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Conserved domains on  [gi|2218444680|pdb|7PXP|H]
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Chain H, Benzoylsuccinyl-CoA thiolase subunit

Protein Classification

thiolase family protein( domain architecture ID 10093593)

thiolase family protein similar to Sulfurisphaera tokodaii acetyl-CoA C-acetyltransferase, which catalyzes the transfer of an acetyl group from acetyl-CoA to another molecule of acetyl-CoA to form acetoacetyl-CoA

CATH:  3.40.47.10
EC:  2.3.1.-
Gene Ontology:  GO:0016746
PubMed:  16356722

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SCP-x_thiolase cd00829
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ...
10-376 2.15e-119

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: 351.18  E-value: 2.15e-119
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H       10 AGVGETKFGKHT-VDFDVLGREAALQAMNGSNIDRPDmIQSAYVGN---GMNDMTTGQAVFRGLGMCGpnLPIINVQSAC 85
Cdd:cd00829   1 VGVGMTPFGRRSdRSPLELAAEAARAALDDAGLEPAD-IDAVVVGNaagGRFQSFPGALIAEYLGLLG--KPATRVEAAG 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H       86 SAGAMAVFCAIKDVATGVTDLSIGVGTENHTMHRQS----GAAFSAARSDIETMHGAVMTGKYAMRATRYMHETGATIED 161
Cdd:cd00829  78 ASGSAAVRAAAAAIASGLADVVLVVGAEKMSDVPTGdeagGRASDLEWEGPEPPGGLTPPALYALAARRYMHRYGTTRED 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H      162 LAMITVKNRKHATHNPYAWFKGAITVEEVVNSRMVAYPMTLQQCCGIADGAAAVVVGSKEMMKKLGiAKPVKVAGVVVES 241
Cdd:cd00829 158 LAKVAVKNHRNAARNPYAQFRKPITVEDVLNSRMIADPLRLLDCCPVSDGAAAVVLASEERARELT-DRPVWILGVGAAS 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H      242 GPYH-NRPRDITGDDITETTSEKLYEESGIGPKEVNILELHDAFTIAELLYYECMGLCKKGDGLKFLRDGQSTYGGQCVV 320
Cdd:cd00829 237 DTPSlSERDDFLSLDAARLAARRAYKMAGITPDDIDVAELYDCFTIAELLALEDLGFCEKGEGGKLVREGDTAIGGDLPV 316
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*.
7PXP_H      321 SPRGGLLSYGHPIGASGAAQIAQNVKQLRGECGGYQVgPTPKVAMSHVTGGGLSGT 376
Cdd:cd00829 317 NTSGGLLSKGHPLGATGLAQAVEAVRQLRGEAGARQV-PGARVGLAHNIGGTGSAA 371
 
Name Accession Description Interval E-value
SCP-x_thiolase cd00829
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ...
10-376 2.15e-119

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: 351.18  E-value: 2.15e-119
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H       10 AGVGETKFGKHT-VDFDVLGREAALQAMNGSNIDRPDmIQSAYVGN---GMNDMTTGQAVFRGLGMCGpnLPIINVQSAC 85
Cdd:cd00829   1 VGVGMTPFGRRSdRSPLELAAEAARAALDDAGLEPAD-IDAVVVGNaagGRFQSFPGALIAEYLGLLG--KPATRVEAAG 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H       86 SAGAMAVFCAIKDVATGVTDLSIGVGTENHTMHRQS----GAAFSAARSDIETMHGAVMTGKYAMRATRYMHETGATIED 161
Cdd:cd00829  78 ASGSAAVRAAAAAIASGLADVVLVVGAEKMSDVPTGdeagGRASDLEWEGPEPPGGLTPPALYALAARRYMHRYGTTRED 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H      162 LAMITVKNRKHATHNPYAWFKGAITVEEVVNSRMVAYPMTLQQCCGIADGAAAVVVGSKEMMKKLGiAKPVKVAGVVVES 241
Cdd:cd00829 158 LAKVAVKNHRNAARNPYAQFRKPITVEDVLNSRMIADPLRLLDCCPVSDGAAAVVLASEERARELT-DRPVWILGVGAAS 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H      242 GPYH-NRPRDITGDDITETTSEKLYEESGIGPKEVNILELHDAFTIAELLYYECMGLCKKGDGLKFLRDGQSTYGGQCVV 320
Cdd:cd00829 237 DTPSlSERDDFLSLDAARLAARRAYKMAGITPDDIDVAELYDCFTIAELLALEDLGFCEKGEGGKLVREGDTAIGGDLPV 316
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*.
7PXP_H      321 SPRGGLLSYGHPIGASGAAQIAQNVKQLRGECGGYQVgPTPKVAMSHVTGGGLSGT 376
Cdd:cd00829 317 NTSGGLLSKGHPLGATGLAQAVEAVRQLRGEAGARQV-PGARVGLAHNIGGTGSAA 371
PRK06064 PRK06064
thiolase domain-containing protein;
5-382 7.36e-99

thiolase domain-containing protein;


Pssm-ID: 235688 [Multi-domain]  Cd Length: 389  Bit Score: 299.12  E-value: 7.36e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H         5 REVYIAGVGETKFGKHT-VDFDVLGREAALQAMNGSNIDRPDmIQSAYVGNGMNDMTTGQ-------AVFRGLGmcgpNL 76
Cdd:PRK06064   2 RDVAIIGVGQTKFGELWdVSLRDLAVEAGLEALEDAGIDGKD-IDAMYVGNMSAGLFVSQehiaaliADYAGLA----PI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H        77 PIINVQSACSAGAMAVFCAIKDVATGVTDLSIGVGTENHT---MHRQSGAAFSAARSDIETMHGAVMTGKYAMRATRYMH 153
Cdd:PRK06064  77 PATRVEAACASGGAALRQAYLAVASGEADVVLAAGVEKMTdvpTPDATEAIARAGDYEWEEFFGATFPGLYALIARRYMH 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H       154 ETGATIEDLAMITVKNRKHATHNPYAWFKGAITVEEVVNSRMVAYPMTLQQCCGIADGAAAVVVGSKEMMKKLgIAKPVK 233
Cdd:PRK06064 157 KYGTTEEDLALVAVKNHYNGSKNPYAQFQKEITVEQVLNSPPVADPLKLLDCSPITDGAAAVILASEEKAKEY-TDTPVW 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H       234 VAGVVVESG--PYHNRpRDITGDDITETTSEKLYEESGIGPKEVNILELHDAFTIAELLYYECMGLCKKGDGLKFLRDGQ 311
Cdd:PRK06064 236 IKASGQASDtiALHDR-KDFTTLDAAVVAAEKAYKMAGIEPKDIDVAEVHDCFTIAEILAYEDLGFAKKGEGGKLAREGQ 314
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
7PXP_H       312 STYGGQCVVSPRGGLLSYGHPIGASGAAQIAQNVKQLRGE-CGGYQVGPTPKVAMSHVTGgglsGTEHAACT 382
Cdd:PRK06064 315 TYIGGDIPVNPSGGLKAKGHPVGATGVSQAVEIVWQLRGEaEKGRQQVIGAGYGLTHNVG----GTGHTAVV 382
Thiolase_N pfam00108
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
7-221 7.72e-11

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: 61.93  E-value: 7.72e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H          7 VYIAGVGETKFGKHTVDF-DV----LGREAALQAMNGSNIDrPDMIQSAYVGNgMNDMTTGQAVFR----GLGMCGPnLP 77
Cdd:pfam00108   1 VVIVSAARTPFGSFGGSLkDVsaveLGAEAIKAALERAGVD-PEDVDEVIVGN-VLQAGEGQNPARqaalKAGIPDS-AP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H         78 IINVQSACSAGAMAVFCAIKDVATGVTDLSIGVGTEN--HTMHRQSGAAFSAARSDIETMHG-------AVMTGKYAMRA 148
Cdd:pfam00108  78 AVTINKVCGSGLKAVYLAAQSIASGDADVVLAGGVESmsHAPYALPTDARSGLKHGDEKKHDllipdglTDAFNGYHMGL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H        149 T--RYMHETGATIEDLAMITVKNRKHATHNPYA-------------WFKGAITV--EEVVNSRMVAYPM----------- 200
Cdd:pfam00108 158 TaeNVAKKYGISREEQDAFAVKSHQKAAAAPKAgkfkdeivpvtvkGRKGKPTVdkDEGIRPPTTAEPLaklkpafdkeg 237
                         250       260
                  ....*....|....*....|...
7PXP_H        201 --TLQQCCGIADGAAAVVVGSKE 221
Cdd:pfam00108 238 tvTAGNASPINDGAAAVLLMSES 260
AcCoA-C-Actrans TIGR01930
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ...
205-372 1.81e-09

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: 58.78  E-value: 1.81e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H        205 CCGIADGAAAVVVGSKEMMKKLG---IAKPV--KVAGVVVE---SGPYHnrprditgdditetTSEKLYEESGIGPKEVN 276
Cdd:TIGR01930 241 SSPLNDGAAALLLMSEEKAKELGltpLARIVsfAVAGVDPEimgLGPVP--------------AIPKALKKAGLSISDID 306
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H        277 ILELHDAFTIAELLYYECMGLckkgDGLKflrdgqstyggqcvVSPRGGLLSYGHPIGASGAAQIAQNVKQLRGECGGYQ 356
Cdd:TIGR01930 307 LFEINEAFAAQVLACIKELGL----DLEK--------------VNVNGGAIALGHPLGASGARIVTTLLHELKRRGGRYG 368
                         170
                  ....*....|....*.
7PXP_H        357 VgptpkVAMSHVTGGG 372
Cdd:TIGR01930 369 L-----ATMCIGGGQG 379
PaaJ COG0183
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ...
206-355 2.21e-07

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: 52.38  E-value: 2.21e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H      206 CGIADGAAAVVVGSKEMMKKLGIakpvKVAGVVVESGpyhnrprdITGDDITETT------SEKLYEESGIGPKEVNILE 279
Cdd:COG0183 246 SGINDGAAALLLMSEEAAKELGL----KPLARIVAYA--------VAGVDPEIMGigpvpaTRKALARAGLTLDDIDLIE 313
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
7PXP_H      280 LHDAF---TIAellyyeCMglckkgDGLKFLRDgqstyggqcVVSPRGGLLSYGHPIGASGAAQIAQNVKQLRGECGGY 355
Cdd:COG0183 314 INEAFaaqVLA------VL------RELGLDPD---------KVNVNGGAIALGHPLGASGARILVTLLHELERRGGRY 371
 
Name Accession Description Interval E-value
SCP-x_thiolase cd00829
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ...
10-376 2.15e-119

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: 351.18  E-value: 2.15e-119
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H       10 AGVGETKFGKHT-VDFDVLGREAALQAMNGSNIDRPDmIQSAYVGN---GMNDMTTGQAVFRGLGMCGpnLPIINVQSAC 85
Cdd:cd00829   1 VGVGMTPFGRRSdRSPLELAAEAARAALDDAGLEPAD-IDAVVVGNaagGRFQSFPGALIAEYLGLLG--KPATRVEAAG 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H       86 SAGAMAVFCAIKDVATGVTDLSIGVGTENHTMHRQS----GAAFSAARSDIETMHGAVMTGKYAMRATRYMHETGATIED 161
Cdd:cd00829  78 ASGSAAVRAAAAAIASGLADVVLVVGAEKMSDVPTGdeagGRASDLEWEGPEPPGGLTPPALYALAARRYMHRYGTTRED 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H      162 LAMITVKNRKHATHNPYAWFKGAITVEEVVNSRMVAYPMTLQQCCGIADGAAAVVVGSKEMMKKLGiAKPVKVAGVVVES 241
Cdd:cd00829 158 LAKVAVKNHRNAARNPYAQFRKPITVEDVLNSRMIADPLRLLDCCPVSDGAAAVVLASEERARELT-DRPVWILGVGAAS 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H      242 GPYH-NRPRDITGDDITETTSEKLYEESGIGPKEVNILELHDAFTIAELLYYECMGLCKKGDGLKFLRDGQSTYGGQCVV 320
Cdd:cd00829 237 DTPSlSERDDFLSLDAARLAARRAYKMAGITPDDIDVAELYDCFTIAELLALEDLGFCEKGEGGKLVREGDTAIGGDLPV 316
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*.
7PXP_H      321 SPRGGLLSYGHPIGASGAAQIAQNVKQLRGECGGYQVgPTPKVAMSHVTGGGLSGT 376
Cdd:cd00829 317 NTSGGLLSKGHPLGATGLAQAVEAVRQLRGEAGARQV-PGARVGLAHNIGGTGSAA 371
PRK06064 PRK06064
thiolase domain-containing protein;
5-382 7.36e-99

thiolase domain-containing protein;


Pssm-ID: 235688 [Multi-domain]  Cd Length: 389  Bit Score: 299.12  E-value: 7.36e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H         5 REVYIAGVGETKFGKHT-VDFDVLGREAALQAMNGSNIDRPDmIQSAYVGNGMNDMTTGQ-------AVFRGLGmcgpNL 76
Cdd:PRK06064   2 RDVAIIGVGQTKFGELWdVSLRDLAVEAGLEALEDAGIDGKD-IDAMYVGNMSAGLFVSQehiaaliADYAGLA----PI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H        77 PIINVQSACSAGAMAVFCAIKDVATGVTDLSIGVGTENHT---MHRQSGAAFSAARSDIETMHGAVMTGKYAMRATRYMH 153
Cdd:PRK06064  77 PATRVEAACASGGAALRQAYLAVASGEADVVLAAGVEKMTdvpTPDATEAIARAGDYEWEEFFGATFPGLYALIARRYMH 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H       154 ETGATIEDLAMITVKNRKHATHNPYAWFKGAITVEEVVNSRMVAYPMTLQQCCGIADGAAAVVVGSKEMMKKLgIAKPVK 233
Cdd:PRK06064 157 KYGTTEEDLALVAVKNHYNGSKNPYAQFQKEITVEQVLNSPPVADPLKLLDCSPITDGAAAVILASEEKAKEY-TDTPVW 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H       234 VAGVVVESG--PYHNRpRDITGDDITETTSEKLYEESGIGPKEVNILELHDAFTIAELLYYECMGLCKKGDGLKFLRDGQ 311
Cdd:PRK06064 236 IKASGQASDtiALHDR-KDFTTLDAAVVAAEKAYKMAGIEPKDIDVAEVHDCFTIAEILAYEDLGFAKKGEGGKLAREGQ 314
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
7PXP_H       312 STYGGQCVVSPRGGLLSYGHPIGASGAAQIAQNVKQLRGE-CGGYQVGPTPKVAMSHVTGgglsGTEHAACT 382
Cdd:PRK06064 315 TYIGGDIPVNPSGGLKAKGHPVGATGVSQAVEIVWQLRGEaEKGRQQVIGAGYGLTHNVG----GTGHTAVV 382
PRK08256 PRK08256
lipid-transfer protein; Provisional
5-372 6.01e-92

lipid-transfer protein; Provisional


Pssm-ID: 181327 [Multi-domain]  Cd Length: 391  Bit Score: 281.40  E-value: 6.01e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H         5 REVYIAGVGETKFGK--HTVDFDVLGREAALQAMNGSNIDRpDMIQSAYVGNGMNDMTTGQAVFRGLGMCGpnLPIINVQ 82
Cdd:PRK08256   1 NKVFVAGVGMTPFEKpgASWDYPDMAAEAGRAALADAGIDY-DAVQQAYVGYVYGDSTSGQRALYEVGMTG--IPIVNVN 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H        83 SACSAGAMAVFCAIKDVATGVTDLSIGVGTENhtMHRQS-GAAFS----------AARSDIETMHGAVMTGKYAMRATR- 150
Cdd:PRK08256  78 NNCSTGSTALFLARQAVRSGAADCALALGFEQ--MQPGAlGSVWDdrpsplerfdKALAELQGFDPAPPALRMFGGAGRe 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H       151 YMHETGATIEDLAMITVKNRKHATHNPYAWFKGAITVEEVVNSRMVAYPMTLQQCCGIADGAAAVVVGSKEMMKKLGIAK 230
Cdd:PRK08256 156 HMEKYGTTAETFAKIGVKARRHAANNPYAQFRDEYTLEDVLASPMIWGPLTRLQCCPPTCGAAAAIVCSEEFARKHGLDR 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H       231 PVKVAGVVVES---GPYHNR-PRDITGDDITETTSEKLYEESGIGPKEVNILELHDAFTIAELLYYECMGLCKKGDGLKF 306
Cdd:PRK08256 236 AVEIVAQAMTTdtpSTFDGRsMIDLVGYDMTRAAAQQVYEQAGIGPEDIDVVELHDCFSANELLTYEALGLCPEGEAEKF 315
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
7PXP_H       307 LRDGQSTYGGQCVVSPRGGLLSYGHPIGASGAAQIAQNVKQLRGECGGYQVgPTPKVAMSHVTG-GG 372
Cdd:PRK08256 316 IDDGDNTYGGRWVVNPSGGLLSKGHPLGATGLAQCAELTWQLRGTAGARQV-EGARLALQHNLGlGG 381
PRK12578 PRK12578
thiolase domain-containing protein;
5-383 2.31e-79

thiolase domain-containing protein;


Pssm-ID: 183606 [Multi-domain]  Cd Length: 385  Bit Score: 248.99  E-value: 2.31e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H         5 REVYIAGVGETKFGKHT-VDFDVLGREAALQAMNGSNIDRPDMiqsayvgngmNDMTTGQAVFRGLGMCgPNLPI----- 78
Cdd:PRK12578   1 RRVAVIGVGNSKFGRRDdVSVQELAWESIKEALNDAGVSQTDI----------ELVVVGSTAYRGIELY-PAPIVaeysg 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H        79 ------INVQSACSAGAMAVFCAIKDVATGVTDLSIGVGTENHT-MHRQSGAAFSAARSDIE---TMHGAVMTGKYAMRA 148
Cdd:PRK12578  70 ltgkvpLRVEAMCATGLAASLTAYTAVASGLVDMAIAVGVDKMTeVDTSTSLAIGGRGGNYQweyHFYGTTFPTYYALYA 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H       149 TRYMHETGATIEDLAMITVKNRKHATHNPYAWFKGAITVEEVVNSRMVAYPMTLQQCCGIADGAAAVVVGSKEMMKKLGI 228
Cdd:PRK12578 150 TRHMAVYGTTEEQMALVSVKAHKYGAMNPKAHFQKPVTVEEVLKSRAISWPIKLLDSCPISDGSATAIFASEEKVKELKI 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H       229 AKPVKVAGVVVESG-PYHNRPRDITGDDITETTSEKLYEESGIGPKEVNILELHDAFTIAELLYYECMGLCKKGDGLKFL 307
Cdd:PRK12578 230 DSPVWITGIGYANDyAYVARRGEWVGFKATQLAARQAYNMAKVTPNDIEVATVHDAFTIAEIMGYEDLGFTEKGKGGKFI 309
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
7PXP_H       308 RDGQSTYGGQCVVSPRGGLLSYGHPIGASGAAQIAQNVKQLRGECGGYQVGPTPKVAMSHVTGgglsGTEHAACTM 383
Cdd:PRK12578 310 EEGQSEKGGKVGVNLFGGLKAKGHPLGATGLSMIYEITKQLRDEAGKLQQPLKKYIGLVHNVG----GTGHFAYVM 381
PRK06157 PRK06157
acetyl-CoA acetyltransferase; Validated
3-371 9.62e-68

acetyl-CoA acetyltransferase; Validated


Pssm-ID: 180433 [Multi-domain]  Cd Length: 398  Bit Score: 219.51  E-value: 9.62e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H         3 LQREVYIAGVGETKFGKH-TVDFDVLGREAALQAMNGSNIDRPDmIQSAYVGNGMNDMTTGQA---VFRGLGMcgPNLPI 78
Cdd:PRK06157   5 IKDKVAILGMGCTKFGERwDAGAEDLMVEAFLEALADAGIEPKD-IDAAWFGTHYDEIGSGKSgtpLSRALRL--PNIPV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H        79 INVQSACSAGAMAVFCAIKDVATGVTDLSIGVGTENHTMHRQSGAAFSAARSDIE-TMHGAVMTGKYAMRATRYMHETGA 157
Cdd:PRK06157  82 TRVENFCATGSEAFRGAVYAVASGAYDIALALGVEKLKDTGYGGLPVANPGTLADmTMPNVTAPGNFAQLASAYAAKYGV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H       158 TIEDL----AMITVKNRKHATHNPYAWFKGAITVEEVVNSRMVAYPMTLQQCCGIADGAAAVVVGSKEMMKKLGIAKPVK 233
Cdd:PRK06157 162 SREDLkramAHVSVKSHANGARNPKAHLRKAVTEEQVLKAPMIAGPLGLFDCCGVSDGAAAAIVTTPEIARALGKKDPVY 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H       234 VAGV--VVESG-PYHNRPRDITGDDITETTSEKLYEESGI-GP-KEVNILELHDAFTIAELLYYECMGLCKKGDGLKFLR 308
Cdd:PRK06157 242 VKALqlAVSNGwELQYNGWDGSYFPTTRIAARKAYREAGItDPrEELSMAEVHDCFSITELVTMEDLGLSERGQAWRDVL 321
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
7PXP_H       309 DGQSTYGGQCVVSPRGGLLSYGHPIGASGAAQIAQNVKQLRGECGGYQVgPTPKVAMSHVTGG 371
Cdd:PRK06157 322 DGFFDADGGLPCQIDGGLKCFGHPIGASGLRMLYEMYLQLLGRAGERQL-KNPRLALTHNLGG 383
PRK06059 PRK06059
lipid-transfer protein; Provisional
5-370 9.88e-65

lipid-transfer protein; Provisional


Pssm-ID: 180373 [Multi-domain]  Cd Length: 399  Bit Score: 211.55  E-value: 9.88e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H         5 REVYIAGVGETKFGKHTVDFDVLGREAALQAMNGSNIDRPDM---IQSAYVGNGMNDMTTGQAVFRGLGMCGpnLPIINV 81
Cdd:PRK06059   4 EPVYILGAGMHPWGKWGRDFVEYGVVAARAALADAGLDWRDVqlvVGADTIRNGYPGFVAGATFAQALGWNG--APVSSS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H        82 QSACSAGAMAVFCAIKDVATGVTDLSIGVGTEnhTMHRQSGAAFSAARSD------IETMhGAVMTGKYAMRATRYMHET 155
Cdd:PRK06059  82 YAACASGSQALQSARAQILAGLCDVALVVGAD--TTPKGFFAPVGGERPDdpdwlrFHLI-GATNPVYFALLARRRMDLY 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H       156 GATIEDLAMITVKNRKHATHNPYAWFKGAITVEEVVNSRMVAYPMTLQQCCGIADGAAAVVVGSKEMMKKL--GIAKPVK 233
Cdd:PRK06059 159 GATVEDFAQVKVKNARHGLLNPNARYRKEVTVEDVLASPVVSDPLRLLDICATSDGAAALIVASKSFARRHlgSVAGVPS 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H       234 VAGVVVESGPYHN---RPRDITGDD----------ITETTSEKLYEESGIGPKEVNILELHDAFTIAELLYYECMGLCKK 300
Cdd:PRK06059 239 VRAISTVTPRYPQhlpELPDIATDStaavpapervFKDQILDAAYAEAGIGPEDLSLAEVYDLSTALELDWYEHLGLCPK 318
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H       301 GDGLKFLRDGQSTYGGQCVVSPRGGLLSYGHPIGASGAAQIAQNVKQLRGECGGYQVgPTPKVAMSHVTG 370
Cdd:PRK06059 319 GEAEALLRSGATTLGGRIPVNPSGGLACFGEAIPAQAIAQVCELTWQLRGQAGGRQV-EGARVGITANQG 387
PRK06365 PRK06365
thiolase domain-containing protein;
2-350 7.28e-53

thiolase domain-containing protein;


Pssm-ID: 235785 [Multi-domain]  Cd Length: 430  Bit Score: 181.65  E-value: 7.28e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H         2 KLQREVYIAGVGETKFGKHT--VDFDVLGREAALQAMNGSNIDRPDMIQS--AYVGNGMNDMTTGQAVFRGLGMCGPnLP 77
Cdd:PRK06365  13 KKSRDVYMVAAGVTKFDKASpyMDFRERVKKAFDYAMNDAGLTLADIDGSvaSYFSDHFQRQLLAGIMVQDYLGLVP-KP 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H        78 IINVQSACSAGAMAVFCAIKDVATGVTDLSIGVGTENHT-MHRQSGAAFSAARSDI--ETMHGAVMTGKYAMRATRYMHE 154
Cdd:PRK06365  92 SKRIEGGGATGGLAFQAGYEEIASGRMDCVAVYGFETMShVNTWKGNEFIALASDTnfDYPLGGFYTGYYAMMAVRHMYE 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H       155 TGATIEDLAMITVKNRKHATHNPYAWFKGAITVEEVVNSRMVAYPMTLQQCCGIADGAAAVVVGSKEmmKKLGIA-KPVK 233
Cdd:PRK06365 172 FGTTVEQLAKVSVKNHGNAIHNPFAQSPMKITVEDVRKSPMVSYPLTRLDVCAMSDGAACAILASED--KAFEITdKPVL 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H       234 VAGvvVESGPYHNRPRDITGDDITETTSEK------------------------LYEESGIGP--KEVNILELHDAFTIA 287
Cdd:PRK06365 250 IKA--IGTGSDTLRLADRPFGEVPLLPNESpddykdlrypgvhsfragrmaakeAYEMAGITDplNDLDLIELHDAYTSS 327
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
7PXP_H       288 ELLYYECMGLCKKGDGLKFLRDGQSTYGGQCVVSPRGGLLSYGHPIGASGAAQIAQNVKQLRG 350
Cdd:PRK06365 328 EIQTYEDLGLCKYGEGGQFIESGKPELPGKLPVNPSGGLLAAGHAVGATGIMQAVFMFWQLQG 390
nondecarbox_cond_enzymes cd00826
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ...
10-372 2.81e-52

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: 179.23  E-value: 2.81e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H       10 AGVGETKFGK----HTVDFDVLGREAALQAMNGSNI---DRPDMIQSAYVG----NGMNDMTTGQAVFRGLGMCGpnLPI 78
Cdd:cd00826   1 AGAAMTAFGKfggeNGADANDLAHEAGAKAIAAALEpagVAAGAVEEACLGqvlgAGEGQNCAQQAAMHAGGLQE--APA 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H       79 INVQSACSAGAMAVFCAIKDVATGVTDLSIGVGTENHTmhrqsgaafSAARSDIETMHGAVMTGKYAMRATRY------- 151
Cdd:cd00826  79 IGMNNLCGSGLRALALAMQLIAGGDANCILAGGFEKME---------TSAENNAKEKHIDVLINKYGMRACPDafalagq 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H      152 -----MHETGATIEDLAMITVKNRK---HATHNPYAWFKGAITVEEVVNSRMVAYP---MTLQQCCGIADGAAAVVVGSK 220
Cdd:cd00826 150 agaeaAEKDGRFKDEFAKFGVKGRKgdiHSDADEYIQFGDEASLDEIAKLRPAFDKedfLTAGNACGLNDGAAAAILMSE 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H      221 EMMKKLGI---AKPVKVAGVVVESGPYHNRPRDI--TGDDITETTSEKLYEESGIGPKEVNILELHDAFTIAELLYYECM 295
Cdd:cd00826 230 AEAQKHGLqskAREIQALEMITDMASTFEDKKVIkmVGGDGPIEAARKALEKAGLGIGDLDLIEAHDAFAANACATNEAL 309
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
7PXP_H      296 GLCKKGDGLKFLRDGQSTYGGQCVVSPRGGLLSYGHPIGASGAAQIAQNVKQLRGECGGYQvGPTPKVAMSHVTGGG 372
Cdd:cd00826 310 GLCPEGQGGALVDRGDNTYGGKSIINPNGGAIAIGHPIGASGAAICAELCFELKGEAGKRQ-GAGAGLALLCIGGGG 385
PRK06158 PRK06158
thiolase; Provisional
144-374 5.04e-52

thiolase; Provisional


Pssm-ID: 180434 [Multi-domain]  Cd Length: 384  Bit Score: 177.92  E-value: 5.04e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H       144 YAMRATRYMHETGATIEDLAMITVKNRKHATHNPYAWFKGAITVEEVVNSRMVAYPMTLQQCCGIADGAAAVVVGSKEMM 223
Cdd:PRK06158 144 YALAAARHMHQYGTTREQLAEVAVAARQWAQLNPEAFMRDPLTIDDVLAARMVSDPLSVRDCCLVTDGAGAVVMVRADRA 223
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H       224 KKLGiAKPVKVAGVVVESGpyHnrpRDITG-DDITET----TSEKLYEESGIGPKEVNILELHDAFTIAELLYYECMGLC 298
Cdd:PRK06158 224 RDLP-RPPVYVLGAAAATW--H---RQISSmPDLTVTaaaeSGPRAFAMAGLTPADIDVVELYDAFTINTILFLEDLGFC 297
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
7PXP_H       299 KKGDGLKFLRDGQSTYGGQCVVSPRGGLLSYGHPiGASGAAQIAQNVKQLRGECGGYQVgPTPKVAMSHVTGGGLS 374
Cdd:PRK06158 298 AKGEGGAFVEGGRIAPGGRLPVNTNGGGLSCVHP-GMYGLFLLIEAVRQLRGEAGERQV-AGAEVALAHGNGGVLS 371
PRK07516 PRK07516
thiolase domain-containing protein;
7-371 6.17e-46

thiolase domain-containing protein;


Pssm-ID: 181013 [Multi-domain]  Cd Length: 389  Bit Score: 162.04  E-value: 6.17e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H         7 VYIAGVGETKFGKH-TVDFDVLGREAALQAMNGSNIDrPDMIQSAYVGNgMNDMTTGQAvFRG--LGMCGPNL---PIIN 80
Cdd:PRK07516   4 ASIVGWAHTPFGKLdAETLESLIVRVAREALAHAGIA-AGDVDGIFLGH-FNAGFSPQD-FPAslVLQADPALrfkPATR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H        81 VQSACSAGAMAVFCAIKDVATGVTDLSIGVGTE--NHTMHRQSG-----AAFSAARSDIetmhGAVMTGKYAMRATRYMH 153
Cdd:PRK07516  81 VENACATGSAAVYAALDAIEAGRARIVLVVGAEkmTATPTAEVGdillgASYLKEEGDT----PGGFAGVFGRIAQAYFQ 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H       154 ETGATIEDLAMITVKNRKHATHNPYAWFKGAITVE--EVVNSR--MVAYPMTLQQCCGIADGAAAVVVGSKEMMKKLgiA 229
Cdd:PRK07516 157 RYGDQSDALAMIAAKNHANGVANPYAQMRKDLGFEfcRTVSEKnpLVAGPLRRTDCSLVSDGAAALVLADAETARAL--Q 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H       230 KPVKVAGVVVESGPYHNRPRDITGDDITETTSEKLYEESGIGPKEVNILELHDAFTIAELLYYECMGLCKKGDGLKFLRD 309
Cdd:PRK07516 235 RAVRFRARAHVNDFLPLSRRDPLAFEGPRRAWQRALAQAGVTLDDLSFVETHDCFTIAELIEYEAMGLAPPGQGARAIRE 314
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
7PXP_H       310 GQSTYGGQCVVSPRGGLLSYGHPIGASGAAQIAQNVKQLRGECGGYQVgPTPKVAMSHVTGG 371
Cdd:PRK07516 315 GWTAKDGKLPVNPSGGLKAKGHPIGATGVSMHVLAAMQLTGEAGGMQI-PGAKLAGVFNMGG 375
PRK07855 PRK07855
lipid-transfer protein; Provisional
9-371 1.26e-45

lipid-transfer protein; Provisional


Pssm-ID: 181147 [Multi-domain]  Cd Length: 386  Bit Score: 161.30  E-value: 1.26e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H         9 IAGVGETKFGKHtvdfdvLGR-------EAALQAMNGSNIDRPDMiqSAYVGNGMnDMTTGQAVFRGLGM---------- 71
Cdd:PRK07855   8 IVGIGATEFSKN------SGRselrlacEAVLAALDDAGLAPSDV--DGLVTFTM-DTNPEIAVARALGIgelkffsrih 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H        72 ------CGPnlpiinVQSAcsagAMAVfcaikdvATGVTDlsigVGTENHTMHRQSGAAF---SAARSDIETMHGAVMTG 142
Cdd:PRK07855  79 ygggaaCAT------VQQA----AMAV-------ATGVAD----VVVCYRAFNERSGMRFgqgQTGLAENPTSTGVDYGW 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H       143 KY-----------AMRATRYMHETGATIEDLAMITVKNRKHATHNPYAWFKG-AITVEEVVNSRMVAYPMTLQQCCGIAD 210
Cdd:PRK07855 138 SYphglltpaawvAMLARRYMHEYGATSEDFGRVAVADRKHAATNPKAWFYGrPITLEDHQNSRWIAEPLRLLDCCQESD 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H       211 GAAAVVVGSKEMMKKLGiAKPVKVAGVVVESGP-------YHNrpRDITGDDITETTSEKLYEESGIGPKEVNILELHDA 283
Cdd:PRK07855 218 GAVALVVTSAERARDLK-QRPAVIKAAAQGSGAdqymmtsYYR--DDITGLPEMGLVARQLWAQSGLGPADIDTAILYDH 294
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H       284 FTIAELLYYECMGLCKKGDGLKFLRDGQSTYGGQCVVSPRGGLLS--YGHpiGASGaaqIAQNVKQLRGEcggyQVGPTP 361
Cdd:PRK07855 295 FTPFVLMQLEELGFCGRGEAKDFIADGALELGGRLPINTHGGQLGeaYIH--GMNG---IAEAVRQLRGT----SVNQVP 365
                        410
                 ....*....|
7PXP_H       362 KVAMSHVTGG 371
Cdd:PRK07855 366 GVENVLVTAG 375
PRK08142 PRK08142
thiolase domain-containing protein;
116-383 9.76e-44

thiolase domain-containing protein;


Pssm-ID: 236164 [Multi-domain]  Cd Length: 388  Bit Score: 156.40  E-value: 9.76e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H       116 TMHRQSGAafSAARSDIETMHGAVMTGKYAMRATRYMHETGATIEDLAMITVKNRKHATHNPYAWFKGAITVEEVVNSRM 195
Cdd:PRK08142 120 TEPRNWGA--DAPDAPFEAPYGPTTHNLYAMCAMRHMHEYGTTSEQLAWIKVAASHHAQHNPHAMLRDVVTVEDVLNSPM 197
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H       196 VAYPMTLQQCCGIADGAAAVVVGSKEMMKKLgiAKP-VKVAGvvveSGPYHNRPRDitGD-DITET----TSEKLYEESG 269
Cdd:PRK08142 198 IADPLHRLDCCVVTDGGGALVVVRPEIARSL--KRPlVKVLG----AGEAIKGQMG--GKvDLTYSgaawSGPAAFAEAG 269
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H       270 IGPKEVNILELHDAFTIAELLYYECMGLCKKGDGLKFLRDGQSTYG-GQCVVSPRGGLLSYGHPIGASGAAQIAQNVKQL 348
Cdd:PRK08142 270 VTPADIKYASIYDSFTITVLMQLEDLGFCKKGEGGKFVADGNLISGvGKLPFNTDGGGLCNNHPANRGGMTKVIEAVRQL 349
                        250       260       270
                 ....*....|....*....|....*....|....*.
7PXP_H       349 RGECG-GYQVgPTPKVAMSHVTGGGLsGTEHAACTM 383
Cdd:PRK08142 350 RGEAHpAVQV-PNCDLALAHGTGGLL-GSRHGSATL 383
PRK08313 PRK08313
thiolase domain-containing protein;
5-372 2.47e-41

thiolase domain-containing protein;


Pssm-ID: 181378 [Multi-domain]  Cd Length: 386  Bit Score: 149.88  E-value: 2.47e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H         5 REVYIAGVGETKF--GKHTVDFDVLGREAALQAMNGSNIDRPDmIQSAYVGNgMNDMttgqavFRGLGMcgPNL------ 76
Cdd:PRK08313   3 RLAAVLGTGQTKYvaKRQDVSMAGLVREAIDRALADAGLTWDD-IDAVVVGK-APDF------FEGVMM--PELfladal 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H        77 -----PIINVQSACSAGAMAVFCAIKDVATGVTDLSIGVGTENHTmhrQSGAAFSAARSDIETMH-GAVMTGKYAMRATR 150
Cdd:PRK08313  73 gatgkPLIRVHTAGSVGGSTAVVAASLVQSGVYRRVLAVAWEKQS---ESNAMWALSIPVPFTKPvGAGAGGYFAPHVRA 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H       151 YMHETGATIEDLAMITVKNRKHATHNPYAWFKGA-ITVEEVVNSRMVAYPMTLQQCCGIADGAAAVVVGSKEMMKKLGIA 229
Cdd:PRK08313 150 YIRRSGAPEHIGAMVAVKDRLNGAKNPYAHLHQPdITLEKVMASQMLWDPIRFDETCPSSDGACAVVIGDEEAADAAAGR 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H       230 KPVKVAGVVVESGPYHNRPRDITGDDITETTSEKLYEESGIGP--KEVNILELHDAFTIAELLYYECMGLCKKGDGLKFL 307
Cdd:PRK08313 230 PVAWIHGTAMRTEPLAFAGRDQVNPQAGRDAAAALWKAAGITDprDEIDVAEIYVPFSWFEPMWLENLGFAPEGEGWKLT 309
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
7PXP_H       308 RDGQSTYGGQCVVSPRGGLLSyGHPIGASGAAQIAQNVKQLRGECGGYQVgPTPKVAMSHVTGGG 372
Cdd:PRK08313 310 EAGETAIGGRLPVNPSGGVLS-SNPIGASGMIRFAEAALQVMGKAGEHQV-DGARKALGHAYGGG 372
PTZ00455 PTZ00455
3-ketoacyl-CoA thiolase; Provisional
43-371 2.55e-39

3-ketoacyl-CoA thiolase; Provisional


Pssm-ID: 240424 [Multi-domain]  Cd Length: 438  Bit Score: 145.42  E-value: 2.55e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H        43 RPDMIQSAYVGNGMNDMTTGQ-----AVFRGLGMCGPNLPIIN-----VQSACSAGAMAVFCAIKDVATGVTDLSIGVGT 112
Cdd:PTZ00455  68 KAALVDKVVVGNFLGELFSSQghlgpAAVGSLGQSGASNALLYkpamrVEGACASGGLAVQSAWEALLAGTSDIALVVGV 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H       113 E-NHTMHRQSGAAFSAARSDIE---TMHGAVMTGKYAMRaTRYMHETGA-TIEDLAMITVKNRKHATHNPYA-WFKGAIT 186
Cdd:PTZ00455 148 EvQTTVSARVGGDYLARAADYRrqrKLDDFTFPCLFAKR-MKYIQEHGHfTMEDTARVAAKAYANGNKNPLAhMHTRKLS 226
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H       187 VEEVV-----NSRMVAYP-----MTLQQCCGIADGAAAVVVGSKEMMKKLGI----AKPVKVAGVVVESGPYHNRPRDIT 252
Cdd:PTZ00455 227 LEFCTgasdkNPKFLGNEtykpfLRMTDCSQVSDGGAGLVLASEEGLQKMGLspndSRLVEIKSLACASGNLYEDPPDAT 306
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H       253 GDDITETTSEKLYEESGIGPKEVNILELHDAFTIAELLYYECMGLCKKGDGLKFLRDGQSTYGGQCVVSPRGGLLSYGHP 332
Cdd:PTZ00455 307 RMFTSRAAAQKALSMAGVKPSDLQVAEVHDCFTIAELLMYEALGIAEYGHAKDLIRNGATALEGRIPVNTGGGLLSFGHP 386
                        330       340       350
                 ....*....|....*....|....*....|....*....
7PXP_H       333 IGASGAAQIAQNVKQLRGECGGYQVGPTPKVAMSHVTGG 371
Cdd:PTZ00455 387 VGATGVKQIMEVYRQMKGQCGEYQMKNIPALGATLNMGG 425
PRK06065 PRK06065
thiolase domain-containing protein;
1-357 1.29e-36

thiolase domain-containing protein;


Pssm-ID: 180379 [Multi-domain]  Cd Length: 392  Bit Score: 137.26  E-value: 1.29e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H         1 MKLQREVYIAGVGETKFGKHTVDF-DVLGREAALQAMN--GSNIDRPDMI-----QSAYVGNGMNdmttGQAVFRGLGmc 72
Cdd:PRK06065   5 IHLNKRVAVIGAGLTLFRRRLLETpQELAWEAASKALDeaGLELKDIDCVvigsaPDAFDGVHMK----GEYLSHGSG-- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H        73 GPNLPIINVQSACSAGAMAVFCAIKDVATGVTDLSIGVGTEN-HTMHRQSGAAFSAARSDI-ETMHGAVMTGKYAMRATR 150
Cdd:PRK06065  79 GIRKPVSRVYVGGATGVMTAIAGWYHVASGLCQKVLAVAEEKmSPARPHPQAVFRYIWDPIlEKPLNPNLIWIFAMEMHR 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H       151 YMHETGATIEDLAMITVKNRKHATHNPYAWFKGAITVEEVVNSRMVAYPMTLQQCCGIADGAAAVVVGSKEMMKKLgIAK 230
Cdd:PRK06065 159 YMATYGIKKEEIALVSVKNKRNALNNPYAQLGSKITVEDVLKSEVLVWPVQLLDVSPVSDGAAAIVLASEDLARRY-TDT 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H       231 PVKVAGVVVESGPYHNRPRDITGDDITETTSEKLYEESGI-GP-KEVNILELHDAFTIAELLYYECMGLCKKGDGLKFLR 308
Cdd:PRK06065 238 PVWVEGVGWTLDNTEWPNRDLAYPRYVEFAARMAYKMAGIeRPrKEIDVAEPYDPFDYKELHHLEGLQLAKRGEAPKLLK 317
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
7PXP_H       309 DGQSTYGGQCVVSPRGGLLSYGHPIGASGAAQIAQNVKQLRGECGGYQV 357
Cdd:PRK06065 318 EGVFDIDGDIPSSPSGGLLGVGNPIAAAGLMKVISIYWQLKGTAGKMQV 366
PRK06066 PRK06066
thiolase domain-containing protein;
95-366 1.64e-32

thiolase domain-containing protein;


Pssm-ID: 180380 [Multi-domain]  Cd Length: 385  Bit Score: 126.02  E-value: 1.64e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H        95 AIKDVATGVTDLSIGVGteNHTMHRQSGAAFSAA------RSDIETMHGAVmtgKYAM-------------------RAT 149
Cdd:PRK06066  77 AMRPTMTVAGDGLQGLA--HAVMHINSGLANVVVveahskPSDILTFSDVV---KFAMdpiyvrpigppnphfiaglDAV 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H       150 RYMHETGATIEDLAMITVKNRKHATHNPYAWFKGAITVEEVVNSRMVAYPMTLQQCCGIADGAAAVVVGSKEMMKKLgIA 229
Cdd:PRK06066 152 KFMSRKGITREDLALVVEKNKKAGLSNPRASYASNISLEDVLSSEYVVYPLTELDIAPFVDGAIVVVLASEEVAKKL-TD 230
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H       230 KPVKVAGV--VVESGPYHNrpRDITGDDITETTSEKLYEESGIGP--KEVNILELHDAFTIAELLYYECMGLCKKGDGLK 305
Cdd:PRK06066 231 DPVWIKGIgwSTESSNLET--AELGKANYMRIAADMAYKMAGIESprKEVDAAEVDDRYSYKELQHIEALRLSEEPEKDS 308
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
7PXP_H       306 FLRDGQSTYGGQCVVSPRGGLLSYGHPIGASGAAQIAQNVKQLRGECGGYQVGPTPKVAMS 366
Cdd:PRK06066 309 LLREGNFDPQGELPVNPSGGHLAKGVPLEASGLSLLLDAVEYLRGEAGARQGKAERAVVAS 369
PRK06289 PRK06289
acetyl-CoA acetyltransferase; Provisional
7-370 4.86e-31

acetyl-CoA acetyltransferase; Provisional


Pssm-ID: 235771 [Multi-domain]  Cd Length: 403  Bit Score: 122.10  E-value: 4.86e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H         7 VYIAGVGETKFG----KHTVDFDVLGREAALQAMNGSNIDrPDMIQSAYVGNGMNDMTTGQAVFRG-LGMCGPNL---PI 78
Cdd:PRK06289   5 VWVLGGYQSDFArnwtKEGRDFADLTREVVDGTLAAAGVD-ADDIEVVHVGNFFGELFAGQGHLGAmPATVHPALwgvPA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H        79 INVQSACSAGAMAVFCAIKDVATGVTDLSIGVGTE-NHTMHRQSGAAF--SAARSDIETMHGAVMTGK-YAMRATRYMHE 154
Cdd:PRK06289  84 SRHEAACASGSVATLAAMADLRAGRYDVALVVGVElMKTVPGDVAAEHlgAAAWTGHEGQDARFPWPSmFARVADEYDRR 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H       155 TGATIEDLAMITVKNRKHATHNPYA----WF--KGAITVEEVVNSrMVAYPMTLQQCCGIADGAAAVVVGSKEMMKKLGI 228
Cdd:PRK06289 164 YGLDEEHLRAIAEINFANARRNPNAqtrgWAfpDEATNDDDATNP-VVEGRLRRQDCSQVTDGGAGVVLASDAYLRDYAD 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H       229 AKPV-KVAGVVVESGP--YHNRPRDITGDDI----TETTSEKLYEESGIGPKEVNILELHDAFTIAELLYYECMGLCKKG 301
Cdd:PRK06289 243 ARPIpRIKGWGHRTAPlgLEQKLDRSAGDPYvlphVRQAVLDAYRRAGVGLDDLDGFEVHDCFTPSEYLAIDHIGLTGPG 322
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
7PXP_H       302 DGLKFLRDGQSTYGGQCVVSPRGGLLSYGHPIGASGAAQIAQNVKQLRGECGGYQVGPTPKVAMSHVTG 370
Cdd:PRK06289 323 ESWKAIENGEIAIGGRLPINPSGGLIGGGHPVGASGVRMLLDAAKQVTGTAGDYQVEGAKTFGTLNIGG 391
thiolase cd00751
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ...
8-374 2.50e-13

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: 70.59  E-value: 2.50e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H        8 YIAGVGETKFGK-----HTVDFDVLGREAALQAMNGSNIDrPDMIQSAYVGNGMNdMTTGQAVFR----GLGMcGPNLPI 78
Cdd:cd00751   1 VIVSAVRTPIGRfggalKDVSADDLGAAVIKALLERAGLD-PEEVDDVIMGNVLQ-AGEGQNPARqaalLAGL-PESVPA 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H       79 INVQSACSAGAMAVFCAIKDVATGVTDLSIGVGTENhtMhrqSGAAFSAARSDIETMHGAV----MTGKYAMRATRYMHE 154
Cdd:cd00751  78 TTVNRVCGSGLQAVALAAQSIAAGEADVVVAGGVES--M---SRAPYLLPKARRGGRLGLNtldgMLDDGLTDPFTGLSM 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H      155 tGATIEDLAM---ITvknRK------HATHNPYA------WFKG---AITVEEVVNSRMVAY-----PMT----LQQC-- 205
Cdd:cd00751 153 -GITAENVAEkygIS---REeqdefaLRSHQRAAaaqeagRFKDeivPVEVPGRKGPVVVDRdegprPDTtlekLAKLkp 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H      206 -------------CGIADGAAAVVVGSKEMMKKLGIakpvKVAGVVVESGpyhnrprdITGDDITETT------SEKLYE 266
Cdd:cd00751 229 afkkdgtvtagnaSGINDGAAAVLLMSEEKAKELGL----KPLARIVGYA--------VAGVDPAIMGigpvpaIPKALK 296
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H      267 ESGIGPKEVNILELHDAFTIAELLYYECMGLckkgDGLKflrdgqstyggqcvVSPRGGLLSYGHPIGASGAAQIAQNVK 346
Cdd:cd00751 297 RAGLTLDDIDLIEINEAFAAQALACLKELGL----DPEK--------------VNVNGGAIALGHPLGASGARIVVTLLH 358
                       410       420
                ....*....|....*....|....*...
7PXP_H      347 QLRGECGGYQVgptpkVAMSHVTGGGLS 374
Cdd:cd00751 359 ELKRRGGRYGL-----ATMCIGGGQGAA 381
cond_enzymes cd00327
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ...
206-382 7.84e-12

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: 64.77  E-value: 7.84e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H      206 CGIADGAAAVVVGSKEMMKKLGIakpvKVAGVVVESgpyhnrprDITGDDITETT----------SEKLYEESGIGPKEV 275
Cdd:cd00327  98 FVFGDGAAAAVVESEEHALRRGA----HPQAEIVST--------AATFDGASMVPavsgeglaraARKALEGAGLTPSDI 165
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H      276 NILELHDAFTIAELLYYECMGLCKKGDGlkflrdgqstyggqcVVSPRGGLLSYGHPIGASGAAQIAQNVKQLRGECG-G 354
Cdd:cd00327 166 DYVEAHGTGTPIGDAVELALGLDPDGVR---------------SPAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIpP 230
                       170       180
                ....*....|....*....|....*...
7PXP_H      355 YQVGPTPKVAMSHvtggGLSGTEHAACT 382
Cdd:cd00327 231 TPREPRTVLLLGF----GLGGTNAAVVL 254
PRK07937 PRK07937
lipid-transfer protein; Provisional
157-371 2.95e-11

lipid-transfer protein; Provisional


Pssm-ID: 181173 [Multi-domain]  Cd Length: 352  Bit Score: 64.33  E-value: 2.95e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H       157 ATIEDLAMITVKNRKHATHNPYAwfKGAITVEEVVNSRMVAYPMTLQQCCGIADGAAAVVVGSKEMMKKLgIAKPVKVAG 236
Cdd:PRK07937 155 WTEEQMAEVAARSRADARRNPSA--EPSISVDELLARPYFADPLRRHDIAPITDGAAAVVLAAGDRAREL-RERPAWITG 231
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H       237 VVVESGPYHNRPRDITGDDITETTSEKLyeeSGIGPKEVNILELHDAFTIAELLYYECMGLckkgdglkflrdgqstyGG 316
Cdd:PRK07937 232 IEHRIESPSLGARDLTRSPSTALAAEAA---TGGDAGGVDVAELHAPFTHQELILREALGL-----------------GD 291
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
7PXP_H       317 QCVVSPRGGLLSyGHPIGASGAAQIAQNVKQ-LRGECGGyqvgptpkvAMSHVTGG 371
Cdd:PRK07937 292 KTKVNPSGGALA-ANPMFAAGLERIGEAARHiWDGSARR---------ALAHATSG 337
Thiolase_N pfam00108
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
7-221 7.72e-11

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: 61.93  E-value: 7.72e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H          7 VYIAGVGETKFGKHTVDF-DV----LGREAALQAMNGSNIDrPDMIQSAYVGNgMNDMTTGQAVFR----GLGMCGPnLP 77
Cdd:pfam00108   1 VVIVSAARTPFGSFGGSLkDVsaveLGAEAIKAALERAGVD-PEDVDEVIVGN-VLQAGEGQNPARqaalKAGIPDS-AP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H         78 IINVQSACSAGAMAVFCAIKDVATGVTDLSIGVGTEN--HTMHRQSGAAFSAARSDIETMHG-------AVMTGKYAMRA 148
Cdd:pfam00108  78 AVTINKVCGSGLKAVYLAAQSIASGDADVVLAGGVESmsHAPYALPTDARSGLKHGDEKKHDllipdglTDAFNGYHMGL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H        149 T--RYMHETGATIEDLAMITVKNRKHATHNPYA-------------WFKGAITV--EEVVNSRMVAYPM----------- 200
Cdd:pfam00108 158 TaeNVAKKYGISREEQDAFAVKSHQKAAAAPKAgkfkdeivpvtvkGRKGKPTVdkDEGIRPPTTAEPLaklkpafdkeg 237
                         250       260
                  ....*....|....*....|...
7PXP_H        201 --TLQQCCGIADGAAAVVVGSKE 221
Cdd:pfam00108 238 tvTAGNASPINDGAAAVLLMSES 260
AcCoA-C-Actrans TIGR01930
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ...
205-372 1.81e-09

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: 58.78  E-value: 1.81e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H        205 CCGIADGAAAVVVGSKEMMKKLG---IAKPV--KVAGVVVE---SGPYHnrprditgdditetTSEKLYEESGIGPKEVN 276
Cdd:TIGR01930 241 SSPLNDGAAALLLMSEEKAKELGltpLARIVsfAVAGVDPEimgLGPVP--------------AIPKALKKAGLSISDID 306
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H        277 ILELHDAFTIAELLYYECMGLckkgDGLKflrdgqstyggqcvVSPRGGLLSYGHPIGASGAAQIAQNVKQLRGECGGYQ 356
Cdd:TIGR01930 307 LFEINEAFAAQVLACIKELGL----DLEK--------------VNVNGGAIALGHPLGASGARIVTTLLHELKRRGGRYG 368
                         170
                  ....*....|....*.
7PXP_H        357 VgptpkVAMSHVTGGG 372
Cdd:TIGR01930 369 L-----ATMCIGGGQG 379
PRK06445 PRK06445
acetyl-CoA C-acetyltransferase;
74-357 1.37e-08

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180563 [Multi-domain]  Cd Length: 394  Bit Score: 56.27  E-value: 1.37e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H        74 PNLPIINVQSACSAGAMAVFCAIKDVATGVTDLSIGVGTENHTM-------HRQSGAAFsaaRSDIETMHGAVMTGkYAM 146
Cdd:PRK06445  84 YNIPAMAVDRQCASSLTTVSIGAMEIATGMADIVIAGGVEHMTRtpmgdnpHIEPNPKL---LTDPKYIEYDLTTG-YVM 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H       147 --RATRYMHETGATIEDLAMITVKNRKHATHN-PYAWFKGAI---TVE-----EVVNSRMVAYPMT-LQQCCGIA----- 209
Cdd:PRK06445 160 glTAEKLAEEAGIKREEMDRWSLRSHQLAAKAiQEGYFKDEIlpiEVEvegkkKVVDVDQSVRPDTsLEKLAKLPpafkp 239
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H       210 -------------DGAAAVVVGSKEMMKKLG---IAKPVKV--AGVvvesgpyhnrPRDITGDDITeTTSEKLYEESGIG 271
Cdd:PRK06445 240 dgvitagnssplnSGASYVLLMSKKAVKKYGlkpMAKIRSFgfAGV----------PPAIMGKGPV-PASKKALEKAGLS 308
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H       272 PKEVNILELHDAFTIAELLYYECMGLCKKgdglkflrdgqstyggqcVVSPRGGLLSYGHPIGASGAAQIAQNVKQLRGE 351
Cdd:PRK06445 309 VKDIDLWEINEAFAVVVLYAIKELGLDPE------------------TVNIKGGAIAIGHPLGATGARIVGTLARQLQIK 370

                 ....*.
7PXP_H       352 CGGYQV 357
Cdd:PRK06445 371 GKDYGV 376
PRK08131 PRK08131
3-oxoadipyl-CoA thiolase;
207-357 2.99e-08

3-oxoadipyl-CoA thiolase;


Pssm-ID: 181242 [Multi-domain]  Cd Length: 401  Bit Score: 55.17  E-value: 2.99e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H       207 GIADGAAAVVVGSKEMMKKLGIAKPVKV---AGVVVEsgpyhnrPRdITGDDITETTSEKLyEESGIGPKEVNILELHDA 283
Cdd:PRK08131 254 GINDGAAALLIGSRAAGEKYGLKPMARIlssAAAGVE-------PR-IMGIGPVEAIKKAL-ARAGLTLDDMDIIEINEA 324
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
7PXP_H       284 FTIAELLyyecmglCKKGDGLKFlRDGQstyggqcvVSPRGGLLSYGHPIGASGAAQIAQNVKQLRGECGGYQV 357
Cdd:PRK08131 325 FASQVLG-------CLKGLGVDF-DDPR--------VNPNGGAIAVGHPLGASGARLALTAARELQRRGKRYAV 382
PRK06366 PRK06366
acetyl-CoA C-acetyltransferase;
5-349 3.89e-08

acetyl-CoA C-acetyltransferase;


Pssm-ID: 102340 [Multi-domain]  Cd Length: 388  Bit Score: 54.63  E-value: 3.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H         5 REVYIAGVGETKFGKHTVDFDV-----LGREAALQAMNGSNIDrPDMIQSAYVGN----GMNDMTTGQAVFRGLGMCGPN 75
Cdd:PRK06366   2 KDVYIVSAKRTAIGKFGRSFSKikapqLGGAAIKAVIDDAKLD-PALVQEVIMGNviqaGVGQNPAGQAAYHAGLPFGVT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H        76 LPIINVqsACSAGAMAVFCAIKDVATGVTDLSIGVGTEN-----------------HTMHR------------------- 119
Cdd:PRK06366  81 KYTVNV--VCASGMLAVESAAREIMLGERDLVIAGGMENmsnapfllpsdlrwgpkHLLHKnykiddamlvdglidafyf 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H       120 --------QSGAAFSAARSDIETMhgAVMTGKYAMRATR-------------YMHETG---ATIEDLAMItvknrkhath 175
Cdd:PRK06366 159 ehmgvsaeRTARKYGITREMADEY--SVQSYERAIRATEsgefrneivpfndLDRDEGirkTTMEDLAKL---------- 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H       176 nPYAWFKGAItveevvnsrmvaypMTLQQCCGIADGAAAVVVGSKEMMKKLGIAKPVKVAGVvvESGPYHnrPRDITGDD 255
Cdd:PRK06366 227 -PPAFDKNGI--------------LTAGNSAQLSDGGSALVMASEKAINEYGLKPIARITGY--ESASLD--PLDFVEAP 287
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H       256 ITETtsEKLYEESGIGPKEVNILELHDAFTIAELLYYECMglckKGDGLKFlrdgqstyggqcvvSPRGGLLSYGHPIGA 335
Cdd:PRK06366 288 IPAT--RKLLEKQNKSIDYYDLVEHNEAFSIASIIVRDQL----KIDNERF--------------NVNGGAVAIGHPIGN 347
                        410
                 ....*....|....
7PXP_H       336 SGAAQIAQNVKQLR 349
Cdd:PRK06366 348 SGSRIIVTLINALK 361
PRK06690 PRK06690
acetyl-CoA C-acyltransferase;
206-357 9.60e-08

acetyl-CoA C-acyltransferase;


Pssm-ID: 180659 [Multi-domain]  Cd Length: 361  Bit Score: 53.62  E-value: 9.60e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H       206 CGIADGAAAVVVGSKEMMKKLGIAKPVKVAGVVVeSGPYHNRPRDITGDDItettsEKLYEESGIGPKEVNILELHDAFT 285
Cdd:PRK06690 215 CGVNDGACAVLVMEEGQARKLGYKPVLRFVRSAV-VGVDPNLPGTGPIFAV-----NKLLNEMNMKVEDIDYFEINEAFA 288
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
7PXP_H       286 IAellyyecMGLCKKGDGLKFLRdgqstyggqcvVSPRGGLLSYGHPIGASGAAQIAQNVKQLRGECGGYQV 357
Cdd:PRK06690 289 SK-------VVACAKELQIPYEK-----------LNVNGGAIALGHPYGASGAMLVTRLFYQAKREDMKYGI 342
PaaJ COG0183
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ...
206-355 2.21e-07

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: 52.38  E-value: 2.21e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H      206 CGIADGAAAVVVGSKEMMKKLGIakpvKVAGVVVESGpyhnrprdITGDDITETT------SEKLYEESGIGPKEVNILE 279
Cdd:COG0183 246 SGINDGAAALLLMSEEAAKELGL----KPLARIVAYA--------VAGVDPEIMGigpvpaTRKALARAGLTLDDIDLIE 313
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
7PXP_H      280 LHDAF---TIAellyyeCMglckkgDGLKFLRDgqstyggqcVVSPRGGLLSYGHPIGASGAAQIAQNVKQLRGECGGY 355
Cdd:COG0183 314 INEAFaaqVLA------VL------RELGLDPD---------KVNVNGGAIALGHPLGASGARILVTLLHELERRGGRY 371
PRK08235 PRK08235
acetyl-CoA C-acetyltransferase;
207-357 1.53e-06

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181311 [Multi-domain]  Cd Length: 393  Bit Score: 49.71  E-value: 1.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H       207 GIADGAAAVVVGSKEMMKKLGIAKPVKVAG---VVVESGPYHNRPrditGDDITEttsekLYEESGIGPKEVNILELHDA 283
Cdd:PRK08235 249 GVNDGAAALVLMSEDRAKQEGRKPLATILAhtaIAVEAKDFPRTP----GYAINA-----LLEKTGKTVEDIDLFEINEA 319
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
7PXP_H       284 FTIAELLYYECMGLckkgDGLKflrdgqstyggqcvVSPRGGLLSYGHPIGASGAAQIAQNVKQLRGECGGYQV 357
Cdd:PRK08235 320 FAAVALASTEIAGI----DPEK--------------VNVNGGAVALGHPIGASGARIIVTLIHELKRRGGGIGI 375
PRK06954 PRK06954
acetyl-CoA C-acetyltransferase;
208-372 3.23e-05

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180775 [Multi-domain]  Cd Length: 397  Bit Score: 45.65  E-value: 3.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H       208 IADGAAAVVVGSKEMMKKLGIAKPVKVAGvvveSGPYHNRPRDITGDDITETtsEKLYEESGIGPKEVNILELHDAFTIA 287
Cdd:PRK06954 254 ISDGAAALVMMRASTAKRLGLAPLARVVG----HSTFAQAPSKFTTAPVGAI--RKLFEKNGWRAAEVDLFEINEAFAVV 327
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H       288 EllyyecMGLCKKgdgLKFLRDGQSTYGGQCVVsprggllsyGHPIGASGAAQIAQNVKQLRGECGGYQVGptpkvamSH 367
Cdd:PRK06954 328 T------MAAMKE---HGLPHEKVNVNGGACAL---------GHPIGASGARILVTLIGALRARGGKRGVA-------SL 382

                 ....*
7PXP_H       368 VTGGG 372
Cdd:PRK06954 383 CIGGG 387
PRK06025 PRK06025
acetyl-CoA C-acetyltransferase;
207-348 3.59e-05

acetyl-CoA C-acetyltransferase;


Pssm-ID: 235675 [Multi-domain]  Cd Length: 417  Bit Score: 45.54  E-value: 3.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H       207 GIADGAAAVVVGSKEMMKKLGI---AKPVKVAGVvvesgpyhnrprditGDDIT------ETTSEKLYEESGIGPKEVNI 277
Cdd:PRK06025 273 GVVDGAAALLLASKAYAEKHGLkprARIVAMANM---------------GDDPTlmlnapVPAAKKVLAKAGLTKDDIDL 337
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
7PXP_H       278 LELHDAFTI-AEllyyecmglckkgdglKFLRDGQSTYGGqcvVSPRGGLLSYGHPIGASGAAQIAQNVKQL 348
Cdd:PRK06025 338 WEINEAFAVvAE----------------KFIRDLDLDRDK---VNVNGGAIALGHPIGATGSILIGTVLDEL 390
PLN02644 PLN02644
acetyl-CoA C-acetyltransferase
208-358 4.94e-05

acetyl-CoA C-acetyltransferase


Pssm-ID: 215347 [Multi-domain]  Cd Length: 394  Bit Score: 45.08  E-value: 4.94e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H       208 IADGAAAVVVGSKEMMKKLGIAKPVKVAGVVvesgpyhnrprDITGDDITETTSEKL-----YEESGIGPKEVNILELHD 282
Cdd:PLN02644 250 ISDGAAALVLVSGEKALELGLQVIAKIRGYA-----------DAAQAPELFTTAPALaipkaLKHAGLEASQVDYYEINE 318
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
7PXP_H       283 AFTIAELLYYECMGLckkgDGLKflrdgqstyggqcvVSPRGGLLSYGHPIGASGAAQIAQNVKQLRGECGGYQVG 358
Cdd:PLN02644 319 AFSVVALANQKLLGL----DPEK--------------VNVHGGAVSLGHPIGCSGARILVTLLGVLRSKNGKYGVA 376
PRK08257 PRK08257
acetyl-CoA acetyltransferase; Validated
173-230 5.50e-05

acetyl-CoA acetyltransferase; Validated


Pssm-ID: 236204 [Multi-domain]  Cd Length: 498  Bit Score: 44.90  E-value: 5.50e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
7PXP_H       173 ATHNPYAWFKGAITVEEVV----NSRMVAYPMTLQQCCGIA-DGAAAVVVGSKEMMKKLGIAK 230
Cdd:PRK08257 202 AAKNPHAWIPRERSAEEIVtptpDNRMIAWPYTKLMNANDMvDQGAAVLLTSVAKARRLGVPE 264
Thiolase_C pfam02803
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
261-372 2.15e-04

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: 40.70  E-value: 2.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H        261 SEKLYEESGIGPKEVNILELHDAFTIAELLYYECMGLckkgDGLKflrdgqstyggqcvVSPRGGLLSYGHPIGASGAAQ 340
Cdd:pfam02803  28 IPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGI----DPEK--------------VNVNGGAIALGHPLGASGARI 89
                          90       100       110
                  ....*....|....*....|....*....|..
7PXP_H        341 IAQNVKQLRGECGGYQVgptpkVAMSHVTGGG 372
Cdd:pfam02803  90 LVTLLHELKRRGGKYGL-----ASLCIGGGQG 116
PRK05790 PRK05790
putative acyltransferase; Provisional
207-338 6.97e-04

putative acyltransferase; Provisional


Pssm-ID: 180261 [Multi-domain]  Cd Length: 393  Bit Score: 41.29  E-value: 6.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PXP_H       207 GIADGAAAVVVGSKEMMKKLG---IAKPVK--VAGV---VVESGPYHnrprditgdditetTSEKLYEESGIGPKEVNIL 278
Cdd:PRK05790 249 GINDGAAAVVVMSEAKAKELGltpLARIVSyaVAGVdpaIMGIGPVP--------------AIRKALEKAGWSLADLDLI 314
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
7PXP_H       279 ELHDAF---TIAellyyecmglCKKGDGLKFLRdgqstyggqcvVSPRGGLLSYGHPIGASGA 338
Cdd:PRK05790 315 EINEAFaaqALA----------VEKELGLDPEK-----------VNVNGGAIALGHPIGASGA 356
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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