|
Name |
Accession |
Description |
Interval |
E-value |
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
7-379 |
5.52e-153 |
|
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; SCP-2 has multiple roles in intracellular lipid circulation and metabolism. The N-terminal presequence in the SCP-x isoform represents a peroxisomal 3-ketacyl-Coa thiolase specific for branched-chain acyl CoAs, which is proteolytically cleaved from the sterol carrier protein.
Pssm-ID: 238425 [Multi-domain] Cd Length: 375 Bit Score: 436.31 E-value: 5.52e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 7 VGAGMIDFGELYEQSFDDLLESAYLSLIEnvDKGVDPSDIDAAWYGT-IDIANEGSSGSAVAHATGLFETPITRVENACA 85
Cdd:cd00829 1 VGVGMTPFGRRSDRSPLELAAEAARAALD--DAGLEPADIDAVVVGNaAGGRFQSFPGALIAEYLGLLGKPATRVEAAGA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 86 TGSDAFRNAAQAVKAGDAEVALVIGAEKMTDSTEGLIASAAL-----ERLWRGRGVTMPAYFGMRATRHLEEYETTREQI 160
Cdd:cd00829 79 SGSAAVRAAAAAIASGLADVVLVVGAEKMSDVPTGDEAGGRAsdlewEGPEPPGGLTPPALYALAARRYMHRYGTTREDL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 161 AEISVKNHENGTKYPHAHQQFECTVEDVKESPTVSYPLNLYDCCPVTDGACAVLVTSEERAREFTDDPIRVAGYGLASDT 240
Cdd:cd00829 159 AKVAVKNHRNAARNPYAQFRKPITVEDVLNSRMIADPLRLLDCCPVSDGAAAVVLASEERARELTDRPVWILGVGAASDT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 241 FQRGAPEALTNFPATRQASSQAYERAGLGPDDIDVAEVHDCFSITELITYEDLGFCEDGKGGQFVDEGRPHLDGDKPVNP 320
Cdd:cd00829 239 PSLSERDDFLSLDAARLAARRAYKMAGITPDDIDVAELYDCFTIAELLALEDLGFCEKGEGGKLVREGDTAIGGDLPVNT 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1224667574 321 SGGLLSKGHPIGATGVAQIAEIFEQLRGEAGDVQVDSPEVGLQHNIGigrnATGAVSCV 379
Cdd:cd00829 319 SGGLLSKGHPLGATGLAQAVEAVRQLRGEAGARQVPGARVGLAHNIG----GTGSAAVV 373
|
|
| PRK06064 |
PRK06064 |
thiolase domain-containing protein; |
1-384 |
1.26e-150 |
|
thiolase domain-containing protein;
Pssm-ID: 235688 [Multi-domain] Cd Length: 389 Bit Score: 430.86 E-value: 1.26e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 1 MTDPHVVGAGMIDFGELYEQSFDDLLESAYLSLIEnvDKGVDPSDIDAAWYGTID---IANEGSSGSAVAHATGLFETPI 77
Cdd:PRK06064 1 MRDVAIIGVGQTKFGELWDVSLRDLAVEAGLEALE--DAGIDGKDIDAMYVGNMSaglFVSQEHIAALIADYAGLAPIPA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 78 TRVENACATGSDAFRNAAQAVKAGDAEVALVIGAEKMTDSTEG----LIASAAlERLWRG-RGVTMPAYFGMRATRHLEE 152
Cdd:PRK06064 79 TRVEAACASGGAALRQAYLAVASGEADVVLAAGVEKMTDVPTPdateAIARAG-DYEWEEfFGATFPGLYALIARRYMHK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 153 YETTREQIAEISVKNHENGTKYPHAHQQFECTVEDVKESPTVSYPLNLYDCCPVTDGACAVLVTSEERAREFTDDPIRVA 232
Cdd:PRK06064 158 YGTTEEDLALVAVKNHYNGSKNPYAQFQKEITVEQVLNSPPVADPLKLLDCSPITDGAAAVILASEEKAKEYTDTPVWIK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 233 GYGLASDTFQRGAPEALTNFPATRQASSQAYERAGLGPDDIDVAEVHDCFSITELITYEDLGFCEDGKGGQFVDEGRPHL 312
Cdd:PRK06064 238 ASGQASDTIALHDRKDFTTLDAAVVAAEKAYKMAGIEPKDIDVAEVHDCFTIAEILAYEDLGFAKKGEGGKLAREGQTYI 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1224667574 313 DGDKPVNPSGGLLSKGHPIGATGVAQIAEIFEQLRGEA--GDVQVDSPEVGLQHNIGigrnATGAVSCVNILER 384
Cdd:PRK06064 318 GGDIPVNPSGGLKAKGHPVGATGVSQAVEIVWQLRGEAekGRQQVIGAGYGLTHNVG----GTGHTAVVHILSR 387
|
|
| PRK06157 |
PRK06157 |
acetyl-CoA acetyltransferase; Validated |
6-385 |
1.43e-118 |
|
acetyl-CoA acetyltransferase; Validated
Pssm-ID: 180433 [Multi-domain] Cd Length: 398 Bit Score: 349.71 E-value: 1.43e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 6 VVGAGMIDFGELYEQSFDDLLESAYLSLIEnvDKGVDPSDIDAAWYGT-IDIANEGSSGSAVAHATGLFETPITRVENAC 84
Cdd:PRK06157 11 ILGMGCTKFGERWDAGAEDLMVEAFLEALA--DAGIEPKDIDAAWFGThYDEIGSGKSGTPLSRALRLPNIPVTRVENFC 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 85 ATGSDAFRNAAQAVKAGDAEVALVIGAEKMTDS-TEGLIASAALERLWR-GRGVTMPAYFGMRATRHLEEY----ETTRE 158
Cdd:PRK06157 89 ATGSEAFRGAVYAVASGAYDIALALGVEKLKDTgYGGLPVANPGTLADMtMPNVTAPGNFAQLASAYAAKYgvsrEDLKR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 159 QIAEISVKNHENGTKYPHAHQQFECTVEDVKESPTVSYPLNLYDCCPVTDGACAVLVTSEERAREFTD-DPIRVAGYGLA 237
Cdd:PRK06157 169 AMAHVSVKSHANGARNPKAHLRKAVTEEQVLKAPMIAGPLGLFDCCGVSDGAAAAIVTTPEIARALGKkDPVYVKALQLA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 238 SDTfqrGAPEA-----LTNFPATRQASSQAYERAGL-GP-DDIDVAEVHDCFSITELITYEDLGFCEDGKGGQFVDEGRP 310
Cdd:PRK06157 249 VSN---GWELQyngwdGSYFPTTRIAARKAYREAGItDPrEELSMAEVHDCFSITELVTMEDLGLSERGQAWRDVLDGFF 325
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1224667574 311 HLDGDKPVNPSGGLLSKGHPIGATGVAQIAEIFEQLRGEAGDVQVDSPEVGLQHNIGiGRNAtGAVSCVNILERP 385
Cdd:PRK06157 326 DADGGLPCQIDGGLKCFGHPIGASGLRMLYEMYLQLLGRAGERQLKNPRLALTHNLG-GAPG-QNVCSVSIVGRE 398
|
|
| PRK12578 |
PRK12578 |
thiolase domain-containing protein; |
6-384 |
6.57e-111 |
|
thiolase domain-containing protein;
Pssm-ID: 183606 [Multi-domain] Cd Length: 385 Bit Score: 329.50 E-value: 6.57e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 6 VVGAGMIDFGELYEQSFDDLlesAYLSLIENV-DKGVDPSDIDAAWYGTIDIAN-EGSSGSAVAHATGLF-ETPItRVEN 82
Cdd:PRK12578 5 VIGVGNSKFGRRDDVSVQEL---AWESIKEALnDAGVSQTDIELVVVGSTAYRGiELYPAPIVAEYSGLTgKVPL-RVEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 83 ACATGSDAFRNAAQAVKAGDAEVALVIGAEKMTD---STEGLIASAALERLWRGR--GVTMPAYFGMRATRHLEEYETTR 157
Cdd:PRK12578 81 MCATGLAASLTAYTAVASGLVDMAIAVGVDKMTEvdtSTSLAIGGRGGNYQWEYHfyGTTFPTYYALYATRHMAVYGTTE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 158 EQIAEISVKNHENGTKYPHAHQQFECTVEDVKESPTVSYPLNLYDCCPVTDGACAVLVTSEERAREF-TDDPIRVAGYGL 236
Cdd:PRK12578 161 EQMALVSVKAHKYGAMNPKAHFQKPVTVEEVLKSRAISWPIKLLDSCPISDGSATAIFASEEKVKELkIDSPVWITGIGY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 237 ASDTFQRGAPEALTNFPATRQASSQAYERAGLGPDDIDVAEVHDCFSITELITYEDLGFCEDGKGGQFVDEGRPHLDGDK 316
Cdd:PRK12578 241 ANDYAYVARRGEWVGFKATQLAARQAYNMAKVTPNDIEVATVHDAFTIAEIMGYEDLGFTEKGKGGKFIEEGQSEKGGKV 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1224667574 317 PVNPSGGLLSKGHPIGATGVAQIAEIFEQLRGEAGDVQVDSPE-VGLQHNIGigrnATGAVSCVNILER 384
Cdd:PRK12578 321 GVNLFGGLKAKGHPLGATGLSMIYEITKQLRDEAGKLQQPLKKyIGLVHNVG----GTGHFAYVMILRR 385
|
|
| PRK08256 |
PRK08256 |
lipid-transfer protein; Provisional |
5-384 |
2.93e-102 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181327 [Multi-domain] Cd Length: 391 Bit Score: 307.60 E-value: 2.93e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 5 HVVGAGMIDF---GElyEQSFDDLL-ESAYLSLIenvDKGVDPSDIDAAWYGTIdiANEGSSGSAVAHATGLFETPITRV 80
Cdd:PRK08256 4 FVAGVGMTPFekpGA--SWDYPDMAaEAGRAALA---DAGIDYDAVQQAYVGYV--YGDSTSGQRALYEVGMTGIPIVNV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 81 ENACATGSDAFRNAAQAVKAGDAEVALVIGAEKMTdstegliaSAALERLWRGRGVTM-------------------PAY 141
Cdd:PRK08256 77 NNNCSTGSTALFLARQAVRSGAADCALALGFEQMQ--------PGALGSVWDDRPSPLerfdkalaelqgfdpappaLRM 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 142 FGMRATRHLEEYETTREQIAEISVKNHENGTKYPHAHQQFECTVEDVKESPTVSYPLNLYDCCPVTDGACAVLVTSEERA 221
Cdd:PRK08256 149 FGGAGREHMEKYGTTAETFAKIGVKARRHAANNPYAQFRDEYTLEDVLASPMIWGPLTRLQCCPPTCGAAAAIVCSEEFA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 222 REF-TDDPIRVAGYGLASD---TFQRGAPEALTNFPATRQASSQAYERAGLGPDDIDVAEVHDCFSITELITYEDLGFCE 297
Cdd:PRK08256 229 RKHgLDRAVEIVAQAMTTDtpsTFDGRSMIDLVGYDMTRAAAQQVYEQAGIGPEDIDVVELHDCFSANELLTYEALGLCP 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 298 DGKGGQFVDEGRPHLDGDKPVNPSGGLLSKGHPIGATGVAQIAEIFEQLRGEAGDVQVDSPEVGLQHNIGIGrnatGAVS 377
Cdd:PRK08256 309 EGEAEKFIDDGDNTYGGRWVVNPSGGLLSKGHPLGATGLAQCAELTWQLRGTAGARQVEGARLALQHNLGLG----GACV 384
|
....*..
gi 1224667574 378 cVNILER 384
Cdd:PRK08256 385 -VTLYQR 390
|
|
| PRK07516 |
PRK07516 |
thiolase domain-containing protein; |
1-384 |
1.06e-92 |
|
thiolase domain-containing protein;
Pssm-ID: 181013 [Multi-domain] Cd Length: 389 Bit Score: 282.99 E-value: 1.06e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 1 MTDPHVVGAGMIDFGELYEQSFDDLLESAYLSLIEnvDKGVDPSDIDAAWYGTID--IANEGSSGSAVAHAT-GLFETPI 77
Cdd:PRK07516 1 MMTASIVGWAHTPFGKLDAETLESLIVRVAREALA--HAGIAAGDVDGIFLGHFNagFSPQDFPASLVLQADpALRFKPA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 78 TRVENACATGSDAFRNAAQAVKAGDAEVALVIGAEKMTDSTEGLIASAALERLWR----GRGVTMPAYFGMRATRHLEEY 153
Cdd:PRK07516 79 TRVENACATGSAAVYAALDAIEAGRARIVLVVGAEKMTATPTAEVGDILLGASYLkeegDTPGGFAGVFGRIAQAYFQRY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 154 ETTREQIAEISVKNHENGTKYPHAHQQ----FE-C-TVEDvkESPTVSYPLNLYDCCPVTDGACAVLVTSEERAREFtDD 227
Cdd:PRK07516 159 GDQSDALAMIAAKNHANGVANPYAQMRkdlgFEfCrTVSE--KNPLVAGPLRRTDCSLVSDGAAALVLADAETARAL-QR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 228 PIRVAGYGLASDTF---QRGApealTNFPATRQASSQAYERAGLGPDDIDVAEVHDCFSITELITYEDLGFCEDGKGGQF 304
Cdd:PRK07516 236 AVRFRARAHVNDFLplsRRDP----LAFEGPRRAWQRALAQAGVTLDDLSFVETHDCFTIAELIEYEAMGLAPPGQGARA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 305 VDEGRPHLDGDKPVNPSGGLLSKGHPIGATGVAQIAEIFEQLRGEAGDVQVDSPEVGLQHNIGigrnATGAVSCVNILER 384
Cdd:PRK07516 312 IREGWTAKDGKLPVNPSGGLKAKGHPIGATGVSMHVLAAMQLTGEAGGMQIPGAKLAGVFNMG----GAAVANYVSILER 387
|
|
| PRK06365 |
PRK06365 |
thiolase domain-containing protein; |
1-385 |
1.37e-79 |
|
thiolase domain-containing protein;
Pssm-ID: 235785 [Multi-domain] Cd Length: 430 Bit Score: 250.98 E-value: 1.37e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 1 MTDPHVVGAGMIDFGE-LYEQSFDDLLESAYLSLIENVDKGVDPSDIDAAWYGTIDIANEGSSGSAVAHATGLFETPITR 79
Cdd:PRK06365 15 SRDVYMVAAGVTKFDKaSPYMDFRERVKKAFDYAMNDAGLTLADIDGSVASYFSDHFQRQLLAGIMVQDYLGLVPKPSKR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 80 VENACATGSDAFRNAAQAVKAGDAEVALVIGAEKM----TDSTEGLIASAALERLWRGRGVTMPAYFGMRATRHLEEYET 155
Cdd:PRK06365 95 IEGGGATGGLAFQAGYEEIASGRMDCVAVYGFETMshvnTWKGNEFIALASDTNFDYPLGGFYTGYYAMMAVRHMYEFGT 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 156 TREQIAEISVKNHENGTKYPHAHQQFECTVEDVKESPTVSYPLNLYDCCPVTDGACAVLVTSEERAREFTDDPIRVAGYG 235
Cdd:PRK06365 175 TVEQLAKVSVKNHGNAIHNPFAQSPMKITVEDVRKSPMVSYPLTRLDVCAMSDGAACAILASEDKAFEITDKPVLIKAIG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 236 LASDTFQR-----GAPEALTN----------------FPATRQASSQAYERAGLGP--DDIDVAEVHDCFSITELITYED 292
Cdd:PRK06365 255 TGSDTLRLadrpfGEVPLLPNespddykdlrypgvhsFRAGRMAAKEAYEMAGITDplNDLDLIELHDAYTSSEIQTYED 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 293 LGFCEDGKGGQFVDEGRPHLDGDKPVNPSGGLLSKGHPIGATGVAQIAEIFEQLRGE------AGDVQVDSPEVGLQHNi 366
Cdd:PRK06365 335 LGLCKYGEGGQFIESGKPELPGKLPVNPSGGLLAAGHAVGATGIMQAVFMFWQLQGRikkhfhDDYLQVKNAKRGLIHS- 413
|
410
....*....|....*....
gi 1224667574 367 gigRNATGAVSCVNILERP 385
Cdd:PRK06365 414 ---HAGTGTYVTVTILEAP 429
|
|
| PRK06059 |
PRK06059 |
lipid-transfer protein; Provisional |
62-376 |
5.25e-73 |
|
lipid-transfer protein; Provisional
Pssm-ID: 180373 [Multi-domain] Cd Length: 399 Bit Score: 232.73 E-value: 5.25e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 62 SGSAVAHATGLFETPITRVENACATGSDAFRNAAQAVKAGDAEVALVIGAEKMTdstEGLIASAALER-------LWRGR 134
Cdd:PRK06059 63 AGATFAQALGWNGAPVSSSYAACASGSQALQSARAQILAGLCDVALVVGADTTP---KGFFAPVGGERpddpdwlRFHLI 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 135 GVTMPAYFGMRATRHLEEYETTREQIAEISVKNHENGTKYPHAHQQFECTVEDVKESPTVSYPLNLYDCCPVTDGACAVL 214
Cdd:PRK06059 140 GATNPVYFALLARRRMDLYGATVEDFAQVKVKNARHGLLNPNARYRKEVTVEDVLASPVVSDPLRLLDICATSDGAAALI 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 215 VTSEERAREFT---DDPIRVAGYGLASDTFQRGAPE---------ALTNFPA---TRQASSQAYERAGLGPDDIDVAEVH 279
Cdd:PRK06059 220 VASKSFARRHLgsvAGVPSVRAISTVTPRYPQHLPElpdiatdstAAVPAPErvfKDQILDAAYAEAGIGPEDLSLAEVY 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 280 DCFSITELITYEDLGFCEDGKGGQFVDEGRPHLDGDKPVNPSGGLLSKGHPIGATGVAQIAEIFEQLRGEAGDVQVDSPE 359
Cdd:PRK06059 300 DLSTALELDWYEHLGLCPKGEAEALLRSGATTLGGRIPVNPSGGLACFGEAIPAQAIAQVCELTWQLRGQAGGRQVEGAR 379
|
330
....*....|....*..
gi 1224667574 360 VGLQHNIGIGRNATGAV 376
Cdd:PRK06059 380 VGITANQGLFGHGSSVI 396
|
|
| PRK06289 |
PRK06289 |
acetyl-CoA acetyltransferase; Provisional |
1-379 |
2.01e-64 |
|
acetyl-CoA acetyltransferase; Provisional
Pssm-ID: 235771 [Multi-domain] Cd Length: 403 Bit Score: 210.70 E-value: 2.01e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 1 MTDPHVVGAGMIDFGELYEQ---SFDDLLESAYLSLIENVdkGVDPSDIDAAWYGTID---IANEGSSGSAVAHAT-GLF 73
Cdd:PRK06289 2 SDDVWVLGGYQSDFARNWTKegrDFADLTREVVDGTLAAA--GVDADDIEVVHVGNFFgelFAGQGHLGAMPATVHpALW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 74 ETPITRVENACATGSDAFRNAAQAVKAGDAEVALVIGAEKM-----TDSTEGLIASAALERLWRGRGVTMPAYFGMRATR 148
Cdd:PRK06289 80 GVPASRHEAACASGSVATLAAMADLRAGRYDVALVVGVELMktvpgDVAAEHLGAAAWTGHEGQDARFPWPSMFARVADE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 149 HLEEYETTREQIAEISVKNHENGTKYPHAHQQF-----ECTVEDVKESPTVSYPLNLYDCCPVTDGACAVLVTSEERARE 223
Cdd:PRK06289 160 YDRRYGLDEEHLRAIAEINFANARRNPNAQTRGwafpdEATNDDDATNPVVEGRLRRQDCSQVTDGGAGVVLASDAYLRD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 224 FTDD-PI-RVAGYG--LASDTFQRGAPEALTN---FPATRQASSQAYERAGLGPDDIDVAEVHDCFSITELITYEDLGFC 296
Cdd:PRK06289 240 YADArPIpRIKGWGhrTAPLGLEQKLDRSAGDpyvLPHVRQAVLDAYRRAGVGLDDLDGFEVHDCFTPSEYLAIDHIGLT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 297 EDGKGGQFVDEGRPHLDGDKPVNPSGGLLSKGHPIGATGVAQIAEIFEQLRGEAGDVQVDSPEVGLQHNIGiGRNATgAV 376
Cdd:PRK06289 320 GPGESWKAIENGEIAIGGRLPINPSGGLIGGGHPVGASGVRMLLDAAKQVTGTAGDYQVEGAKTFGTLNIG-GSTTT-TV 397
|
...
gi 1224667574 377 SCV 379
Cdd:PRK06289 398 SFV 400
|
|
| nondecarbox_cond_enzymes |
cd00826 |
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ... |
7-379 |
2.10e-62 |
|
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic cleavage of 3-ketoacyl-CoA into acyl-CoA and acetyl-CoA, a 2-step reaction involving a covalent intermediate formed with a catalytic cysteine. There are 2 functional different classes: thiolase-I (3-ketoacyl-CoA thiolase) and thiolase-II (acetoacetyl-CoA thiolase). Thiolase-I can cleave longer fatty acid molecules and plays an important role in the beta-oxidative degradation of fatty acids. Thiolase-II has a high substrate specificity. Although it can cleave acetoacyl-CoA, its main function is the synthesis of acetoacyl-CoA from two molecules of acetyl-CoA, which gives it importance in several biosynthetic pathways.
Pssm-ID: 238422 [Multi-domain] Cd Length: 393 Bit Score: 205.42 E-value: 2.10e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 7 VGAGMIDFGELYEQS---FDDLLESAYLSLIENVDK--GVDPSDIDAAWYGTIDIANEGSSGS--AVAHATGLFETPITR 79
Cdd:cd00826 1 AGAAMTAFGKFGGENgadANDLAHEAGAKAIAAALEpaGVAAGAVEEACLGQVLGAGEGQNCAqqAAMHAGGLQEAPAIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 80 VENACATGSDAFRNAAQAVKAGDAEVALVIGAEKMTDSTEGLIASAALERLWRGRGVT----MPAYFGMRATRHLEEYET 155
Cdd:cd00826 81 MNNLCGSGLRALALAMQLIAGGDANCILAGGFEKMETSAENNAKEKHIDVLINKYGMRacpdAFALAGQAGAEAAEKDGR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 156 TREQIAEISVKN---HENGTKYPHAHQQFECTVEDV-KESPTVSYP--LNLYDCCPVTDGACAVLVTSEERAREFTDDPI 229
Cdd:cd00826 161 FKDEFAKFGVKGrkgDIHSDADEYIQFGDEASLDEIaKLRPAFDKEdfLTAGNACGLNDGAAAAILMSEAEAQKHGLQSK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 230 RVA--GYGLASD---TFQRGAPEALTNFPATRQASSQAYERAGLGPDDIDVAEVHDCFSITELITYEDLGFCEDGKGGQF 304
Cdd:cd00826 241 AREiqALEMITDmasTFEDKKVIKMVGGDGPIEAARKALEKAGLGIGDLDLIEAHDAFAANACATNEALGLCPEGQGGAL 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1224667574 305 VDEGRPHLDGDKPVNPSGGLLSKGHPIGATGVAQIAEIFEQLRGEAGDVQVDSPEVGLQHNIGIGrnatGAVSCV 379
Cdd:cd00826 321 VDRGDNTYGGKSIINPNGGAIAIGHPIGASGAAICAELCFELKGEAGKRQGAGAGLALLCIGGGG----GAAMCI 391
|
|
| PRK06158 |
PRK06158 |
thiolase; Provisional |
6-367 |
4.34e-62 |
|
thiolase; Provisional
Pssm-ID: 180434 [Multi-domain] Cd Length: 384 Bit Score: 204.11 E-value: 4.34e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 6 VVGAGMIDFGELYEQSFDDLLESAYLSLIEnvDKGVDPSDIDAAWYGTIDianEGSSGSAVAHATGLfeTPitRVENACA 85
Cdd:PRK06158 12 IVGAATAGLGEAPGLSAMELLAQAAHRALA--DAGLTMADVDGLFTASPD---DALWGLSVAEYLGI--RP--RFVDGTM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 86 TGSDAF----RNAAQAVKAGDAEVALVigaekMTDSTEGLIASAALERL----WRG--RGVTMPAYFGMRATRHLEEYET 155
Cdd:PRK06158 83 IGGSSFlahlLPAALALEAGLCDVALI-----CYGSNQRSAGGKLRSMLdpqpYEApyKPVNPVSAYALAAARHMHQYGT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 156 TREQIAEISVKNHENGTKYPHAHQQFECTVEDVKESPTVSYPLNLYDCCPVTDGACAVLVTSEERAREFTDDPIRVAGYG 235
Cdd:PRK06158 158 TREQLAEVAVAARQWAQLNPEAFMRDPLTIDDVLAARMVSDPLSVRDCCLVTDGAGAVVMVRADRARDLPRPPVYVLGAA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 236 LASDTFQRGAPEALTNFPAtRQASSQAYERAGLGPDDIDVAEVHDCFSITELITYEDLGFCEDGKGGQFVDEGRPHLDGD 315
Cdd:PRK06158 238 AATWHRQISSMPDLTVTAA-AESGPRAFAMAGLTPADIDVVELYDAFTINTILFLEDLGFCAKGEGGAFVEGGRIAPGGR 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1224667574 316 KPVNPSGGLLSKGHPiGATGVAQIAEIFEQLRGEAGDVQVDSPEVGLQHNIG 367
Cdd:PRK06158 317 LPVNTNGGGLSCVHP-GMYGLFLLIEAVRQLRGEAGERQVAGAEVALAHGNG 367
|
|
| PTZ00455 |
PTZ00455 |
3-ketoacyl-CoA thiolase; Provisional |
52-379 |
2.36e-60 |
|
3-ketoacyl-CoA thiolase; Provisional
Pssm-ID: 240424 [Multi-domain] Cd Length: 438 Bit Score: 201.27 E-value: 2.36e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 52 GTIDIANEGSSGSAVAhATGLFETPITRVENACATGSDAFRNAAQAVKAGDAEVALVIGAEKMTDST--EG---LIASAA 126
Cdd:PTZ00455 89 GHLGPAAVGSLGQSGA-SNALLYKPAMRVEGACASGGLAVQSAWEALLAGTSDIALVVGVEVQTTVSarVGgdyLARAAD 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 127 LERLWRGRGVTMPAYFGMRATRHLEEYETTREQIAEISVKNHENGTKYPHAHQQF------ECTVEDVKE-----SPTVS 195
Cdd:PTZ00455 168 YRRQRKLDDFTFPCLFAKRMKYIQEHGHFTMEDTARVAAKAYANGNKNPLAHMHTrklsleFCTGASDKNpkflgNETYK 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 196 YPLNLYDCCPVTDGACAVLVTSEERAREFTDDP-----IRVAGYGLASDTFQRGAPEAlTNFPATRQASSQAYERAGLGP 270
Cdd:PTZ00455 248 PFLRMTDCSQVSDGGAGLVLASEEGLQKMGLSPndsrlVEIKSLACASGNLYEDPPDA-TRMFTSRAAAQKALSMAGVKP 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 271 DDIDVAEVHDCFSITELITYEDLGFCEDGKGGQFVDEGRPHLDGDKPVNPSGGLLSKGHPIGATGVAQIAEIFEQLRGEA 350
Cdd:PTZ00455 327 SDLQVAEVHDCFTIAELLMYEALGIAEYGHAKDLIRNGATALEGRIPVNTGGGLLSFGHPVGATGVKQIMEVYRQMKGQC 406
|
330 340 350
....*....|....*....|....*....|
gi 1224667574 351 GDVQV-DSPEVGLQHNIGiGRNATgAVSCV 379
Cdd:PTZ00455 407 GEYQMkNIPALGATLNMG-GDDKT-AVSTV 434
|
|
| PRK08142 |
PRK08142 |
thiolase domain-containing protein; |
94-384 |
9.80e-54 |
|
thiolase domain-containing protein;
Pssm-ID: 236164 [Multi-domain] Cd Length: 388 Bit Score: 182.59 E-value: 9.80e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 94 AAQAVKAGDAEVALVIGAEKmtDSTEGliASAALERLWRG-----------RGVTMPAYfGMRATRHLEEYETTREQIAE 162
Cdd:PRK08142 92 AAQAIAAGKCSVALITLAGR--PRSEG--SSGTEPRNWGAdapdapfeapyGPTTHNLY-AMCAMRHMHEYGTTSEQLAW 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 163 ISVKNHENGTKYPHAHQQFECTVEDVKESPTVSYPLNLYDCCPVTDGACAVLVTSEERAREFTDDPIRVAGYGLASDTfQ 242
Cdd:PRK08142 167 IKVAASHHAQHNPHAMLRDVVTVEDVLNSPMIADPLHRLDCCVVTDGGGALVVVRPEIARSLKRPLVKVLGAGEAIKG-Q 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 243 RGAPEALTnFPATRQASSQAYERAGLGPDDIDVAEVHDCFSITELITYEDLGFCEDGKGGQFVDEGR-PHLDGDKPVNPS 321
Cdd:PRK08142 246 MGGKVDLT-YSGAAWSGPAAFAEAGVTPADIKYASIYDSFTITVLMQLEDLGFCKKGEGGKFVADGNlISGVGKLPFNTD 324
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1224667574 322 GGLLSKGHPIGATGVAQIAEIFEQLRGEAG-DVQVDSPEVGLQHNIGiGRNATGAVSCVNILER 384
Cdd:PRK08142 325 GGGLCNNHPANRGGMTKVIEAVRQLRGEAHpAVQVPNCDLALAHGTG-GLLGSRHGSATLILER 387
|
|
| PRK06065 |
PRK06065 |
thiolase domain-containing protein; |
6-358 |
1.61e-52 |
|
thiolase domain-containing protein;
Pssm-ID: 180379 [Multi-domain] Cd Length: 392 Bit Score: 179.25 E-value: 1.61e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 6 VVGAGMIDFGELYEQSFDDLlesAYLSLIENVDK-GVDPSDIDAAWYGTIDIANEG--SSGSAVAHATGLFETPITRVEN 82
Cdd:PRK06065 13 VIGAGLTLFRRRLLETPQEL---AWEAASKALDEaGLELKDIDCVVIGSAPDAFDGvhMKGEYLSHGSGGIRKPVSRVYV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 83 ACATGSDAFRNAAQAVKAGDAEVALVIGAEKMtdSTEGLIASAALERLW-----RGRGVTMPAYFGMRATRHLEEYETTR 157
Cdd:PRK06065 90 GGATGVMTAIAGWYHVASGLCQKVLAVAEEKM--SPARPHPQAVFRYIWdpileKPLNPNLIWIFAMEMHRYMATYGIKK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 158 EQIAEISVKNHENGTKYPHAHQQFECTVEDVKESPTVSYPLNLYDCCPVTDGACAVLVTSEERAREFTDDPIRVAGYGLA 237
Cdd:PRK06065 168 EEIALVSVKNKRNALNNPYAQLGSKITVEDVLKSEVLVWPVQLLDVSPVSDGAAAIVLASEDLARRYTDTPVWVEGVGWT 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 238 SDTFQRGAPEalTNFPA-TRQASSQAYERAGL-GP-DDIDVAEVHDCFSITELITYEDLGFCEDGKGGQFVDEGRPHLDG 314
Cdd:PRK06065 248 LDNTEWPNRD--LAYPRyVEFAARMAYKMAGIeRPrKEIDVAEPYDPFDYKELHHLEGLQLAKRGEAPKLLKEGVFDIDG 325
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1224667574 315 DKPVNPSGGLLSKGHPIGATGVAQIAEIFEQLRGEAGDVQVDSP 358
Cdd:PRK06065 326 DIPSSPSGGLLGVGNPIAAAGLMKVISIYWQLKGTAGKMQVKKP 369
|
|
| PRK08313 |
PRK08313 |
thiolase domain-containing protein; |
38-369 |
8.35e-48 |
|
thiolase domain-containing protein;
Pssm-ID: 181378 [Multi-domain] Cd Length: 386 Bit Score: 166.83 E-value: 8.35e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 38 DKGVDPSDIDAAWYGTIDIANEGSSGS--AVAHATGLFETPITRVENACATGSDAFRNAAQAVKAGDAEVALVIGAEKMT 115
Cdd:PRK08313 38 DAGLTWDDIDAVVVGKAPDFFEGVMMPelFLADALGATGKPLIRVHTAGSVGGSTAVVAASLVQSGVYRRVLAVAWEKQS 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 116 DSTE--GL-IASAALERLWRGRGvtmpAYFGMRATRHLEEYETTREQIAEISVKNHENGTKYPHAH-QQFECTVEDVKES 191
Cdd:PRK08313 118 ESNAmwALsIPVPFTKPVGAGAG----GYFAPHVRAYIRRSGAPEHIGAMVAVKDRLNGAKNPYAHlHQPDITLEKVMAS 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 192 PTVSYPLNLYDCCPVTDGACAVLVTSEERAREFTDDPIR-VAGYGLASDTFQRgAPEALTNFPATRQASSQAYERAGLGP 270
Cdd:PRK08313 194 QMLWDPIRFDETCPSSDGACAVVIGDEEAADAAAGRPVAwIHGTAMRTEPLAF-AGRDQVNPQAGRDAAAALWKAAGITD 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 271 --DDIDVAEVHDCFSITELITYEDLGFCEDGKGGQFVDEGRPHLDGDKPVNPSGGLLSkGHPIGATGVAQIAEIFEQLRG 348
Cdd:PRK08313 273 prDEIDVAEIYVPFSWFEPMWLENLGFAPEGEGWKLTEAGETAIGGRLPVNPSGGVLS-SNPIGASGMIRFAEAALQVMG 351
|
330 340
....*....|....*....|.
gi 1224667574 349 EAGDVQVDSPEVGLQHNIGIG 369
Cdd:PRK08313 352 KAGEHQVDGARKALGHAYGGG 372
|
|
| PRK06066 |
PRK06066 |
thiolase domain-containing protein; |
93-381 |
6.83e-47 |
|
thiolase domain-containing protein;
Pssm-ID: 180380 [Multi-domain] Cd Length: 385 Bit Score: 164.15 E-value: 6.83e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 93 NAAQAVKAGDAEVALVIGAEKMTD-STEGLIASAALERLW-RGRGVTMPAYF-GMRATRHLEEYETTREQIAEISVKNHE 169
Cdd:PRK06066 94 HAVMHINSGLANVVVVEAHSKPSDiLTFSDVVKFAMDPIYvRPIGPPNPHFIaGLDAVKFMSRKGITREDLALVVEKNKK 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 170 NGTKYPHAHQQFECTVEDVKESPTVSYPLNLYDCCPVTDGACAVLVTSEERAREFTDDPIRVAGYGLASDTFQRGAPEaL 249
Cdd:PRK06066 174 AGLSNPRASYASNISLEDVLSSEYVVYPLTELDIAPFVDGAIVVVLASEEVAKKLTDDPVWIKGIGWSTESSNLETAE-L 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 250 TNFPATRQASSQAYERAGLG-PD-DIDVAEVHDCFSITELITYEDLGFCEDGKGGQFVDEGRPHLDGDKPVNPSGGLLSK 327
Cdd:PRK06066 253 GKANYMRIAADMAYKMAGIEsPRkEVDAAEVDDRYSYKELQHIEALRLSEEPEKDSLLREGNFDPQGELPVNPSGGHLAK 332
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1224667574 328 GHPIGATGVAQIAEIFEQLRGEAGDVQVDSpEVGLQHNIGIGRNATGAVSCVNI 381
Cdd:PRK06066 333 GVPLEASGLSLLLDAVEYLRGEAGARQGKA-ERAVVASWRGIPTLTGSVVVVER 385
|
|
| PRK07855 |
PRK07855 |
lipid-transfer protein; Provisional |
38-359 |
6.19e-46 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181147 [Multi-domain] Cd Length: 386 Bit Score: 161.68 E-value: 6.19e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 38 DKGVDPSDIDAAWYGTIDIANEgssgSAVAHATGLFE-TPITRVEN----ACATgsdaFRNAAQAVKAGDAEVALVIGAE 112
Cdd:PRK07855 38 DAGLAPSDVDGLVTFTMDTNPE----IAVARALGIGElKFFSRIHYgggaACAT----VQQAAMAVATGVADVVVCYRAF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 113 K---------MTDSTEGLIASAALERLW-RGRGVTMPAYF-GMRATRHLEEYETTREQIAEISV--KNHENGTKYPHAHQ 179
Cdd:PRK07855 110 NersgmrfgqGQTGLAENPTSTGVDYGWsYPHGLLTPAAWvAMLARRYMHEYGATSEDFGRVAVadRKHAATNPKAWFYG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 180 QfECTVEDVKESPTVSYPLNLYDCCPVTDGACAVLVTSEERAREFTDDPIRV--AGYGLASDTFQRGA--PEALTNFPAT 255
Cdd:PRK07855 190 R-PITLEDHQNSRWIAEPLRLLDCCQESDGAVALVVTSAERARDLKQRPAVIkaAAQGSGADQYMMTSyyRDDITGLPEM 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 256 RQASSQAYERAGLGPDDIDVAEVHDCFSITELITYEDLGFCEDGKGGQFVDEGRPHLDGDKPVNPSGGLLSKGHPIGATG 335
Cdd:PRK07855 269 GLVARQLWAQSGLGPADIDTAILYDHFTPFVLMQLEELGFCGRGEAKDFIADGALELGGRLPINTHGGQLGEAYIHGMNG 348
|
330 340
....*....|....*....|....
gi 1224667574 336 vaqIAEIFEQLRGEAGDvQVDSPE 359
Cdd:PRK07855 349 ---IAEAVRQLRGTSVN-QVPGVE 368
|
|
| AcCoA-C-Actrans |
TIGR01930 |
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ... |
15-347 |
7.61e-31 |
|
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze the thiolysis of a linear fatty acid CoA (or acetoacetyl-CoA) using a second CoA molecule to produce acetyl-CoA and a CoA-ester product two carbons shorter (or, alternatively, the condensation of two molecules of acetyl-CoA to produce acetoacetyl-CoA and CoA). This enzyme is also known as "thiolase", "3-ketoacyl-CoA thiolase", "beta-ketothiolase" and "Fatty oxidation complex beta subunit". When catalyzing the degradative reaction on fatty acids the corresponding EC number is 2.3.1.16. The condensation reaction corresponds to 2.3.1.9. Note that the enzymes which catalyze the condensation are generally not involved in fatty acid biosynthesis, which is carried out by a decarboxylating condensation of acetyl and malonyl esters of acyl carrier proteins. Rather, this activity may produce acetoacetyl-CoA for pathways such as IPP biosynthesis in the absence of sufficient fatty acid oxidation. [Fatty acid and phospholipid metabolism, Other]
Pssm-ID: 273881 [Multi-domain] Cd Length: 385 Bit Score: 121.18 E-value: 7.61e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 15 GELYEQSFDDLLESAYLSLIENVdkGVDPSDIDAAWYGTIDIANEGSS-GSAVAHATGL-FETPITRVENACATGSDAFR 92
Cdd:TIGR01930 14 GSLKDVSAEDLGAAVIKELLERN--PLDPELIDDVIFGNVLQAGEQQNiARQAALLAGLpESVPAYTVNRQCASGLQAVI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 93 NAAQAVKAGDAEVALVIGAEKMTDSTEGLIAS-AALERLWRGRGVTMPAYF----------GMRATRHLEEYETTREQIA 161
Cdd:TIGR01930 92 LAAQLIRAGEADVVVAGGVESMSRVPYGVPRSlRWGVKPGNAELEDARLKDltdantglpmGVTAENLAKKYGISREEQD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 162 EISVKNHENGTKyphAHQQ-------FECTVEDVKESPTVSY------PLNL------------------YDCCPVTDGA 210
Cdd:TIGR01930 172 EYALRSHQRAAK---AWEEglfkdeiVPVTVKGRKGPVTVSSdegirpNTTLeklaklkpafdpdgtvtaGNSSPLNDGA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 211 CAVLVTSEERAREFTDDPI-RVAGYGLASdtfqrGAPEALTNFPAtrQASSQAYERAGLGPDDIDVAEVHDCFSITELIT 289
Cdd:TIGR01930 249 AALLLMSEEKAKELGLTPLaRIVSFAVAG-----VDPEIMGLGPV--PAIPKALKKAGLSISDIDLFEINEAFAAQVLAC 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1224667574 290 YEDLGfcedgkggqfvdegrphLDGDKpVNPSGGLLSKGHPIGATGVAQIAEIFEQLR 347
Cdd:TIGR01930 322 IKELG-----------------LDLEK-VNVNGGAIALGHPLGASGARIVTTLLHELK 361
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
40-347 |
4.85e-27 |
|
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of 3-ketoacyl-CoA into acyl-CoA and acetyl-CoA, a 2-step reaction involving a covalent intermediate formed with a catalytic cysteine. They are found in prokaryotes and eukaryotes (cytosol, microbodies and mitochondria). There are 2 functional different classes: thiolase-I (3-ketoacyl-CoA thiolase) and thiolase-II (acetoacetyl-CoA thiolase). Thiolase-I can cleave longer fatty acid molecules and plays an important role in the beta-oxidative degradation of fatty acids. Thiolase-II has a high substrate specificity. Although it can cleave acetoacyl-CoA, its main function is the synthesis of acetoacyl-CoA from two molecules of acetyl-CoA, which gives it importance in several biosynthetic pathways.
Pssm-ID: 238383 [Multi-domain] Cd Length: 386 Bit Score: 110.65 E-value: 4.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 40 GVDPSDIDAAWYGTIDIANEGSSGS-AVAHATGL-FETPITRVENACATGSDAFRNAAQAVKAGDAEVALVIGAEKMTDS 117
Cdd:cd00751 38 GLDPEEVDDVIMGNVLQAGEGQNPArQAALLAGLpESVPATTVNRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 118 TEGLIASAALERLWRGRGVTMPAYF----------GMRATRHLEEYETTREQIAEISVKNH-------ENG--------- 171
Cdd:cd00751 118 PYLLPKARRGGRLGLNTLDGMLDDGltdpftglsmGITAENVAEKYGISREEQDEFALRSHqraaaaqEAGrfkdeivpv 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 172 -TKYPHAHQQFE--------CTVEDV-------KESPTVSYplnlYDCCPVTDGACAVLVTSEERAREFTDDPI-RVAGY 234
Cdd:cd00751 198 eVPGRKGPVVVDrdegprpdTTLEKLaklkpafKKDGTVTA----GNASGINDGAAAVLLMSEEKAKELGLKPLaRIVGY 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 235 GLASDtfqrgAPEALTNFPATrqASSQAYERAGLGPDDIDVAEVHDCFSITELITYEDLGfcedgkggqfvdegrphLDG 314
Cdd:cd00751 274 AVAGV-----DPAIMGIGPVP--AIPKALKRAGLTLDDIDLIEINEAFAAQALACLKELG-----------------LDP 329
|
330 340 350
....*....|....*....|....*....|...
gi 1224667574 315 DKpVNPSGGLLSKGHPIGATGVAQIAEIFEQLR 347
Cdd:cd00751 330 EK-VNVNGGAIALGHPLGASGARIVVTLLHELK 361
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
6-219 |
2.33e-26 |
|
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl synthase (pfam00109), and also chalcone synthase.
Pssm-ID: 459676 [Multi-domain] Cd Length: 260 Bit Score: 106.23 E-value: 2.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 6 VVGAGMIDFGE----LYEQSFDDLLESAYLSLIEnvDKGVDPSDIDAAWYGTIDIANEGSSGS-AVAHATGL-FETPITR 79
Cdd:pfam00108 3 IVSAARTPFGSfggsLKDVSAVELGAEAIKAALE--RAGVDPEDVDEVIVGNVLQAGEGQNPArQAALKAGIpDSAPAVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 80 VENACATGSDAFRNAAQAVKAGDAEVALVIGAEKMTDSTEGL----IASAALER-------LWRGRGVTMPAYF-GMRAT 147
Cdd:pfam00108 81 INKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALptdaRSGLKHGDekkhdllIPDGLTDAFNGYHmGLTAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 148 RHLEEYETTREQIAEISVKNHENGTKYPHAHQ---------------QFECTVEDVKESPTVSYPLNLY----------- 201
Cdd:pfam00108 161 NVAKKYGISREEQDAFAVKSHQKAAAAPKAGKfkdeivpvtvkgrkgKPTVDKDEGIRPPTTAEPLAKLkpafdkegtvt 240
|
250 260
....*....|....*....|
gi 1224667574 202 --DCCPVTDGACAVLVTSEE 219
Cdd:pfam00108 241 agNASPINDGAAAVLLMSES 260
|
|
| PRK07937 |
PRK07937 |
lipid-transfer protein; Provisional |
90-353 |
1.45e-25 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181173 [Multi-domain] Cd Length: 352 Bit Score: 105.93 E-value: 1.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 90 AFRNAAQAVKAGDAEVALVIGAEKMTDSTEGLIASAALER-----LWRGRgVTMPayfGMRATRHLEEYETTREQIAEIS 164
Cdd:PRK07937 89 ALYEAWVKLLTGEVDTALVYGFGKSSAGTLRRVLALQLDPytvapLWPDS-VSMA---GLQARAGLDAGKWTEEQMAEVA 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 165 VKNHENGTKYPHAhqQFECTVEDVKESPTVSYPLNLYDCCPVTDGACAVLVTSEERAREFTDDPIRVAGYGLASDTFQRG 244
Cdd:PRK07937 165 ARSRADARRNPSA--EPSISVDELLARPYFADPLRRHDIAPITDGAAAVVLAAGDRARELRERPAWITGIEHRIESPSLG 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 245 APEaLTNFPATRQASSQAyerAGLGPDDIDVAEVHDCFSITELITYEDLGfcedgkggqfvdegrphLDGDKPVNPSGGL 324
Cdd:PRK07937 243 ARD-LTRSPSTALAAEAA---TGGDAGGVDVAELHAPFTHQELILREALG-----------------LGDKTKVNPSGGA 301
|
250 260 270
....*....|....*....|....*....|
gi 1224667574 325 LSkGHPIGATGVAQIAEIFEQ-LRGEAGDV 353
Cdd:PRK07937 302 LA-ANPMFAAGLERIGEAARHiWDGSARRA 330
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
40-347 |
1.04e-23 |
|
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 439953 [Multi-domain] Cd Length: 391 Bit Score: 101.30 E-value: 1.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 40 GVDPSDIDAAWYGTIDIANEGSSGS-AVAHATGL-FETPITRVENACATGSDAFRNAAQAVKAGDAEVALVIGAEKMTD- 116
Cdd:COG0183 42 GLDPEAVDDVILGCVLQAGQGQNPArQAALLAGLpESVPAVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRa 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 117 ------STEGLIASAALERLWRGRGVTMPAYF---GMRATRHLEEYETTREQIAEISVKNHEngtKYPHAHQQ--FE--- 182
Cdd:COG0183 122 pmllpkARWGYRMNAKLVDPMINPGLTDPYTGlsmGETAENVAERYGISREEQDAFALRSHQ---RAAAAIAAgrFDdei 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 183 --CTVEDVKESPTVSYplnlyD-----------------------------CCPVTDGACAVLVTSEERAREFTDDPI-R 230
Cdd:COG0183 199 vpVEVPDRKGEVVVDR-----DegprpdttleklaklkpafkkdgtvtagnASGINDGAAALLLMSEEAAKELGLKPLaR 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 231 VAGYGLAsdtfqRGAPEALTNFPAtrQASSQAYERAGLGPDDIDVAEVHDCFSITELITYEDLGfcedgkggqfvdegrp 310
Cdd:COG0183 274 IVAYAVA-----GVDPEIMGIGPV--PATRKALARAGLTLDDIDLIEINEAFAAQVLAVLRELG---------------- 330
|
330 340 350
....*....|....*....|....*....|....*..
gi 1224667574 311 hLDGDKpVNPSGGLLSKGHPIGATGVAQIAEIFEQLR 347
Cdd:COG0183 331 -LDPDK-VNVNGGAIALGHPLGASGARILVTLLHELE 365
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
38-373 |
8.41e-21 |
|
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) Claisen-like condensation reaction. Members are share strong structural similarity, and are involved in the synthesis and degradation of fatty acids, and the production of polyketides, a diverse group of natural products.
Pssm-ID: 238201 [Multi-domain] Cd Length: 254 Bit Score: 90.58 E-value: 8.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 38 DKGVDPSDIDAAWYGTIDIANEGSSGSA-VAHATGLFETPITRVENACATGSDAFRNAAQAVKAGDAEVALVIGAEKmtd 116
Cdd:cd00327 21 DAGLSKGPIVGVIVGTTGGSGEFSGAAGqLAYHLGISGGPAYSVNQACATGLTALALAVQQVQNGKADIVLAGGSEE--- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 117 stegliasaalerlwrgrgvtmpayfgmratrhleeyettreqiaeisvknhengtkyphahqqfectvedvkesptvsy 196
Cdd:cd00327 --------------------------------------------------------------------------------
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 197 plnlydcCPVTDGACAVLVTSEERAREFTDDPI-RVAGYGLASDTFQRGAPEALTNFPAtrqASSQAYERAGLGPDDIDV 275
Cdd:cd00327 98 -------FVFGDGAAAAVVESEEHALRRGAHPQaEIVSTAATFDGASMVPAVSGEGLAR---AARKALEGAGLTPSDIDY 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 276 AEVHDCFSITELITYEDLGFCEdgkggqfvdegrphlDGDKPVNPSGGLLSKGHPIGATGVAQIAEIFEQLRGEAGDVQV 355
Cdd:cd00327 168 VEAHGTGTPIGDAVELALGLDP---------------DGVRSPAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIPPTP 232
|
330 340
....*....|....*....|
gi 1224667574 356 DSPEVGL--QHNIGiGRNAT 373
Cdd:cd00327 233 REPRTVLllGFGLG-GTNAA 251
|
|
| PLN02644 |
PLN02644 |
acetyl-CoA C-acetyltransferase |
40-357 |
3.16e-16 |
|
acetyl-CoA C-acetyltransferase
Pssm-ID: 215347 [Multi-domain] Cd Length: 394 Bit Score: 79.37 E-value: 3.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 40 GVDPSDIDAAWYGTIDIANEGSSGS--AVAHATGLFETPITRVENACATGSDAFRNAAQAVKAGDAEVALVIGAEKMTDS 117
Cdd:PLN02644 41 GVDPALVQEVFFGNVLSANLGQAPArqAALGAGLPPSTICTTVNKVCASGMKAVMLAAQSIQLGINDVVVAGGMESMSNA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 118 TEGLIASAALERLwrGRGVTMPAYF-------------GMRATRHLEEYETTREQIAEISVKNHENGTKyPHAHQQFEC- 183
Cdd:PLN02644 121 PKYLPEARKGSRL--GHDTVVDGMLkdglwdvyndfgmGVCAELCADQYSISREEQDAYAIQSYERAIA-AQEAGAFAWe 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 184 --------------TVEDVKESPTVSYPLNLYDCCPV----------------TDGACAVLVTSEERAREFTDDPI-RVA 232
Cdd:PLN02644 198 ivpvevpggrgrpsVIVDKDEGLGKFDPAKLRKLRPSfkedggsvtagnassiSDGAAALVLVSGEKALELGLQVIaKIR 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 233 GYGLASdtfqrGAPEALTNFPATrqASSQAYERAGLGPDDIDVAEVHDCFSITELITYEDLGfcedgkggqfvdegrphL 312
Cdd:PLN02644 278 GYADAA-----QAPELFTTAPAL--AIPKALKHAGLEASQVDYYEINEAFSVVALANQKLLG-----------------L 333
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1224667574 313 DGDKpVNPSGGLLSKGHPIGATGVAQIAEIFEQLRGEAGDVQVDS 357
Cdd:PLN02644 334 DPEK-VNVHGGAVSLGHPIGCSGARILVTLLGVLRSKNGKYGVAG 377
|
|
| PRK09051 |
PRK09051 |
beta-ketothiolase BktB; |
74-335 |
6.49e-16 |
|
beta-ketothiolase BktB;
Pssm-ID: 181625 [Multi-domain] Cd Length: 394 Bit Score: 78.46 E-value: 6.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 74 ETPITRVENACATGSDAFRNAAQAVKAGDAEVALVIGAEKMTDSTEGLIASAALERLWRGRGVTM-------P---AYFG 143
Cdd:PRK09051 80 ETPAFNVNRLCGSGLQAIVSAAQAILLGDADVAIGGGAESMSRAPYLLPAARWGARMGDAKLVDMmvgalhdPfgtIHMG 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 144 MRATRHLEEYETTREQIAEISVKNHENGTKYPHA-------------------------HQQFECTVED--------VKE 190
Cdd:PRK09051 160 VTAENVAAKYGISREAQDALALESHRRAAAAIAAgyfkdqivpveiktrkgevvfdtdeHVRADTTLEDlaklkpvfKKE 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 191 SPTVSYPlnlyDCCPVTDGACAVLVTSEERAREFTDDPI-RVAGYGLAsdtfqrGAPEALTNF---PATRQAssqaYERA 266
Cdd:PRK09051 240 NGTVTAG----NASGINDGAAAVVLAEADAAEARGLKPLaRLVGYAHA------GVDPEYMGIgpvPATQKA----LERA 305
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1224667574 267 GLGPDDIDVAEVHDCFSITELITYEDLGFcedgkggqfvdegrphlDGDKpVNPSGGLLSKGHPIGATG 335
Cdd:PRK09051 306 GLTVADLDVIEANEAFAAQACAVTRELGL-----------------DPAK-VNPNGSGISLGHPVGATG 356
|
|
| PRK06366 |
PRK06366 |
acetyl-CoA C-acetyltransferase; |
1-347 |
9.81e-16 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 102340 [Multi-domain] Cd Length: 388 Bit Score: 78.13 E-value: 9.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 1 MTDPHVVGAGMIDFGElYEQSFD-----DLLESAYLSLIEnvDKGVDPSDIDAAWYGTIDIANEGS--SGSAVAHATGLF 73
Cdd:PRK06366 1 MKDVYIVSAKRTAIGK-FGRSFSkikapQLGGAAIKAVID--DAKLDPALVQEVIMGNVIQAGVGQnpAGQAAYHAGLPF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 74 ETPITRVENACATGSDAFRNAAQAVKAGDAEVALVIGAEKMTDSTegLIASAALErlWRGR----------------GVT 137
Cdd:PRK06366 78 GVTKYTVNVVCASGMLAVESAAREIMLGERDLVIAGGMENMSNAP--FLLPSDLR--WGPKhllhknykiddamlvdGLI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 138 MPAYF---GMRATRHLEEYETTREQIAEISVKNHENGTKYPHAHQ------QFE----------CTVEDVKESPTV---S 195
Cdd:PRK06366 154 DAFYFehmGVSAERTARKYGITREMADEYSVQSYERAIRATESGEfrneivPFNdldrdegirkTTMEDLAKLPPAfdkN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 196 YPLNLYDCCPVTDGACAVLVTSEERAREFTDDPI-RVAGYGLAS----DTFQrgAPealtnFPATRQAssqaYERAGLGP 270
Cdd:PRK06366 234 GILTAGNSAQLSDGGSALVMASEKAINEYGLKPIaRITGYESASldplDFVE--AP-----IPATRKL----LEKQNKSI 302
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1224667574 271 DDIDVAEVHDCFSITELITYEDLgfcedgkggqfvdegrpHLDGDKpVNPSGGLLSKGHPIGATGVAQIAEIFEQLR 347
Cdd:PRK06366 303 DYYDLVEHNEAFSIASIIVRDQL-----------------KIDNER-FNVNGGAVAIGHPIGNSGSRIIVTLINALK 361
|
|
| PRK05790 |
PRK05790 |
putative acyltransferase; Provisional |
40-335 |
1.14e-15 |
|
putative acyltransferase; Provisional
Pssm-ID: 180261 [Multi-domain] Cd Length: 393 Bit Score: 77.89 E-value: 1.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 40 GVDPSDIDAAWYGTIDIANEGSS-GSAVAHATGL-FETPITRVENACATGSDAFRNAAQAVKAGDAEVALVIGAEKMT-- 115
Cdd:PRK05790 42 GVPPEQVDEVIMGQVLQAGAGQNpARQAALKAGLpVEVPALTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQESMSqa 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 116 -----DSTEG-------LIASAALERLWRG-RGVTMpayfGMRATRHLEEYETTREQIAEISVKNH-------ENGT--- 172
Cdd:PRK05790 122 phvlpGSRWGqkmgdveLVDTMIHDGLTDAfNGYHM----GITAENLAEQYGITREEQDEFALASQqkaeaaiKAGRfkd 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 173 --------------------KYPhahqQFECTVEDV-------KESPTV----SYPLNlydccpvtDGACAVLVTSEERA 221
Cdd:PRK05790 198 eivpvtikqrkgdpvvvdtdEHP----RPDTTAESLaklrpafDKDGTVtagnASGIN--------DGAAAVVVMSEAKA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 222 REFTDDPI-RVAGYGLASdtfqrGAPEALTNFPAtrQASSQAYERAGLGPDDIDVAEVHDCFSITELITYEDLGfcedgk 300
Cdd:PRK05790 266 KELGLTPLaRIVSYAVAG-----VDPAIMGIGPV--PAIRKALEKAGWSLADLDLIEINEAFAAQALAVEKELG------ 332
|
330 340 350
....*....|....*....|....*....|....*
gi 1224667574 301 ggqfvdegrphLDGDKpVNPSGGLLSKGHPIGATG 335
Cdd:PRK05790 333 -----------LDPEK-VNVNGGAIALGHPIGASG 355
|
|
| PRK07851 |
PRK07851 |
acetyl-CoA C-acetyltransferase; |
40-339 |
1.27e-15 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181146 [Multi-domain] Cd Length: 406 Bit Score: 77.74 E-value: 1.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 40 GVDPSDIDAAWYGTIDIANEGSS--GSAVAHATGLFETPITRVENACATGSDAFRNAAQAVKAGDAEVALVIGAEKMT-- 115
Cdd:PRK07851 44 ALDPTDIDDLMLGCGLPGGEQGFnmARVVAVLLGYDFLPGTTVNRYCSSSLQTTRMAFHAIKAGEGDVFISAGVETVSrf 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 116 --------DSTEGLIASAALER----------LW---RGRGVTMPAYFGMRAT------------RHLEEYETTREQIAE 162
Cdd:PRK07851 124 akgnsdslPDTKNPLFAEAQARtaaraeggaeAWhdpREDGLLPDVYIAMGQTaenvaqltgisrEEQDEWGVRSQNRAE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 163 ISVKNH-----------ENGTKY-----PHAhqqfECTVEDVKESPTVSYP---LNLYDCCPVTDGACAVLVTSEERARE 223
Cdd:PRK07851 204 EAIANGffereitpvtlPDGTVVstddgPRA----GTTYEKVSQLKPVFRPdgtVTAGNACPLNDGAAAVVIMSDTKARE 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 224 FTDDPI-RVAGYGLASDTfqrgaPEALTNFPAtrQASSQAYERAGLGPDDIDVAEVHDCFSITELITYEDLGfcedgkgg 302
Cdd:PRK07851 280 LGLTPLaRIVSTGVSGLS-----PEIMGLGPV--EASKQALARAGMSIDDIDLVEINEAFAAQVLPSARELG-------- 344
|
330 340 350
....*....|....*....|....*....|....*..
gi 1224667574 303 qfvdegrphLDGDKpVNPSGGLLSKGHPIGATGvAQI 339
Cdd:PRK07851 345 ---------IDEDK-LNVSGGAIALGHPFGMTG-ARI 370
|
|
| PRK09050 |
PRK09050 |
beta-ketoadipyl CoA thiolase; Validated |
40-340 |
1.71e-14 |
|
beta-ketoadipyl CoA thiolase; Validated
Pssm-ID: 181624 [Multi-domain] Cd Length: 401 Bit Score: 74.22 E-value: 1.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 40 GVDPSDIDAAWYGTidiANE-GSSGSAVAHATGLF-----ETPITRVENACATGSDAFRNAAQAVKAGDAEVALVIGAEK 113
Cdd:PRK09050 43 GVDWEAVDDVIYGC---ANQaGEDNRNVARMSALLaglpvSVPGTTINRLCGSGMDAVGTAARAIKAGEAELMIAGGVES 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 114 MT-------DSTEGLIASAALERL---WRGRGVTMPAYFG---MRATRH--LEEYETTRE-QIA------EISVKNHENG 171
Cdd:PRK09050 120 MSrapfvmgKADSAFSRQAEIFDTtigWRFVNPLMKAQYGvdsMPETAEnvAEDYNISRAdQDAfalrsqQRAAAAQAAG 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 172 T--------KYPH-----------AHQQFECTVEDVKESPTVSYP---LNLYDCCPVTDGACAVLVTSEERAREFTDDPI 229
Cdd:PRK09050 200 FlaeeivpvTIPQkkgdpvvvdrdEHPRPETTLEALAKLKPVFRPdgtVTAGNASGVNDGAAALLLASEAAAKKHGLTPR 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 230 -RVAGYGLAsdtfqrGAPEALTNF---PATRQASsqayERAGLGPDDIDVAEVHDCFSITELITYEDLGFCEDgkggqfv 305
Cdd:PRK09050 280 aRILGMATA------GVEPRIMGIgpaPATRKLL----ARLGLTIDQFDVIELNEAFAAQGLAVLRQLGLADD------- 342
|
330 340 350
....*....|....*....|....*....|....*
gi 1224667574 306 degrphldgDKPVNPSGGLLSKGHPIGATGvAQIA 340
Cdd:PRK09050 343 ---------DARVNPNGGAIALGHPLGMSG-ARLV 367
|
|
| PRK06445 |
PRK06445 |
acetyl-CoA C-acetyltransferase; |
23-361 |
1.92e-14 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180563 [Multi-domain] Cd Length: 394 Bit Score: 73.99 E-value: 1.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 23 DDLLESAYLSLIENVdkGVDPSDIDAAWYGTIDIANEGSS--GSAVAHATGL-FETPITRVENACATGSDAFRNAAQAVK 99
Cdd:PRK06445 33 EELAAMLINRLIEKT--GIKPEEIDDIITGCALQVGENWLygGRHPIFLARLpYNIPAMAVDRQCASSLTTVSIGAMEIA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 100 AGDAEVALVIGAEKMT----------DSTEGLIASAALERLWRGRGVTMpayfGMRATRHLEEYETTREQIAEISVKNHE 169
Cdd:PRK06445 111 TGMADIVIAGGVEHMTrtpmgdnphiEPNPKLLTDPKYIEYDLTTGYVM----GLTAEKLAEEAGIKREEMDRWSLRSHQ 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 170 NGTK-----------YPHAHQ--------------QFECTVEDVKESPTVSYP---LNLYDCCPVTDGACAVLVTSEERA 221
Cdd:PRK06445 187 LAAKaiqegyfkdeiLPIEVEvegkkkvvdvdqsvRPDTSLEKLAKLPPAFKPdgvITAGNSSPLNSGASYVLLMSKKAV 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 222 REFTDDPI-RVAGYGLAsdtfqrGAPEALTN---FPATRQAssqaYERAGLGPDDIDVAEVHDCFSITELITYEDLGfce 297
Cdd:PRK06445 267 KKYGLKPMaKIRSFGFA------GVPPAIMGkgpVPASKKA----LEKAGLSVKDIDLWEINEAFAVVVLYAIKELG--- 333
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1224667574 298 dgkggqfVDEGRphldgdkpVNPSGGLLSKGHPIGATGVAQIAEIFEQLRGEAGDVQVDSPEVG 361
Cdd:PRK06445 334 -------LDPET--------VNIKGGAIAIGHPLGATGARIVGTLARQLQIKGKDYGVATLCVG 382
|
|
| PRK07801 |
PRK07801 |
acetyl-CoA C-acetyltransferase; |
40-351 |
2.71e-14 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181123 [Multi-domain] Cd Length: 382 Bit Score: 73.59 E-value: 2.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 40 GVDPSDIDAAWYGTIDiaNEGSSGSAVAH----ATGL-FETPITRVENACATGSDAFRNAAQAVKAGDAEVALVIGAEKM 114
Cdd:PRK07801 42 GIDPAAVDDVIFGCVD--TIGPQAGNIARtswlAAGLpEEVPGVTVDRQCGSSQQAIHFAAQAVMSGTQDLVVAGGVQNM 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 115 TDSTEGLIASAALE----------RLWRGRGVTMPAYFGMRATRHLEEYETTREQIAEISVKNHENGTKYPHAhQQFE-- 182
Cdd:PRK07801 120 SQIPISSAMTAGEQlgftspfaesKGWLHRYGDQEVSQFRGAELIAEKWGISREEMERFALESHRRAFAAIRA-GRFDne 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 183 -CTVEDVK--ESPTVSYPLNLYDCCPVT--------------DGACAVLVTSEE---------RAREFT-----DDPIrv 231
Cdd:PRK07801 199 iVPVGGVTvdEGPRETSLEKMAGLKPLVeggrltaavasqisDGASAVLLASERavkrhgltpRARIHHlsvrgDDPV-- 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 232 agyglasdtFQRGAPealtnFPATRQAssqaYERAGLGPDDIDVAEVHDCFSITELITYEDLGFcedgkggqfvdegrph 311
Cdd:PRK07801 277 ---------FMLTAP-----IPATRYA----LEKTGLSIDDIDVVEINEAFAPVVLAWLKETGA---------------- 322
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1224667574 312 lDGDKpVNPSGGLLSKGHPIGATGVAQIAEIFEQLRGEAG 351
Cdd:PRK07801 323 -DPAK-VNPNGGAIALGHPLGATGAKLMTTLLHELERTGG 360
|
|
| PRK06205 |
PRK06205 |
acetyl-CoA C-acetyltransferase; |
40-336 |
7.69e-14 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235741 [Multi-domain] Cd Length: 404 Bit Score: 72.33 E-value: 7.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 40 GVDPSDIDAAWYGTIDIANEGSS-GSAVAHATGL-FETPITRVENACATGSDAFRNAAQAVKAGDAEVALVIGAEKM--- 114
Cdd:PRK06205 42 GIDPARIDDVIFGQGYPNGEAPAiGRVAALDAGLpVTVPGMQLDRRCGSGLQAVITAAMQVQTGAADVVIAGGAESMsnv 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 115 ----TDSTEGlIASAALE---RLWRGR----GVTMPAYFGMRATRH--LEEYETTREQIAEISVKNHENGTKyPHAHQQF 181
Cdd:PRK06205 122 efytTDMRWG-VRGGGVQlhdRLARGRetagGRRFPVPGGMIETAEnlRREYGISREEQDALAVRSHQRAVA-AQEAGRF 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 182 --------------ECTVEDVKESPTVSYPLN--------LYDCCP---VT--------DGACAVLVTSEERAREFTDDP 228
Cdd:PRK06205 200 ddeivpvtvpqrkgDPTVVDRDEHPRADTTLEslaklrpiMGKQDPeatVTagnasgqnDAAAACLVTTEDKAEELGLRP 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 229 I-RVAGYGLAsdtfqrGAPEALTNF---PATRQAssqaYERAGLGPDDIDVAEVHDCFSITELITYEDLGFCEDgkggqf 304
Cdd:PRK06205 280 LaRLVSWAVA------GVEPSRMGIgpvPATEKA----LARAGLTLDDIDLIELNEAFAAQVLAVLKEWGFGAD------ 343
|
330 340 350
....*....|....*....|....*....|..
gi 1224667574 305 vDEGRphldgdkpVNPSGGLLSKGHPIGATGV 336
Cdd:PRK06205 344 -DEER--------LNVNGSGISLGHPVGATGG 366
|
|
| fadA |
PRK08947 |
3-ketoacyl-CoA thiolase; Reviewed |
23-335 |
3.33e-13 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181592 [Multi-domain] Cd Length: 387 Bit Score: 70.38 E-value: 3.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 23 DDLleSAYL--SLIENVDKgVDPSDIDAAWYGTIDIANEgsSGSAVAHATGLF-----ETPITRVENACATGSDAFRNAA 95
Cdd:PRK08947 28 EDL--SAHLmrSLLARNPA-LDPAEIDDIIWGCVQQTLE--QGFNIARNAALLagiphSVPAVTVNRLCGSSMQALHDAA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 96 QAVKAGDAEVALVIGAEKM--------TDSTEGL---IASAA------LERLWRGRGVT--MPAYFGMRAtrHLEEYETT 156
Cdd:PRK08947 103 RAIMTGDGDVFLIGGVEHMghvpmnhgVDFHPGLsknVAKAAgmmgltAEMLGKMHGISreQQDAFAARS--HQRAWAAT 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 157 RE-----QIaeISVKNH-ENGTKYPHAHQQ---FECTVEDVKESPTVSYPLNlydcCPVT--------DGACAVLVTSEE 219
Cdd:PRK08947 181 QEgrfknEI--IPTEGHdADGVLKLFDYDEvirPETTVEALAALRPAFDPVN----GTVTagtssalsDGASAMLVMSES 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 220 RAREFTDDPI-RVAGYGLAsdtfqrGAPEALTNF---PATRQAssqaYERAGLGPDDIDVAEVHDCFSITELITYEDLGF 295
Cdd:PRK08947 255 RAKELGLKPRaRIRSMAVA------GCDPSIMGYgpvPATQKA----LKRAGLSISDIDVFELNEAFAAQSLPCLKDLGL 324
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1224667574 296 CEDgkggqfVDEgrphldgdkPVNPSGGLLSKGHPIGATG 335
Cdd:PRK08947 325 LDK------MDE---------KVNLNGGAIALGHPLGCSG 349
|
|
| PRK08235 |
PRK08235 |
acetyl-CoA C-acetyltransferase; |
40-351 |
6.88e-13 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181311 [Multi-domain] Cd Length: 393 Bit Score: 69.36 E-value: 6.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 40 GVDPSDIDAAWYGTIDIANEGSSGS-AVAHATGL-FETPITRVENACATGSDAFRNAAQAVKAGDAEVALVIGAEKMTDS 117
Cdd:PRK08235 42 NVSAEDVEEVIMGTVLQGGQGQIPSrQAARAAGIpWEVQTETVNKVCASGLRAVTLADQIIRAGDASVIVAGGMESMSNA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 118 TEGLIASAALERLWRG---------------RGVTMPAYFGMRAtrhlEEYETTREQIAEISVKNHENGTKYPHA----- 177
Cdd:PRK08235 122 PYILPGARWGYRMGDNevidlmvadgltcafSGVHMGVYGGEVA----KELGISREAQDEWAYRSHQRAVSAHEEgrfee 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 178 --------HQQFECTVEDVKESPTVSYPLN-LYDCCP---------------VTDGACAVLVTSEERAREFTDDPIRVAg 233
Cdd:PRK08235 198 eivpvtipQRKGDPIVVAKDEAPRKDTTIEkLAKLKPvfdktgtitagnapgVNDGAAALVLMSEDRAKQEGRKPLATI- 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 234 ygLAsdtFQRGAPEAlTNFPATR-QASSQAYERAGLGPDDIDVAEVHDCFSITELITYEDLGFcedgkggqfvdegrphl 312
Cdd:PRK08235 277 --LA---HTAIAVEA-KDFPRTPgYAINALLEKTGKTVEDIDLFEINEAFAAVALASTEIAGI----------------- 333
|
330 340 350
....*....|....*....|....*....|....*....
gi 1224667574 313 DGDKpVNPSGGLLSKGHPIGATGVAQIAEIFEQLRGEAG 351
Cdd:PRK08235 334 DPEK-VNVNGGAVALGHPIGASGARIIVTLIHELKRRGG 371
|
|
| PRK06633 |
PRK06633 |
acetyl-CoA C-acetyltransferase; |
44-347 |
1.72e-11 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168632 [Multi-domain] Cd Length: 392 Bit Score: 65.05 E-value: 1.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 44 SDIDAAWYGTIDIAN--EGSSGSAVAHATGLF-----ETPITRVENACATGSDAFRNAAQAVKAGDAEVALVIGAEKMTD 116
Cdd:PRK06633 42 SKIDPALVNEVILGQviTGGSGQNPARQTLIHagipkEVPGYTINKVCGSGLKSVALAANSIMTGDNEIVIAGGQENMSL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 117 STEGLIASAA-------LERLWRGRGVT---MPAYFGMRATRHLEEYETTREQIAEISVKNHENGTKYPHAH------QQ 180
Cdd:PRK06633 122 GMHGSYIRAGakfgdikMVDLMQYDGLTdvfSGVFMGITAENISKQFNISRQEQDEFALSSHKKAAKAQLAGifkdeiLP 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 181 FECTVE--------DVKESPTVSYPLnLYDCCP---------------VTDGACAVLVTSEERAREFTDDPI-RVAGYGL 236
Cdd:PRK06633 202 IEVTIKkttslfdhDETVRPDTSLEI-LSKLRPafdkngvvtagnassINDGAACLMVVSEEALKKHNLTPLaRIVSYAS 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 237 ASDTfqrgaPEALTNFPATrqASSQAYERAGLGPDDIDVAEVHDCFSITELITYEDLGFcedgkggqfvdegrphlDGDK 316
Cdd:PRK06633 281 AGVD-----PSIMGTAPVP--ASQKALSKAGWSVNDLEVIEVNEAFAAQSIYVNREMKW-----------------DMEK 336
|
330 340 350
....*....|....*....|....*....|.
gi 1224667574 317 pVNPSGGLLSKGHPIGATGVAQIAEIFEQLR 347
Cdd:PRK06633 337 -VNINGGAIAIGHPIGASGGRVLITLIHGLR 366
|
|
| PRK08257 |
PRK08257 |
acetyl-CoA acetyltransferase; Validated |
94-353 |
1.82e-11 |
|
acetyl-CoA acetyltransferase; Validated
Pssm-ID: 236204 [Multi-domain] Cd Length: 498 Bit Score: 65.32 E-value: 1.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 94 AAQAVKAGDAEVALVIGAEkmTDSTEGLIASAALERLW-------------RGR----------GVTMPAYF-GM--RAT 147
Cdd:PRK08257 99 AALRIAAGEADVALVAGAE--AQSTATKLRKAGEKLDWtpqdegpladrggDPRpmaspaelrhGLDRPVYVyPLfeNAL 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 148 RH-----LEEYettREQIAEISVKNHENGTKYPHAHQQFECTVEDVKespTVSyPLNLYDCCPVT---------DGACAV 213
Cdd:PRK08257 177 RAalgrsPEEH---RAEMGELWAPFSAVAAKNPHAWIPRERSAEEIV---TPT-PDNRMIAWPYTklmnandmvDQGAAV 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 214 LVTSEERAREFTDDPIR---VAGYGLASDTFQRGAPEALTNFPATRQASSQAYERAGLGPDDIDVAEVHDCFSITELITY 290
Cdd:PRK08257 250 LLTSVAKARRLGVPEDRwvyLHGGADAHDPYDILERPDLHRSPAIRAAGRRALALAGLGIDDIDAFDLYSCFPSAVQVAA 329
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1224667574 291 EDLGfcedgkggqfvdegrphLDGDKPVNPS--GGLLSKGHPIGATGVAQIAEIFEQLRGEAGDV 353
Cdd:PRK08257 330 RELG-----------------LDLDDPRPLTvtGGLPFFGGPGNNYVTHAIAEMVERLRANPGRR 377
|
|
| fadI |
PRK08963 |
3-ketoacyl-CoA thiolase; Reviewed |
40-351 |
3.18e-11 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181597 [Multi-domain] Cd Length: 428 Bit Score: 64.23 E-value: 3.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 40 GVDPSDIDAAWYGTI-------DIANEgssgsaVAHATGL-FETPITRVENACATGSDAFRNAAQAVKAGDAEVALVIGA 111
Cdd:PRK08963 45 EIDPELIEQLVFGQVvqmpeapNIARE------IVLGTGMnVHTDAYSVSRACATSFQAVANVAESIMAGTIDIGIAGGA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 112 EKMTDSTEGLIA--SAALERLWRGR-----------------------------GVTMpayfGMRATRHLEEYETTREQI 160
Cdd:PRK08963 119 DSSSVLPIGVSKklARALVDLNKARtlgqrlklfsrlrlrdllpvppavaeystGLRM----GDTAEQMAKTYGISREEQ 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 161 AEISVKNHENGTK----------YPHAH-QQFECTVED----VKESPTVSYP-LN-LYD----------CCPVTDGACAV 213
Cdd:PRK08963 195 DALAHRSHQLAAQawaegklddeVMTAHvPPYKQPLEEdnniRGDSTLEDYAkLRpAFDrkhgtvtaanSTPLTDGAAAV 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 214 LVTSEERAREFTDDPIrvaGYgLASDTFQ-RGAPEALTNFPAtrQASSQAYERAGLGPDDIDVAEVHDCFSITELITYEd 292
Cdd:PRK08963 275 LLMSESRAKALGLTPL---GY-LRSYAFAaIDVWQDMLLGPA--YATPLALERAGLTLADLTLIDMHEAFAAQTLANLQ- 347
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1224667574 293 lGFCEDgkggQFVDE--GRPH----LDGDKpVNPSGGLLSKGHPIGATGVAQIAEIFEQLRGEAG 351
Cdd:PRK08963 348 -MFASE----RFAREklGRSQaigeVDMSK-FNVLGGSIAYGHPFAATGARMITQTLHELRRRGG 406
|
|
| PRK06025 |
PRK06025 |
acetyl-CoA C-acetyltransferase; |
206-346 |
4.39e-11 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235675 [Multi-domain] Cd Length: 417 Bit Score: 64.03 E-value: 4.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 206 VTDGACAVLVTSEERAREFTDDP-IRVAGYGLASDTfqrgaPEALTNFPATrqASSQAYERAGLGPDDIDVAEVHDCFSI 284
Cdd:PRK06025 274 VVDGAAALLLASKAYAEKHGLKPrARIVAMANMGDD-----PTLMLNAPVP--AAKKVLAKAGLTKDDIDLWEINEAFAV 346
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1224667574 285 TELITYEDLGfcedgkggqfvdegrphLDGDKpVNPSGGLLSKGHPIGATGVAQIAEIFEQL 346
Cdd:PRK06025 347 VAEKFIRDLD-----------------LDRDK-VNVNGGAIALGHPIGATGSILIGTVLDEL 390
|
|
| PRK09052 |
PRK09052 |
acetyl-CoA C-acyltransferase; |
23-347 |
2.03e-10 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 181626 [Multi-domain] Cd Length: 399 Bit Score: 61.94 E-value: 2.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 23 DDLLESAYLSLIENVdKGVDPSDIDAAWYGTIdiANEGSSGSAVAHA----TGLFET-PITRVENACATGSDAFRNAAQA 97
Cdd:PRK09052 32 DDLLAHVLRSAVAQV-PGLDPKLIEDAIVGCA--MPEAEQGLNVARIgallAGLPNSvGGVTVNRFCASGLQAVAMAADR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 98 VKAGDAEVALVIGAEKMTD-STEGLIASAALERLWRGRGVTMpAY-FGMRATRHLEEYETTREQIAEISVKNH------- 168
Cdd:PRK09052 109 IRVGEADVMIAAGVESMSMvPMMGNKPSMSPAIFARDENVGI-AYgMGLTAEKVAEQWKVSREDQDAFALESHqkaiaaq 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 169 ENG------TKYP-HAHQQFECTVE--------DVKESPTVSYPLN-LYDCCPV---------------TDGACAVLVTS 217
Cdd:PRK09052 188 QAGefkdeiTPYEiTERFPDLATGEvdvktrtvDLDEGPRADTSLEgLAKLKPVfankgsvtagnssqtSDGAGAVILVS 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 218 EERAREFTDDPI-RVAGYGLAsdtfqrG-APEALTNFPatRQASSQAYERAGLGPDDIDVAEVHDCFSITELITYEDLGf 295
Cdd:PRK09052 268 EKALKQFNLTPLaRFVSFAVA------GvPPEIMGIGP--IEAIPAALKQAGLKQDDLDWIELNEAFAAQSLAVIRDLG- 338
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1224667574 296 cedgkggqfvdegrphLDGDKpVNPSGGLLSKGHPIGATGVAQIAEIFEQLR 347
Cdd:PRK09052 339 ----------------LDPSK-VNPLGGAIALGHPLGATGAIRTATVVHGLR 373
|
|
| Thiolase_C |
pfam02803 |
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
258-351 |
6.06e-10 |
|
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl synthase (pfam00109), and also chalcone synthase.
Pssm-ID: 397094 [Multi-domain] Cd Length: 123 Bit Score: 56.50 E-value: 6.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 258 ASSQAYERAGLGPDDIDVAEVHDCFSITELITYEDLGFcedgkggqfvdegrphlDGDKpVNPSGGLLSKGHPIGATGVA 337
Cdd:pfam02803 27 AIPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGI-----------------DPEK-VNVNGGAIALGHPLGASGAR 88
|
90
....*....|....
gi 1224667574 338 QIAEIFEQLRGEAG 351
Cdd:pfam02803 89 ILVTLLHELKRRGG 102
|
|
| PLN02287 |
PLN02287 |
3-ketoacyl-CoA thiolase |
23-347 |
8.20e-10 |
|
3-ketoacyl-CoA thiolase
Pssm-ID: 215161 [Multi-domain] Cd Length: 452 Bit Score: 60.16 E-value: 8.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 23 DDLLESAYLSLIENVdkGVDPSDIDAAWYGTIdIANegSSGSAV-----AHATGLFET-PITRVENACATGSDAFRNAAQ 96
Cdd:PLN02287 72 DDLLAPVLKAVVEKT--GLNPSEVGDIVVGTV-LAP--GSQRANecrmaAFYAGFPETvPVRTVNRQCSSGLQAVADVAA 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 97 AVKAGDAEVALVIGAEKMTD---STEGLIaSAALERLWRGRGVTMPayFGMRATRHLEEYETTREQIAEISVKNHEN--- 170
Cdd:PLN02287 147 AIKAGFYDIGIGAGVESMTTnpmAWEGGV-NPRVESFSQAQDCLLP--MGITSENVAERFGVTREEQDQAAVESHRKaaa 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 171 --------------GTKY--PHAHQQFECTV-ED--VKESPTVSYPLNLY------------DCCPVTDGACAVLVTSEE 219
Cdd:PLN02287 224 atasgkfkdeivpvHTKIvdPKTGEEKPIVIsVDdgIRPNTTLADLAKLKpvfkkngtttagNSSQVSDGAGAVLLMKRS 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 220 RAREfTDDPIRVAGYGLASDtfqrGAPEALTNF-PATrqASSQAYERAGLGPDDIDVAEVHDCFSITELITYEDLGfced 298
Cdd:PLN02287 304 VAMQ-KGLPILGVFRSFAAV----GVDPAVMGIgPAV--AIPAAVKAAGLELDDIDLFEINEAFASQFVYCCKKLG---- 372
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1224667574 299 gkggqfvdegrphLDGDKpVNPSGGLLSKGHPIGATGVAQIAEIFEQLR 347
Cdd:PLN02287 373 -------------LDPEK-VNVNGGAIALGHPLGATGARCVATLLHEMK 407
|
|
| PRK09268 |
PRK09268 |
acetyl-CoA C-acetyltransferase; |
205-345 |
1.36e-09 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236440 [Multi-domain] Cd Length: 427 Bit Score: 59.53 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 205 PVTDGACAVLVTSEERAREFTddpIRVAGYGLASDT----FQRGaPEALTNFPAtrQASSQAYERAGLGPDDIDVAEVHD 280
Cdd:PRK09268 263 PLTDGASVVLLASEEWAAEHG---LPVLAYLVDAETaavdFVHG-KEGLLMAPA--YAVPRLLARNGLTLQDFDFYEIHE 336
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1224667574 281 CFSITELIT---YEDLGFCEDGKGgqfVDEGRPHLDGDKpVNPSGGLLSKGHPIGATG---VAQIAEIFEQ 345
Cdd:PRK09268 337 AFASQVLATlkaWEDEEYCRERLG---LDAPLGSIDRSK-LNVNGSSLAAGHPFAATGgriVATLAKLLAE 403
|
|
| PRK06954 |
PRK06954 |
acetyl-CoA C-acetyltransferase; |
40-361 |
2.07e-09 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180775 [Multi-domain] Cd Length: 397 Bit Score: 58.75 E-value: 2.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 40 GVDPSDIDAAWYGTIDIANEGSS-GSAVAHATGL-FETPITRVENACATGSDAFRNAAQAVKAGDAEVALVIGAEKMTDS 117
Cdd:PRK06954 47 GLKPEQIDEVVMGCVLPAGQGQApARQAALGAGLpLSVGCTTVNKMCGSGMRAAMFAHDMLVAGSVDVIVAGGMESMTNA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 118 TEGLIASAALERLWRG----------------RGVTMpayfGMRATRHLEEYETTREQ---------------------- 159
Cdd:PRK06954 127 PYLLPKARGGMRMGHGqvldhmfldgledaydKGRLM----GTFAEECAGEYGFTREAqdafaieslarakranedgsfa 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 160 --IAEISVKNHENGTKYPHAHQQFECTVEDV---KESPTVSYPLNLYDCCPVTDGACAVLVTSEERAREFTDDPI-RVAG 233
Cdd:PRK06954 203 weIAPVTVAGKKGDTVIDRDEQPFKANPEKIptlKPAFSKTGTVTAANSSSISDGAAALVMMRASTAKRLGLAPLaRVVG 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 234 YGlasdTFQRgAPEALTNFPATrqASSQAYERAGLGPDDIDVAEVHDCFSITELITYEDLGFcedgkggqfvdegrPHld 313
Cdd:PRK06954 283 HS----TFAQ-APSKFTTAPVG--AIRKLFEKNGWRAAEVDLFEINEAFAVVTMAAMKEHGL--------------PH-- 339
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1224667574 314 gDKpVNPSGGLLSKGHPIGATGVAQIAEIFEQLRGEAGDVQVDSPEVG 361
Cdd:PRK06954 340 -EK-VNVNGGACALGHPIGASGARILVTLIGALRARGGKRGVASLCIG 385
|
|
| PRK07850 |
PRK07850 |
steroid 3-ketoacyl-CoA thiolase; |
25-346 |
4.31e-09 |
|
steroid 3-ketoacyl-CoA thiolase;
Pssm-ID: 181145 [Multi-domain] Cd Length: 387 Bit Score: 57.81 E-value: 4.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 25 LLESAYLSLIENVdkGVDPSDIDAAWYGTIDIANEGS---SGSAVAHATGLFETPITRVENACATGSDAFRNAAQAVKAG 101
Cdd:PRK07850 29 LLGAVQRAVLDRA--GIDPGDVEQVIGGCVTQAGEQSnniTRTAWLHAGLPYHVGATTIDCQCGSAQQANHLVAGLIAAG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 102 DAEVALVIGAEKMtdSTEGLIASA---------------------ALERLWRGRGVTMPAY--FGM----RATRHLEEYE 154
Cdd:PRK07850 107 AIDVGIACGVEAM--SRVPLGANAgpgrglprpdswdidmpnqfeAAERIAKRRGITREDVdaFGLrsqrRAAQAWAEGR 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 155 TTREqIAEISV------KNHENGTKYPHAHQQF-ECTVEDVKE-SPTVSYPLNLY-DCCPVTDGACAVLVTSEERAREFT 225
Cdd:PRK07850 185 FDRE-ISPVQApvldeeGQPTGETRLVTRDQGLrDTTMEGLAGlKPVLEGGIHTAgTSSQISDGAAAVLWMDEDRARALG 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 226 DDP-IRVAGYGLASdtfqrGAPEALTNFPAtrQASSQAYERAGLGPDDIDVAEVHDCFSITELityedlgfcedgkggQF 304
Cdd:PRK07850 264 LRPrARIVAQALVG-----AEPYYHLDGPV--QATAKVLEKAGMKIGDIDLVEINEAFASVVL---------------SW 321
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1224667574 305 VDEGRPhlDGDKpVNPSGGLLSKGHPIGATGVAQIAEIFEQL 346
Cdd:PRK07850 322 AQVHEP--DMDK-VNVNGGAIALGHPVGSTGARLITTALHEL 360
|
|
| PRK06690 |
PRK06690 |
acetyl-CoA C-acyltransferase; |
33-349 |
1.35e-08 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180659 [Multi-domain] Cd Length: 361 Bit Score: 55.93 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 33 LIENVDKGVDPsDIDAAWYGTIdIANEGSSGSAVAHATGL-FETPITRVENACATGSDAFRNAAQAVKAGDAEVALVIGA 111
Cdd:PRK06690 32 LLTFLSKGMER-EIDDVILGNV-VGPGGNVARLSALEAGLgLHIPGVTIDRQCGAGLEAIRTACHFIQGGAGKCYIAGGV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 112 EkmTDSTEGLIASAALERLWRGRgvtmPAyFGMRATRHLEEYETTREQIAEI-------SVKNHENGTKYPH-------- 176
Cdd:PRK06690 110 E--STSTSPFQNRARFSPETIGD----PD-MGVAAEYVAERYNITREMQDEYaclsykrTLQALEKGYIHEEilsfngll 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 177 -----AHQQFECTVEDVKESPTVSYPLNLYDCCPVTDGACAVLVTSEERAREFTDDPIRvagyglasdTFQRGAPEALT- 250
Cdd:PRK06690 183 desikKEMNYERIIKRTKPAFLHNGTVTAGNSCGVNDGACAVLVMEEGQARKLGYKPVL---------RFVRSAVVGVDp 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 251 NFPATRQ--ASSQAYERAGLGPDDIDVAEVHDCFSITELITYEDLGFCEDgkggqfvdegrphldgdkPVNPSGGLLSKG 328
Cdd:PRK06690 254 NLPGTGPifAVNKLLNEMNMKVEDIDYFEINEAFASKVVACAKELQIPYE------------------KLNVNGGAIALG 315
|
330 340
....*....|....*....|.
gi 1224667574 329 HPIGATGVAQIAEIFEQLRGE 349
Cdd:PRK06690 316 HPYGASGAMLVTRLFYQAKRE 336
|
|
| PRK05656 |
PRK05656 |
acetyl-CoA C-acetyltransferase; |
40-335 |
1.45e-08 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168156 Cd Length: 393 Bit Score: 56.05 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 40 GVDPSDIDAAWYGTIDIANEGSSGS--AVAHATGLFETPITRVENACATGSDAFRNAAQAVKAGDAEVALVIGAEKMTDS 117
Cdd:PRK05656 42 GLDPAQVDEVILGQVLTAGAGQNPArqAAIKAGLPHSVPAMTLNKVCGSGLKALHLAAQAIRCGDAEVIIAGGQENMSLA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 118 TEGLIASAALERLWRGRGV-TMPA----------YFGMRATRHLEEYETTREQIAEISVKNHENGTKYPHA--------- 177
Cdd:PRK05656 122 PYVLPGARTGLRMGHAQLVdSMITdglwdafndyHMGITAENLVEKYGISREAQDAFAAASQQKAVAAIEAgrfddeitp 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 178 ----HQQFECTVEDVKESP---TVSYPL-------------NLYDCCPVTDGACAVLVTSEERAREFtDDPI--RVAGYG 235
Cdd:PRK05656 202 ilipQRKGEPLAFATDEQPragTTAESLaklkpafkkdgsvTAGNASSLNDGAAAVLLMSAAKAKAL-GLPVlaKIAAYA 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 236 LAsdtfqrGAPEALTNFpATRQASSQAYERAGLGPDDIDVAEVHDCFSITELITYEDLGFcedgkggqfvdegrphlDGD 315
Cdd:PRK05656 281 NA------GVDPAIMGI-GPVSATRRCLDKAGWSLAELDLIEANEAFAAQSLAVGKELGW-----------------DAA 336
|
330 340
....*....|....*....|
gi 1224667574 316 KpVNPSGGLLSKGHPIGATG 335
Cdd:PRK05656 337 K-VNVNGGAIALGHPIGASG 355
|
|
| PRK06504 |
PRK06504 |
acetyl-CoA C-acetyltransferase; |
40-335 |
1.38e-07 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180595 [Multi-domain] Cd Length: 390 Bit Score: 52.81 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 40 GVDPSDIDAAWYGTIDIANEGSSGSA--VAHATGLFE-TPITRVENACATGSDAFRNAAQAVKAGDAEVALVIGAEKMTD 116
Cdd:PRK06504 42 GADPALIEDVIMGCVSQVGEQATNVArnAVLASKLPEsVPGTSIDRQCGSSQQALHFAAQAVMSGTMDIVIAAGVESMTR 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 117 STEGLIA------------SAALERlwRGRGVTMPAYFGmrATRHLEEYETTREQIAEISVKNH---------------- 168
Cdd:PRK06504 122 VPMGSPStlpaknglghykSPGMEE--RYPGIQFSQFTG--AEMMAKKYGLSKDQLDEFALQSHqraiaatqagkfkaei 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 169 -------ENGTKYPHAHQQ---FECTVEDVKESPTVSY--PLNLYDCCPVTDGACAVLVTSEERAREFTDDPI-RVAGYg 235
Cdd:PRK06504 198 vpleitrADGSGEMHTVDEgirFDATLEGIAGVKLIAEggRLTAATASQICDGASGVMVVNERGLKALGVKPLaRIHHM- 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 236 lasdTFQRGAPEALTNFPATrqASSQAYERAGLGPDDIDVAEVHDCFSITELITYEDLGfcedgkggqfVDEGRphldgd 315
Cdd:PRK06504 277 ----TVIGGDPVIMLEAPLP--ATERALKKAGMKIDDIDLYEVNEAFASVPLAWLKATG----------ADPER------ 334
|
330 340
....*....|....*....|
gi 1224667574 316 kpVNPSGGLLSKGHPIGATG 335
Cdd:PRK06504 335 --LNVNGGAIALGHPLGASG 352
|
|
| PRK08131 |
PRK08131 |
3-oxoadipyl-CoA thiolase; |
15-335 |
1.54e-07 |
|
3-oxoadipyl-CoA thiolase;
Pssm-ID: 181242 [Multi-domain] Cd Length: 401 Bit Score: 52.86 E-value: 1.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 15 GELYEQSFDDLLESAYLSLIENvdKGVDPSDIDAAWYGTIDIANEGSSGSA--VAHATGL-FETPITRVENACATGSDAF 91
Cdd:PRK08131 19 GALASVRPDDLAATVIRRLLEK--SGFPGDDIEDVILGCTNQAGEDSRNVArnALLLAGLpVTVPGQTVNRLCASGLAAV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 92 RNAAQAVKAGDAEVALVIGAEKMT--------------------DSTEGliASAALERLWRGRGV-TMP-------AYFG 143
Cdd:PRK08131 97 IDAARAITCGEGDLYLAGGVESMSrapfvmgkaesafsrdakvfDTTIG--ARFPNPKIVAQYGNdSMPetgdnvaAEFG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 144 MR-------ATRHLEEYETTREQ------IAEISVKNhenGTKYP------HAHQQFECTVEDVKESPTvsyplnLYDCC 204
Cdd:PRK08131 175 ISredadrfAAQSQAKYQAAKEEgffadeITPIEVPQ---GRKLPpklvaeDEHPRPSSTVEALTKLKP------LFEGG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 205 PVT--------DGACAVLVTSEERAREFTDDPI-RVAGYGLASDtfqrgAPEALTNFPAtrQASSQAYERAGLGPDDIDV 275
Cdd:PRK08131 246 VVTagnasginDGAAALLIGSRAAGEKYGLKPMaRILSSAAAGV-----EPRIMGIGPV--EAIKKALARAGLTLDDMDI 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1224667574 276 AEVHDCFSITELITYEDLGfcedgkggqfvdegrphLDGDKP-VNPSGGLLSKGHPIGATG 335
Cdd:PRK08131 319 IEINEAFASQVLGCLKGLG-----------------VDFDDPrVNPNGGAIAVGHPLGASG 362
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
26-274 |
2.86e-07 |
|
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible for the elongation steps in fatty acid biosynthesis. KASIII catalyses the initial condensation and KAS I and II catalyze further elongation steps by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP.
Pssm-ID: 238430 [Multi-domain] Cd Length: 406 Bit Score: 52.16 E-value: 2.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 26 LESAYLSLIENVDKGVDPSDIDAAwygtidIANEGSSgsAVAHATGLfETPITRVENACATGSDAFRNAAQAVKAGDAEV 105
Cdd:cd00834 112 IEEAYRALLEKGPRRVSPFFVPMA------LPNMAAG--QVAIRLGL-RGPNYTVSTACASGAHAIGDAARLIRLGRADV 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 106 ALVIGAEkmTDSTEGLIASaalerlwrgrgvtmpaYFGMRATrhleeyettreqiaeisvknhengtkyphahqqfectv 185
Cdd:cd00834 183 VIAGGAE--ALITPLTLAG----------------FAALRAL-------------------------------------- 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 186 edvkeSPTVSYPLNLydCCP---------VTDGACAVLVTSEERAREFTDDPI-RVAGYGLASDTFQRGAPEAltNFPAT 255
Cdd:cd00834 207 -----STRNDDPEKA--SRPfdkdrdgfvLGEGAGVLVLESLEHAKARGAKIYaEILGYGASSDAYHITAPDP--DGEGA 277
|
250
....*....|....*....
gi 1224667574 256 RQASSQAYERAGLGPDDID 274
Cdd:cd00834 278 ARAMRAALADAGLSPEDID 296
|
|
| PRK08242 |
PRK08242 |
acetyl-CoA C-acetyltransferase; |
208-335 |
3.22e-07 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236197 [Multi-domain] Cd Length: 402 Bit Score: 51.81 E-value: 3.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 208 DGACAVLVTSEE---------RAReftddpIRVAGYGLASDTFQRGAPEaltnfPATRQAssqaYERAGLGPDDIDVAEV 278
Cdd:PRK08242 261 DGAAAVLIGSEEagkalglkpRAR------IVATATIGSDPTIMLTGPV-----PATRKA----LAKAGLTVDDIDLFEL 325
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1224667574 279 HDCFSITELITYEDLGfcedgkggqfvdegrphLDGDKpVNPSGGLLSKGHPIGATG 335
Cdd:PRK08242 326 NEAFASVVLRFMQALD-----------------IPHDK-VNVNGGAIAMGHPLGATG 364
|
|
| init_cond_enzymes |
cd00827 |
"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
40-112 |
6.18e-07 |
|
"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, including beta-ketoacyl [ACP] synthase, type III and polyketide synthases, type III, which include chalcone synthase and related enzymes. They are characterized by the utlization of CoA substrate primers, as well as the nature of their active site residues.
Pssm-ID: 238423 [Multi-domain] Cd Length: 324 Bit Score: 50.89 E-value: 6.18e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1224667574 40 GVDPSDIDAAWYGT---IDIAneGSSGSAVAHATGLFETPITRVENACATGSDAFRNAAQAVKAGDAEVALVIGAE 112
Cdd:cd00827 64 GIDPDDIGLLIVATespIDKG--KSAATYLAELLGLTNAEAFDLKQACYGGTAALQLAANLVESGPWRYALVVASD 137
|
|
| PksG |
COG3425 |
3-hydroxy-3-methylglutaryl CoA synthase [Lipid transport and metabolism]; ... |
38-111 |
7.62e-07 |
|
3-hydroxy-3-methylglutaryl CoA synthase [Lipid transport and metabolism]; 3-hydroxy-3-methylglutaryl CoA synthase is part of the Pathway/BioSystem: Isoprenoid biosynthesis
Pssm-ID: 442651 [Multi-domain] Cd Length: 382 Bit Score: 50.56 E-value: 7.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 38 DKGVDPSDIDAAWYGT---IDiaNEGSSGSAVAHATGLFETpiTR---VENACATGSDAFRNAAQAVKAGDAEVALVIGA 111
Cdd:COG3425 65 RAGIDPSDIGAVYVGTesgPD--ASKPIATYVHGALGLPPN--CRafeLKFACYAGTAALQAALGWVASGPNKKALVIAS 140
|
|
| FabH |
COG0332 |
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl- ... |
40-116 |
1.28e-05 |
|
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl-[acyl-carrier-protein] synthase III is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440101 [Multi-domain] Cd Length: 323 Bit Score: 46.64 E-value: 1.28e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1224667574 40 GVDPSDIDAAWYGTI--DIAnEGSSGSAVAHATGLFETPITRVENACATGSDAFRNAAQAVKAGDAEVALVIGAEKMTD 116
Cdd:COG0332 67 GIDPEDIDLIIVATVtpDYL-FPSTACLVQHKLGAKNAAAFDINAACSGFVYALSVAAALIRSGQAKNVLVVGAETLSR 144
|
|
| PRK04262 |
PRK04262 |
hypothetical protein; Provisional |
40-111 |
1.20e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 235266 [Multi-domain] Cd Length: 347 Bit Score: 43.74 E-value: 1.20e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1224667574 40 GVDPSDIDAAWYGTidianEG------SSGSAVAHATGL-FETPITRVENACATGSDAFRNAAQAVKAGDAEVALVIGA 111
Cdd:PRK04262 67 GIDPKEIGAVYVGS-----EShpyavkPTATIVAEALGAtPDLTAADLEFACKAGTAALQAAMGLVKSGMIKYALAIGA 140
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
82-112 |
2.32e-04 |
|
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism]; 3-oxoacyl-(acyl-carrier-protein) synthase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440073 [Multi-domain] Cd Length: 409 Bit Score: 42.77 E-value: 2.32e-04
10 20 30
....*....|....*....|....*....|.
gi 1224667574 82 NACATGSDAFRNAAQAVKAGDAEVALVIGAE 112
Cdd:COG0304 159 TACASGAHAIGEAYRLIRRGRADVMIAGGAE 189
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
62-353 |
8.40e-04 |
|
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new carbon-carbon bond by a decarboxylating Claisen-like condensation reaction. Members are involved in the synthesis of fatty acids and polyketides, a diverse group of natural products. Both pathways are an iterative series of additions of small carbon units, usually acetate, to a nascent acyl group. There are 2 classes of decarboxylating condensing enzymes, which can be distinguished by sequence similarity, type of active site residues and type of primer units (acetyl CoA or acyl carrier protein (ACP) linked units).
Pssm-ID: 238421 [Multi-domain] Cd Length: 332 Bit Score: 41.08 E-value: 8.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 62 SGSAVAHATGL-FETPITRVENACATGSDAFRNAAQAVKAGDAEVALVIGAEKMtdstegliasaalerLWRGRGVTMPA 140
Cdd:cd00825 73 PGASGQIATPLgIHGPAYDVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEEL---------------AAPMDCEFDAM 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 141 YFGMRATRHLEEYETTREQIAeisvknhengtkyphahqqfectvedvkesptvsyplnlydccpVTDGACAVLVTSEER 220
Cdd:cd00825 138 GALSTPEKASRTFDAAADGFV--------------------------------------------FGDGAGALVVEELEH 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 221 AREFTDDPI-RVAGYGLASDTFQRGAPeaLTNFPATRQASSQAYERAGLGPDDIDVAEVHDCfSITELITYEDLGFCEDg 299
Cdd:cd00825 174 ALARGAHIYaEIVGTAATIDGAGMGAF--APSAEGLARAAKEALAVAGLTVWDIDYLVAHGT-GTPIGDVKELKLLRSE- 249
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1224667574 300 kggqfvdegrphlDGDKPVNPSGGLLSKGHPIGATGVAQIAEIFeqLRGEAGDV 353
Cdd:cd00825 250 -------------FGDKSPAVSATKAMTGNLSSAAVVLAVDEAV--LMLEHGFI 288
|
|
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
212-363 |
8.48e-04 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 41.19 E-value: 8.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 212 AVLV-TSEERAREFTDDPI-RVAGYGLASDTFQRGAPEalTNFPATRQASSQAYERAGLGPDDIDVAEVHdcfsitelit 289
Cdd:PRK05952 213 AILVlESAELAQKRGAKIYgQILGFGLTCDAYHMSAPE--PDGKSAIAAIQQCLARSGLTPEDIDYIHAH---------- 280
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1224667574 290 yedlgfcedGKGGQFVDEGRP----HLDGDKP-VNPSGGllSKGHPIGATGVAQIAEIFEQLRGeagdvQVDSPEVGLQ 363
Cdd:PRK05952 281 ---------GTATRLNDQREAnliqALFPHRVaVSSTKG--ATGHTLGASGALGVAFSLLALRH-----QQLPPCVGLQ 343
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
76-280 |
2.98e-03 |
|
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, including beta-ketoacyl [ACP] synthase, type I and II and polyketide synthases.They are characterized by the utlization of acyl carrier protein (ACP) thioesters as primer substrates, as well as the nature of their active site residues.
Pssm-ID: 238424 [Multi-domain] Cd Length: 407 Bit Score: 39.34 E-value: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 76 PITRVENACATGSDAFRNAAQAVKAGDAEVALVIGAEKMTDstEGLIASAAlerlwrgrgvtmpayfgMRATrhleeyET 155
Cdd:cd00828 154 PIKTPVGACATALEALDLAVEAIRSGKADIVVVGGVEDPLE--EGLSGFAN-----------------MGAL------ST 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224667574 156 TREQIAEISVKNHENGTkyphahqQFeCTVEdvkesptvsyplnlydccpvtdGACAVLVTSEERAREFTDDPI-RVAGY 234
Cdd:cd00828 209 AEEEPEEMSRPFDETRD-------GF-VEAE----------------------GAGVLVLERAELALARGAPIYgRVAGT 258
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1224667574 235 GLASDTFQRGAPEALtnfPATRQASSQAYERAGLGPDDIDVAEVHD 280
Cdd:cd00828 259 ASTTDGAGRSVPAGG---KGIARAIRTALAKAGLSLDDLDVISAHG 301
|
|
| KAS_III |
cd00830 |
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty ... |
40-116 |
4.71e-03 |
|
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty acid synthase systems. It is found in bacteria and plants. Elongation of fatty acids in the type II systems occurs by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP. KASIII initiates this process by specifically using acetyl-CoA over acyl-CoA.
Pssm-ID: 238426 [Multi-domain] Cd Length: 320 Bit Score: 38.68 E-value: 4.71e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1224667574 40 GVDPSDIDAAWYGTI-DIANEGSSGSAVAHATGLFETPITRVENACATGSDAFRNAAQAVKAGDAEVALVIGAEKMTD 116
Cdd:cd00830 66 GIDADDIDLIIVATStPDYLFPATACLVQARLGAKNAAAFDINAACSGFLYGLSTAAGLIRSGGAKNVLVVGAETLSR 143
|
|
| ACP_syn_III |
pfam08545 |
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III; This domain is found on 3-Oxoacyl- ... |
80-116 |
6.73e-03 |
|
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III; This domain is found on 3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III EC:2.3.1.180, the enzyme responsible for initiating the chain of reactions of the fatty acid synthase in plants and bacteria.
Pssm-ID: 430064 [Multi-domain] Cd Length: 80 Bit Score: 35.18 E-value: 6.73e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1224667574 80 VENACATGSDAFRNAAQAVKAGDAEVALVIGAEKMTD 116
Cdd:pfam08545 3 INAACSGFVYALSTAAALIRSGRAKNVLVIGAETLSK 39
|
|
| PRK06816 |
PRK06816 |
StlD/DarB family beta-ketosynthase; |
84-113 |
7.57e-03 |
|
StlD/DarB family beta-ketosynthase;
Pssm-ID: 235866 Cd Length: 378 Bit Score: 37.97 E-value: 7.57e-03
10 20 30
....*....|....*....|....*....|
gi 1224667574 84 CATGSDAFRNAAQAVKAGDAEVALVIGAEK 113
Cdd:PRK06816 124 CAAGMMALKYAYLSVKAGESRNAVATASEL 153
|
|
| PRK06333 |
PRK06333 |
beta-ketoacyl-ACP synthase; |
73-127 |
7.80e-03 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235781 [Multi-domain] Cd Length: 424 Bit Score: 38.06 E-value: 7.80e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1224667574 73 FETPITRVENACATGSDAFRNAAQAVKAGDAEVALVIGAEKMTD--STEGLIASAAL 127
Cdd:PRK06333 162 FKGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGTEAAIDrvSLAGFAAARAL 218
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
208-279 |
8.75e-03 |
|
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different products, called polyketides, by successive decarboxylating Claisen condensations. PKSs can be divided into 2 groups, modular type I PKSs consisting of one or more large multifunctional proteins and iterative type II PKSs, complexes of several monofunctional subunits.
Pssm-ID: 238429 [Multi-domain] Cd Length: 421 Bit Score: 37.92 E-value: 8.75e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1224667574 208 DGACAVLVTSEERAREftD-DPIR--VAGYGLASDtfqrGAPEALT--NFPATRQASSQAYERAGLGPDDIDVAEVH 279
Cdd:cd00833 235 EGVGVVVLKRLSDALR--DgDRIYavIRGSAVNQD----GRTKGITapSGEAQAALIRRAYARAGVDPSDIDYVEAH 305
|
|
| |
