NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1897357825|ref|NP_001373617|]
View 

acetyl-CoA acetyltransferase, mitochondrial isoform e [Homo sapiens]

Protein Classification

thiolase family protein( domain architecture ID 10091456)

thiolase family protein may 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; such as acetyl-CoA 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:0006635
PubMed:  16356722
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
thiolase cd00751
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ...
1-336 7.11e-173

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: 485.06  E-value: 7.11e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825   1 MGNVLQGGEGQAPTRQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGSTPY 80
Cdd:cd00751    49 MGNVLQAGEGQNPARQAALLAGLPESVPATTVNRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGG 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825  81 -GGVKLEDLIVKDGLTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTVKGQPdVV 159
Cdd:cd00751   129 rLGLNTLDGMLDDGLTDPFTGLSMGITAENVAEKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEVPGRKGP-VV 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825 160 VKEDEEYKR-VDFSKVPKLKTVFqKENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIA 238
Cdd:cd00751   208 VDRDEGPRPdTTLEKLAKLKPAF-KKDGTVTAGNASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIG 286
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825 239 PVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALKQ--GE 316
Cdd:cd00751   287 PVPAIPKALKRAGLTLDDIDLIEINEAFAAQALACLKELGLDPEKVNVNGGAIALGHPLGASGARIVVTLLHELKRrgGR 366
                         330       340
                  ....*....|....*....|
gi 1897357825 317 YGLASICNGGGGASAMLIQK 336
Cdd:cd00751   367 YGLATMCIGGGQGAAMVIER 386
 
Name Accession Description Interval E-value
thiolase cd00751
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ...
1-336 7.11e-173

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: 485.06  E-value: 7.11e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825   1 MGNVLQGGEGQAPTRQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGSTPY 80
Cdd:cd00751    49 MGNVLQAGEGQNPARQAALLAGLPESVPATTVNRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGG 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825  81 -GGVKLEDLIVKDGLTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTVKGQPdVV 159
Cdd:cd00751   129 rLGLNTLDGMLDDGLTDPFTGLSMGITAENVAEKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEVPGRKGP-VV 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825 160 VKEDEEYKR-VDFSKVPKLKTVFqKENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIA 238
Cdd:cd00751   208 VDRDEGPRPdTTLEKLAKLKPAF-KKDGTVTAGNASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIG 286
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825 239 PVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALKQ--GE 316
Cdd:cd00751   287 PVPAIPKALKRAGLTLDDIDLIEINEAFAAQALACLKELGLDPEKVNVNGGAIALGHPLGASGARIVVTLLHELKRrgGR 366
                         330       340
                  ....*....|....*....|
gi 1897357825 317 YGLASICNGGGGASAMLIQK 336
Cdd:cd00751   367 YGLATMCIGGGQGAAMVIER 386
PaaJ COG0183
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ...
1-337 4.21e-162

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: 457.99  E-value: 4.21e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825   1 MGNVLQGGEGQAPTRQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGSTPY 80
Cdd:COG0183    53 LGCVLQAGQGQNPARQAALLAGLPESVPAVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMLLPKARWGY 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825  81 GG-VKLEDLIVKDGLTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTVKGQpDVV 159
Cdd:COG0183   133 RMnAKLVDPMINPGLTDPYTGLSMGETAENVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVEVPDRKG-EVV 211
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825 160 VKEDEEYKR-VDFSKVPKLKTVFqKENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIA 238
Cdd:COG0183   212 VDRDEGPRPdTTLEKLAKLKPAF-KKDGTVTAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIG 290
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825 239 PVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALKQ--GE 316
Cdd:COG0183   291 PVPATRKALARAGLTLDDIDLIEINEAFAAQVLAVLRELGLDPDKVNVNGGAIALGHPLGASGARILVTLLHELERrgGR 370
                         330       340
                  ....*....|....*....|.
gi 1897357825 317 YGLASICNGGGGASAMLIQKL 337
Cdd:COG0183   371 YGLATMCIGGGQGIALIIERV 391
PLN02644 PLN02644
acetyl-CoA C-acetyltransferase
1-337 4.01e-156

acetyl-CoA C-acetyltransferase


Pssm-ID: 215347 [Multi-domain]  Cd Length: 394  Bit Score: 443.00  E-value: 4.01e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825   1 MGNVLQGGEGQAPTRQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVM--NRGST 78
Cdd:PLN02644   52 FGNVLSANLGQAPARQAALGAGLPPSTICTTVNKVCASGMKAVMLAAQSIQLGINDVVVAGGMESMSNAPKYLpeARKGS 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825  79 PYGGVKLEDLIVKDGLTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTV-KGQPD 157
Cdd:PLN02644  132 RLGHDTVVDGMLKDGLWDVYNDFGMGVCAELCADQYSISREEQDAYAIQSYERAIAAQEAGAFAWEIVPVEVPGgRGRPS 211
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825 158 VVVKEDEEYKRVDFSKVPKLKTVFQKENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPI 237
Cdd:PLN02644  212 VIVDKDEGLGKFDPAKLRKLRPSFKEDGGSVTAGNASSISDGAAALVLVSGEKALELGLQVIAKIRGYADAAQAPELFTT 291
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825 238 APVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALKQ--G 315
Cdd:PLN02644  292 APALAIPKALKHAGLEASQVDYYEINEAFSVVALANQKLLGLDPEKVNVHGGAVSLGHPIGCSGARILVTLLGVLRSknG 371
                         330       340
                  ....*....|....*....|..
gi 1897357825 316 EYGLASICNGGGGASAMLIQKL 337
Cdd:PLN02644  372 KYGVAGICNGGGGASAIVVELM 393
AcCoA-C-Actrans TIGR01930
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ...
1-335 2.05e-144

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: 412.78  E-value: 2.05e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825   1 MGNVLQGGEGQAPTRQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGSTP- 79
Cdd:TIGR01930  48 FGNVLQAGEQQNIARQAALLAGLPESVPAYTVNRQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGVPRSLRWg 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825  80 --YGGVKLEDLIVKDgLTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTVKGQPD 157
Cdd:TIGR01930 128 vkPGNAELEDARLKD-LTDANTGLPMGVTAENLAKKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVTVKGRKGPV 206
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825 158 VVVKEDEEYKRVDFSKVPKLKTVFqKENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPI 237
Cdd:TIGR01930 207 TVSSDEGIRPNTTLEKLAKLKPAF-DPDGTVTAGNSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGL 285
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825 238 APVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALKQ--G 315
Cdd:TIGR01930 286 GPVPAIPKALKKAGLSISDIDLFEINEAFAAQVLACIKELGLDLEKVNVNGGAIALGHPLGASGARIVTTLLHELKRrgG 365
                         330       340
                  ....*....|....*....|
gi 1897357825 316 EYGLASICNGGGGASAMLIQ 335
Cdd:TIGR01930 366 RYGLATMCIGGGQGAAVILE 385
Thiolase_N pfam00108
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
1-209 2.48e-91

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: 273.41  E-value: 2.48e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825   1 MGNVLQGGEGQAPTRQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMN---RGS 77
Cdd:pfam00108  50 VGNVLQAGEGQNPARQAALKAGIPDSAPAVTINKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALPtdaRSG 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825  78 TPYGGVKLEDLIVKDGLTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTVKGQPD 157
Cdd:pfam00108 130 LKHGDEKKHDLLIPDGLTDAFNGYHMGLTAENVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDEIVPVTVKGRKGKP 209
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1897357825 158 VVVKEDEEYKRVDFSKVPKLKTVFQKEnGTVTAANASTLNDGAAALVLMTAD 209
Cdd:pfam00108 210 TVDKDEGIRPPTTAEPLAKLKPAFDKE-GTVTAGNASPINDGAAAVLLMSES 260
 
Name Accession Description Interval E-value
thiolase cd00751
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ...
1-336 7.11e-173

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: 485.06  E-value: 7.11e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825   1 MGNVLQGGEGQAPTRQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGSTPY 80
Cdd:cd00751    49 MGNVLQAGEGQNPARQAALLAGLPESVPATTVNRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGG 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825  81 -GGVKLEDLIVKDGLTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTVKGQPdVV 159
Cdd:cd00751   129 rLGLNTLDGMLDDGLTDPFTGLSMGITAENVAEKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEVPGRKGP-VV 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825 160 VKEDEEYKR-VDFSKVPKLKTVFqKENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIA 238
Cdd:cd00751   208 VDRDEGPRPdTTLEKLAKLKPAF-KKDGTVTAGNASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIG 286
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825 239 PVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALKQ--GE 316
Cdd:cd00751   287 PVPAIPKALKRAGLTLDDIDLIEINEAFAAQALACLKELGLDPEKVNVNGGAIALGHPLGASGARIVVTLLHELKRrgGR 366
                         330       340
                  ....*....|....*....|
gi 1897357825 317 YGLASICNGGGGASAMLIQK 336
Cdd:cd00751   367 YGLATMCIGGGQGAAMVIER 386
PaaJ COG0183
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ...
1-337 4.21e-162

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: 457.99  E-value: 4.21e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825   1 MGNVLQGGEGQAPTRQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGSTPY 80
Cdd:COG0183    53 LGCVLQAGQGQNPARQAALLAGLPESVPAVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMLLPKARWGY 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825  81 GG-VKLEDLIVKDGLTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTVKGQpDVV 159
Cdd:COG0183   133 RMnAKLVDPMINPGLTDPYTGLSMGETAENVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVEVPDRKG-EVV 211
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825 160 VKEDEEYKR-VDFSKVPKLKTVFqKENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIA 238
Cdd:COG0183   212 VDRDEGPRPdTTLEKLAKLKPAF-KKDGTVTAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIG 290
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825 239 PVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALKQ--GE 316
Cdd:COG0183   291 PVPATRKALARAGLTLDDIDLIEINEAFAAQVLAVLRELGLDPDKVNVNGGAIALGHPLGASGARILVTLLHELERrgGR 370
                         330       340
                  ....*....|....*....|.
gi 1897357825 317 YGLASICNGGGGASAMLIQKL 337
Cdd:COG0183   371 YGLATMCIGGGQGIALIIERV 391
PLN02644 PLN02644
acetyl-CoA C-acetyltransferase
1-337 4.01e-156

acetyl-CoA C-acetyltransferase


Pssm-ID: 215347 [Multi-domain]  Cd Length: 394  Bit Score: 443.00  E-value: 4.01e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825   1 MGNVLQGGEGQAPTRQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVM--NRGST 78
Cdd:PLN02644   52 FGNVLSANLGQAPARQAALGAGLPPSTICTTVNKVCASGMKAVMLAAQSIQLGINDVVVAGGMESMSNAPKYLpeARKGS 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825  79 PYGGVKLEDLIVKDGLTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTV-KGQPD 157
Cdd:PLN02644  132 RLGHDTVVDGMLKDGLWDVYNDFGMGVCAELCADQYSISREEQDAYAIQSYERAIAAQEAGAFAWEIVPVEVPGgRGRPS 211
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825 158 VVVKEDEEYKRVDFSKVPKLKTVFQKENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPI 237
Cdd:PLN02644  212 VIVDKDEGLGKFDPAKLRKLRPSFKEDGGSVTAGNASSISDGAAALVLVSGEKALELGLQVIAKIRGYADAAQAPELFTT 291
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825 238 APVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALKQ--G 315
Cdd:PLN02644  292 APALAIPKALKHAGLEASQVDYYEINEAFSVVALANQKLLGLDPEKVNVHGGAVSLGHPIGCSGARILVTLLGVLRSknG 371
                         330       340
                  ....*....|....*....|..
gi 1897357825 316 EYGLASICNGGGGASAMLIQKL 337
Cdd:PLN02644  372 KYGVAGICNGGGGASAIVVELM 393
AcCoA-C-Actrans TIGR01930
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ...
1-335 2.05e-144

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: 412.78  E-value: 2.05e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825   1 MGNVLQGGEGQAPTRQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGSTP- 79
Cdd:TIGR01930  48 FGNVLQAGEQQNIARQAALLAGLPESVPAYTVNRQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGVPRSLRWg 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825  80 --YGGVKLEDLIVKDgLTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTVKGQPD 157
Cdd:TIGR01930 128 vkPGNAELEDARLKD-LTDANTGLPMGVTAENLAKKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVTVKGRKGPV 206
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825 158 VVVKEDEEYKRVDFSKVPKLKTVFqKENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPI 237
Cdd:TIGR01930 207 TVSSDEGIRPNTTLEKLAKLKPAF-DPDGTVTAGNSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGL 285
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825 238 APVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALKQ--G 315
Cdd:TIGR01930 286 GPVPAIPKALKKAGLSISDIDLFEINEAFAAQVLACIKELGLDLEKVNVNGGAIALGHPLGASGARIVTTLLHELKRrgG 365
                         330       340
                  ....*....|....*....|
gi 1897357825 316 EYGLASICNGGGGASAMLIQ 335
Cdd:TIGR01930 366 RYGLATMCIGGGQGAAVILE 385
PRK05790 PRK05790
putative acyltransferase; Provisional
1-334 4.41e-141

putative acyltransferase; Provisional


Pssm-ID: 180261 [Multi-domain]  Cd Length: 393  Bit Score: 404.53  E-value: 4.41e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825   1 MGNVLQGGEGQAPTRQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMN--RGST 78
Cdd:PRK05790   53 MGQVLQAGAGQNPARQAALKAGLPVEVPALTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQESMSQAPHVLPgsRWGQ 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825  79 PYGGVKLEDLIVKDGLTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTVKGQPDV 158
Cdd:PRK05790  133 KMGDVELVDTMIHDGLTDAFNGYHMGITAENLAEQYGITREEQDEFALASQQKAEAAIKAGRFKDEIVPVTIKQRKGDPV 212
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825 159 VVKEDeEYKRVDFS--KVPKLKTVFqKENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFP 236
Cdd:PRK05790  213 VVDTD-EHPRPDTTaeSLAKLRPAF-DKDGTVTAGNASGINDGAAAVVVMSEAKAKELGLTPLARIVSYAVAGVDPAIMG 290
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825 237 IAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALK--Q 314
Cdd:PRK05790  291 IGPVPAIRKALEKAGWSLADLDLIEINEAFAAQALAVEKELGLDPEKVNVNGGAIALGHPIGASGARILVTLLHEMKrrG 370
                         330       340
                  ....*....|....*....|
gi 1897357825 315 GEYGLASICNGGGGASAMLI 334
Cdd:PRK05790  371 AKKGLATLCIGGGQGVALIV 390
PRK08235 PRK08235
acetyl-CoA C-acetyltransferase;
1-335 9.67e-133

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181311 [Multi-domain]  Cd Length: 393  Bit Score: 383.68  E-value: 9.67e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825   1 MGNVLQGGEGQAPTRQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGSTPY 80
Cdd:PRK08235   53 MGTVLQGGQGQIPSRQAARAAGIPWEVQTETVNKVCASGLRAVTLADQIIRAGDASVIVAGGMESMSNAPYILPGARWGY 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825  81 --GGVKLEDLIVKDGLTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVT-VKGQPD 157
Cdd:PRK08235  133 rmGDNEVIDLMVADGLTCAFSGVHMGVYGGEVAKELGISREAQDEWAYRSHQRAVSAHEEGRFEEEIVPVTIPqRKGDPI 212
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825 158 VVVKEDEEYKRVDFSKVPKLKTVFQKEnGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPI 237
Cdd:PRK08235  213 VVAKDEAPRKDTTIEKLAKLKPVFDKT-GTITAGNAPGVNDGAAALVLMSEDRAKQEGRKPLATILAHTAIAVEAKDFPR 291
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825 238 APVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALKQ--G 315
Cdd:PRK08235  292 TPGYAINALLEKTGKTVEDIDLFEINEAFAAVALASTEIAGIDPEKVNVNGGAVALGHPIGASGARIIVTLIHELKRrgG 371
                         330       340
                  ....*....|....*....|
gi 1897357825 316 EYGLASICNGGGGASAMLIQ 335
Cdd:PRK08235  372 GIGIAAICSGGGQGDAVLIE 391
PRK06954 PRK06954
acetyl-CoA C-acetyltransferase;
1-335 5.39e-106

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180775 [Multi-domain]  Cd Length: 397  Bit Score: 315.68  E-value: 5.39e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825   1 MGNVLQGGEGQAPTRQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVM--NRGST 78
Cdd:PRK06954   58 MGCVLPAGQGQAPARQAALGAGLPLSVGCTTVNKMCGSGMRAAMFAHDMLVAGSVDVIVAGGMESMTNAPYLLpkARGGM 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825  79 PYGGVKLEDLIVKDGLTDVYNKIH-MGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTVKGQpD 157
Cdd:PRK06954  138 RMGHGQVLDHMFLDGLEDAYDKGRlMGTFAEECAGEYGFTREAQDAFAIESLARAKRANEDGSFAWEIAPVTVAGKKG-D 216
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825 158 VVVKEDEEYKRVDFSKVPKLKTVFQKeNGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPI 237
Cdd:PRK06954  217 TVIDRDEQPFKANPEKIPTLKPAFSK-TGTVTAANSSSISDGAAALVMMRASTAKRLGLAPLARVVGHSTFAQAPSKFTT 295
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825 238 APVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALKQ--G 315
Cdd:PRK06954  296 APVGAIRKLFEKNGWRAAEVDLFEINEAFAVVTMAAMKEHGLPHEKVNVNGGACALGHPIGASGARILVTLIGALRArgG 375
                         330       340
                  ....*....|....*....|
gi 1897357825 316 EYGLASICNGGGGASAMLIQ 335
Cdd:PRK06954  376 KRGVASLCIGGGEATAMGIE 395
PRK09051 PRK09051
beta-ketothiolase BktB;
15-337 2.70e-99

beta-ketothiolase BktB;


Pssm-ID: 181625 [Multi-domain]  Cd Length: 394  Bit Score: 298.41  E-value: 2.70e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825  15 RQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVM--NRGSTPYGGVKLEDLIVkD 92
Cdd:PRK09051   69 RVAAINAGVPQETPAFNVNRLCGSGLQAIVSAAQAILLGDADVAIGGGAESMSRAPYLLpaARWGARMGDAKLVDMMV-G 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825  93 GLTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTV-TVKGqpDVVVKEDEEYKR-VD 170
Cdd:PRK09051  148 ALHDPFGTIHMGVTAENVAAKYGISREAQDALALESHRRAAAAIAAGYFKDQIVPVEIkTRKG--EVVFDTDEHVRAdTT 225
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825 171 FSKVPKLKTVFQKENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDV 250
Cdd:PRK09051  226 LEDLAKLKPVFKKENGTVTAGNASGINDGAAAVVLAEADAAEARGLKPLARLVGYAHAGVDPEYMGIGPVPATQKALERA 305
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825 251 GLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALK--QGEYGLASICNGGGG 328
Cdd:PRK09051  306 GLTVADLDVIEANEAFAAQACAVTRELGLDPAKVNPNGSGISLGHPVGATGAIITVKALYELQriGGRYALVTMCIGGGQ 385

                  ....*....
gi 1897357825 329 ASAMLIQKL 337
Cdd:PRK09051  386 GIAAIFERL 394
PRK05656 PRK05656
acetyl-CoA C-acetyltransferase;
1-336 3.27e-94

acetyl-CoA C-acetyltransferase;


Pssm-ID: 168156  Cd Length: 393  Bit Score: 285.63  E-value: 3.27e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825   1 MGNVLQGGEGQAPTRQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVM--NRGST 78
Cdd:PRK05656   53 LGQVLTAGAGQNPARQAAIKAGLPHSVPAMTLNKVCGSGLKALHLAAQAIRCGDAEVIIAGGQENMSLAPYVLpgARTGL 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825  79 PYGGVKLEDLIVKDGLTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTV-TVKGQPD 157
Cdd:PRK05656  133 RMGHAQLVDSMITDGLWDAFNDYHMGITAENLVEKYGISREAQDAFAAASQQKAVAAIEAGRFDDEITPILIpQRKGEPL 212
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825 158 VVVKEDEEYKRVDFSKVPKLKTVFQKEnGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPI 237
Cdd:PRK05656  213 AFATDEQPRAGTTAESLAKLKPAFKKD-GSVTAGNASSLNDGAAAVLLMSAAKAKALGLPVLAKIAAYANAGVDPAIMGI 291
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825 238 APVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHAL--KQG 315
Cdd:PRK05656  292 GPVSATRRCLDKAGWSLAELDLIEANEAFAAQSLAVGKELGWDAAKVNVNGGAIALGHPIGASGCRVLVTLLHEMirRDA 371
                         330       340
                  ....*....|....*....|.
gi 1897357825 316 EYGLASICNGGGGASAMLIQK 336
Cdd:PRK05656  372 KKGLATLCIGGGQGVALAIER 392
PRK06633 PRK06633
acetyl-CoA C-acetyltransferase;
1-335 1.28e-92

acetyl-CoA C-acetyltransferase;


Pssm-ID: 168632 [Multi-domain]  Cd Length: 392  Bit Score: 281.53  E-value: 1.28e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825   1 MGNVLQGGEGQAPTRQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMS---NVPYVmnRGS 77
Cdd:PRK06633   54 LGQVITGGSGQNPARQTLIHAGIPKEVPGYTINKVCGSGLKSVALAANSIMTGDNEIVIAGGQENMSlgmHGSYI--RAG 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825  78 TPYGGVKLEDLIVKDGLTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTVKGQPD 157
Cdd:PRK06633  132 AKFGDIKMVDLMQYDGLTDVFSGVFMGITAENISKQFNISRQEQDEFALSSHKKAAKAQLAGIFKDEILPIEVTIKKTTS 211
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825 158 VVVKEDEEYKRVDFSKVPKLKTVFQKeNGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPI 237
Cdd:PRK06633  212 LFDHDETVRPDTSLEILSKLRPAFDK-NGVVTAGNASSINDGAACLMVVSEEALKKHNLTPLARIVSYASAGVDPSIMGT 290
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825 238 APVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALK--QG 315
Cdd:PRK06633  291 APVPASQKALSKAGWSVNDLEVIEVNEAFAAQSIYVNREMKWDMEKVNINGGAIAIGHPIGASGGRVLITLIHGLRraKA 370
                         330       340
                  ....*....|....*....|
gi 1897357825 316 EYGLASICNGGGGASAMLIQ 335
Cdd:PRK06633  371 KKGLVTLCIGGGMGMAMCVE 390
PRK09050 PRK09050
beta-ketoadipyl CoA thiolase; Validated
15-337 2.47e-91

beta-ketoadipyl CoA thiolase; Validated


Pssm-ID: 181624 [Multi-domain]  Cd Length: 401  Bit Score: 278.38  E-value: 2.47e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825  15 RQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGSTPYG-GVKLEDL----- 88
Cdd:PRK09050   69 RMSALLAGLPVSVPGTTINRLCGSGMDAVGTAARAIKAGEAELMIAGGVESMSRAPFVMGKADSAFSrQAEIFDTtigwr 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825  89 IVKDGLTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTVKGQPDVVVKEDEeYKR 168
Cdd:PRK09050  149 FVNPLMKAQYGVDSMPETAENVAEDYNISRADQDAFALRSQQRAAAAQAAGFLAEEIVPVTIPQKKGDPVVVDRDE-HPR 227
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825 169 VDFS--KVPKLKTVFqKENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMV 246
Cdd:PRK09050  228 PETTleALAKLKPVF-RPDGTVTAGNASGVNDGAAALLLASEAAAKKHGLTPRARILGMATAGVEPRIMGIGPAPATRKL 306
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825 247 LKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEI--DPQKVNINGGAVSLGHPIGMSGARIVGHLTHALKQ--GEYGLASI 322
Cdd:PRK09050  307 LARLGLTIDQFDVIELNEAFAAQGLAVLRQLGLadDDARVNPNGGAIALGHPLGMSGARLVLTALHQLERtgGRYALCTM 386
                         330
                  ....*....|....*
gi 1897357825 323 CNGGGGASAMLIQKL 337
Cdd:PRK09050  387 CIGVGQGIALAIERV 401
Thiolase_N pfam00108
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
1-209 2.48e-91

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: 273.41  E-value: 2.48e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825   1 MGNVLQGGEGQAPTRQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMN---RGS 77
Cdd:pfam00108  50 VGNVLQAGEGQNPARQAALKAGIPDSAPAVTINKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALPtdaRSG 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825  78 TPYGGVKLEDLIVKDGLTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTVKGQPD 157
Cdd:pfam00108 130 LKHGDEKKHDLLIPDGLTDAFNGYHMGLTAENVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDEIVPVTVKGRKGKP 209
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1897357825 158 VVVKEDEEYKRVDFSKVPKLKTVFQKEnGTVTAANASTLNDGAAALVLMTAD 209
Cdd:pfam00108 210 TVDKDEGIRPPTTAEPLAKLKPAFDKE-GTVTAGNASPINDGAAAVLLMSES 260
PRK06366 PRK06366
acetyl-CoA C-acetyltransferase;
1-335 1.73e-83

acetyl-CoA C-acetyltransferase;


Pssm-ID: 102340 [Multi-domain]  Cd Length: 388  Bit Score: 258.02  E-value: 1.73e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825   1 MGNVLQGGEGQAPTRQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNR----- 75
Cdd:PRK06366   53 MGNVIQAGVGQNPAGQAAYHAGLPFGVTKYTVNVVCASGMLAVESAAREIMLGERDLVIAGGMENMSNAPFLLPSdlrwg 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825  76 -GSTPYGGVKLEDLIVKDGLTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVtvkg 154
Cdd:PRK06366  133 pKHLLHKNYKIDDAMLVDGLIDAFYFEHMGVSAERTARKYGITREMADEYSVQSYERAIRATESGEFRNEIVPFND---- 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825 155 qpdvvVKEDEEYKRVDFSKVPKLKTVFQKeNGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPID 234
Cdd:PRK06366  209 -----LDRDEGIRKTTMEDLAKLPPAFDK-NGILTAGNSAQLSDGGSALVMASEKAINEYGLKPIARITGYESASLDPLD 282
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825 235 FPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALKQ 314
Cdd:PRK06366  283 FVEAPIPATRKLLEKQNKSIDYYDLVEHNEAFSIASIIVRDQLKIDNERFNVNGGAVAIGHPIGNSGSRIIVTLINALKT 362
                         330       340
                  ....*....|....*....|...
gi 1897357825 315 G--EYGLASICNGGGGASAMLIQ 335
Cdd:PRK06366  363 RhmKTGLATLCHGGGGAHTLTLE 385
PRK06205 PRK06205
acetyl-CoA C-acetyltransferase;
8-327 4.91e-83

acetyl-CoA C-acetyltransferase;


Pssm-ID: 235741 [Multi-domain]  Cd Length: 404  Bit Score: 257.22  E-value: 4.91e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825   8 GEGQAPTRQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMN--RGSTPYGGVKL 85
Cdd:PRK06205   60 GEAPAIGRVAALDAGLPVTVPGMQLDRRCGSGLQAVITAAMQVQTGAADVVIAGGAESMSNVEFYTTdmRWGVRGGGVQL 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825  86 EDLIVKDGLT---DVYNKIH-MGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTVKGQPDVVVK 161
Cdd:PRK06205  140 HDRLARGRETaggRRFPVPGgMIETAENLRREYGISREEQDALAVRSHQRAVAAQEAGRFDDEIVPVTVPQRKGDPTVVD 219
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825 162 EDEEYkRVDFS--KVPKLKTVFQK--ENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPI 237
Cdd:PRK06205  220 RDEHP-RADTTleSLAKLRPIMGKqdPEATVTAGNASGQNDAAAACLVTTEDKAEELGLRPLARLVSWAVAGVEPSRMGI 298
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825 238 APVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQ---KVNINGGAVSLGHPIGMSGARIVGHLTHALK- 313
Cdd:PRK06205  299 GPVPATEKALARAGLTLDDIDLIELNEAFAAQVLAVLKEWGFGADdeeRLNVNGSGISLGHPVGATGGRILATLLRELQr 378
                         330
                  ....*....|....*
gi 1897357825 314 -QGEYGLASICNGGG 327
Cdd:PRK06205  379 rQARYGLETMCIGGG 393
PRK06445 PRK06445
acetyl-CoA C-acetyltransferase;
15-336 3.92e-82

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180563 [Multi-domain]  Cd Length: 394  Bit Score: 254.65  E-value: 3.92e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825  15 RQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGSTPYGGVKLEDLIVKDGL 94
Cdd:PRK06445   74 RHPIFLARLPYNIPAMAVDRQCASSLTTVSIGAMEIATGMADIVIAGGVEHMTRTPMGDNPHIEPNPKLLTDPKYIEYDL 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825  95 TDVYNkihMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTVKGQPDVVVKEDEEYKRVDFSKV 174
Cdd:PRK06445  154 TTGYV---MGLTAEKLAEEAGIKREEMDRWSLRSHQLAAKAIQEGYFKDEILPIEVEVEGKKKVVDVDQSVRPDTSLEKL 230
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825 175 PKLKTVFqKENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKK 254
Cdd:PRK06445  231 AKLPPAF-KPDGVITAGNSSPLNSGASYVLLMSKKAVKKYGLKPMAKIRSFGFAGVPPAIMGKGPVPASKKALEKAGLSV 309
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825 255 EDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHAL--KQGEYGLASICNGGGGASAM 332
Cdd:PRK06445  310 KDIDLWEINEAFAVVVLYAIKELGLDPETVNIKGGAIAIGHPLGATGARIVGTLARQLqiKGKDYGVATLCVGGGQGGAV 389

                  ....
gi 1897357825 333 LIQK 336
Cdd:PRK06445  390 VLER 393
PRK09052 PRK09052
acetyl-CoA C-acyltransferase;
15-337 3.79e-79

acetyl-CoA C-acyltransferase;


Pssm-ID: 181626 [Multi-domain]  Cd Length: 399  Bit Score: 246.84  E-value: 3.79e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825  15 RQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGS-TPYGGVKLEDLIVKDG 93
Cdd:PRK09052   74 RIGALLAGLPNSVGGVTVNRFCASGLQAVAMAADRIRVGEADVMIAAGVESMSMVPMMGNKPSmSPAIFARDENVGIAYG 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825  94 ltdvynkihMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTVKgQPD-----VVVKEDE---- 164
Cdd:PRK09052  154 ---------MGLTAEKVAEQWKVSREDQDAFALESHQKAIAAQQAGEFKDEITPYEITER-FPDlatgeVDVKTRTvdld 223
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825 165 EYKRVDFS--KVPKLKTVFQKEnGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYA 242
Cdd:PRK09052  224 EGPRADTSleGLAKLKPVFANK-GSVTAGNSSQTSDGAGAVILVSEKALKQFNLTPLARFVSFAVAGVPPEIMGIGPIEA 302
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825 243 ASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHAL--KQGEYGLA 320
Cdd:PRK09052  303 IPAALKQAGLKQDDLDWIELNEAFAAQSLAVIRDLGLDPSKVNPLGGAIALGHPLGATGAIRTATVVHGLrrTNLKYGMV 382
                         330
                  ....*....|....*..
gi 1897357825 321 SICNGGGGASAMLIQKL 337
Cdd:PRK09052  383 TMCVGTGMGAAGIFERL 399
PRK07108 PRK07108
acetyl-CoA C-acyltransferase;
6-337 2.92e-77

acetyl-CoA C-acyltransferase;


Pssm-ID: 180843 [Multi-domain]  Cd Length: 392  Bit Score: 241.98  E-value: 2.92e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825   6 QGGEGQAPTRQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGstpyggvKL 85
Cdd:PRK07108   60 EGATGANIARQIALRAGLPVTVPGMTVNRFCSSGLQTIALAAQRVIAGEGDVFVAGGVESISCVQNEMNRH-------ML 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825  86 EDLIVKDGLTDVYnkIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTVKGQ---------P 156
Cdd:PRK07108  133 REGWLVEHKPEIY--WSMLQTAENVAKRYGISKERQDEYGVQSQQRAAAAQAAGRFDDEIVPITVTAGVAdkatgrlftK 210
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825 157 DVVVKEDEEYkRVDFSK--VPKLKTVFqkENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPID 234
Cdd:PRK07108  211 EVTVSADEGI-RPDTTLegVSKIRSAL--PGGVITAGNASQFSDGASACVVMNAKVAEREGLQPLGIFRGFAVAGCEPDE 287
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825 235 FPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGhltHALKQ 314
Cdd:PRK07108  288 MGIGPVFAVPKLLKQAGLKVDDIDLWELNEAFAVQVLYCRDTLGIPMDRLNVNGGAIAVGHPYGVSGARLTG---HALIE 364
                         330       340
                  ....*....|....*....|....*...
gi 1897357825 315 GE-----YGLASICNGGGGASAMLIQKL 337
Cdd:PRK07108  365 GKrrgakYVVVTMCIGGGQGAAGLFEVL 392
PRK08170 PRK08170
acetyl-CoA C-acetyltransferase;
1-337 5.38e-76

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181265 [Multi-domain]  Cd Length: 426  Bit Score: 239.53  E-value: 5.38e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825   1 MGNVLQGGEGQAPTRQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGSTPY 80
Cdd:PRK08170   54 LGCAMPSPDEANIARVVALRLGCGEKVPAWTVQRNCASGMQALDSAAANIALGRADLVLAGGVEAMSHAPLLFSEKMVRW 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825  81 ---------GGVKLEDL-------------IVKdGLTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEA 138
Cdd:PRK08170  134 lagwyaaksIGQKLAALgklrpsylapvigLLR-GLTDPVVGLNMGQTAEVLAHRFGITREQMDAYAARSHQRLAAAQAE 212
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825 139 GKFGnEVIPVtVTVKGQpdvvVKEDEEYKRVDFS--KVPKLKTVFQKENGTVTAANASTLNDGAAALVLMTADAAKRLNV 216
Cdd:PRK08170  213 GRLK-EVVPL-FDRDGK----FYDHDDGVRPDSSmeKLAKLKPFFDRPYGRVTAGNSSQITDGACWLLLASEEAVKKYGL 286
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825 217 TPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKML-----------------EI 279
Cdd:PRK08170  287 PPLGRIVDSQWAALDPSQMGLGPVHAATPLLQRHGLTLEDLDLWEINEAFAAQVLACLAAWadeeycreqlgldgalgEL 366
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825 280 DPQKVNINGGAVSLGHPIGMSGARIVGHLTHALKQ--GEYGLASICNGGGGASAMLIQKL 337
Cdd:PRK08170  367 DRERLNVDGGAIALGHPVGASGARIVLHLLHALKRrgTKRGIAAICIGGGQGGAMLLERV 426
PRK06504 PRK06504
acetyl-CoA C-acetyltransferase;
1-337 8.21e-75

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180595 [Multi-domain]  Cd Length: 390  Bit Score: 235.39  E-value: 8.21e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825   1 MGNVLQGGE-GQAPTRQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPyvMNRGSTp 79
Cdd:PRK06504   53 MGCVSQVGEqATNVARNAVLASKLPESVPGTSIDRQCGSSQQALHFAAQAVMSGTMDIVIAAGVESMTRVP--MGSPST- 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825  80 yggvkledLIVKDGLTDV--------YNKIH----MGscAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIP 147
Cdd:PRK06504  130 --------LPAKNGLGHYkspgmeerYPGIQfsqfTG--AEMMAKKYGLSKDQLDEFALQSHQRAIAATQAGKFKAEIVP 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825 148 VTVTVKGQPDVVVKEDEEYkRVDFS--KVPKLKTVfqKENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAF 225
Cdd:PRK06504  200 LEITRADGSGEMHTVDEGI-RFDATleGIAGVKLI--AEGGRLTAATASQICDGASGVMVVNERGLKALGVKPLARIHHM 276
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825 226 ADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIV 305
Cdd:PRK06504  277 TVIGGDPVIMLEAPLPATERALKKAGMKIDDIDLYEVNEAFASVPLAWLKATGADPERLNVNGGAIALGHPLGASGTKLM 356
                         330       340       350
                  ....*....|....*....|....*....|....
gi 1897357825 306 GHLTHALKQ--GEYGLASICNGGGGASAMLIQKL 337
Cdd:PRK06504  357 TTLVHALKQrgKRYGLQTMCEGGGMANVTIVERL 390
PRK08131 PRK08131
3-oxoadipyl-CoA thiolase;
1-336 1.43e-74

3-oxoadipyl-CoA thiolase;


Pssm-ID: 181242 [Multi-domain]  Cd Length: 401  Bit Score: 235.44  E-value: 1.43e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825   1 MGNVLQGGE-GQAPTRQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGSTP 79
Cdd:PRK08131   53 LGCTNQAGEdSRNVARNALLLAGLPVTVPGQTVNRLCASGLAAVIDAARAITCGEGDLYLAGGVESMSRAPFVMGKAESA 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825  80 YGgvklEDLIVKDG----------LTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVT 149
Cdd:PRK08131  133 FS----RDAKVFDTtigarfpnpkIVAQYGNDSMPETGDNVAAEFGISREDADRFAAQSQAKYQAAKEEGFFADEITPIE 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825 150 V-TVKGQPDVVVKEDEEYK-RVDFSKVPKLKTVFqkENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFAD 227
Cdd:PRK08131  209 VpQGRKLPPKLVAEDEHPRpSSTVEALTKLKPLF--EGGVVTAGNASGINDGAAALLIGSRAAGEKYGLKPMARILSSAA 286
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825 228 AAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEI--DPQKVNINGGAVSLGHPIGMSGARIV 305
Cdd:PRK08131  287 AGVEPRIMGIGPVEAIKKALARAGLTLDDMDIIEINEAFASQVLGCLKGLGVdfDDPRVNPNGGAIAVGHPLGASGARLA 366
                         330       340       350
                  ....*....|....*....|....*....|...
gi 1897357825 306 GHLTHALK--QGEYGLASICNGGGGASAMLIQK 336
Cdd:PRK08131  367 LTAARELQrrGKRYAVVSLCIGVGQGLAMVIER 399
PRK07661 PRK07661
acetyl-CoA C-acetyltransferase;
21-331 1.62e-73

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181072 [Multi-domain]  Cd Length: 391  Bit Score: 232.33  E-value: 1.62e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825  21 AGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVmnrgstpyGGVKLEDLIVKDGLTDVYnk 100
Cdd:PRK07661   75 AGLPYTVPAITINRYCSSGLQSIAYGAERIMLGHSEAVIAGGAESMSLVPMM--------GHVVRPNPRLVEAAPEYY-- 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825 101 IHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTV-------KGQPDVVVKEDEEYKRVDFSK 173
Cdd:PRK07661  145 MGMGHTAEQVAVKYGISREDQDAFAVRSHQRAAKALAEGKFADEIVPVDVTLrtvgennKLQEETITFSQDEGVRADTTL 224
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825 174 --VPKLKTVFQKeNGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVG 251
Cdd:PRK07661  225 eiLGKLRPAFNV-KGSVTAGNSSQMSDGAAAVLLMDREKAESDGLKPLAKFRSFAVAGVPPEVMGIGPIAAIPKALKLAG 303
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825 252 LKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALK-QGE-YGLASICNGGGGA 329
Cdd:PRK07661  304 LELSDIGLFELNEAFASQSIQVIRELGLDEEKVNVNGGAIALGHPLGCTGAKLTLSLIHEMKrRNEqFGIVTMCIGGGMG 383

                  ..
gi 1897357825 330 SA 331
Cdd:PRK07661  384 AA 385
PRK07851 PRK07851
acetyl-CoA C-acetyltransferase;
1-337 4.18e-73

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181146 [Multi-domain]  Cd Length: 406  Bit Score: 231.82  E-value: 4.18e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825   1 MGNVLQGGE-GQAPTRQAVLGAGLPiSTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNvpYVM-NRGST 78
Cdd:PRK07851   55 LGCGLPGGEqGFNMARVVAVLLGYD-FLPGTTVNRYCSSSLQTTRMAFHAIKAGEGDVFISAGVETVSR--FAKgNSDSL 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825  79 P-------------------YGGVKLEDLIVKDGLTDVYnkIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAG 139
Cdd:PRK07851  132 PdtknplfaeaqartaaraeGGAEAWHDPREDGLLPDVY--IAMGQTAENVAQLTGISREEQDEWGVRSQNRAEEAIANG 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825 140 KFGNEVIPVTVtvkgqPD--VVVKEDEEYKRVDFSKVPKLKTVFqKENGTVTAANASTLNDGAAALVLMTADAAKRLNVT 217
Cdd:PRK07851  210 FFEREITPVTL-----PDgtVVSTDDGPRAGTTYEKVSQLKPVF-RPDGTVTAGNACPLNDGAAAVVIMSDTKARELGLT 283
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825 218 PLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPI 297
Cdd:PRK07851  284 PLARIVSTGVSGLSPEIMGLGPVEASKQALARAGMSIDDIDLVEINEAFAAQVLPSARELGIDEDKLNVSGGAIALGHPF 363
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1897357825 298 GMSGARIVGHLTHALK--QGEYGLASICNGGGGASAMLIQKL 337
Cdd:PRK07851  364 GMTGARITTTLLNNLQthDKTFGLETMCVGGGQGMAMVLERL 405
PRK07801 PRK07801
acetyl-CoA C-acetyltransferase;
1-337 1.32e-72

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181123 [Multi-domain]  Cd Length: 382  Bit Score: 229.59  E-value: 1.32e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825   1 MGNVLQGGeGQAP--TRQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVP--YVMNRG 76
Cdd:PRK07801   53 FGCVDTIG-PQAGniARTSWLAAGLPEEVPGVTVDRQCGSSQQAIHFAAQAVMSGTQDLVVAGGVQNMSQIPisSAMTAG 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825  77 -----STPYGGVKledlivkdGLTDVYNK--IHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVT 149
Cdd:PRK07801  132 eqlgfTSPFAESK--------GWLHRYGDqeVSQFRGAELIAEKWGISREEMERFALESHRRAFAAIRAGRFDNEIVPVG 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825 150 vtvkgqpDVVVkeDEEYKRVDFSKVPKLKTVFqkENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAA 229
Cdd:PRK07801  204 -------GVTV--DEGPRETSLEKMAGLKPLV--EGGRLTAAVASQISDGASAVLLASERAVKRHGLTPRARIHHLSVRG 272
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825 230 VEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLT 309
Cdd:PRK07801  273 DDPVFMLTAPIPATRYALEKTGLSIDDIDVVEINEAFAPVVLAWLKETGADPAKVNPNGGAIALGHPLGATGAKLMTTLL 352
                         330       340       350
                  ....*....|....*....|....*....|
gi 1897357825 310 HALKQ--GEYGLASICNGGGGASAMLIQKL 337
Cdd:PRK07801  353 HELERtgGRYGLQTMCEGGGTANVTIIERL 382
fadA PRK08947
3-ketoacyl-CoA thiolase; Reviewed
15-337 1.80e-72

3-ketoacyl-CoA thiolase; Reviewed


Pssm-ID: 181592 [Multi-domain]  Cd Length: 387  Bit Score: 229.47  E-value: 1.80e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825  15 RQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPyvMNRGSTPYggvkledlivkDGL 94
Cdd:PRK08947   70 RNAALLAGIPHSVPAVTVNRLCGSSMQALHDAARAIMTGDGDVFLIGGVEHMGHVP--MNHGVDFH-----------PGL 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825  95 TDVYNKIH--MGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTvtvkGQpdvvvKEDEEYKRVDFS 172
Cdd:PRK08947  137 SKNVAKAAgmMGLTAEMLGKMHGISREQQDAFAARSHQRAWAATQEGRFKNEIIPTE----GH-----DADGVLKLFDYD 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825 173 KV----------PKLKTVFQKENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYA 242
Cdd:PRK08947  208 EVirpettvealAALRPAFDPVNGTVTAGTSSALSDGASAMLVMSESRAKELGLKPRARIRSMAVAGCDPSIMGYGPVPA 287
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825 243 ASMVLKDVGLKKEDIAMWEVNEAF---SLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALKQ--GEY 317
Cdd:PRK08947  288 TQKALKRAGLSISDIDVFELNEAFaaqSLPCLKDLGLLDKMDEKVNLNGGAIALGHPLGCSGARISTTLLNLMERkdAQF 367
                         330       340
                  ....*....|....*....|
gi 1897357825 318 GLASICNGGGGASAMLIQKL 337
Cdd:PRK08947  368 GLATMCIGLGQGIATVFERV 387
fadI PRK08963
3-ketoacyl-CoA thiolase; Reviewed
2-335 2.74e-70

3-ketoacyl-CoA thiolase; Reviewed


Pssm-ID: 181597 [Multi-domain]  Cd Length: 428  Bit Score: 224.86  E-value: 2.74e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825   2 GNVLQGGEGQAPTRQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVP----------- 70
Cdd:PRK08963   57 GQVVQMPEAPNIAREIVLGTGMNVHTDAYSVSRACATSFQAVANVAESIMAGTIDIGIAGGADSSSVLPigvskklaral 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825  71 YVMNRGST------PYGGVKLEDLI-VKDGLTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGN 143
Cdd:PRK08963  137 VDLNKARTlgqrlkLFSRLRLRDLLpVPPAVAEYSTGLRMGDTAEQMAKTYGISREEQDALAHRSHQLAAQAWAEGKLDD 216
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825 144 EVIPVTVTVKGQP---DVVVKEDEeykrvDFSKVPKLKTVFQKENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLA 220
Cdd:PRK08963  217 EVMTAHVPPYKQPleeDNNIRGDS-----TLEDYAKLRPAFDRKHGTVTAANSTPLTDGAAAVLLMSESRAKALGLTPLG 291
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825 221 RIVAFADAAVEPI-DFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKML-----------------EIDPQ 282
Cdd:PRK08963  292 YLRSYAFAAIDVWqDMLLGPAYATPLALERAGLTLADLTLIDMHEAFAAQTLANLQMFaserfareklgrsqaigEVDMS 371
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1897357825 283 KVNINGGAVSLGHPIGMSGARIVGHLTHALKQ--GEYGLASICNGGGGASAMLIQ 335
Cdd:PRK08963  372 KFNVLGGSIAYGHPFAATGARMITQTLHELRRrgGGLGLTTACAAGGLGAAMVLE 426
PRK08242 PRK08242
acetyl-CoA C-acetyltransferase;
1-337 1.58e-69

acetyl-CoA C-acetyltransferase;


Pssm-ID: 236197 [Multi-domain]  Cd Length: 402  Bit Score: 222.07  E-value: 1.58e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825   1 MGNVLQGGE-GQAPTRQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGSTP 79
Cdd:PRK08242   55 LGCVTPVGDqGADIARTAVLAAGLPETVPGVQINRFCASGLEAVNLAAAKVRSGWDDLVIAGGVESMSRVPMGSDGGAWA 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825  80 yggvkledliVKDGLTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVtvtvKGQPDVV 159
Cdd:PRK08242  135 ----------MDPSTNFPTYFVPQGISADLIATKYGFSREDVDAYAVESQQRAAAAWAEGYFAKSVVPV----KDQNGLT 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825 160 VKEDEEYKR--VDFSKVPKLKTVFQ--------------------KENGTVTAANASTLNDGAAALVLMTADAAKRLNVT 217
Cdd:PRK08242  201 ILDHDEHMRpgTTMESLAKLKPSFAmmgemggfdavalqkypeveRINHVHHAGNSSGIVDGAAAVLIGSEEAGKALGLK 280
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825 218 PLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPI 297
Cdd:PRK08242  281 PRARIVATATIGSDPTIMLTGPVPATRKALAKAGLTVDDIDLFELNEAFASVVLRFMQALDIPHDKVNVNGGAIAMGHPL 360
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1897357825 298 GMSGARIVGHLTHAL--KQGEYGLASICNGGGGASAMLIQKL 337
Cdd:PRK08242  361 GATGAMILGTVLDELerRGKRTALITLCVGGGMGIATIIERV 402
PLN02287 PLN02287
3-ketoacyl-CoA thiolase
2-333 9.64e-69

3-ketoacyl-CoA thiolase


Pssm-ID: 215161 [Multi-domain]  Cd Length: 452  Bit Score: 221.56  E-value: 9.64e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825   2 GNVLQGGEGQA-PTRQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGSTPy 80
Cdd:PLN02287   99 GTVLAPGSQRAnECRMAAFYAGFPETVPVRTVNRQCSSGLQAVADVAAAIKAGFYDIGIGAGVESMTTNPMAWEGGVNP- 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825  81 ggvKLEDL-IVKDGLtdvynkIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTV------TVK 153
Cdd:PLN02287  178 ---RVESFsQAQDCL------LPMGITSENVAERFGVTREEQDQAAVESHRKAAAATASGKFKDEIVPVHTkivdpkTGE 248
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825 154 GQPDVVVKEDEEYKRVDFSKVPKLKTVFqKENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPI 233
Cdd:PLN02287  249 EKPIVISVDDGIRPNTTLADLAKLKPVF-KKNGTTTAGNSSQVSDGAGAVLLMKRSVAMQKGLPILGVFRSFAAVGVDPA 327
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825 234 DFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALK 313
Cdd:PLN02287  328 VMGIGPAVAIPAAVKAAGLELDDIDLFEINEAFASQFVYCCKKLGLDPEKVNVNGGAIALGHPLGATGARCVATLLHEMK 407
                         330       340
                  ....*....|....*....|....*
gi 1897357825 314 Q----GEYGLASICNGGG-GASAML 333
Cdd:PLN02287  408 RrgkdCRFGVVSMCIGTGmGAAAVF 432
PRK07850 PRK07850
steroid 3-ketoacyl-CoA thiolase;
2-337 9.20e-68

steroid 3-ketoacyl-CoA thiolase;


Pssm-ID: 181145 [Multi-domain]  Cd Length: 387  Bit Score: 217.28  E-value: 9.20e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825   2 GNVLQGGE-GQAPTRQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGSTPy 80
Cdd:PRK07850   54 GCVTQAGEqSNNITRTAWLHAGLPYHVGATTIDCQCGSAQQANHLVAGLIAAGAIDVGIACGVEAMSRVPLGANAGPGR- 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825  81 GGVKLEDLIVkdgltDVYNKIhmgSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTV---KGQP- 156
Cdd:PRK07850  133 GLPRPDSWDI-----DMPNQF---EAAERIAKRRGITREDVDAFGLRSQRRAAQAWAEGRFDREISPVQAPVldeEGQPt 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825 157 --DVVVKEDEEYKRVDFSKVPKLKTVFqkENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPID 234
Cdd:PRK07850  205 geTRLVTRDQGLRDTTMEGLAGLKPVL--EGGIHTAGTSSQISDGAAAVLWMDEDRARALGLRPRARIVAQALVGAEPYY 282
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825 235 FPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALKQ 314
Cdd:PRK07850  283 HLDGPVQATAKVLEKAGMKIGDIDLVEINEAFASVVLSWAQVHEPDMDKVNVNGGAIALGHPVGSTGARLITTALHELER 362
                         330       340
                  ....*....|....*....|....*
gi 1897357825 315 --GEYGLASICNGGGGASAMLIQKL 337
Cdd:PRK07850  363 tdKSTALITMCAGGALSTGTIIERI 387
PRK06690 PRK06690
acetyl-CoA C-acyltransferase;
1-337 1.56e-63

acetyl-CoA C-acyltransferase;


Pssm-ID: 180659 [Multi-domain]  Cd Length: 361  Bit Score: 205.77  E-value: 1.56e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825   1 MGNVLQGGEGQAptRQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGSTPy 80
Cdd:PRK06690   49 LGNVVGPGGNVA--RLSALEAGLGLHIPGVTIDRQCGAGLEAIRTACHFIQGGAGKCYIAGGVESTSTSPFQNRARFSP- 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825  81 ggvkledlivkdgltDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTvtvkGQPDVVV 160
Cdd:PRK06690  126 ---------------ETIGDPDMGVAAEYVAERYNITREMQDEYACLSYKRTLQALEKGYIHEEILSFN----GLLDESI 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825 161 KEDEEYKRVdfskVPKLKTVFQKeNGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPV 240
Cdd:PRK06690  187 KKEMNYERI----IKRTKPAFLH-NGTVTAGNSCGVNDGACAVLVMEEGQARKLGYKPVLRFVRSAVVGVDPNLPGTGPI 261
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825 241 YAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALKQ--GEYG 318
Cdd:PRK06690  262 FAVNKLLNEMNMKVEDIDYFEINEAFASKVVACAKELQIPYEKLNVNGGAIALGHPYGASGAMLVTRLFYQAKRedMKYG 341
                         330
                  ....*....|....*....
gi 1897357825 319 LASICNGGGGASAMLIQKL 337
Cdd:PRK06690  342 IATLGIGGGIGLALLFEKV 360
Thiolase_C pfam02803
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
216-336 3.50e-59

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: 186.31  E-value: 3.50e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825 216 VTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGH 295
Cdd:pfam02803   1 LKPLARIRSYATAGVDPAIMGIGPAYAIPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGIDPEKVNVNGGAIALGH 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1897357825 296 PIGMSGARIVGHLTHALKQ--GEYGLASICNGGGGASAMLIQK 336
Cdd:pfam02803  81 PLGASGARILVTLLHELKRrgGKYGLASLCIGGGQGVAMIIER 123
PRK06025 PRK06025
acetyl-CoA C-acetyltransferase;
7-337 2.77e-55

acetyl-CoA C-acetyltransferase;


Pssm-ID: 235675 [Multi-domain]  Cd Length: 417  Bit Score: 185.75  E-value: 2.77e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825   7 GGEGQAPTRQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMS----NVPYVMNRGSTPYGg 82
Cdd:PRK06025   63 GKQGGDLGRMAALDAGYDIKASGVTLDRFCGGGITSVNLAAAQIMSGMEDLVIAGGTEMMSytaaMAAEDMAAGKPPLG- 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825  83 vkledliVKDG---LTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTvtvkgQPDVV 159
Cdd:PRK06025  142 -------MGSGnlrLRALHPQSHQGVCGDAIATMEGITREALDALGLESQRRAARAIKEGRFDKSLVPVY-----RDDGS 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825 160 VKED-EEYKRVDFSK--VPKLKTVFQK-------ENGTV------------------TAANASTLNDGAAALVLMTADAA 211
Cdd:PRK06025  210 VALDhEEFPRPQTTAegLAALKPAFTAiadypldDKGTTyrglinqkypdleikhvhHAGNSSGVVDGAAALLLASKAYA 289
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825 212 KRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAV 291
Cdd:PRK06025  290 EKHGLKPRARIVAMANMGDDPTLMLNAPVPAAKKVLAKAGLTKDDIDLWEINEAFAVVAEKFIRDLDLDRDKVNVNGGAI 369
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1897357825 292 SLGHPIGMSGARIVGHLTHALKQ--GEYGLASICNGGGGASAMLIQKL 337
Cdd:PRK06025  370 ALGHPIGATGSILIGTVLDELERrgLKRGLVTMCAAGGMAPAIIIERV 417
PRK09268 PRK09268
acetyl-CoA C-acetyltransferase;
14-336 6.18e-48

acetyl-CoA C-acetyltransferase;


Pssm-ID: 236440 [Multi-domain]  Cd Length: 427  Bit Score: 166.61  E-value: 6.18e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825  14 TRQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYV-----------MNRGSTPYGG 82
Cdd:PRK09268   71 TRECVLGSALSPYTPAYDLQQACGTGLEAAILVANKIALGQIDSGIAGGVDTTSDAPIAvneglrkilleLNRAKTTGDR 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825  83 VKL------EDLIV--------KDGLTdvynkihMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPV 148
Cdd:PRK09268  151 LKAlgklrpKHLAPeiprngepRTGLS-------MGEHAAITAKEWGISREAQDELAAASHQNLAAAYDRGFFDDLITPF 223
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825 149 TVTVKGQ---PDVVVKedeeykrvdfsKVPKLKTVFQK-ENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVA 224
Cdd:PRK09268  224 LGLTRDNnlrPDSSLE-----------KLAKLKPVFGKgGRATMTAGNSTPLTDGASVVLLASEEWAAEHGLPVLAYLVD 292
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825 225 FADAAVEPIDFP----IAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLE-----------------IDPQK 283
Cdd:PRK09268  293 AETAAVDFVHGKegllMAPAYAVPRLLARNGLTLQDFDFYEIHEAFASQVLATLKAWEdeeycrerlgldaplgsIDRSK 372
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1897357825 284 VNINGGAVSLGHPIGMSGARIVGHLTHAL--KQGEYGLASICNGGGGASAMLIQK 336
Cdd:PRK09268  373 LNVNGSSLAAGHPFAATGGRIVATLAKLLaeKGSGRGLISICAAGGQGVTAILER 427
nondecarbox_cond_enzymes cd00826
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ...
1-335 8.63e-44

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


Pssm-ID: 238422 [Multi-domain]  Cd Length: 393  Bit Score: 154.96  E-value: 8.63e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825   1 MGNVLQGGEGQAPTRQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPyvmnrgstpy 80
Cdd:cd00826    50 LGQVLGAGEGQNCAQQAAMHAGGLQEAPAIGMNNLCGSGLRALALAMQLIAGGDANCILAGGFEKMETSA---------- 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825  81 ggvklEDLIVKDGLTDVYNKIHMgscaentakklniaRNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVtvKGQPDVVV 160
Cdd:cd00826   120 -----ENNAKEKHIDVLINKYGM--------------RACPDAFALAGQAGAEAAEKDGRFKDEFAKFGV--KGRKGDIH 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825 161 KEDEEYKR----VDFSKVPKLKTVFQKEnGTVTAANASTLNDGAAALVLMTADAA-------KRLNVTPLARIVAFADAA 229
Cdd:cd00826   179 SDADEYIQfgdeASLDEIAKLRPAFDKE-DFLTAGNACGLNDGAAAAILMSEAEAqkhglqsKAREIQALEMITDMASTF 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825 230 VEPIDFPIA----PVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQK------------------VNIN 287
Cdd:cd00826   258 EDKKVIKMVggdgPIEAARKALEKAGLGIGDLDLIEAHDAFAANACATNEALGLCPEGqggalvdrgdntyggksiINPN 337
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1897357825 288 GGAVSLGHPIGMSGARIVGHLTHALKQGEY-------GLASICNGGGGASAMLIQ 335
Cdd:cd00826   338 GGAIAIGHPIGASGAAICAELCFELKGEAGkrqgagaGLALLCIGGGGGAAMCIE 392
cond_enzymes cd00327
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ...
190-334 3.77e-13

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: 68.24  E-value: 3.77e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825 190 AANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPI----APVYAASMVLKDVGLKKEDIAMWEVNEA 265
Cdd:cd00327    94 GSEEFVFGDGAAAAVVESEEHALRRGAHPQAEIVSTAATFDGASMVPAvsgeGLARAARKALEGAGLTPSDIDYVEAHGT 173
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825 266 FSLVVLANIKMLEIDPQKV---NINGGAVSLGHPIGMSGARIVGHLTHALKQGEY---------GLASICNGGGGASAML 333
Cdd:cd00327   174 GTPIGDAVELALGLDPDGVrspAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIpptpreprtVLLLGFGLGGTNAAVV 253

                  .
gi 1897357825 334 I 334
Cdd:cd00327   254 L 254
SCP-x_thiolase cd00829
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ...
2-331 1.02e-11

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: 65.36  E-value: 1.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825   2 GNVLQGGEGQAPTRQAVLGAGLPIsTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGSTPyG 81
Cdd:cd00829    44 GNAAGGRFQSFPGALIAEYLGLLG-KPATRVEAAGASGSAAVRAAAAAIASGLADVVLVVGAEKMSDVPTGDEAGGRA-S 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825  82 GVKLEDLIVKDGLT--DVYNKI---HM---GSCAENTAKklnIARNEQDAYAINSYtrskaAWEAGkfgneviPVTV-TV 152
Cdd:cd00829   122 DLEWEGPEPPGGLTppALYALAarrYMhryGTTREDLAK---VAVKNHRNAARNPY-----AQFRK-------PITVeDV 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825 153 KGQPDVVvkedEEYKRVDFSKVpklktvfqkengtvtaanastlNDGAAALVLMTADAAKRLNVTPlARIVAFADA---- 228
Cdd:cd00829   187 LNSRMIA----DPLRLLDCCPV----------------------SDGAAAVVLASEERARELTDRP-VWILGVGAAsdtp 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825 229 ---AVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKML---------------EIDPQ---KVNIN 287
Cdd:cd00829   240 slsERDDFLSLDAARLAARRAYKMAGITPDDIDVAELYDCFTIAELLALEDLgfcekgeggklvregDTAIGgdlPVNTS 319
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1897357825 288 GGAVSLGHPIGMSGARIVGHLTHALKqGEYG--------LASICNGGGGASA 331
Cdd:cd00829   320 GGLLSKGHPLGATGLAQAVEAVRQLR-GEAGarqvpgarVGLAHNIGGTGSA 370
PRK06064 PRK06064
thiolase domain-containing protein;
21-331 1.86e-07

thiolase domain-containing protein;


Pssm-ID: 235688 [Multi-domain]  Cd Length: 389  Bit Score: 52.21  E-value: 1.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825  21 AGLPiSTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVP---------------YVMNRGSTPyggvkl 85
Cdd:PRK06064   71 AGLA-PIPATRVEAACASGGAALRQAYLAVASGEADVVLAAGVEKMTDVPtpdateaiaragdyeWEEFFGATF------ 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825  86 edlivkDGLTDVYNKIHM---GSCAENTAKklnIARNEQDAYAINSYtrskaaweaGKFGNEvipVTVtvkgqpDVVVKE 162
Cdd:PRK06064  144 ------PGLYALIARRYMhkyGTTEEDLAL---VAVKNHYNGSKNPY---------AQFQKE---ITV------EQVLNS 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825 163 deeykrvdfSKVPKLKTVFqkengtvtaaNASTLNDGAAALVLMTADAAKRLNVTPLaRIVAFADAavepIDFPI----- 237
Cdd:PRK06064  197 ---------PPVADPLKLL----------DCSPITDGAAAVILASEEKAKEYTDTPV-WIKASGQA----SDTIAlhdrk 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825 238 ------APVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKML-----------------EIDPQ-KVNINGGAVSL 293
Cdd:PRK06064  253 dfttldAAVVAAEKAYKMAGIEPKDIDVAEVHDCFTIAEILAYEDLgfakkgeggklaregqtYIGGDiPVNPSGGLKAK 332
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1897357825 294 GHPIGMSGARIVGHLTHALKQG-----------EYGLASicN-GGGGASA 331
Cdd:PRK06064  333 GHPVGATGVSQAVEIVWQLRGEaekgrqqvigaGYGLTH--NvGGTGHTA 380
PRK06157 PRK06157
acetyl-CoA acetyltransferase; Validated
194-305 2.78e-07

acetyl-CoA acetyltransferase; Validated


Pssm-ID: 180433 [Multi-domain]  Cd Length: 398  Bit Score: 51.57  E-value: 2.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825 194 STLNDGAAALVLMTADAAKRLNVTPLARIVAFAdAAVEP--------IDFPIAP--VYAASMVLKDVGLK--KEDIAMWE 261
Cdd:PRK06157  214 CGVSDGAAAAIVTTPEIARALGKKDPVYVKALQ-LAVSNgwelqyngWDGSYFPttRIAARKAYREAGITdpREELSMAE 292
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1897357825 262 VNEAFSLVVLANIKMLEIDPQ------------------KVNINGGAVSLGHPIGMSGARIV 305
Cdd:PRK06157  293 VHDCFSITELVTMEDLGLSERgqawrdvldgffdadgglPCQIDGGLKCFGHPIGASGLRML 354
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
17-68 3.51e-06

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: 48.30  E-value: 3.51e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1897357825  17 AVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSN 68
Cdd:cd00834   142 GQVAIRLGLRGPNYTVSTACASGAHAIGDAARLIRLGRADVVIAGGAEALIT 193
FabB COG0304
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...
28-73 2.56e-05

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: 45.47  E-value: 2.56e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1897357825  28 PCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNvPYVM 73
Cdd:COG0304   153 PNYTVSTACASGAHAIGEAYRLIRRGRADVMIAGGAEAAIT-PLGL 197
PRK07314 PRK07314
beta-ketoacyl-ACP synthase II;
28-65 5.46e-05

beta-ketoacyl-ACP synthase II;


Pssm-ID: 235987 [Multi-domain]  Cd Length: 411  Bit Score: 44.39  E-value: 5.46e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1897357825  28 PCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMES 65
Cdd:PRK07314  154 PNHSIVTACATGAHAIGDAARLIAYGDADVMVAGGAEA 191
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
28-66 3.16e-04

Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains. The N-terminal domain contains most of the structures involved in dimer formation and also the active site cysteine.


Pssm-ID: 425468 [Multi-domain]  Cd Length: 251  Bit Score: 41.47  E-value: 3.16e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1897357825  28 PCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESM 66
Cdd:pfam00109 165 PSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLL 203
PTZ00455 PTZ00455
3-ketoacyl-CoA thiolase; Provisional
194-322 8.14e-04

3-ketoacyl-CoA thiolase; Provisional


Pssm-ID: 240424 [Multi-domain]  Cd Length: 438  Bit Score: 41.03  E-value: 8.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897357825 194 STLNDGAAALVLMTADAAKRLNVTP----LARIVAFADAAVEPIDFP------IAPVYAASMVLKDVGLKKEDIAMWEVN 263
Cdd:PTZ00455  256 SQVSDGGAGLVLASEEGLQKMGLSPndsrLVEIKSLACASGNLYEDPpdatrmFTSRAAAQKALSMAGVKPSDLQVAEVH 335
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1897357825 264 EAFSLVVLANIKMLEI-DPQK-----------------VNINGGAVSLGHPIGMSGARIVGHLTHALKQ--GEYGLASI 322
Cdd:PTZ00455  336 DCFTIAELLMYEALGIaEYGHakdlirngatalegripVNTGGGLLSFGHPVGATGVKQIMEVYRQMKGqcGEYQMKNI 414
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
196-257 2.85e-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: 39.06  E-value: 2.85e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1897357825 196 LNDGAAALVLMTADAAKRLNVTPLARIVAFA---DAA--VEPIDFPIAPVYAASMVLKDVGLKKEDI 257
Cdd:cd00834   229 LGEGAGVLVLESLEHAKARGAKIYAEILGYGassDAYhiTAPDPDGEGAARAMRAALADAGLSPEDI 295
elong_cond_enzymes cd00828
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ...
1-67 3.64e-03

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


Pssm-ID: 238424 [Multi-domain]  Cd Length: 407  Bit Score: 38.96  E-value: 3.64e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1897357825   1 MGNVLQGGEGQAPTRQAVLGAGLPIST-PCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMS 67
Cdd:cd00828   126 NPYVSPKWMLSPNTVAGWVNILLLSSHgPIKTPVGACATALEALDLAVEAIRSGKADIVVVGGVEDPL 193
FabB COG0304
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...
199-257 7.66e-03

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: 37.77  E-value: 7.66e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1897357825 199 GAAALVLMTADAAKRLNVTPLARIVAFA---DAA--VEPIDFPIAPVYAASMVLKDVGLKKEDI 257
Cdd:COG0304   232 GAGVLVLEELEHAKARGAKIYAEVVGYGassDAYhiTAPAPDGEGAARAMRAALKDAGLSPEDI 295
 
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