NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|523666866|ref|WP_020798200|]
View 

MULTISPECIES: thiolase family protein [Pseudomonas]

Protein Classification

thiolase family protein( domain architecture ID 11415132)

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

CATH:  3.40.47.10
EC:  2.3.1.-
Gene Ontology:  GO:0016746|GO:0016747
SCOP:  4000245

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PaaJ COG0183
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ...
1-390 0e+00

Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is part of the Pathway/BioSystem: Fatty acid biosynthesis


:

Pssm-ID: 439953 [Multi-domain]  Cd Length: 391  Bit Score: 529.25  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866   1 MKDIVIVDAVRTPIGKFRGSLAGVRADHLGSLVISRLLERVDVSPTLVDDVIFGNVTQIGeQSANIARTALLGAGWPVTV 80
Cdd:COG0183    1 MREVVIVDAVRTPFGRFGGALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQAG-QGQNPARQAALLAGLPESV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866  81 AGLTIDRKCGSGEVAVHMAVGAIAAGAADIVVAGGAENMSRVPMGSNREIHGAAFGWMAAQR---------YELTSQGEA 151
Cdd:COG0183   80 PAVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMLLPKARWGYRMNAKLVDPminpgltdpYTGLSMGET 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 152 AERMADKWALSRDALDDFAFASHQRAATACDAGYFDNETIPVVVEELREKElsepagVLRQDETIRRDTSREKLSTLKTS 231
Cdd:COG0183  160 AENVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVEVPDRKGEV------VVDRDEGPRPDTTLEKLAKLKPA 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 232 FRPDtGRITAGNSSQISDGAAALLLMSADTAKKLGLKARARVVAFTTVGSDPTLMLTGPIAATQKVLAKAGLSINDIDLF 311
Cdd:COG0183  234 FKKD-GTVTAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIGPVPATRKALARAGLTLDDIDLI 312
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 523666866 312 EVNEAFASVPLAWMQETGVPHSKLNVNGGAIALGHPLGASGARLMTTMLNELERRGGRYGLQAICCAGGMGTATIIERL 390
Cdd:COG0183  313 EINEAFAAQVLAVLRELGLDPDKVNVNGGAIALGHPLGASGARILVTLLHELERRGGRYGLATMCIGGGQGIALIIERV 391
 
Name Accession Description Interval E-value
PaaJ COG0183
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ...
1-390 0e+00

Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 439953 [Multi-domain]  Cd Length: 391  Bit Score: 529.25  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866   1 MKDIVIVDAVRTPIGKFRGSLAGVRADHLGSLVISRLLERVDVSPTLVDDVIFGNVTQIGeQSANIARTALLGAGWPVTV 80
Cdd:COG0183    1 MREVVIVDAVRTPFGRFGGALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQAG-QGQNPARQAALLAGLPESV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866  81 AGLTIDRKCGSGEVAVHMAVGAIAAGAADIVVAGGAENMSRVPMGSNREIHGAAFGWMAAQR---------YELTSQGEA 151
Cdd:COG0183   80 PAVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMLLPKARWGYRMNAKLVDPminpgltdpYTGLSMGET 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 152 AERMADKWALSRDALDDFAFASHQRAATACDAGYFDNETIPVVVEELREKElsepagVLRQDETIRRDTSREKLSTLKTS 231
Cdd:COG0183  160 AENVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVEVPDRKGEV------VVDRDEGPRPDTTLEKLAKLKPA 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 232 FRPDtGRITAGNSSQISDGAAALLLMSADTAKKLGLKARARVVAFTTVGSDPTLMLTGPIAATQKVLAKAGLSINDIDLF 311
Cdd:COG0183  234 FKKD-GTVTAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIGPVPATRKALARAGLTLDDIDLI 312
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 523666866 312 EVNEAFASVPLAWMQETGVPHSKLNVNGGAIALGHPLGASGARLMTTMLNELERRGGRYGLQAICCAGGMGTATIIERL 390
Cdd:COG0183  313 EINEAFAAQVLAVLRELGLDPDKVNVNGGAIALGHPLGASGARILVTLLHELERRGGRYGLATMCIGGGQGIALIIERV 391
thiolase cd00751
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ...
5-389 0e+00

Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of 3-ketoacyl-CoA into acyl-CoA and acetyl-CoA, a 2-step reaction involving a covalent intermediate formed with a catalytic cysteine. They are found in prokaryotes and eukaryotes (cytosol, microbodies and mitochondria). There are 2 functional different classes: thiolase-I (3-ketoacyl-CoA thiolase) and thiolase-II (acetoacetyl-CoA thiolase). Thiolase-I can cleave longer fatty acid molecules and plays an important role in the beta-oxidative degradation of fatty acids. Thiolase-II has a high substrate specificity. Although it can cleave acetoacyl-CoA, its main function is the synthesis of acetoacyl-CoA from two molecules of acetyl-CoA, which gives it importance in several biosynthetic pathways.


Pssm-ID: 238383 [Multi-domain]  Cd Length: 386  Bit Score: 513.57  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866   5 VIVDAVRTPIGKFRGSLAGVRADHLGSLVISRLLERVDVSPTLVDDVIFGNVTQIGEqSANIARTALLGAGWPVTVAGLT 84
Cdd:cd00751    1 VIVSAVRTPIGRFGGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGE-GQNPARQAALLAGLPESVPATT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866  85 IDRKCGSGEVAVHMAVGAIAAGAADIVVAGGAENMSRVPMGSNREIHGAAFG---------WMAAQRYELTSQGEAAERM 155
Cdd:cd00751   80 VNRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGRLGlntldgmldDGLTDPFTGLSMGITAENV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 156 ADKWALSRDALDDFAFASHQRAATACDAGYFDNETIPVVVEELREKElsepagVLRQDETIRRDTSREKLSTLKTSFRPD 235
Cdd:cd00751  160 AEKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEVPGRKGPV------VVDRDEGPRPDTTLEKLAKLKPAFKKD 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 236 tGRITAGNSSQISDGAAALLLMSADTAKKLGLKARARVVAFTTVGSDPTLMLTGPIAATQKVLAKAGLSINDIDLFEVNE 315
Cdd:cd00751  234 -GTVTAGNASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDIDLIEINE 312
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 523666866 316 AFASVPLAWMQETGVPHSKLNVNGGAIALGHPLGASGARLMTTMLNELERRGGRYGLQAICCAGGMGTATIIER 389
Cdd:cd00751  313 AFAAQALACLKELGLDPEKVNVNGGAIALGHPLGASGARIVVTLLHELKRRGGRYGLATMCIGGGQGAAMVIER 386
AcCoA-C-Actrans TIGR01930
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ...
6-388 4.05e-158

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: 449.76  E-value: 4.05e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866    6 IVDAVRTPIGKFRGSLAGVRADHLGSLVISRLLERVDVSPTLVDDVIFGNVTQIGEQsANIARTALLGAGWPVTVAGLTI 85
Cdd:TIGR01930   1 IVAAARTPIGKFGGSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLQAGEQ-QNIARQAALLAGLPESVPAYTV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866   86 DRKCGSGEVAVHMAVGAIAAGAADIVVAGGAENMSRVPMGSNREIHGAA---FGWMAAQR-------YELTSQGEAAERM 155
Cdd:TIGR01930  80 NRQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGVPRSLRWGVkpgNAELEDARlkdltdaNTGLPMGVTAENL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866  156 ADKWALSRDALDDFAFASHQRAATACDAGYFDNETIPVVVEELREKElsepagVLRQDETIRRDTSREKLSTLKTSFRPD 235
Cdd:TIGR01930 160 AKKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVTVKGRKGPV------TVSSDEGIRPNTTLEKLAKLKPAFDPD 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866  236 tGRITAGNSSQISDGAAALLLMSADTAKKLGLKARARVVAFTTVGSDPTLMLTGPIAATQKVLAKAGLSINDIDLFEVNE 315
Cdd:TIGR01930 234 -GTVTAGNSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALKKAGLSISDIDLFEINE 312
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 523666866  316 AFASVPLAWMQETGVPHSKLNVNGGAIALGHPLGASGARLMTTMLNELERRGGRYGLQAICCAGGMGTATIIE 388
Cdd:TIGR01930 313 AFAAQVLACIKELGLDLEKVNVNGGAIALGHPLGASGARIVTTLLHELKRRGGRYGLATMCIGGGQGAAVILE 385
PRK07801 PRK07801
acetyl-CoA C-acetyltransferase;
1-390 1.30e-157

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181123 [Multi-domain]  Cd Length: 382  Bit Score: 448.39  E-value: 1.30e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866   1 MKDIVIVDAVRTPIGKFRGSLAGVRADHLGSLVISRLLERVDVSPTLVDDVIFGNVTQIGEQSANIARTALLGAGWPVTV 80
Cdd:PRK07801   1 MAEAYIVDAVRTPVGKRKGGLAGVHPADLGAHVLKGLVDRTGIDPAAVDDVIFGCVDTIGPQAGNIARTSWLAAGLPEEV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866  81 AGLTIDRKCGSGEVAVHMAVGAIAAGAADIVVAGGAENMSRVPMGSNReIHGAAFG----------WMAaqRY--ELTSQ 148
Cdd:PRK07801  81 PGVTVDRQCGSSQQAIHFAAQAVMSGTQDLVVAGGVQNMSQIPISSAM-TAGEQLGftspfaeskgWLH--RYgdQEVSQ 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 149 GEAAERMADKWALSRDALDDFAFASHQRAATACDAGYFDNETIPVvveelrekelsepaGVLRQDETIRrDTSREKLSTL 228
Cdd:PRK07801 158 FRGAELIAEKWGISREEMERFALESHRRAFAAIRAGRFDNEIVPV--------------GGVTVDEGPR-ETSLEKMAGL 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 229 KTSFrpDTGRITAGNSSQISDGAAALLLMSADTAKKLGLKARARVVAFTTVGSDPTLMLTGPIAATQKVLAKAGLSINDI 308
Cdd:PRK07801 223 KPLV--EGGRLTAAVASQISDGASAVLLASERAVKRHGLTPRARIHHLSVRGDDPVFMLTAPIPATRYALEKTGLSIDDI 300
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 309 DLFEVNEAFASVPLAWMQETGVPHSKLNVNGGAIALGHPLGASGARLMTTMLNELERRGGRYGLQAICCAGGMGTATIIE 388
Cdd:PRK07801 301 DVVEINEAFAPVVLAWLKETGADPAKVNPNGGAIALGHPLGATGAKLMTTLLHELERTGGRYGLQTMCEGGGTANVTIIE 380

                 ..
gi 523666866 389 RL 390
Cdd:PRK07801 381 RL 382
Thiolase_N pfam00108
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
4-260 3.52e-70

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: 221.02  E-value: 3.52e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866    4 IVIVDAVRTPIGKFRGSLAGVRADHLGSLVISRLLERVDVSPTLVDDVIFGNVTQiGEQSANIARTALLGAGWPVTVAGL 83
Cdd:pfam00108   1 VVIVSAARTPFGSFGGSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQ-AGEGQNPARQAALKAGIPDSAPAV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866   84 TIDRKCGSGEVAVHMAVGAIAAGAADIVVAGGAENMSRVPMGSNREIH-GAAFGwmAAQRYELTS------------QGE 150
Cdd:pfam00108  80 TINKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALPTDARsGLKHG--DEKKHDLLIpdgltdafngyhMGL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866  151 AAERMADKWALSRDALDDFAFASHQRAATACDAGYFDNETIPVVVEELREKelsepaGVLRQDETIRRDTSREKLSTLKT 230
Cdd:pfam00108 158 TAENVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDEIVPVTVKGRKGK------PTVDKDEGIRPPTTAEPLAKLKP 231
                         250       260       270
                  ....*....|....*....|....*....|
gi 523666866  231 SFRPDtGRITAGNSSQISDGAAALLLMSAD 260
Cdd:pfam00108 232 AFDKE-GTVTAGNASPINDGAAAVLLMSES 260
 
Name Accession Description Interval E-value
PaaJ COG0183
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ...
1-390 0e+00

Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 439953 [Multi-domain]  Cd Length: 391  Bit Score: 529.25  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866   1 MKDIVIVDAVRTPIGKFRGSLAGVRADHLGSLVISRLLERVDVSPTLVDDVIFGNVTQIGeQSANIARTALLGAGWPVTV 80
Cdd:COG0183    1 MREVVIVDAVRTPFGRFGGALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQAG-QGQNPARQAALLAGLPESV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866  81 AGLTIDRKCGSGEVAVHMAVGAIAAGAADIVVAGGAENMSRVPMGSNREIHGAAFGWMAAQR---------YELTSQGEA 151
Cdd:COG0183   80 PAVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMLLPKARWGYRMNAKLVDPminpgltdpYTGLSMGET 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 152 AERMADKWALSRDALDDFAFASHQRAATACDAGYFDNETIPVVVEELREKElsepagVLRQDETIRRDTSREKLSTLKTS 231
Cdd:COG0183  160 AENVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVEVPDRKGEV------VVDRDEGPRPDTTLEKLAKLKPA 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 232 FRPDtGRITAGNSSQISDGAAALLLMSADTAKKLGLKARARVVAFTTVGSDPTLMLTGPIAATQKVLAKAGLSINDIDLF 311
Cdd:COG0183  234 FKKD-GTVTAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIGPVPATRKALARAGLTLDDIDLI 312
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 523666866 312 EVNEAFASVPLAWMQETGVPHSKLNVNGGAIALGHPLGASGARLMTTMLNELERRGGRYGLQAICCAGGMGTATIIERL 390
Cdd:COG0183  313 EINEAFAAQVLAVLRELGLDPDKVNVNGGAIALGHPLGASGARILVTLLHELERRGGRYGLATMCIGGGQGIALIIERV 391
thiolase cd00751
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ...
5-389 0e+00

Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of 3-ketoacyl-CoA into acyl-CoA and acetyl-CoA, a 2-step reaction involving a covalent intermediate formed with a catalytic cysteine. They are found in prokaryotes and eukaryotes (cytosol, microbodies and mitochondria). There are 2 functional different classes: thiolase-I (3-ketoacyl-CoA thiolase) and thiolase-II (acetoacetyl-CoA thiolase). Thiolase-I can cleave longer fatty acid molecules and plays an important role in the beta-oxidative degradation of fatty acids. Thiolase-II has a high substrate specificity. Although it can cleave acetoacyl-CoA, its main function is the synthesis of acetoacyl-CoA from two molecules of acetyl-CoA, which gives it importance in several biosynthetic pathways.


Pssm-ID: 238383 [Multi-domain]  Cd Length: 386  Bit Score: 513.57  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866   5 VIVDAVRTPIGKFRGSLAGVRADHLGSLVISRLLERVDVSPTLVDDVIFGNVTQIGEqSANIARTALLGAGWPVTVAGLT 84
Cdd:cd00751    1 VIVSAVRTPIGRFGGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGE-GQNPARQAALLAGLPESVPATT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866  85 IDRKCGSGEVAVHMAVGAIAAGAADIVVAGGAENMSRVPMGSNREIHGAAFG---------WMAAQRYELTSQGEAAERM 155
Cdd:cd00751   80 VNRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGRLGlntldgmldDGLTDPFTGLSMGITAENV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 156 ADKWALSRDALDDFAFASHQRAATACDAGYFDNETIPVVVEELREKElsepagVLRQDETIRRDTSREKLSTLKTSFRPD 235
Cdd:cd00751  160 AEKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEVPGRKGPV------VVDRDEGPRPDTTLEKLAKLKPAFKKD 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 236 tGRITAGNSSQISDGAAALLLMSADTAKKLGLKARARVVAFTTVGSDPTLMLTGPIAATQKVLAKAGLSINDIDLFEVNE 315
Cdd:cd00751  234 -GTVTAGNASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDIDLIEINE 312
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 523666866 316 AFASVPLAWMQETGVPHSKLNVNGGAIALGHPLGASGARLMTTMLNELERRGGRYGLQAICCAGGMGTATIIER 389
Cdd:cd00751  313 AFAAQALACLKELGLDPEKVNVNGGAIALGHPLGASGARIVVTLLHELKRRGGRYGLATMCIGGGQGAAMVIER 386
AcCoA-C-Actrans TIGR01930
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ...
6-388 4.05e-158

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: 449.76  E-value: 4.05e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866    6 IVDAVRTPIGKFRGSLAGVRADHLGSLVISRLLERVDVSPTLVDDVIFGNVTQIGEQsANIARTALLGAGWPVTVAGLTI 85
Cdd:TIGR01930   1 IVAAARTPIGKFGGSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLQAGEQ-QNIARQAALLAGLPESVPAYTV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866   86 DRKCGSGEVAVHMAVGAIAAGAADIVVAGGAENMSRVPMGSNREIHGAA---FGWMAAQR-------YELTSQGEAAERM 155
Cdd:TIGR01930  80 NRQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGVPRSLRWGVkpgNAELEDARlkdltdaNTGLPMGVTAENL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866  156 ADKWALSRDALDDFAFASHQRAATACDAGYFDNETIPVVVEELREKElsepagVLRQDETIRRDTSREKLSTLKTSFRPD 235
Cdd:TIGR01930 160 AKKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVTVKGRKGPV------TVSSDEGIRPNTTLEKLAKLKPAFDPD 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866  236 tGRITAGNSSQISDGAAALLLMSADTAKKLGLKARARVVAFTTVGSDPTLMLTGPIAATQKVLAKAGLSINDIDLFEVNE 315
Cdd:TIGR01930 234 -GTVTAGNSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALKKAGLSISDIDLFEINE 312
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 523666866  316 AFASVPLAWMQETGVPHSKLNVNGGAIALGHPLGASGARLMTTMLNELERRGGRYGLQAICCAGGMGTATIIE 388
Cdd:TIGR01930 313 AFAAQVLACIKELGLDLEKVNVNGGAIALGHPLGASGARIVTTLLHELKRRGGRYGLATMCIGGGQGAAVILE 385
PRK07801 PRK07801
acetyl-CoA C-acetyltransferase;
1-390 1.30e-157

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181123 [Multi-domain]  Cd Length: 382  Bit Score: 448.39  E-value: 1.30e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866   1 MKDIVIVDAVRTPIGKFRGSLAGVRADHLGSLVISRLLERVDVSPTLVDDVIFGNVTQIGEQSANIARTALLGAGWPVTV 80
Cdd:PRK07801   1 MAEAYIVDAVRTPVGKRKGGLAGVHPADLGAHVLKGLVDRTGIDPAAVDDVIFGCVDTIGPQAGNIARTSWLAAGLPEEV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866  81 AGLTIDRKCGSGEVAVHMAVGAIAAGAADIVVAGGAENMSRVPMGSNReIHGAAFG----------WMAaqRY--ELTSQ 148
Cdd:PRK07801  81 PGVTVDRQCGSSQQAIHFAAQAVMSGTQDLVVAGGVQNMSQIPISSAM-TAGEQLGftspfaeskgWLH--RYgdQEVSQ 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 149 GEAAERMADKWALSRDALDDFAFASHQRAATACDAGYFDNETIPVvveelrekelsepaGVLRQDETIRrDTSREKLSTL 228
Cdd:PRK07801 158 FRGAELIAEKWGISREEMERFALESHRRAFAAIRAGRFDNEIVPV--------------GGVTVDEGPR-ETSLEKMAGL 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 229 KTSFrpDTGRITAGNSSQISDGAAALLLMSADTAKKLGLKARARVVAFTTVGSDPTLMLTGPIAATQKVLAKAGLSINDI 308
Cdd:PRK07801 223 KPLV--EGGRLTAAVASQISDGASAVLLASERAVKRHGLTPRARIHHLSVRGDDPVFMLTAPIPATRYALEKTGLSIDDI 300
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 309 DLFEVNEAFASVPLAWMQETGVPHSKLNVNGGAIALGHPLGASGARLMTTMLNELERRGGRYGLQAICCAGGMGTATIIE 388
Cdd:PRK07801 301 DVVEINEAFAPVVLAWLKETGADPAKVNPNGGAIALGHPLGATGAKLMTTLLHELERTGGRYGLQTMCEGGGTANVTIIE 380

                 ..
gi 523666866 389 RL 390
Cdd:PRK07801 381 RL 382
PRK05790 PRK05790
putative acyltransferase; Provisional
1-390 6.55e-150

putative acyltransferase; Provisional


Pssm-ID: 180261 [Multi-domain]  Cd Length: 393  Bit Score: 429.19  E-value: 6.55e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866   1 MKDIVIVDAVRTPIGKFRGSLAGVRADHLGSLVISRLLERVDVSPTLVDDVIFGNVTQIGeQSANIARTALLGAGWPVTV 80
Cdd:PRK05790   1 MKDVVIVSAARTPIGKFGGALKDVSAVELGAIVIKAALERAGVPPEQVDEVIMGQVLQAG-AGQNPARQAALKAGLPVEV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866  81 AGLTIDRKCGSGEVAVHMAVGAIAAGAADIVVAGGAENMSRVP--MGSNREihGAAFGWMAAQ----------RYELTSQ 148
Cdd:PRK05790  80 PALTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQESMSQAPhvLPGSRW--GQKMGDVELVdtmihdgltdAFNGYHM 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 149 GEAAERMADKWALSRDALDDFAFASHQRAATACDAGYFDNETIPVVVEELREKELsepagVLRQDETIRRDTSREKLSTL 228
Cdd:PRK05790 158 GITAENLAEQYGITREEQDEFALASQQKAEAAIKAGRFKDEIVPVTIKQRKGDPV-----VVDTDEHPRPDTTAESLAKL 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 229 KTSFRPDtGRITAGNSSQISDGAAALLLMSADTAKKLGLKARARVVAFTTVGSDPTLMLTGPIAATQKVLAKAGLSINDI 308
Cdd:PRK05790 233 RPAFDKD-GTVTAGNASGINDGAAAVVVMSEAKAKELGLTPLARIVSYAVAGVDPAIMGIGPVPAIRKALEKAGWSLADL 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 309 DLFEVNEAFASVPLAWMQETGVPHSKLNVNGGAIALGHPLGASGARLMTTMLNELERRGGRYGLQAICCAGGMGTATIIE 388
Cdd:PRK05790 312 DLIEINEAFAAQALAVEKELGLDPEKVNVNGGAIALGHPIGASGARILVTLLHEMKRRGAKKGLATLCIGGGQGVALIVE 391

                 ..
gi 523666866 389 RL 390
Cdd:PRK05790 392 RP 393
PRK08242 PRK08242
acetyl-CoA C-acetyltransferase;
1-390 3.96e-146

acetyl-CoA C-acetyltransferase;


Pssm-ID: 236197 [Multi-domain]  Cd Length: 402  Bit Score: 420.06  E-value: 3.96e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866   1 MKDIVIVDAVRTPIGKFR--GSLAGVRADHLGSLVISRLLERVDVSPTLVDDVIFGNVTQIGEQSANIARTALLGAGWPV 78
Cdd:PRK08242   1 MTEAYIYDAVRTPRGKGKkdGSLHEVKPVRLAAGLLEALRDRNGLDTAAVDDVVLGCVTPVGDQGADIARTAVLAAGLPE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866  79 TVAGLTIDRKCGSGEVAVHMAVGAIAAGAADIVVAGGAENMSRVPMGSNreihGAAFGW--MAAQRYELTSQGEAAERMA 156
Cdd:PRK08242  81 TVPGVQINRFCASGLEAVNLAAAKVRSGWDDLVIAGGVESMSRVPMGSD----GGAWAMdpSTNFPTYFVPQGISADLIA 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 157 DKWALSRDALDDFAFASHQRAATACDAGYFDNETIPVvveelrekelSEPAG--VLRQDETIRRDTSREKLSTLKTSFR- 233
Cdd:PRK08242 157 TKYGFSREDVDAYAVESQQRAAAAWAEGYFAKSVVPV----------KDQNGltILDHDEHMRPGTTMESLAKLKPSFAm 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 234 ---------------PDTGRI----TAGNSSQISDGAAALLLMSADTAKKLGLKARARVVAFTTVGSDPTLMLTGPIAAT 294
Cdd:PRK08242 227 mgemggfdavalqkyPEVERInhvhHAGNSSGIVDGAAAVLIGSEEAGKALGLKPRARIVATATIGSDPTIMLTGPVPAT 306
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 295 QKVLAKAGLSINDIDLFEVNEAFASVPLAWMQETGVPHSKLNVNGGAIALGHPLGASGARLMTTMLNELERRGGRYGLQA 374
Cdd:PRK08242 307 RKALAKAGLTVDDIDLFELNEAFASVVLRFMQALDIPHDKVNVNGGAIAMGHPLGATGAMILGTVLDELERRGKRTALIT 386
                        410
                 ....*....|....*.
gi 523666866 375 ICCAGGMGTATIIERL 390
Cdd:PRK08242 387 LCVGGGMGIATIIERV 402
PRK07850 PRK07850
steroid 3-ketoacyl-CoA thiolase;
1-390 8.33e-139

steroid 3-ketoacyl-CoA thiolase;


Pssm-ID: 181145 [Multi-domain]  Cd Length: 387  Bit Score: 401.02  E-value: 8.33e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866   1 MKDIVIVDAVRTPIGKFRGSLAGVRADHLGSLVISRLLERVDVSPTLVDDVIFGNVTQIGEQSANIARTALLGAGWPVTV 80
Cdd:PRK07850   1 MGNPVIVEAVRTPIGKRNGWLSGLHAAELLGAVQRAVLDRAGIDPGDVEQVIGGCVTQAGEQSNNITRTAWLHAGLPYHV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866  81 AGLTIDRKCGSGEVAVHMAVGAIAAGAADIVVAGGAENMSRVPMGSNREiHGAAFGWMAAQRYELTSQGEAAERMADKWA 160
Cdd:PRK07850  81 GATTIDCQCGSAQQANHLVAGLIAAGAIDVGIACGVEAMSRVPLGANAG-PGRGLPRPDSWDIDMPNQFEAAERIAKRRG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 161 LSRDALDDFAFASHQRAATACDAGYFDNETIPVVVEELREKelSEPAGVLR---QDETIRrDTSREKLSTLKTSFrpDTG 237
Cdd:PRK07850 160 ITREDVDAFGLRSQRRAAQAWAEGRFDREISPVQAPVLDEE--GQPTGETRlvtRDQGLR-DTTMEGLAGLKPVL--EGG 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 238 RITAGNSSQISDGAAALLLMSADTAKKLGLKARARVVAFTTVGSDPTLMLTGPIAATQKVLAKAGLSINDIDLFEVNEAF 317
Cdd:PRK07850 235 IHTAGTSSQISDGAAAVLWMDEDRARALGLRPRARIVAQALVGAEPYYHLDGPVQATAKVLEKAGMKIGDIDLVEINEAF 314
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 523666866 318 ASVPLAWMQETGVPHSKLNVNGGAIALGHPLGASGARLMTTMLNELERRGGRYGLQAICCAGGMGTATIIERL 390
Cdd:PRK07850 315 ASVVLSWAQVHEPDMDKVNVNGGAIALGHPVGSTGARLITTALHELERTDKSTALITMCAGGALSTGTIIERI 387
PRK06504 PRK06504
acetyl-CoA C-acetyltransferase;
1-390 1.47e-134

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180595 [Multi-domain]  Cd Length: 390  Bit Score: 390.24  E-value: 1.47e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866   1 MKDIVIVDAVRTPIGKFRGSLAGVRADHLGSLVISRLLERVDVSPTLVDDVIFGNVTQIGEQSANIARTALLGAGWPVTV 80
Cdd:PRK06504   1 MAEAYIVAAARTAGGRKGGRLAGWHPADLAAQVLDALVDRSGADPALIEDVIMGCVSQVGEQATNVARNAVLASKLPESV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866  81 AGLTIDRKCGSGEVAVHMAVGAIAAGAADIVVAGGAENMSRVPMGSNREIHG-AAFGWMAAQRYE------LTSQGEAAE 153
Cdd:PRK06504  81 PGTSIDRQCGSSQQALHFAAQAVMSGTMDIVIAAGVESMTRVPMGSPSTLPAkNGLGHYKSPGMEerypgiQFSQFTGAE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 154 RMADKWALSRDALDDFAFASHQRAATACDAGYFDNETIPVvveelrEKELSEPAGVLRQ-DETIRRDTSREKLSTLKTSf 232
Cdd:PRK06504 161 MMAKKYGLSKDQLDEFALQSHQRAIAATQAGKFKAEIVPL------EITRADGSGEMHTvDEGIRFDATLEGIAGVKLI- 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 233 rPDTGRITAGNSSQISDGAAALLLMSADTAKKLGLKARARVVAFTTVGSDPTLMLTGPIAATQKVLAKAGLSINDIDLFE 312
Cdd:PRK06504 234 -AEGGRLTAATASQICDGASGVMVVNERGLKALGVKPLARIHHMTVIGGDPVIMLEAPLPATERALKKAGMKIDDIDLYE 312
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 523666866 313 VNEAFASVPLAWMQETGVPHSKLNVNGGAIALGHPLGASGARLMTTMLNELERRGGRYGLQAICCAGGMGTATIIERL 390
Cdd:PRK06504 313 VNEAFASVPLAWLKATGADPERLNVNGGAIALGHPLGASGTKLMTTLVHALKQRGKRYGLQTMCEGGGMANVTIVERL 390
PRK09050 PRK09050
beta-ketoadipyl CoA thiolase; Validated
1-390 1.62e-128

beta-ketoadipyl CoA thiolase; Validated


Pssm-ID: 181624 [Multi-domain]  Cd Length: 401  Bit Score: 375.45  E-value: 1.62e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866   1 MKDIVIVDAVRTPIGKFRGSLAGVRADHLGSLVISRLLER-VDVSPTLVDDVIFGNVTQIGEQSANIARTALLGAGWPVT 79
Cdd:PRK09050   1 MTEAFICDAIRTPIGRYGGALSSVRADDLGAVPLKALMARnPGVDWEAVDDVIYGCANQAGEDNRNVARMSALLAGLPVS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866  80 VAGLTIDRKCGSGEVAVHMAVGAIAAGAADIVVAGGAENMSRVP--MGS-------NREIHGAAFGW------MAAQrYE 144
Cdd:PRK09050  81 VPGTTINRLCGSGMDAVGTAARAIKAGEAELMIAGGVESMSRAPfvMGKadsafsrQAEIFDTTIGWrfvnplMKAQ-YG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 145 LTSQGEAAERMADKWALSRDALDDFAFASHQRAATACDAGYFDNETIPVVVEELRekelSEPAgVLRQDETIRRDTSREK 224
Cdd:PRK09050 160 VDSMPETAENVAEDYNISRADQDAFALRSQQRAAAAQAAGFLAEEIVPVTIPQKK----GDPV-VVDRDEHPRPETTLEA 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 225 LSTLKTSFRPDtGRITAGNSSQISDGAAALLLMSADTAKKLGLKARARVVAFTTVGSDPTLMLTGPIAATQKVLAKAGLS 304
Cdd:PRK09050 235 LAKLKPVFRPD-GTVTAGNASGVNDGAAALLLASEAAAKKHGLTPRARILGMATAGVEPRIMGIGPAPATRKLLARLGLT 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 305 INDIDLFEVNEAFASVPLAWMQETGVPH--SKLNVNGGAIALGHPLGASGARLMTTMLNELERRGGRYGLQAICCAGGMG 382
Cdd:PRK09050 314 IDQFDVIELNEAFAAQGLAVLRQLGLADddARVNPNGGAIALGHPLGMSGARLVLTALHQLERTGGRYALCTMCIGVGQG 393

                 ....*...
gi 523666866 383 TATIIERL 390
Cdd:PRK09050 394 IALAIERV 401
fadA PRK08947
3-ketoacyl-CoA thiolase; Reviewed
1-390 1.03e-120

3-ketoacyl-CoA thiolase; Reviewed


Pssm-ID: 181592 [Multi-domain]  Cd Length: 387  Bit Score: 355.04  E-value: 1.03e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866   1 MKDIVIVDAVRTPIGKFR-GSLAGVRADHLGSLVISRLLER-VDVSPTLVDDVIFGNVTQIGEQSANIARTALLGAGWPV 78
Cdd:PRK08947   1 MEDVVIVDAIRTPMGRSKgGAFRNVRAEDLSAHLMRSLLARnPALDPAEIDDIIWGCVQQTLEQGFNIARNAALLAGIPH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866  79 TVAGLTIDRKCGSGEVAVHMAVGAIAAGAADIVVAGGAENMSRVPMgsnreIHGAAFGWMAAQRYELTS--QGEAAERMA 156
Cdd:PRK08947  81 SVPAVTVNRLCGSSMQALHDAARAIMTGDGDVFLIGGVEHMGHVPM-----NHGVDFHPGLSKNVAKAAgmMGLTAEMLG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 157 DKWALSRDALDDFAFASHQRAATACDAGYFDNETIPVvveelrekELSEPAGVLR---QDETIRRDTSREKLSTLKTSFR 233
Cdd:PRK08947 156 KMHGISREQQDAFAARSHQRAWAATQEGRFKNEIIPT--------EGHDADGVLKlfdYDEVIRPETTVEALAALRPAFD 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 234 PDTGRITAGNSSQISDGAAALLLMSADTAKKLGLKARARVVAFTTVGSDPTLMLTGPIAATQKVLAKAGLSINDIDLFEV 313
Cdd:PRK08947 228 PVNGTVTAGTSSALSDGASAMLVMSESRAKELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISDIDVFEL 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 314 NEAFASVPLAWMQETGVPHS---KLNVNGGAIALGHPLGASGARLMTTMLNELERRGGRYGLQAICCAGGMGTATIIERL 390
Cdd:PRK08947 308 NEAFAAQSLPCLKDLGLLDKmdeKVNLNGGAIALGHPLGCSGARISTTLLNLMERKDAQFGLATMCIGLGQGIATVFERV 387
PRK06205 PRK06205
acetyl-CoA C-acetyltransferase;
1-389 1.69e-112

acetyl-CoA C-acetyltransferase;


Pssm-ID: 235741 [Multi-domain]  Cd Length: 404  Bit Score: 334.65  E-value: 1.69e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866   1 MKDIVIVDAVRTPIGKFRGSLAGVRADHLGSLVISRLLERVDVSPTLVDDVIFGNVTQIGEQSAnIARTALLGAGWPVTV 80
Cdd:PRK06205   1 MRDAVICEPVRTPVGRFGGAFKDVPAEELAATVIRALVERTGIDPARIDDVIFGQGYPNGEAPA-IGRVAALDAGLPVTV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866  81 AGLTIDRKCGSGEVAVHMAVGAIAAGAADIVVAGGAENMSRVPMGSNREIHGAAFGWMAAQ----RYELTSQG------- 149
Cdd:PRK06205  80 PGMQLDRRCGSGLQAVITAAMQVQTGAADVVIAGGAESMSNVEFYTTDMRWGVRGGGVQLHdrlaRGRETAGGrrfpvpg 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 150 ---EAAERMADKWALSRDALDDFAFASHQRAATACDAGYFDNETIPVVVEELRekelSEPAgVLRQDETIRRDTSREKLS 226
Cdd:PRK06205 160 gmiETAENLRREYGISREEQDALAVRSHQRAVAAQEAGRFDDEIVPVTVPQRK----GDPT-VVDRDEHPRADTTLESLA 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 227 TLKT---SFRPDtGRITAGNSSQISDGAAALLLMSADTAKKLGLKARARVVAFTTVGSDPTLMLTGPIAATQKVLAKAGL 303
Cdd:PRK06205 235 KLRPimgKQDPE-ATVTAGNASGQNDAAAACLVTTEDKAEELGLRPLARLVSWAVAGVEPSRMGIGPVPATEKALARAGL 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 304 SINDIDLFEVNEAFASVPLAWMQETGVP---HSKLNVNGGAIALGHPLGASGARLMTTMLNELERRGGRYGLQAICCAGG 380
Cdd:PRK06205 314 TLDDIDLIELNEAFAAQVLAVLKEWGFGaddEERLNVNGSGISLGHPVGATGGRILATLLRELQRRQARYGLETMCIGGG 393

                 ....*....
gi 523666866 381 MGTATIIER 389
Cdd:PRK06205 394 QGLAAVFER 402
PRK06445 PRK06445
acetyl-CoA C-acetyltransferase;
1-389 1.15e-111

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180563 [Multi-domain]  Cd Length: 394  Bit Score: 332.07  E-value: 1.15e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866   1 MKDIVIVDAVRTPIGKFRGS------LAGVRADHLGSLVISRLLERVDVSPTLVDDVIFGNVTQIGEQSANIARTALLGA 74
Cdd:PRK06445   1 LEDVYLVDFARTAFSRFRPKdpqkdvFNNIRPEELAAMLINRLIEKTGIKPEEIDDIITGCALQVGENWLYGGRHPIFLA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866  75 GWPVTVAGLTIDRKCGSGEVAVHMAVGAIAAGAADIVVAGGAENMSRVPMGSNR--EIHGAAFGWMAAQRYELT---SQG 149
Cdd:PRK06445  81 RLPYNIPAMAVDRQCASSLTTVSIGAMEIATGMADIVIAGGVEHMTRTPMGDNPhiEPNPKLLTDPKYIEYDLTtgyVMG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 150 EAAERMADKWALSRDALDDFAFASHQRAATACDAGYFDNETIPVVVEELREKElsepagVLRQDETIRRDTSREKLSTLK 229
Cdd:PRK06445 161 LTAEKLAEEAGIKREEMDRWSLRSHQLAAKAIQEGYFKDEILPIEVEVEGKKK------VVDVDQSVRPDTSLEKLAKLP 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 230 TSFRPDtGRITAGNSSQISDGAAALLLMSADTAKKLGLKARARVVAFTTVGSDPTLMLTGPIAATQKVLAKAGLSINDID 309
Cdd:PRK06445 235 PAFKPD-GVITAGNSSPLNSGASYVLLMSKKAVKKYGLKPMAKIRSFGFAGVPPAIMGKGPVPASKKALEKAGLSVKDID 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 310 LFEVNEAFASVPLAWMQETGVPHSKLNVNGGAIALGHPLGASGARLMTTMLNELERRGGRYGLQAICCAGGMGTATIIER 389
Cdd:PRK06445 314 LWEINEAFAVVVLYAIKELGLDPETVNIKGGAIAIGHPLGATGARIVGTLARQLQIKGKDYGVATLCVGGGQGGAVVLER 393
PRK09051 PRK09051
beta-ketothiolase BktB;
1-390 4.04e-111

beta-ketothiolase BktB;


Pssm-ID: 181625 [Multi-domain]  Cd Length: 394  Bit Score: 330.77  E-value: 4.04e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866   1 MKDIVIVDAVRTPIGKFRGSLAGVRADHLGSLVISRLLERVDVSPTLVDDVIFGNVTQIGEQSANIARTALLGAGWPVTV 80
Cdd:PRK09051   2 MREVVVVSGVRTAIGTFGGSLKDVAPTDLGATVVREALARAGVDPDQVGHVVFGHVIPTEPRDMYLSRVAAINAGVPQET 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866  81 AGLTIDRKCGSGEVAVHMAVGAIAAGAADIVVAGGAENMSRVPMGSNREIHGAAFGWMAAQRYELTS---------QGEA 151
Cdd:PRK09051  82 PAFNVNRLCGSGLQAIVSAAQAILLGDADVAIGGGAESMSRAPYLLPAARWGARMGDAKLVDMMVGAlhdpfgtihMGVT 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 152 AERMADKWALSRDALDDFAFASHQRAATACDAGYFDNETIPVVVEElREKELsepagVLRQDETIRRDTSREKLSTLKTS 231
Cdd:PRK09051 162 AENVAAKYGISREAQDALALESHRRAAAAIAAGYFKDQIVPVEIKT-RKGEV-----VFDTDEHVRADTTLEDLAKLKPV 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 232 FRPDTGRITAGNSSQISDGAAALLLMSADTAKKLGLKARARVVAFTTVGSDPTLMLTGPIAATQKVLAKAGLSINDIDLF 311
Cdd:PRK09051 236 FKKENGTVTAGNASGINDGAAAVVLAEADAAEARGLKPLARLVGYAHAGVDPEYMGIGPVPATQKALERAGLTVADLDVI 315
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 523666866 312 EVNEAFASVPLAWMQETGVPHSKLNVNGGAIALGHPLGASGARLMTTMLNELERRGGRYGLQAICCAGGMGTATIIERL 390
Cdd:PRK09051 316 EANEAFAAQACAVTRELGLDPAKVNPNGSGISLGHPVGATGAIITVKALYELQRIGGRYALVTMCIGGGQGIAAIFERL 394
PRK08235 PRK08235
acetyl-CoA C-acetyltransferase;
1-388 8.47e-110

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181311 [Multi-domain]  Cd Length: 393  Bit Score: 327.44  E-value: 8.47e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866   1 MKDIVIVDAVRTPIGKFRGSLAGVRADHLGSLVISRLLERVDVSPTLVDDVIFGNVTQIGeQSANIARTALLGAGWPVTV 80
Cdd:PRK08235   1 MSKTVIVSAARTPFGKFGGSLKDVKATELGGIAIKEALERANVSAEDVEEVIMGTVLQGG-QGQIPSRQAARAAGIPWEV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866  81 AGLTIDRKCGSGEVAVHMAVGAIAAGAADIVVAGGAENMSRVP-----------MGSNREIHGAAFG--WMAAQRYELTS 147
Cdd:PRK08235  80 QTETVNKVCASGLRAVTLADQIIRAGDASVIVAGGMESMSNAPyilpgarwgyrMGDNEVIDLMVADglTCAFSGVHMGV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 148 QGEAAermADKWALSRDALDDFAFASHQRAATACDAGYFDNETIPVVVEELREKELsepagVLRQDETIRRDTSREKLST 227
Cdd:PRK08235 160 YGGEV---AKELGISREAQDEWAYRSHQRAVSAHEEGRFEEEIVPVTIPQRKGDPI-----VVAKDEAPRKDTTIEKLAK 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 228 LKTSFRPDtGRITAGNSSQISDGAAALLLMSADTAKKLGLKARARVVAFTTVGSDPTLMLTGPIAATQKVLAKAGLSIND 307
Cdd:PRK08235 232 LKPVFDKT-GTITAGNAPGVNDGAAALVLMSEDRAKQEGRKPLATILAHTAIAVEAKDFPRTPGYAINALLEKTGKTVED 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 308 IDLFEVNEAFASVPLAWMQETGVPHSKLNVNGGAIALGHPLGASGARLMTTMLNELERRGGRYGLQAICCAGGMGTATII 387
Cdd:PRK08235 311 IDLFEINEAFAAVALASTEIAGIDPEKVNVNGGAVALGHPIGASGARIIVTLIHELKRRGGGIGIAAICSGGGQGDAVLI 390

                 .
gi 523666866 388 E 388
Cdd:PRK08235 391 E 391
PRK07661 PRK07661
acetyl-CoA C-acetyltransferase;
1-390 3.98e-108

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181072 [Multi-domain]  Cd Length: 391  Bit Score: 322.86  E-value: 3.98e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866   1 MKDIVIVDAVRTPIGKF-RGSLAGVRADHLGSLVISRLLERVDVSPTLVDDVIFGNVTQIGEQSANIARTALLGAGWPVT 79
Cdd:PRK07661   1 MREAVIVAGARTPVGKAkKGSLKTVRPDDLGALVVKETLKRAGNYEGPIDDLIIGCAMPEAEQGLNMARNIGALAGLPYT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866  80 VAGLTIDRKCGSGEVAVHMAVGAIAAGAADIVVAGGAENMSRVPMGSNREIHGAAFGWMAAQRYelTSQGEAAERMADKW 159
Cdd:PRK07661  81 VPAITINRYCSSGLQSIAYGAERIMLGHSEAVIAGGAESMSLVPMMGHVVRPNPRLVEAAPEYY--MGMGHTAEQVAVKY 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 160 ALSRDALDDFAFASHQRAATACDAGYFDNETIPVVVEELR---EKELSEPAGVLRQDETIRRDTSREKLSTLKTSFRPDt 236
Cdd:PRK07661 159 GISREDQDAFAVRSHQRAAKALAEGKFADEIVPVDVTLRTvgeNNKLQEETITFSQDEGVRADTTLEILGKLRPAFNVK- 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 237 GRITAGNSSQISDGAAALLLMSADTAKKLGLKARARVVAFTTVGSDPTLMLTGPIAATQKVLAKAGLSINDIDLFEVNEA 316
Cdd:PRK07661 238 GSVTAGNSSQMSDGAAAVLLMDREKAESDGLKPLAKFRSFAVAGVPPEVMGIGPIAAIPKALKLAGLELSDIGLFELNEA 317
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 523666866 317 FASVPLAWMQETGVPHSKLNVNGGAIALGHPLGASGARLMTTMLNELERRGGRYGLQAICCAGGMGTATIIERL 390
Cdd:PRK07661 318 FASQSIQVIRELGLDEEKVNVNGGAIALGHPLGCTGAKLTLSLIHEMKRRNEQFGIVTMCIGGGMGAAGVFELL 391
PRK09052 PRK09052
acetyl-CoA C-acyltransferase;
1-390 5.69e-108

acetyl-CoA C-acyltransferase;


Pssm-ID: 181626 [Multi-domain]  Cd Length: 399  Bit Score: 322.72  E-value: 5.69e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866   1 MKDIVIVDAVRTPIGKF-RGSLAGVRADHLGSLVISRLLERV-DVSPTLVDDVIFGNVTQIGEQSANIARTALLGAGWPV 78
Cdd:PRK09052   5 LQDAYIVAATRTPVGKApRGMFKNTRPDDLLAHVLRSAVAQVpGLDPKLIEDAIVGCAMPEAEQGLNVARIGALLAGLPN 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866  79 TVAGLTIDRKCGSGEVAVHMAVGAIAAGAADIVVAGGAENMSRVPMGSNR-----------EIHGAAFGwmaaqryelts 147
Cdd:PRK09052  85 SVGGVTVNRFCASGLQAVAMAADRIRVGEADVMIAAGVESMSMVPMMGNKpsmspaifardENVGIAYG----------- 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 148 QGEAAERMADKWALSRDALDDFAFASHQRAATACDAGYFDNETIPVVVEE----LREKELSEPAGVLRQDETIRRDTSRE 223
Cdd:PRK09052 154 MGLTAEKVAEQWKVSREDQDAFALESHQKAIAAQQAGEFKDEITPYEITErfpdLATGEVDVKTRTVDLDEGPRADTSLE 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 224 KLSTLKTSFRPdTGRITAGNSSQISDGAAALLLMSADTAKKLGLKARARVVAFTTVGSDPTLMLTGPIAATQKVLAKAGL 303
Cdd:PRK09052 234 GLAKLKPVFAN-KGSVTAGNSSQTSDGAGAVILVSEKALKQFNLTPLARFVSFAVAGVPPEIMGIGPIEAIPAALKQAGL 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 304 SINDIDLFEVNEAFASVPLAWMQETGVPHSKLNVNGGAIALGHPLGASGARLMTTMLNELERRGGRYGLQAICCAGGMGT 383
Cdd:PRK09052 313 KQDDLDWIELNEAFAAQSLAVIRDLGLDPSKVNPLGGAIALGHPLGATGAIRTATVVHGLRRTNLKYGMVTMCVGTGMGA 392

                 ....*..
gi 523666866 384 ATIIERL 390
Cdd:PRK09052 393 AGIFERL 399
PLN02644 PLN02644
acetyl-CoA C-acetyltransferase
2-391 4.76e-107

acetyl-CoA C-acetyltransferase


Pssm-ID: 215347 [Multi-domain]  Cd Length: 394  Bit Score: 320.50  E-value: 4.76e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866   2 KDIVIVDAVRTPIGKFRGSLAGVRADHLGSLVISRLLERVDVSPTLVDDVIFGNVTqigeqSANI----ARTALLGAGWP 77
Cdd:PLN02644   1 RDVCIVGVARTPIGGFLGSLSSLSATELGSIAIQAALERAGVDPALVQEVFFGNVL-----SANLgqapARQAALGAGLP 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866  78 VTVAGLTIDRKCGSGEVAVHMAVGAIAAGAADIVVAGGAENMSRVPMGSNREIHGAAFG-------------WMAaqrYE 144
Cdd:PLN02644  76 PSTICTTVNKVCASGMKAVMLAAQSIQLGINDVVVAGGMESMSNAPKYLPEARKGSRLGhdtvvdgmlkdglWDV---YN 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 145 LTSQGEAAERMADKWALSRDALDDFAFASHQRAATACDAGYFDNETIPVVVEELREKelsePAGVLRQDETIRRdTSREK 224
Cdd:PLN02644 153 DFGMGVCAELCADQYSISREEQDAYAIQSYERAIAAQEAGAFAWEIVPVEVPGGRGR----PSVIVDKDEGLGK-FDPAK 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 225 LSTLKTSFRPDTGRITAGNSSQISDGAAALLLMSADTAKKLGLKARARVVAFTTVGSDPTLMLTGPIAATQKVLAKAGLS 304
Cdd:PLN02644 228 LRKLRPSFKEDGGSVTAGNASSISDGAAALVLVSGEKALELGLQVIAKIRGYADAAQAPELFTTAPALAIPKALKHAGLE 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 305 INDIDLFEVNEAFASVPLAWMQETGVPHSKLNVNGGAIALGHPLGASGARLMTTMLNELERRGGRYGLQAICCAGGMGTA 384
Cdd:PLN02644 308 ASQVDYYEINEAFSVVALANQKLLGLDPEKVNVHGGAVSLGHPIGCSGARILVTLLGVLRSKNGKYGVAGICNGGGGASA 387

                 ....*..
gi 523666866 385 TIIERLD 391
Cdd:PLN02644 388 IVVELMQ 394
PRK06025 PRK06025
acetyl-CoA C-acetyltransferase;
1-390 7.76e-104

acetyl-CoA C-acetyltransferase;


Pssm-ID: 235675 [Multi-domain]  Cd Length: 417  Bit Score: 312.87  E-value: 7.76e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866   1 MKDIVIVDAVRTP--IGKF-RGSLAGVRADHLGSLVISRLLERVDVSPTLVDDVIFGNVTQIGEQSANIARTALLGAGWP 77
Cdd:PRK06025   1 MAEAYIIDAVRTPrgIGKVgKGALAHLHPQHLAATVLKALAERNGLNTADVDDIIWSTSSQRGKQGGDLGRMAALDAGYD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866  78 VTVAGLTIDRKCGSGEVAVHMAVGAIAAGAADIVVAGGAENMS-RVPMGSNREIHGAAFGWMAAQRYEL------TSQGE 150
Cdd:PRK06025  81 IKASGVTLDRFCGGGITSVNLAAAQIMSGMEDLVIAGGTEMMSyTAAMAAEDMAAGKPPLGMGSGNLRLralhpqSHQGV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 151 AAERMADKWALSRDALDDFAFASHQRAATACDAGYFDNETIPVVVEELREkelsepagVLRQDETIRRDTSREKLSTLKT 230
Cdd:PRK06025 161 CGDAIATMEGITREALDALGLESQRRAARAIKEGRFDKSLVPVYRDDGSV--------ALDHEEFPRPQTTAEGLAALKP 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 231 SFRP------DTGRIT-------------------AGNSSQISDGAAALLLMSADTAKKLGLKARARVVAFTTVGSDPTL 285
Cdd:PRK06025 233 AFTAiadyplDDKGTTyrglinqkypdleikhvhhAGNSSGVVDGAAALLLASKAYAEKHGLKPRARIVAMANMGDDPTL 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 286 MLTGPIAATQKVLAKAGLSINDIDLFEVNEAFASVPLAWMQETGVPHSKLNVNGGAIALGHPLGASGARLMTTMLNELER 365
Cdd:PRK06025 313 MLNAPVPAAKKVLAKAGLTKDDIDLWEINEAFAVVAEKFIRDLDLDRDKVNVNGGAIALGHPIGATGSILIGTVLDELER 392
                        410       420
                 ....*....|....*....|....*
gi 523666866 366 RGGRYGLQAICCAGGMGTATIIERL 390
Cdd:PRK06025 393 RGLKRGLVTMCAAGGMAPAIIIERV 417
PRK05656 PRK05656
acetyl-CoA C-acetyltransferase;
1-389 2.71e-100

acetyl-CoA C-acetyltransferase;


Pssm-ID: 168156  Cd Length: 393  Bit Score: 302.96  E-value: 2.71e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866   1 MKDIVIVDAVRTPIGKFRGSLAGVRADHLGSLVISRLLERVDVSPTLVDDVIFGNVTQIGeQSANIARTALLGAGWPVTV 80
Cdd:PRK05656   1 MQDVVIVAATRTAIGSFQGSLANIPAVELGAAVIRRLLEQTGLDPAQVDEVILGQVLTAG-AGQNPARQAAIKAGLPHSV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866  81 AGLTIDRKCGSGEVAVHMAVGAIAAGAADIVVAGGAENMSRVP-----------MGSNREIHGAAFG--WMAAQRYELts 147
Cdd:PRK05656  80 PAMTLNKVCGSGLKALHLAAQAIRCGDAEVIIAGGQENMSLAPyvlpgartglrMGHAQLVDSMITDglWDAFNDYHM-- 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 148 qGEAAERMADKWALSRDALDDFAFASHQRAATACDAGYFDNETIPVVVEELRekelSEPAgVLRQDETIRRDTSREKLST 227
Cdd:PRK05656 158 -GITAENLVEKYGISREAQDAFAAASQQKAVAAIEAGRFDDEITPILIPQRK----GEPL-AFATDEQPRAGTTAESLAK 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 228 LKTSFRPDtGRITAGNSSQISDGAAALLLMSADTAKKLGLKARARVVAFTTVGSDPTLMLTGPIAATQKVLAKAGLSIND 307
Cdd:PRK05656 232 LKPAFKKD-GSVTAGNASSLNDGAAAVLLMSAAKAKALGLPVLAKIAAYANAGVDPAIMGIGPVSATRRCLDKAGWSLAE 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 308 IDLFEVNEAFASVPLAWMQETGVPHSKLNVNGGAIALGHPLGASGARLMTTMLNELERRGGRYGLQAICCAGGMGTATII 387
Cdd:PRK05656 311 LDLIEANEAFAAQSLAVGKELGWDAAKVNVNGGAIALGHPIGASGCRVLVTLLHEMIRRDAKKGLATLCIGGGQGVALAI 390

                 ..
gi 523666866 388 ER 389
Cdd:PRK05656 391 ER 392
PLN02287 PLN02287
3-ketoacyl-CoA thiolase
3-391 2.57e-98

3-ketoacyl-CoA thiolase


Pssm-ID: 215161 [Multi-domain]  Cd Length: 452  Bit Score: 300.14  E-value: 2.57e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866   3 DIVIVDAVRTPIGKF-RGSLAGVRADHLGSLVISRLLERVDVSPTLVDDVIFGNVTQIGEQSANIARTALLGAGWPVTVA 81
Cdd:PLN02287  47 DVVIVAAYRTPICKAkRGGFKDTYPDDLLAPVLKAVVEKTGLNPSEVGDIVVGTVLAPGSQRANECRMAAFYAGFPETVP 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866  82 GLTIDRKCGSGEVAVHMAVGAIAAGAADIVVAGGAENMSRVPMGSNREIHGAAFGWMAAQRYeLTSQGEAAERMADKWAL 161
Cdd:PLN02287 127 VRTVNRQCSSGLQAVADVAAAIKAGFYDIGIGAGVESMTTNPMAWEGGVNPRVESFSQAQDC-LLPMGITSENVAERFGV 205
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 162 SRDALDDFAFASHQRAATACDAGYFDNETIPVVVEELREKELSEPAGVLRQDETIRRDTSREKLSTLKTSFRPDtGRITA 241
Cdd:PLN02287 206 TREEQDQAAVESHRKAAAATASGKFKDEIVPVHTKIVDPKTGEEKPIVISVDDGIRPNTTLADLAKLKPVFKKN-GTTTA 284
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 242 GNSSQISDGAAALLLMSADTAKKLGLKARARVVAFTTVGSDPTLMLTGPIAATQKVLAKAGLSINDIDLFEVNEAFASVP 321
Cdd:PLN02287 285 GNSSQVSDGAGAVLLMKRSVAMQKGLPILGVFRSFAAVGVDPAVMGIGPAVAIPAAVKAAGLELDDIDLFEINEAFASQF 364
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 523666866 322 LAWMQETGVPHSKLNVNGGAIALGHPLGASGARLMTTMLNELERRG--GRYGLQAICCAGGMGTATIIERLD 391
Cdd:PLN02287 365 VYCCKKLGLDPEKVNVNGGAIALGHPLGATGARCVATLLHEMKRRGkdCRFGVVSMCIGTGMGAAAVFERGD 436
PRK07851 PRK07851
acetyl-CoA C-acetyltransferase;
1-390 1.07e-95

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181146 [Multi-domain]  Cd Length: 406  Bit Score: 291.52  E-value: 1.07e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866   1 MKDIVIVDAVRTPIGK-FRGSLAGVRADHLGSLVISRLLERV-DVSPTLVDDVIFGNVTQIGEQSANIARTALLGAGWPv 78
Cdd:PRK07851   1 MPEAVIVSTARSPIGRaFKGSLKDMRPDDLAAQMVRAALDKVpALDPTDIDDLMLGCGLPGGEQGFNMARVVAVLLGYD- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866  79 TVAGLTIDRKCGSGEVAVHMAVGAIAAGAADIVVAGGAENMSRVPMGSNREI---HGAAFGwMAAQRYELTSQGEA---- 151
Cdd:PRK07851  80 FLPGTTVNRYCSSSLQTTRMAFHAIKAGEGDVFISAGVETVSRFAKGNSDSLpdtKNPLFA-EAQARTAARAEGGAeawh 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 152 ------------------AERMADKWALSRDALDDFAFASHQRAATACDAGYFDNETIPVVVeelrekelsePAG-VLRQ 212
Cdd:PRK07851 159 dpredgllpdvyiamgqtAENVAQLTGISREEQDEWGVRSQNRAEEAIANGFFEREITPVTL----------PDGtVVST 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 213 DETIRRDTSREKLSTLKTSFRPDtGRITAGNSSQISDGAAALLLMSADTAKKLGLKARARVVAFTTVGSDPTLMLTGPIA 292
Cdd:PRK07851 229 DDGPRAGTTYEKVSQLKPVFRPD-GTVTAGNACPLNDGAAAVVIMSDTKARELGLTPLARIVSTGVSGLSPEIMGLGPVE 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 293 ATQKVLAKAGLSINDIDLFEVNEAFASVPLAWMQETGVPHSKLNVNGGAIALGHPLGASGARLMTTMLNELERRGGRYGL 372
Cdd:PRK07851 308 ASKQALARAGMSIDDIDLVEINEAFAAQVLPSARELGIDEDKLNVSGGAIALGHPFGMTGARITTTLLNNLQTHDKTFGL 387
                        410
                 ....*....|....*...
gi 523666866 373 QAICCAGGMGTATIIERL 390
Cdd:PRK07851 388 ETMCVGGGQGMAMVLERL 405
PRK08131 PRK08131
3-oxoadipyl-CoA thiolase;
1-391 8.13e-94

3-oxoadipyl-CoA thiolase;


Pssm-ID: 181242 [Multi-domain]  Cd Length: 401  Bit Score: 286.67  E-value: 8.13e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866   1 MKDIVIVDAVRTPIGKFRGSLAGVRADHLGSLVISRLLERVDVSPTLVDDVIFGNVTQIGEQSANIARTALLGAGWPVTV 80
Cdd:PRK08131   1 MLDAYIYDGLRSPFGRHAGALASVRPDDLAATVIRRLLEKSGFPGDDIEDVILGCTNQAGEDSRNVARNALLLAGLPVTV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866  81 AGLTIDRKCGSGEVAVHMAVGAIAAGAADIVVAGGAENMSRVP--MGS-----NREIH------GAAF-GWMAAQRYELT 146
Cdd:PRK08131  81 PGQTVNRLCASGLAAVIDAARAITCGEGDLYLAGGVESMSRAPfvMGKaesafSRDAKvfdttiGARFpNPKIVAQYGND 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 147 SQGEAAERMADKWALSRDALDDFAFASHQRAATACDAGYFDNETIPVVVEELREKelsePAGVLRQDETIRRDTSREKLS 226
Cdd:PRK08131 161 SMPETGDNVAAEFGISREDADRFAAQSQAKYQAAKEEGFFADEITPIEVPQGRKL----PPKLVAEDEHPRPSSTVEALT 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 227 TLKTSFrpDTGRITAGNSSQISDGAAALLLMSADTAKKLGLKARARVVAFTTVGSDPTLMLTGPIAATQKVLAKAGLSIN 306
Cdd:PRK08131 237 KLKPLF--EGGVVTAGNASGINDGAAALLIGSRAAGEKYGLKPMARILSSAAAGVEPRIMGIGPVEAIKKALARAGLTLD 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 307 DIDLFEVNEAFASVPLAWMQETGVPH--SKLNVNGGAIALGHPLGASGARLMTTMLNELERRGGRYGLQAICCAGGMGTA 384
Cdd:PRK08131 315 DMDIIEINEAFASQVLGCLKGLGVDFddPRVNPNGGAIAVGHPLGASGARLALTAARELQRRGKRYAVVSLCIGVGQGLA 394

                 ....*..
gi 523666866 385 TIIERLD 391
Cdd:PRK08131 395 MVIERVS 401
PRK07108 PRK07108
acetyl-CoA C-acyltransferase;
1-390 4.00e-91

acetyl-CoA C-acyltransferase;


Pssm-ID: 180843 [Multi-domain]  Cd Length: 392  Bit Score: 279.35  E-value: 4.00e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866   1 MKDIVIVDAVRTPIGK-FRGSLAGVRADHLGSLVISRLLERVDVSPTLVDDVIFGNVTQIGEQSANIARTALLGAGWPVT 79
Cdd:PRK07108   1 MTEAVIVSTARTPLAKsWRGAFNMTHGATLGGHVVQHAVERAKLDPAEVEDVIMGCANPEGATGANIARQIALRAGLPVT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866  80 VAGLTIDRKCGSGEVAVHMAVGAIAAGAADIVVAGGAENMSRVPMGSNReiHGAAFGWMAAQRYELT-SQGEAAERMADK 158
Cdd:PRK07108  81 VPGMTVNRFCSSGLQTIALAAQRVIAGEGDVFVAGGVESISCVQNEMNR--HMLREGWLVEHKPEIYwSMLQTAENVAKR 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 159 WALSRDALDDFAFASHQRAATACDAGYFDNETIPVVVE---------ELREKELSepagvLRQDETIRRDTSREKLSTLK 229
Cdd:PRK07108 159 YGISKERQDEYGVQSQQRAAAAQAAGRFDDEIVPITVTagvadkatgRLFTKEVT-----VSADEGIRPDTTLEGVSKIR 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 230 TSFrpDTGRITAGNSSQISDGAAALLLMSADTAKKLGLKARARVVAFTTVGSDPTLMLTGPIAATQKVLAKAGLSINDID 309
Cdd:PRK07108 234 SAL--PGGVITAGNASQFSDGASACVVMNAKVAEREGLQPLGIFRGFAVAGCEPDEMGIGPVFAVPKLLKQAGLKVDDID 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 310 LFEVNEAFASVPLAWMQETGVPHSKLNVNGGAIALGHPLGASGARLMTTMLNELERRGGRYGLQAICCAGGMGTATIIER 389
Cdd:PRK07108 312 LWELNEAFAVQVLYCRDTLGIPMDRLNVNGGAIAVGHPYGVSGARLTGHALIEGKRRGAKYVVVTMCIGGGQGAAGLFEV 391

                 .
gi 523666866 390 L 390
Cdd:PRK07108 392 L 392
PRK06633 PRK06633
acetyl-CoA C-acetyltransferase;
1-388 6.73e-91

acetyl-CoA C-acetyltransferase;


Pssm-ID: 168632 [Multi-domain]  Cd Length: 392  Bit Score: 278.84  E-value: 6.73e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866   1 MKDIVIVDAVRTPIGKFRGSLAGVRADHLGSLVISRLLERVDVSPTLVDDVIFGNVTQiGEQSANIARTALLGAGWPVTV 80
Cdd:PRK06633   2 TKPVYITHAKRTAFGSFMGSLSTTPAPMLAAHLIKDILQNSKIDPALVNEVILGQVIT-GGSGQNPARQTLIHAGIPKEV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866  81 AGLTIDRKCGSGEVAVHMAVGAIAAGAADIVVAGGAENMSRVPMGSNREIhGAAFG---WMAAQRYE-LTS------QGE 150
Cdd:PRK06633  81 PGYTINKVCGSGLKSVALAANSIMTGDNEIVIAGGQENMSLGMHGSYIRA-GAKFGdikMVDLMQYDgLTDvfsgvfMGI 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 151 AAERMADKWALSRDALDDFAFASHQRAATACDAGYFDNETIPVvveelrEKELSEPAGVLRQDETIRRDTSREKLSTLKT 230
Cdd:PRK06633 160 TAENISKQFNISRQEQDEFALSSHKKAAKAQLAGIFKDEILPI------EVTIKKTTSLFDHDETVRPDTSLEILSKLRP 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 231 SFRPDtGRITAGNSSQISDGAAALLLMSADTAKKLGLKARARVVAFTTVGSDPTLMLTGPIAATQKVLAKAGLSINDIDL 310
Cdd:PRK06633 234 AFDKN-GVVTAGNASSINDGAACLMVVSEEALKKHNLTPLARIVSYASAGVDPSIMGTAPVPASQKALSKAGWSVNDLEV 312
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 523666866 311 FEVNEAFASVPLAWMQETGVPHSKLNVNGGAIALGHPLGASGARLMTTMLNELERRGGRYGLQAICCAGGMGTATIIE 388
Cdd:PRK06633 313 IEVNEAFAAQSIYVNREMKWDMEKVNINGGAIAIGHPIGASGGRVLITLIHGLRRAKAKKGLVTLCIGGGMGMAMCVE 390
fadI PRK08963
3-ketoacyl-CoA thiolase; Reviewed
4-389 2.80e-90

3-ketoacyl-CoA thiolase; Reviewed


Pssm-ID: 181597 [Multi-domain]  Cd Length: 428  Bit Score: 278.41  E-value: 2.80e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866   4 IVIVDAVRTPIGKFRGSLAGVRADHLGSLVISRLLERVDVSPTLVDDVIFGNVTQIGEqSANIARTALLGAGWPVTVAGL 83
Cdd:PRK08963   7 IAIVSGLRTPFAKQATAFHGIPAVDLGKMVVGELLARSEIDPELIEQLVFGQVVQMPE-APNIAREIVLGTGMNVHTDAY 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866  84 TIDRKCGSGEVAVHMAVGAIAAGAADIVVAGGAENMSRVPMGSNRE----IHGAAFGWMAAQRYELTSQ----------- 148
Cdd:PRK08963  86 SVSRACATSFQAVANVAESIMAGTIDIGIAGGADSSSVLPIGVSKKlaraLVDLNKARTLGQRLKLFSRlrlrdllpvpp 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 149 -----------GEAAERMADKWALSRDALDDFAFASHQRAATACDAGYFDNETIPVVVEELREkelsepagVLRQDETIR 217
Cdd:PRK08963 166 avaeystglrmGDTAEQMAKTYGISREEQDALAHRSHQLAAQAWAEGKLDDEVMTAHVPPYKQ--------PLEEDNNIR 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 218 RDTSREKLSTLKTSFRPDTGRITAGNSSQISDGAAALLLMSADTAKKLGLK--ARARVVAFT--TVGSDptlMLTGPIAA 293
Cdd:PRK08963 238 GDSTLEDYAKLRPAFDRKHGTVTAANSTPLTDGAAAVLLMSESRAKALGLTplGYLRSYAFAaiDVWQD---MLLGPAYA 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 294 TQKVLAKAGLSINDIDLFEVNEAFASVPLAWMQETG-----------------VPHSKLNVNGGAIALGHPLGASGARLM 356
Cdd:PRK08963 315 TPLALERAGLTLADLTLIDMHEAFAAQTLANLQMFAserfareklgrsqaigeVDMSKFNVLGGSIAYGHPFAATGARMI 394
                        410       420       430
                 ....*....|....*....|....*....|...
gi 523666866 357 TTMLNELERRGGRYGLQAICCAGGMGTATIIER 389
Cdd:PRK08963 395 TQTLHELRRRGGGLGLTTACAAGGLGAAMVLEV 427
PRK06954 PRK06954
acetyl-CoA C-acetyltransferase;
4-388 1.49e-88

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180775 [Multi-domain]  Cd Length: 397  Bit Score: 272.92  E-value: 1.49e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866   4 IVIVDAVRTPIGKFRGSLAGVRADHLGSLVISRLLERVDVSPTLVDDVIFGNVTQIGEQSANiARTALLGAGWPVTVAGL 83
Cdd:PRK06954   9 IVIASAARTPMAAFQGEFASLTAPQLGAAAIAAAVERAGLKPEQIDEVVMGCVLPAGQGQAP-ARQAALGAGLPLSVGCT 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866  84 TIDRKCGSGEVAVHMAVGAIAAGAADIVVAGGAENMSRVPM------GSNREIHGAAFGWMAAQRYELT-----SQGEAA 152
Cdd:PRK06954  88 TVNKMCGSGMRAAMFAHDMLVAGSVDVIVAGGMESMTNAPYllpkarGGMRMGHGQVLDHMFLDGLEDAydkgrLMGTFA 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 153 ERMADKWALSRDALDDFAFASHQRAATACDAGYFDNETIPVVVEELREKElsepagVLRQDETIRRdTSREKLSTLKTSF 232
Cdd:PRK06954 168 EECAGEYGFTREAQDAFAIESLARAKRANEDGSFAWEIAPVTVAGKKGDT------VIDRDEQPFK-ANPEKIPTLKPAF 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 233 RPDtGRITAGNSSQISDGAAALLLMSADTAKKLGLKARARVVAFTTVGSDPTLMLTGPIAATQKVLAKAGLSINDIDLFE 312
Cdd:PRK06954 241 SKT-GTVTAANSSSISDGAAALVMMRASTAKRLGLAPLARVVGHSTFAQAPSKFTTAPVGAIRKLFEKNGWRAAEVDLFE 319
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 523666866 313 VNEAFASVPLAWMQETGVPHSKLNVNGGAIALGHPLGASGARLMTTMLNELERRGGRYGLQAICCAGGMGTATIIE 388
Cdd:PRK06954 320 INEAFAVVTMAAMKEHGLPHEKVNVNGGACALGHPIGASGARILVTLIGALRARGGKRGVASLCIGGGEATAMGIE 395
PRK06690 PRK06690
acetyl-CoA C-acyltransferase;
5-390 6.93e-83

acetyl-CoA C-acyltransferase;


Pssm-ID: 180659 [Multi-domain]  Cd Length: 361  Bit Score: 257.39  E-value: 6.93e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866   5 VIVDAVRTPIGKFRGSLAGVRADHLGSLVISRLLERVdvsPTLVDDVIFGNVTQIGeqsANIARTALLGAGWPVTVAGLT 84
Cdd:PRK06690   4 VIVEAKRTPIGKKNGMLKDYEVQQLAAPLLTFLSKGM---EREIDDVILGNVVGPG---GNVARLSALEAGLGLHIPGVT 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866  85 IDRKCGSGEVAVHMAVGAIAAGAADIVVAGGAENMSRVPMgSNReihgAAFgwmAAQRYELTSQGEAAERMADKWALSRD 164
Cdd:PRK06690  78 IDRQCGAGLEAIRTACHFIQGGAGKCYIAGGVESTSTSPF-QNR----ARF---SPETIGDPDMGVAAEYVAERYNITRE 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 165 ALDDFAFASHQRAATACDAGYFDNETIPVvveelrekelsepAGVLrqDETIRRDTSREKL-STLKTSFRPDtGRITAGN 243
Cdd:PRK06690 150 MQDEYACLSYKRTLQALEKGYIHEEILSF-------------NGLL--DESIKKEMNYERIiKRTKPAFLHN-GTVTAGN 213
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 244 SSQISDGAAALLLMSADTAKKLGLKARARVVAFTTVGSDPTLMLTGPIAATQKVLAKAGLSINDIDLFEVNEAFASVPLA 323
Cdd:PRK06690 214 SCGVNDGACAVLVMEEGQARKLGYKPVLRFVRSAVVGVDPNLPGTGPIFAVNKLLNEMNMKVEDIDYFEINEAFASKVVA 293
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 523666866 324 WMQETGVPHSKLNVNGGAIALGHPLGASGARLMTTMLNELERRGGRYGLQAICCAGGMGTATIIERL 390
Cdd:PRK06690 294 CAKELQIPYEKLNVNGGAIALGHPYGASGAMLVTRLFYQAKREDMKYGIATLGIGGGIGLALLFEKV 360
PRK08170 PRK08170
acetyl-CoA C-acetyltransferase;
1-390 1.39e-81

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181265 [Multi-domain]  Cd Length: 426  Bit Score: 256.10  E-value: 1.39e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866   1 MKDIVIVDAVRTPIGKFRGSLAGVRADHLGSLVISRLLERVDVSPTLVDDVIFGNVTQIGEQsANIARTALLGAGWPVTV 80
Cdd:PRK08170   2 ARPVYIVDGARTPFLKARGGPGPFSASDLAVAAGRALLNRQPFAPDDLDEVILGCAMPSPDE-ANIARVVALRLGCGEKV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866  81 AGLTIDRKCGSGEVAVHMAVGAIAAGAADIVVAGGAENMSRVPMGSNREIHGAAFGWMAAQ--------------RY--- 143
Cdd:PRK08170  81 PAWTVQRNCASGMQALDSAAANIALGRADLVLAGGVEAMSHAPLLFSEKMVRWLAGWYAAKsigqklaalgklrpSYlap 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 144 ------ELT------SQGEAAERMADKWALSRDALDDFAFASHQRAATACDAGYFdNETIPVVVEELRekelsepagVLR 211
Cdd:PRK08170 161 vigllrGLTdpvvglNMGQTAEVLAHRFGITREQMDAYAARSHQRLAAAQAEGRL-KEVVPLFDRDGK---------FYD 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 212 QDETIRRDTSREKLSTLKTSFRPDTGRITAGNSSQISDGAAALLLMSADTAKKLGLKARARVVAFTTVGSDPTLMLTGPI 291
Cdd:PRK08170 231 HDDGVRPDSSMEKLAKLKPFFDRPYGRVTAGNSSQITDGACWLLLASEEAVKKYGLPPLGRIVDSQWAALDPSQMGLGPV 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 292 AATQKVLAKAGLSINDIDLFEVNEAFASVPL----AW------MQETGVPHS-------KLNVNGGAIALGHPLGASGAR 354
Cdd:PRK08170 311 HAATPLLQRHGLTLEDLDLWEINEAFAAQVLaclaAWadeeycREQLGLDGAlgeldreRLNVDGGAIALGHPVGASGAR 390
                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 523666866 355 LMTTMLNELERRGGRYGLQAICCAGGMGTATIIERL 390
Cdd:PRK08170 391 IVLHLLHALKRRGTKRGIAAICIGGGQGGAMLLERV 426
PRK06366 PRK06366
acetyl-CoA C-acetyltransferase;
1-391 2.98e-74

acetyl-CoA C-acetyltransferase;


Pssm-ID: 102340 [Multi-domain]  Cd Length: 388  Bit Score: 236.06  E-value: 2.98e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866   1 MKDIVIVDAVRTPIGKFRGSLAGVRADHLGSLVISRLLERVDVSPTLVDDVIFGNVTQIGeQSANIARTALLGAGWPVTV 80
Cdd:PRK06366   1 MKDVYIVSAKRTAIGKFGRSFSKIKAPQLGGAAIKAVIDDAKLDPALVQEVIMGNVIQAG-VGQNPAGQAAYHAGLPFGV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866  81 AGLTIDRKCGSGEVAVHMAVGAIAAGAADIVVAGGAENMSRVP--------------MGSNREIHGAAF--GWMAAQRYE 144
Cdd:PRK06366  80 TKYTVNVVCASGMLAVESAAREIMLGERDLVIAGGMENMSNAPfllpsdlrwgpkhlLHKNYKIDDAMLvdGLIDAFYFE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 145 ltSQGEAAERMADKWALSRDALDDFAFASHQRAATACDAGYFDNETIPVvveelrekelsepaGVLRQDETIRRdTSREK 224
Cdd:PRK06366 160 --HMGVSAERTARKYGITREMADEYSVQSYERAIRATESGEFRNEIVPF--------------NDLDRDEGIRK-TTMED 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 225 LSTLKTSFRPDtGRITAGNSSQISDGAAALLLMSADTAKKLGLKARARVVAFTTVGSDPTLMLTGPIAATQKVLAKAGLS 304
Cdd:PRK06366 223 LAKLPPAFDKN-GILTAGNSAQLSDGGSALVMASEKAINEYGLKPIARITGYESASLDPLDFVEAPIPATRKLLEKQNKS 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 305 INDIDLFEVNEAFASVPLAWMQETGVPHSKLNVNGGAIALGHPLGASGARLMTTMLNELERRGGRYGLQAICCAGGMGTA 384
Cdd:PRK06366 302 IDYYDLVEHNEAFSIASIIVRDQLKIDNERFNVNGGAVAIGHPIGNSGSRIIVTLINALKTRHMKTGLATLCHGGGGAHT 381

                 ....*..
gi 523666866 385 TIIERLD 391
Cdd:PRK06366 382 LTLEMVE 388
Thiolase_N pfam00108
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
4-260 3.52e-70

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: 221.02  E-value: 3.52e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866    4 IVIVDAVRTPIGKFRGSLAGVRADHLGSLVISRLLERVDVSPTLVDDVIFGNVTQiGEQSANIARTALLGAGWPVTVAGL 83
Cdd:pfam00108   1 VVIVSAARTPFGSFGGSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQ-AGEGQNPARQAALKAGIPDSAPAV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866   84 TIDRKCGSGEVAVHMAVGAIAAGAADIVVAGGAENMSRVPMGSNREIH-GAAFGwmAAQRYELTS------------QGE 150
Cdd:pfam00108  80 TINKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALPTDARsGLKHG--DEKKHDLLIpdgltdafngyhMGL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866  151 AAERMADKWALSRDALDDFAFASHQRAATACDAGYFDNETIPVVVEELREKelsepaGVLRQDETIRRDTSREKLSTLKT 230
Cdd:pfam00108 158 TAENVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDEIVPVTVKGRKGK------PTVDKDEGIRPPTTAEPLAKLKP 231
                         250       260       270
                  ....*....|....*....|....*....|
gi 523666866  231 SFRPDtGRITAGNSSQISDGAAALLLMSAD 260
Cdd:pfam00108 232 AFDKE-GTVTAGNASPINDGAAAVLLMSES 260
PRK09268 PRK09268
acetyl-CoA C-acetyltransferase;
147-389 5.24e-55

acetyl-CoA C-acetyltransferase;


Pssm-ID: 236440 [Multi-domain]  Cd Length: 427  Bit Score: 187.03  E-value: 5.24e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 147 SQGEAAERMADKWALSRDALDDFAFASHQRAATACDAGYFDnetipvvveelrekELSEPAGVLRQDETIRRDTSREKLS 226
Cdd:PRK09268 177 SMGEHAAITAKEWGISREAQDELAAASHQNLAAAYDRGFFD--------------DLITPFLGLTRDNNLRPDSSLEKLA 242
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 227 TLKTSF-RPDTGRITAGNSSQISDGAAALLLMSADTAKKLGLKARARVVAFTTV------GSDPTLMltGPIAATQKVLA 299
Cdd:PRK09268 243 KLKPVFgKGGRATMTAGNSTPLTDGASVVLLASEEWAAEHGLPVLAYLVDAETAavdfvhGKEGLLM--APAYAVPRLLA 320
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 300 KAGLSINDIDLFEVNEAFASVPL----AWMQET-------------GVPHSKLNVNGGAIALGHPLGASGARLMTTMLNE 362
Cdd:PRK09268 321 RNGLTLQDFDFYEIHEAFASQVLatlkAWEDEEycrerlgldaplgSIDRSKLNVNGSSLAAGHPFAATGGRIVATLAKL 400
                        250       260
                 ....*....|....*....|....*..
gi 523666866 363 LERRGGRYGLQAICCAGGMGTATIIER 389
Cdd:PRK09268 401 LAEKGSGRGLISICAAGGQGVTAILER 427
Thiolase_C pfam02803
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
267-389 7.49e-55

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: 176.68  E-value: 7.49e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866  267 LKARARVVAFTTVGSDPTLMLTGPIAATQKVLAKAGLSINDIDLFEVNEAFASVPLAWMQETGVPHSKLNVNGGAIALGH 346
Cdd:pfam02803   1 LKPLARIRSYATAGVDPAIMGIGPAYAIPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGIDPEKVNVNGGAIALGH 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 523666866  347 PLGASGARLMTTMLNELERRGGRYGLQAICCAGGMGTATIIER 389
Cdd:pfam02803  81 PLGASGARILVTLLHELKRRGGKYGLASLCIGGGQGVAMIIER 123
nondecarbox_cond_enzymes cd00826
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ...
7-388 2.68e-45

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: 160.74  E-value: 2.68e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866   7 VDAVRTPIGKF---RGSLAGVRADHLGSLVISRLLERVDVSPTLVDDVIFGNVTQIGEQSaNIARTALLGAGWPVTVAGL 83
Cdd:cd00826    1 AGAAMTAFGKFggeNGADANDLAHEAGAKAIAAALEPAGVAAGAVEEACLGQVLGAGEGQ-NCAQQAAMHAGGLQEAPAI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866  84 TIDRKCGSGEVAVHMAVGAIAAGAADIVVAGGAENMSRVPMGSNREIHgaafgwmaaqryeltsqgeaAERMADKWAlSR 163
Cdd:cd00826   80 GMNNLCGSGLRALALAMQLIAGGDANCILAGGFEKMETSAENNAKEKH--------------------IDVLINKYG-MR 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 164 DALDDFAFASHQRAATACDAGYFDNETIPVVVEELREKELSEpagvlrQDETIR--RDTSREKLSTLKTSFRPDtGRITA 241
Cdd:cd00826  139 ACPDAFALAGQAGAEAAEKDGRFKDEFAKFGVKGRKGDIHSD------ADEYIQfgDEASLDEIAKLRPAFDKE-DFLTA 211
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 242 GNSSQISDGAAALLLMSADTAKKLGLKARA-------RVVAFTTVGSDPT----LMLTGPIAATQKVLAKAGLSINDIDL 310
Cdd:cd00826  212 GNACGLNDGAAAAILMSEAEAQKHGLQSKAreiqaleMITDMASTFEDKKvikmVGGDGPIEAARKALEKAGLGIGDLDL 291
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 311 FEVNEAFASVPLAWMQETGV------------------PHSKLNVNGGAIALGHPLGASGARLMTTMLNELERRGG---- 368
Cdd:cd00826  292 IEAHDAFAANACATNEALGLcpegqggalvdrgdntygGKSIINPNGGAIAIGHPIGASGAAICAELCFELKGEAGkrqg 371
                        410       420
                 ....*....|....*....|.
gi 523666866 369 -RYGLQAICCAGGMGTATIIE 388
Cdd:cd00826  372 aGAGLALLCIGGGGGAAMCIE 392
SCP-x_thiolase cd00829
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ...
33-387 3.42e-19

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: 88.09  E-value: 3.42e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866  33 VISRLLERVDVSPTLVDDVIFGNVTQIGEQS---ANIARTALLGAGWPVTVagltiDRKCGSGEVAVHMAVGAIAAGAAD 109
Cdd:cd00829   23 AARAALDDAGLEPADIDAVVVGNAAGGRFQSfpgALIAEYLGLLGKPATRV-----EAAGASGSAAVRAAAAAIASGLAD 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 110 IVVAGGAENMSRVPMGSNREIHGAAFGWMAAQRYELTSQ----GEAAERMADKWALSRDALDDFAFASHQRAATACDAGY 185
Cdd:cd00829   98 VVLVVGAEKMSDVPTGDEAGGRASDLEWEGPEPPGGLTPpalyALAARRYMHRYGTTREDLAKVAVKNHRNAARNPYAQF 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 186 FDNETipvVVEELREKELSEPagvlrqdetirrdtsreklstlktsfrpdtgrITAGNSSQISDGAAALLLMSADTAKKL 265
Cdd:cd00829  178 RKPIT---VEDVLNSRMIADP--------------------------------LRLLDCCPVSDGAAAVVLASEERAREL 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 266 GLKArARVVAfTTVGSDPTLM--------LTGPIAATQKVLAKAGLSINDIDLFEVNEAFASVPLAWMQETG-------- 329
Cdd:cd00829  223 TDRP-VWILG-VGAASDTPSLserddflsLDAARLAARRAYKMAGITPDDIDVAELYDCFTIAELLALEDLGfcekgegg 300
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 330 -------------VPHsklNVNGGAIALGHPLGASGARlmttMLNELER--RGGRYGLQAICC-------AGGMGTATII 387
Cdd:cd00829  301 klvregdtaiggdLPV---NTSGGLLSKGHPLGATGLA----QAVEAVRqlRGEAGARQVPGArvglahnIGGTGSAAVV 373
cond_enzymes cd00327
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ...
241-387 6.59e-14

Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) Claisen-like condensation reaction. Members are share strong structural similarity, and are involved in the synthesis and degradation of fatty acids, and the production of polyketides, a diverse group of natural products.


Pssm-ID: 238201 [Multi-domain]  Cd Length: 254  Bit Score: 70.94  E-value: 6.59e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 241 AGNSSQISDGAAALLLMSADTAKKLGLKARARVVAFTTVGSDPT----LMLTGPIAATQKVLAKAGLSINDIDLFEVNEA 316
Cdd:cd00327   94 GSEEFVFGDGAAAAVVESEEHALRRGAHPQAEIVSTAATFDGASmvpaVSGEGLARAARKALEGAGLTPSDIDYVEAHGT 173
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 317 FASVPLAWMQETGVPHSK---LNVNGGAIALGHPLGASGARLMTTMLNELE-------RRGGRYGLQAICCAGGMGTATI 386
Cdd:cd00327  174 GTPIGDAVELALGLDPDGvrsPAVSATLIMTGHPLGAAGLAILDELLLMLEhefipptPREPRTVLLLGFGLGGTNAAVV 253

                 .
gi 523666866 387 I 387
Cdd:cd00327  254 L 254
PTZ00455 PTZ00455
3-ketoacyl-CoA thiolase; Provisional
245-375 1.58e-10

3-ketoacyl-CoA thiolase; Provisional


Pssm-ID: 240424 [Multi-domain]  Cd Length: 438  Bit Score: 62.22  E-value: 1.58e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 245 SQISDGAAALLLMSADTAKKLGLKAR-ARVVAFTTVGS----------DPTLMLTGPIAAtQKVLAKAGLSINDIDLFEV 313
Cdd:PTZ00455 256 SQVSDGGAGLVLASEEGLQKMGLSPNdSRLVEIKSLACasgnlyedppDATRMFTSRAAA-QKALSMAGVKPSDLQVAEV 334
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 314 NEAFASVPLAWMQETGVP---HSK---------------LNVNGGAIALGHPLGASGARLMTTMLNELERRGGRYGLQAI 375
Cdd:PTZ00455 335 HDCFTIAELLMYEALGIAeygHAKdlirngatalegripVNTGGGLLSFGHPVGATGVKQIMEVYRQMKGQCGEYQMKNI 414
PRK07516 PRK07516
thiolase domain-containing protein;
245-352 2.08e-10

thiolase domain-containing protein;


Pssm-ID: 181013 [Multi-domain]  Cd Length: 389  Bit Score: 61.89  E-value: 2.08e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 245 SQISDGAAALLLMSADTAKKL----GLKARARVVAFTTVGSDPTLMLTGPIAATQKVLAKAGLSINDIDLFEVNEAFASV 320
Cdd:PRK07516 213 SLVSDGAAALVLADAETARALqravRFRARAHVNDFLPLSRRDPLAFEGPRRAWQRALAQAGVTLDDLSFVETHDCFTIA 292
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 523666866 321 PL--------------------AWMQETGvphsKLNVN--GGAIALGHPLGASG 352
Cdd:PRK07516 293 ELieyeamglappgqgaraireGWTAKDG----KLPVNpsGGLKAKGHPIGATG 342
PRK06064 PRK06064
thiolase domain-containing protein;
244-354 2.90e-09

thiolase domain-containing protein;


Pssm-ID: 235688 [Multi-domain]  Cd Length: 389  Bit Score: 58.37  E-value: 2.90e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 244 SSQISDGAAALLLMSADTAKKL---GLKARARVVAFTTVG-SDPTLMLT--GPIAATQKVLAKAGLSINDIDLFEVNEAF 317
Cdd:PRK06064 208 CSPITDGAAAVILASEEKAKEYtdtPVWIKASGQASDTIAlHDRKDFTTldAAVVAAEKAYKMAGIEPKDIDVAEVHDCF 287
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 523666866 318 ASVPLAWMQETG---------------------VPhskLNVNGGAIALGHPLGASGAR 354
Cdd:PRK06064 288 TIAEILAYEDLGfakkgeggklaregqtyiggdIP---VNPSGGLKAKGHPVGATGVS 342
PRK06289 PRK06289
acetyl-CoA acetyltransferase; Provisional
237-356 2.40e-07

acetyl-CoA acetyltransferase; Provisional


Pssm-ID: 235771 [Multi-domain]  Cd Length: 403  Bit Score: 52.38  E-value: 2.40e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 237 GRITAGNSSQISDGAAALLLMSADTAKKLGlKAR--ARVVAF--TTVG----------SDPTLMLTGPIAATQKVLAKAG 302
Cdd:PRK06289 212 GRLRRQDCSQVTDGGAGVVLASDAYLRDYA-DARpiPRIKGWghRTAPlgleqkldrsAGDPYVLPHVRQAVLDAYRRAG 290
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 523666866 303 LSINDIDLFEVNEAFASVPLAWMQETGV----------------PHSKLNVN--GGAIALGHPLGASGARLM 356
Cdd:PRK06289 291 VGLDDLDGFEVHDCFTPSEYLAIDHIGLtgpgeswkaiengeiaIGGRLPINpsGGLIGGGHPVGASGVRML 362
PRK08256 PRK08256
lipid-transfer protein; Provisional
248-352 6.71e-06

lipid-transfer protein; Provisional


Pssm-ID: 181327 [Multi-domain]  Cd Length: 391  Bit Score: 47.59  E-value: 6.71e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 248 SDGAAALLLMSADTAKKLGLKARARVV--AFTT--------------VGSDPTlmltgpIAATQKVLAKAGLSINDIDLF 311
Cdd:PRK08256 214 TCGAAAAIVCSEEFARKHGLDRAVEIVaqAMTTdtpstfdgrsmidlVGYDMT------RAAAQQVYEQAGIGPEDIDVV 287
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 523666866 312 EVNEAFAS------VPLAWMQETGVPhsKL--------------NVNGGAIALGHPLGASG 352
Cdd:PRK08256 288 ELHDCFSAnelltyEALGLCPEGEAE--KFiddgdntyggrwvvNPSGGLLSKGHPLGATG 346
PRK05952 PRK05952
beta-ketoacyl-ACP synthase;
249-353 1.69e-05

beta-ketoacyl-ACP synthase;


Pssm-ID: 235653 [Multi-domain]  Cd Length: 381  Bit Score: 46.58  E-value: 1.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 249 DGAAALLLMSADTAKKLGLKARARVVAFTTV-----GSDPTLMLTGPIAATQKVLAKAGLSINDIDLF-------EVNEA 316
Cdd:PRK05952 210 EGGAILVLESAELAQKRGAKIYGQILGFGLTcdayhMSAPEPDGKSAIAAIQQCLARSGLTPEDIDYIhahgtatRLNDQ 289
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 523666866 317 FASvplAWMQeTGVPHsKLNVNGGAIALGHPLGASGA 353
Cdd:PRK05952 290 REA---NLIQ-ALFPH-RVAVSSTKGATGHTLGASGA 321
PRK12578 PRK12578
thiolase domain-containing protein;
243-368 1.78e-05

thiolase domain-containing protein;


Pssm-ID: 183606 [Multi-domain]  Cd Length: 385  Bit Score: 46.38  E-value: 1.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 243 NSSQISDGAAALLLMSADTAKKLGLKArarVVAFTTVG--SDPTLM--------LTGPIAATQKVLAKAGLSINDIDLFE 312
Cdd:PRK12578 205 DSCPISDGSATAIFASEEKVKELKIDS---PVWITGIGyaNDYAYVarrgewvgFKATQLAARQAYNMAKVTPNDIEVAT 281
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 523666866 313 VNEAFASVPLAWMQETGVPHS----------------KLNVN--GGAIALGHPLGASGARLMTTMLNELERRGG 368
Cdd:PRK12578 282 VHDAFTIAEIMGYEDLGFTEKgkggkfieegqsekggKVGVNlfGGLKAKGHPLGATGLSMIYEITKQLRDEAG 355
PRK08257 PRK08257
acetyl-CoA acetyltransferase; Validated
249-372 2.36e-05

acetyl-CoA acetyltransferase; Validated


Pssm-ID: 236204 [Multi-domain]  Cd Length: 498  Bit Score: 46.06  E-value: 2.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 249 DGAAALLLMSADTAKKLGLkARARVVAF--TTVGSDPTLMLTGP--------IAATQKVLAKAGLSINDIDLFEVNEAFA 318
Cdd:PRK08257 244 DQGAAVLLTSVAKARRLGV-PEDRWVYLhgGADAHDPYDILERPdlhrspaiRAAGRRALALAGLGIDDIDAFDLYSCFP 322
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 523666866 319 SVPLAWMQETGVPHSK---LNVNGgaialGHPL-GASGARLMT----TMLNELERRGGRYGL 372
Cdd:PRK08257 323 SAVQVAARELGLDLDDprpLTVTG-----GLPFfGGPGNNYVThaiaEMVERLRANPGRRGL 379
PRK06157 PRK06157
acetyl-CoA acetyltransferase; Validated
247-369 3.07e-05

acetyl-CoA acetyltransferase; Validated


Pssm-ID: 180433 [Multi-domain]  Cd Length: 398  Bit Score: 45.79  E-value: 3.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 247 ISDGAAALLLMSADTAKKLGLKARARVVAFT-TVGSDPTLMLTG--------PIAATQKVLAKAGLS--INDIDLFEVNE 315
Cdd:PRK06157 216 VSDGAAAAIVTTPEIARALGKKDPVYVKALQlAVSNGWELQYNGwdgsyfptTRIAARKAYREAGITdpREELSMAEVHD 295
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 523666866 316 AFASVPLAWMQETG---------------------VPhskLNVNGGAIALGHPLGASGARLMTTM-LNELERRGGR 369
Cdd:PRK06157 296 CFSITELVTMEDLGlsergqawrdvldgffdadggLP---CQIDGGLKCFGHPIGASGLRMLYEMyLQLLGRAGER 368
elong_cond_enzymes cd00828
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ...
248-366 9.22e-05

"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, including beta-ketoacyl [ACP] synthase, type I and II and polyketide synthases.They are characterized by the utlization of acyl carrier protein (ACP) thioesters as primer substrates, as well as the nature of their active site residues.


Pssm-ID: 238424 [Multi-domain]  Cd Length: 407  Bit Score: 44.35  E-value: 9.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 248 SDGAAALLLMSADTAKKLGLKARARvVAFTTVGSDP-----TLMLTGPIAATQKVLAKAGLSINDIDLfeVNEAFASVPL 322
Cdd:cd00828  230 AEGAGVLVLERAELALARGAPIYGR-VAGTASTTDGagrsvPAGGKGIARAIRTALAKAGLSLDDLDV--ISAHGTSTPA 306
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 523666866 323 AWMQETGVPHSKLNVNGGAIAL-------GHPLGASGARLMTTMLNELERR 366
Cdd:cd00828  307 NDVAESRAIAEVAGALGAPLPVtaqkalfGHSKGAAGALQLIGALQSLEHG 357
FabB COG0304
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...
247-353 8.89e-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: 41.23  E-value: 8.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 247 ISDGAAALLLMSADTAKKLGLKARARVVAF--TTVGSDPTLM---LTGPIAATQKVLAKAGLSINDIDLfeVNeafA--- 318
Cdd:COG0304  229 LGEGAGVLVLEELEHAKARGAKIYAEVVGYgaSSDAYHITAPapdGEGAARAMRAALKDAGLSPEDIDY--IN---Ahgt 303
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 523666866 319 SVPLAWMQET-------GVPHSKLNVNggAI--ALGHPLGASGA 353
Cdd:COG0304  304 STPLGDAAETkaikrvfGDHAYKVPVS--STksMTGHLLGAAGA 345
PRK06059 PRK06059
lipid-transfer protein; Provisional
248-329 1.00e-03

lipid-transfer protein; Provisional


Pssm-ID: 180373 [Multi-domain]  Cd Length: 399  Bit Score: 40.90  E-value: 1.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 248 SDGAAALLLMSADTAKKLGLKARA--RVVAFTTV--------------GSDPTLMLTGPI-----AATQKVLAKAGLSIN 306
Cdd:PRK06059 212 SDGAAALIVASKSFARRHLGSVAGvpSVRAISTVtprypqhlpelpdiATDSTAAVPAPErvfkdQILDAAYAEAGIGPE 291
                         90       100
                 ....*....|....*....|...
gi 523666866 307 DIDLFEVNEAFASVPLAWMQETG 329
Cdd:PRK06059 292 DLSLAEVYDLSTALELDWYEHLG 314
PRK06158 PRK06158
thiolase; Provisional
247-347 1.16e-03

thiolase; Provisional


Pssm-ID: 180434 [Multi-domain]  Cd Length: 384  Bit Score: 40.78  E-value: 1.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 247 ISDGAAALLLMSADTAKKLGLK-----ARARVVAFTTVGSDPTLMLTGPIAATQKVLAKAGLSINDIDLFEVNEAFASVP 321
Cdd:PRK06158 208 VTDGAGAVVMVRADRARDLPRPpvyvlGAAAATWHRQISSMPDLTVTAAAESGPRAFAMAGLTPADIDVVELYDAFTINT 287
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 523666866 322 LAWMQETG----------------VPHSKL--NVNGGAIALGHP 347
Cdd:PRK06158 288 ILFLEDLGfcakgeggafveggriAPGGRLpvNTNGGGLSCVHP 331
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
247-353 2.29e-03

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: 39.83  E-value: 2.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666866 247 ISDGAAALLLMSADTAKKLGLKARARVV-------AFTTVGSDPTLMltGPIAATQKVLAKAGLSINDIDLfeVN----- 314
Cdd:cd00834  229 LGEGAGVLVLESLEHAKARGAKIYAEILgygassdAYHITAPDPDGE--GAARAMRAALADAGLSPEDIDY--INahgts 304
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 523666866 315 -------EAFAsvplawMQETGVPH-SKLNVNG--GAIalGHPLGASGA 353
Cdd:cd00834  305 tplndaaESKA------IKRVFGEHaKKVPVSStkSMT--GHLLGAAGA 345
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH