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Conserved domains on  [gi|1897358309|ref|NP_001373607|]
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acetyl-CoA acetyltransferase, mitochondrial isoform c [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

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List of domain hits

 Name Accession Description Interval E-value
thiolase cd00751
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ...
 41-321 1.05e-138

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: 397.62  E-value: 1.05e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309  41 DVMVAGGMESMSNVPYVMNRGSTPY-GGVKLEDLIVKDGLTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKA 119
Cdd:cd00751   104 DVVVAGGVESMSRAPYLLPKARRGGrLGLNTLDGMLDDGLTDPFTGLSMGITAENVAEKYGISREEQDEFALRSHQRAAA 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309 120 AWEAGKFGNEVIPVTVTVKGQPdVVVKEDEEYKR-VDFSKVPKLKTVFqKENGTVTAANASTLNDGAAALVLMTADAAKR 198
Cdd:cd00751   184 AQEAGRFKDEIVPVEVPGRKGP-VVVDRDEGPRPdTTLEKLAKLKPAF-KKDGTVTAGNASGINDGAAAVLLMSEEKAKE 261

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309 199 LNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSL 278
Cdd:cd00751   262 LGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDIDLIEINEAFAAQALACLKELGLDPEKVNVNGGAIAL 341

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1897358309 279 GHPIGMSGARIVGHLTHALKQ--GEYGLASICNGGGGASAMLIQK 321
Cdd:cd00751   342 GHPLGASGARIVVTLLHELKRrgGRYGLATMCIGGGQGAAMVIER 386
 
Name Accession Description Interval E-value
thiolase cd00751
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ...
 41-321 1.05e-138

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: 397.62  E-value: 1.05e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309  41 DVMVAGGMESMSNVPYVMNRGSTPY-GGVKLEDLIVKDGLTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKA 119
Cdd:cd00751   104 DVVVAGGVESMSRAPYLLPKARRGGrLGLNTLDGMLDDGLTDPFTGLSMGITAENVAEKYGISREEQDEFALRSHQRAAA 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309 120 AWEAGKFGNEVIPVTVTVKGQPdVVVKEDEEYKR-VDFSKVPKLKTVFqKENGTVTAANASTLNDGAAALVLMTADAAKR 198
Cdd:cd00751   184 AQEAGRFKDEIVPVEVPGRKGP-VVVDRDEGPRPdTTLEKLAKLKPAF-KKDGTVTAGNASGINDGAAAVLLMSEEKAKE 261

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309 199 LNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSL 278
Cdd:cd00751   262 LGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDIDLIEINEAFAAQALACLKELGLDPEKVNVNGGAIAL 341

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1897358309 279 GHPIGMSGARIVGHLTHALKQ--GEYGLASICNGGGGASAMLIQK 321
Cdd:cd00751   342 GHPLGASGARIVVTLLHELKRrgGRYGLATMCIGGGQGAAMVIER 386
PaaJ COG0183
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ...
 41-322 1.13e-128

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: 372.48  E-value: 1.13e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309  41 DVMVAGGMESMSNVPYVMNRGSTPYGG-VKLEDLIVKDGLTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKA 119
Cdd:COG0183   108 DVVIAGGVESMSRAPMLLPKARWGYRMnAKLVDPMINPGLTDPYTGLSMGETAENVAERYGISREEQDAFALRSHQRAAA 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309 120 AWEAGKFGNEVIPVTVTVKGQpDVVVKEDEEYKR-VDFSKVPKLKTVFqKENGTVTAANASTLNDGAAALVLMTADAAKR 198
Cdd:COG0183   188 AIAAGRFDDEIVPVEVPDRKG-EVVVDRDEGPRPdTTLEKLAKLKPAF-KKDGTVTAGNASGINDGAAALLLMSEEAAKE 265

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309 199 LNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSL 278
Cdd:COG0183   266 LGLKPLARIVAYAVAGVDPEIMGIGPVPATRKALARAGLTLDDIDLIEINEAFAAQVLAVLRELGLDPDKVNVNGGAIAL 345

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1897358309 279 GHPIGMSGARIVGHLTHALKQ--GEYGLASICNGGGGASAMLIQKL 322
Cdd:COG0183   346 GHPLGASGARILVTLLHELERrgGRYGLATMCIGGGQGIALIIERV 391
PLN02644 PLN02644
acetyl-CoA C-acetyltransferase
 38-322 5.57e-120

acetyl-CoA C-acetyltransferase


Pssm-ID: 215347 [Multi-domain]  Cd Length: 394  Bit Score: 350.55  E-value: 5.57e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309  38 TLKDVMVAGGMESMSNVPYVM--NRGSTPYGGVKLEDLIVKDGLTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYT 115
Cdd:PLN02644  104 GINDVVVAGGMESMSNAPKYLpeARKGSRLGHDTVVDGMLKDGLWDVYNDFGMGVCAELCADQYSISREEQDAYAIQSYE 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309 116 RSKAAWEAGKFGNEVIPVTVTV-KGQPDVVVKEDEEYKRVDFSKVPKLKTVFQKENGTVTAANASTLNDGAAALVLMTAD 194
Cdd:PLN02644  184 RAIAAQEAGAFAWEIVPVEVPGgRGRPSVIVDKDEGLGKFDPAKLRKLRPSFKEDGGSVTAGNASSISDGAAALVLVSGE 263

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309 195 AAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGG 274
Cdd:PLN02644  264 KALELGLQVIAKIRGYADAAQAPELFTTAPALAIPKALKHAGLEASQVDYYEINEAFSVVALANQKLLGLDPEKVNVHGG 343

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1897358309 275 AVSLGHPIGMSGARIVGHLTHALKQ--GEYGLASICNGGGGASAMLIQKL 322
Cdd:PLN02644  344 AVSLGHPIGCSGARILVTLLGVLRSknGKYGVAGICNGGGGASAIVVELM 393
AcCoA-C-Actrans TIGR01930
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ...
 41-320 9.29e-117

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: 341.90  E-value: 9.29e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309  41 DVMVAGGMESMSNVPYVMNRGSTP---YGGVKLEDLIVKDgLTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRS 117
Cdd:TIGR01930 103 DVVVAGGVESMSRVPYGVPRSLRWgvkPGNAELEDARLKD-LTDANTGLPMGVTAENLAKKYGISREEQDEYALRSHQRA 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309 118 KAAWEAGKFGNEVIPVTVTVKGQPDVVVKEDEEYKRVDFSKVPKLKTVFqKENGTVTAANASTLNDGAAALVLMTADAAK 197
Cdd:TIGR01930 182 AKAWEEGLFKDEIVPVTVKGRKGPVTVSSDEGIRPNTTLEKLAKLKPAF-DPDGTVTAGNSSPLNDGAAALLLMSEEKAK 260

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309 198 RLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVS 277
Cdd:TIGR01930 261 ELGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALKKAGLSISDIDLFEINEAFAAQVLACIKELGLDLEKVNVNGGAIA 340

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1897358309 278 LGHPIGMSGARIVGHLTHALKQ--GEYGLASICNGGGGASAMLIQ 320
Cdd:TIGR01930 341 LGHPLGASGARIVTTLLHELKRrgGRYGLATMCIGGGQGAAVILE 385
Thiolase_C pfam02803
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
 201-321 1.60e-60

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: 189.39  E-value: 1.60e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309 201 VTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGH 280
Cdd:pfam02803   1 LKPLARIRSYATAGVDPAIMGIGPAYAIPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGIDPEKVNVNGGAIALGH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1897358309 281 PIGMSGARIVGHLTHALKQ--GEYGLASICNGGGGASAMLIQK 321
Cdd:pfam02803  81 PLGASGARILVTLLHELKRrgGKYGLASLCIGGGQGVAMIIER 123
 
Name Accession Description Interval E-value
thiolase cd00751
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ...
 41-321 1.05e-138

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: 397.62  E-value: 1.05e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309  41 DVMVAGGMESMSNVPYVMNRGSTPY-GGVKLEDLIVKDGLTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKA 119
Cdd:cd00751   104 DVVVAGGVESMSRAPYLLPKARRGGrLGLNTLDGMLDDGLTDPFTGLSMGITAENVAEKYGISREEQDEFALRSHQRAAA 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309 120 AWEAGKFGNEVIPVTVTVKGQPdVVVKEDEEYKR-VDFSKVPKLKTVFqKENGTVTAANASTLNDGAAALVLMTADAAKR 198
Cdd:cd00751   184 AQEAGRFKDEIVPVEVPGRKGP-VVVDRDEGPRPdTTLEKLAKLKPAF-KKDGTVTAGNASGINDGAAAVLLMSEEKAKE 261

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309 199 LNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSL 278
Cdd:cd00751   262 LGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDIDLIEINEAFAAQALACLKELGLDPEKVNVNGGAIAL 341

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1897358309 279 GHPIGMSGARIVGHLTHALKQ--GEYGLASICNGGGGASAMLIQK 321
Cdd:cd00751   342 GHPLGASGARIVVTLLHELKRrgGRYGLATMCIGGGQGAAMVIER 386
PaaJ COG0183
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ...
 41-322 1.13e-128

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: 372.48  E-value: 1.13e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309  41 DVMVAGGMESMSNVPYVMNRGSTPYGG-VKLEDLIVKDGLTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKA 119
Cdd:COG0183   108 DVVIAGGVESMSRAPMLLPKARWGYRMnAKLVDPMINPGLTDPYTGLSMGETAENVAERYGISREEQDAFALRSHQRAAA 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309 120 AWEAGKFGNEVIPVTVTVKGQpDVVVKEDEEYKR-VDFSKVPKLKTVFqKENGTVTAANASTLNDGAAALVLMTADAAKR 198
Cdd:COG0183   188 AIAAGRFDDEIVPVEVPDRKG-EVVVDRDEGPRPdTTLEKLAKLKPAF-KKDGTVTAGNASGINDGAAALLLMSEEAAKE 265

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309 199 LNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSL 278
Cdd:COG0183   266 LGLKPLARIVAYAVAGVDPEIMGIGPVPATRKALARAGLTLDDIDLIEINEAFAAQVLAVLRELGLDPDKVNVNGGAIAL 345

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1897358309 279 GHPIGMSGARIVGHLTHALKQ--GEYGLASICNGGGGASAMLIQKL 322
Cdd:COG0183   346 GHPLGASGARILVTLLHELERrgGRYGLATMCIGGGQGIALIIERV 391
PLN02644 PLN02644
acetyl-CoA C-acetyltransferase
 38-322 5.57e-120

acetyl-CoA C-acetyltransferase


Pssm-ID: 215347 [Multi-domain]  Cd Length: 394  Bit Score: 350.55  E-value: 5.57e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309  38 TLKDVMVAGGMESMSNVPYVM--NRGSTPYGGVKLEDLIVKDGLTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYT 115
Cdd:PLN02644  104 GINDVVVAGGMESMSNAPKYLpeARKGSRLGHDTVVDGMLKDGLWDVYNDFGMGVCAELCADQYSISREEQDAYAIQSYE 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309 116 RSKAAWEAGKFGNEVIPVTVTV-KGQPDVVVKEDEEYKRVDFSKVPKLKTVFQKENGTVTAANASTLNDGAAALVLMTAD 194
Cdd:PLN02644  184 RAIAAQEAGAFAWEIVPVEVPGgRGRPSVIVDKDEGLGKFDPAKLRKLRPSFKEDGGSVTAGNASSISDGAAALVLVSGE 263

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309 195 AAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGG 274
Cdd:PLN02644  264 KALELGLQVIAKIRGYADAAQAPELFTTAPALAIPKALKHAGLEASQVDYYEINEAFSVVALANQKLLGLDPEKVNVHGG 343

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1897358309 275 AVSLGHPIGMSGARIVGHLTHALKQ--GEYGLASICNGGGGASAMLIQKL 322
Cdd:PLN02644  344 AVSLGHPIGCSGARILVTLLGVLRSknGKYGVAGICNGGGGASAIVVELM 393
AcCoA-C-Actrans TIGR01930
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ...
 41-320 9.29e-117

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: 341.90  E-value: 9.29e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309  41 DVMVAGGMESMSNVPYVMNRGSTP---YGGVKLEDLIVKDgLTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRS 117
Cdd:TIGR01930 103 DVVVAGGVESMSRVPYGVPRSLRWgvkPGNAELEDARLKD-LTDANTGLPMGVTAENLAKKYGISREEQDEYALRSHQRA 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309 118 KAAWEAGKFGNEVIPVTVTVKGQPDVVVKEDEEYKRVDFSKVPKLKTVFqKENGTVTAANASTLNDGAAALVLMTADAAK 197
Cdd:TIGR01930 182 AKAWEEGLFKDEIVPVTVKGRKGPVTVSSDEGIRPNTTLEKLAKLKPAF-DPDGTVTAGNSSPLNDGAAALLLMSEEKAK 260

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309 198 RLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVS 277
Cdd:TIGR01930 261 ELGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALKKAGLSISDIDLFEINEAFAAQVLACIKELGLDLEKVNVNGGAIA 340

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1897358309 278 LGHPIGMSGARIVGHLTHALKQ--GEYGLASICNGGGGASAMLIQ 320
Cdd:TIGR01930 341 LGHPLGASGARIVTTLLHELKRrgGRYGLATMCIGGGQGAAVILE 385
PRK05790 PRK05790
putative acyltransferase; Provisional
 41-319 2.97e-112

putative acyltransferase; Provisional


Pssm-ID: 180261 [Multi-domain]  Cd Length: 393  Bit Score: 330.58  E-value: 2.97e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309  41 DVMVAGGMESMSNVPYVMN--RGSTPYGGVKLEDLIVKDGLTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSK 118
Cdd:PRK05790  108 DIVVAGGQESMSQAPHVLPgsRWGQKMGDVELVDTMIHDGLTDAFNGYHMGITAENLAEQYGITREEQDEFALASQQKAE 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309 119 AAWEAGKFGNEVIPVTVTVKGQPDVVVKEDeEYKRVDFS--KVPKLKTVFqKENGTVTAANASTLNDGAAALVLMTADAA 196
Cdd:PRK05790  188 AAIKAGRFKDEIVPVTIKQRKGDPVVVDTD-EHPRPDTTaeSLAKLRPAF-DKDGTVTAGNASGINDGAAAVVVMSEAKA 265

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309 197 KRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAV 276
Cdd:PRK05790  266 KELGLTPLARIVSYAVAGVDPAIMGIGPVPAIRKALEKAGWSLADLDLIEINEAFAAQALAVEKELGLDPEKVNVNGGAI 345

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1897358309 277 SLGHPIGMSGARIVGHLTHALK--QGEYGLASICNGGGGASAMLI 319
Cdd:PRK05790  346 ALGHPIGASGARILVTLLHEMKrrGAKKGLATLCIGGGQGVALIV 390
PRK08235 PRK08235
acetyl-CoA C-acetyltransferase;
41-320 2.67e-105

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181311 [Multi-domain]  Cd Length: 393  Bit Score: 313.19  E-value: 2.67e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309  41 DVMVAGGMESMSNVPYVMNRGSTPY--GGVKLEDLIVKDGLTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSK 118
Cdd:PRK08235  108 SVIVAGGMESMSNAPYILPGARWGYrmGDNEVIDLMVADGLTCAFSGVHMGVYGGEVAKELGISREAQDEWAYRSHQRAV 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309 119 AAWEAGKFGNEVIPVTVT-VKGQPDVVVKEDEEYKRVDFSKVPKLKTVFQKEnGTVTAANASTLNDGAAALVLMTADAAK 197
Cdd:PRK08235  188 SAHEEGRFEEEIVPVTIPqRKGDPIVVAKDEAPRKDTTIEKLAKLKPVFDKT-GTITAGNAPGVNDGAAALVLMSEDRAK 266

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309 198 RLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVS 277
Cdd:PRK08235  267 QEGRKPLATILAHTAIAVEAKDFPRTPGYAINALLEKTGKTVEDIDLFEINEAFAAVALASTEIAGIDPEKVNVNGGAVA 346

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1897358309 278 LGHPIGMSGARIVGHLTHALKQ--GEYGLASICNGGGGASAMLIQ 320
Cdd:PRK08235  347 LGHPIGASGARIIVTLIHELKRrgGGIGIAAICSGGGQGDAVLIE 391
PRK09051 PRK09051
beta-ketothiolase BktB;
41-322 2.76e-84

beta-ketothiolase BktB;


Pssm-ID: 181625 [Multi-domain]  Cd Length: 394  Bit Score: 259.51  E-value: 2.76e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309  41 DVMVAGGMESMSNVPYVM--NRGSTPYGGVKLEDLIVkDGLTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSK 118
Cdd:PRK09051  110 DVAIGGGAESMSRAPYLLpaARWGARMGDAKLVDMMV-GALHDPFGTIHMGVTAENVAAKYGISREAQDALALESHRRAA 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309 119 AAWEAGKFGNEVIPVTV-TVKGqpDVVVKEDEEYKR-VDFSKVPKLKTVFQKENGTVTAANASTLNDGAAALVLMTADAA 196
Cdd:PRK09051  189 AAIAAGYFKDQIVPVEIkTRKG--EVVFDTDEHVRAdTTLEDLAKLKPVFKKENGTVTAGNASGINDGAAAVVLAEADAA 266

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309 197 KRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAV 276
Cdd:PRK09051  267 EARGLKPLARLVGYAHAGVDPEYMGIGPVPATQKALERAGLTVADLDVIEANEAFAAQACAVTRELGLDPAKVNPNGSGI 346

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1897358309 277 SLGHPIGMSGARIVGHLTHALK--QGEYGLASICNGGGGASAMLIQKL 322
Cdd:PRK09051  347 SLGHPVGATGAIITVKALYELQriGGRYALVTMCIGGGQGIAAIFERL 394
PRK06954 PRK06954
acetyl-CoA C-acetyltransferase;
41-320 3.25e-80

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180775 [Multi-domain]  Cd Length: 397  Bit Score: 249.04  E-value: 3.25e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309  41 DVMVAGGMESMSNVPYVM--NRGSTPYGGVKLEDLIVKDGLTDVYNKIH-MGSCAENTAKKLNIARNEQDAYAINSYTRS 117
Cdd:PRK06954  113 DVIVAGGMESMTNAPYLLpkARGGMRMGHGQVLDHMFLDGLEDAYDKGRlMGTFAEECAGEYGFTREAQDAFAIESLARA 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309 118 KAAWEAGKFGNEVIPVTVTVKGQpDVVVKEDEEYKRVDFSKVPKLKTVFQKeNGTVTAANASTLNDGAAALVLMTADAAK 197
Cdd:PRK06954  193 KRANEDGSFAWEIAPVTVAGKKG-DTVIDRDEQPFKANPEKIPTLKPAFSK-TGTVTAANSSSISDGAAALVMMRASTAK 270

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309 198 RLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVS 277
Cdd:PRK06954  271 RLGLAPLARVVGHSTFAQAPSKFTTAPVGAIRKLFEKNGWRAAEVDLFEINEAFAVVTMAAMKEHGLPHEKVNVNGGACA 350

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1897358309 278 LGHPIGMSGARIVGHLTHALKQ--GEYGLASICNGGGGASAMLIQ 320
Cdd:PRK06954  351 LGHPIGASGARILVTLIGALRArgGKRGVASLCIGGGEATAMGIE 395
PRK09050 PRK09050
beta-ketoadipyl CoA thiolase; Validated
 41-322 5.63e-74

beta-ketoadipyl CoA thiolase; Validated


Pssm-ID: 181624 [Multi-domain]  Cd Length: 401  Bit Score: 233.31  E-value: 5.63e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309  41 DVMVAGGMESMSNVPYVMNRGSTPYG-GVKLEDL-----IVKDGLTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSY 114
Cdd:PRK09050  110 ELMIAGGVESMSRAPFVMGKADSAFSrQAEIFDTtigwrFVNPLMKAQYGVDSMPETAENVAEDYNISRADQDAFALRSQ 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309 115 TRSKAAWEAGKFGNEVIPVTVTVKGQPDVVVKEDEeYKRVDFS--KVPKLKTVFqKENGTVTAANASTLNDGAAALVLMT 192
Cdd:PRK09050  190 QRAAAAQAAGFLAEEIVPVTIPQKKGDPVVVDRDE-HPRPETTleALAKLKPVF-RPDGTVTAGNASGVNDGAAALLLAS 267

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309 193 ADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEI--DPQKVN 270
Cdd:PRK09050  268 EAAAKKHGLTPRARILGMATAGVEPRIMGIGPAPATRKLLARLGLTIDQFDVIELNEAFAAQGLAVLRQLGLadDDARVN 347

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1897358309 271 INGGAVSLGHPIGMSGARIVGHLTHALKQ--GEYGLASICNGGGGASAMLIQKL 322
Cdd:PRK09050  348 PNGGAIALGHPLGMSGARLVLTALHQLERtgGRYALCTMCIGVGQGIALAIERV 401
PRK06205 PRK06205
acetyl-CoA C-acetyltransferase;
41-312 1.70e-72

acetyl-CoA C-acetyltransferase;


Pssm-ID: 235741 [Multi-domain]  Cd Length: 404  Bit Score: 229.49  E-value: 1.70e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309  41 DVMVAGGMESMSNVPYVMN--RGSTPYGGVKLEDLIVKDGLT---DVYNKIH-MGSCAENTAKKLNIARNEQDAYAINSY 114
Cdd:PRK06205  108 DVVIAGGAESMSNVEFYTTdmRWGVRGGGVQLHDRLARGRETaggRRFPVPGgMIETAENLRREYGISREEQDALAVRSH 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309 115 TRSKAAWEAGKFGNEVIPVTVTVKGQPDVVVKEDEEYkRVDFS--KVPKLKTVFQK--ENGTVTAANASTLNDGAAALVL 190
Cdd:PRK06205  188 QRAVAAQEAGRFDDEIVPVTVPQRKGDPTVVDRDEHP-RADTTleSLAKLRPIMGKqdPEATVTAGNASGQNDAAAACLV 266

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309 191 MTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQ--- 267
Cdd:PRK06205  267 TTEDKAEELGLRPLARLVSWAVAGVEPSRMGIGPVPATEKALARAGLTLDDIDLIELNEAFAAQVLAVLKEWGFGADdee 346

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1897358309 268 KVNINGGAVSLGHPIGMSGARIVGHLTHALK--QGEYGLASICNGGG 312
Cdd:PRK06205  347 RLNVNGSGISLGHPVGATGGRILATLLRELQrrQARYGLETMCIGGG 393
PRK06445 PRK06445
acetyl-CoA C-acetyltransferase;
41-321 3.75e-72

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180563 [Multi-domain]  Cd Length: 394  Bit Score: 228.45  E-value: 3.75e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309  41 DVMVAGGMESMSNVPYVMNRGSTPYGGVKLEDLIVKDGLTDVYNkihMGSCAENTAKKLNIARNEQDAYAINSYTRSKAA 120
Cdd:PRK06445  115 DIVIAGGVEHMTRTPMGDNPHIEPNPKLLTDPKYIEYDLTTGYV---MGLTAEKLAEEAGIKREEMDRWSLRSHQLAAKA 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309 121 WEAGKFGNEVIPVTVTVKGQPDVVVKEDEEYKRVDFSKVPKLKTVFqKENGTVTAANASTLNDGAAALVLMTADAAKRLN 200
Cdd:PRK06445  192 IQEGYFKDEILPIEVEVEGKKKVVDVDQSVRPDTSLEKLAKLPPAF-KPDGVITAGNSSPLNSGASYVLLMSKKAVKKYG 270

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309 201 VTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGH 280
Cdd:PRK06445  271 LKPMAKIRSFGFAGVPPAIMGKGPVPASKKALEKAGLSVKDIDLWEINEAFAVVVLYAIKELGLDPETVNIKGGAIAIGH 350

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1897358309 281 PIGMSGARIVGHLTHAL--KQGEYGLASICNGGGGASAMLIQK 321
Cdd:PRK06445  351 PLGATGARIVGTLARQLqiKGKDYGVATLCVGGGQGGAVVLER 393
PRK06633 PRK06633
acetyl-CoA C-acetyltransferase;
41-320 2.75e-71

acetyl-CoA C-acetyltransferase;


Pssm-ID: 168632 [Multi-domain]  Cd Length: 392  Bit Score: 226.06  E-value: 2.75e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309  41 DVMVAGGMESMS---NVPYVmnRGSTPYGGVKLEDLIVKDGLTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRS 117
Cdd:PRK06633  109 EIVIAGGQENMSlgmHGSYI--RAGAKFGDIKMVDLMQYDGLTDVFSGVFMGITAENISKQFNISRQEQDEFALSSHKKA 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309 118 KAAWEAGKFGNEVIPVTVTVKGQPDVVVKEDEEYKRVDFSKVPKLKTVFQKeNGTVTAANASTLNDGAAALVLMTADAAK 197
Cdd:PRK06633  187 AKAQLAGIFKDEILPIEVTIKKTTSLFDHDETVRPDTSLEILSKLRPAFDK-NGVVTAGNASSINDGAACLMVVSEEALK 265

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309 198 RLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVS 277
Cdd:PRK06633  266 KHNLTPLARIVSYASAGVDPSIMGTAPVPASQKALSKAGWSVNDLEVIEVNEAFAAQSIYVNREMKWDMEKVNINGGAIA 345

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1897358309 278 LGHPIGMSGARIVGHLTHALK--QGEYGLASICNGGGGASAMLIQ 320
Cdd:PRK06633  346 IGHPIGASGGRVLITLIHGLRraKAKKGLVTLCIGGGMGMAMCVE 390
PRK05656 PRK05656
acetyl-CoA C-acetyltransferase;
41-321 8.11e-71

acetyl-CoA C-acetyltransferase;


Pssm-ID: 168156  Cd Length: 393  Bit Score: 224.77  E-value: 8.11e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309  41 DVMVAGGMESMSNVPYVM--NRGSTPYGGVKLEDLIVKDGLTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSK 118
Cdd:PRK05656  108 EVIIAGGQENMSLAPYVLpgARTGLRMGHAQLVDSMITDGLWDAFNDYHMGITAENLVEKYGISREAQDAFAAASQQKAV 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309 119 AAWEAGKFGNEVIPVTV-TVKGQPDVVVKEDEEYKRVDFSKVPKLKTVFQKEnGTVTAANASTLNDGAAALVLMTADAAK 197
Cdd:PRK05656  188 AAIEAGRFDDEITPILIpQRKGEPLAFATDEQPRAGTTAESLAKLKPAFKKD-GSVTAGNASSLNDGAAAVLLMSAAKAK 266

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309 198 RLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVS 277
Cdd:PRK05656  267 ALGLPVLAKIAAYANAGVDPAIMGIGPVSATRRCLDKAGWSLAELDLIEANEAFAAQSLAVGKELGWDAAKVNVNGGAIA 346

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1897358309 278 LGHPIGMSGARIVGHLTHAL--KQGEYGLASICNGGGGASAMLIQK 321
Cdd:PRK05656  347 LGHPIGASGCRVLVTLLHEMirRDAKKGLATLCIGGGQGVALAIER 392
PRK07851 PRK07851
acetyl-CoA C-acetyltransferase;
79-322 8.13e-67

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181146 [Multi-domain]  Cd Length: 406  Bit Score: 214.87  E-value: 8.13e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309  79 LTDVYnkIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVtvkgqPD--VVVKEDEEYKRVDF 156
Cdd:PRK07851  166 LPDVY--IAMGQTAENVAQLTGISREEQDEWGVRSQNRAEEAIANGFFEREITPVTL-----PDgtVVSTDDGPRAGTTY 238

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309 157 SKVPKLKTVFqKENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVG 236
Cdd:PRK07851  239 EKVSQLKPVF-RPDGTVTAGNACPLNDGAAAVVIMSDTKARELGLTPLARIVSTGVSGLSPEIMGLGPVEASKQALARAG 317

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309 237 LKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALK--QGEYGLASICNGGGGA 314
Cdd:PRK07851  318 MSIDDIDLVEINEAFAAQVLPSARELGIDEDKLNVSGGAIALGHPFGMTGARITTTLLNNLQthDKTFGLETMCVGGGQG 397


                  ....*...
gi 1897358309 315 SAMLIQKL 322
Cdd:PRK07851  398 MAMVLERL 405
PRK08170 PRK08170
acetyl-CoA C-acetyltransferase;
41-322 2.92e-66

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181265 [Multi-domain]  Cd Length: 426  Bit Score: 214.11  E-value: 2.92e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309  41 DVMVAGGMESMSNVPYVMNRGSTPY---------GGVKLEDL-------------IVKdGLTDVYNKIHMGSCAENTAKK 98
Cdd:PRK08170  109 DLVLAGGVEAMSHAPLLFSEKMVRWlagwyaaksIGQKLAALgklrpsylapvigLLR-GLTDPVVGLNMGQTAEVLAHR 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309  99 LNIARNEQDAYAINSYTRSKAAWEAGKFGnEVIPVtVTVKGQpdvvVKEDEEYKRVDFS--KVPKLKTVFQKENGTVTAA 176
Cdd:PRK08170  188 FGITREQMDAYAARSHQRLAAAQAEGRLK-EVVPL-FDRDGK----FYDHDDGVRPDSSmeKLAKLKPFFDRPYGRVTAG 261

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309 177 NASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVL 256
Cdd:PRK08170  262 NSSQITDGACWLLLASEEAVKKYGLPPLGRIVDSQWAALDPSQMGLGPVHAATPLLQRHGLTLEDLDLWEINEAFAAQVL 341

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309 257 ANIKML-----------------EIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALKQ--GEYGLASICNGGGGASAM 317
Cdd:PRK08170  342 ACLAAWadeeycreqlgldgalgELDRERLNVDGGAIALGHPVGASGARIVLHLLHALKRrgTKRGIAAICIGGGQGGAM 421


                  ....*
gi 1897358309 318 LIQKL 322
Cdd:PRK08170  422 LLERV 426
PRK09052 PRK09052
acetyl-CoA C-acyltransferase;
41-322 1.53e-65

acetyl-CoA C-acyltransferase;


Pssm-ID: 181626 [Multi-domain]  Cd Length: 399  Bit Score: 211.40  E-value: 1.53e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309  41 DVMVAGGMESMSNVPYVMNRGS-TPYGGVKLEDLIVKDGltdvynkihMGSCAENTAKKLNIARNEQDAYAINSYTRSKA 119
Cdd:PRK09052  115 DVMIAAGVESMSMVPMMGNKPSmSPAIFARDENVGIAYG---------MGLTAEKVAEQWKVSREDQDAFALESHQKAIA 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309 120 AWEAGKFGNEVIPVTVTVKgQPD-----VVVKEDE----EYKRVDFS--KVPKLKTVFQKEnGTVTAANASTLNDGAAAL 188
Cdd:PRK09052  186 AQQAGEFKDEITPYEITER-FPDlatgeVDVKTRTvdldEGPRADTSleGLAKLKPVFANK-GSVTAGNSSQTSDGAGAV 263

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309 189 VLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQK 268
Cdd:PRK09052  264 ILVSEKALKQFNLTPLARFVSFAVAGVPPEIMGIGPIEAIPAALKQAGLKQDDLDWIELNEAFAAQSLAVIRDLGLDPSK 343

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1897358309 269 VNINGGAVSLGHPIGMSGARIVGHLTHAL--KQGEYGLASICNGGGGASAMLIQKL 322
Cdd:PRK09052  344 VNPLGGAIALGHPLGATGAIRTATVVHGLrrTNLKYGMVTMCVGTGMGAAGIFERL 399
PRK06366 PRK06366
acetyl-CoA C-acetyltransferase;
40-320 1.21e-62

acetyl-CoA C-acetyltransferase;


Pssm-ID: 102340 [Multi-domain]  Cd Length: 388  Bit Score: 203.70  E-value: 1.21e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309  40 KDVMVAGGMESMSNVPYVMNR------GSTPYGGVKLEDLIVKDGLTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINS 113
Cdd:PRK06366  107 RDLVIAGGMENMSNAPFLLPSdlrwgpKHLLHKNYKIDDAMLVDGLIDAFYFEHMGVSAERTARKYGITREMADEYSVQS 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309 114 YTRSKAAWEAGKFGNEVIPVTVtvkgqpdvvVKEDEEYKRVDFSKVPKLKTVFQKeNGTVTAANASTLNDGAAALVLMTA 193
Cdd:PRK06366  187 YERAIRATESGEFRNEIVPFND---------LDRDEGIRKTTMEDLAKLPPAFDK-NGILTAGNSAQLSDGGSALVMASE 256

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309 194 DAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNING 273
Cdd:PRK06366  257 KAINEYGLKPIARITGYESASLDPLDFVEAPIPATRKLLEKQNKSIDYYDLVEHNEAFSIASIIVRDQLKIDNERFNVNG 336

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1897358309 274 GAVSLGHPIGMSGARIVGHLTHALKQG--EYGLASICNGGGGASAMLIQ 320
Cdd:PRK06366  337 GAVAIGHPIGNSGSRIIVTLINALKTRhmKTGLATLCHGGGGAHTLTLE 385
PRK07108 PRK07108
acetyl-CoA C-acyltransferase;
41-322 8.15e-62

acetyl-CoA C-acyltransferase;


Pssm-ID: 180843 [Multi-domain]  Cd Length: 392  Bit Score: 201.54  E-value: 8.15e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309  41 DVMVAGGMESMSNVPYVMNRGstpyggvKLEDLIVKDGLTDVYnkIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAA 120
Cdd:PRK07108  110 DVFVAGGVESISCVQNEMNRH-------MLREGWLVEHKPEIY--WSMLQTAENVAKRYGISKERQDEYGVQSQQRAAAA 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309 121 WEAGKFGNEVIPVTVTVKGQ---------PDVVVKEDEEYkRVDFSK--VPKLKTVFqkENGTVTAANASTLNDGAAALV 189
Cdd:PRK07108  181 QAAGRFDDEIVPITVTAGVAdkatgrlftKEVTVSADEGI-RPDTTLegVSKIRSAL--PGGVITAGNASQFSDGASACV 257

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309 190 LMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKV 269
Cdd:PRK07108  258 VMNAKVAEREGLQPLGIFRGFAVAGCEPDEMGIGPVFAVPKLLKQAGLKVDDIDLWELNEAFAVQVLYCRDTLGIPMDRL 337

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1897358309 270 NINGGAVSLGHPIGMSGARIVGhltHALKQGE-----YGLASICNGGGGASAMLIQKL 322
Cdd:PRK07108  338 NVNGGAIAVGHPYGVSGARLTG---HALIEGKrrgakYVVVTMCIGGGQGAAGLFEVL 392
Thiolase_C pfam02803
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
 201-321 1.60e-60

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: 189.39  E-value: 1.60e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309 201 VTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGH 280
Cdd:pfam02803   1 LKPLARIRSYATAGVDPAIMGIGPAYAIPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGIDPEKVNVNGGAIALGH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1897358309 281 PIGMSGARIVGHLTHALKQ--GEYGLASICNGGGGASAMLIQK 321
Cdd:pfam02803  81 PLGASGARILVTLLHELKRrgGKYGLASLCIGGGQGVAMIIER 123
PRK07661 PRK07661
acetyl-CoA C-acetyltransferase;
41-316 3.22e-60

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181072 [Multi-domain]  Cd Length: 391  Bit Score: 197.28  E-value: 3.22e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309  41 DVMVAGGMESMSNVPYVmnrgstpyGGVKLEDLIVKDGLTDVYnkIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAA 120
Cdd:PRK07661  110 EAVIAGGAESMSLVPMM--------GHVVRPNPRLVEAAPEYY--MGMGHTAEQVAVKYGISREDQDAFAVRSHQRAAKA 179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309 121 WEAGKFGNEVIPVTVTV-------KGQPDVVVKEDEEYKRVDFSK--VPKLKTVFQKeNGTVTAANASTLNDGAAALVLM 191
Cdd:PRK07661  180 LAEGKFADEIVPVDVTLrtvgennKLQEETITFSQDEGVRADTTLeiLGKLRPAFNV-KGSVTAGNSSQMSDGAAAVLLM 258

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309 192 TADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNI 271
Cdd:PRK07661  259 DREKAESDGLKPLAKFRSFAVAGVPPEVMGIGPIAAIPKALKLAGLELSDIGLFELNEAFASQSIQVIRELGLDEEKVNV 338

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1897358309 272 NGGAVSLGHPIGMSGARIVGHLTHALK-QGE-YGLASICNGGGGASA 316
Cdd:PRK07661  339 NGGAIALGHPLGCTGAKLTLSLIHEMKrRNEqFGIVTMCIGGGMGAA 385
Thiolase_N pfam00108
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
 41-194 1.83e-59

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: 191.36  E-value: 1.83e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309  41 DVMVAGGMESMSNVPYVMN---RGSTPYGGVKLEDLIVKDGLTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRS 117
Cdd:pfam00108 105 DVVLAGGVESMSHAPYALPtdaRSGLKHGDEKKHDLLIPDGLTDAFNGYHMGLTAENVAKKYGISREEQDAFAVKSHQKA 184

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1897358309 118 KAAWEAGKFGNEVIPVTVTVKGQPDVVVKEDEEYKRVDFSKVPKLKTVFQKEnGTVTAANASTLNDGAAALVLMTAD 194
Cdd:pfam00108 185 AAAPKAGKFKDEIVPVTVKGRKGKPTVDKDEGIRPPTTAEPLAKLKPAFDKE-GTVTAGNASPINDGAAAVLLMSES 260
PRK07801 PRK07801
acetyl-CoA C-acetyltransferase;
41-322 4.83e-59

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181123 [Multi-domain]  Cd Length: 382  Bit Score: 194.16  E-value: 4.83e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309  41 DVMVAGGMESMSNVP--YVMNRG-----STPYGGVKledlivkdGLTDVYNK--IHMGSCAENTAKKLNIARNEQDAYAI 111
Cdd:PRK07801  109 DLVVAGGVQNMSQIPisSAMTAGeqlgfTSPFAESK--------GWLHRYGDqeVSQFRGAELIAEKWGISREEMERFAL 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309 112 NSYTRSKAAWEAGKFGNEVIPVTvtvkgqpDVVVkeDEEYKRVDFSKVPKLKTVFqkENGTVTAANASTLNDGAAALVLM 191
Cdd:PRK07801  181 ESHRRAFAAIRAGRFDNEIVPVG-------GVTV--DEGPRETSLEKMAGLKPLV--EGGRLTAAVASQISDGASAVLLA 249

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309 192 TADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNI 271
Cdd:PRK07801  250 SERAVKRHGLTPRARIHHLSVRGDDPVFMLTAPIPATRYALEKTGLSIDDIDVVEINEAFAPVVLAWLKETGADPAKVNP 329

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1897358309 272 NGGAVSLGHPIGMSGARIVGHLTHALKQ--GEYGLASICNGGGGASAMLIQKL 322
Cdd:PRK07801  330 NGGAIALGHPLGATGAKLMTTLLHELERtgGRYGLQTMCEGGGTANVTIIERL 382
fadA PRK08947
3-ketoacyl-CoA thiolase; Reviewed
 41-322 2.32e-58

3-ketoacyl-CoA thiolase; Reviewed


Pssm-ID: 181592 [Multi-domain]  Cd Length: 387  Bit Score: 192.49  E-value: 2.32e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309  41 DVMVAGGMESMSNVPyvMNRGSTPYggvkledlivkDGLTDVYNKIH--MGSCAENTAKKLNIARNEQDAYAINSYTRSK 118
Cdd:PRK08947  111 DVFLIGGVEHMGHVP--MNHGVDFH-----------PGLSKNVAKAAgmMGLTAEMLGKMHGISREQQDAFAARSHQRAW 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309 119 AAWEAGKFGNEVIPVTvtvkGQpdvvvKEDEEYKRVDFSKV----------PKLKTVFQKENGTVTAANASTLNDGAAAL 188
Cdd:PRK08947  178 AATQEGRFKNEIIPTE----GH-----DADGVLKLFDYDEVirpettvealAALRPAFDPVNGTVTAGTSSALSDGASAM 248

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309 189 VLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAF---SLVVLANIKMLEID 265
Cdd:PRK08947  249 LVMSESRAKELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISDIDVFELNEAFaaqSLPCLKDLGLLDKM 328

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1897358309 266 PQKVNINGGAVSLGHPIGMSGARIVGHLTHALKQ--GEYGLASICNGGGGASAMLIQKL 322
Cdd:PRK08947  329 DEKVNLNGGAIALGHPLGCSGARISTTLLNLMERkdAQFGLATMCIGLGQGIATVFERV 387
PRK06504 PRK06504
acetyl-CoA C-acetyltransferase;
41-322 7.87e-58

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180595 [Multi-domain]  Cd Length: 390  Bit Score: 191.10  E-value: 7.87e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309  41 DVMVAGGMESMSNVPyvMNRGSTpyggvkledLIVKDGLTDV--------YNKIH----MGscAENTAKKLNIARNEQDA 108
Cdd:PRK06504  109 DIVIAAGVESMTRVP--MGSPST---------LPAKNGLGHYkspgmeerYPGIQfsqfTG--AEMMAKKYGLSKDQLDE 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309 109 YAINSYTRSKAAWEAGKFGNEVIPVTVTVKGQPDVVVKEDEEYkRVDFS--KVPKLKTVfqKENGTVTAANASTLNDGAA 186
Cdd:PRK06504  176 FALQSHQRAIAATQAGKFKAEIVPLEITRADGSGEMHTVDEGI-RFDATleGIAGVKLI--AEGGRLTAATASQICDGAS 252

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309 187 ALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDP 266
Cdd:PRK06504  253 GVMVVNERGLKALGVKPLARIHHMTVIGGDPVIMLEAPLPATERALKKAGMKIDDIDLYEVNEAFASVPLAWLKATGADP 332

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1897358309 267 QKVNINGGAVSLGHPIGMSGARIVGHLTHALKQ--GEYGLASICNGGGGASAMLIQKL 322
Cdd:PRK06504  333 ERLNVNGGAIALGHPLGASGTKLMTTLVHALKQrgKRYGLQTMCEGGGMANVTIVERL 390
PLN02287 PLN02287
3-ketoacyl-CoA thiolase
 41-318 2.31e-57

3-ketoacyl-CoA thiolase


Pssm-ID: 215161 [Multi-domain]  Cd Length: 452  Bit Score: 191.52  E-value: 2.31e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309  41 DVMVAGGMESMSNVPYVMNRGSTPyggvKLEDL-IVKDGLtdvynkIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKA 119
Cdd:PLN02287  154 DIGIGAGVESMTTNPMAWEGGVNP----RVESFsQAQDCL------LPMGITSENVAERFGVTREEQDQAAVESHRKAAA 223

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309 120 AWEAGKFGNEVIPVTV------TVKGQPDVVVKEDEEYKRVDFSKVPKLKTVFqKENGTVTAANASTLNDGAAALVLMTA 193
Cdd:PLN02287  224 ATASGKFKDEIVPVHTkivdpkTGEEKPIVISVDDGIRPNTTLADLAKLKPVF-KKNGTTTAGNSSQVSDGAGAVLLMKR 302

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309 194 DAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNING 273
Cdd:PLN02287  303 SVAMQKGLPILGVFRSFAAVGVDPAVMGIGPAVAIPAAVKAAGLELDDIDLFEINEAFASQFVYCCKKLGLDPEKVNVNG 382

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1897358309 274 GAVSLGHPIGMSGARIVGHLTHALKQ----GEYGLASICNGGG-GASAML 318
Cdd:PLN02287  383 GAIALGHPLGATGARCVATLLHEMKRrgkdCRFGVVSMCIGTGmGAAAVF 432
fadI PRK08963
3-ketoacyl-CoA thiolase; Reviewed
 41-320 2.42e-57

3-ketoacyl-CoA thiolase; Reviewed


Pssm-ID: 181597 [Multi-domain]  Cd Length: 428  Bit Score: 190.97  E-value: 2.42e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309  41 DVMVAGGMESMSNVP-----------YVMNRGST------PYGGVKLEDLI-VKDGLTDVYNKIHMGSCAENTAKKLNIA 102
Cdd:PRK08963  111 DIGIAGGADSSSVLPigvskklaralVDLNKARTlgqrlkLFSRLRLRDLLpVPPAVAEYSTGLRMGDTAEQMAKTYGIS 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309 103 RNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTVKGQP---DVVVKEDEeykrvDFSKVPKLKTVFQKENGTVTAANAS 179
Cdd:PRK08963  191 REEQDALAHRSHQLAAQAWAEGKLDDEVMTAHVPPYKQPleeDNNIRGDS-----TLEDYAKLRPAFDRKHGTVTAANST 265

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309 180 TLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPI-DFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLAN 258
Cdd:PRK08963  266 PLTDGAAAVLLMSESRAKALGLTPLGYLRSYAFAAIDVWqDMLLGPAYATPLALERAGLTLADLTLIDMHEAFAAQTLAN 345

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309 259 IKML-----------------EIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALKQ--GEYGLASICNGGGGASAMLI 319
Cdd:PRK08963  346 LQMFaserfareklgrsqaigEVDMSKFNVLGGSIAYGHPFAATGARMITQTLHELRRrgGGLGLTTACAAGGLGAAMVL 425


                  .
gi 1897358309 320 Q 320
Cdd:PRK08963  426 E 426
PRK08131 PRK08131
3-oxoadipyl-CoA thiolase;
41-321 6.10e-57

3-oxoadipyl-CoA thiolase;


Pssm-ID: 181242 [Multi-domain]  Cd Length: 401  Bit Score: 189.22  E-value: 6.10e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309  41 DVMVAGGMESMSNVPYVMNRGSTPYGgvklEDLIVKDG----------LTDVYNKIHMGSCAENTAKKLNIARNEQDAYA 110
Cdd:PRK08131  109 DLYLAGGVESMSRAPFVMGKAESAFS----RDAKVFDTtigarfpnpkIVAQYGNDSMPETGDNVAAEFGISREDADRFA 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309 111 INSYTRSKAAWEAGKFGNEVIPVTV-TVKGQPDVVVKEDEEYK-RVDFSKVPKLKTVFqkENGTVTAANASTLNDGAAAL 188
Cdd:PRK08131  185 AQSQAKYQAAKEEGFFADEITPIEVpQGRKLPPKLVAEDEHPRpSSTVEALTKLKPLF--EGGVVTAGNASGINDGAAAL 262

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309 189 VLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEI--DP 266
Cdd:PRK08131  263 LIGSRAAGEKYGLKPMARILSSAAAGVEPRIMGIGPVEAIKKALARAGLTLDDMDIIEINEAFASQVLGCLKGLGVdfDD 342

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1897358309 267 QKVNINGGAVSLGHPIGMSGARIVghLTHA----LKQGEYGLASICNGGGGASAMLIQK 321
Cdd:PRK08131  343 PRVNPNGGAIAVGHPLGASGARLA--LTAArelqRRGKRYAVVSLCIGVGQGLAMVIER 399
PRK07850 PRK07850
steroid 3-ketoacyl-CoA thiolase;
41-322 1.04e-55

steroid 3-ketoacyl-CoA thiolase;


Pssm-ID: 181145 [Multi-domain]  Cd Length: 387  Bit Score: 185.70  E-value: 1.04e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309  41 DVMVAGGMESMSNVPYVMNRGSTPyGGVKLEDLIVkdgltDVYNKIhmgSCAENTAKKLNIARNEQDAYAINSYTRSKAA 120
Cdd:PRK07850  109 DVGIACGVEAMSRVPLGANAGPGR-GLPRPDSWDI-----DMPNQF---EAAERIAKRRGITREDVDAFGLRSQRRAAQA 179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309 121 WEAGKFGNEVIPVTVTV---KGQP---DVVVKEDEEYKRVDFSKVPKLKTVFqkENGTVTAANASTLNDGAAALVLMTAD 194
Cdd:PRK07850  180 WAEGRFDREISPVQAPVldeEGQPtgeTRLVTRDQGLRDTTMEGLAGLKPVL--EGGIHTAGTSSQISDGAAAVLWMDED 257

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309 195 AAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGG 274
Cdd:PRK07850  258 RARALGLRPRARIVAQALVGAEPYYHLDGPVQATAKVLEKAGMKIGDIDLVEINEAFASVVLSWAQVHEPDMDKVNVNGG 337

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1897358309 275 AVSLGHPIGMSGARIVGHLTHALKQ--GEYGLASICNGGGGASAMLIQKL 322
Cdd:PRK07850  338 AIALGHPVGSTGARLITTALHELERtdKSTALITMCAGGALSTGTIIERI 387
PRK08242 PRK08242
acetyl-CoA C-acetyltransferase;
41-322 6.01e-54

acetyl-CoA C-acetyltransferase;


Pssm-ID: 236197 [Multi-domain]  Cd Length: 402  Bit Score: 181.23  E-value: 6.01e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309  41 DVMVAGGMESMSNVPYVMNRGSTPyggvkledliVKDGLTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAA 120
Cdd:PRK08242  111 DLVIAGGVESMSRVPMGSDGGAWA----------MDPSTNFPTYFVPQGISADLIATKYGFSREDVDAYAVESQQRAAAA 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309 121 WEAGKFGNEVIPVtvtvKGQPDVVVKEDEEYKR--VDFSKVPKLKTVFQ--------------------KENGTVTAANA 178
Cdd:PRK08242  181 WAEGYFAKSVVPV----KDQNGLTILDHDEHMRpgTTMESLAKLKPSFAmmgemggfdavalqkypeveRINHVHHAGNS 256

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309 179 STLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLAN 258
Cdd:PRK08242  257 SGIVDGAAAVLIGSEEAGKALGLKPRARIVATATIGSDPTIMLTGPVPATRKALAKAGLTVDDIDLFELNEAFASVVLRF 336

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1897358309 259 IKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHAL--KQGEYGLASICNGGGGASAMLIQKL 322
Cdd:PRK08242  337 MQALDIPHDKVNVNGGAIAMGHPLGATGAMILGTVLDELerRGKRTALITLCVGGGMGIATIIERV 402
PRK06690 PRK06690
acetyl-CoA C-acyltransferase;
44-322 6.56e-51

acetyl-CoA C-acyltransferase;


Pssm-ID: 180659 [Multi-domain]  Cd Length: 361  Bit Score: 172.26  E-value: 6.56e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309  44 VAGGMESMSNVPYVMNRGSTPyggvkledlivkdgltDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEA 123
Cdd:PRK06690  105 IAGGVESTSTSPFQNRARFSP----------------ETIGDPDMGVAAEYVAERYNITREMQDEYACLSYKRTLQALEK 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309 124 GKFGNEVIPVTvtvkGQPDVVVKEDEEYKRVdfskVPKLKTVFQKeNGTVTAANASTLNDGAAALVLMTADAAKRLNVTP 203
Cdd:PRK06690  169 GYIHEEILSFN----GLLDESIKKEMNYERI----IKRTKPAFLH-NGTVTAGNSCGVNDGACAVLVMEEGQARKLGYKP 239

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309 204 LARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIG 283
Cdd:PRK06690  240 VLRFVRSAVVGVDPNLPGTGPIFAVNKLLNEMNMKVEDIDYFEINEAFASKVVACAKELQIPYEKLNVNGGAIALGHPYG 319

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1897358309 284 MSGARIVGHLTHALKQ--GEYGLASICNGGGGASAMLIQKL 322
Cdd:PRK06690  320 ASGAMLVTRLFYQAKRedMKYGIATLGIGGGIGLALLFEKV 360
PRK06025 PRK06025
acetyl-CoA C-acetyltransferase;
39-322 1.88e-45

acetyl-CoA C-acetyltransferase;


Pssm-ID: 235675 [Multi-domain]  Cd Length: 417  Bit Score: 159.56  E-value: 1.88e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309  39 LKDVMVAGGMESMS----NVPYVMNRGSTPYGgvkledliVKDG---LTDVYNKIHMGSCAENTAKKLNIARNEQDAYAI 111
Cdd:PRK06025  110 MEDLVIAGGTEMMSytaaMAAEDMAAGKPPLG--------MGSGnlrLRALHPQSHQGVCGDAIATMEGITREALDALGL 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309 112 NSYTRSKAAWEAGKFGNEVIPVTvtvkgQPDVVVKED-EEYKRVDFSK--VPKLKTVFQK-------ENGTVT------- 174
Cdd:PRK06025  182 ESQRRAARAIKEGRFDKSLVPVY-----RDDGSVALDhEEFPRPQTTAegLAALKPAFTAiadypldDKGTTYrglinqk 256

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309 175 -----------AANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIA 243
Cdd:PRK06025  257 ypdleikhvhhAGNSSGVVDGAAALLLASKAYAEKHGLKPRARIVAMANMGDDPTLMLNAPVPAAKKVLAKAGLTKDDID 336

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309 244 MWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALKQ--GEYGLASICNGGGGASAMLIQK 321
Cdd:PRK06025  337 LWEINEAFAVVAEKFIRDLDLDRDKVNVNGGAIALGHPIGATGSILIGTVLDELERrgLKRGLVTMCAAGGMAPAIIIER 416


                  .
gi 1897358309 322 L 322
Cdd:PRK06025  417 V 417
PRK09268 PRK09268
acetyl-CoA C-acetyltransferase;
88-321 4.02e-38

acetyl-CoA C-acetyltransferase;


Pssm-ID: 236440 [Multi-domain]  Cd Length: 427  Bit Score: 140.04  E-value: 4.02e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309  88 MGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTVKGQ---PDVVVKedeeykrvdfsKVPKLKT 164
Cdd:PRK09268  178 MGEHAAITAKEWGISREAQDELAAASHQNLAAAYDRGFFDDLITPFLGLTRDNnlrPDSSLE-----------KLAKLKP 246

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309 165 VFQK-ENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFP----IAPVYAASMVLKDVGLKK 239
Cdd:PRK09268  247 VFGKgGRATMTAGNSTPLTDGASVVLLASEEWAAEHGLPVLAYLVDAETAAVDFVHGKegllMAPAYAVPRLLARNGLTL 326

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309 240 EDIAMWEVNEAFSLVVLANIKMLE-----------------IDPQKVNINGGAVSLGHPIGMSGARIVGHLTHAL--KQG 300
Cdd:PRK09268  327 QDFDFYEIHEAFASQVLATLKAWEdeeycrerlgldaplgsIDRSKLNVNGSSLAAGHPFAATGGRIVATLAKLLaeKGS 406

                         250       260
                  ....*....|....*....|.
gi 1897358309 301 EYGLASICNGGGGASAMLIQK 321
Cdd:PRK09268  407 GRGLISICAAGGQGVTAILER 427
nondecarbox_cond_enzymes cd00826
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ...
 88-320 9.42e-32

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: 122.22  E-value: 9.42e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309  88 MGSCAENTAKKLNI--------ARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVtvKGQPDVVVKEDEEYKR----VD 155
Cdd:cd00826   115 METSAENNAKEKHIdvlinkygMRACPDAFALAGQAGAEAAEKDGRFKDEFAKFGV--KGRKGDIHSDADEYIQfgdeAS 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309 156 FSKVPKLKTVFQKEnGTVTAANASTLNDGAAALVLMTADAA-------KRLNVTPLARIVAFADAAVEPIDFPIA----P 224
Cdd:cd00826   193 LDEIAKLRPAFDKE-DFLTAGNACGLNDGAAAAILMSEAEAqkhglqsKAREIQALEMITDMASTFEDKKVIKMVggdgP 271

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309 225 VYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQK------------------VNINGGAVSLGHPIGMSG 286
Cdd:cd00826   272 IEAARKALEKAGLGIGDLDLIEAHDAFAANACATNEALGLCPEGqggalvdrgdntyggksiINPNGGAIAIGHPIGASG 351

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1897358309 287 ARIVGHLTHALKQGEY-------GLASICNGGGGASAMLIQ 320
Cdd:cd00826   352 AAICAELCFELKGEAGkrqgagaGLALLCIGGGGGAAMCIE 392
cond_enzymes cd00327
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ...
 175-319 5.86e-14

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


Pssm-ID: 238201 [Multi-domain]  Cd Length: 254  Bit Score: 70.55  E-value: 5.86e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309 175 AANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPI----APVYAASMVLKDVGLKKEDIAMWEVNEA 250
Cdd:cd00327    94 GSEEFVFGDGAAAAVVESEEHALRRGAHPQAEIVSTAATFDGASMVPAvsgeGLARAARKALEGAGLTPSDIDYVEAHGT 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309 251 FSLVVLANIKMLEIDPQKV---NINGGAVSLGHPIGMSGARIVGHLTHALKQGEY---------GLASICNGGGGASAML 318
Cdd:cd00327   174 GTPIGDAVELALGLDPDGVrspAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIpptpreprtVLLLGFGLGGTNAAVV 253


                  .
gi 1897358309 319 I 319
Cdd:cd00327   254 L 254
SCP-x_thiolase cd00829
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ...
 182-316 1.68e-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: 64.21  E-value: 1.68e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309 182 NDGAAALVLMTADAAKRLNVTPlARIVAFADA-------AVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLV 254
Cdd:cd00829   205 SDGAAAVVLASEERARELTDRP-VWILGVGAAsdtpslsERDDFLSLDAARLAARRAYKMAGITPDDIDVAELYDCFTIA 283

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309 255 VLANIKML---------------EIDPQ---KVNINGGAVSLGHPIGMSGARIVGHLTHALKqGEYG--------LASIC 308
Cdd:cd00829   284 ELLALEDLgfcekgeggklvregDTAIGgdlPVNTSGGLLSKGHPLGATGLAQAVEAVRQLR-GEAGarqvpgarVGLAH 362


                  ....*...
gi 1897358309 309 NGGGGASA 316
Cdd:cd00829   363 NIGGTGSA 370
PRK06157 PRK06157
acetyl-CoA acetyltransferase; Validated
 179-290 1.41e-07

acetyl-CoA acetyltransferase; Validated


Pssm-ID: 180433 [Multi-domain]  Cd Length: 398  Bit Score: 52.34  E-value: 1.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309 179 STLNDGAAALVLMTADAAKRLNVTPLARIVAFAdAAVEP--------IDFPIAP--VYAASMVLKDVGLK--KEDIAMWE 246
Cdd:PRK06157  214 CGVSDGAAAAIVTTPEIARALGKKDPVYVKALQ-LAVSNgwelqyngWDGSYFPttRIAARKAYREAGITdpREELSMAE 292

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1897358309 247 VNEAFSLVVLANIKMLEIDPQ------------------KVNINGGAVSLGHPIGMSGARIV 290
Cdd:PRK06157  293 VHDCFSITELVTMEDLGLSERgqawrdvldgffdadgglPCQIDGGLKCFGHPIGASGLRML 354
PTZ00455 PTZ00455
3-ketoacyl-CoA thiolase; Provisional
 179-307 4.04e-04

3-ketoacyl-CoA thiolase; Provisional


Pssm-ID: 240424 [Multi-domain]  Cd Length: 438  Bit Score: 41.80  E-value: 4.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897358309 179 STLNDGAAALVLMTADAAKRLNVTP----LARIVAFADAAVEPIDFP------IAPVYAASMVLKDVGLKKEDIAMWEVN 248
Cdd:PTZ00455  256 SQVSDGGAGLVLASEEGLQKMGLSPndsrLVEIKSLACASGNLYEDPpdatrmFTSRAAAQKALSMAGVKPSDLQVAEVH 335

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1897358309 249 EAFSLVVLANIKMLEI-DPQK-----------------VNINGGAVSLGHPIGMSGARIVGHLTHALKQ--GEYGLASI 307
Cdd:PTZ00455  336 DCFTIAELLMYEALGIaEYGHakdlirngatalegripVNTGGGLLSFGHPVGATGVKQIMEVYRQMKGqcGEYQMKNI 414
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
 181-242 1.85e-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: 39.83  E-value: 1.85e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1897358309 181 LNDGAAALVLMTADAAKRLNVTPLARIVAFA---DAA--VEPIDFPIAPVYAASMVLKDVGLKKEDI 242
Cdd:cd00834   229 LGEGAGVLVLESLEHAKARGAKIYAEILGYGassDAYhiTAPDPDGEGAARAMRAALADAGLSPEDI 295
FabB COG0304
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...
 184-242 5.40e-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: 38.15  E-value: 5.40e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1897358309 184 GAAALVLMTADAAKRLNVTPLARIVAFA---DAA--VEPIDFPIAPVYAASMVLKDVGLKKEDI 242
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.
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