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Conserved domains on  [gi|1060771814|ref|WP_069145568|]
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MULTISPECIES: acetyl-CoA C-acetyltransferase [Rhodococcus]

Protein Classification

acetyl-CoA C-acetyltransferase( domain architecture ID 11482136)

acetyl-CoA C-acetyltransferase catalyzes the condensation of two acetyl-CoA molecules to form acetoacetyl-CoA, essentially joining two two-carbon units together to create a four-carbon unit, with the release of a CoA molecule; this reaction is a key step in the synthesis of ketone bodies and fatty acid metabolism

CATH:  3.40.47.10
EC:  2.3.1.9
Gene Ontology:  GO:0003985
SCOP:  4000245

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK06205 PRK06205
acetyl-CoA C-acetyltransferase;
1-398 0e+00

acetyl-CoA C-acetyltransferase;


:

Pssm-ID: 235741 [Multi-domain]  Cd Length: 404  Bit Score: 665.15  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814   1 MKRAALVAPVRTAVGRFGGALRDVPAESLAATVVKETVRRSGIDPSRIDDVAMGQSYANSEAPCIGRWAALEAGLPISVA 80
Cdd:PRK06205    1 MRDAVICEPVRTPVGRFGGAFKDVPAEELAATVIRALVERTGIDPARIDDVIFGQGYPNGEAPAIGRVAALDAGLPVTVP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814  81 GFQTDRRCGTGLQAIVTAAMMVQTGAADVVLAGGVESMSGIEHYTTGARWGTKSGGLQLFDRLDRGRERSQPEwRFGRIS 160
Cdd:PRK06205   81 GMQLDRRCGSGLQAVITAAMQVQTGAADVVIAGGAESMSNVEFYTTDMRWGVRGGGVQLHDRLARGRETAGGR-RFPVPG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 161 GMIETAENVATRCGITREESDAFAVESHRKATLARESGRFDAEIVAVELTDRKGNVTQFRADEGIRPDTSLETLARLRAV 240
Cdd:PRK06205  160 GMIETAENLRREYGISREEQDALAVRSHQRAVAAQEAGRFDDEIVPVTVPQRKGDPTVVDRDEHPRADTTLESLAKLRPI 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 241 ----SEGGVVTAGNASQQNDAAAAMLVVAEDRLDELGLEPIGFLDSWAAAGCEPALMGLGPVAAVSKLFARTGAGFADFD 316
Cdd:PRK06205  240 mgkqDPEATVTAGNASGQNDAAAACLVTTEDKAEELGLRPLARLVSWAVAGVEPSRMGIGPVPATEKALARAGLTLDDID 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 317 LVELNEAFACQVLGVVKEWGF--EDLDRLNVNGSGISLGHPVGATGARMATTALHELGRRGGGKALLTMCIGGGQGMAAV 394
Cdd:PRK06205  320 LIELNEAFAAQVLAVLKEWGFgaDDEERLNVNGSGISLGHPVGATGGRILATLLRELQRRQARYGLETMCIGGGQGLAAV 399

                  ....
gi 1060771814 395 VESA 398
Cdd:PRK06205  400 FERV 403
 
Name Accession Description Interval E-value
PRK06205 PRK06205
acetyl-CoA C-acetyltransferase;
1-398 0e+00

acetyl-CoA C-acetyltransferase;


Pssm-ID: 235741 [Multi-domain]  Cd Length: 404  Bit Score: 665.15  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814   1 MKRAALVAPVRTAVGRFGGALRDVPAESLAATVVKETVRRSGIDPSRIDDVAMGQSYANSEAPCIGRWAALEAGLPISVA 80
Cdd:PRK06205    1 MRDAVICEPVRTPVGRFGGAFKDVPAEELAATVIRALVERTGIDPARIDDVIFGQGYPNGEAPAIGRVAALDAGLPVTVP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814  81 GFQTDRRCGTGLQAIVTAAMMVQTGAADVVLAGGVESMSGIEHYTTGARWGTKSGGLQLFDRLDRGRERSQPEwRFGRIS 160
Cdd:PRK06205   81 GMQLDRRCGSGLQAVITAAMQVQTGAADVVIAGGAESMSNVEFYTTDMRWGVRGGGVQLHDRLARGRETAGGR-RFPVPG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 161 GMIETAENVATRCGITREESDAFAVESHRKATLARESGRFDAEIVAVELTDRKGNVTQFRADEGIRPDTSLETLARLRAV 240
Cdd:PRK06205  160 GMIETAENLRREYGISREEQDALAVRSHQRAVAAQEAGRFDDEIVPVTVPQRKGDPTVVDRDEHPRADTTLESLAKLRPI 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 241 ----SEGGVVTAGNASQQNDAAAAMLVVAEDRLDELGLEPIGFLDSWAAAGCEPALMGLGPVAAVSKLFARTGAGFADFD 316
Cdd:PRK06205  240 mgkqDPEATVTAGNASGQNDAAAACLVTTEDKAEELGLRPLARLVSWAVAGVEPSRMGIGPVPATEKALARAGLTLDDID 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 317 LVELNEAFACQVLGVVKEWGF--EDLDRLNVNGSGISLGHPVGATGARMATTALHELGRRGGGKALLTMCIGGGQGMAAV 394
Cdd:PRK06205  320 LIELNEAFAAQVLAVLKEWGFgaDDEERLNVNGSGISLGHPVGATGGRILATLLRELQRRQARYGLETMCIGGGQGLAAV 399

                  ....
gi 1060771814 395 VESA 398
Cdd:PRK06205  400 FERV 403
PaaJ COG0183
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ...
1-396 1.11e-179

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: 504.99  E-value: 1.11e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814   1 MKRAALVAPVRTAVGRFGGALRDVPAESLAATVVKETVRRSGIDPSRIDDVAMGQSYANSEAPCIGRWAALEAGLPISVA 80
Cdd:COG0183     1 MREVVIVDAVRTPFGRFGGALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQAGQGQNPARQAALLAGLPESVP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814  81 GFQTDRRCGTGLQAIVTAAMMVQTGAADVVLAGGVESMSGIEHYTTGARWGTKSGGlQLFDRLDRGRErsqpEWRFGRIS 160
Cdd:COG0183    81 AVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMLLPKARWGYRMNA-KLVDPMINPGL----TDPYTGLS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 161 gMIETAENVATRCGITREESDAFAVESHRKATLARESGRFDAEIVAVELTDRKGNVTqFRADEGIRPDTSLETLARLRAV 240
Cdd:COG0183   156 -MGETAENVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVEVPDRKGEVV-VDRDEGPRPDTTLEKLAKLKPA 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 241 -SEGGVVTAGNASQQNDAAAAMLVVAEDRLDELGLEPIGFLDSWAAAGCEPALMGLGPVAAVSKLFARTGAGFADFDLVE 319
Cdd:COG0183   234 fKKDGTVTAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIGPVPATRKALARAGLTLDDIDLIE 313
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1060771814 320 LNEAFACQVLGVVKEWGFeDLDRLNVNGSGISLGHPVGATGARMATTALHELGRRGGGKALLTMCIGGGQGMAAVVE 396
Cdd:COG0183   314 INEAFAAQVLAVLRELGL-DPDKVNVNGGAIALGHPLGASGARILVTLLHELERRGGRYGLATMCIGGGQGIALIIE 389
thiolase cd00751
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ...
5-396 6.99e-174

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: 490.07  E-value: 6.99e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814   5 ALVAPVRTAVGRFGGALRDVPAESLAATVVKETVRRSGIDPSRIDDVAMGQSYANSEAPCIGRWAALEAGLPISVAGFQT 84
Cdd:cd00751     1 VIVSAVRTPIGRFGGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGEGQNPARQAALLAGLPESVPATTV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814  85 DRRCGTGLQAIVTAAMMVQTGAADVVLAGGVESMSGIEHYTTGARWGTKSGGLQLFDRLDRGRERSQPEWrfgrisGMIE 164
Cdd:cd00751    81 NRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGRLGLNTLDGMLDDGLTDPFTGL------SMGI 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 165 TAENVATRCGITREESDAFAVESHRKATLARESGRFDAEIVAVELTDRKGNVTqFRADEGIRPDTSLETLARLRAV-SEG 243
Cdd:cd00751   155 TAENVAEKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEVPGRKGPVV-VDRDEGPRPDTTLEKLAKLKPAfKKD 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 244 GVVTAGNASQQNDAAAAMLVVAEDRLDELGLEPIGFLDSWAAAGCEPALMGLGPVAAVSKLFARTGAGFADFDLVELNEA 323
Cdd:cd00751   234 GTVTAGNASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDIDLIEINEA 313
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1060771814 324 FACQVLGVVKEWGFeDLDRLNVNGSGISLGHPVGATGARMATTALHELGRRGGGKALLTMCIGGGQGMAAVVE 396
Cdd:cd00751   314 FAAQALACLKELGL-DPEKVNVNGGAIALGHPLGASGARIVVTLLHELKRRGGRYGLATMCIGGGQGAAMVIE 385
AcCoA-C-Actrans TIGR01930
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ...
7-396 5.19e-145

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: 417.01  E-value: 5.19e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814   7 VAPVRTAVGRFGGALRDVPAESLAATVVKETVRRSGIDPSRIDDVAMGQSYANSEAPCIGRWAALEAGLPISVAGFQTDR 86
Cdd:TIGR01930   2 VAAARTPIGKFGGSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLQAGEQQNIARQAALLAGLPESVPAYTVNR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814  87 RCGTGLQAIVTAAMMVQTGAADVVLAGGVESMSGIEHYTT-GARWGTKSGGLQLFDRLDRGRERSQPEWRfgrisgMIET 165
Cdd:TIGR01930  82 QCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGVPrSLRWGVKPGNAELEDARLKDLTDANTGLP------MGVT 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 166 AENVATRCGITREESDAFAVESHRKATLARESGRFDAEIVAVELTDRKGNVTqFRADEGIRPDTSLETLARLRAVS-EGG 244
Cdd:TIGR01930 156 AENLAKKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVTVKGRKGPVT-VSSDEGIRPNTTLEKLAKLKPAFdPDG 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 245 VVTAGNASQQNDAAAAMLVVAEDRLDELGLEPIGFLDSWAAAGCEPALMGLGPVAAVSKLFARTGAGFADFDLVELNEAF 324
Cdd:TIGR01930 235 TVTAGNSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALKKAGLSISDIDLFEINEAF 314
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1060771814 325 ACQVLGVVKEWGFeDLDRLNVNGSGISLGHPVGATGARMATTALHELGRRGGGKALLTMCIGGGQGMAAVVE 396
Cdd:TIGR01930 315 AAQVLACIKELGL-DLEKVNVNGGAIALGHPLGASGARIVTTLLHELKRRGGRYGLATMCIGGGQGAAVILE 385
Thiolase_N pfam00108
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
5-267 5.58e-71

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: 223.33  E-value: 5.58e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814   5 ALVAPVRTAVGRFGGALRDVPAESLAATVVKETVRRSGIDPSRIDDVAMGQSYANSEAPCIGRWAALEAGLPISVAGFQT 84
Cdd:pfam00108   2 VIVSAARTPFGSFGGSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQAGEGQNPARQAALKAGIPDSAPAVTI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814  85 DRRCGTGLQAIVTAAMMVQTGAADVVLAGGVESMSGIEHY-TTGARWGTKSGGLQLFDRLDRgrersQPEWRFGRISGMI 163
Cdd:pfam00108  82 NKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYAlPTDARSGLKHGDEKKHDLLIP-----DGLTDAFNGYHMG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 164 ETAENVATRCGITREESDAFAVESHRKATLARESGRFDAEIVAVELTDRKGnVTQFRADEGIRPDTSLETLARLR-AVSE 242
Cdd:pfam00108 157 LTAENVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDEIVPVTVKGRKG-KPTVDKDEGIRPPTTAEPLAKLKpAFDK 235
                         250       260
                  ....*....|....*....|....*
gi 1060771814 243 GGVVTAGNASQQNDAAAAMLVVAED 267
Cdd:pfam00108 236 EGTVTAGNASPINDGAAAVLLMSES 260
 
Name Accession Description Interval E-value
PRK06205 PRK06205
acetyl-CoA C-acetyltransferase;
1-398 0e+00

acetyl-CoA C-acetyltransferase;


Pssm-ID: 235741 [Multi-domain]  Cd Length: 404  Bit Score: 665.15  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814   1 MKRAALVAPVRTAVGRFGGALRDVPAESLAATVVKETVRRSGIDPSRIDDVAMGQSYANSEAPCIGRWAALEAGLPISVA 80
Cdd:PRK06205    1 MRDAVICEPVRTPVGRFGGAFKDVPAEELAATVIRALVERTGIDPARIDDVIFGQGYPNGEAPAIGRVAALDAGLPVTVP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814  81 GFQTDRRCGTGLQAIVTAAMMVQTGAADVVLAGGVESMSGIEHYTTGARWGTKSGGLQLFDRLDRGRERSQPEwRFGRIS 160
Cdd:PRK06205   81 GMQLDRRCGSGLQAVITAAMQVQTGAADVVIAGGAESMSNVEFYTTDMRWGVRGGGVQLHDRLARGRETAGGR-RFPVPG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 161 GMIETAENVATRCGITREESDAFAVESHRKATLARESGRFDAEIVAVELTDRKGNVTQFRADEGIRPDTSLETLARLRAV 240
Cdd:PRK06205  160 GMIETAENLRREYGISREEQDALAVRSHQRAVAAQEAGRFDDEIVPVTVPQRKGDPTVVDRDEHPRADTTLESLAKLRPI 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 241 ----SEGGVVTAGNASQQNDAAAAMLVVAEDRLDELGLEPIGFLDSWAAAGCEPALMGLGPVAAVSKLFARTGAGFADFD 316
Cdd:PRK06205  240 mgkqDPEATVTAGNASGQNDAAAACLVTTEDKAEELGLRPLARLVSWAVAGVEPSRMGIGPVPATEKALARAGLTLDDID 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 317 LVELNEAFACQVLGVVKEWGF--EDLDRLNVNGSGISLGHPVGATGARMATTALHELGRRGGGKALLTMCIGGGQGMAAV 394
Cdd:PRK06205  320 LIELNEAFAAQVLAVLKEWGFgaDDEERLNVNGSGISLGHPVGATGGRILATLLRELQRRQARYGLETMCIGGGQGLAAV 399

                  ....
gi 1060771814 395 VESA 398
Cdd:PRK06205  400 FERV 403
PaaJ COG0183
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ...
1-396 1.11e-179

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: 504.99  E-value: 1.11e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814   1 MKRAALVAPVRTAVGRFGGALRDVPAESLAATVVKETVRRSGIDPSRIDDVAMGQSYANSEAPCIGRWAALEAGLPISVA 80
Cdd:COG0183     1 MREVVIVDAVRTPFGRFGGALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQAGQGQNPARQAALLAGLPESVP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814  81 GFQTDRRCGTGLQAIVTAAMMVQTGAADVVLAGGVESMSGIEHYTTGARWGTKSGGlQLFDRLDRGRErsqpEWRFGRIS 160
Cdd:COG0183    81 AVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMLLPKARWGYRMNA-KLVDPMINPGL----TDPYTGLS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 161 gMIETAENVATRCGITREESDAFAVESHRKATLARESGRFDAEIVAVELTDRKGNVTqFRADEGIRPDTSLETLARLRAV 240
Cdd:COG0183   156 -MGETAENVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVEVPDRKGEVV-VDRDEGPRPDTTLEKLAKLKPA 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 241 -SEGGVVTAGNASQQNDAAAAMLVVAEDRLDELGLEPIGFLDSWAAAGCEPALMGLGPVAAVSKLFARTGAGFADFDLVE 319
Cdd:COG0183   234 fKKDGTVTAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIGPVPATRKALARAGLTLDDIDLIE 313
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1060771814 320 LNEAFACQVLGVVKEWGFeDLDRLNVNGSGISLGHPVGATGARMATTALHELGRRGGGKALLTMCIGGGQGMAAVVE 396
Cdd:COG0183   314 INEAFAAQVLAVLRELGL-DPDKVNVNGGAIALGHPLGASGARILVTLLHELERRGGRYGLATMCIGGGQGIALIIE 389
thiolase cd00751
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ...
5-396 6.99e-174

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: 490.07  E-value: 6.99e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814   5 ALVAPVRTAVGRFGGALRDVPAESLAATVVKETVRRSGIDPSRIDDVAMGQSYANSEAPCIGRWAALEAGLPISVAGFQT 84
Cdd:cd00751     1 VIVSAVRTPIGRFGGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGEGQNPARQAALLAGLPESVPATTV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814  85 DRRCGTGLQAIVTAAMMVQTGAADVVLAGGVESMSGIEHYTTGARWGTKSGGLQLFDRLDRGRERSQPEWrfgrisGMIE 164
Cdd:cd00751    81 NRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGRLGLNTLDGMLDDGLTDPFTGL------SMGI 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 165 TAENVATRCGITREESDAFAVESHRKATLARESGRFDAEIVAVELTDRKGNVTqFRADEGIRPDTSLETLARLRAV-SEG 243
Cdd:cd00751   155 TAENVAEKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEVPGRKGPVV-VDRDEGPRPDTTLEKLAKLKPAfKKD 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 244 GVVTAGNASQQNDAAAAMLVVAEDRLDELGLEPIGFLDSWAAAGCEPALMGLGPVAAVSKLFARTGAGFADFDLVELNEA 323
Cdd:cd00751   234 GTVTAGNASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDIDLIEINEA 313
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1060771814 324 FACQVLGVVKEWGFeDLDRLNVNGSGISLGHPVGATGARMATTALHELGRRGGGKALLTMCIGGGQGMAAVVE 396
Cdd:cd00751   314 FAAQALACLKELGL-DPEKVNVNGGAIALGHPLGASGARIVVTLLHELKRRGGRYGLATMCIGGGQGAAMVIE 385
PRK05790 PRK05790
putative acyltransferase; Provisional
1-396 1.48e-153

putative acyltransferase; Provisional


Pssm-ID: 180261 [Multi-domain]  Cd Length: 393  Bit Score: 438.82  E-value: 1.48e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814   1 MKRAALVAPVRTAVGRFGGALRDVPAESLAATVVKETVRRSGIDPSRIDDVAMGQSYANSEAPCIGRWAALEAGLPISVA 80
Cdd:PRK05790    1 MKDVVIVSAARTPIGKFGGALKDVSAVELGAIVIKAALERAGVPPEQVDEVIMGQVLQAGAGQNPARQAALKAGLPVEVP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814  81 GFQTDRRCGTGLQAIVTAAMMVQTGAADVVLAGGVESMSGIEHYTTGARWGTKSGGLQLFDRLDR-GRERSqpewrFGRI 159
Cdd:PRK05790   81 ALTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQESMSQAPHVLPGSRWGQKMGDVELVDTMIHdGLTDA-----FNGY 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 160 SgMIETAENVATRCGITREESDAFAVESHRKATLARESGRFDAEIVAVELTDRKGNVTQFRADEGIRPDTSLETLARLR- 238
Cdd:PRK05790  156 H-MGITAENLAEQYGITREEQDEFALASQQKAEAAIKAGRFKDEIVPVTIKQRKGDPVVVDTDEHPRPDTTAESLAKLRp 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 239 AVSEGGVVTAGNASQQNDAAAAMLVVAEDRLDELGLEPIGFLDSWAAAGCEPALMGLGPVAAVSKLFARTGAGFADFDLV 318
Cdd:PRK05790  235 AFDKDGTVTAGNASGINDGAAAVVVMSEAKAKELGLTPLARIVSYAVAGVDPAIMGIGPVPAIRKALEKAGWSLADLDLI 314
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1060771814 319 ELNEAFACQVLGVVKEWGFeDLDRLNVNGSGISLGHPVGATGARMATTALHELGRRGGGKALLTMCIGGGQGMAAVVE 396
Cdd:PRK05790  315 EINEAFAAQALAVEKELGL-DPEKVNVNGGAIALGHPIGASGARILVTLLHEMKRRGAKKGLATLCIGGGQGVALIVE 391
AcCoA-C-Actrans TIGR01930
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ...
7-396 5.19e-145

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: 417.01  E-value: 5.19e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814   7 VAPVRTAVGRFGGALRDVPAESLAATVVKETVRRSGIDPSRIDDVAMGQSYANSEAPCIGRWAALEAGLPISVAGFQTDR 86
Cdd:TIGR01930   2 VAAARTPIGKFGGSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLQAGEQQNIARQAALLAGLPESVPAYTVNR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814  87 RCGTGLQAIVTAAMMVQTGAADVVLAGGVESMSGIEHYTT-GARWGTKSGGLQLFDRLDRGRERSQPEWRfgrisgMIET 165
Cdd:TIGR01930  82 QCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGVPrSLRWGVKPGNAELEDARLKDLTDANTGLP------MGVT 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 166 AENVATRCGITREESDAFAVESHRKATLARESGRFDAEIVAVELTDRKGNVTqFRADEGIRPDTSLETLARLRAVS-EGG 244
Cdd:TIGR01930 156 AENLAKKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVTVKGRKGPVT-VSSDEGIRPNTTLEKLAKLKPAFdPDG 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 245 VVTAGNASQQNDAAAAMLVVAEDRLDELGLEPIGFLDSWAAAGCEPALMGLGPVAAVSKLFARTGAGFADFDLVELNEAF 324
Cdd:TIGR01930 235 TVTAGNSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALKKAGLSISDIDLFEINEAF 314
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1060771814 325 ACQVLGVVKEWGFeDLDRLNVNGSGISLGHPVGATGARMATTALHELGRRGGGKALLTMCIGGGQGMAAVVE 396
Cdd:TIGR01930 315 AAQVLACIKELGL-DLEKVNVNGGAIALGHPLGASGARIVTTLLHELKRRGGRYGLATMCIGGGQGAAVILE 385
PRK09051 PRK09051
beta-ketothiolase BktB;
1-396 1.89e-136

beta-ketothiolase BktB;


Pssm-ID: 181625 [Multi-domain]  Cd Length: 394  Bit Score: 395.48  E-value: 1.89e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814   1 MKRAALVAPVRTAVGRFGGALRDVPAESLAATVVKETVRRSGIDPSRIDDVAMGQSyANSEA--PCIGRWAALEAGLPIS 78
Cdd:PRK09051    2 MREVVVVSGVRTAIGTFGGSLKDVAPTDLGATVVREALARAGVDPDQVGHVVFGHV-IPTEPrdMYLSRVAAINAGVPQE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814  79 VAGFQTDRRCGTGLQAIVTAAMMVQTGAADVVLAGGVESMSGIEHYTTGARWGTKSGGLQLFDRLDRGRerSQPewrFGR 158
Cdd:PRK09051   81 TPAFNVNRLCGSGLQAIVSAAQAILLGDADVAIGGGAESMSRAPYLLPAARWGARMGDAKLVDMMVGAL--HDP---FGT 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 159 ISgMIETAENVATRCGITREESDAFAVESHRKATLARESGRFDAEIVAVELTDRKGNVtQFRADEGIRPDTSLETLARLR 238
Cdd:PRK09051  156 IH-MGVTAENVAAKYGISREAQDALALESHRRAAAAIAAGYFKDQIVPVEIKTRKGEV-VFDTDEHVRADTTLEDLAKLK 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 239 AV--SEGGVVTAGNASQQNDAAAAMLVVAEDRLDELGLEPIGFLDSWAAAGCEPALMGLGPVAAVSKLFARTGAGFADFD 316
Cdd:PRK09051  234 PVfkKENGTVTAGNASGINDGAAAVVLAEADAAEARGLKPLARLVGYAHAGVDPEYMGIGPVPATQKALERAGLTVADLD 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 317 LVELNEAFACQVLGVVKEWGFeDLDRLNVNGSGISLGHPVGATGARMATTALHELGRRGGGKALLTMCIGGGQGMAAVVE 396
Cdd:PRK09051  314 VIEANEAFAAQACAVTRELGL-DPAKVNPNGSGISLGHPVGATGAIITVKALYELQRIGGRYALVTMCIGGGQGIAAIFE 392
PRK09050 PRK09050
beta-ketoadipyl CoA thiolase; Validated
1-396 5.44e-115

beta-ketoadipyl CoA thiolase; Validated


Pssm-ID: 181624 [Multi-domain]  Cd Length: 401  Bit Score: 341.16  E-value: 5.44e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814   1 MKRAALVAPVRTAVGRFGGALRDVPAESLAATVVKETV-RRSGIDPSRIDDVAMG-QSYANSEAPCIGRWAALEAGLPIS 78
Cdd:PRK09050    1 MTEAFICDAIRTPIGRYGGALSSVRADDLGAVPLKALMaRNPGVDWEAVDDVIYGcANQAGEDNRNVARMSALLAGLPVS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814  79 VAGFQTDRRCGTGLQAIVTAAMMVQTGAADVVLAGGVESMSGIEhYTTGARWGTKSGGLQLFDrldrgrerSQPEWRFGR 158
Cdd:PRK09050   81 VPGTTINRLCGSGMDAVGTAARAIKAGEAELMIAGGVESMSRAP-FVMGKADSAFSRQAEIFD--------TTIGWRFVN 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 159 --------ISGMIETAENVATRCGITREESDAFAVESHRKATLARESGRFDAEIVAVELTDRKGNVTQFRADEGIRPDTS 230
Cdd:PRK09050  152 plmkaqygVDSMPETAENVAEDYNISRADQDAFALRSQQRAAAAQAAGFLAEEIVPVTIPQKKGDPVVVDRDEHPRPETT 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 231 LETLARLRAV-SEGGVVTAGNASQQNDAAAAMLVVAEDRLDELGLEPIGFLDSWAAAGCEPALMGLGPVAAVSKLFARTG 309
Cdd:PRK09050  232 LEALAKLKPVfRPDGTVTAGNASGVNDGAAALLLASEAAAKKHGLTPRARILGMATAGVEPRIMGIGPAPATRKLLARLG 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 310 AGFADFDLVELNEAFACQVLGVVKEWGF-EDLDRLNVNGSGISLGHPVGATGARMATTALHELGRRGGGKALLTMCIGGG 388
Cdd:PRK09050  312 LTIDQFDVIELNEAFAAQGLAVLRQLGLaDDDARVNPNGGAIALGHPLGMSGARLVLTALHQLERTGGRYALCTMCIGVG 391

                  ....*...
gi 1060771814 389 QGMAAVVE 396
Cdd:PRK09050  392 QGIALAIE 399
pcaF TIGR02430
3-oxoadipyl-CoA thiolase; Members of this family are designated beta-ketoadipyl CoA thiolase, ...
2-396 2.59e-107

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: 321.35  E-value: 2.59e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814   2 KRAALVAPVRTAVGRFGGALRDVPAESLAATVVKETV-RRSGIDPSRIDDVAMG-QSYANSEAPCIGRWAALEAGLPISV 79
Cdd:TIGR02430   1 REAYICDAIRTPIGRYGGSLSSVRADDLAAVPIKALLaRNPQLDWAAIDDVIYGcANQAGEDNRNVARMAALLAGLPVSV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814  80 AGFQTDRRCGTGLQAIVTAAMMVQTGAADVVLAGGVESMSGIEhYTTGARWGTKSGGLQLFDrldrgrerSQPEWRFGR- 158
Cdd:TIGR02430  81 PGTTVNRLCGSGLDAIGMAARAIKAGEADLLIAGGVESMSRAP-FVMGKADSAFSRSAKIED--------TTIGWRFINp 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 159 -------ISGMIETAENVATRCGITREESDAFAVESHRKATLARESGRFDAEIVAVELTDRKGNVTQFRADEGIRPDTSL 231
Cdd:TIGR02430 152 lmkalygVDSMPETAENVAEEFGISREDQDAFALRSQQRTAAAQASGFFAEEIVPVVIPQKKGEPTVVDQDEHPRPETTL 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 232 ETLARLRAV-SEGGVVTAGNASQQNDAAAAMLVVAEDRLDELGLEPIGFLDSWAAAGCEPALMGLGPVAAVSKLFARTGA 310
Cdd:TIGR02430 232 EGLAKLKPVvRPDGTVTAGNASGVNDGAAALLLASEEAVQRHGLTPRARILAAATAGVEPRIMGIGPVPATQKLLARAGL 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 311 GFADFDLVELNEAFACQVLGVVKEWGFEDLD-RLNVNGSGISLGHPVGATGARMATTALHELGRRGGGKALLTMCIGGGQ 389
Cdd:TIGR02430 312 SIDQFDVIELNEAFAAQALAVLRELGLADDDaRVNPNGGAIALGHPLGASGARLVLTALRQLERSGGRYALCTMCIGVGQ 391

                  ....*..
gi 1060771814 390 GMAAVVE 396
Cdd:TIGR02430 392 GIALAIE 398
fadA PRK08947
3-ketoacyl-CoA thiolase; Reviewed
1-396 8.80e-107

3-ketoacyl-CoA thiolase; Reviewed


Pssm-ID: 181592 [Multi-domain]  Cd Length: 387  Bit Score: 319.60  E-value: 8.80e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814   1 MKRAALVAPVRTAVGRF-GGALRDVPAESLAATVVKETVRRS-GIDPSRIDDVAMG-------QSYAnseapcIGRWAAL 71
Cdd:PRK08947    1 MEDVVIVDAIRTPMGRSkGGAFRNVRAEDLSAHLMRSLLARNpALDPAEIDDIIWGcvqqtleQGFN------IARNAAL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814  72 EAGLPISVAGFQTDRRCGTGLQAIVTAAMMVQTGAADVVLAGGVESMS------GIEHYTTGARWGTKSGGLqlfdrldr 145
Cdd:PRK08947   75 LAGIPHSVPAVTVNRLCGSSMQALHDAARAIMTGDGDVFLIGGVEHMGhvpmnhGVDFHPGLSKNVAKAAGM-------- 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 146 grersqpewrfgrisgMIETAENVATRCGITREESDAFAVESHRKATLARESGRFDAEIVAVELTDRKGNVTQFRADEGI 225
Cdd:PRK08947  147 ----------------MGLTAEMLGKMHGISREQQDAFAARSHQRAWAATQEGRFKNEIIPTEGHDADGVLKLFDYDEVI 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 226 RPDTSLETLARLRAVSE--GGVVTAGNASQQNDAAAAMLVVAEDRLDELGLEPIGFLDSWAAAGCEPALMGLGPVAAVSK 303
Cdd:PRK08947  211 RPETTVEALAALRPAFDpvNGTVTAGTSSALSDGASAMLVMSESRAKELGLKPRARIRSMAVAGCDPSIMGYGPVPATQK 290
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 304 LFARTGAGFADFDLVELNEAFACQVLGVVKEWGFEDL--DRLNVNGSGISLGHPVGATGARMATTALHELGRRGGGKALL 381
Cdd:PRK08947  291 ALKRAGLSISDIDVFELNEAFAAQSLPCLKDLGLLDKmdEKVNLNGGAIALGHPLGCSGARISTTLLNLMERKDAQFGLA 370
                         410
                  ....*....|....*
gi 1060771814 382 TMCIGGGQGMAAVVE 396
Cdd:PRK08947  371 TMCIGLGQGIATVFE 385
PRK07661 PRK07661
acetyl-CoA C-acetyltransferase;
1-396 4.62e-103

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181072 [Multi-domain]  Cd Length: 391  Bit Score: 310.14  E-value: 4.62e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814   1 MKRAALVAPVRTAVGRFG-GALRDVPAESLAATVVKETVRRSGIDPSRIDDVAMGQSYANSEAPC-IGRWAALEAGLPIS 78
Cdd:PRK07661    1 MREAVIVAGARTPVGKAKkGSLKTVRPDDLGALVVKETLKRAGNYEGPIDDLIIGCAMPEAEQGLnMARNIGALAGLPYT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814  79 VAGFQTDRRCGTGLQAIVTAAMMVQTGAADVVLAGGVESMSGIehyttgarwgtKSGGLQLfdRLDRGRERSQPEWRFGr 158
Cdd:PRK07661   81 VPAITINRYCSSGLQSIAYGAERIMLGHSEAVIAGGAESMSLV-----------PMMGHVV--RPNPRLVEAAPEYYMG- 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 159 isgMIETAENVATRCGITREESDAFAVESHRKATLARESGRFDAEIVAVELTDRK----GNVTQ----FRADEGIRPDTS 230
Cdd:PRK07661  147 ---MGHTAEQVAVKYGISREDQDAFAVRSHQRAAKALAEGKFADEIVPVDVTLRTvgenNKLQEetitFSQDEGVRADTT 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 231 LETLARLR-AVSEGGVVTAGNASQQNDAAAAMLVVAEDRLDELGLEPIGFLDSWAAAGCEPALMGLGPVAAVSKLFARTG 309
Cdd:PRK07661  224 LEILGKLRpAFNVKGSVTAGNSSQMSDGAAAVLLMDREKAESDGLKPLAKFRSFAVAGVPPEVMGIGPIAAIPKALKLAG 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 310 AGFADFDLVELNEAFACQVLGVVKEWGFeDLDRLNVNGSGISLGHPVGATGARMATTALHELGRRGGGKALLTMCIGGGQ 389
Cdd:PRK07661  304 LELSDIGLFELNEAFASQSIQVIRELGL-DEEKVNVNGGAIALGHPLGCTGAKLTLSLIHEMKRRNEQFGIVTMCIGGGM 382

                  ....*..
gi 1060771814 390 GMAAVVE 396
Cdd:PRK07661  383 GAAGVFE 389
PRK05656 PRK05656
acetyl-CoA C-acetyltransferase;
1-396 3.39e-102

acetyl-CoA C-acetyltransferase;


Pssm-ID: 168156  Cd Length: 393  Bit Score: 308.36  E-value: 3.39e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814   1 MKRAALVAPVRTAVGRFGGALRDVPAESLAATVVKETVRRSGIDPSRIDDVAMGQSYANSEAPCIGRWAALEAGLPISVA 80
Cdd:PRK05656    1 MQDVVIVAATRTAIGSFQGSLANIPAVELGAAVIRRLLEQTGLDPAQVDEVILGQVLTAGAGQNPARQAAIKAGLPHSVP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814  81 GFQTDRRCGTGLQAIVTAAMMVQTGAADVVLAGGVESMSGIEHYTTGARWGTKSGGLQLFDRLdrgreRSQPEWRFGRIS 160
Cdd:PRK05656   81 AMTLNKVCGSGLKALHLAAQAIRCGDAEVIIAGGQENMSLAPYVLPGARTGLRMGHAQLVDSM-----ITDGLWDAFNDY 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 161 GMIETAENVATRCGITREESDAFAVESHRKATLARESGRFDAEIVAVELTDRKGNVTQFRADEGIRPDTSLETLARLR-A 239
Cdd:PRK05656  156 HMGITAENLVEKYGISREAQDAFAAASQQKAVAAIEAGRFDDEITPILIPQRKGEPLAFATDEQPRAGTTAESLAKLKpA 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 240 VSEGGVVTAGNASQQNDAAAAMLVVAEDRLDELGLEPIGFLDSWAAAGCEPALMGLGPVAAVSKLFARTGAGFADFDLVE 319
Cdd:PRK05656  236 FKKDGSVTAGNASSLNDGAAAVLLMSAAKAKALGLPVLAKIAAYANAGVDPAIMGIGPVSATRRCLDKAGWSLAELDLIE 315
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1060771814 320 LNEAFACQVLGVVKEWGFeDLDRLNVNGSGISLGHPVGATGARMATTALHELGRRGGGKALLTMCIGGGQGMAAVVE 396
Cdd:PRK05656  316 ANEAFAAQSLAVGKELGW-DAAKVNVNGGAIALGHPIGASGCRVLVTLLHEMIRRDAKKGLATLCIGGGQGVALAIE 391
PRK06633 PRK06633
acetyl-CoA C-acetyltransferase;
11-397 4.53e-101

acetyl-CoA C-acetyltransferase;


Pssm-ID: 168632 [Multi-domain]  Cd Length: 392  Bit Score: 305.42  E-value: 4.53e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814  11 RTAVGRFGGALRDVPAESLAATVVKETVRRSGIDPSRIDDVAMGQSYANSEAPCIGRWAALEAGLPISVAGFQTDRRCGT 90
Cdd:PRK06633   12 RTAFGSFMGSLSTTPAPMLAAHLIKDILQNSKIDPALVNEVILGQVITGGSGQNPARQTLIHAGIPKEVPGYTINKVCGS 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814  91 GLQAIVTAAMMVQTGAADVVLAGGVESMSgIEHYTTGARWGTKSGGLQLFDRLdrgrersQPEWRFGRISG--MIETAEN 168
Cdd:PRK06633   92 GLKSVALAANSIMTGDNEIVIAGGQENMS-LGMHGSYIRAGAKFGDIKMVDLM-------QYDGLTDVFSGvfMGITAEN 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 169 VATRCGITREESDAFAVESHRKATLARESGRFDAEIVAVELTDRKgNVTQFRADEGIRPDTSLETLARLR-AVSEGGVVT 247
Cdd:PRK06633  164 ISKQFNISRQEQDEFALSSHKKAAKAQLAGIFKDEILPIEVTIKK-TTSLFDHDETVRPDTSLEILSKLRpAFDKNGVVT 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 248 AGNASQQNDAAAAMLVVAEDRLDELGLEPIGFLDSWAAAGCEPALMGLGPVAAVSKLFARTGAGFADFDLVELNEAFACQ 327
Cdd:PRK06633  243 AGNASSINDGAACLMVVSEEALKKHNLTPLARIVSYASAGVDPSIMGTAPVPASQKALSKAGWSVNDLEVIEVNEAFAAQ 322
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 328 VLGVVKEWGFeDLDRLNVNGSGISLGHPVGATGARMATTALHELGRRGGGKALLTMCIGGGQGMAAVVES 397
Cdd:PRK06633  323 SIYVNREMKW-DMEKVNINGGAIAIGHPIGASGGRVLITLIHGLRRAKAKKGLVTLCIGGGMGMAMCVEA 391
PRK09052 PRK09052
acetyl-CoA C-acyltransferase;
1-396 7.61e-100

acetyl-CoA C-acyltransferase;


Pssm-ID: 181626 [Multi-domain]  Cd Length: 399  Bit Score: 302.31  E-value: 7.61e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814   1 MKRAALVAPVRTAVGRF-GGALRDVPAESLAATVVKETVRR-SGIDPSRIDDVAMGQSYANSEAPC-IGRWAALEAGLPI 77
Cdd:PRK09052    5 LQDAYIVAATRTPVGKApRGMFKNTRPDDLLAHVLRSAVAQvPGLDPKLIEDAIVGCAMPEAEQGLnVARIGALLAGLPN 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814  78 SVAGFQTDRRCGTGLQAIVTAAMMVQTGAADVVLAGGVESMSGIehyttgARWGTK-SGGLQLFDRldrgrersqpEWRF 156
Cdd:PRK09052   85 SVGGVTVNRFCASGLQAVAMAADRIRVGEADVMIAAGVESMSMV------PMMGNKpSMSPAIFAR----------DENV 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 157 GRISGMIETAENVATRCGITREESDAFAVESHRKATLARESGRFDAEIVAVELTDRK-----GNVTQFR----ADEGIRP 227
Cdd:PRK09052  149 GIAYGMGLTAEKVAEQWKVSREDQDAFALESHQKAIAAQQAGEFKDEITPYEITERFpdlatGEVDVKTrtvdLDEGPRA 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 228 DTSLETLARLRAV-SEGGVVTAGNASQQNDAAAAMLVVAEDRLDELGLEPIGFLDSWAAAGCEPALMGLGPVAAVSKLFA 306
Cdd:PRK09052  229 DTSLEGLAKLKPVfANKGSVTAGNSSQTSDGAGAVILVSEKALKQFNLTPLARFVSFAVAGVPPEIMGIGPIEAIPAALK 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 307 RTGAGFADFDLVELNEAFACQVLGVVKEWGFeDLDRLNVNGSGISLGHPVGATGARMATTALHELGRRGGGKALLTMCIG 386
Cdd:PRK09052  309 QAGLKQDDLDWIELNEAFAAQSLAVIRDLGL-DPSKVNPLGGAIALGHPLGATGAIRTATVVHGLRRTNLKYGMVTMCVG 387
                         410
                  ....*....|
gi 1060771814 387 GGQGMAAVVE 396
Cdd:PRK09052  388 TGMGAAGIFE 397
PRK08235 PRK08235
acetyl-CoA C-acetyltransferase;
1-396 8.22e-99

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181311 [Multi-domain]  Cd Length: 393  Bit Score: 299.32  E-value: 8.22e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814   1 MKRAALVAPVRTAVGRFGGALRDVPAESLAATVVKETVRRSGIDPSRIDDVAMGQSYANSEAPCIGRWAALEAGLPISVA 80
Cdd:PRK08235    1 MSKTVIVSAARTPFGKFGGSLKDVKATELGGIAIKEALERANVSAEDVEEVIMGTVLQGGQGQIPSRQAARAAGIPWEVQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814  81 GFQTDRRCGTGLQAIVTAAMMVQTGAADVVLAGGVESMSGIEHYTTGARWGTKSGGLQLFDrldrGRERSQPEWRFGRIS 160
Cdd:PRK08235   81 TETVNKVCASGLRAVTLADQIIRAGDASVIVAGGMESMSNAPYILPGARWGYRMGDNEVID----LMVADGLTCAFSGVH 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 161 gMIETAENVATRCGITREESDAFAVESHRKATLARESGRFDAEIVAVELTDRKGNVTQFRADEGIRPDTSLETLARLRAV 240
Cdd:PRK08235  157 -MGVYGGEVAKELGISREAQDEWAYRSHQRAVSAHEEGRFEEEIVPVTIPQRKGDPIVVAKDEAPRKDTTIEKLAKLKPV 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 241 SEG-GVVTAGNASQQNDAAAAMLVVAEDRLDELGLEPIGFLDSWAAAGCEPALMGLGPVAAVSKLFARTGAGFADFDLVE 319
Cdd:PRK08235  236 FDKtGTITAGNAPGVNDGAAALVLMSEDRAKQEGRKPLATILAHTAIAVEAKDFPRTPGYAINALLEKTGKTVEDIDLFE 315
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1060771814 320 LNEAFACQVLGVVKEWGFeDLDRLNVNGSGISLGHPVGATGARMATTALHELGRRGGGKALLTMCIGGGQGMAAVVE 396
Cdd:PRK08235  316 INEAFAAVALASTEIAGI-DPEKVNVNGGAVALGHPIGASGARIIVTLIHELKRRGGGIGIAAICSGGGQGDAVLIE 391
PRK07108 PRK07108
acetyl-CoA C-acyltransferase;
1-396 4.88e-98

acetyl-CoA C-acyltransferase;


Pssm-ID: 180843 [Multi-domain]  Cd Length: 392  Bit Score: 297.45  E-value: 4.88e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814   1 MKRAALVAPVRTAVGR-FGGALRDVPAESLAATVVKETVRRSGIDPSRIDDVAMGqsYANSEAPC---IGRWAALEAGLP 76
Cdd:PRK07108    1 MTEAVIVSTARTPLAKsWRGAFNMTHGATLGGHVVQHAVERAKLDPAEVEDVIMG--CANPEGATganIARQIALRAGLP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814  77 ISVAGFQTDRRCGTGLQAIVTAAMMVQTGAADVVLAGGVESMSGIE----HYTTGARWGTKSgglqlfdrldrgrersQP 152
Cdd:PRK07108   79 VTVPGMTVNRFCSSGLQTIALAAQRVIAGEGDVFVAGGVESISCVQnemnRHMLREGWLVEH----------------KP 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 153 E--WrfgrisGMIETAENVATRCGITREESDAFAVESHRKATLARESGRFDAEIVAV------------ELTDRKGNVTq 218
Cdd:PRK07108  143 EiyW------SMLQTAENVAKRYGISKERQDEYGVQSQQRAAAAQAAGRFDDEIVPItvtagvadkatgRLFTKEVTVS- 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 219 frADEGIRPDTSLETLARLRAVSEGGVVTAGNASQQNDAAAAMLVVAEDRLDELGLEPIGFLDSWAAAGCEPALMGLGPV 298
Cdd:PRK07108  216 --ADEGIRPDTTLEGVSKIRSALPGGVITAGNASQFSDGASACVVMNAKVAEREGLQPLGIFRGFAVAGCEPDEMGIGPV 293
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 299 AAVSKLFARTGAGFADFDLVELNEAFACQVLGVVKEWGFeDLDRLNVNGSGISLGHPVGATGARMATTALHELGRRGGGK 378
Cdd:PRK07108  294 FAVPKLLKQAGLKVDDIDLWELNEAFAVQVLYCRDTLGI-PMDRLNVNGGAIAVGHPYGVSGARLTGHALIEGKRRGAKY 372
                         410
                  ....*....|....*...
gi 1060771814 379 ALLTMCIGGGQGMAAVVE 396
Cdd:PRK07108  373 VVVTMCIGGGQGAAGLFE 390
PRK07801 PRK07801
acetyl-CoA C-acetyltransferase;
1-396 2.12e-96

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181123 [Multi-domain]  Cd Length: 382  Bit Score: 292.77  E-value: 2.12e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814   1 MKRAALVAPVRTAVGRFGGALRDVPAESLAATVVKETVRRSGIDPSRIDDVAMG-QSYANSEAPCIGRWAALEAGLPISV 79
Cdd:PRK07801    1 MAEAYIVDAVRTPVGKRKGGLAGVHPADLGAHVLKGLVDRTGIDPAAVDDVIFGcVDTIGPQAGNIARTSWLAAGLPEEV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814  80 AGFQTDRRCGTGLQAIVTAAMMVQTGAADVVLAGGVESMSGI---EHYTTGARWG--TKSGGLQLFdrldRGRERSQPEW 154
Cdd:PRK07801   81 PGVTVDRQCGSSQQAIHFAAQAVMSGTQDLVVAGGVQNMSQIpisSAMTAGEQLGftSPFAESKGW----LHRYGDQEVS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 155 RFgrisgmiETAENVATRCGITREESDAFAVESHRKATLARESGRFDAEIVAVEltdrkgnvtQFRADEGIRpDTSLETL 234
Cdd:PRK07801  157 QF-------RGAELIAEKWGISREEMERFALESHRRAFAAIRAGRFDNEIVPVG---------GVTVDEGPR-ETSLEKM 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 235 ARLRAVSEGGVVTAGNASQQNDAAAAMLVVAEDRLDELGLEPIGFLDSWAAAGCEPALMGLGPVAAVSKLFARTGAGFAD 314
Cdd:PRK07801  220 AGLKPLVEGGRLTAAVASQISDGASAVLLASERAVKRHGLTPRARIHHLSVRGDDPVFMLTAPIPATRYALEKTGLSIDD 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 315 FDLVELNEAFACQVLGVVKEWGFeDLDRLNVNGSGISLGHPVGATGARMATTALHELGRRGGGKALLTMCIGGGQGMAAV 394
Cdd:PRK07801  300 IDVVEINEAFAPVVLAWLKETGA-DPAKVNPNGGAIALGHPLGATGAKLMTTLLHELERTGGRYGLQTMCEGGGTANVTI 378

                  ..
gi 1060771814 395 VE 396
Cdd:PRK07801  379 IE 380
PRK08131 PRK08131
3-oxoadipyl-CoA thiolase;
1-396 7.48e-96

3-oxoadipyl-CoA thiolase;


Pssm-ID: 181242 [Multi-domain]  Cd Length: 401  Bit Score: 292.07  E-value: 7.48e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814   1 MKRAALVAPVRTAVGRFGGALRDVPAESLAATVVKETVRRSGIDPSRIDDVAMGQS-YANSEAPCIGRWAALEAGLPISV 79
Cdd:PRK08131    1 MLDAYIYDGLRSPFGRHAGALASVRPDDLAATVIRRLLEKSGFPGDDIEDVILGCTnQAGEDSRNVARNALLLAGLPVTV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814  80 AGFQTDRRCGTGLQAIVTAAMMVQTGAADVVLAGGVESMSGIEhYTTGARWGTKSGGLQLFDRLDRGR-ERSQPEWRFGR 158
Cdd:PRK08131   81 PGQTVNRLCASGLAAVIDAARAITCGEGDLYLAGGVESMSRAP-FVMGKAESAFSRDAKVFDTTIGARfPNPKIVAQYGN 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 159 ISgMIETAENVATRCGITREESDAFAVESHRKATLARESGRFDAEIVAVEL-TDRKGNVTQFRADEGIRPDTSLETLARL 237
Cdd:PRK08131  160 DS-MPETGDNVAAEFGISREDADRFAAQSQAKYQAAKEEGFFADEITPIEVpQGRKLPPKLVAEDEHPRPSSTVEALTKL 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 238 RAVSEGGVVTAGNASQQNDAAAAMLVVAEDRLDELGLEPIGFLDSWAAAGCEPALMGLGPVAAVSKLFARTGAGFADFDL 317
Cdd:PRK08131  239 KPLFEGGVVTAGNASGINDGAAALLIGSRAAGEKYGLKPMARILSSAAAGVEPRIMGIGPVEAIKKALARAGLTLDDMDI 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 318 VELNEAFACQVLGVVKEWGFE-DLDRLNVNGSGISLGHPVGATGARMATTALHELGRRGGGKALLTMCIGGGQGMAAVVE 396
Cdd:PRK08131  319 IEINEAFASQVLGCLKGLGVDfDDPRVNPNGGAIAVGHPLGASGARLALTAARELQRRGKRYAVVSLCIGVGQGLAMVIE 398
PRK06504 PRK06504
acetyl-CoA C-acetyltransferase;
1-396 2.21e-95

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180595 [Multi-domain]  Cd Length: 390  Bit Score: 290.48  E-value: 2.21e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814   1 MKRAALVAPVRTAVGRFGGALRDVPAESLAATVVKETVRRSGIDPSRIDDVAMG-QSYANSEAPCIGRWAALEAGLPISV 79
Cdd:PRK06504    1 MAEAYIVAAARTAGGRKGGRLAGWHPADLAAQVLDALVDRSGADPALIEDVIMGcVSQVGEQATNVARNAVLASKLPESV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814  80 AGFQTDRRCGTGLQAIVTAAMMVQTGAADVVLAGGVESMSGIEHYTTGArWGTKSGglqLFDRLDRGRERSQPEWRFGRI 159
Cdd:PRK06504   81 PGTSIDRQCGSSQQALHFAAQAVMSGTMDIVIAAGVESMTRVPMGSPST-LPAKNG---LGHYKSPGMEERYPGIQFSQF 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 160 SGmietAENVATRCGITREESDAFAVESHRKATLARESGRFDAEIVAVELTDRKGNVTQFRADEGIRPDTSLETLARLRA 239
Cdd:PRK06504  157 TG----AEMMAKKYGLSKDQLDEFALQSHQRAIAATQAGKFKAEIVPLEITRADGSGEMHTVDEGIRFDATLEGIAGVKL 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 240 VSEGGVVTAGNASQQNDAAAAMLVVAEDRLDELGLEPIGFLDSWAAAGCEPALMGLGPVAAVSKLFARTGAGFADFDLVE 319
Cdd:PRK06504  233 IAEGGRLTAATASQICDGASGVMVVNERGLKALGVKPLARIHHMTVIGGDPVIMLEAPLPATERALKKAGMKIDDIDLYE 312
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1060771814 320 LNEAFACQVLGVVKEWGfEDLDRLNVNGSGISLGHPVGATGARMATTALHELGRRGGGKALLTMCIGGGQGMAAVVE 396
Cdd:PRK06504  313 VNEAFASVPLAWLKATG-ADPERLNVNGGAIALGHPLGASGTKLMTTLVHALKQRGKRYGLQTMCEGGGMANVTIVE 388
PLN02287 PLN02287
3-ketoacyl-CoA thiolase
6-396 3.73e-94

3-ketoacyl-CoA thiolase


Pssm-ID: 215161 [Multi-domain]  Cd Length: 452  Bit Score: 289.36  E-value: 3.73e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814   6 LVAPVRTAVGRFG-GALRDVPAESLAATVVKETVRRSGIDPSRIDDVAMGQSYANSEAPCIG-RWAALEAGLPISVAGFQ 83
Cdd:PLN02287   50 IVAAYRTPICKAKrGGFKDTYPDDLLAPVLKAVVEKTGLNPSEVGDIVVGTVLAPGSQRANEcRMAAFYAGFPETVPVRT 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814  84 TDRRCGTGLQAIVTAAMMVQTGAADVVLAGGVESMSgiehyTTGARW-GTKSGGLQLFDRldrGRERSQPewrfgrisgM 162
Cdd:PLN02287  130 VNRQCSSGLQAVADVAAAIKAGFYDIGIGAGVESMT-----TNPMAWeGGVNPRVESFSQ---AQDCLLP---------M 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 163 IETAENVATRCGITREESDAFAVESHRKATLARESGRFDAEIVAV--ELTDRK-GNVTQF--RADEGIRPDTSLETLARL 237
Cdd:PLN02287  193 GITSENVAERFGVTREEQDQAAVESHRKAAAATASGKFKDEIVPVhtKIVDPKtGEEKPIviSVDDGIRPNTTLADLAKL 272
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 238 RAV-SEGGVVTAGNASQQNDAAAAMLVVAEDRLDELGLEPIGFLDSWAAAGCEPALMGLGPVAAVSKLFARTGAGFADFD 316
Cdd:PLN02287  273 KPVfKKNGTTTAGNSSQVSDGAGAVLLMKRSVAMQKGLPILGVFRSFAAVGVDPAVMGIGPAVAIPAAVKAAGLELDDID 352
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 317 LVELNEAFACQVLGVVKEWGFeDLDRLNVNGSGISLGHPVGATGARMATTALHELGRRGGGK--ALLTMCIGGGQGMAAV 394
Cdd:PLN02287  353 LFEINEAFASQFVYCCKKLGL-DPEKVNVNGGAIALGHPLGATGARCVATLLHEMKRRGKDCrfGVVSMCIGTGMGAAAV 431

                  ..
gi 1060771814 395 VE 396
Cdd:PLN02287  432 FE 433
PRK08242 PRK08242
acetyl-CoA C-acetyltransferase;
10-396 1.20e-91

acetyl-CoA C-acetyltransferase;


Pssm-ID: 236197 [Multi-domain]  Cd Length: 402  Bit Score: 281.39  E-value: 1.20e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814  10 VRTAVGRF--GGALRDVPAESLAATVVKETVRRSGIDPSRIDDVAMG-QSYANSEAPCIGRWAALEAGLPISVAGFQTDR 86
Cdd:PRK08242   10 VRTPRGKGkkDGSLHEVKPVRLAAGLLEALRDRNGLDTAAVDDVVLGcVTPVGDQGADIARTAVLAAGLPETVPGVQINR 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814  87 RCGTGLQAIVTAAMMVQTGAADVVLAGGVESMSGIEHYTTGARWGTksgglqlfdrldrgrersQPEWRFGriSGMIE-- 164
Cdd:PRK08242   90 FCASGLEAVNLAAAKVRSGWDDLVIAGGVESMSRVPMGSDGGAWAM------------------DPSTNFP--TYFVPqg 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 165 -TAENVATRCGITREESDAFAVESHRKATLARESGRFDAEIVAVelTDRKGnVTQFRADEGIRPDTSLETLARLRAVSE- 242
Cdd:PRK08242  150 iSADLIATKYGFSREDVDAYAVESQQRAAAAWAEGYFAKSVVPV--KDQNG-LTILDHDEHMRPGTTMESLAKLKPSFAm 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 243 ----GG-----------------VVTAGNASQQNDAAAAMLVVAEDRLDELGLEPIGFLDSWAAAGCEPALMGLGPVAAV 301
Cdd:PRK08242  227 mgemGGfdavalqkypeverinhVHHAGNSSGIVDGAAAVLIGSEEAGKALGLKPRARIVATATIGSDPTIMLTGPVPAT 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 302 SKLFARTGAGFADFDLVELNEAFACQVLGVVKEWGFeDLDRLNVNGSGISLGHPVGATGARMATTALHELGRRGGGKALL 381
Cdd:PRK08242  307 RKALAKAGLTVDDIDLFELNEAFASVVLRFMQALDI-PHDKVNVNGGAIAMGHPLGATGAMILGTVLDELERRGKRTALI 385
                         410
                  ....*....|....*
gi 1060771814 382 TMCIGGGQGMAAVVE 396
Cdd:PRK08242  386 TLCVGGGMGIATIIE 400
PRK06445 PRK06445
acetyl-CoA C-acetyltransferase;
1-396 7.80e-91

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180563 [Multi-domain]  Cd Length: 394  Bit Score: 278.91  E-value: 7.80e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814   1 MKRAALVAPVRTAVGRFG------GALRDVPAESLAATVVKETVRRSGIDPSRIDDVAMGQSYANSEA-PCIGRWAALEA 73
Cdd:PRK06445    1 LEDVYLVDFARTAFSRFRpkdpqkDVFNNIRPEELAAMLINRLIEKTGIKPEEIDDIITGCALQVGENwLYGGRHPIFLA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814  74 GLPISVAGFQTDRRCGTGLQAIVTAAMMVQTGAADVVLAGGVESMSGIEHYttgarwgtKSGGLQLFDRLDRGRERSQPE 153
Cdd:PRK06445   81 RLPYNIPAMAVDRQCASSLTTVSIGAMEIATGMADIVIAGGVEHMTRTPMG--------DNPHIEPNPKLLTDPKYIEYD 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 154 WRFGRISGMieTAENVATRCGITREESDAFAVESHRKATLARESGRFDAEIVAVElTDRKGNVTQFRADEGIRPDTSLET 233
Cdd:PRK06445  153 LTTGYVMGL--TAEKLAEEAGIKREEMDRWSLRSHQLAAKAIQEGYFKDEILPIE-VEVEGKKKVVDVDQSVRPDTSLEK 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 234 LARLR-AVSEGGVVTAGNASQQNDAAAAMLVVAEDRLDELGLEPIGFLDSWAAAGCEPALMGLGPVAAVSKLFARTGAGF 312
Cdd:PRK06445  230 LAKLPpAFKPDGVITAGNSSPLNSGASYVLLMSKKAVKKYGLKPMAKIRSFGFAGVPPAIMGKGPVPASKKALEKAGLSV 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 313 ADFDLVELNEAFACQVLGVVKEWGFeDLDRLNVNGSGISLGHPVGATGARMATTALHELGRRGGGKALLTMCIGGGQGMA 392
Cdd:PRK06445  310 KDIDLWEINEAFAVVVLYAIKELGL-DPETVNIKGGAIAIGHPLGATGARIVGTLARQLQIKGKDYGVATLCVGGGQGGA 388

                  ....
gi 1060771814 393 AVVE 396
Cdd:PRK06445  389 VVLE 392
fadA TIGR02445
fatty oxidation complex, beta subunit FadA; This subunit of the FadBA complex has acetyl-CoA ...
6-396 3.20e-90

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: 277.21  E-value: 3.20e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814   6 LVAPVRTAVGRF-GGALRDVPAESLAATVVKETV-RRSGIDPSRIDDVAMGQSYANSEAPC-IGRWAALEAGLPISVAGF 82
Cdd:TIGR02445   4 IVDFGRTPMGRSkGGAFRNTRAEDLSAHLMSKLLaRNPKVDPAEVEDIYWGCVQQTLEQGFnIARNAALLAQIPHTSAAV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814  83 QTDRRCGTGLQAIVTAAMMVQTGAADVVLAGGVESMS------GIEHYTTGARWGTKSGGLqlfdrldrgrersqpewrf 156
Cdd:TIGR02445  84 TVNRLCGSSMQALHDAARAIMTGDADVCLVGGVEHMGhvpmmhGVDFHPGMSLHVAKAAGM------------------- 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 157 grisgMIETAENVATRCGITREESDAFAVESHRKATLARESGRFDAEIVAVELTDRKGNVTQFRADEGIRPDTSLETLAR 236
Cdd:TIGR02445 145 -----MGLTAEMLGKMHGISREQQDAFAARSHARAHAATQEGKFKNEIIPTQGHDADGFLKQFDYDEVIRPETTVESLAA 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 237 LRAV--SEGGVVTAGNASQQNDAAAAMLVVAEDRLDELGLEPIGFLDSWAAAGCEPALMGLGPVAAVSKLFARTGAGFAD 314
Cdd:TIGR02445 220 LRPAfdPKNGTVTAGTSSALSDGASAMLVMSEQRANELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISD 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 315 FDLVELNEAFACQVLGVVKEWGFEDL--DRLNVNGSGISLGHPVGATGARMATTALHELGRRGGGKALLTMCIGGGQGMA 392
Cdd:TIGR02445 300 IDVFELNEAFAAQALPCLKDLGLLDKmdEKVNLNGGAIALGHPLGCSGARISTTLLNLMEQKDATFGLATMCIGLGQGIA 379

                  ....
gi 1060771814 393 AVVE 396
Cdd:TIGR02445 380 TVFE 383
PRK07851 PRK07851
acetyl-CoA C-acetyltransferase;
1-396 6.76e-90

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181146 [Multi-domain]  Cd Length: 406  Bit Score: 276.88  E-value: 6.76e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814   1 MKRAALVAPVRTAVGR-FGGALRDVPAESLAATVVKETVRR-SGIDPSRIDDVAMGQSYANSEAPC-IGRWAALEAGLPi 77
Cdd:PRK07851    1 MPEAVIVSTARSPIGRaFKGSLKDMRPDDLAAQMVRAALDKvPALDPTDIDDLMLGCGLPGGEQGFnMARVVAVLLGYD- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814  78 SVAGFQTDRRCGTGLQAIVTAAMMVQTGAADVVLAGGVESMSGiehYTTGARWGTKSGGLQLFD----RLDRGRERSQPE 153
Cdd:PRK07851   80 FLPGTTVNRYCSSSLQTTRMAFHAIKAGEGDVFISAGVETVSR---FAKGNSDSLPDTKNPLFAeaqaRTAARAEGGAEA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 154 WRFGRISG--------MIETAENVATRCGITREESDAFAVESHRKATLARESGRFDAEIVAVELTDrkGNVTqfRADEGI 225
Cdd:PRK07851  157 WHDPREDGllpdvyiaMGQTAENVAQLTGISREEQDEWGVRSQNRAEEAIANGFFEREITPVTLPD--GTVV--STDDGP 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 226 RPDTSLETLARLRAV-SEGGVVTAGNASQQNDAAAAMLVVAEDRLDELGLEPIGFLDSWAAAGCEPALMGLGPVAAVSKL 304
Cdd:PRK07851  233 RAGTTYEKVSQLKPVfRPDGTVTAGNACPLNDGAAAVVIMSDTKARELGLTPLARIVSTGVSGLSPEIMGLGPVEASKQA 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 305 FARTGAGFADFDLVELNEAFACQVLGVVKEWGFeDLDRLNVNGSGISLGHPVGATGARMATTALHELGRRGGGKALLTMC 384
Cdd:PRK07851  313 LARAGMSIDDIDLVEINEAFAAQVLPSARELGI-DEDKLNVSGGAIALGHPFGMTGARITTTLLNNLQTHDKTFGLETMC 391
                         410
                  ....*....|..
gi 1060771814 385 IGGGQGMAAVVE 396
Cdd:PRK07851  392 VGGGQGMAMVLE 403
fadI PRK08963
3-ketoacyl-CoA thiolase; Reviewed
3-398 9.29e-90

3-ketoacyl-CoA thiolase; Reviewed


Pssm-ID: 181597 [Multi-domain]  Cd Length: 428  Bit Score: 277.25  E-value: 9.29e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814   3 RAALVAPVRTAVGRFGGALRDVPAESLAATVVKETVRRSGIDPSRIDDVAMGQSYANSEAPCIGRWAALEAGLPISVAGF 82
Cdd:PRK08963    6 RIAIVSGLRTPFAKQATAFHGIPAVDLGKMVVGELLARSEIDPELIEQLVFGQVVQMPEAPNIAREIVLGTGMNVHTDAY 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814  83 QTDRRCGTGLQAIVTAAMMVQTGAADVVLAGGVESMSGIE-----------HYTTGARwgTKSGGLQLFDRLDRGRERSQ 151
Cdd:PRK08963   86 SVSRACATSFQAVANVAESIMAGTIDIGIAGGADSSSVLPigvskklaralVDLNKAR--TLGQRLKLFSRLRLRDLLPV 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 152 P----EWRFGRisGMIETAENVATRCGITREESDAFAVESHRKATLARESGRFDAEIVAVELTDRKgnvTQFRADEGIRP 227
Cdd:PRK08963  164 PpavaEYSTGL--RMGDTAEQMAKTYGISREEQDALAHRSHQLAAQAWAEGKLDDEVMTAHVPPYK---QPLEEDNNIRG 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 228 DTSLETLARLRAV--SEGGVVTAGNASQQNDAAAAMLVVAEDRLDELGLEPIGFLDSWAAAGCEPAL-MGLGPVAAVSKL 304
Cdd:PRK08963  239 DSTLEDYAKLRPAfdRKHGTVTAANSTPLTDGAAAVLLMSESRAKALGLTPLGYLRSYAFAAIDVWQdMLLGPAYATPLA 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 305 FARTGAGFADFDLVELNEAFACQVLGVVKEWGFE----------------DLDRLNVNGSGISLGHPVGATGARMATTAL 368
Cdd:PRK08963  319 LERAGLTLADLTLIDMHEAFAAQTLANLQMFASErfareklgrsqaigevDMSKFNVLGGSIAYGHPFAATGARMITQTL 398
                         410       420       430
                  ....*....|....*....|....*....|
gi 1060771814 369 HELGRRGGGKALLTMCIGGGQGMAAVVESA 398
Cdd:PRK08963  399 HELRRRGGGLGLTTACAAGGLGAAMVLEVE 428
PRK07850 PRK07850
steroid 3-ketoacyl-CoA thiolase;
1-396 7.78e-88

steroid 3-ketoacyl-CoA thiolase;


Pssm-ID: 181145 [Multi-domain]  Cd Length: 387  Bit Score: 271.21  E-value: 7.78e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814   1 MKRAALVAPVRTAVGRFGGALRDVPAESLAATVVKETVRRSGIDPSRIDDVAMG-QSYANSEAPCIGRWAALEAGLPISV 79
Cdd:PRK07850    1 MGNPVIVEAVRTPIGKRNGWLSGLHAAELLGAVQRAVLDRAGIDPGDVEQVIGGcVTQAGEQSNNITRTAWLHAGLPYHV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814  80 AGFQTDRRCGTGLQAIVTAAMMVQTGAADVVLAGGVESMSGIehyTTGARWGTksgglqlfdrlDRGRERSQpEWRFGrI 159
Cdd:PRK07850   81 GATTIDCQCGSAQQANHLVAGLIAAGAIDVGIACGVEAMSRV---PLGANAGP-----------GRGLPRPD-SWDID-M 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 160 SGMIETAENVATRCGITREESDAFAVESHRKATLARESGRFDAEIVAVE--LTDRKGNVTQFRA----DEGIRpDTSLET 233
Cdd:PRK07850  145 PNQFEAAERIAKRRGITREDVDAFGLRSQRRAAQAWAEGRFDREISPVQapVLDEEGQPTGETRlvtrDQGLR-DTTMEG 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 234 LARLRAVSEGGVVTAGNASQQNDAAAAMLVVAEDRLDELGLEPIGFLDSWAAAGCEPALMGLGPVAAVSKLFARTGAGFA 313
Cdd:PRK07850  224 LAGLKPVLEGGIHTAGTSSQISDGAAAVLWMDEDRARALGLRPRARIVAQALVGAEPYYHLDGPVQATAKVLEKAGMKIG 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 314 DFDLVELNEAFACQVLGVVKEWGfEDLDRLNVNGSGISLGHPVGATGARMATTALHELGRRGGGKALLTMCIGGGQGMAA 393
Cdd:PRK07850  304 DIDLVEINEAFASVVLSWAQVHE-PDMDKVNVNGGAIALGHPVGSTGARLITTALHELERTDKSTALITMCAGGALSTGT 382

                  ...
gi 1060771814 394 VVE 396
Cdd:PRK07850  383 IIE 385
PRK08170 PRK08170
acetyl-CoA C-acetyltransferase;
40-397 1.39e-86

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181265 [Multi-domain]  Cd Length: 426  Bit Score: 269.19  E-value: 1.39e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814  40 RSGIDPSRIDDVAMGQSYANSEAPCIGRWAALEAGLPISVAGFQTDRRCGTGLQAIVTAAMMVQTGAADVVLAGGVESMS 119
Cdd:PRK08170   41 RQPFAPDDLDEVILGCAMPSPDEANIARVVALRLGCGEKVPAWTVQRNCASGMQALDSAAANIALGRADLVLAGGVEAMS 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 120 --GIEHYTTGARW-----GTKSGGLQLfdrldrgreRSQPEWR-------FGRISG---------MIETAENVATRCGIT 176
Cdd:PRK08170  121 haPLLFSEKMVRWlagwyAAKSIGQKL---------AALGKLRpsylapvIGLLRGltdpvvglnMGQTAEVLAHRFGIT 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 177 REESDAFAVESHRKATLARESGRFdAEIVAveLTDRKGNVtqFRADEGIRPDTSLETLARLRAVSEG--GVVTAGNASQQ 254
Cdd:PRK08170  192 REQMDAYAARSHQRLAAAQAEGRL-KEVVP--LFDRDGKF--YDHDDGVRPDSSMEKLAKLKPFFDRpyGRVTAGNSSQI 266
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 255 NDAAAAMLVVAEDRLDELGLEPIGFLDSWAAAGCEPALMGLGPVAAVSKLFARTGAGFADFDLVELNEAFACQVLGVVKE 334
Cdd:PRK08170  267 TDGACWLLLASEEAVKKYGLPPLGRIVDSQWAALDPSQMGLGPVHAATPLLQRHGLTLEDLDLWEINEAFAAQVLACLAA 346
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1060771814 335 W----------------GFEDLDRLNVNGSGISLGHPVGATGARMATTALHELGRRGGGKALLTMCIGGGQGMAAVVES 397
Cdd:PRK08170  347 WadeeycreqlgldgalGELDRERLNVDGGAIALGHPVGASGARIVLHLLHALKRRGTKRGIAAICIGGGQGGAMLLER 425
PLN02644 PLN02644
acetyl-CoA C-acetyltransferase
6-396 1.41e-76

acetyl-CoA C-acetyltransferase


Pssm-ID: 215347 [Multi-domain]  Cd Length: 394  Bit Score: 242.31  E-value: 1.41e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814   6 LVAPVRTAVGRFGGALRDVPAESLAATVVKETVRRSGIDPSRIDDVAMGQ--SYANSEAPCigRWAALEAGLPISVAGFQ 83
Cdd:PLN02644    5 IVGVARTPIGGFLGSLSSLSATELGSIAIQAALERAGVDPALVQEVFFGNvlSANLGQAPA--RQAALGAGLPPSTICTT 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814  84 TDRRCGTGLQAIVTAAMMVQTGAADVVLAGGVESMSGIEHYTTGARWGTKSGGLQLFDRLDRgrersQPEWRFGRISGMI 163
Cdd:PLN02644   83 VNKVCASGMKAVMLAAQSIQLGINDVVVAGGMESMSNAPKYLPEARKGSRLGHDTVVDGMLK-----DGLWDVYNDFGMG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 164 ETAENVATRCGITREESDAFAVESHRKATLARESGRFDAEIVAVELTDRKGNVTQFRA-DEGIRpDTSLETLARLRAV-- 240
Cdd:PLN02644  158 VCAELCADQYSISREEQDAYAIQSYERAIAAQEAGAFAWEIVPVEVPGGRGRPSVIVDkDEGLG-KFDPAKLRKLRPSfk 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 241 SEGGVVTAGNASQQNDAAAAMLVVAEDRLDELGLEPIGFLDSWAAAGCEPALMGLGPVAAVSKLFARTGAGFADFDLVEL 320
Cdd:PLN02644  237 EDGGSVTAGNASSISDGAAALVLVSGEKALELGLQVIAKIRGYADAAQAPELFTTAPALAIPKALKHAGLEASQVDYYEI 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 321 NEAFA------CQVLGVvkewgfeDLDRLNVNGSGISLGHPVGATGARMATTALHELGRRGGGKALLTMCIGGGQGMAAV 394
Cdd:PLN02644  317 NEAFSvvalanQKLLGL-------DPEKVNVHGGAVSLGHPIGCSGARILVTLLGVLRSKNGKYGVAGICNGGGGASAIV 389

                  ..
gi 1060771814 395 VE 396
Cdd:PLN02644  390 VE 391
Thiolase_N pfam00108
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
5-267 5.58e-71

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: 223.33  E-value: 5.58e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814   5 ALVAPVRTAVGRFGGALRDVPAESLAATVVKETVRRSGIDPSRIDDVAMGQSYANSEAPCIGRWAALEAGLPISVAGFQT 84
Cdd:pfam00108   2 VIVSAARTPFGSFGGSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQAGEGQNPARQAALKAGIPDSAPAVTI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814  85 DRRCGTGLQAIVTAAMMVQTGAADVVLAGGVESMSGIEHY-TTGARWGTKSGGLQLFDRLDRgrersQPEWRFGRISGMI 163
Cdd:pfam00108  82 NKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYAlPTDARSGLKHGDEKKHDLLIP-----DGLTDAFNGYHMG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 164 ETAENVATRCGITREESDAFAVESHRKATLARESGRFDAEIVAVELTDRKGnVTQFRADEGIRPDTSLETLARLR-AVSE 242
Cdd:pfam00108 157 LTAENVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDEIVPVTVKGRKG-KPTVDKDEGIRPPTTAEPLAKLKpAFDK 235
                         250       260
                  ....*....|....*....|....*
gi 1060771814 243 GGVVTAGNASQQNDAAAAMLVVAED 267
Cdd:pfam00108 236 EGTVTAGNASPINDGAAAVLLMSES 260
PRK06954 PRK06954
acetyl-CoA C-acetyltransferase;
6-396 4.13e-68

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180775 [Multi-domain]  Cd Length: 397  Bit Score: 220.53  E-value: 4.13e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814   6 LVAPVRTAVGRFGGALRDVPAESLAATVVKETVRRSGIDPSRIDDVAMGQSYANSEAPCIGRWAALEAGLPISVAGFQTD 85
Cdd:PRK06954   11 IASAARTPMAAFQGEFASLTAPQLGAAAIAAAVERAGLKPEQIDEVVMGCVLPAGQGQAPARQAALGAGLPLSVGCTTVN 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814  86 RRCGTGLQAIVTAAMMVQTGAADVVLAGGVESMSGIEHYTTGARWGTKSGGLQLFDR--LDrGRERSqpeWRFGRISGMI 163
Cdd:PRK06954   91 KMCGSGMRAAMFAHDMLVAGSVDVIVAGGMESMTNAPYLLPKARGGMRMGHGQVLDHmfLD-GLEDA---YDKGRLMGTF 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 164 etAENVATRCGITREESDAFAVESHRKATLARESGRFDAEIVAVELTDRKGNVTQFRaDEGIRpDTSLETLARLR-AVSE 242
Cdd:PRK06954  167 --AEECAGEYGFTREAQDAFAIESLARAKRANEDGSFAWEIAPVTVAGKKGDTVIDR-DEQPF-KANPEKIPTLKpAFSK 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 243 GGVVTAGNASQQNDAAAAMLVVAEDRLDELGLEPIGFLDSWAAAGCEPALMGLGPVAAVSKLFARTGAGFADFDLVELNE 322
Cdd:PRK06954  243 TGTVTAANSSSISDGAAALVMMRASTAKRLGLAPLARVVGHSTFAQAPSKFTTAPVGAIRKLFEKNGWRAAEVDLFEINE 322
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1060771814 323 AFACQVLGVVKEWGFEDlDRLNVNGSGISLGHPVGATGARMATTALHELGRRGGGKALLTMCIGGGQGMAAVVE 396
Cdd:PRK06954  323 AFAVVTMAAMKEHGLPH-EKVNVNGGACALGHPIGASGARILVTLIGALRARGGKRGVASLCIGGGEATAMGIE 395
PRK06366 PRK06366
acetyl-CoA C-acetyltransferase;
1-396 8.14e-66

acetyl-CoA C-acetyltransferase;


Pssm-ID: 102340 [Multi-domain]  Cd Length: 388  Bit Score: 214.49  E-value: 8.14e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814   1 MKRAALVAPVRTAVGRFGGALRDVPAESLAATVVKETVRRSGIDPSRIDDVAMGQSYANSEAPCIGRWAALEAGLPISVA 80
Cdd:PRK06366    1 MKDVYIVSAKRTAIGKFGRSFSKIKAPQLGGAAIKAVIDDAKLDPALVQEVIMGNVIQAGVGQNPAGQAAYHAGLPFGVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814  81 GFQTDRRCGTGLQAIVTAAMMVQTGAADVVLAGGVESMSGIEHY-TTGARWGTKsgglQLfdrLDRGRERSQPEWRFGRI 159
Cdd:PRK06366   81 KYTVNVVCASGMLAVESAAREIMLGERDLVIAGGMENMSNAPFLlPSDLRWGPK----HL---LHKNYKIDDAMLVDGLI 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 160 SG-----MIETAENVATRCGITREESDAFAVESHRKATLARESGRFDAEIVAVELTDRkgnvtqfraDEGIRpDTSLETL 234
Cdd:PRK06366  154 DAfyfehMGVSAERTARKYGITREMADEYSVQSYERAIRATESGEFRNEIVPFNDLDR---------DEGIR-KTTMEDL 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 235 ARLR-AVSEGGVVTAGNASQQNDAAAAMLVVAEDRLDELGLEPIGFLDSWAAAGCEPALMGLGPVAAVSKLFARTGAGFA 313
Cdd:PRK06366  224 AKLPpAFDKNGILTAGNSAQLSDGGSALVMASEKAINEYGLKPIARITGYESASLDPLDFVEAPIPATRKLLEKQNKSID 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 314 DFDLVELNEAFACQVLgVVKEWGFEDLDRLNVNGSGISLGHPVGATGARMATTALHELGRRGGGKALLTMCIGGGQGMAA 393
Cdd:PRK06366  304 YYDLVEHNEAFSIASI-IVRDQLKIDNERFNVNGGAVAIGHPIGNSGSRIIVTLINALKTRHMKTGLATLCHGGGGAHTL 382

                  ...
gi 1060771814 394 VVE 396
Cdd:PRK06366  383 TLE 385
PRK06025 PRK06025
acetyl-CoA C-acetyltransferase;
1-396 1.73e-65

acetyl-CoA C-acetyltransferase;


Pssm-ID: 235675 [Multi-domain]  Cd Length: 417  Bit Score: 214.25  E-value: 1.73e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814   1 MKRAALVAPVRT--AVGRFG-GALRDVPAESLAATVVKETVRRSGIDPSRIDDVAMGQSYAN-SEAPCIGRWAALEAGLP 76
Cdd:PRK06025    1 MAEAYIIDAVRTprGIGKVGkGALAHLHPQHLAATVLKALAERNGLNTADVDDIIWSTSSQRgKQGGDLGRMAALDAGYD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814  77 ISVAGFQTDRRCGTGLQAIVTAAMMVQTGAADVVLAGGVESMSgiehYTTGARWGTKSGGLQLFdRLDRGRERSQ---PE 153
Cdd:PRK06025   81 IKASGVTLDRFCGGGITSVNLAAAQIMSGMEDLVIAGGTEMMS----YTAAMAAEDMAAGKPPL-GMGSGNLRLRalhPQ 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 154 WRFGRisgmieTAENVATRCGITREESDAFAVESHRKATLARESGRFDAEIVAVelTDRKGNVTqFRADEGIRPDTSLET 233
Cdd:PRK06025  156 SHQGV------CGDAIATMEGITREALDALGLESQRRAARAIKEGRFDKSLVPV--YRDDGSVA-LDHEEFPRPQTTAEG 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 234 LARLRA---------VSEGG------------------VVTAGNASQQNDAAAAMLVVAEDRLDELGLEPIGFLDSWAAA 286
Cdd:PRK06025  227 LAALKPaftaiadypLDDKGttyrglinqkypdleikhVHHAGNSSGVVDGAAALLLASKAYAEKHGLKPRARIVAMANM 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 287 GCEPALMGLGPVAAVSKLFARTGAGFADFDLVELNEAFAcqvlgVVKEWGFEDL----DRLNVNGSGISLGHPVGATGAR 362
Cdd:PRK06025  307 GDDPTLMLNAPVPAAKKVLAKAGLTKDDIDLWEINEAFA-----VVAEKFIRDLdldrDKVNVNGGAIALGHPIGATGSI 381
                         410       420       430
                  ....*....|....*....|....*....|....
gi 1060771814 363 MATTALHELGRRGGGKALLTMCIGGGQGMAAVVE 396
Cdd:PRK06025  382 LIGTVLDELERRGLKRGLVTMCAAGGMAPAIIIE 415
PRK06690 PRK06690
acetyl-CoA C-acyltransferase;
3-396 6.14e-62

acetyl-CoA C-acyltransferase;


Pssm-ID: 180659 [Multi-domain]  Cd Length: 361  Bit Score: 203.46  E-value: 6.14e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814   3 RAALVAPVRTAVGRFGGALRDVPAESLAATVVKETVRrsGIDPSrIDDVAMGQsyANSEAPCIGRWAALEAGLPISVAGF 82
Cdd:PRK06690    2 RAVIVEAKRTPIGKKNGMLKDYEVQQLAAPLLTFLSK--GMERE-IDDVILGN--VVGPGGNVARLSALEAGLGLHIPGV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814  83 QTDRRCGTGLQAIVTAAMMVQTGAADVVLAGGVESMSGIEHyttgarwgtksgglqlfdrldRGRERSQPEWrFGRISgM 162
Cdd:PRK06690   77 TIDRQCGAGLEAIRTACHFIQGGAGKCYIAGGVESTSTSPF---------------------QNRARFSPET-IGDPD-M 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 163 IETAENVATRCGITREESDAFAVESHRKATLARESGRFDAEIVAVeltdrkGNVtqfrADEGIRPDTSLETL-ARLRAV- 240
Cdd:PRK06690  134 GVAAEYVAERYNITREMQDEYACLSYKRTLQALEKGYIHEEILSF------NGL----LDESIKKEMNYERIiKRTKPAf 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 241 SEGGVVTAGNASQQNDAAAAMLVVAEDRLDELGLEPI-GFLDSwAAAGCEPALMGLGPVAAVSKLFARTGAGFADFDLVE 319
Cdd:PRK06690  204 LHNGTVTAGNSCGVNDGACAVLVMEEGQARKLGYKPVlRFVRS-AVVGVDPNLPGTGPIFAVNKLLNEMNMKVEDIDYFE 282
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1060771814 320 LNEAFACQVLGVVKEWGFEdLDRLNVNGSGISLGHPVGATGARMATTALHELGRRGGGKALLTMCIGGGQGMAAVVE 396
Cdd:PRK06690  283 INEAFASKVVACAKELQIP-YEKLNVNGGAIALGHPYGASGAMLVTRLFYQAKREDMKYGIATLGIGGGIGLALLFE 358
PRK09268 PRK09268
acetyl-CoA C-acetyltransferase;
1-397 9.21e-56

acetyl-CoA C-acetyltransferase;


Pssm-ID: 236440 [Multi-domain]  Cd Length: 427  Bit Score: 189.34  E-value: 9.21e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814   1 MKRAALVAPVRTAVGRFGGALRDVPAESLAATVVKETVRRSGIDPSRIDDVAMGQSYANSEAPCIGRWAALEAGLPISVA 80
Cdd:PRK09268    6 VRRVAILGGNRIPFARSNGAYADASNQDMLTAALDGLVDRFGLQGERLGEVVAGAVLKHSRDFNLTRECVLGSALSPYTP 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814  81 GFQTDRRCGTGLQAIVTAAMMVQTGAADVVLAGGVESMS--------GIEHYTTGARWGTKSGG-LQLFDRLDRGRERSQ 151
Cdd:PRK09268   86 AYDLQQACGTGLEAAILVANKIALGQIDSGIAGGVDTTSdapiavneGLRKILLELNRAKTTGDrLKALGKLRPKHLAPE 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 152 P----EWRFGRisGMIETAENVATRCGITREESDAFAVESHRKATLARESGRFDAEIvaveltdrkgnvTQFRA---DEG 224
Cdd:PRK09268  166 IprngEPRTGL--SMGEHAAITAKEWGISREAQDELAAASHQNLAAAYDRGFFDDLI------------TPFLGltrDNN 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 225 IRPDTSLETLARLRAV---SEGGVVTAGNASQQNDAAAAMLVVAEDRLDELGLEPIGFL-DSWAAA-----GCEPALMGl 295
Cdd:PRK09268  232 LRPDSSLEKLAKLKPVfgkGGRATMTAGNSTPLTDGASVVLLASEEWAAEHGLPVLAYLvDAETAAvdfvhGKEGLLMA- 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 296 gPVAAVSKLFARTGAGFADFDLVELNEAFACQVLGVVKEW----------------GFEDLDRLNVNGSGISLGHPVGAT 359
Cdd:PRK09268  311 -PAYAVPRLLARNGLTLQDFDFYEIHEAFASQVLATLKAWedeeycrerlgldaplGSIDRSKLNVNGSSLAAGHPFAAT 389
                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 1060771814 360 GARMATTALHELGRRGGGKALLTMCIGGGQGMAAVVES 397
Cdd:PRK09268  390 GGRIVATLAKLLAEKGSGRGLISICAAGGQGVTAILER 427
nondecarbox_cond_enzymes cd00826
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ...
7-397 4.30e-53

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: 181.54  E-value: 4.30e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814   7 VAPVRTAVGRFGG---ALRDVPAESLAATVVKETVRRSGIDPSRIDDVAMGQSYANSEAPCIGRWAALEAGLPISVAGFQ 83
Cdd:cd00826     1 AGAAMTAFGKFGGengADANDLAHEAGAKAIAAALEPAGVAAGAVEEACLGQVLGAGEGQNCAQQAAMHAGGLQEAPAIG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814  84 TDRRCGTGLQAIVTAAMMVQTGAADVVLAGGVESMSgiehYTtgarwgtksgglqlfdrldrgrERSQP-EWRFgrisgm 162
Cdd:cd00826    81 MNNLCGSGLRALALAMQLIAGGDANCILAGGFEKME----TS----------------------AENNAkEKHI------ 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 163 ietaeNVATRCGITREESDAFAVESHRKATLARESGRFDAEIVAVELTDRKGNVTQFrADEGIR--PDTSLETLARLRAV 240
Cdd:cd00826   129 -----DVLINKYGMRACPDAFALAGQAGAEAAEKDGRFKDEFAKFGVKGRKGDIHSD-ADEYIQfgDEASLDEIAKLRPA 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 241 -SEGGVVTAGNASQQNDAAAAMLVVAEDRLDELGLE-------PIGFLDSWAAAGCEPA----LMGLGPVAAVSKLFART 308
Cdd:cd00826   203 fDKEDFLTAGNACGLNDGAAAAILMSEAEAQKHGLQskareiqALEMITDMASTFEDKKvikmVGGDGPIEAARKALEKA 282
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 309 GAGFADFDLVELNEAFACQVLGVVKEWGFE-------DLDR----------LNVNGSGISLGHPVGATGARMATTALHEL 371
Cdd:cd00826   283 GLGIGDLDLIEAHDAFAANACATNEALGLCpegqggaLVDRgdntyggksiINPNGGAIAIGHPIGASGAAICAELCFEL 362
                         410       420       430
                  ....*....|....*....|....*....|.
gi 1060771814 372 GRRGG-----GKALLTMCIGGGQGMAAVVES 397
Cdd:cd00826   363 KGEAGkrqgaGAGLALLCIGGGGGAAMCIES 393
Thiolase_C pfam02803
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
274-396 4.73e-43

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: 146.25  E-value: 4.73e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 274 LEPIGFLDSWAAAGCEPALMGLGPVAAVSKLFARTGAGFADFDLVELNEAFACQVLGVVKEWGFeDLDRLNVNGSGISLG 353
Cdd:pfam02803   1 LKPLARIRSYATAGVDPAIMGIGPAYAIPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGI-DPEKVNVNGGAIALG 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1060771814 354 HPVGATGARMATTALHELGRRGGGKALLTMCIGGGQGMAAVVE 396
Cdd:pfam02803  80 HPLGASGARILVTLLHELKRRGGKYGLASLCIGGGQGVAMIIE 122
SCP-x_thiolase cd00829
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ...
19-396 6.86e-20

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: 90.40  E-value: 6.86e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814  19 GALRDVPAESLAATVVKETVRRSGIDPSRIDDVAMGQSYANSEAPCIGRWAALEAGLPISVAgFQTDRRCGTGLQAIVTA 98
Cdd:cd00829     9 GRRSDRSPLELAAEAARAALDDAGLEPADIDAVVVGNAAGGRFQSFPGALIAEYLGLLGKPA-TRVEAAGASGSAAVRAA 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814  99 AMMVQTGAADVVLAGGVESMSgieHYTTGARWGTKSGglqlfdRLDRGRERSQPEWRFGRISGMIETAenVATRCGITRE 178
Cdd:cd00829    88 AAAIASGLADVVLVVGAEKMS---DVPTGDEAGGRAS------DLEWEGPEPPGGLTPPALYALAARR--YMHRYGTTRE 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 179 ESDAFAVESHRKATLARESgrfdaeivaveltdrkgnvtQFRADEgirpdtSLETLARLRAVSEggVVTAGNASQQNDAA 258
Cdd:cd00829   157 DLAKVAVKNHRNAARNPYA--------------------QFRKPI------TVEDVLNSRMIAD--PLRLLDCCPVSDGA 208
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 259 AAMLVVAEDRLDELGLEPIGFL------DSWAAAGCEPALMGLGPVAAVSKLFARTGAGFADFDLVELNEAF------AC 326
Cdd:cd00829   209 AAVVLASEERARELTDRPVWILgvgaasDTPSLSERDDFLSLDAARLAARRAYKMAGITPDDIDVAELYDCFtiaellAL 288
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 327 QVLGVVK--------EWGFEDLD-RLNVNGSG--ISLGHPVGATGARMATTALHELGRRGGG----KALLTMCIGGGQGM 391
Cdd:cd00829   289 EDLGFCEkgeggklvREGDTAIGgDLPVNTSGglLSKGHPLGATGLAQAVEAVRQLRGEAGArqvpGARVGLAHNIGGTG 368

                  ....*
gi 1060771814 392 AAVVE 396
Cdd:cd00829   369 SAAVV 373
PRK06064 PRK06064
thiolase domain-containing protein;
19-395 4.65e-11

thiolase domain-containing protein;


Pssm-ID: 235688 [Multi-domain]  Cd Length: 389  Bit Score: 63.76  E-value: 4.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814  19 GALRDVPAESLAATVVKETVRRSGIDPSRIDDVAMGQSYAN--SEAPCIGRWAALEAGLPiSVAGFQTDRRCGTGLQAIV 96
Cdd:PRK06064   15 GELWDVSLRDLAVEAGLEALEDAGIDGKDIDAMYVGNMSAGlfVSQEHIAALIADYAGLA-PIPATRVEAACASGGAALR 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814  97 TAAMMVQTGAADVVLAGGVESMSGIEHYTTGARWGTKSgglqlfdrlDRgrersqpEWR------FGRISGMIETAEnvA 170
Cdd:PRK06064   94 QAYLAVASGEADVVLAAGVEKMTDVPTPDATEAIARAG---------DY-------EWEeffgatFPGLYALIARRY--M 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 171 TRCGITREESDAFAVESHRKATlaresgrfdaeivaveltdrKGNVTQFRADegirpdTSLETLARLRAVSEGgvVTAGN 250
Cdd:PRK06064  156 HKYGTTEEDLALVAVKNHYNGS--------------------KNPYAQFQKE------ITVEQVLNSPPVADP--LKLLD 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 251 ASQQNDAAAAMLVVAEDRLDELGLEPIGFLDSWAAAGC-----EPALMGLGP-VAAVSKLFARTGAGFADFDLVELNEAF 324
Cdd:PRK06064  208 CSPITDGAAAVILASEEKAKEYTDTPVWIKASGQASDTialhdRKDFTTLDAaVVAAEKAYKMAGIEPKDIDVAEVHDCF 287
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 325 ------ACQVLGVVK--------EWGFEDLD-RLNVNGSG--ISLGHPVGATGARMATTALHEL-GRRGGGKallTMCIG 386
Cdd:PRK06064  288 tiaeilAYEDLGFAKkgeggklaREGQTYIGgDIPVNPSGglKAKGHPVGATGVSQAVEIVWQLrGEAEKGR---QQVIG 364

                  ....*....
gi 1060771814 387 GGQGMAAVV 395
Cdd:PRK06064  365 AGYGLTHNV 373
cond_enzymes cd00327
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ...
245-395 3.71e-10

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: 59.77  E-value: 3.71e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 245 VVTAGNASQQNDAAAAMLVVAEDRLDELGLEPIGFLDSWAA----AGCEPALMGLGPVAAVSKLFARTGAGFADFDLVEL 320
Cdd:cd00327    91 LAGGSEEFVFGDGAAAAVVESEEHALRRGAHPQAEIVSTAAtfdgASMVPAVSGEGLARAARKALEGAGLTPSDIDYVEA 170
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 321 NEAFACQVLGVVKE--WGFEDLDRLNVNGSGISLGHPVGATGARMATTALHEL-------GRRGGGKALLTMCIGGGQGM 391
Cdd:cd00327   171 HGTGTPIGDAVELAlgLDPDGVRSPAVSATLIMTGHPLGAAGLAILDELLLMLehefippTPREPRTVLLLGFGLGGTNA 250

                  ....
gi 1060771814 392 AAVV 395
Cdd:cd00327   251 AVVL 254
PRK12578 PRK12578
thiolase domain-containing protein;
7-363 4.19e-10

thiolase domain-containing protein;


Pssm-ID: 183606 [Multi-domain]  Cd Length: 385  Bit Score: 61.01  E-value: 4.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814   7 VAPVRTAVGRFGgALRDVPAESLAATVVKETVRRSGIDPSRIDDVAMG----QSYANSEAPCIGRWAALEAGLPISVagf 82
Cdd:PRK12578    3 VAVIGVGNSKFG-RRDDVSVQELAWESIKEALNDAGVSQTDIELVVVGstayRGIELYPAPIVAEYSGLTGKVPLRV--- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814  83 qtDRRCGTGLQAIVTAAMMVQTGAADVVLAGGVESMSGIEHYTTGArWGTKSGGLQLfdrldrgrERSQPEWRFGRISGM 162
Cdd:PRK12578   79 --EAMCATGLAASLTAYTAVASGLVDMAIAVGVDKMTEVDTSTSLA-IGGRGGNYQW--------EYHFYGTTFPTYYAL 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 163 IETAEnvATRCGITREESDAFAVESHRKATLaRESGRFDAEIvaveltdrkgnvtqfradegirpdtSLETLARLRAVSE 242
Cdd:PRK12578  148 YATRH--MAVYGTTEEQMALVSVKAHKYGAM-NPKAHFQKPV-------------------------TVEEVLKSRAISW 199
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 243 GgvVTAGNASQQNDAAAAMLVVAEDRLDELGL------EPIGFLDSWAAAGCEPALMGL-GPVAAVSKLFARTGAGFADF 315
Cdd:PRK12578  200 P--IKLLDSCPISDGSATAIFASEEKVKELKIdspvwiTGIGYANDYAYVARRGEWVGFkATQLAARQAYNMAKVTPNDI 277
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1060771814 316 DLVELNEAF------ACQVLGVVK--------EWGFEDLD-RLNVN--GSGISLGHPVGATGARM 363
Cdd:PRK12578  278 EVATVHDAFtiaeimGYEDLGFTEkgkggkfiEEGQSEKGgKVGVNlfGGLKAKGHPLGATGLSM 342
PRK06289 PRK06289
acetyl-CoA acetyltransferase; Provisional
28-387 6.34e-07

acetyl-CoA acetyltransferase; Provisional


Pssm-ID: 235771 [Multi-domain]  Cd Length: 403  Bit Score: 51.23  E-value: 6.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814  28 SLAATVVKETVRRSGIDPSRIDDV----AMGQSYANSeapciGRWAALEAGLPISVAGFQTDRR---CGTGLQAIVTAAM 100
Cdd:PRK06289   28 DLTREVVDGTLAAAGVDADDIEVVhvgnFFGELFAGQ-----GHLGAMPATVHPALWGVPASRHeaaCASGSVATLAAMA 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 101 MVQTGAADVVLAGGVESMSGIEHYTTGARWGTKSGGlqlfdrldrGRERSQPEWRFGRISGMIetAENVATRCGITREES 180
Cdd:PRK06289  103 DLRAGRYDVALVVGVELMKTVPGDVAAEHLGAAAWT---------GHEGQDARFPWPSMFARV--ADEYDRRYGLDEEHL 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 181 DAFAVESH---RKATLARESG-RFDAEIvaveltdrkgnvtqFRADEGIRPDTSletlARLRAVseggvvtagNASQQND 256
Cdd:PRK06289  172 RAIAEINFanaRRNPNAQTRGwAFPDEA--------------TNDDDATNPVVE----GRLRRQ---------DCSQVTD 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 257 AAAAMLVVAEDRLDEL-GLEPIGFLDSWaaaGCEPALMGLGPV---------------AAVSKLFARTGAGFADFDLVEL 320
Cdd:PRK06289  225 GGAGVVLASDAYLRDYaDARPIPRIKGW---GHRTAPLGLEQKldrsagdpyvlphvrQAVLDAYRRAGVGLDDLDGFEV 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 321 NEAF------ACQVLGVV---KEW-----GFEDLD-RLNVNGSG--ISLGHPVGATGARMATTALHEL-GRRG-----GG 377
Cdd:PRK06289  302 HDCFtpseylAIDHIGLTgpgESWkaienGEIAIGgRLPINPSGglIGGGHPVGASGVRMLLDAAKQVtGTAGdyqveGA 381
                         410
                  ....*....|
gi 1060771814 378 KALLTMCIGG 387
Cdd:PRK06289  382 KTFGTLNIGG 391
PTZ00455 PTZ00455
3-ketoacyl-CoA thiolase; Provisional
27-362 1.74e-06

3-ketoacyl-CoA thiolase; Provisional


Pssm-ID: 240424 [Multi-domain]  Cd Length: 438  Bit Score: 49.89  E-value: 1.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814  27 ESLAATVVKETVRRSGID--PSRIDDVAMGQSYAN--SEAPCIGRWAALEAGLPISVAGF------QTDRRCGTGLQAIV 96
Cdd:PTZ00455   49 EELLATAIQGTLENTGLDgkAALVDKVVVGNFLGElfSSQGHLGPAAVGSLGQSGASNALlykpamRVEGACASGGLAVQ 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814  97 TAAMMVQTGAADVVLAGGVEsmsgiEHYTTGARwgtkSGGLQLFDRLDRGRERSQPEWRF-----GRISGMIETAEnvat 171
Cdd:PTZ00455  129 SAWEALLAGTSDIALVVGVE-----VQTTVSAR----VGGDYLARAADYRRQRKLDDFTFpclfaKRMKYIQEHGH---- 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 172 rcgITREESDAFAVESHRKATLARESGRFDAEIVAVELTDRKGNVTQFRADEGIRPdtsletlarlravseggVVTAGNA 251
Cdd:PTZ00455  196 ---FTMEDTARVAAKAYANGNKNPLAHMHTRKLSLEFCTGASDKNPKFLGNETYKP-----------------FLRMTDC 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 252 SQQNDAAAAMLVVAEDRLDELGLEP-----IGFLDSWAAAG-----CEPALMGLGPVAAVSKLFARTGAGFADFDLVELN 321
Cdd:PTZ00455  256 SQVSDGGAGLVLASEEGLQKMGLSPndsrlVEIKSLACASGnlyedPPDATRMFTSRAAAQKALSMAGVKPSDLQVAEVH 335
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1060771814 322 EAFAC------QVLGVVKEWGFEDLDR-----------LNVNGSGISLGHPVGATGAR 362
Cdd:PTZ00455  336 DCFTIaellmyEALGIAEYGHAKDLIRngatalegripVNTGGGLLSFGHPVGATGVK 393
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
88-119 5.37e-05

Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible for the elongation steps in fatty acid biosynthesis. KASIII catalyses the initial condensation and KAS I and II catalyze further elongation steps by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP.


Pssm-ID: 238430 [Multi-domain]  Cd Length: 406  Bit Score: 44.84  E-value: 5.37e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1060771814  88 CGTGLQAIVTAAMMVQTGAADVVLAGGVESMS 119
Cdd:cd00834   161 CASGAHAIGDAARLIRLGRADVVIAGGAEALI 192
FabB COG0304
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...
88-118 1.34e-04

3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism]; 3-oxoacyl-(acyl-carrier-protein) synthase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440073 [Multi-domain]  Cd Length: 409  Bit Score: 43.93  E-value: 1.34e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1060771814  88 CGTGLQAIVTAAMMVQTGAADVVLAGGVESM 118
Cdd:COG0304   161 CASGAHAIGEAYRLIRRGRADVMIAGGAEAA 191
PRK08256 PRK08256
lipid-transfer protein; Provisional
29-360 1.75e-04

lipid-transfer protein; Provisional


Pssm-ID: 181327 [Multi-domain]  Cd Length: 391  Bit Score: 43.35  E-value: 1.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814  29 LAATVVKETVRRSGIDPSRIDDVAMGQSYANSeapCIGRWAALEAGL---PIsvagFQTDRRCGTGLQAIVTAAMMVQTG 105
Cdd:PRK08256   25 MAAEAGRAALADAGIDYDAVQQAYVGYVYGDS---TSGQRALYEVGMtgiPI----VNVNNNCSTGSTALFLARQAVRSG 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 106 AADVVLAGGVESMsgiehyTTGARWGTKSGGLQLFDRLDRGRERSQPE-------WRFGriSGMIETAEnvatRCGITRE 178
Cdd:PRK08256   98 AADCALALGFEQM------QPGALGSVWDDRPSPLERFDKALAELQGFdpappalRMFG--GAGREHME----KYGTTAE 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 179 ESDAFAVESHRKAtlaresgrfdaeivaveltdRKGNVTQFRaDEgirpdTSLETLARLRAVSEGgvVTAGNASQQNDAA 258
Cdd:PRK08256  166 TFAKIGVKARRHA--------------------ANNPYAQFR-DE-----YTLEDVLASPMIWGP--LTRLQCCPPTCGA 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 259 AAMLVVAEDRLDELGL----EPIG------FLDSWAAAGCePALMGLG-PVAAVSKLFARTGAGFADFDLVELNEAFAC- 326
Cdd:PRK08256  218 AAAIVCSEEFARKHGLdravEIVAqamttdTPSTFDGRSM-IDLVGYDmTRAAAQQVYEQAGIGPEDIDVVELHDCFSAn 296
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1060771814 327 -----QVLGVVKEWGFEDL---------DRLNVNGSG--ISLGHPVGATG 360
Cdd:PRK08256  297 elltyEALGLCPEGEAEKFiddgdntygGRWVVNPSGglLSKGHPLGATG 346
PRK07516 PRK07516
thiolase domain-containing protein;
1-376 6.55e-04

thiolase domain-containing protein;


Pssm-ID: 181013 [Multi-domain]  Cd Length: 389  Bit Score: 41.47  E-value: 6.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814   1 MKRAALVAPVRTAVGRfggaLRDVPAESLAATVVKETVRRSGIDPSRIDDVAMGQsyANSEAPCIGRWAALEAGLPISVA 80
Cdd:PRK07516    1 MMTASIVGWAHTPFGK----LDAETLESLIVRVAREALAHAGIAAGDVDGIFLGH--FNAGFSPQDFPASLVLQADPALR 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814  81 GFQTDR---RCGTGLQAIVTAAMMVQTGAADVVLAGGVESMsgiehyttgarwgTKSGGLQLFDRLDRG---RERSQPEW 154
Cdd:PRK07516   75 FKPATRvenACATGSAAVYAALDAIEAGRARIVLVVGAEKM-------------TATPTAEVGDILLGAsylKEEGDTPG 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 155 RFGRISGMIetAENVATRCGITREESDAFAVESHRKAtlaresgrfdaeiVAVELTdrkgnvtQFRADEGirpdtsletL 234
Cdd:PRK07516  142 GFAGVFGRI--AQAYFQRYGDQSDALAMIAAKNHANG-------------VANPYA-------QMRKDLG---------F 190
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 235 ARLRAVSEGGVVTAG-----NASQQNDAAAAMLVVAEDRLDELGlEPIGFL------DSWAAAGCEPALMGlGPVAAVSK 303
Cdd:PRK07516  191 EFCRTVSEKNPLVAGplrrtDCSLVSDGAAALVLADAETARALQ-RAVRFRarahvnDFLPLSRRDPLAFE-GPRRAWQR 268
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814 304 LFARTGAGFADFDLVELNEAFAC------QVLG---------VVKE-WGFEDlDRLNVNGSG--ISLGHPVGATGARM-A 364
Cdd:PRK07516  269 ALAQAGVTLDDLSFVETHDCFTIaelieyEAMGlappgqgarAIREgWTAKD-GKLPVNPSGglKAKGHPIGATGVSMhV 347
                         410
                  ....*....|..
gi 1060771814 365 TTALHELGRRGG 376
Cdd:PRK07516  348 LAAMQLTGEAGG 359
PRK06157 PRK06157
acetyl-CoA acetyltransferase; Validated
7-116 7.54e-04

acetyl-CoA acetyltransferase; Validated


Pssm-ID: 180433 [Multi-domain]  Cd Length: 398  Bit Score: 41.55  E-value: 7.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814   7 VAPVRTAVGRFGGALrDVPAESLAATVVKETVRRSGIDPSRIDDVAMGQSYansEAPCIGRwaaleAGLPISVA-GFQ-- 83
Cdd:PRK06157    9 VAILGMGCTKFGERW-DAGAEDLMVEAFLEALADAGIEPKDIDAAWFGTHY---DEIGSGK-----SGTPLSRAlRLPni 79
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1060771814  84 ----TDRRCGTGLQAIVTAAMMVQTGAADVVLAGGVE 116
Cdd:PRK06157   80 pvtrVENFCATGSEAFRGAVYAVASGAYDIALALGVE 116
PRK05952 PRK05952
beta-ketoacyl-ACP synthase;
88-117 9.84e-04

beta-ketoacyl-ACP synthase;


Pssm-ID: 235653 [Multi-domain]  Cd Length: 381  Bit Score: 40.81  E-value: 9.84e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1060771814  88 CGTGLQAIVTAAMMVQTGAADVVLAGGVES 117
Cdd:PRK05952  146 CATGLWAIAQGVELIQTGQCQRVIAGAVEA 175
cond_enzymes cd00327
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ...
26-117 1.34e-03

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: 40.12  E-value: 1.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060771814  26 AESLAATVVKETVRRSGIDPSRIDDVAMGQSYANSEAPCIGRWAALEAGLPiSVAGFQTDRRCGTGLQAIVTAAMMVQTG 105
Cdd:cd00327     7 ASELGFEAAEQAIADAGLSKGPIVGVIVGTTGGSGEFSGAAGQLAYHLGIS-GGPAYSVNQACATGLTALALAVQQVQNG 85
                          90
                  ....*....|..
gi 1060771814 106 AADVVLAGGVES 117
Cdd:cd00327    86 KADIVLAGGSEE 97
PRK07314 PRK07314
beta-ketoacyl-ACP synthase II;
88-117 7.12e-03

beta-ketoacyl-ACP synthase II;


Pssm-ID: 235987 [Multi-domain]  Cd Length: 411  Bit Score: 38.23  E-value: 7.12e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1060771814  88 CGTGLQAIVTAAMMVQTGAADVVLAGGVES 117
Cdd:PRK07314  162 CATGAHAIGDAARLIAYGDADVMVAGGAEA 191
 
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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