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Conserved domains on  [gi|522136349|ref|WP_020647558|]
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thiolase family protein [Amycolatopsis balhimycina]

Protein Classification

thiolase family protein( domain architecture ID 11415132)

thiolase family protein such as 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|GO:0016747
SCOP:  4000245

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PaaJ COG0183
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ...
1-397 0e+00

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: 544.28  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349   1 MTDAVIVDAVRTPIGKgkPNGTLSGVHPVDLHAHALRSLVERTGIDPGRIDDVISGAVGQVGeQSMNTARWAALAAGLPE 80
Cdd:COG0183    1 MREVVIVDAVRTPFGR--FGGALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQAG-QGQNPARQAALLAGLPE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349  81 SVPAVTVDRQCGSSQQAVHFAAQGVIAGAYDVVIASGVESMSRVPMGSQAA--GRDPFGPQVAARYPDGL------VPQG 152
Cdd:COG0183   78 SVPAVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMLLPKArwGYRMNAKLVDPMINPGLtdpytgLSMG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 153 ISAELIAAKWGLTRAQLDEFSAESHQRAAKAWAGGKFAAEVVPLKAPGPDGTlREVTTDETVRPGTTPEILAGLKPAFRA 232
Cdd:COG0183  158 ETAENVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVEVPDRKGE-VVVDRDEGPRPDTTLEKLAKLKPAFKK 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 233 DvweqrfpelGwHVTAGNSSPINDGAAAVLITSSETAAALGLKPRARIHSFAVAGDDPLYMLTGVVPATRKVLARAGLEV 312
Cdd:COG0183  237 D---------G-TVTAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIGPVPATRKALARAGLTL 306
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 313 SDIDAFEVNEAFASVVLAWQAEIGADLAKVNVNGGAIALGHPLGGSGARLLTTLLSVLEQTGGRYGLHTMCEAGGLANAT 392
Cdd:COG0183  307 DDIDLIEINEAFAAQVLAVLRELGLDPDKVNVNGGAIALGHPLGASGARILVTLLHELERRGGRYGLATMCIGGGQGIAL 386

                 ....*
gi 522136349 393 IIERL 397
Cdd:COG0183  387 IIERV 391
 
Name Accession Description Interval E-value
PaaJ COG0183
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ...
1-397 0e+00

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: 544.28  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349   1 MTDAVIVDAVRTPIGKgkPNGTLSGVHPVDLHAHALRSLVERTGIDPGRIDDVISGAVGQVGeQSMNTARWAALAAGLPE 80
Cdd:COG0183    1 MREVVIVDAVRTPFGR--FGGALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQAG-QGQNPARQAALLAGLPE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349  81 SVPAVTVDRQCGSSQQAVHFAAQGVIAGAYDVVIASGVESMSRVPMGSQAA--GRDPFGPQVAARYPDGL------VPQG 152
Cdd:COG0183   78 SVPAVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMLLPKArwGYRMNAKLVDPMINPGLtdpytgLSMG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 153 ISAELIAAKWGLTRAQLDEFSAESHQRAAKAWAGGKFAAEVVPLKAPGPDGTlREVTTDETVRPGTTPEILAGLKPAFRA 232
Cdd:COG0183  158 ETAENVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVEVPDRKGE-VVVDRDEGPRPDTTLEKLAKLKPAFKK 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 233 DvweqrfpelGwHVTAGNSSPINDGAAAVLITSSETAAALGLKPRARIHSFAVAGDDPLYMLTGVVPATRKVLARAGLEV 312
Cdd:COG0183  237 D---------G-TVTAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIGPVPATRKALARAGLTL 306
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 313 SDIDAFEVNEAFASVVLAWQAEIGADLAKVNVNGGAIALGHPLGGSGARLLTTLLSVLEQTGGRYGLHTMCEAGGLANAT 392
Cdd:COG0183  307 DDIDLIEINEAFAAQVLAVLRELGLDPDKVNVNGGAIALGHPLGASGARILVTLLHELERRGGRYGLATMCIGGGQGIAL 386

                 ....*
gi 522136349 393 IIERL 397
Cdd:COG0183  387 IIERV 391
thiolase cd00751
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ...
5-396 0e+00

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: 534.75  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349   5 VIVDAVRTPIGKGkpNGTLSGVHPVDLHAHALRSLVERTGIDPGRIDDVISGAVGQVGEqSMNTARWAALAAGLPESVPA 84
Cdd:cd00751    1 VIVSAVRTPIGRF--GGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGE-GQNPARQAALLAGLPESVPA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349  85 VTVDRQCGSSQQAVHFAAQGVIAGAYDVVIASGVESMSRVPMGSQAAGRDPFGPQV--------AARYPDGLVPQGISAE 156
Cdd:cd00751   78 TTVNRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGRLGLNtldgmlddGLTDPFTGLSMGITAE 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 157 LIAAKWGLTRAQLDEFSAESHQRAAKAWAGGKFAAEVVPLKAPGPDGTLrEVTTDETVRPGTTPEILAGLKPAFRADvwe 236
Cdd:cd00751  158 NVAEKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEVPGRKGPV-VVDRDEGPRPDTTLEKLAKLKPAFKKD--- 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 237 qrfpelgWHVTAGNSSPINDGAAAVLITSSETAAALGLKPRARIHSFAVAGDDPLYMLTGVVPATRKVLARAGLEVSDID 316
Cdd:cd00751  234 -------GTVTAGNASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDID 306
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 317 AFEVNEAFASVVLAWQAEIGADLAKVNVNGGAIALGHPLGGSGARLLTTLLSVLEQTGGRYGLHTMCEAGGLANATIIER 396
Cdd:cd00751  307 LIEINEAFAAQALACLKELGLDPEKVNVNGGAIALGHPLGASGARIVVTLLHELKRRGGRYGLATMCIGGGQGAAMVIER 386
PRK07801 PRK07801
acetyl-CoA C-acetyltransferase;
1-397 6.75e-176

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181123 [Multi-domain]  Cd Length: 382  Bit Score: 495.00  E-value: 6.75e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349   1 MTDAVIVDAVRTPIGKGKpnGTLSGVHPVDLHAHALRSLVERTGIDPGRIDDVISGAVGQVGEQSMNTARWAALAAGLPE 80
Cdd:PRK07801   1 MAEAYIVDAVRTPVGKRK--GGLAGVHPADLGAHVLKGLVDRTGIDPAAVDDVIFGCVDTIGPQAGNIARTSWLAAGLPE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349  81 SVPAVTVDRQCGSSQQAVHFAAQGVIAGAYDVVIASGVESMSRVPMGSQAAGRDPFG--------PQVAARYPDGLVPQG 152
Cdd:PRK07801  79 EVPGVTVDRQCGSSQQAIHFAAQAVMSGTQDLVVAGGVQNMSQIPISSAMTAGEQLGftspfaesKGWLHRYGDQEVSQF 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 153 ISAELIAAKWGLTRAQLDEFSAESHQRAAKAWAGGKFAAEVVPLKApgpdgtlreVTTDETVRPgTTPEILAGLKPAFRa 232
Cdd:PRK07801 159 RGAELIAEKWGISREEMERFALESHRRAFAAIRAGRFDNEIVPVGG---------VTVDEGPRE-TSLEKMAGLKPLVE- 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 233 dvweqrfpelGWHVTAGNSSPINDGAAAVLITSSETAAALGLKPRARIHSFAVAGDDPLYMLTGVVPATRKVLARAGLEV 312
Cdd:PRK07801 228 ----------GGRLTAAVASQISDGASAVLLASERAVKRHGLTPRARIHHLSVRGDDPVFMLTAPIPATRYALEKTGLSI 297
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 313 SDIDAFEVNEAFASVVLAWQAEIGADLAKVNVNGGAIALGHPLGGSGARLLTTLLSVLEQTGGRYGLHTMCEAGGLANAT 392
Cdd:PRK07801 298 DDIDVVEINEAFAPVVLAWLKETGADPAKVNPNGGAIALGHPLGATGAKLMTTLLHELERTGGRYGLQTMCEGGGTANVT 377

                 ....*
gi 522136349 393 IIERL 397
Cdd:PRK07801 378 IIERL 382
AcCoA-C-Actrans TIGR01930
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ...
6-395 6.92e-172

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: 485.19  E-value: 6.92e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349    6 IVDAVRTPIGKgkPNGTLSGVHPVDLHAHALRSLVERTGIDPGRIDDVISGAVGQVGEQsMNTARWAALAAGLPESVPAV 85
Cdd:TIGR01930   1 IVAAARTPIGK--FGGSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLQAGEQ-QNIARQAALLAGLPESVPAY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349   86 TVDRQCGSSQQAVHFAAQGVIAGAYDVVIASGVESMSRVPMGSQAAGRDPFGPQVAARY---------PDGLVPQGISAE 156
Cdd:TIGR01930  78 TVNRQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGVPRSLRWGVKPGNAELEdarlkdltdANTGLPMGVTAE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349  157 LIAAKWGLTRAQLDEFSAESHQRAAKAWAGGKFAAEVVPLKAPGPDGTLrEVTTDETVRPGTTPEILAGLKPAFRADvwe 236
Cdd:TIGR01930 158 NLAKKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVTVKGRKGPV-TVSSDEGIRPNTTLEKLAKLKPAFDPD--- 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349  237 qrfpelgWHVTAGNSSPINDGAAAVLITSSETAAALGLKPRARIHSFAVAGDDPLYMLTGVVPATRKVLARAGLEVSDID 316
Cdd:TIGR01930 234 -------GTVTAGNSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALKKAGLSISDID 306
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 522136349  317 AFEVNEAFASVVLAWQAEIGADLAKVNVNGGAIALGHPLGGSGARLLTTLLSVLEQTGGRYGLHTMCEAGGLANATIIE 395
Cdd:TIGR01930 307 LFEINEAFAAQVLACIKELGLDLEKVNVNGGAIALGHPLGASGARIVTTLLHELKRRGGRYGLATMCIGGGQGAAVILE 385
Thiolase_N pfam00108
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
5-267 7.51e-77

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: 238.36  E-value: 7.51e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349    5 VIVDAVRTPIGKGKpnGTLSGVHPVDLHAHALRSLVERTGIDPGRIDDVISGAVGQVGEQSmNTARWAALAAGLPESVPA 84
Cdd:pfam00108   2 VIVSAARTPFGSFG--GSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQAGEGQ-NPARQAALKAGIPDSAPA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349   85 VTVDRQCGSSQQAVHFAAQGVIAGAYDVVIASGVESMSRVPMGSQAAGRDPFGPQVAARY----PDGL------VPQGIS 154
Cdd:pfam00108  79 VTINKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALPTDARSGLKHGDEKKHdlliPDGLtdafngYHMGLT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349  155 AELIAAKWGLTRAQLDEFSAESHQRAAKAWAGGKFAAEVVPLKAPGPDGTLrEVTTDETVRPGTTPEILAGLKPAFRADv 234
Cdd:pfam00108 159 AENVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDEIVPVTVKGRKGKP-TVDKDEGIRPPTTAEPLAKLKPAFDKE- 236
                         250       260       270
                  ....*....|....*....|....*....|...
gi 522136349  235 weqrfpelgWHVTAGNSSPINDGAAAVLITSSE 267
Cdd:pfam00108 237 ---------GTVTAGNASPINDGAAAVLLMSES 260
 
Name Accession Description Interval E-value
PaaJ COG0183
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ...
1-397 0e+00

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: 544.28  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349   1 MTDAVIVDAVRTPIGKgkPNGTLSGVHPVDLHAHALRSLVERTGIDPGRIDDVISGAVGQVGeQSMNTARWAALAAGLPE 80
Cdd:COG0183    1 MREVVIVDAVRTPFGR--FGGALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQAG-QGQNPARQAALLAGLPE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349  81 SVPAVTVDRQCGSSQQAVHFAAQGVIAGAYDVVIASGVESMSRVPMGSQAA--GRDPFGPQVAARYPDGL------VPQG 152
Cdd:COG0183   78 SVPAVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMLLPKArwGYRMNAKLVDPMINPGLtdpytgLSMG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 153 ISAELIAAKWGLTRAQLDEFSAESHQRAAKAWAGGKFAAEVVPLKAPGPDGTlREVTTDETVRPGTTPEILAGLKPAFRA 232
Cdd:COG0183  158 ETAENVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVEVPDRKGE-VVVDRDEGPRPDTTLEKLAKLKPAFKK 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 233 DvweqrfpelGwHVTAGNSSPINDGAAAVLITSSETAAALGLKPRARIHSFAVAGDDPLYMLTGVVPATRKVLARAGLEV 312
Cdd:COG0183  237 D---------G-TVTAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIGPVPATRKALARAGLTL 306
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 313 SDIDAFEVNEAFASVVLAWQAEIGADLAKVNVNGGAIALGHPLGGSGARLLTTLLSVLEQTGGRYGLHTMCEAGGLANAT 392
Cdd:COG0183  307 DDIDLIEINEAFAAQVLAVLRELGLDPDKVNVNGGAIALGHPLGASGARILVTLLHELERRGGRYGLATMCIGGGQGIAL 386

                 ....*
gi 522136349 393 IIERL 397
Cdd:COG0183  387 IIERV 391
thiolase cd00751
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ...
5-396 0e+00

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: 534.75  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349   5 VIVDAVRTPIGKGkpNGTLSGVHPVDLHAHALRSLVERTGIDPGRIDDVISGAVGQVGEqSMNTARWAALAAGLPESVPA 84
Cdd:cd00751    1 VIVSAVRTPIGRF--GGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGE-GQNPARQAALLAGLPESVPA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349  85 VTVDRQCGSSQQAVHFAAQGVIAGAYDVVIASGVESMSRVPMGSQAAGRDPFGPQV--------AARYPDGLVPQGISAE 156
Cdd:cd00751   78 TTVNRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGRLGLNtldgmlddGLTDPFTGLSMGITAE 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 157 LIAAKWGLTRAQLDEFSAESHQRAAKAWAGGKFAAEVVPLKAPGPDGTLrEVTTDETVRPGTTPEILAGLKPAFRADvwe 236
Cdd:cd00751  158 NVAEKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEVPGRKGPV-VVDRDEGPRPDTTLEKLAKLKPAFKKD--- 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 237 qrfpelgWHVTAGNSSPINDGAAAVLITSSETAAALGLKPRARIHSFAVAGDDPLYMLTGVVPATRKVLARAGLEVSDID 316
Cdd:cd00751  234 -------GTVTAGNASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDID 306
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 317 AFEVNEAFASVVLAWQAEIGADLAKVNVNGGAIALGHPLGGSGARLLTTLLSVLEQTGGRYGLHTMCEAGGLANATIIER 396
Cdd:cd00751  307 LIEINEAFAAQALACLKELGLDPEKVNVNGGAIALGHPLGASGARIVVTLLHELKRRGGRYGLATMCIGGGQGAAMVIER 386
PRK07801 PRK07801
acetyl-CoA C-acetyltransferase;
1-397 6.75e-176

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181123 [Multi-domain]  Cd Length: 382  Bit Score: 495.00  E-value: 6.75e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349   1 MTDAVIVDAVRTPIGKGKpnGTLSGVHPVDLHAHALRSLVERTGIDPGRIDDVISGAVGQVGEQSMNTARWAALAAGLPE 80
Cdd:PRK07801   1 MAEAYIVDAVRTPVGKRK--GGLAGVHPADLGAHVLKGLVDRTGIDPAAVDDVIFGCVDTIGPQAGNIARTSWLAAGLPE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349  81 SVPAVTVDRQCGSSQQAVHFAAQGVIAGAYDVVIASGVESMSRVPMGSQAAGRDPFG--------PQVAARYPDGLVPQG 152
Cdd:PRK07801  79 EVPGVTVDRQCGSSQQAIHFAAQAVMSGTQDLVVAGGVQNMSQIPISSAMTAGEQLGftspfaesKGWLHRYGDQEVSQF 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 153 ISAELIAAKWGLTRAQLDEFSAESHQRAAKAWAGGKFAAEVVPLKApgpdgtlreVTTDETVRPgTTPEILAGLKPAFRa 232
Cdd:PRK07801 159 RGAELIAEKWGISREEMERFALESHRRAFAAIRAGRFDNEIVPVGG---------VTVDEGPRE-TSLEKMAGLKPLVE- 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 233 dvweqrfpelGWHVTAGNSSPINDGAAAVLITSSETAAALGLKPRARIHSFAVAGDDPLYMLTGVVPATRKVLARAGLEV 312
Cdd:PRK07801 228 ----------GGRLTAAVASQISDGASAVLLASERAVKRHGLTPRARIHHLSVRGDDPVFMLTAPIPATRYALEKTGLSI 297
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 313 SDIDAFEVNEAFASVVLAWQAEIGADLAKVNVNGGAIALGHPLGGSGARLLTTLLSVLEQTGGRYGLHTMCEAGGLANAT 392
Cdd:PRK07801 298 DDIDVVEINEAFAPVVLAWLKETGADPAKVNPNGGAIALGHPLGATGAKLMTTLLHELERTGGRYGLQTMCEGGGTANVT 377

                 ....*
gi 522136349 393 IIERL 397
Cdd:PRK07801 378 IIERL 382
AcCoA-C-Actrans TIGR01930
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ...
6-395 6.92e-172

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: 485.19  E-value: 6.92e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349    6 IVDAVRTPIGKgkPNGTLSGVHPVDLHAHALRSLVERTGIDPGRIDDVISGAVGQVGEQsMNTARWAALAAGLPESVPAV 85
Cdd:TIGR01930   1 IVAAARTPIGK--FGGSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLQAGEQ-QNIARQAALLAGLPESVPAY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349   86 TVDRQCGSSQQAVHFAAQGVIAGAYDVVIASGVESMSRVPMGSQAAGRDPFGPQVAARY---------PDGLVPQGISAE 156
Cdd:TIGR01930  78 TVNRQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGVPRSLRWGVKPGNAELEdarlkdltdANTGLPMGVTAE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349  157 LIAAKWGLTRAQLDEFSAESHQRAAKAWAGGKFAAEVVPLKAPGPDGTLrEVTTDETVRPGTTPEILAGLKPAFRADvwe 236
Cdd:TIGR01930 158 NLAKKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVTVKGRKGPV-TVSSDEGIRPNTTLEKLAKLKPAFDPD--- 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349  237 qrfpelgWHVTAGNSSPINDGAAAVLITSSETAAALGLKPRARIHSFAVAGDDPLYMLTGVVPATRKVLARAGLEVSDID 316
Cdd:TIGR01930 234 -------GTVTAGNSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALKKAGLSISDID 306
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 522136349  317 AFEVNEAFASVVLAWQAEIGADLAKVNVNGGAIALGHPLGGSGARLLTTLLSVLEQTGGRYGLHTMCEAGGLANATIIE 395
Cdd:TIGR01930 307 LFEINEAFAAQVLACIKELGLDLEKVNVNGGAIALGHPLGASGARIVTTLLHELKRRGGRYGLATMCIGGGQGAAVILE 385
PRK08242 PRK08242
acetyl-CoA C-acetyltransferase;
1-397 4.81e-167

acetyl-CoA C-acetyltransferase;


Pssm-ID: 236197 [Multi-domain]  Cd Length: 402  Bit Score: 473.60  E-value: 4.81e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349   1 MTDAVIVDAVRTPIGKGKPNGTLSGVHPVDLHAHALRSLVERTGIDPGRIDDVISGAVGQVGEQSMNTARWAALAAGLPE 80
Cdd:PRK08242   1 MTEAYIYDAVRTPRGKGKKDGSLHEVKPVRLAAGLLEALRDRNGLDTAAVDDVVLGCVTPVGDQGADIARTAVLAAGLPE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349  81 SVPAVTVDRQCGSSQQAVHFAAQGVIAGAYDVVIASGVESMSRVPMGSQAaGRDPFGPQVAarYPDGLVPQGISAELIAA 160
Cdd:PRK08242  81 TVPGVQINRFCASGLEAVNLAAAKVRSGWDDLVIAGGVESMSRVPMGSDG-GAWAMDPSTN--FPTYFVPQGISADLIAT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 161 KWGLTRAQLDEFSAESHQRAAKAWAGGKFAAEVVPLKapGPDGtLREVTTDETVRPGTTPEILAGLKPAFRA-------- 232
Cdd:PRK08242 158 KYGFSREDVDAYAVESQQRAAAAWAEGYFAKSVVPVK--DQNG-LTILDHDEHMRPGTTMESLAKLKPSFAMmgemggfd 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 233 DVWEQRFPELGW--HV-TAGNSSPINDGAAAVLITSSETAAALGLKPRARIHSFAVAGDDPLYMLTGVVPATRKVLARAG 309
Cdd:PRK08242 235 AVALQKYPEVERinHVhHAGNSSGIVDGAAAVLIGSEEAGKALGLKPRARIVATATIGSDPTIMLTGPVPATRKALAKAG 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 310 LEVSDIDAFEVNEAFASVVLAWQAEIGADLAKVNVNGGAIALGHPLGGSGARLLTTLLSVLEQTGGRYGLHTMCEAGGLA 389
Cdd:PRK08242 315 LTVDDIDLFELNEAFASVVLRFMQALDIPHDKVNVNGGAIAMGHPLGATGAMILGTVLDELERRGKRTALITLCVGGGMG 394

                 ....*...
gi 522136349 390 NATIIERL 397
Cdd:PRK08242 395 IATIIERV 402
PRK06504 PRK06504
acetyl-CoA C-acetyltransferase;
1-397 3.21e-166

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180595 [Multi-domain]  Cd Length: 390  Bit Score: 471.14  E-value: 3.21e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349   1 MTDAVIVDAVRTpiGKGKPNGTLSGVHPVDLHAHALRSLVERTGIDPGRIDDVISGAVGQVGEQSMNTARWAALAAGLPE 80
Cdd:PRK06504   1 MAEAYIVAAART--AGGRKGGRLAGWHPADLAAQVLDALVDRSGADPALIEDVIMGCVSQVGEQATNVARNAVLASKLPE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349  81 SVPAVTVDRQCGSSQQAVHFAAQGVIAGAYDVVIASGVESMSRVPMGSQAAG--RDPFG----PQVAARYPDGLVPQGIS 154
Cdd:PRK06504  79 SVPGTSIDRQCGSSQQALHFAAQAVMSGTMDIVIAAGVESMTRVPMGSPSTLpaKNGLGhyksPGMEERYPGIQFSQFTG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 155 AELIAAKWGLTRAQLDEFSAESHQRAAKAWAGGKFAAEVVPLKAPGPDGTLREVTTDETVRPGTTPEILAGLKPAFRadv 234
Cdd:PRK06504 159 AEMMAKKYGLSKDQLDEFALQSHQRAIAATQAGKFKAEIVPLEITRADGSGEMHTVDEGIRFDATLEGIAGVKLIAE--- 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 235 weqrfpelGWHVTAGNSSPINDGAAAVLITSSETAAALGLKPRARIHSFAVAGDDPLYMLTGVVPATRKVLARAGLEVSD 314
Cdd:PRK06504 236 --------GGRLTAATASQICDGASGVMVVNERGLKALGVKPLARIHHMTVIGGDPVIMLEAPLPATERALKKAGMKIDD 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 315 IDAFEVNEAFASVVLAWQAEIGADLAKVNVNGGAIALGHPLGGSGARLLTTLLSVLEQTGGRYGLHTMCEAGGLANATII 394
Cdd:PRK06504 308 IDLYEVNEAFASVPLAWLKATGADPERLNVNGGAIALGHPLGASGTKLMTTLVHALKQRGKRYGLQTMCEGGGMANVTIV 387

                 ...
gi 522136349 395 ERL 397
Cdd:PRK06504 388 ERL 390
PRK07850 PRK07850
steroid 3-ketoacyl-CoA thiolase;
1-397 4.06e-149

steroid 3-ketoacyl-CoA thiolase;


Pssm-ID: 181145 [Multi-domain]  Cd Length: 387  Bit Score: 427.60  E-value: 4.06e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349   1 MTDAVIVDAVRTPIGKgkPNGTLSGVHPVDLHAHALRSLVERTGIDPGRIDDVISGAVGQVGEQSMNTARWAALAAGLPE 80
Cdd:PRK07850   1 MGNPVIVEAVRTPIGK--RNGWLSGLHAAELLGAVQRAVLDRAGIDPGDVEQVIGGCVTQAGEQSNNITRTAWLHAGLPY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349  81 SVPAVTVDRQCGSSQQAVHFAAQGVIAGAYDVVIASGVESMSRVPMGsQAAGRDPfGPQVAARYPDGLVPQGISAELIAA 160
Cdd:PRK07850  79 HVGATTIDCQCGSAQQANHLVAGLIAAGAIDVGIACGVEAMSRVPLG-ANAGPGR-GLPRPDSWDIDMPNQFEAAERIAK 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 161 KWGLTRAQLDEFSAESHQRAAKAWAGGKFAAEVVPLKAP------GPDGTLREVTTDETVRPgTTPEILAGLKPAFradv 234
Cdd:PRK07850 157 RRGITREDVDAFGLRSQRRAAQAWAEGRFDREISPVQAPvldeegQPTGETRLVTRDQGLRD-TTMEGLAGLKPVL---- 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 235 weqrfpELGWHvTAGNSSPINDGAAAVLITSSETAAALGLKPRARIHSFAVAGDDPLYMLTGVVPATRKVLARAGLEVSD 314
Cdd:PRK07850 232 ------EGGIH-TAGTSSQISDGAAAVLWMDEDRARALGLRPRARIVAQALVGAEPYYHLDGPVQATAKVLEKAGMKIGD 304
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 315 IDAFEVNEAFASVVLAWQAEIGADLAKVNVNGGAIALGHPLGGSGARLLTTLLSVLEQTGGRYGLHTMCEAGGLANATII 394
Cdd:PRK07850 305 IDLVEINEAFASVVLSWAQVHEPDMDKVNVNGGAIALGHPVGSTGARLITTALHELERTDKSTALITMCAGGALSTGTII 384

                 ...
gi 522136349 395 ERL 397
Cdd:PRK07850 385 ERI 387
PRK05790 PRK05790
putative acyltransferase; Provisional
1-397 2.64e-148

putative acyltransferase; Provisional


Pssm-ID: 180261 [Multi-domain]  Cd Length: 393  Bit Score: 425.34  E-value: 2.64e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349   1 MTDAVIVDAVRTPIGKGkpNGTLSGVHPVDLHAHALRSLVERTGIDPGRIDDVISGAVGQVGeQSMNTARWAALAAGLPE 80
Cdd:PRK05790   1 MKDVVIVSAARTPIGKF--GGALKDVSAVELGAIVIKAALERAGVPPEQVDEVIMGQVLQAG-AGQNPARQAALKAGLPV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349  81 SVPAVTVDRQCGSSQQAVHFAAQGVIAGAYDVVIASGVESMSRVP---MGSQAAGRDPFGPQVAARYPDGL------VPQ 151
Cdd:PRK05790  78 EVPALTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQESMSQAPhvlPGSRWGQKMGDVELVDTMIHDGLtdafngYHM 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 152 GISAELIAAKWGLTRAQLDEFSAESHQRAAKAWAGGKFAAEVVPLKAPGPDGTLREVTTDETVRPGTTPEILAGLKPAFR 231
Cdd:PRK05790 158 GITAENLAEQYGITREEQDEFALASQQKAEAAIKAGRFKDEIVPVTIKQRKGDPVVVDTDEHPRPDTTAESLAKLRPAFD 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 232 ADvweqrfpelGwHVTAGNSSPINDGAAAVLITSSETAAALGLKPRARIHSFAVAGDDPLYMLTGVVPATRKVLARAGLE 311
Cdd:PRK05790 238 KD---------G-TVTAGNASGINDGAAAVVVMSEAKAKELGLTPLARIVSYAVAGVDPAIMGIGPVPAIRKALEKAGWS 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 312 VSDIDAFEVNEAFASVVLAWQAEIGADLAKVNVNGGAIALGHPLGGSGARLLTTLLSVLEQTGGRYGLHTMCEAGGLANA 391
Cdd:PRK05790 308 LADLDLIEINEAFAAQALAVEKELGLDPEKVNVNGGAIALGHPIGASGARILVTLLHEMKRRGAKKGLATLCIGGGQGVA 387

                 ....*.
gi 522136349 392 TIIERL 397
Cdd:PRK05790 388 LIVERP 393
fadA PRK08947
3-ketoacyl-CoA thiolase; Reviewed
1-397 1.39e-136

3-ketoacyl-CoA thiolase; Reviewed


Pssm-ID: 181592 [Multi-domain]  Cd Length: 387  Bit Score: 395.49  E-value: 1.39e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349   1 MTDAVIVDAVRTPIGKGKpNGTLSGVHPVDLHAHALRSLVERT-GIDPGRIDDVISGAVGQVGEQSMNTARWAALAAGLP 79
Cdd:PRK08947   1 MEDVVIVDAIRTPMGRSK-GGAFRNVRAEDLSAHLMRSLLARNpALDPAEIDDIIWGCVQQTLEQGFNIARNAALLAGIP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349  80 ESVPAVTVDRQCGSSQQAVHFAAQGVIAGAYDVVIASGVESMSRVPMGSqaaGRDpFGPQVAARYPDGLVPQGISAELIA 159
Cdd:PRK08947  80 HSVPAVTVNRLCGSSMQALHDAARAIMTGDGDVFLIGGVEHMGHVPMNH---GVD-FHPGLSKNVAKAAGMMGLTAEMLG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 160 AKWGLTRAQLDEFSAESHQRAAKAWAGGKFAAEVVPLKAPGPDGTLREVTTDETVRPGTTPEILAGLKPAFRadvweqrf 239
Cdd:PRK08947 156 KMHGISREQQDAFAARSHQRAWAATQEGRFKNEIIPTEGHDADGVLKLFDYDEVIRPETTVEALAALRPAFD-------- 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 240 PELGwHVTAGNSSPINDGAAAVLITSSETAAALGLKPRARIHSFAVAGDDPLYMLTGVVPATRKVLARAGLEVSDIDAFE 319
Cdd:PRK08947 228 PVNG-TVTAGTSSALSDGASAMLVMSESRAKELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISDIDVFE 306
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 320 VNEAFASVVLAWQAEIG-ADLA--KVNVNGGAIALGHPLGGSGARLLTTLLSVLEQTGGRYGLHTMCEAGGLANATIIER 396
Cdd:PRK08947 307 LNEAFAAQSLPCLKDLGlLDKMdeKVNLNGGAIALGHPLGCSGARISTTLLNLMERKDAQFGLATMCIGLGQGIATVFER 386

                 .
gi 522136349 397 L 397
Cdd:PRK08947 387 V 387
PRK06205 PRK06205
acetyl-CoA C-acetyltransferase;
1-398 1.79e-124

acetyl-CoA C-acetyltransferase;


Pssm-ID: 235741 [Multi-domain]  Cd Length: 404  Bit Score: 365.46  E-value: 1.79e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349   1 MTDAVIVDAVRTPIGKGkpNGTLSGVHPVDLHAHALRSLVERTGIDPGRIDDVISGAVGQVGEqSMNTARWAALAAGLPE 80
Cdd:PRK06205   1 MRDAVICEPVRTPVGRF--GGAFKDVPAEELAATVIRALVERTGIDPARIDDVIFGQGYPNGE-APAIGRVAALDAGLPV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349  81 SVPAVTVDRQCGSSQQAVHFAAQGVIAGAYDVVIASGVESMSRVP-----------MGSQ------AAGRDPFGPqvaAR 143
Cdd:PRK06205  78 TVPGMQLDRRCGSGLQAVITAAMQVQTGAADVVIAGGAESMSNVEfyttdmrwgvrGGGVqlhdrlARGRETAGG---RR 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 144 YPdglVPQGI--SAELIAAKWGLTRAQLDEFSAESHQRAAKAWAGGKFAAEVVPLKAPGPDGTLREVTTDETVRPGTTPE 221
Cdd:PRK06205 155 FP---VPGGMieTAENLRREYGISREEQDALAVRSHQRAVAAQEAGRFDDEIVPVTVPQRKGDPTVVDRDEHPRADTTLE 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 222 ILAGLKPafradVWEQRFPELGwhVTAGNSSPINDGAAAVLITSSETAAALGLKPRARIHSFAVAGDDPLYMLTGVVPAT 301
Cdd:PRK06205 232 SLAKLRP-----IMGKQDPEAT--VTAGNASGQNDAAAACLVTTEDKAEELGLRPLARLVSWAVAGVEPSRMGIGPVPAT 304
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 302 RKVLARAGLEVSDIDAFEVNEAFASVVLAWQAEIG---ADLAKVNVNGGAIALGHPLGGSGARLLTTLLSVLEQTGGRYG 378
Cdd:PRK06205 305 EKALARAGLTLDDIDLIELNEAFAAQVLAVLKEWGfgaDDEERLNVNGSGISLGHPVGATGGRILATLLRELQRRQARYG 384
                        410       420
                 ....*....|....*....|
gi 522136349 379 LHTMCEAGGLANATIIERLA 398
Cdd:PRK06205 385 LETMCIGGGQGLAAVFERVN 404
PRK09050 PRK09050
beta-ketoadipyl CoA thiolase; Validated
1-397 1.48e-121

beta-ketoadipyl CoA thiolase; Validated


Pssm-ID: 181624 [Multi-domain]  Cd Length: 401  Bit Score: 357.73  E-value: 1.48e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349   1 MTDAVIVDAVRTPIGKGkpNGTLSGVHPVDLHAHALRSLVERT-GIDPGRIDDVISGAVGQVGEQSMNTARWAALAAGLP 79
Cdd:PRK09050   1 MTEAFICDAIRTPIGRY--GGALSSVRADDLGAVPLKALMARNpGVDWEAVDDVIYGCANQAGEDNRNVARMSALLAGLP 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349  80 ESVPAVTVDRQCGSSQQAVHFAAQGVIAGAYDVVIASGVESMSRVP--MG--SQAAGRDP-----------FGPQVAARY 144
Cdd:PRK09050  79 VSVPGTTINRLCGSGMDAVGTAARAIKAGEAELMIAGGVESMSRAPfvMGkaDSAFSRQAeifdttigwrfVNPLMKAQY 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 145 PDGLVPQgiSAELIAAKWGLTRAQLDEFSAESHQRAAKAWAGGKFAAEVVPLKAPGPDGTLREVTTDETVRPGTTPEILA 224
Cdd:PRK09050 159 GVDSMPE--TAENVAEDYNISRADQDAFALRSQQRAAAAQAAGFLAEEIVPVTIPQKKGDPVVVDRDEHPRPETTLEALA 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 225 GLKPAFRAdvweqrfpelGWHVTAGNSSPINDGAAAVLITSSETAAALGLKPRARIHSFAVAGDDPLYMLTGVVPATRKV 304
Cdd:PRK09050 237 KLKPVFRP----------DGTVTAGNASGVNDGAAALLLASEAAAKKHGLTPRARILGMATAGVEPRIMGIGPAPATRKL 306
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 305 LARAGLEVSDIDAFEVNEAFASVVLAWQAEIGA--DLAKVNVNGGAIALGHPLGGSGARLLTTLLSVLEQTGGRYGLHTM 382
Cdd:PRK09050 307 LARLGLTIDQFDVIELNEAFAAQGLAVLRQLGLadDDARVNPNGGAIALGHPLGMSGARLVLTALHQLERTGGRYALCTM 386
                        410
                 ....*....|....*
gi 522136349 383 CEAGGLANATIIERL 397
Cdd:PRK09050 387 CIGVGQGIALAIERV 401
PRK09051 PRK09051
beta-ketothiolase BktB;
1-397 1.33e-119

beta-ketothiolase BktB;


Pssm-ID: 181625 [Multi-domain]  Cd Length: 394  Bit Score: 352.72  E-value: 1.33e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349   1 MTDAVIVDAVRTPIGKGkpNGTLSGVHPVDLHAHALRSLVERTGIDPGRIDDVISGAVGQVGEQSMNTARWAALAAGLPE 80
Cdd:PRK09051   2 MREVVVVSGVRTAIGTF--GGSLKDVAPTDLGATVVREALARAGVDPDQVGHVVFGHVIPTEPRDMYLSRVAAINAGVPQ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349  81 SVPAVTVDRQCGSSQQAVHFAAQGVIAGAYDVVIASGVESMSRVP-----------MGSQ-------AAGRDPFGpqvaa 142
Cdd:PRK09051  80 ETPAFNVNRLCGSGLQAIVSAAQAILLGDADVAIGGGAESMSRAPyllpaarwgarMGDAklvdmmvGALHDPFG----- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 143 rypdgLVPQGISAELIAAKWGLTRAQLDEFSAESHQRAAKAWAGGKFAAEVVPLKAPGPDGTLrEVTTDETVRPGTTPEI 222
Cdd:PRK09051 155 -----TIHMGVTAENVAAKYGISREAQDALALESHRRAAAAIAAGYFKDQIVPVEIKTRKGEV-VFDTDEHVRADTTLED 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 223 LAGLKPAFRADvweqrfpelGWHVTAGNSSPINDGAAAVLITSSETAAALGLKPRARIHSFAVAGDDPLYMLTGVVPATR 302
Cdd:PRK09051 229 LAKLKPVFKKE---------NGTVTAGNASGINDGAAAVVLAEADAAEARGLKPLARLVGYAHAGVDPEYMGIGPVPATQ 299
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 303 KVLARAGLEVSDIDAFEVNEAFASVVLAWQAEIGADLAKVNVNGGAIALGHPLGGSGARLLTTLLSVLEQTGGRYGLHTM 382
Cdd:PRK09051 300 KALERAGLTVADLDVIEANEAFAAQACAVTRELGLDPAKVNPNGSGISLGHPVGATGAIITVKALYELQRIGGRYALVTM 379
                        410
                 ....*....|....*
gi 522136349 383 CEAGGLANATIIERL 397
Cdd:PRK09051 380 CIGGGQGIAAIFERL 394
PRK06445 PRK06445
acetyl-CoA C-acetyltransferase;
1-396 6.82e-119

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180563 [Multi-domain]  Cd Length: 394  Bit Score: 350.95  E-value: 6.82e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349   1 MTDAVIVDAVRTPIGKGKPN----GTLSGVHPVDLHAHALRSLVERTGIDPGRIDDVISGAVGQVGEQSMNTARWAALAA 76
Cdd:PRK06445   1 LEDVYLVDFARTAFSRFRPKdpqkDVFNNIRPEELAAMLINRLIEKTGIKPEEIDDIITGCALQVGENWLYGGRHPIFLA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349  77 GLPESVPAVTVDRQCGSSQQAVHFAAQGVIAGAYDVVIASGVESMSRVPMGSqaagrDPF-GPQVA-------ARY--PD 146
Cdd:PRK06445  81 RLPYNIPAMAVDRQCASSLTTVSIGAMEIATGMADIVIAGGVEHMTRTPMGD-----NPHiEPNPKlltdpkyIEYdlTT 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 147 GLVpQGISAELIAAKWGLTRAQLDEFSAESHQRAAKAWAGGKFAAEVVPLKAPGpDGTLREVTTDETVRPGTTPEILAGL 226
Cdd:PRK06445 156 GYV-MGLTAEKLAEEAGIKREEMDRWSLRSHQLAAKAIQEGYFKDEILPIEVEV-EGKKKVVDVDQSVRPDTSLEKLAKL 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 227 KPAFRADvweqrfpelgWHVTAGNSSPINDGAAAVLITSSETAAALGLKPRARIHSFAVAGDDPLYMLTGVVPATRKVLA 306
Cdd:PRK06445 234 PPAFKPD----------GVITAGNSSPLNSGASYVLLMSKKAVKKYGLKPMAKIRSFGFAGVPPAIMGKGPVPASKKALE 303
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 307 RAGLEVSDIDAFEVNEAFASVVLAWQAEIGADLAKVNVNGGAIALGHPLGGSGARLLTTLLSVLEQTGGRYGLHTMCEAG 386
Cdd:PRK06445 304 KAGLSVKDIDLWEINEAFAVVVLYAIKELGLDPETVNIKGGAIAIGHPLGATGARIVGTLARQLQIKGKDYGVATLCVGG 383
                        410
                 ....*....|
gi 522136349 387 GLANATIIER 396
Cdd:PRK06445 384 GQGGAVVLER 393
PRK06025 PRK06025
acetyl-CoA C-acetyltransferase;
1-397 9.37e-119

acetyl-CoA C-acetyltransferase;


Pssm-ID: 235675 [Multi-domain]  Cd Length: 417  Bit Score: 351.39  E-value: 9.37e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349   1 MTDAVIVDAVRTPIGKGKP-NGTLSGVHPVDLHAHALRSLVERTGIDPGRIDDVISGAVGQVGEQSMNTARWAALAAGLP 79
Cdd:PRK06025   1 MAEAYIIDAVRTPRGIGKVgKGALAHLHPQHLAATVLKALAERNGLNTADVDDIIWSTSSQRGKQGGDLGRMAALDAGYD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349  80 ESVPAVTVDRQCGSSQQAVHFAAQGVIAGAYDVVIASGVESMSRVPMGSQ---AAGRDPFG-----PQVAARYPDGlvPQ 151
Cdd:PRK06025  81 IKASGVTLDRFCGGGITSVNLAAAQIMSGMEDLVIAGGTEMMSYTAAMAAedmAAGKPPLGmgsgnLRLRALHPQS--HQ 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 152 GISAELIAAKWGLTRAQLDEFSAESHQRAAKAWAGGKFAAEVVPLKapGPDGTLrEVTTDETVRPGTTPEILAGLKPAFR 231
Cdd:PRK06025 159 GVCGDAIATMEGITREALDALGLESQRRAARAIKEGRFDKSLVPVY--RDDGSV-ALDHEEFPRPQTTAEGLAALKPAFT 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 232 A--------------DVWEQRFPELGW-HVT-AGNSSPINDGAAAVLITSSETAAALGLKPRARIHSFAVAGDDPLYMLT 295
Cdd:PRK06025 236 AiadyplddkgttyrGLINQKYPDLEIkHVHhAGNSSGVVDGAAALLLASKAYAEKHGLKPRARIVAMANMGDDPTLMLN 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 296 GVVPATRKVLARAGLEVSDIDAFEVNEAFASVVLAWQAEIGADLAKVNVNGGAIALGHPLGGSGARLLTTLLSVLEQTGG 375
Cdd:PRK06025 316 APVPAAKKVLAKAGLTKDDIDLWEINEAFAVVAEKFIRDLDLDRDKVNVNGGAIALGHPIGATGSILIGTVLDELERRGL 395
                        410       420
                 ....*....|....*....|..
gi 522136349 376 RYGLHTMCEAGGLANATIIERL 397
Cdd:PRK06025 396 KRGLVTMCAAGGMAPAIIIERV 417
PRK07661 PRK07661
acetyl-CoA C-acetyltransferase;
1-397 3.04e-116

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181072 [Multi-domain]  Cd Length: 391  Bit Score: 344.04  E-value: 3.04e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349   1 MTDAVIVDAVRTPIGKGKpNGTLSGVHPVDLHAHALRSLVERTGIDPGRIDDVISGAVGQVGEQSMNTARWAALAAGLPE 80
Cdd:PRK07661   1 MREAVIVAGARTPVGKAK-KGSLKTVRPDDLGALVVKETLKRAGNYEGPIDDLIIGCAMPEAEQGLNMARNIGALAGLPY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349  81 SVPAVTVDRQCGSSQQAVHFAAQGVIAGAYDVVIASGVESMSRVPMGSQAAGRDPfgpQVAARYPDGLVPQGISAELIAA 160
Cdd:PRK07661  80 TVPAITINRYCSSGLQSIAYGAERIMLGHSEAVIAGGAESMSLVPMMGHVVRPNP---RLVEAAPEYYMGMGHTAEQVAV 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 161 KWGLTRAQLDEFSAESHQRAAKAWAGGKFAAEVVP----LKAPGPDGTLRE----VTTDETVRPGTTPEILAGLKPAFRA 232
Cdd:PRK07661 157 KYGISREDQDAFAVRSHQRAAKALAEGKFADEIVPvdvtLRTVGENNKLQEetitFSQDEGVRADTTLEILGKLRPAFNV 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 233 dvweqrfpelGWHVTAGNSSPINDGAAAVLITSSETAAALGLKPRARIHSFAVAGDDPLYMLTGVVPATRKVLARAGLEV 312
Cdd:PRK07661 237 ----------KGSVTAGNSSQMSDGAAAVLLMDREKAESDGLKPLAKFRSFAVAGVPPEVMGIGPIAAIPKALKLAGLEL 306
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 313 SDIDAFEVNEAFASVVLAWQAEIGADLAKVNVNGGAIALGHPLGGSGARLLTTLLSVLEQTGGRYGLHTMCEAGGLANAT 392
Cdd:PRK07661 307 SDIGLFELNEAFASQSIQVIRELGLDEEKVNVNGGAIALGHPLGCTGAKLTLSLIHEMKRRNEQFGIVTMCIGGGMGAAG 386

                 ....*
gi 522136349 393 IIERL 397
Cdd:PRK07661 387 VFELL 391
PRK09052 PRK09052
acetyl-CoA C-acyltransferase;
1-397 2.60e-115

acetyl-CoA C-acyltransferase;


Pssm-ID: 181626 [Multi-domain]  Cd Length: 399  Bit Score: 341.98  E-value: 2.60e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349   1 MTDAVIVDAVRTPIGKGkPNGTLSGVHPVDLHAHALRSLVERT-GIDPGRIDDVISGAVGQVGEQSMNTARWAALAAGLP 79
Cdd:PRK09052   5 LQDAYIVAATRTPVGKA-PRGMFKNTRPDDLLAHVLRSAVAQVpGLDPKLIEDAIVGCAMPEAEQGLNVARIGALLAGLP 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349  80 ESVPAVTVDRQCGSSQQAVHFAAQGVIAGAYDVVIASGVESMSRVPMGsqaaGRDP-FGPQVAARYPD-----GLvpqGI 153
Cdd:PRK09052  84 NSVGGVTVNRFCASGLQAVAMAADRIRVGEADVMIAAGVESMSMVPMM----GNKPsMSPAIFARDENvgiayGM---GL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 154 SAELIAAKWGLTRAQLDEFSAESHQRAAKAWAGGKFAAEVVPL----KAPGPDG-----TLREVTTDETVRPGTTPEILA 224
Cdd:PRK09052 157 TAEKVAEQWKVSREDQDAFALESHQKAIAAQQAGEFKDEITPYeiteRFPDLATgevdvKTRTVDLDEGPRADTSLEGLA 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 225 GLKPAFRAdvweqrfpelGWHVTAGNSSPINDGAAAVLITSSETAAALGLKPRARIHSFAVAGDDPLYMLTGVVPATRKV 304
Cdd:PRK09052 237 KLKPVFAN----------KGSVTAGNSSQTSDGAGAVILVSEKALKQFNLTPLARFVSFAVAGVPPEIMGIGPIEAIPAA 306
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 305 LARAGLEVSDIDAFEVNEAFASVVLAWQAEIGADLAKVNVNGGAIALGHPLGGSGARLLTTLLSVLEQTGGRYGLHTMCE 384
Cdd:PRK09052 307 LKQAGLKQDDLDWIELNEAFAAQSLAVIRDLGLDPSKVNPLGGAIALGHPLGATGAIRTATVVHGLRRTNLKYGMVTMCV 386
                        410
                 ....*....|...
gi 522136349 385 AGGLANATIIERL 397
Cdd:PRK09052 387 GTGMGAAGIFERL 399
fadA TIGR02445
fatty oxidation complex, beta subunit FadA; This subunit of the FadBA complex has acetyl-CoA ...
3-396 1.20e-113

fatty oxidation complex, beta subunit FadA; This subunit of the FadBA complex has acetyl-CoA C-acyltransferase (EC 2.3.1.16) activity, and is also known as beta-ketothiolase and fatty oxidation complex, beta subunit. This protein is almost always located adjacent to FadB (TIGR02437). The FadBA complex is the major complex active for beta-oxidation of fatty acids in E. coli. [Fatty acid and phospholipid metabolism, Degradation]


Pssm-ID: 131498  Cd Length: 385  Bit Score: 337.30  E-value: 1.20e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349    3 DAVIVDAVRTPIGKGKpNGTLSGVHPVDLHAHALRSLVER-TGIDPGRIDDVISGAVGQVGEQSMNTARWAALAAGLPES 81
Cdd:TIGR02445   1 DVVIVDFGRTPMGRSK-GGAFRNTRAEDLSAHLMSKLLARnPKVDPAEVEDIYWGCVQQTLEQGFNIARNAALLAQIPHT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349   82 VPAVTVDRQCGSSQQAVHFAAQGVIAGAYDVVIASGVESMSRVPMGSqaaGRDpFGPQVAARYPDGLVPQGISAELIAAK 161
Cdd:TIGR02445  80 SAAVTVNRLCGSSMQALHDAARAIMTGDADVCLVGGVEHMGHVPMMH---GVD-FHPGMSLHVAKAAGMMGLTAEMLGKM 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349  162 WGLTRAQLDEFSAESHQRAAKAWAGGKFAAEVVPLKAPGPDGTLREVTTDETVRPGTTPEILAGLKPAFRAdvweqrfpe 241
Cdd:TIGR02445 156 HGISREQQDAFAARSHARAHAATQEGKFKNEIIPTQGHDADGFLKQFDYDEVIRPETTVESLAALRPAFDP--------- 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349  242 LGWHVTAGNSSPINDGAAAVLITSSETAAALGLKPRARIHSFAVAGDDPLYMLTGVVPATRKVLARAGLEVSDIDAFEVN 321
Cdd:TIGR02445 227 KNGTVTAGTSSALSDGASAMLVMSEQRANELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISDIDVFELN 306
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 522136349  322 EAFASVVLAWQAEIGA-DL--AKVNVNGGAIALGHPLGGSGARLLTTLLSVLEQTGGRYGLHTMCEAGGLANATIIER 396
Cdd:TIGR02445 307 EAFAAQALPCLKDLGLlDKmdEKVNLNGGAIALGHPLGCSGARISTTLLNLMEQKDATFGLATMCIGLGQGIATVFER 384
pcaF TIGR02430
3-oxoadipyl-CoA thiolase; Members of this family are designated beta-ketoadipyl CoA thiolase, ...
2-397 7.07e-111

3-oxoadipyl-CoA thiolase; Members of this family are designated beta-ketoadipyl CoA thiolase, an enzyme that acts at the end of pathways for the degradation of protocatechuate (from benzoate and related compounds) and of phenylacetic acid.


Pssm-ID: 131483  Cd Length: 400  Bit Score: 330.59  E-value: 7.07e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349    2 TDAVIVDAVRTPIGKgkPNGTLSGVHPVDLHAHALRSLVERT-GIDPGRIDDVISGAVGQVGEQSMNTARWAALAAGLPE 80
Cdd:TIGR02430   1 REAYICDAIRTPIGR--YGGSLSSVRADDLAAVPIKALLARNpQLDWAAIDDVIYGCANQAGEDNRNVARMAALLAGLPV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349   81 SVPAVTVDRQCGSSQQAVHFAAQGVIAGAYDVVIASGVESMSRVP--MGSQAAgrdPFG----------------PQVAA 142
Cdd:TIGR02430  79 SVPGTTVNRLCGSGLDAIGMAARAIKAGEADLLIAGGVESMSRAPfvMGKADS---AFSrsakiedttigwrfinPLMKA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349  143 RYPDGLVPQgiSAELIAAKWGLTRAQLDEFSAESHQRAAKAWAGGKFAAEVVPLKAPGPDGTLREVTTDETVRPGTTPEI 222
Cdd:TIGR02430 156 LYGVDSMPE--TAENVAEEFGISREDQDAFALRSQQRTAAAQASGFFAEEIVPVVIPQKKGEPTVVDQDEHPRPETTLEG 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349  223 LAGLKPAFRADvweqrfpelgWHVTAGNSSPINDGAAAVLITSSETAAALGLKPRARIHSFAVAGDDPLYMLTGVVPATR 302
Cdd:TIGR02430 234 LAKLKPVVRPD----------GTVTAGNASGVNDGAAALLLASEEAVQRHGLTPRARILAAATAGVEPRIMGIGPVPATQ 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349  303 KVLARAGLEVSDIDAFEVNEAFASVVLAWQAEIGA--DLAKVNVNGGAIALGHPLGGSGARLLTTLLSVLEQTGGRYGLH 380
Cdd:TIGR02430 304 KLLARAGLSIDQFDVIELNEAFAAQALAVLRELGLadDDARVNPNGGAIALGHPLGASGARLVLTALRQLERSGGRYALC 383
                         410
                  ....*....|....*..
gi 522136349  381 TMCEAGGLANATIIERL 397
Cdd:TIGR02430 384 TMCIGVGQGIALAIERV 400
PLN02287 PLN02287
3-ketoacyl-CoA thiolase
3-396 8.96e-111

3-ketoacyl-CoA thiolase


Pssm-ID: 215161 [Multi-domain]  Cd Length: 452  Bit Score: 332.11  E-value: 8.96e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349   3 DAVIVDAVRTPIGKGKpNGTLSGVHPVDLHAHALRSLVERTGIDPGRIDDVISGAVGQVGEQSMNTARWAALAAGLPESV 82
Cdd:PLN02287  47 DVVIVAAYRTPICKAK-RGGFKDTYPDDLLAPVLKAVVEKTGLNPSEVGDIVVGTVLAPGSQRANECRMAAFYAGFPETV 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349  83 PAVTVDRQCGSSQQAVHFAAQGVIAGAYDVVIASGVESMSRVPMGSQAagrdPFGPQVAA--RYPDGLVPQGISAELIAA 160
Cdd:PLN02287 126 PVRTVNRQCSSGLQAVADVAAAIKAGFYDIGIGAGVESMTTNPMAWEG----GVNPRVESfsQAQDCLLPMGITSENVAE 201
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 161 KWGLTRAQLDEFSAESHQRAAKAWAGGKFAAEVVPLKAPGPDGTLRE-----VTTDETVRPGTTPEILAGLKPAFRADvw 235
Cdd:PLN02287 202 RFGVTREEQDQAAVESHRKAAAATASGKFKDEIVPVHTKIVDPKTGEekpivISVDDGIRPNTTLADLAKLKPVFKKN-- 279
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 236 eqrfpelgWHVTAGNSSPINDGAAAVLITSSETAAALGLKPRARIHSFAVAGDDPLYMLTGVVPATRKVLARAGLEVSDI 315
Cdd:PLN02287 280 --------GTTTAGNSSQVSDGAGAVLLMKRSVAMQKGLPILGVFRSFAAVGVDPAVMGIGPAVAIPAAVKAAGLELDDI 351
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 316 DAFEVNEAFASVVLAWQAEIGADLAKVNVNGGAIALGHPLGGSGARLLTTLLSVLEQTG--GRYGLHTMCEAGGLANATI 393
Cdd:PLN02287 352 DLFEINEAFASQFVYCCKKLGLDPEKVNVNGGAIALGHPLGATGARCVATLLHEMKRRGkdCRFGVVSMCIGTGMGAAAV 431

                 ...
gi 522136349 394 IER 396
Cdd:PLN02287 432 FER 434
PRK07851 PRK07851
acetyl-CoA C-acetyltransferase;
1-398 1.02e-108

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181146 [Multi-domain]  Cd Length: 406  Bit Score: 325.42  E-value: 1.02e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349   1 MTDAVIVDAVRTPIGK-GKpnGTLSGVHPVDLHAHALRSLVERT-GIDPGRIDDVISGAVGQVGEQSMNTARWAALAAGL 78
Cdd:PRK07851   1 MPEAVIVSTARSPIGRaFK--GSLKDMRPDDLAAQMVRAALDKVpALDPTDIDDLMLGCGLPGGEQGFNMARVVAVLLGY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349  79 PeSVPAVTVDRQCGSSQQAVHFAAQGVIAGAYDVVIASGVESMSRVPMGS---------------------QAAGRDPF- 136
Cdd:PRK07851  79 D-FLPGTTVNRYCSSSLQTTRMAFHAIKAGEGDVFISAGVETVSRFAKGNsdslpdtknplfaeaqartaaRAEGGAEAw 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 137 -GPQVAARYPDGLVPQGISAELIAAKWGLTRAQLDEFSAESHQRAAKAWAGGKFAAEVVPLKAPgpDGTLreVTTDETVR 215
Cdd:PRK07851 158 hDPREDGLLPDVYIAMGQTAENVAQLTGISREEQDEWGVRSQNRAEEAIANGFFEREITPVTLP--DGTV--VSTDDGPR 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 216 PGTTPEILAGLKPAFRADvweqrfpelgWHVTAGNSSPINDGAAAVLITSSETAAALGLKPRARIHSFAVAGDDPLYMLT 295
Cdd:PRK07851 234 AGTTYEKVSQLKPVFRPD----------GTVTAGNACPLNDGAAAVVIMSDTKARELGLTPLARIVSTGVSGLSPEIMGL 303
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 296 GVVPATRKVLARAGLEVSDIDAFEVNEAFASVVLAWQAEIGADLAKVNVNGGAIALGHPLGGSGARLLTTLLSVLEQTGG 375
Cdd:PRK07851 304 GPVEASKQALARAGMSIDDIDLVEINEAFAAQVLPSARELGIDEDKLNVSGGAIALGHPFGMTGARITTTLLNNLQTHDK 383
                        410       420
                 ....*....|....*....|...
gi 522136349 376 RYGLHTMCEAGGLANATIIERLA 398
Cdd:PRK07851 384 TFGLETMCVGGGQGMAMVLERLS 406
PRK05656 PRK05656
acetyl-CoA C-acetyltransferase;
1-396 4.25e-98

acetyl-CoA C-acetyltransferase;


Pssm-ID: 168156  Cd Length: 393  Bit Score: 297.57  E-value: 4.25e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349   1 MTDAVIVDAVRTPIGKGKpnGTLSGVHPVDLHAHALRSLVERTGIDPGRIDDVISGAVGQVGeQSMNTARWAALAAGLPE 80
Cdd:PRK05656   1 MQDVVIVAATRTAIGSFQ--GSLANIPAVELGAAVIRRLLEQTGLDPAQVDEVILGQVLTAG-AGQNPARQAAIKAGLPH 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349  81 SVPAVTVDRQCGSSQQAVHFAAQGVIAGAYDVVIASGVESMSRVPM---GSQAAGRDPFGPQVAARYPDGL------VPQ 151
Cdd:PRK05656  78 SVPAMTLNKVCGSGLKALHLAAQAIRCGDAEVIIAGGQENMSLAPYvlpGARTGLRMGHAQLVDSMITDGLwdafndYHM 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 152 GISAELIAAKWGLTRAQLDEFSAESHQRAAKAWAGGKFAAEVVPLKAPGPDGTLREVTTDETVRPGTTPEILAGLKPAFR 231
Cdd:PRK05656 158 GITAENLVEKYGISREAQDAFAAASQQKAVAAIEAGRFDDEITPILIPQRKGEPLAFATDEQPRAGTTAESLAKLKPAFK 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 232 ADvweqrfpelgWHVTAGNSSPINDGAAAVLITSSETAAALGLKPRARIHSFAVAGDDPLYMLTGVVPATRKVLARAGLE 311
Cdd:PRK05656 238 KD----------GSVTAGNASSLNDGAAAVLLMSAAKAKALGLPVLAKIAAYANAGVDPAIMGIGPVSATRRCLDKAGWS 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 312 VSDIDAFEVNEAFASVVLAWQAEIGADLAKVNVNGGAIALGHPLGGSGARLLTTLLSVLEQTGGRYGLHTMCEAGGLANA 391
Cdd:PRK05656 308 LAELDLIEANEAFAAQSLAVGKELGWDAAKVNVNGGAIALGHPIGASGCRVLVTLLHEMIRRDAKKGLATLCIGGGQGVA 387

                 ....*
gi 522136349 392 TIIER 396
Cdd:PRK05656 388 LAIER 392
PLN02644 PLN02644
acetyl-CoA C-acetyltransferase
2-398 2.37e-95

acetyl-CoA C-acetyltransferase


Pssm-ID: 215347 [Multi-domain]  Cd Length: 394  Bit Score: 290.84  E-value: 2.37e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349   2 TDAVIVDAVRTPIGKGkpNGTLSGVHPVDLHAHALRSLVERTGIDPGRIDDVISGAV-----GQVgeqsmnTARWAALAA 76
Cdd:PLN02644   1 RDVCIVGVARTPIGGF--LGSLSSLSATELGSIAIQAALERAGVDPALVQEVFFGNVlsanlGQA------PARQAALGA 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349  77 GLPESVPAVTVDRQCGSSQQAVHFAAQGVIAGAYDVVIASGVESMSRVPM---GSQAAGRDPFGPQVAARYPDGL----- 148
Cdd:PLN02644  73 GLPPSTICTTVNKVCASGMKAVMLAAQSIQLGINDVVVAGGMESMSNAPKylpEARKGSRLGHDTVVDGMLKDGLwdvyn 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 149 -VPQGISAELIAAKWGLTRAQLDEFSAESHQRAAKAWAGGKFAAEVVPLKAPGPDGTL-REVTTDETVRPgTTPEILAGL 226
Cdd:PLN02644 153 dFGMGVCAELCADQYSISREEQDAYAIQSYERAIAAQEAGAFAWEIVPVEVPGGRGRPsVIVDKDEGLGK-FDPAKLRKL 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 227 KPAFRADvweqrfpelGWHVTAGNSSPINDGAAAVLITSSETAAALGLKPRARIHSFAVAGDDPLYMLTGVVPATRKVLA 306
Cdd:PLN02644 232 RPSFKED---------GGSVTAGNASSISDGAAALVLVSGEKALELGLQVIAKIRGYADAAQAPELFTTAPALAIPKALK 302
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 307 RAGLEVSDIDAFEVNEAFASVVLAWQAEIGADLAKVNVNGGAIALGHPLGGSGARLLTTLLSVLEQTGGRYGLHTMCEAG 386
Cdd:PLN02644 303 HAGLEASQVDYYEINEAFSVVALANQKLLGLDPEKVNVHGGAVSLGHPIGCSGARILVTLLGVLRSKNGKYGVAGICNGG 382
                        410
                 ....*....|..
gi 522136349 387 GLANATIIERLA 398
Cdd:PLN02644 383 GGASAIVVELMQ 394
PRK08131 PRK08131
3-oxoadipyl-CoA thiolase;
1-396 3.19e-94

3-oxoadipyl-CoA thiolase;


Pssm-ID: 181242 [Multi-domain]  Cd Length: 401  Bit Score: 287.83  E-value: 3.19e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349   1 MTDAVIVDAVRTPIGKGkpNGTLSGVHPVDLHAHALRSLVERTGIDPGRIDDVISGAVGQVGEQSMNTARWAALAAGLPE 80
Cdd:PRK08131   1 MLDAYIYDGLRSPFGRH--AGALASVRPDDLAATVIRRLLEKSGFPGDDIEDVILGCTNQAGEDSRNVARNALLLAGLPV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349  81 SVPAVTVDRQCGSSQQAVHFAAQGVIAGAYDVVIASGVESMSRVPM----GSQAAGRDP--FGPQVAARYPDGLV----- 149
Cdd:PRK08131  79 TVPGQTVNRLCASGLAAVIDAARAITCGEGDLYLAGGVESMSRAPFvmgkAESAFSRDAkvFDTTIGARFPNPKIvaqyg 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 150 ----PQgiSAELIAAKWGLTRAQLDEFSAESHQRAAKAWAGGKFAAEVVPLKAP-GPDGTLREVTTDETVRPGTTPEILA 224
Cdd:PRK08131 159 ndsmPE--TGDNVAAEFGISREDADRFAAQSQAKYQAAKEEGFFADEITPIEVPqGRKLPPKLVAEDEHPRPSSTVEALT 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 225 GLKPAFRADVweqrfpelgwhVTAGNSSPINDGAAAVLITSSETAAALGLKPRARIHSFAVAGDDPLYMLTGVVPATRKV 304
Cdd:PRK08131 237 KLKPLFEGGV-----------VTAGNASGINDGAAALLIGSRAAGEKYGLKPMARILSSAAAGVEPRIMGIGPVEAIKKA 305
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 305 LARAGLEVSDIDAFEVNEAFASVVLAW--QAEIGADLAKVNVNGGAIALGHPLGGSGARLLTTLLSVLEQTGGRYGLHTM 382
Cdd:PRK08131 306 LARAGLTLDDMDIIEINEAFASQVLGClkGLGVDFDDPRVNPNGGAIAVGHPLGASGARLALTAARELQRRGKRYAVVSL 385
                        410
                 ....*....|....
gi 522136349 383 CEAGGLANATIIER 396
Cdd:PRK08131 386 CIGVGQGLAMVIER 399
PRK08235 PRK08235
acetyl-CoA C-acetyltransferase;
1-395 6.28e-93

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181311 [Multi-domain]  Cd Length: 393  Bit Score: 284.30  E-value: 6.28e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349   1 MTDAVIVDAVRTPIGKGkpNGTLSGVHPVDLHAHALRSLVERTGIDPGRIDDVISGAVGQVGeQSMNTARWAALAAGLPE 80
Cdd:PRK08235   1 MSKTVIVSAARTPFGKF--GGSLKDVKATELGGIAIKEALERANVSAEDVEEVIMGTVLQGG-QGQIPSRQAARAAGIPW 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349  81 SVPAVTVDRQCGSSQQAVHFAAQGVIAGAYDVVIASGVESMSRVPMGSQAA---GRDPFGPQVAARYPDGL------VPQ 151
Cdd:PRK08235  78 EVQTETVNKVCASGLRAVTLADQIIRAGDASVIVAGGMESMSNAPYILPGArwgYRMGDNEVIDLMVADGLtcafsgVHM 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 152 GISAELIAAKWGLTRAQLDEFSAESHQRAAKAWAGGKFAAEVVPLKAPGPDGTLREVTTDETVRPGTTPEILAGLKPAFR 231
Cdd:PRK08235 158 GVYGGEVAKELGISREAQDEWAYRSHQRAVSAHEEGRFEEEIVPVTIPQRKGDPIVVAKDEAPRKDTTIEKLAKLKPVFD 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 232 ADvweqrfpelgWHVTAGNSSPINDGAAAVLITSSETAAALGLKPRARIHSFAVAGDDPLYMLTGVVPATRKVLARAGLE 311
Cdd:PRK08235 238 KT----------GTITAGNAPGVNDGAAALVLMSEDRAKQEGRKPLATILAHTAIAVEAKDFPRTPGYAINALLEKTGKT 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 312 VSDIDAFEVNEAFASVVLAWQAEIGADLAKVNVNGGAIALGHPLGGSGARLLTTLLSVLEQTGGRYGLHTMCEAGGLANA 391
Cdd:PRK08235 308 VEDIDLFEINEAFAAVALASTEIAGIDPEKVNVNGGAVALGHPIGASGARIIVTLIHELKRRGGGIGIAAICSGGGQGDA 387

                 ....
gi 522136349 392 TIIE 395
Cdd:PRK08235 388 VLIE 391
PRK07108 PRK07108
acetyl-CoA C-acyltransferase;
1-397 1.13e-92

acetyl-CoA C-acyltransferase;


Pssm-ID: 180843 [Multi-domain]  Cd Length: 392  Bit Score: 283.58  E-value: 1.13e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349   1 MTDAVIVDAVRTPIGKGKpNGTLSGVHPVDLHAHALRSLVERTGIDPGRIDDVISGAVGQVGEQSMNTARWAALAAGLPE 80
Cdd:PRK07108   1 MTEAVIVSTARTPLAKSW-RGAFNMTHGATLGGHVVQHAVERAKLDPAEVEDVIMGCANPEGATGANIARQIALRAGLPV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349  81 SVPAVTVDRQCGSSQQAVHFAAQGVIAGAYDVVIASGVESMSRVpmgSQAAGRDPF-GPQVAARYPDGLVPQGISAELIA 159
Cdd:PRK07108  80 TVPGMTVNRFCSSGLQTIALAAQRVIAGEGDVFVAGGVESISCV---QNEMNRHMLrEGWLVEHKPEIYWSMLQTAENVA 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 160 AKWGLTRAQLDEFSAESHQRAAKAWAGGKFAAEVVPL--------KAPGPDGTlREVTT--DETVRPGTTPEILAGLKPA 229
Cdd:PRK07108 157 KRYGISKERQDEYGVQSQQRAAAAQAAGRFDDEIVPItvtagvadKATGRLFT-KEVTVsaDEGIRPDTTLEGVSKIRSA 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 230 FRADVweqrfpelgwhVTAGNSSPINDGAAAVLITSSETAAALGLKPRARIHSFAVAGDDPLYMLTGVVPATRKVLARAG 309
Cdd:PRK07108 236 LPGGV-----------ITAGNASQFSDGASACVVMNAKVAEREGLQPLGIFRGFAVAGCEPDEMGIGPVFAVPKLLKQAG 304
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 310 LEVSDIDAFEVNEAFASVVLAWQAEIGADLAKVNVNGGAIALGHPLGGSGARLLTTLLSVLEQTGGRYGLHTMCEAGGLA 389
Cdd:PRK07108 305 LKVDDIDLWELNEAFAVQVLYCRDTLGIPMDRLNVNGGAIAVGHPYGVSGARLTGHALIEGKRRGAKYVVVTMCIGGGQG 384

                 ....*...
gi 522136349 390 NATIIERL 397
Cdd:PRK07108 385 AAGLFEVL 392
PRK06633 PRK06633
acetyl-CoA C-acetyltransferase;
1-395 3.02e-89

acetyl-CoA C-acetyltransferase;


Pssm-ID: 168632 [Multi-domain]  Cd Length: 392  Bit Score: 274.99  E-value: 3.02e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349   1 MTDAV-IVDAVRTPIGKGKpnGTLSGVHPVDLHAHALRSLVERTGIDPGRIDDVISGAVgQVGEQSMNTARWAALAAGLP 79
Cdd:PRK06633   1 MTKPVyITHAKRTAFGSFM--GSLSTTPAPMLAAHLIKDILQNSKIDPALVNEVILGQV-ITGGSGQNPARQTLIHAGIP 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349  80 ESVPAVTVDRQCGSSQQAVHFAAQGVIAGAYDVVIASGVESMSRVPMGSQAAGRDPFG--PQVAARYPDGL------VPQ 151
Cdd:PRK06633  78 KEVPGYTINKVCGSGLKSVALAANSIMTGDNEIVIAGGQENMSLGMHGSYIRAGAKFGdiKMVDLMQYDGLtdvfsgVFM 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 152 GISAELIAAKWGLTRAQLDEFSAESHQRAAKAWAGGKFAAEVVPLKApgpdgTLREVTT----DETVRPGTTPEILAGLK 227
Cdd:PRK06633 158 GITAENISKQFNISRQEQDEFALSSHKKAAKAQLAGIFKDEILPIEV-----TIKKTTSlfdhDETVRPDTSLEILSKLR 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 228 PAFRADVweqrfpelgwHVTAGNSSPINDGAAAVLITSSETAAALGLKPRARIHSFAVAGDDPLYMLTGVVPATRKVLAR 307
Cdd:PRK06633 233 PAFDKNG----------VVTAGNASSINDGAACLMVVSEEALKKHNLTPLARIVSYASAGVDPSIMGTAPVPASQKALSK 302
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 308 AGLEVSDIDAFEVNEAFASVVLAWQAEIGADLAKVNVNGGAIALGHPLGGSGARLLTTLLSVLEQTGGRYGLHTMCEAGG 387
Cdd:PRK06633 303 AGWSVNDLEVIEVNEAFAAQSIYVNREMKWDMEKVNINGGAIAIGHPIGASGGRVLITLIHGLRRAKAKKGLVTLCIGGG 382

                 ....*...
gi 522136349 388 LANATIIE 395
Cdd:PRK06633 383 MGMAMCVE 390
PRK08170 PRK08170
acetyl-CoA C-acetyltransferase;
6-397 8.14e-85

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181265 [Multi-domain]  Cd Length: 426  Bit Score: 264.57  E-value: 8.14e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349   6 IVDAVRTPI--GKGKPNGtlsgVHPVDLHAHALRSLVERTGIDPGRIDDVISGAVgQVGEQSMNTARWAALAAGLPESVP 83
Cdd:PRK08170   7 IVDGARTPFlkARGGPGP----FSASDLAVAAGRALLNRQPFAPDDLDEVILGCA-MPSPDEANIARVVALRLGCGEKVP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349  84 AVTVDRQCGSSQQAVHFAAQGVIAGAYDVVIASGVESMSRVPMGSQAAGRDPFGPQVAAR------------YPDGLVP- 150
Cdd:PRK08170  82 AWTVQRNCASGMQALDSAAANIALGRADLVLAGGVEAMSHAPLLFSEKMVRWLAGWYAAKsigqklaalgklRPSYLAPv 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 151 ---------------QGISAELIAAKWGLTRAQLDEFSAESHQRAAKAWAGGKFAaEVVPLKAPgpDGTLREvtTDETVR 215
Cdd:PRK08170 162 igllrgltdpvvglnMGQTAEVLAHRFGITREQMDAYAARSHQRLAAAQAEGRLK-EVVPLFDR--DGKFYD--HDDGVR 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 216 PGTTPEILAGLKPAFradvwEQRFPElgwhVTAGNSSPINDGAAAVLITSSETAAALGLKPRARIHSFAVAGDDPLYMLT 295
Cdd:PRK08170 237 PDSSMEKLAKLKPFF-----DRPYGR----VTAGNSSQITDGACWLLLASEEAVKKYGLPPLGRIVDSQWAALDPSQMGL 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 296 GVVPATRKVLARAGLEVSDIDAFEVNEAFASVVL----AWQAE------------IGA-DLAKVNVNGGAIALGHPLGGS 358
Cdd:PRK08170 308 GPVHAATPLLQRHGLTLEDLDLWEINEAFAAQVLaclaAWADEeycreqlgldgaLGElDRERLNVDGGAIALGHPVGAS 387
                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 522136349 359 GARLLTTLLSVLEQTGGRYGLHTMCEAGGLANATIIERL 397
Cdd:PRK08170 388 GARIVLHLLHALKRRGTKRGIAAICIGGGQGGAMLLERV 426
fadI PRK08963
3-ketoacyl-CoA thiolase; Reviewed
4-396 1.23e-84

3-ketoacyl-CoA thiolase; Reviewed


Pssm-ID: 181597 [Multi-domain]  Cd Length: 428  Bit Score: 264.15  E-value: 1.23e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349   4 AVIVDAVRTPIGKgkpNGT-LSGVHPVDLHAHALRSLVERTGIDPGRIDDVISGAVGQVGEqSMNTARWAALAAGLPESV 82
Cdd:PRK08963   7 IAIVSGLRTPFAK---QATaFHGIPAVDLGKMVVGELLARSEIDPELIEQLVFGQVVQMPE-APNIAREIVLGTGMNVHT 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349  83 PAVTVDRQCGSSQQAVHFAAQGVIAGAYDVVIASGVESMSRVPMG-------------------------SQAAGRD--P 135
Cdd:PRK08963  83 DAYSVSRACATSFQAVANVAESIMAGTIDIGIAGGADSSSVLPIGvskklaralvdlnkartlgqrlklfSRLRLRDllP 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 136 FGPQVAaRYPDGLVpQGISAELIAAKWGLTRAQLDEFSAESHQRAAKAWAGGKFAAEVVPLKAPGPDGTLREvttDETVR 215
Cdd:PRK08963 163 VPPAVA-EYSTGLR-MGDTAEQMAKTYGISREEQDALAHRSHQLAAQAWAEGKLDDEVMTAHVPPYKQPLEE---DNNIR 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 216 PGTTPEILAGLKPAFradvwEQRFPElgwhVTAGNSSPINDGAAAVLITSSETAAALGLKPRARIHSFAVAGDDPLY-ML 294
Cdd:PRK08963 238 GDSTLEDYAKLRPAF-----DRKHGT----VTAANSTPLTDGAAAVLLMSESRAKALGLTPLGYLRSYAFAAIDVWQdML 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 295 TGVVPATRKVLARAGLEVSDIDAFEVNEAFASVVLA----------------WQAEIG-ADLAKVNVNGGAIALGHPLGG 357
Cdd:PRK08963 309 LGPAYATPLALERAGLTLADLTLIDMHEAFAAQTLAnlqmfaserfareklgRSQAIGeVDMSKFNVLGGSIAYGHPFAA 388
                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 522136349 358 SGARLLTTLLSVLEQTGGRYGLHTMCEAGGLANATIIER 396
Cdd:PRK08963 389 TGARMITQTLHELRRRGGGLGLTTACAAGGLGAAMVLEV 427
PRK06690 PRK06690
acetyl-CoA C-acyltransferase;
4-398 1.43e-81

acetyl-CoA C-acyltransferase;


Pssm-ID: 180659 [Multi-domain]  Cd Length: 361  Bit Score: 254.31  E-value: 1.43e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349   4 AVIVDAVRTPIGKgkPNGTLSGVHPVDLHAHALRSLVErtGIDPgRIDDVISG-AVGQVGeqsmNTARWAALAAGLPESV 82
Cdd:PRK06690   3 AVIVEAKRTPIGK--KNGMLKDYEVQQLAAPLLTFLSK--GMER-EIDDVILGnVVGPGG----NVARLSALEAGLGLHI 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349  83 PAVTVDRQCGSSQQAVHFAAQGVIAGAYDVVIASGVESMSRVPMGSQAAgrdpFGPQVAARyPDglvpQGISAELIAAKW 162
Cdd:PRK06690  74 PGVTIDRQCGAGLEAIRTACHFIQGGAGKCYIAGGVESTSTSPFQNRAR----FSPETIGD-PD----MGVAAEYVAERY 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 163 GLTRAQLDEFSAESHQRAAKAWAGGKFAAEVVPLkapgpDGTLrevttDETVRPGTTPE-ILAGLKPAFRADvweqrfpe 241
Cdd:PRK06690 145 NITREMQDEYACLSYKRTLQALEKGYIHEEILSF-----NGLL-----DESIKKEMNYErIIKRTKPAFLHN-------- 206
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 242 lgWHVTAGNSSPINDGAAAVLITSSETAAALGLKPRARIHSFAVAGDDPLYMLTGVVPATRKVLARAGLEVSDIDAFEVN 321
Cdd:PRK06690 207 --GTVTAGNSCGVNDGACAVLVMEEGQARKLGYKPVLRFVRSAVVGVDPNLPGTGPIFAVNKLLNEMNMKVEDIDYFEIN 284
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 522136349 322 EAFASVVLAWQAEIGADLAKVNVNGGAIALGHPLGGSGARLLTTLLSVLEQTGGRYGLHTMCEAGGLANATIIERLA 398
Cdd:PRK06690 285 EAFASKVVACAKELQIPYEKLNVNGGAIALGHPYGASGAMLVTRLFYQAKREDMKYGIATLGIGGGIGLALLFEKVE 361
Thiolase_N pfam00108
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
5-267 7.51e-77

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: 238.36  E-value: 7.51e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349    5 VIVDAVRTPIGKGKpnGTLSGVHPVDLHAHALRSLVERTGIDPGRIDDVISGAVGQVGEQSmNTARWAALAAGLPESVPA 84
Cdd:pfam00108   2 VIVSAARTPFGSFG--GSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQAGEGQ-NPARQAALKAGIPDSAPA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349   85 VTVDRQCGSSQQAVHFAAQGVIAGAYDVVIASGVESMSRVPMGSQAAGRDPFGPQVAARY----PDGL------VPQGIS 154
Cdd:pfam00108  79 VTINKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALPTDARSGLKHGDEKKHdlliPDGLtdafngYHMGLT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349  155 AELIAAKWGLTRAQLDEFSAESHQRAAKAWAGGKFAAEVVPLKAPGPDGTLrEVTTDETVRPGTTPEILAGLKPAFRADv 234
Cdd:pfam00108 159 AENVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDEIVPVTVKGRKGKP-TVDKDEGIRPPTTAEPLAKLKPAFDKE- 236
                         250       260       270
                  ....*....|....*....|....*....|...
gi 522136349  235 weqrfpelgWHVTAGNSSPINDGAAAVLITSSE 267
Cdd:pfam00108 237 ---------GTVTAGNASPINDGAAAVLLMSES 260
PRK06366 PRK06366
acetyl-CoA C-acetyltransferase;
1-395 3.71e-75

acetyl-CoA C-acetyltransferase;


Pssm-ID: 102340 [Multi-domain]  Cd Length: 388  Bit Score: 238.76  E-value: 3.71e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349   1 MTDAVIVDAVRTPIGK-GKpngTLSGVHPVDLHAHALRSLVERTGIDPGRIDDVISGAVGQVGeQSMNTARWAALAAGLP 79
Cdd:PRK06366   1 MKDVYIVSAKRTAIGKfGR---SFSKIKAPQLGGAAIKAVIDDAKLDPALVQEVIMGNVIQAG-VGQNPAGQAAYHAGLP 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349  80 ESVPAVTVDRQCGSSQQAVHFAAQGVIAGAYDVVIASGVESMSRVPMGSQAAGRdpFGPQVA---------ARYPDGLVP 150
Cdd:PRK06366  77 FGVTKYTVNVVCASGMLAVESAAREIMLGERDLVIAGGMENMSNAPFLLPSDLR--WGPKHLlhknykiddAMLVDGLID 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 151 ------QGISAELIAAKWGLTRAQLDEFSAESHQRAAKAWAGGKFAAEVVPLKapgpdgtlrEVTTDETVRPgTTPEILA 224
Cdd:PRK06366 155 afyfehMGVSAERTARKYGITREMADEYSVQSYERAIRATESGEFRNEIVPFN---------DLDRDEGIRK-TTMEDLA 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 225 GLKPAFRADVWeqrfpelgwhVTAGNSSPINDGAAAVLITSSETAAALGLKPRARIHSFAVAGDDPLYMLTGVVPATRKV 304
Cdd:PRK06366 225 KLPPAFDKNGI----------LTAGNSAQLSDGGSALVMASEKAINEYGLKPIARITGYESASLDPLDFVEAPIPATRKL 294
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 305 LARAGLEVSDIDAFEVNEAF--ASVVLAWQAEIgaDLAKVNVNGGAIALGHPLGGSGARLLTTLLSVLEQTGGRYGLHTM 382
Cdd:PRK06366 295 LEKQNKSIDYYDLVEHNEAFsiASIIVRDQLKI--DNERFNVNGGAVAIGHPIGNSGSRIIVTLINALKTRHMKTGLATL 372
                        410
                 ....*....|...
gi 522136349 383 CEAGGLANATIIE 395
Cdd:PRK06366 373 CHGGGGAHTLTLE 385
PRK06954 PRK06954
acetyl-CoA C-acetyltransferase;
5-395 4.14e-75

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180775 [Multi-domain]  Cd Length: 397  Bit Score: 238.64  E-value: 4.14e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349   5 VIVDAVRTPIGKGKpnGTLSGVHPVDLHAHALRSLVERTGIDPGRIDDVISGAVGQVGeQSMNTARWAALAAGLPESVPA 84
Cdd:PRK06954  10 VIASAARTPMAAFQ--GEFASLTAPQLGAAAIAAAVERAGLKPEQIDEVVMGCVLPAG-QGQAPARQAALGAGLPLSVGC 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349  85 VTVDRQCGSSQQAVHFAAQGVIAGAYDVVIASGVESMSRVPM---GSQAAGRDPFGPQVAARYPDGLVP-------QGIS 154
Cdd:PRK06954  87 TTVNKMCGSGMRAAMFAHDMLVAGSVDVIVAGGMESMTNAPYllpKARGGMRMGHGQVLDHMFLDGLEDaydkgrlMGTF 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 155 AELIAAKWGLTRAQLDEFSAESHQRAAKAWAGGKFAAEVVPLKAPGPDGTLrEVTTDETVRPgTTPEILAGLKPAFRADv 234
Cdd:PRK06954 167 AEECAGEYGFTREAQDAFAIESLARAKRANEDGSFAWEIAPVTVAGKKGDT-VIDRDEQPFK-ANPEKIPTLKPAFSKT- 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 235 weqrfpelgWHVTAGNSSPINDGAAAVLITSSETAAALGLKPRARIHSFAVAGDDPLYMLTGVVPATRKVLARAGLEVSD 314
Cdd:PRK06954 244 ---------GTVTAANSSSISDGAAALVMMRASTAKRLGLAPLARVVGHSTFAQAPSKFTTAPVGAIRKLFEKNGWRAAE 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 315 IDAFEVNEAFASVVLAWQAEIGADLAKVNVNGGAIALGHPLGGSGARLLTTLLSVLEQTGGRYGLHTMCEAGGLANATII 394
Cdd:PRK06954 315 VDLFEINEAFAVVTMAAMKEHGLPHEKVNVNGGACALGHPIGASGARILVTLIGALRARGGKRGVASLCIGGGEATAMGI 394

                 .
gi 522136349 395 E 395
Cdd:PRK06954 395 E 395
PRK09268 PRK09268
acetyl-CoA C-acetyltransferase;
1-396 9.43e-64

acetyl-CoA C-acetyltransferase;


Pssm-ID: 236440 [Multi-domain]  Cd Length: 427  Bit Score: 210.14  E-value: 9.43e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349   1 MTDAVIVDAVRTPIGKGkpNGTLSGVHPVDLHAHALRSLVERTGIDPGRIDDVISGAVGQvGEQSMNTARWAALAAGLPE 80
Cdd:PRK09268   6 VRRVAILGGNRIPFARS--NGAYADASNQDMLTAALDGLVDRFGLQGERLGEVVAGAVLK-HSRDFNLTRECVLGSALSP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349  81 SVPAVTVDRQCGSSQQAVHFAAQGVIAGAYDVVIASGVESMSRVPMGS--------QAAGRDPFGPQ----VAARYPDGL 148
Cdd:PRK09268  83 YTPAYDLQQACGTGLEAAILVANKIALGQIDSGIAGGVDTTSDAPIAVneglrkilLELNRAKTTGDrlkaLGKLRPKHL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 149 VPQ---------GIS----AELIAAKWGLTRAQLDEFSAESHQRAAKAWAGGKFAAEVVPLKApgpdgtlreVTTDETVR 215
Cdd:PRK09268 163 APEiprngeprtGLSmgehAAITAKEWGISREAQDELAAASHQNLAAAYDRGFFDDLITPFLG---------LTRDNNLR 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 216 PGTTPEILAGLKPAFraDVWEQRfpelgwHVTAGNSSPINDGAAAVLITSSETAAALGLKPRARIHSFAVA------GDD 289
Cdd:PRK09268 234 PDSSLEKLAKLKPVF--GKGGRA------TMTAGNSTPLTDGASVVLLASEEWAAEHGLPVLAYLVDAETAavdfvhGKE 305
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 290 PLYML-TGVVPatrKVLARAGLEVSDIDAFEVNEAFASVVL----AWQAE------------IGA-DLAKVNVNGGAIAL 351
Cdd:PRK09268 306 GLLMApAYAVP---RLLARNGLTLQDFDFYEIHEAFASQVLatlkAWEDEeycrerlgldapLGSiDRSKLNVNGSSLAA 382
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 522136349 352 GHPLGGSGARLLTTLLSVLEQTGGRYGLHTMCEAGGLANATIIER 396
Cdd:PRK09268 383 GHPFAATGGRIVATLAKLLAEKGSGRGLISICAAGGQGVTAILER 427
Thiolase_C pfam02803
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
274-396 5.94e-49

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: 161.66  E-value: 5.94e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349  274 LKPRARIHSFAVAGDDPLYMLTGVVPATRKVLARAGLEVSDIDAFEVNEAFASVVLAWQAEIGADLAKVNVNGGAIALGH 353
Cdd:pfam02803   1 LKPLARIRSYATAGVDPAIMGIGPAYAIPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGIDPEKVNVNGGAIALGH 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 522136349  354 PLGGSGARLLTTLLSVLEQTGGRYGLHTMCEAGGLANATIIER 396
Cdd:pfam02803  81 PLGASGARILVTLLHELKRRGGKYGLASLCIGGGQGVAMIIER 123
nondecarbox_cond_enzymes cd00826
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ...
17-395 8.38e-44

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: 156.88  E-value: 8.38e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349  17 GKPNGTLSGVHPVDLH---AHALRSLVERTGIDPGRIDDVISGAVGQVGEQSmNTARWAALAAGLPESVPAVTVDRQCGS 93
Cdd:cd00826    9 GKFGGENGADANDLAHeagAKAIAAALEPAGVAAGAVEEACLGQVLGAGEGQ-NCAQQAAMHAGGLQEAPAIGMNNLCGS 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349  94 SQQAVHFAAQGVIAGAYDVVIASGVESMSrvpmgsqaagrdpfgpqvaarYPDGLVPQGISAELIAAKWGLtRAQLDEFS 173
Cdd:cd00826   88 GLRALALAMQLIAGGDANCILAGGFEKME---------------------TSAENNAKEKHIDVLINKYGM-RACPDAFA 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 174 AESHQRAAKAWAGGKFAAEVVPLKAPGPDGTlREVTTDETVRPGT--TPEILAGLKPAFRADVWeqrfpelgwhVTAGNS 251
Cdd:cd00826  146 LAGQAGAEAAEKDGRFKDEFAKFGVKGRKGD-IHSDADEYIQFGDeaSLDEIAKLRPAFDKEDF----------LTAGNA 214
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 252 SPINDGAAAVLITSSETAA-------ALGLKPRARIHSFAVAGDDP----LYMLTGVVPATRKVLARAGLEVSDIDAFEV 320
Cdd:cd00826  215 CGLNDGAAAAILMSEAEAQkhglqskAREIQALEMITDMASTFEDKkvikMVGGDGPIEAARKALEKAGLGIGDLDLIEA 294
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 321 NEAFASVVLAWQAEIGADLAK------------------VNVNGGAIALGHPLGGSGARLLTTLLSVL-----EQTGGRY 377
Cdd:cd00826  295 HDAFAANACATNEALGLCPEGqggalvdrgdntyggksiINPNGGAIAIGHPIGASGAAICAELCFELkgeagKRQGAGA 374
                        410
                 ....*....|....*...
gi 522136349 378 GLHTMCEAGGLANATIIE 395
Cdd:cd00826  375 GLALLCIGGGGGAAMCIE 392
SCP-x_thiolase cd00829
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ...
21-363 9.46e-31

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: 120.83  E-value: 9.46e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349  21 GTLSGVHPVDLHAHALRSLVERTGIDPGRIDDVISGAVGQVGEQSMNTARwAALAAGLPEsVPAVTVDRQCGSSQQAVHF 100
Cdd:cd00829    9 GRRSDRSPLELAAEAARAALDDAGLEPADIDAVVVGNAAGGRFQSFPGAL-IAEYLGLLG-KPATRVEAAGASGSAAVRA 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 101 AAQGVIAGAYDVVIASGVESMSRVPMGSQAAGRD-PFGPQVAARYPDGLVPQ--GISAELIAAKWGLTRAQLDEFSAESH 177
Cdd:cd00829   87 AAAAIASGLADVVLVVGAEKMSDVPTGDEAGGRAsDLEWEGPEPPGGLTPPAlyALAARRYMHRYGTTREDLAKVAVKNH 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 178 QRAAK---AWAGGKFAAEVVpLKApgpdgtlrevttdetvRPGTTPeilaglkpafradvweqrfpelgwhVTAGNSSPI 254
Cdd:cd00829  167 RNAARnpyAQFRKPITVEDV-LNS----------------RMIADP-------------------------LRLLDCCPV 204
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 255 NDGAAAVLITSSETAAALGLKPrARIHSFAVAGD-------DPLYMLTGVVPATRKVLARAGLEVSDIDAFEVNEAFASV 327
Cdd:cd00829  205 SDGAAAVVLASEERARELTDRP-VWILGVGAASDtpslserDDFLSLDAARLAARRAYKMAGITPDDIDVAELYDCFTIA 283
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 522136349 328 VLAW-------------------QAEIGADLAkVNVNGGAIALGHPLGGSGARLL 363
Cdd:cd00829  284 ELLAledlgfcekgeggklvregDTAIGGDLP-VNTSGGLLSKGHPLGATGLAQA 337
PRK06064 PRK06064
thiolase domain-containing protein;
1-361 2.18e-22

thiolase domain-containing protein;


Pssm-ID: 235688 [Multi-domain]  Cd Length: 389  Bit Score: 97.66  E-value: 2.18e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349   1 MTDAVIVDAVRTPIGKgkpngtLSGVHPVDLHAHALRSLVERTGIDPGRIDDVISG--AVGQVGEQSmNTARWAALAAGL 78
Cdd:PRK06064   1 MRDVAIIGVGQTKFGE------LWDVSLRDLAVEAGLEALEDAGIDGKDIDAMYVGnmSAGLFVSQE-HIAALIADYAGL 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349  79 PeSVPAVTVDRQCGSSQQAVHFAAQGVIAGAYDVVIASGVESMSRVP------MGSQAAGRD---PFGPQVAARYpdglv 149
Cdd:PRK06064  74 A-PIPATRVEAACASGGAALRQAYLAVASGEADVVLAAGVEKMTDVPtpdateAIARAGDYEweeFFGATFPGLY----- 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 150 pqGISAELIAAKWGLTRAQLDEFSAESHQRAAKawaggkfaaevvplkapGPDGTLREVTTDETVrpgttpeilagLKPA 229
Cdd:PRK06064 148 --ALIARRYMHKYGTTEEDLALVAVKNHYNGSK-----------------NPYAQFQKEITVEQV-----------LNSP 197
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 230 FRAdvweqrfpelgWHVTAGNSSPINDGAAAVLITSSETAAALGLKPrARIHSFAVAGD-------DPLYMLTGVVPATR 302
Cdd:PRK06064 198 PVA-----------DPLKLLDCSPITDGAAAVILASEEKAKEYTDTP-VWIKASGQASDtialhdrKDFTTLDAAVVAAE 265
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 522136349 303 KVLARAGLEVSDIDAFEVNEAF-------------------ASVVLAWQAEIGADLAkVNVNGGAIALGHPLGGSGAR 361
Cdd:PRK06064 266 KAYKMAGIEPKDIDVAEVHDCFtiaeilayedlgfakkgegGKLAREGQTYIGGDIP-VNPSGGLKAKGHPVGATGVS 342
cond_enzymes cd00327
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ...
248-371 7.98e-14

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: 70.94  E-value: 7.98e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 248 AGNSSPINDGAAAVLITSSETAAALGLKPRARIHSFAVAGDD----PLYMLTGVVPATRKVLARAGLEVSDIDAFEVNEA 323
Cdd:cd00327   94 GSEEFVFGDGAAAAVVESEEHALRRGAHPQAEIVSTAATFDGasmvPAVSGEGLARAARKALEGAGLTPSDIDYVEAHGT 173
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 522136349 324 FASVVLAWQAEIGAD---LAKVNVNGGAIALGHPLGGSGARLLTTLLSVLE 371
Cdd:cd00327  174 GTPIGDAVELALGLDpdgVRSPAVSATLIMTGHPLGAAGLAILDELLLMLE 224
PRK06289 PRK06289
acetyl-CoA acetyltransferase; Provisional
30-378 4.79e-13

acetyl-CoA acetyltransferase; Provisional


Pssm-ID: 235771 [Multi-domain]  Cd Length: 403  Bit Score: 70.10  E-value: 4.79e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349  30 DLHAHALRSLVERTGIDPgriDDVISGAVGQ-VGEQSMNTARWAALAAGLPES---VPAVTVDRQCGSSQQAVHFAAQGV 105
Cdd:PRK06289  28 DLTREVVDGTLAAAGVDA---DDIEVVHVGNfFGELFAGQGHLGAMPATVHPAlwgVPASRHEAACASGSVATLAAMADL 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 106 IAGAYDVVIASGVESMSRVP-------MGSQA-AGRDpfgpQVAARYPdglVPQGIS--AELIAAKWGLTRAQLDEFSAE 175
Cdd:PRK06289 105 RAGRYDVALVVGVELMKTVPgdvaaehLGAAAwTGHE----GQDARFP---WPSMFArvADEYDRRYGLDEEHLRAIAEI 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 176 SHQRA-------AKAWAggkfaaevVPLKAPGPDGTLREVTTDETVRPgttpeilaglkpafradvweqrfpelgwhvta 248
Cdd:PRK06289 178 NFANArrnpnaqTRGWA--------FPDEATNDDDATNPVVEGRLRRQ-------------------------------- 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 249 gNSSPINDGAAAVLITSSETAAALGLK-PRARI----HSFA--------VAGDDPLYMLTGVVPATRKVLARAGLEVSDI 315
Cdd:PRK06289 218 -DCSQVTDGGAGVVLASDAYLRDYADArPIPRIkgwgHRTAplgleqklDRSAGDPYVLPHVRQAVLDAYRRAGVGLDDL 296
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 316 DAFEVNEAF-ASVVLA------------WQA------EIGADLAkVNVNGGAIALGHPLGGSGARLlttLLSVLEQTGGR 376
Cdd:PRK06289 297 DGFEVHDCFtPSEYLAidhigltgpgesWKAiengeiAIGGRLP-INPSGGLIGGGHPVGASGVRM---LLDAAKQVTGT 372

                 ..
gi 522136349 377 YG 378
Cdd:PRK06289 373 AG 374
PRK06157 PRK06157
acetyl-CoA acetyltransferase; Validated
76-376 1.97e-11

acetyl-CoA acetyltransferase; Validated


Pssm-ID: 180433 [Multi-domain]  Cd Length: 398  Bit Score: 65.05  E-value: 1.97e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349  76 AGLPESVP------AVT-VDRQCGSSQQAVHFAAQGVIAGAYDVVIASGVESMSRVpmGSQAAGRDPFGPQVAARYPDGL 148
Cdd:PRK06157  66 SGTPLSRAlrlpniPVTrVENFCATGSEAFRGAVYAVASGAYDIALALGVEKLKDT--GYGGLPVANPGTLADMTMPNVT 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 149 VPQGIS--AELIAAKWGLTRAQLDE----FSAESHQRAAKawaggkfaaevvplkapGPDGTLREVTTDETVRpgTTPeI 222
Cdd:PRK06157 144 APGNFAqlASAYAAKYGVSREDLKRamahVSVKSHANGAR-----------------NPKAHLRKAVTEEQVL--KAP-M 203
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 223 LAGlkpafradvweqrfpELGWHvtagNSSPINDGAAAVLITSSETAAALGLKPRARIHSFAVA----------GDDPLY 292
Cdd:PRK06157 204 IAG---------------PLGLF----DCCGVSDGAAAAIVTTPEIARALGKKDPVYVKALQLAvsngwelqynGWDGSY 264
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 293 MLTgVVPATRKVLARAGLE--VSDIDAFEVNEAFA--SVVL-----------AWQA------EIGADLAkVNVNGGAIAL 351
Cdd:PRK06157 265 FPT-TRIAARKAYREAGITdpREELSMAEVHDCFSitELVTmedlglsergqAWRDvldgffDADGGLP-CQIDGGLKCF 342
                        330       340
                 ....*....|....*....|....*.
gi 522136349 352 GHPLGGSGARLLTTL-LSVLEQTGGR 376
Cdd:PRK06157 343 GHPIGASGLRMLYEMyLQLLGRAGER 368
PRK12578 PRK12578
thiolase domain-containing protein;
30-375 8.39e-11

thiolase domain-containing protein;


Pssm-ID: 183606 [Multi-domain]  Cd Length: 385  Bit Score: 62.94  E-value: 8.39e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349  30 DLHAHALRSLVERTGIDPGRIDDVISGAVGQVGEQSMnTARWAALAAGLPESVPaVTVDRQCGSSQQAVHFAAQGVIAGA 109
Cdd:PRK12578  23 ELAWESIKEALNDAGVSQTDIELVVVGSTAYRGIELY-PAPIVAEYSGLTGKVP-LRVEAMCATGLAASLTAYTAVASGL 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 110 YDVVIASGVESMSRVPMGSQAA--GRDP--------FGPQVAARYpdglvpqGISAELIAAKWGLTRAQLDEFSAESHQR 179
Cdd:PRK12578 101 VDMAIAVGVDKMTEVDTSTSLAigGRGGnyqweyhfYGTTFPTYY-------ALYATRHMAVYGTTEEQMALVSVKAHKY 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 180 AAKawaggkfaaevvplkapGPDGTLREVTTDEtvrpgttpeilaglkpafraDVWEQRFpeLGWHVTAGNSSPINDGAA 259
Cdd:PRK12578 174 GAM-----------------NPKAHFQKPVTVE--------------------EVLKSRA--ISWPIKLLDSCPISDGSA 214
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 260 AVLITSSETAAALGLKPRARIHSFAVAGDDPlYM--------LTGVVPATRKVLARAGLEVSDIDAFEVNEAF------- 324
Cdd:PRK12578 215 TAIFASEEKVKELKIDSPVWITGIGYANDYA-YVarrgewvgFKATQLAARQAYNMAKVTPNDIEVATVHDAFtiaeimg 293
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 522136349 325 ------------ASVVLAWQAEIGADLAkVNVNGGAIALGHPLGGSGARLLTTLLSVLEQTGG 375
Cdd:PRK12578 294 yedlgftekgkgGKFIEEGQSEKGGKVG-VNLFGGLKAKGHPLGATGLSMIYEITKQLRDEAG 355
PRK08257 PRK08257
acetyl-CoA acetyltransferase; Validated
11-339 7.99e-10

acetyl-CoA acetyltransferase; Validated


Pssm-ID: 236204 [Multi-domain]  Cd Length: 498  Bit Score: 60.31  E-value: 7.99e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349  11 RTP--IGKG----KPNGTLSGVHPVDLHAHALRSLVERTGIDP--GRIDDVisGAVGQVGEQSMNTARWAALAAGLPesv 82
Cdd:PRK08257   4 RTPviVGVGqvteRPDDPAYGLEPVDLMAAAARAAAADAGADAvlEAIDSV--AVVNQLSWRYRDPPGLLAERLGAD--- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349  83 PAVTVDRQCG--SSQQAVHFAAQGVIAGAYDVVIASGVESMSRVpMGSQAAGRDP-FGPQVAARYPDGLV-------PQG 152
Cdd:PRK08257  79 PARTVYSPVGgnSPQRLVNEAALRIAAGEADVALVAGAEAQSTA-TKLRKAGEKLdWTPQDEGPLADRGGdprpmasPAE 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 153 ISAEL-------------IAAKWGLTRAQLDEFSAESHQRAAKAWAGGKFAAevvplkapgpdgTLREVTTDETVRPGtt 219
Cdd:PRK08257 158 LRHGLdrpvyvyplfenaLRAALGRSPEEHRAEMGELWAPFSAVAAKNPHAW------------IPRERSAEEIVTPT-- 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 220 peilaglkPAFRADVWEqrFPELGwhvtagNSSPINDGAAAVLITSSETAAALGLkPRAR---IHSFAVAGDDPLYML-- 294
Cdd:PRK08257 224 --------PDNRMIAWP--YTKLM------NANDMVDQGAAVLLTSVAKARRLGV-PEDRwvyLHGGADAHDPYDILErp 286
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 522136349 295 -----TGVVPATRKVLARAGLEVSDIDAFEVNEAFASVVLAWQAEIGADL 339
Cdd:PRK08257 287 dlhrsPAIRAAGRRALALAGLGIDDIDAFDLYSCFPSAVQVAARELGLDL 336
PTZ00455 PTZ00455
3-ketoacyl-CoA thiolase; Provisional
83-390 8.22e-10

3-ketoacyl-CoA thiolase; Provisional


Pssm-ID: 240424 [Multi-domain]  Cd Length: 438  Bit Score: 60.29  E-value: 8.22e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349  83 PAVTVDRQCGSSQQAVHFAAQGVIAGAYDVVIASGVESMSRVpmgSQAAGRDPFGPqvAARYPDGLVPQGISAELIAAKW 162
Cdd:PTZ00455 112 PAMRVEGACASGGLAVQSAWEALLAGTSDIALVVGVEVQTTV---SARVGGDYLAR--AADYRRQRKLDDFTFPCLFAKR 186
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 163 GLTRAQLDEFSAESHQR-AAKAWAGGKfaaevvplKAPGPDGTLREVTTDETVrpGTTPEilaglKPAFRADvweqrfPE 241
Cdd:PTZ00455 187 MKYIQEHGHFTMEDTARvAAKAYANGN--------KNPLAHMHTRKLSLEFCT--GASDK-----NPKFLGN------ET 245
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 242 LGWHVTAGNSSPINDGAAAVLITSSETAAALGLKPR----ARIHSFAVAG-------DDPLYMLTGVVpATRKVLARAGL 310
Cdd:PTZ00455 246 YKPFLRMTDCSQVSDGGAGLVLASEEGLQKMGLSPNdsrlVEIKSLACASgnlyedpPDATRMFTSRA-AAQKALSMAGV 324
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 311 EVSDIDAFEVNEAFA-SVVLAWQAEIGADLAK-----------------VNVNGGAIALGHPLGGSGARLLTTLLSVLEQ 372
Cdd:PTZ00455 325 KPSDLQVAEVHDCFTiAELLMYEALGIAEYGHakdlirngatalegripVNTGGGLLSFGHPVGATGVKQIMEVYRQMKG 404
                        330
                 ....*....|....*...
gi 522136349 373 TGGRYGLHTMCEAGGLAN 390
Cdd:PTZ00455 405 QCGEYQMKNIPALGATLN 422
PRK08256 PRK08256
lipid-transfer protein; Provisional
82-359 1.37e-08

lipid-transfer protein; Provisional


Pssm-ID: 181327 [Multi-domain]  Cd Length: 391  Bit Score: 56.06  E-value: 1.37e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349  82 VPAVTVDRQCGSSQQAVHFAAQGVIAGAYDVVIASGVESMSRVPMGSQAAGR----DPFGPQVAARYPDGLVPQ-----G 152
Cdd:PRK08256  71 IPIVNVNNNCSTGSTALFLARQAVRSGAADCALALGFEQMQPGALGSVWDDRpsplERFDKALAELQGFDPAPPalrmfG 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 153 ISAELIAAKWGLTRAQLDEFSAESHQRAAKawaggkfaaevvplkapGPDGTLREVTTDETVRpgTTPEILAGLkpafra 232
Cdd:PRK08256 151 GAGREHMEKYGTTAETFAKIGVKARRHAAN-----------------NPYAQFRDEYTLEDVL--ASPMIWGPL------ 205
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 233 dvweqrfpelgwhvTAGNSSPINDGAAAVLITSSETAAALGLKPRARIHSFAVAGD-----DPLYMLTGV-----VPATR 302
Cdd:PRK08256 206 --------------TRLQCCPPTCGAAAAIVCSEEFARKHGLDRAVEIVAQAMTTDtpstfDGRSMIDLVgydmtRAAAQ 271
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 522136349 303 KVLARAGLEVSDIDAFEVNEAFAS-VVLAWQA-----EIGAdlAK--------------VNVNGGAIALGHPLGGSG 359
Cdd:PRK08256 272 QVYEQAGIGPEDIDVVELHDCFSAnELLTYEAlglcpEGEA--EKfiddgdntyggrwvVNPSGGLLSKGHPLGATG 346
PRK07516 PRK07516
thiolase domain-containing protein;
1-359 1.57e-08

thiolase domain-containing protein;


Pssm-ID: 181013 [Multi-domain]  Cd Length: 389  Bit Score: 56.11  E-value: 1.57e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349   1 MTDAVIVDAVRTPIGKgkpngtLSGVHPVDLHAHALRSLVERTGIDPGRIDDVIsgaVGQvgeqsMNTARW-----AALA 75
Cdd:PRK07516   1 MMTASIVGWAHTPFGK------LDAETLESLIVRVAREALAHAGIAAGDVDGIF---LGH-----FNAGFSpqdfpASLV 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349  76 AGLPES---VPAVTVDRQCGSSQQAVHFAAQGVIAGAYDVVIASGVESMSRVP----------MGSQAAGRDP------- 135
Cdd:PRK07516  67 LQADPAlrfKPATRVENACATGSAAVYAALDAIEAGRARIVLVVGAEKMTATPtaevgdillgASYLKEEGDTpggfagv 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 136 FGpQVAARYPDGLVPQGISAELIAAKwgltraqldefsaeSHQRA-AKAWA------GGKFAAEVVPlKAPGPDGTLRev 208
Cdd:PRK07516 147 FG-RIAQAYFQRYGDQSDALAMIAAK--------------NHANGvANPYAqmrkdlGFEFCRTVSE-KNPLVAGPLR-- 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 209 ttdetvrpgttpeilaglkpafRADVweqrfpelgwhvtagnsSPINDGAAAVLITSSETAAALglkPRA-RIHSFAVAG 287
Cdd:PRK07516 209 ----------------------RTDC-----------------SLVSDGAAALVLADAETARAL---QRAvRFRARAHVN 246
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 288 D-------DPLYMlTGVVPATRKVLARAGLEVSDIDAFEVNEAFA--------SVVLAWQAEiGADLAK----------- 341
Cdd:PRK07516 247 DflplsrrDPLAF-EGPRRAWQRALAQAGVTLDDLSFVETHDCFTiaelieyeAMGLAPPGQ-GARAIRegwtakdgklp 324
                        410
                 ....*....|....*...
gi 522136349 342 VNVNGGAIALGHPLGGSG 359
Cdd:PRK07516 325 VNPSGGLKAKGHPIGATG 342
PRK07103 PRK07103
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
257-367 7.33e-04

polyketide beta-ketoacyl:acyl carrier protein synthase; Validated


Pssm-ID: 180839 [Multi-domain]  Cd Length: 410  Bit Score: 41.56  E-value: 7.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 257 GAAAVLITSSETAAALGLKPRARIHSFAVAGD---DPLYMLTGVVPATRKVLARAGLEVSDIDAfeVNEAFASVVLAWQA 333
Cdd:PRK07103 240 ACGAVVLESAESARRRGARPYAKLLGWSMRLDanrGPDPSLEGEMRVIRAALRRAGLGPEDIDY--VNPHGTGSPLGDET 317
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 522136349 334 EI----GADLAKVNVNGGAIALGHPLGGSGA-RLLTTLL 367
Cdd:PRK07103 318 ELaalfASGLAHAWINATKSLTGHGLSAAGIvELIATLL 356
PRK07855 PRK07855
lipid-transfer protein; Provisional
256-362 1.41e-03

lipid-transfer protein; Provisional


Pssm-ID: 181147 [Multi-domain]  Cd Length: 386  Bit Score: 40.35  E-value: 1.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 256 DGAAAVLITSSETAAALGLKPrARIHSFAVAGDDPLYMLT-------------GVVpaTRKVLARAGLEVSDIDAFEVNE 322
Cdd:PRK07855 217 DGAVALVVTSAERARDLKQRP-AVIKAAAQGSGADQYMMTsyyrdditglpemGLV--ARQLWAQSGLGPADIDTAILYD 293
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 522136349 323 AFASVVLaWQAE----IGADLAKVNVNGGAIALGH--PLGGSGARL 362
Cdd:PRK07855 294 HFTPFVL-MQLEelgfCGRGEAKDFIADGALELGGrlPINTHGGQL 338
PRK08313 PRK08313
thiolase domain-containing protein;
240-359 1.53e-03

thiolase domain-containing protein;


Pssm-ID: 181378 [Multi-domain]  Cd Length: 386  Bit Score: 40.48  E-value: 1.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522136349 240 PELGWHVTAGNSSPINDGAAAVLITSSETAAALGLKPRARIHSFAvAGDDPLYML-------TGVVPATRKVLARAGLE- 311
Cdd:PRK08313 194 QMLWDPIRFDETCPSSDGACAVVIGDEEAADAAAGRPVAWIHGTA-MRTEPLAFAgrdqvnpQAGRDAAAALWKAAGITd 272
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 522136349 312 -VSDIDAFEV-------------NEAFASVVLAWQA------EIGADLAkVNVNGGAIAlGHPLGGSG 359
Cdd:PRK08313 273 pRDEIDVAEIyvpfswfepmwleNLGFAPEGEGWKLteagetAIGGRLP-VNPSGGVLS-SNPIGASG 338
 
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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