAAKV 629
Cdd:cd12118 420 VVARPDEKWGEVPCAFVELkEGAKVTEEEIIAFCREHLAGFMVP-----KTVVFGELPKTSTGKI 479
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
274-629 |
2.39e-09 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 60.02 E-value: 2.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 274 ALMLFSSGTTR-EKGKKP---KRILHTHGGVLAQICKevGFgFDCKEDDVFYWMTNFgWMMAPWEIVGALH-FGATLVCf 348
Cdd:PRK13390 151 AVMLYSSGTTGfPKGIQPdlpGRDVDAPGDPIVAIAR--AF-YDISESDIYYSSAPI-YHAAPLRWCSMVHaLGGTVVL- 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 349 egAPSYPKPDRIfGIIERYKVSIFGSTPG-FIAGLRKNHISGDDFNLSSLR----------------ILGSTGSILfsen 411
Cdd:PRK13390 226 --AKRFDAQATL-GHVERYRITVTQMVPTmFVRLLKLDADVRTRYDVSSLRavihaaapcpvdvkhaMIDWLGPIV---- 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 412 WEWFFSvfgkgkcpinniiggTEMLGCFAQNLPNIPCKIGSVGVFALGM-------GGDIFNEKGESVRRETGRVvcthP 484
Cdd:PRK13390 299 YEYYSS---------------TEAHGMTFIDSPDWLAHPGSVGRSVLGDlhicdddGNELPAGRIGTVYFERDRL----P 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 485 FpsmtrGFYADEEGYQETYFSAFRGVWAHGDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIESALIGFRAaefrVMEA 564
Cdd:PRK13390 360 F-----RYLNDPEKTAAAQHPAHPFWTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPA----VHDV 430
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1277171962 565 IAVGIPDKNSENKIICFV-ILEGQDRLTETDEAALRSVVADIVNPQAkPERIFAIKELPRNAAAKV 629
Cdd:PRK13390 431 AVIGVPDPEMGEQVKAVIqLVEGIRGSDELARELIDYTRSRIAHYKA-PRSVEFVDELPRTPTGKL 495
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
505-638 |
2.67e-09 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 59.29 E-value: 2.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 505 SAFRGVWAHGDFAE-----MDE-----DGFVFMRGRSDDIINKNGIKFSPANIESALIGFRAaefrVMEAIAVGIPDKNS 574
Cdd:PRK07824 219 KGYRNPVDPDPFAEpgwfrTDDlgaldDGVLTVLGRADDAISTGGLTVLPQVVEAALATHPA----VADCAVFGLPDDRL 294
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1277171962 575 ENKIICFVILEGQDRLTEtdeAALRSVVADIVNPQAKPERIFAIKELPRNAAAKVPYKAISRVF 638
Cdd:PRK07824 295 GQRVVAAVVGDGGPAPTL---EALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVRRF 355
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
127-630 |
2.85e-09 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 60.03 E-value: 2.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 127 IASAMKAHGIGKGDFVGMCMPISIDSIAVMFACFKIGAVcmqMAPTTSTDGTKDIVDHVRIARAKMFFMADSYSYGGKNf 206
Cdd:PLN03102 52 LAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAV---LNPINTRLDATSIAAILRHAKPKILFVDRSFEPLARE- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 207 TLEKIHQGVSDIfSVRHIVVFENDAPHSPFSpfvfgkKEMRsvfWDDFCKQGKST---IARTERCNAEDVALML-FSSGT 282
Cdd:PLN03102 128 VLHLLSSEDSNL-NLPVIFIHEIDFPKRPSS------EELD---YECLIQRGEPTpslVARMFRIQDEHDPISLnYTSGT 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 283 TREkgkkPKRILHTHGGVLAQICKEVgFGFDCKEDDVFYWMTNF----GWMMaPWEIVGAlhfGATLVCFE--GAPsypk 356
Cdd:PLN03102 198 TAD----PKGVVISHRGAYLSTLSAI-IGWEMGTCPVYLWTLPMfhcnGWTF-TWGTAAR---GGTSVCMRhvTAP---- 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 357 pdRIFGIIERYKVSIFGSTPGFIAGLRKnhisGDDFNLS---------------------SLRILG-----------STG 404
Cdd:PLN03102 265 --EIYKNIEMHNVTHMCCVPTVFNILLK----GNSLDLSprsgpvhvltggspppaalvkKVQRLGfqvmhayglteATG 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 405 SILFSEnW--EWffsvfgkGKCPINNIIGGTEMLGCFAQNLPNIpckigsvgvfalgmggDIFNEKG-ESVRRE---TGR 478
Cdd:PLN03102 339 PVLFCE-WqdEW-------NRLPENQQMELKARQGVSILGLADV----------------DVKNKETqESVPRDgktMGE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 479 VVCTHPfpSMTRGFYADEEGYQEtyfsAFRGVWAH-GDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIESALIGFRaa 557
Cdd:PLN03102 395 IVIKGS--SIMKGYLKNPKATSE----AFKHGWLNtGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYP-- 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 558 efRVMEAIAVGIPDKNSENKIICFVILEGQDRLTETDEAALRSVVADIVN------PQAK-PERIFAIKELPRNAAAKVP 630
Cdd:PLN03102 467 --KVLETAVVAMPHPTWGETPCAFVVLEKGETTKEDRVDKLVTRERDLIEycrenlPHFMcPRKVVFLQELPKNGNGKIL 544
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
248-629 |
4.15e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 59.31 E-value: 4.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 248 SVFWDDFCKQGKSTIARTERCNAEDVALMLFSSGTTREkgkkPKRILHTHGGV------LAQickevgfGFDCKEDDVFY 321
Cdd:PRK07867 129 SPAWADELAAHRDAEPPFRVADPDDLFMLIFTSGTSGD----PKAVRCTHRKVasagvmLAQ-------RFGLGPDDVCY 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 322 W-MTNF--GWMMAPWEIvgALHFGATLVcfegapsypkpdrifgIIERYKVSifgstpGFIAGLRK------NHI----- 387
Cdd:PRK07867 198 VsMPLFhsNAVMAGWAV--ALAAGASIA----------------LRRKFSAS------GFLPDVRRygatyaNYVgkpls 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 388 -------SGDDFNlSSLRIL----GSTGSIlfsenwEWFFSVFGkgkCPINNIIGGTEmLGCFAQNLPNIPCkiGSVGVF 456
Cdd:PRK07867 254 yvlatpeRPDDAD-NPLRIVygneGAPGDI------ARFARRFG---CVVVDGFGSTE-GGVAITRTPDTPP--GALGPL 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 457 ALGM-----------GGDIFNEKGESVRRE-TGRVVCTHPfPSMTRGFYADEEGYQETyfsaFRGVWAH-GDFAEMDEDG 523
Cdd:PRK07867 321 PPGVaivdpdtgtecPPAEDADGRLLNADEaIGELVNTAG-PGGFEGYYNDPEADAER----MRGGVYWsGDLAYRDADG 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 524 FVFMRGRSDDIINKNGIKFSPANIESALIGFRAAEfrvmEAIAVGIPDKNSENKIICFVILEGQDRLTETDEAALRSVVA 603
Cdd:PRK07867 396 YAYFAGRLGDWMRVDGENLGTAPIERILLRYPDAT----EVAVYAVPDPVVGDQVMAALVLAPGAKFDPDAFAEFLAAQP 471
|
410 420
....*....|....*....|....*.
gi 1277171962 604 DiVNPQAKPERIFAIKELPRNAAAKV 629
Cdd:PRK07867 472 D-LGPKQWPSYVRVCAELPRTATFKV 496
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
509-629 |
4.26e-09 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 59.39 E-value: 4.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 509 GVWAHGDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIESALigfrAAEFRVMEAIAVGIPDKNSENKIICFVILEGQD 588
Cdd:PRK13382 416 GFMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTL----ATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGA 491
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1277171962 589 RLTETDeaaLRSVVADIVNPQAKPERIFAIKELPRNAAAKV 629
Cdd:PRK13382 492 SATPET---LKQHVRDNLANYKVPRDIVVLDELPRGATGKI 529
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
116-594 |
5.03e-09 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 59.44 E-value: 5.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 116 TFWQLKLLVDTIASAMKAHGIGKGDFVGMCMPISIDSIAVMFACFKIGA--VCMQMAPTTSTdgtkdiVDHV-RIARAKM 192
Cdd:PRK08315 45 TYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAilVTINPAYRLSE------LEYAlNQSGCKA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 193 FFMADSY---SYggknftLEKIHQGVSDIfsvRHIVVFENDAPHSPFSPFVF--GKKEMRSVF-WDDFCKQGKST----- 261
Cdd:PRK08315 119 LIAADGFkdsDY------VAMLYELAPEL---ATCEPGQLQSARLPELRRVIflGDEKHPGMLnFDELLALGRAVddael 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 262 IARTERCNAEDVALMLFSSGTTrekGKkPKRILHTHGGVL--------AQ-------ICKEVGFgFDCkeddvfywmtnF 326
Cdd:PRK08315 190 AARQATLDPDDPINIQYTSGTT---GF-PKGATLTHRNILnngyfigeAMklteedrLCIPVPL-YHC-----------F 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 327 GWMMApweIVGALHFGATLVcfegapsYP----KPDRIFGIIERYK-VSIFGSTPGFIAGLrkNHISGDDFNLSSLR--I 399
Cdd:PRK08315 254 GMVLG---NLACVTHGATMV-------YPgegfDPLATLAAVEEERcTALYGVPTMFIAEL--DHPDFARFDLSSLRtgI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 400 L-GSTgsilfsenwewffsvfgkgkCPI------NNIIGGTEMLGCFAQN-------------------------LPNIP 447
Cdd:PRK08315 322 MaGSP--------------------CPIevmkrvIDKMHMSEVTIAYGMTetspvstqtrtddplekrvttvgraLPHLE 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 448 CKIgsvgvfalgmggdIFNEKGESVRR-ETGRVvCTHPFPSMtRGFYADEEGYQETYFSAfrGvWAH-GDFAEMDEDGFV 525
Cdd:PRK08315 382 VKI-------------VDPETGETVPRgEQGEL-CTRGYSVM-KGYWNDPEKTAEAIDAD--G-WMHtGDLAVMDEEGYV 443
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1277171962 526 FMRGRSDDIINKNGIKFSPANIEsaligfraaEF-----RVMEAIAVGIPD-KNSEnkIIC-FVIL-EGQDrLTETD 594
Cdd:PRK08315 444 NIVGRIKDMIIRGGENIYPREIE---------EFlythpKIQDVQVVGVPDeKYGE--EVCaWIILrPGAT-LTEED 508
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
109-629 |
5.76e-09 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 58.94 E-value: 5.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 109 SGKkRAITFWQLKLLVDTIASAMKAHGIGKGDFVGMCMPISIDSIAVMFACFKIGAVCMQMAPTTSTD---------GTK 179
Cdd:PRK12406 7 SGD-RRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEeiayiledsGAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 180 DIVDHVRIARAkmffMADSysyggknftlekIHQGVSdIFSVRH----IVVFENDAPHSPFSPFvfgkkemrSVFWDDFC 255
Cdd:PRK12406 86 VLIAHADLLHG----LASA------------LPAGVT-VLSVPTppeiAAAYRISPALLTPPAG--------AIDWEGWL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 256 KQGKSTIARTercnAEDVALMLFSSGTT-REKGKKPKRILHTHGGVLAQIcKEVGFGFdckEDDVFYWMTNFGWMMAPWE 334
Cdd:PRK12406 141 AQQEPYDGPP----VPQPQSMIYTSGTTgHPKGVRRAAPTPEQAAAAEQM-RALIYGL---KPGIRALLTGPLYHSAPNA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 335 I-VGALHFGATLVC---FEgapsypkPDRIFGIIERYKVSIFGSTPG-FIAGLRKNHISGDDFNLSSLRilgstgsilfs 409
Cdd:PRK12406 213 YgLRAGRLGGVLVLqprFD-------PEELLQLIERHRITHMHMVPTmFIRLLKLPEEVRAKYDVSSLR----------- 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 410 enwewfFSVFGKGKCP--------------INNIIGGTE---MLGCFAQNLPNIPckiGSVGVFALGMGGDIFNEKGESV 472
Cdd:PRK12406 275 ------HVIHAAAPCPadvkramiewwgpvIYEYYGSTEsgaVTFATSEDALSHP---GTVGKAAPGAELRFVDEDGRPL 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 473 RR-ETGRVVCTHP-FPSMTrgFYADEEGYQEtyfsAFRGVW-AHGDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIES 549
Cdd:PRK12406 346 PQgEIGEIYSRIAgNPDFT--YHNKPEKRAE----IDRGGFiTSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEA 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 550 ALIGFRAaefrVMEAIAVGIPDKNSENKIICFVILEGQDRLTETD-EAALRSVVADIvnpqAKPERIFAIKELPRNAAAK 628
Cdd:PRK12406 420 VLHAVPG----VHDCAVFGIPDAEFGEALMAVVEPQPGATLDEADiRAQLKARLAGY----KVPKHIEIMAELPREDSGK 491
|
.
gi 1277171962 629 V 629
Cdd:PRK12406 492 I 492
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
271-634 |
6.55e-09 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 58.63 E-value: 6.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 271 EDVALMLFSSGTTrekgKKPKRILHTHGGVL-AQICKEVGFGFDCKEDDVFYwMTNFGWMMAPWEIVGALHFGATLV-CF 348
Cdd:cd17650 93 EDLAYVIYTSGTT----GKPKGVMVEHRNVAhAAHAWRREYELDSFPVRLLQ-MASFSFDVFAGDFARSLLNGGTLViCP 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 349 EGAPSypKPDRIFGIIERYKVSIFGSTPGFIAGLRKnHISGDDFNLSSLRILGSTGSILFSENWEWFFSVFGKGKCPINN 428
Cdd:cd17650 168 DEVKL--DPAALYDLILKSRITLMESTPALIRPVMA-YVYRNGLDLSAMRLLIVGSDGCKAQDFKTLAARFGQGMRIINS 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 429 IiGGTEmlgcfaqnlpnipCKIGSvGVFALGMGGDIfnekgesvrrETGRVVCTHPFPSMT------------------- 489
Cdd:cd17650 245 Y-GVTE-------------ATIDS-TYYEEGRDPLG----------DSANVPIGRPLPNTAmyvlderlqpqpvgvagel 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 490 --------RGFYADEEGYQETY----FSAFRGVWAHGDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIESALigfrAA 557
Cdd:cd17650 300 yiggagvaRGYLNRPELTAERFvenpFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQL----AR 375
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1277171962 558 EFRVMEAIAVGIPDKNSENKIICFVILEGQdrlteTDEAALRSVVADIVNPQAKPERIFAIKELPRNAAAKVPYKAI 634
Cdd:cd17650 376 HPAIDEAVVAVREDKGGEARLCAYVVAAAT-----LNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
261-635 |
7.67e-09 |
|
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: 58.57 E-value: 7.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 261 TIARTERCNAEDVALMLFSSGTTrekgKKPKRILHTHGGVL---AQICKEvgFGFDCKEDDVFYWMTNFGWMMAPWEIVG 337
Cdd:cd17648 84 TGARVVITNSTDLAYAIYTSGTT----GKPKGVLVEHGSVVnlrTSLSER--YFGRDNGDEAVLFFSNYVFDFFVEQMTL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 338 ALHFGATLVCFEGAPSYpKPDRIFGIIERYKVSIFGSTPGFIaglrkNHIsgdDF-NLSSLRILGSTGSILFSENWEWFF 416
Cdd:cd17648 158 ALLNGQKLVVPPDEMRF-DPDRFYAYINREKVTYLSGTPSVL-----QQY---DLaRLPHLKRVDAAGEEFTAPVFEKLR 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 417 SVFGKgkcPINNIIGGTEM------------------LGCfaqNLPNIPC----------KIGSVGvfALGMGGDIFNEk 468
Cdd:cd17648 229 SRFAG---LIINAYGPTETtvtnhkrffpgdqrfdksLGR---PVRNTKCyvlndamkrvPVGAVG--ELYLGGDGVAR- 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 469 GESVRRE-TGRVVCTHPfpsmtrgFYADEEGYQETYFSAFRGvwahGDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANI 547
Cdd:cd17648 300 GYLNRPElTAERFLPNP-------FQTEQERARGRNARLYKT----GDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEV 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 548 ESALIGFRAaefrVMEAIAV-----GIPDKNSENKIICFVILEgqdrlTET-DEAALRSVVADIVNPQAKPERIFAIKEL 621
Cdd:cd17648 369 EAALASYPG----VRECAVVakedaSQAQSRIQKYLVGYYLPE-----PGHvPESDLLSFLRAKLPRYMVPARLVRLEGI 439
|
410
....*....|....
gi 1277171962 622 PRNAAAKVPYKAIS 635
Cdd:cd17648 440 PVTINGKLDVRALP 453
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
113-634 |
7.92e-09 |
|
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: 58.53 E-value: 7.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 113 RAITFWQLKLLVDTIASAMKAHGIGKGDFVGMCMPISIDSIAVMFACFKIGAVCMQMAPTTSTDgtkdivdhvRIARAkm 192
Cdd:cd17649 11 QSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAE---------RLRYM-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 193 ffMADSysyggknftlekihqGVSDIFSvrhivvfendapHSPfspfvfgkkemrsvfwddfckqgkstiartercnaED 272
Cdd:cd17649 80 --LEDS---------------GAGLLLT------------HHP-----------------------------------RQ 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 273 VALMLFSSGTTrekgKKPKRILHTHGGvLAQICKEVGFGFDCKEDDVFYWMTNFGWMMAPWEIVGALHFGATLVcFEGAP 352
Cdd:cd17649 96 LAYVIYTSGST----GTPKGVAVSHGP-LAAHCQATAERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVV-LRPDE 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 353 SYPKPDRIFGIIERYKVSIFGSTPGFIAGLRKNHISGDDFNLSSLRILGSTGSILFSENW-------EWFFSVFGKG--- 422
Cdd:cd17649 170 LWASADELAEMVRELGVTVLDLPPAYLQQLAEEADRTGDGRPPSLRLYIFGGEALSPELLrrwlkapVRLFNAYGPTeat 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 423 ------KCPINNIIGGTEM-LGcfaQNLPNI----------PCKIGSVGVFALGmggdifnekGESVRRE-TGRVVCTH- 483
Cdd:cd17649 250 vtplvwKCEAGAARAGASMpIG---RPLGGRsayildadlnPVPVGVTGELYIG---------GEGLARGyLGRPELTAe 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 484 ---PFPSMTRGfyadeegyQETYFSafrgvwahGDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIESALIGFRAaefr 560
Cdd:cd17649 318 rfvPDPFGAPG--------SRLYRT--------GDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPG---- 377
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1277171962 561 VMEAIAVGIPDkNSENKIICFVILEGQDRLTETDeAALRSVVADIVNPQAKPERIFAIKELPRNAAAKVPYKAI 634
Cdd:cd17649 378 VREAAVVALDG-AGGKQLVAYVVLRAAAAQPELR-AQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKAL 449
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
113-571 |
2.06e-08 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 57.31 E-value: 2.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 113 RAITFWQLKLLVDTIASAMKAHGIGKGDFVGMCMPISIDSIAVMFACFKIGAV----------------CMQMAPTTStd 176
Cdd:PRK10946 47 RQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGVApvnalfshqrselnayASQIEPALL-- 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 177 gtkdIVDhvriaRAKMFFMADSYsyggknftlekIHQGVSDIFSVRHIVVFENDAPHS-------PFSPFVFGkkemrsv 249
Cdd:PRK10946 125 ----IAD-----RQHALFSDDDF-----------LNTLVAEHSSLRVVLLLNDDGEHSlddainhPAEDFTAT------- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 250 fwddfckqgkSTiartercNAEDVALMLFSSGTTrekgKKPKRILHTHGGVL------AQICkevgfGFDCKeddvfywm 323
Cdd:PRK10946 178 ----------PS-------PADEVAFFQLSGGST----GTPKLIPRTHNDYYysvrrsVEIC-----GFTPQ-------- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 324 TNF--------GWMMAPWEIVGALHFGATLVCfegAPSyPKPDRIFGIIERYKVSIFGSTPGFIA-GLRKNHISGDDFNL 394
Cdd:PRK10946 224 TRYlcalpaahNYPMSSPGALGVFLAGGTVVL---APD-PSATLCFPLIEKHQVNVTALVPPAVSlWLQAIAEGGSRAQL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 395 SSLRILgSTGSILFSENW-EWFFSVFGkgkCPINNIIGGTEMLGCFAQnLPNIPCKI-GSVGvfaLGMGGD----IFNEK 468
Cdd:PRK10946 300 ASLKLL-QVGGARLSETLaRRIPAELG---CQLQQVFGMAEGLVNYTR-LDDSDERIfTTQG---RPMSPDdevwVADAD 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 469 GESVRR-ETGRVvcthpfpsMTRGFYA---------------DEEGYqetYFSafrgvwahGDFAEMDEDGFVFMRGRSD 532
Cdd:PRK10946 372 GNPLPQgEVGRL--------MTRGPYTfrgyykspqhnasafDANGF---YCS--------GDLVSIDPDGYITVVGREK 432
|
490 500 510
....*....|....*....|....*....|....*....
gi 1277171962 533 DIINKNGIKFSPANIESALIGFRAaefrVMEAIAVGIPD 571
Cdd:PRK10946 433 DQINRGGEKIAAEEIENLLLRHPA----VIHAALVSMED 467
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
547-628 |
2.27e-08 |
|
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: 51.39 E-value: 2.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 547 IESALIGFRAaefrVMEAIAVGIPDKNSENKIICFVILEGQdrlTETDEAALRSVVADIVNPQAKPERIFAIKELPRNAA 626
Cdd:pfam13193 2 VESALVSHPA----VAEAAVVGVPDELKGEAPVAFVVLKPG---VELLEEELVAHVREELGPYAVPKEVVFVDELPKTRS 74
|
..
gi 1277171962 627 AK 628
Cdd:pfam13193 75 GK 76
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
115-629 |
1.29e-07 |
|
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: 54.58 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 115 ITFWQLKLLVDTIASAMKAHGIGKGDFVGMCMPISIDSIAVMFACFKIGAVCMQMAPTTSTDgtkdivdhvRIARakmff 194
Cdd:cd12114 13 LTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAA---------RREA----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 195 madsysyggknftlekihqgvsdIFSVRHIVVFENDAPHSPFSPFVFgkkemrSVFWDDFCKQGKSTIARTERCNAEDVA 274
Cdd:cd12114 79 -----------------------ILADAGARLVLTDGPDAQLDVAVF------DVLILDLDALAAPAPPPPVDVAPDDLA 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 275 LMLFSSGTTrekGKkPKRILHTHGGVLAQICkEVGFGFDCKEDDVFYWMTNFGWMMAPWEIVGALHFGATLVCFEGAPSy 354
Cdd:cd12114 130 YVIFTSGST---GT-PKGVMISHRAALNTIL-DINRRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARR- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 355 PKPDRIFGIIERYKVSIFGSTPGfIAGLRKNHISGDDFNLSSLRIlgstgsILFSENWewffsvfgkgkcpinniIGgte 434
Cdd:cd12114 204 RDPAHWAELIERHGVTLWNSVPA-LLEMLLDVLEAAQALLPSLRL------VLLSGDW-----------------IP--- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 435 mlgcfaQNLPNIPCKIGSVGVFaLGMGG-------DIFNEKGE------SV------RRETGRVVCTH--PFP------- 486
Cdd:cd12114 257 ------LDLPARLRALAPDARL-ISLGGateasiwSIYHPIDEvppdwrSIpygrplANQRYRVLDPRgrDCPdwvpgel 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 487 -----SMTRGFYADEEGYQETYFSAFRGVWAH--GDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIESALIGFRAaef 559
Cdd:cd12114 330 wiggrGVALGYLGDPELTAARFVTHPDGERLYrtGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPG--- 406
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 560 rVMEAIAVGIPDKNsENKIICFVILEGQDrlTETDEAALRSVVADIVNPQAKPERIFAIKELPRNAAAKV 629
Cdd:cd12114 407 -VARAVVVVLGDPG-GKRLAAFVVPDNDG--TPIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKV 472
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
269-552 |
1.42e-07 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341240 [Multi-domain] Cd Length: 463 Bit Score: 54.37 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 269 NAEDVALMLFSSGTTrekgKKPKRILHTHGGVLAQI--CKEVGFgfdCKEDDVFYWMTNFGWMMA-PWEIVGALHFGATL 345
Cdd:cd05914 87 DEDDVALINYTSGTT----GNSKGVMLTYRNIVSNVdgVKEVVL---LGKGDKILSILPLHHIYPlTFTLLLPLLNGAHV 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 346 VCFEGAPSypkPDRIFGIIERYKVSIFGSTPGFIAGLRKNHI------SGDDFNLSSLRILGSTGSILFSENWEWF---F 416
Cdd:cd05914 160 VFLDKIPS---AKIIALAFAQVTPTLGVPVPLVIEKIFKMDIipkltlKKFKFKLAKKINNRKIRKLAFKKVHEAFggnI 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 417 SVFGKGKCPINNII---------------GGTEMLGCFAQNLPNiPCKIGSVGVFALGMGGDIFNEKGESvrrETGRVVC 481
Cdd:cd05914 237 KEFVIGGAKINPDVeeflrtigfpytigyGMTETAPIISYSPPN-RIRLGSAGKVIDGVEVRIDSPDPAT---GEGEIIV 312
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1277171962 482 THPfpSMTRGFYADEEGYQEtyfsAF-RGVWAH-GDFAEMDEDGFVFMRGRSDD-IINKNGIKFSPANIESALI 552
Cdd:cd05914 313 RGP--NVMKGYYKNPEATAE----AFdKDGWFHtGDLGKIDAEGYLYIRGRKKEmIVLSSGKNIYPEEIEAKIN 380
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
511-629 |
1.61e-07 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 54.50 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 511 WAH-GDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIESALigfrAAEFRVMEAIAVGIPDKNSeNKIICFVILEGQDR 589
Cdd:PRK08751 438 WLHtGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVI----AMMPGVLEVAAVGVPDEKS-GEIVKVVIVKKDPA 512
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1277171962 590 LTETD-EAALRSVVADIVNPQAKPERifaiKELPRNAAAKV 629
Cdd:PRK08751 513 LTAEDvKAHARANLTGYKQPRIIEFR----KELPKTNVGKI 549
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
486-641 |
1.62e-07 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 54.51 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 486 PSMTRGFYADEEgyqeTYFSAFRGVWAH-GDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIESALigfrAAEFRVMEA 564
Cdd:PRK05852 388 TTVVRGYLGDPT----ITAANFTDGWLRtGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVL----ASHPNVMEA 459
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1277171962 565 IAVGIPDKNSENKIICFVILEGQDRLTETDEAAL-RSVVAdivnPQAKPERIFAIKELPRNAAAKVPYKAISRVFCDR 641
Cdd:PRK05852 460 AVFGVPDQLYGEAVAAVIVPRESAPPTAEELVQFcRERLA----AFEIPASFQEASGLPHTAKGSLDRRAVAEQFGHS 533
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
256-583 |
3.26e-07 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 53.29 E-value: 3.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 256 KQGKSTIARTERCNAEDVALMLFSSGTTrekgKKPKRILHTHGGVLAQICKEVGFGFDCKEDDVFYWMTNFGWMMAPWEI 335
Cdd:PRK12492 192 RQGRGLSLKPVPVGLDDIAVLQYTGGTT----GLAKGAMLTHGNLVANMLQVRACLSQLGPDGQPLMKEGQEVMIAPLPL 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 336 VGALHFGATLVCFEGAPSY----PKPDRIFGIIERYKVSIFGSTPG----FIAGLrkNHISGDDFNLSSLRILGSTGSIL 407
Cdd:PRK12492 268 YHIYAFTANCMCMMVSGNHnvliTNPRDIPGFIKELGKWRFSALLGlntlFVALM--DHPGFKDLDFSALKLTNSGGTAL 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 408 FSENWEWFFSVFGkgkCPINNIIGGTEMLGCFAQNLPNIPCKIGSVGVFALGMGGDIFNEKG-ESVRRETGRVvCTHPfP 486
Cdd:PRK12492 346 VKATAERWEQLTG---CTIVEGYGLTETSPVASTNPYGELARLGTVGIPVPGTALKVIDDDGnELPLGERGEL-CIKG-P 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 487 SMTRGFYADEEGYQETYFSafRGVWAHGDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIESALIgfraAEFRVMEAIA 566
Cdd:PRK12492 421 QVMKGYWQQPEATAEALDA--EGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVM----AHPKVANCAA 494
|
330
....*....|....*..
gi 1277171962 567 VGIPDKNSENKIICFVI 583
Cdd:PRK12492 495 IGVPDERSGEAVKLFVV 511
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
113-633 |
4.02e-07 |
|
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: 53.05 E-value: 4.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 113 RAITFWQLKLLVDTIASAMKAHGIGKGDFVGMCMPISIDSIAVMFACFKIGAVCMQMAPTTSTDgtkdivdhvRIArakm 192
Cdd:cd17646 22 RTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPAD---------RLA---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 193 FFMADSysygGKNFTLEKIHQGVSDIFSVRHIVVFENDAPHSPFSPfvfgkkemrsvfwddfckqgksTIARTERCNAed 272
Cdd:cd17646 89 YMLADA----GPAVVLTTADLAARLPAGGDVALLGDEALAAPPATP----------------------PLVPPRPDNL-- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 273 vALMLFSSGTTrekGKkPKRILHTHGGV---LAQICKEVGFGfdckEDDVFYWMTNFGWMMAPWEIVGALHFGATLVcfe 349
Cdd:cd17646 141 -AYVIYTSGST---GR-PKGVMVTHAGIvnrLLWMQDEYPLG----PGDRVLQKTPLSFDVSVWELFWPLVAGARLV--- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 350 gapsYPKPDR------IFGIIERYKVSIFGSTPG----FIAglrknhiSGDDFNLSSLRILGSTGSILFSENWEWFFSVF 419
Cdd:cd17646 209 ----VARPGGhrdpayLAALIREHGVTTCHFVPSmlrvFLA-------EPAAGSCASLRRVFCSGEALPPELAARFLALP 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 420 GkgkCPINNIIGGTEML------GCFAqNLPNIPCKIGS----VGVFAL---------GMGGDIFnEKGESVRR------ 474
Cdd:cd17646 278 G---AELHNLYGPTEAAidvthwPVRG-PAETPSVPIGRpvpnTRLYVLddalrpvpvGVPGELY-LGGVQLARgylgrp 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 475 -ETGRVVCTHPFPSMTRgfyadeegyqetyfsafrgVWAHGDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIESALig 553
Cdd:cd17646 353 aLTAERFVPDPFGPGSR-------------------MYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAAL-- 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 554 frAAEFRVMEAIAVGIPDKNSENKIICFVIleGQDRLTETDEAALRSVVADIVNPQAKPERIFAIKELPRNAAAKVPYKA 633
Cdd:cd17646 412 --AAHPAVTHAVVVARAAPAGAARLVGYVV--PAAGAAGPDTAALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAA 487
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
270-629 |
4.67e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 53.11 E-value: 4.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 270 AEDVALMLFSSGTTrekgKKPKRILHTHGgVLAQICKEVGFGFDCKEDDVFYW-MTNF--GWMMAPWEIvgALHFGATLV 346
Cdd:PRK13388 149 AMDPFMLIFTSGTT----GAPKAVRCSHG-RLAFAGRALTERFGLTRDDVCYVsMPLFhsNAVMAGWAP--AVASGAAVA 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 347 cfegAPSYPKPDRIFGIIERYKVSIF---GSTPGFI-AGLRKNhisgDDFNlSSLRI-LGSTGSIlfsENWEWFFSVFGk 421
Cdd:PRK13388 222 ----LPAKFSASGFLDDVRRYGATYFnyvGKPLAYIlATPERP----DDAD-NPLRVaFGNEASP---RDIAEFSRRFG- 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 422 gkCPINNIIGGTEMlGCFAQNLPNIPCkiGSVGVFALGM---GGDIFNEKGESVRRETGRV----------VCTHPfPSM 488
Cdd:PRK13388 289 --CQVEDGYGSSEG-AVIVVREPGTPP--GSIGRGAPGVaiyNPETLTECAVARFDAHGALlnadeaigelVNTAG-AGF 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 489 TRGFYADEEGYQETyfsaFRGVWA-HGDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIESALIGFRAaefrVMEAIAV 567
Cdd:PRK13388 363 FEGYYNNPEATAER----MRHGMYwSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPA----INRVAVY 434
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1277171962 568 GIPDKNSENKIICFVILEGQDRLTETDEAALRSVVADIvNPQAKPERIFAIKELPRNAAAKV 629
Cdd:PRK13388 435 AVPDERVGDQVMAALVLRDGATFDPDAFAAFLAAQPDL-GTKAWPRYVRIAADLPSTATNKV 495
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
376-592 |
1.16e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 51.69 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 376 PGFIAGLRKNHISG--------------DDF---NLSSLRILGSTGSILFSENWEWFFSVFGkgkCPINNIIGGTEMLGC 438
Cdd:PRK05677 290 PAMVKELGKWKFSGfvglntlfvalcnnEAFrklDFSALKLTLSGGMALQLATAERWKEVTG---CAICEGYGMTETSPV 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 439 FAQNlPNIPCKIGSVGVFALGMGGDIFNEKGESVRR-ETGRVvCTHPfPSMTRGFYADEEGYQETYFSafRGVWAHGDFA 517
Cdd:PRK05677 367 VSVN-PSQAIQVGTIGIPVPSTLCKVIDDDGNELPLgEVGEL-CVKG-PQVMKGYWQRPEATDEILDS--DGWLKTGDIA 441
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1277171962 518 EMDEDGFVFMRGRSDDIINKNGIKFSPANIESALigfrAAEFRVMEAIAVGIPDKNSENKIICFVILEGQDRLTE 592
Cdd:PRK05677 442 LIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVL----AALPGVLQCAAIGVPDEKSGEAIKVFVVVKPGETLTK 512
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
467-629 |
1.17e-06 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 51.52 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 467 EKGESVRRETGRVVCTHPFPSMtRGFYADEEgyqETYFSAFRGVWAH-GDFAEMDEDGFVFMRGRSDDIINKNGIKFSPA 545
Cdd:PLN02330 378 DTGRSLPKNTPGELCVRSQCVM-QGYYNNKE---ETDRTIDEDGWLHtGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPA 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 546 NIESALIGFRAAEfrvmEAIAVGIPDKNS-ENKIICFVIlegQDRLTETDEAALrSVVADIVNPQAKPERIFAIKELPRN 624
Cdd:PLN02330 454 ELEAILLTHPSVE----DAAVVPLPDEEAgEIPAACVVI---NPKAKESEEDIL-NFVAANVAHYKKVRVVQFVDSIPKS 525
|
....*
gi 1277171962 625 AAAKV 629
Cdd:PLN02330 526 LSGKI 530
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
486-635 |
1.73e-06 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 51.16 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 486 PSMTRGFYADEEGYQETYFSAfrgvWAH-GDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIEsaligfRAAE--FRVM 562
Cdd:PRK05857 382 PANMLGYWNNPERTAEVLIDG----WVNtGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVD------RIAEgvSGVR 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 563 EAIAVGIPDKNSENKIICFVILEgqdrlTETDEAALRSVVADIV-------NPQAKPERIFAIKELPRNAAAKVPYKAIS 635
Cdd:PRK05857 452 EAACYEIPDEEFGALVGLAVVAS-----AELDESAARALKHTIAarfrresEPMARPSTIVIVTDIPRTQSGKVMRASLA 526
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
251-629 |
2.48e-06 |
|
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: 50.51 E-value: 2.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 251 WDDFCKQGKSTIARTERCNAEDVALMLFSSGTTrekgKKPKRILHTHGGVLAQiCKEVGFGFDCKEDDVFYWMTNF---- 326
Cdd:cd05915 133 GYLAYEEALGEEADPVRVPERAACGMAYTTGTT----GLPKGVVYSHRALVLH-SLAASLVDGTALSEKDVVLPVVpmfh 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 327 --GWMMApWEIVGalhFGATLVCFEgapSYPKPDRIFGIIERYKVSIFGSTP---GFIAGLRKNhisgddfnlsslrilg 401
Cdd:cd05915 208 vnAWCLP-YAATL---VGAKQVLPG---PRLDPASLVELFDGEGVTFTAGVPtvwLALADYLES---------------- 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 402 stgsilFSENWEWFFSVFGKGKCPiNNIIGGTEMLGCFAQNLPNIPCKIGSVGVFALGM---------------GGDIFN 466
Cdd:cd05915 265 ------TGHRLKTLRRLVVGGSAA-PRSLIARFERMGVEVRQGYGLTETSPVVVQNFVKshleslseeekltlkAKTGLP 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 467 EKGESVR------------RETGRVVCTHPFPSMTrGFYADEEGyqeTYFSAFRGVWAHG-DFAEMDEDGFVFMRGRSDD 533
Cdd:cd05915 338 IPLVRLRvadeegrpvpkdGKALGEVQLKGPWITG-GYYGNEEA---TRSALTPDGFFRTgDIAVWDEEGYVEIKDRLKD 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 534 IINKNGIKFSPANIESALIGFRAaefrVMEAIAVGIPDKNSENKIICFVIL-EGQDRLTETDEAALRSvvadIVNPQAKP 612
Cdd:cd05915 414 LIKSGGEWISSVDLENALMGHPK----VKEAAVVAIPHPKWQERPLAVVVPrGEKPTPEELNEHLLKA----GFAKWQLP 485
|
410
....*....|....*..
gi 1277171962 613 ERIFAIKELPRNAAAKV 629
Cdd:cd05915 486 DAYVFAEEIPRTSAGKF 502
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
97-302 |
2.69e-06 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 50.48 E-value: 2.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 97 LGSKVCVcyEHESGKKRAITFWQLKLLVDTIASAMKAHGIGKGDFVGMCMPISIDSIAVMFACFKIGAVCMQMAPTTSTD 176
Cdd:PLN02736 63 LGTRIRV--DGTVGEYKWMTYGEAGTARTAIGSGLVQHGIPKGACVGLYFINRPEWLIVDHACSAYSYVSVPLYDTLGPD 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 177 GTKDIVDHVRIarAKMFFMADsysyggknfTLEKIHQGVSDIFSVRHIVVFENDAPHSPFSPfvfGKKEMRSVFWDDFCK 256
Cdd:PLN02736 141 AVKFIVNHAEV--AAIFCVPQ---------TLNTLLSCLSEIPSVRLIVVVGGADEPLPSLP---SGTGVEIVTYSKLLA 206
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1277171962 257 QGKSTIARTERCNAEDVALMLFSSGTTrekgKKPKRILHTHGGVLA 302
Cdd:PLN02736 207 QGRSSPQPFRPPKPEDVATICYTSGTT----GTPKGVVLTHGNLIA 248
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
514-634 |
2.72e-06 |
|
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: 50.39 E-value: 2.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 514 GDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIESALIGFRAaefrVMEAIAVGIPDKNSENKIICFVILEGQDRLTET 593
Cdd:cd12115 334 GDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPG----VREAVVVAIGDAAGERRLVAYIVAEPGAAGLVE 409
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1277171962 594 DeaaLRSVVADIVNPQAKPERIFAIKELPRNAAAKVPYKAI 634
Cdd:cd12115 410 D---LRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
115-321 |
3.37e-06 |
|
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: 50.29 E-value: 3.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 115 ITFWQLKLLVDTIASAMKAHGI--GKGDFVGMCMPISIDSIAVMFACFKIGAVCMQMAPTTSTDGTKDIVDHVRIArakm 192
Cdd:cd05927 6 ISYKEVAERADNIGSALRSLGGkpAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEIS---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 193 ffmadsysyggknftlekihqgvsdifsvrhIVVFENDaphspfspfvfgkkeMRSVFWDDFCKQGKSTIARTERCNAED 272
Cdd:cd05927 82 -------------------------------IVFCDAG---------------VKVYSLEEFEKLGKKNKVPPPPPKPED 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1277171962 273 VALMLFSSGTTREkgkkPKRILHTHGGVLAQIC---KEVGFGFDCKEDDVFY 321
Cdd:cd05927 116 LATICYTSGTTGN----PKGVMLTHGNIVSNVAgvfKILEILNKINPTDVYI 163
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
357-629 |
4.57e-06 |
|
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: 49.19 E-value: 4.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 357 PDRIFGIIERYKVSIFGSTPGfIAGLRKNHISGDDFNLSSLRILGSTGSILFSENWE-----WFFSVFGKGKcpinniig 431
Cdd:cd17637 77 PAEALELIEEEKVTLMGSFPP-ILSNLLDAAEKSGVDLSSLRHVLGLDAPETIQRFEettgaTFWSLYGQTE-------- 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 432 gTEMLGCFAQNLPnipcKIGSVGVFALGMGGDIFNEKGESVRR-ETGRVVCTHPFPSMtrGFYADEEGYQETyfsaFRGV 510
Cdd:cd17637 148 -TSGLVTLSPYRE----RPGSAGRPGPLVRVRIVDDNDRPVPAgETGEIVVRGPLVFQ--GYWNLPELTAYT----FRNG 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 511 WAH-GDFAEMDEDGFVFMRGRS--DDIINKNGIKFSPANIESALIGFRAaefrVMEAIAVGIPD-KNSEN-KIICfVILE 585
Cdd:cd17637 217 WHHtGDLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPA----IAEVCVIGVPDpKWGEGiKAVC-VLKP 291
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1277171962 586 GQdRLTetdEAALRSVVADIVNPQAKPERIFAIKELPRNAAAKV 629
Cdd:cd17637 292 GA-TLT---ADELIEFVGSRIARYKKPRYVVFVEALPKTADGSI 331
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
464-629 |
4.97e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 49.39 E-value: 4.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 464 IFNEKGESVRR-ETGRVVCTHPFPSMtrGFYADEEGYQETYFSAFRGVwahGDFAEMDEDGFVFMRGRSDDIINKNGIKF 542
Cdd:PRK07638 320 ICNEAGEEVQKgEIGTVYVKSPQFFM--GYIIGGVLARELNADGWMTV---RDVGYEDEEGFIYIVGREKNMILFGGINI 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 543 SPANIESALIGFRAAEfrvmEAIAVGIPDKNSENKIIcfVILEGQdrlteTDEAALRSVVADIVNPQAKPERIFAIKELP 622
Cdd:PRK07638 395 FPEEIESVLHEHPAVD----EIVVIGVPDSYWGEKPV--AIIKGS-----ATKQQLKSFCLQRLSSFKIPKEWHFVDEIP 463
|
....*..
gi 1277171962 623 RNAAAKV 629
Cdd:PRK07638 464 YTNSGKI 470
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
509-594 |
7.46e-06 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 48.90 E-value: 7.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 509 GVWAHGDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIESALigfrAAEFRVMEAIAVGIPDKNSENKIICFVILEgQD 588
Cdd:PRK08974 432 GWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVV----MLHPKVLEVAAVGVPSEVSGEAVKIFVVKK-DP 506
|
....*.
gi 1277171962 589 RLTETD 594
Cdd:PRK08974 507 SLTEEE 512
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
98-633 |
7.78e-06 |
|
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: 48.83 E-value: 7.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 98 GSKVCVCYEHESgkkraITFWQLKLLVDTIASAMKAHGIGKGDFVGMCMPISIDSIAVMFACFKIGAVCMQMAPTTSTDg 177
Cdd:cd12116 1 PDATAVRDDDRS-----LSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPAD- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 178 tkdivdhvRIArakmFFMADSysyggknftlekihqGVSdifsvrhIVVFENDAPHSPFSPFVfgkkemrsVFWDDFCKQ 257
Cdd:cd12116 75 --------RLR----YILEDA---------------EPA-------LVLTDDALPDRLPAGLP--------VLLLALAAA 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 258 GKSTIARTERCNAEDVALMLFSSGTTrekgKKPKRILHTHGGV---LAQICKEVGFGfdckEDDVFYWMTNFGWMMAPWE 334
Cdd:cd12116 113 AAAPAAPRTPVSPDDLAYVIYTSGST----GRPKGVVVSHRNLvnfLHSMRERLGLG----PGDRLLAVTTYAFDISLLE 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 335 IVGALHFGATLVCFEGAPSYpKPDRIFGIIERYKVSIFGSTPGFIAGLrknhISGDDFNLSSLRIL-GstGSILFSENWE 413
Cdd:cd12116 185 LLLPLLAGARVVIAPRETQR-DPEALARLIEAHSITVMQATPATWRML----LDAGWQGRAGLTALcG--GEALPPDLAA 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 414 WFFS-------VFG----------------KGKCPINNIIGGTEMLGCFAQNLPnIPckIGSVGVFALGmggdifnekGE 470
Cdd:cd12116 258 RLLSrvgslwnLYGptettiwstaarvtaaAGPIPIGRPLANTQVYVLDAALRP-VP--PGVPGELYIG---------GD 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 471 SVRR-------ETGRVVCTHPF-PSMTRgfyadeegyqetyfsAFRGvwahGDFAEMDEDGFVFMRGRSDDIINKNGIKF 542
Cdd:cd12116 326 GVAQgylgrpaLTAERFVPDPFaGPGSR---------------LYRT----GDLVRRRADGRLEYLGRADGQVKIRGHRI 386
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 543 SPANIESALigfrAAEFRVMEAIAVGIPDKNSEnKIICFVILEGQDRLtetDEAALRSVVADIVNPQAKPERIFAIKELP 622
Cdd:cd12116 387 ELGEIEAAL----AAHPGVAQAAVVVREDGGDR-RLVAYVVLKAGAAP---DAAALRAHLRATLPAYMVPSAFVRLDALP 458
|
570
....*....|.
gi 1277171962 623 RNAAAKVPYKA 633
Cdd:cd12116 459 LTANGKLDRKA 469
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
490-571 |
8.71e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 48.79 E-value: 8.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 490 RGFYADEEGYQEtyfsAFRGVWAH-GDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIESALIGFRAaefrVMEAIAVG 568
Cdd:PRK08162 400 KGYLKNPKATEE----AFAGGWFHtGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPA----VLVAAVVA 471
|
...
gi 1277171962 569 IPD 571
Cdd:PRK08162 472 KPD 474
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
486-649 |
1.52e-05 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 48.07 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 486 PSMTRGFYADeegyqetyFSAFRGVWAHGDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIESALigfRAAEFrVMEAI 565
Cdd:PRK07445 309 QSLALGYYPQ--------ILDSQGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAI---LATGL-VQDVC 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 566 AVGIPDKNSENKIICFVIleGQDrlTETDEAALRSVVADIVNPQAKPERIFAIKELPRNAAAKvpykaISRVFCDRYVIA 645
Cdd:PRK07445 377 VLGLPDPHWGEVVTAIYV--PKD--PSISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGK-----INRQQLQQIAVQ 447
|
....
gi 1277171962 646 QTRV 649
Cdd:PRK07445 448 RLGL 451
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
269-570 |
1.80e-05 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 47.89 E-value: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 269 NAEDVALMLFSSGTTrekgKKPKRILHTHGGVLAQICKEVGFgFDCKEDDVfywMTNFgwmMAPWEIVG----ALH--FG 342
Cdd:PRK06334 181 DPEDVAVILFTSGTE----KLPKGVPLTHANLLANQRACLKF-FSPKEDDV---MMSF---LPPFHAYGfnscTLFplLS 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 343 ATLVCFEGAPSYPKpdRIFGIIERYKVSIFGSTPGFIAGLRKNhISGDDFNLSSLRILGSTGSI----LFSENWEWFFSV 418
Cdd:PRK06334 250 GVPVVFAYNPLYPK--KIVEMIDEAKVTFLGSTPVFFDYILKT-AKKQESCLPSLRFVVIGGDAfkdsLYQEALKTFPHI 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 419 fgkgkcPINNIIGGTEMLGCFAQNLPNIPCKIGSVGVFALGMGGDIFNE--KGESVRRETGRVVCTHpfPSMTRGFYADE 496
Cdd:PRK06334 327 ------QLRQGYGTTECSPVITINTVNSPKHESCVGMPIRGMDVLIVSEetKVPVSSGETGLVLTRG--TSLFSGYLGED 398
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1277171962 497 EGYQetyFSAFRG-VW-AHGDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIESALI-GFRAAEFRVMEAIAV-GIP 570
Cdd:PRK06334 399 FGQG---FVELGGeTWyVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMeGFGQNAADHAGPLVVcGLP 473
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
459-606 |
1.89e-05 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 47.69 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 459 GMGGDIFNEKGESV-RRETGRVVCTHPfpSMTRGFYADEE--------GYQETyfsafrgvwahGDFAEMdEDGFVFMRG 529
Cdd:PRK09192 393 GHEIEIRNEAGMPLpERVVGHICVRGP--SLMSGYFRDEEsqdvlaadGWLDT-----------GDLGYL-LDGYLYITG 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 530 RSDDIINKNGIKFSPANIEsaligfRAAE----FRVMEAIAVGIPDKNSEnKIICFVilegQDRLTETDE-AALRSVVAD 604
Cdd:PRK09192 459 RAKDLIIINGRNIWPQDIE------WIAEqepeLRSGDAAAFSIAQENGE-KIVLLV----QCRISDEERrGQLIHALAA 527
|
..
gi 1277171962 605 IV 606
Cdd:PRK09192 528 LV 529
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
113-321 |
2.17e-05 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 47.56 E-value: 2.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 113 RAITFWQLKLLVDTIASAMKAHGIGKGDFVGMCMPISIDSIAVMFACFKIGAVCmQMAPTTSTDgtkDIVDH-VRIARAk 191
Cdd:PRK08279 61 QSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVV-ALLNTQQRG---AVLAHsLNLVDA- 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 192 mffmadsysyggknftlekihqgvsdifsvRHIVV-------FENDAPH---SPFSPFVFGKKEMRSVFWDDF--CKQGK 259
Cdd:PRK08279 136 ------------------------------KHLIVgeelveaFEEARADlarPPRLWVAGGDTLDDPEGYEDLaaAAAGA 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1277171962 260 STIARTERCN--AEDVALMLFSSGTTrekGkKPKRILHTHGGVLAqickeVGFGF----DCKEDDVFY 321
Cdd:PRK08279 186 PTTNPASRSGvtAKDTAFYIYTSGTT---G-LPKAAVMSHMRWLK-----AMGGFggllRLTPDDVLY 244
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
514-629 |
2.81e-05 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 47.18 E-value: 2.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 514 GDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIE-----------SALIGFRAAEFRvmEA-IAVGIPDKNSEnkiicf 581
Cdd:PRK07514 382 GDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEgeidelpgvveSAVIGVPHPDFG--EGvTAVVVPKPGAA------ 453
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1277171962 582 vilegqdrlteTDEAALRSVVADIVnpqAK---PERIFAIKELPRNAAAKV 629
Cdd:PRK07514 454 -----------LDEAAILAALKGRL---ARfkqPKRVFFVDELPRNTMGKV 490
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
113-194 |
3.82e-05 |
|
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: 46.58 E-value: 3.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 113 RAITFWQLKLLVDTIASAMKAHGIGKGDFVGMCMPISIDSIAVMFACFKIGAVcmqMAPTTSTDGTKDIVDHVRIARAKM 192
Cdd:cd05940 2 EALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAV---AALINYNLRGESLAHCLNVSSAKH 78
|
..
gi 1277171962 193 FF 194
Cdd:cd05940 79 LV 80
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
113-376 |
1.62e-04 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 45.15 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 113 RAITFWQLKLLVDTIASAMKAHGIGKGDFVGMCMPISIDSIAVMFACFKIGAVCMQMAPTTSTDgtkdivdhvRIArakm 192
Cdd:PRK12467 1598 QELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRE---------RLA---- 1664
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 193 FFMADSysyggknftlekihqGVSDIFSVRHIvvfendAPHSPFSpfvfgkKEMRSVFWD--DFCKQGKSTIARTERCNA 270
Cdd:PRK12467 1665 YMIEDS---------------GIELLLTQSHL------QARLPLP------DGLRSLVLDqeDDWLEGYSDSNPAVNLAP 1717
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 271 EDVALMLFSSGTTrekgKKPKRILHTHGGVLAQICKeVGFGFDCKEDDVFYWMTNFGWMMAPWEIVGALHFGATLVCfeG 350
Cdd:PRK12467 1718 QNLAYVIYTSGST----GRPKGAGNRHGALVNRLCA-TQEAYQLSAADVVLQFTSFAFDVSVWELFWPLINGARLVI--A 1790
|
250 260
....*....|....*....|....*..
gi 1277171962 351 APS-YPKPDRIFGIIERYKVSIFGSTP 376
Cdd:PRK12467 1791 PPGaHRDPEQLIQLIERQQVTTLHFVP 1817
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
486-640 |
4.68e-04 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 43.20 E-value: 4.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 486 PSMTRGFYA------DEEGYQETyfsafrgvwahGDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIESALIGFRaaef 559
Cdd:PRK06018 392 PAVAAAYYRvdgeilDDDGFFDT-----------GDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHP---- 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 560 RVMEAIAVGIPD-KNSENKIICFVILEGQdrlTETDEAALRSVVADIvnpqAK---PERIFAIKELPRNAAAKVPYKAIS 635
Cdd:PRK06018 457 KVAEAAVIGVYHpKWDERPLLIVQLKPGE---TATREEILKYMDGKI----AKwwmPDDVAFVDAIPHTATGKILKTALR 529
|
....*
gi 1277171962 636 RVFCD 640
Cdd:PRK06018 530 EQFKD 534
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
514-629 |
5.01e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 43.10 E-value: 5.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 514 GDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIESALIGFRaaefRVMEAIAVGIPDkNSENKIICF-VILEgqdrlTE 592
Cdd:PRK08308 296 KDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLP----GVQEAVVYRGKD-PVAGERVKAkVISH-----EE 365
|
90 100 110
....*....|....*....|....*....|....*..
gi 1277171962 593 TDEAALRSVVADIVNPQAKPERIFAIKELPRNAAAKV 629
Cdd:PRK08308 366 IDPVQLREWCIQHLAPYQVPHEIESVTEIPKNANGKV 402
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
506-598 |
5.04e-04 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 43.29 E-value: 5.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 506 AFRGVWAH-GDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIESALIGFRAaefrVMEAIAVGIPDKNSENKIICFVIL 584
Cdd:PLN02479 426 AFANGWFHsGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPA----VLEASVVARPDERWGESPCAFVTL 501
|
90
....*....|....*
gi 1277171962 585 -EGQDRlteTDEAAL 598
Cdd:PLN02479 502 kPGVDK---SDEAAL 513
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
115-638 |
7.57e-04 |
|
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: 42.53 E-value: 7.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 115 ITFWQLKLLVDTIASAMKAHGIGKGDFVGMCMPISIDSIAVMFACFKIGAVCMQMAPTTSTDGTKDIvdhvriarakmff 194
Cdd:cd05918 25 LTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLDPSHPLQRLQEI------------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 195 madsysyggknftlekihqgvsdifsvrhivvfendaphspfspfvfgkkemrsvfwddfCKQGKSTIARTERcnAEDVA 274
Cdd:cd05918 92 ------------------------------------------------------------LQDTGAKVVLTSS--PSDAA 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 275 LMLFSSGTTrekgKKPKRILHTHG----GVLAQIcKEVGFGfdckEDDVFYWMTNFGWMMAPWEIVGALHFGATlVCfeg 350
Cdd:cd05918 110 YVIFTSGST----GKPKGVVIEHRalstSALAHG-RALGLT----SESRVLQFASYTFDVSILEIFTTLAAGGC-LC--- 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 351 APS-YPKPDRIFGIIERYKVSIFGSTPGFIAGLRKNhisgddfNLSSLRILGSTGSILFSENWE-W-----FFSVFGKGK 423
Cdd:cd05918 177 IPSeEDRLNDLAGFINRLRVTWAFLTPSVARLLDPE-------DVPSLRTLVLGGEALTQSDVDtWadrvrLINAYGPAE 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 424 CPIN------------NIIGGTemLGCFA-----QNlPNIPCKIGSVGvfALGMGGdifnekgesvrretgrvvcthpfP 486
Cdd:cd05918 250 CTIAatvspvvpstdpRNIGRP--LGATCwvvdpDN-HDRLVPIGAVG--ELLIEG-----------------------P 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 487 SMTRGFYADEE---------------GYQETYFSAFRGvwahGDFAEMDEDG-FVFMrGRSDDIINKNGIKFSPANIESA 550
Cdd:cd05918 302 ILARGYLNDPEktaaafiedpawlkqEGSGRGRRLYRT----GDLVRYNPDGsLEYV-GRKDTQVKIRGQRVELGEIEHH 376
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 551 LigfRAAEFRVMEAIA--VGIPDKNSENKIICFVILEGqDRLTETDEAALRSVVADIVNPQAK---------------PE 613
Cdd:cd05918 377 L---RQSLPGAKEVVVevVKPKDGSSSPQLVAFVVLDG-SSSGSGDGDSLFLEPSDEFRALVAelrsklrqrlpsymvPS 452
|
570 580
....*....|....*....|....*
gi 1277171962 614 RIFAIKELPRNAAAKVPYKAISRVF 638
Cdd:cd05918 453 VFLPLSHLPLTASGKIDRRALRELA 477
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
514-594 |
1.47e-03 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 41.54 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 514 GDFAEMDEDGFVFMRGRSDDIINKNGIKFSPANIESALigfrAAEFRVMEAIAVGIPDKNSENKIICFVILEGQDrLTET 593
Cdd:PRK07059 440 GDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVV----ASHPGVLEVAAVGVPDEHSGEAVKLFVVKKDPA-LTEE 514
|
.
gi 1277171962 594 D 594
Cdd:PRK07059 515 D 515
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
208-304 |
3.24e-03 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 40.87 E-value: 3.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277171962 208 LEKIHQGVSDIFSVRHIVVFENDAPHSPFSPFVFGKKEMRSvfWDDFCKQGKSTIARTERCNAEDVALMLFSSGTTrekg 287
Cdd:PLN02387 189 LKKLIDISSQLETVKRVIYMDDEGVDSDSSLSGSSNWTVSS--FSEVEKLGKENPVDPDLPSPNDIAVIMYTSGST---- 262
|
90
....*....|....*..
gi 1277171962 288 KKPKRILHTHGGVLAQI 304
Cdd:PLN02387 263 GLPKGVMMTHGNIVATV 279
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
116-165 |
4.68e-03 |
|
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: 40.14 E-value: 4.68e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1277171962 116 TFWQLKLLVDTIASAMKAHGIGKGDFVGMCMPISIDSIAVMFACFKIGAV 165
Cdd:cd05910 4 SFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAV 53
|
|
| |
