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Conserved domains on  [gi|296480314|tpg|DAA22429|]
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TPA: acetyl-CoA acetyltransferase, mitochondrial precursor [Bos taurus]

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 ...
38-421 0e+00

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


:

Pssm-ID: 238383 [Multi-domain]  Cd Length: 386  Bit Score: 547.85  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314  38 VIVSAIRTPIGSFLGSLSSLPATKLGSIAIQGAIEKAGIPKEEVKEAYMGNVLQGGEGQAPTRQAVLGAGLPISTPCTTI 117
Cdd:cd00751    1 VIVSAVRTPIGRFGGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGEGQNPARQAALLAGLPESVPATTV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 118 NKVCASGMKAIMMASQNLMCGHQDVMVAGGMESMSNVPYVMNRGATPY-GGVKLEDLIVKDGLTDVYNKIHMGNCAENTA 196
Cdd:cd00751   81 NRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGrLGLNTLDGMLDDGLTDPFTGLSMGITAENVA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 197 KKLNITREEQDTYALNSYTRSKAAWEAGRFGNEVVPVTITVKGKPdVVVKEDEEYKR-VDFSKIPKLKTVFqRENGTVTA 275
Cdd:cd00751  161 EKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEVPGRKGP-VVVDRDEGPRPdTTLEKLAKLKPAF-KKDGTVTA 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 276 ANASTLNDGAAAVVLMTADAAKRLNVKPLARIAAFADAAVEPIDFPLAPAYAVPKVLKDAGLKKEDITMWEVNEAFSVVV 355
Cdd:cd00751  239 GNASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDIDLIEINEAFAAQA 318
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 296480314 356 LANIKMLEMDPQKVNINGGAVSLGHPIGMSGARIVVHLAHALKQ--GEYGLASICNGGGGASAMLIQK 421
Cdd:cd00751  319 LACLKELGLDPEKVNVNGGAIALGHPLGASGARIVVTLLHELKRrgGRYGLATMCIGGGQGAAMVIER 386
 
Name Accession Description Interval E-value
thiolase cd00751
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ...
38-421 0e+00

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


Pssm-ID: 238383 [Multi-domain]  Cd Length: 386  Bit Score: 547.85  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314  38 VIVSAIRTPIGSFLGSLSSLPATKLGSIAIQGAIEKAGIPKEEVKEAYMGNVLQGGEGQAPTRQAVLGAGLPISTPCTTI 117
Cdd:cd00751    1 VIVSAVRTPIGRFGGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGEGQNPARQAALLAGLPESVPATTV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 118 NKVCASGMKAIMMASQNLMCGHQDVMVAGGMESMSNVPYVMNRGATPY-GGVKLEDLIVKDGLTDVYNKIHMGNCAENTA 196
Cdd:cd00751   81 NRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGrLGLNTLDGMLDDGLTDPFTGLSMGITAENVA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 197 KKLNITREEQDTYALNSYTRSKAAWEAGRFGNEVVPVTITVKGKPdVVVKEDEEYKR-VDFSKIPKLKTVFqRENGTVTA 275
Cdd:cd00751  161 EKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEVPGRKGP-VVVDRDEGPRPdTTLEKLAKLKPAF-KKDGTVTA 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 276 ANASTLNDGAAAVVLMTADAAKRLNVKPLARIAAFADAAVEPIDFPLAPAYAVPKVLKDAGLKKEDITMWEVNEAFSVVV 355
Cdd:cd00751  239 GNASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDIDLIEINEAFAAQA 318
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 296480314 356 LANIKMLEMDPQKVNINGGAVSLGHPIGMSGARIVVHLAHALKQ--GEYGLASICNGGGGASAMLIQK 421
Cdd:cd00751  319 LACLKELGLDPEKVNVNGGAIALGHPLGASGARIVVTLLHELKRrgGRYGLATMCIGGGQGAAMVIER 386
PaaJ COG0183
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ...
35-422 0e+00

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


Pssm-ID: 439953 [Multi-domain]  Cd Length: 391  Bit Score: 523.86  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314  35 NEVVIVSAIRTPIGSFLGSLSSLPATKLGSIAIQGAIEKAGIPKEEVKEAYMGNVLQGGEGQAPTRQAVLGAGLPISTPC 114
Cdd:COG0183    2 REVVIVDAVRTPFGRFGGALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQAGQGQNPARQAALLAGLPESVPA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 115 TTINKVCASGMKAIMMASQNLMCGHQDVMVAGGMESMSNVPYVMNRGATPYGG-VKLEDLIVKDGLTDVYNKIHMGNCAE 193
Cdd:COG0183   82 VTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMLLPKARWGYRMnAKLVDPMINPGLTDPYTGLSMGETAE 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 194 NTAKKLNITREEQDTYALNSYTRSKAAWEAGRFGNEVVPVTITVKgKPDVVVKEDEEYKR-VDFSKIPKLKTVFqRENGT 272
Cdd:COG0183  162 NVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVEVPDR-KGEVVVDRDEGPRPdTTLEKLAKLKPAF-KKDGT 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 273 VTAANASTLNDGAAAVVLMTADAAKRLNVKPLARIAAFADAAVEPIDFPLAPAYAVPKVLKDAGLKKEDITMWEVNEAFS 352
Cdd:COG0183  240 VTAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIGPVPATRKALARAGLTLDDIDLIEINEAFA 319
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 296480314 353 VVVLANIKMLEMDPQKVNINGGAVSLGHPIGMSGARIVVHLAHALKQ--GEYGLASICNGGGGASAMLIQKL 422
Cdd:COG0183  320 AQVLAVLRELGLDPDKVNVNGGAIALGHPLGASGARILVTLLHELERrgGRYGLATMCIGGGQGIALIIERV 391
PLN02644 PLN02644
acetyl-CoA C-acetyltransferase
36-422 0e+00

acetyl-CoA C-acetyltransferase


Pssm-ID: 215347 [Multi-domain]  Cd Length: 394  Bit Score: 521.96  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314  36 EVVIVSAIRTPIGSFLGSLSSLPATKLGSIAIQGAIEKAGIPKEEVKEAYMGNVLQGGEGQAPTRQAVLGAGLPISTPCT 115
Cdd:PLN02644   2 DVCIVGVARTPIGGFLGSLSSLSATELGSIAIQAALERAGVDPALVQEVFFGNVLSANLGQAPARQAALGAGLPPSTICT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 116 TINKVCASGMKAIMMASQNLMCGHQDVMVAGGMESMSNVPYVM--NRGATPYGGVKLEDLIVKDGLTDVYNKIHMGNCAE 193
Cdd:PLN02644  82 TVNKVCASGMKAVMLAAQSIQLGINDVVVAGGMESMSNAPKYLpeARKGSRLGHDTVVDGMLKDGLWDVYNDFGMGVCAE 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 194 NTAKKLNITREEQDTYALNSYTRSKAAWEAGRFGNEVVPVTITV-KGKPDVVVKEDEEYKRVDFSKIPKLKTVFQRENGT 272
Cdd:PLN02644 162 LCADQYSISREEQDAYAIQSYERAIAAQEAGAFAWEIVPVEVPGgRGRPSVIVDKDEGLGKFDPAKLRKLRPSFKEDGGS 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 273 VTAANASTLNDGAAAVVLMTADAAKRLNVKPLARIAAFADAAVEPIDFPLAPAYAVPKVLKDAGLKKEDITMWEVNEAFS 352
Cdd:PLN02644 242 VTAGNASSISDGAAALVLVSGEKALELGLQVIAKIRGYADAAQAPELFTTAPALAIPKALKHAGLEASQVDYYEINEAFS 321
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 296480314 353 VVVLANIKMLEMDPQKVNINGGAVSLGHPIGMSGARIVVHLAHALKQ--GEYGLASICNGGGGASAMLIQKL 422
Cdd:PLN02644 322 VVALANQKLLGLDPEKVNVHGGAVSLGHPIGCSGARILVTLLGVLRSknGKYGVAGICNGGGGASAIVVELM 393
AcCoA-C-Actrans TIGR01930
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ...
39-420 7.38e-166

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: 470.94  E-value: 7.38e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314   39 IVSAIRTPIGSFLGSLSSLPATKLGSIAIQGAIEKAGIPKEEVKEAYMGNVLQGGEGQAPTRQAVLGAGLPISTPCTTIN 118
Cdd:TIGR01930   1 IVAAARTPIGKFGGSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLQAGEQQNIARQAALLAGLPESVPAYTVN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314  119 KVCASGMKAIMMASQNLMCGHQDVMVAGGMESMSNVPYVMNRGATP---YGGVKLEDLIVKDgLTDVYNKIHMGNCAENT 195
Cdd:TIGR01930  81 RQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGVPRSLRWgvkPGNAELEDARLKD-LTDANTGLPMGVTAENL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314  196 AKKLNITREEQDTYALNSYTRSKAAWEAGRFGNEVVPVTITVKGKPDVVVKEDEEYKRVDFSKIPKLKTVFqRENGTVTA 275
Cdd:TIGR01930 160 AKKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVTVKGRKGPVTVSSDEGIRPNTTLEKLAKLKPAF-DPDGTVTA 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314  276 ANASTLNDGAAAVVLMTADAAKRLNVKPLARIAAFADAAVEPIDFPLAPAYAVPKVLKDAGLKKEDITMWEVNEAFSVVV 355
Cdd:TIGR01930 239 GNSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALKKAGLSISDIDLFEINEAFAAQV 318
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 296480314  356 LANIKMLEMDPQKVNINGGAVSLGHPIGMSGARIVVHLAHALKQ--GEYGLASICNGGGGASAMLIQ 420
Cdd:TIGR01930 319 LACIKELGLDLEKVNVNGGAIALGHPLGASGARIVTTLLHELKRrgGRYGLATMCIGGGQGAAVILE 385
Thiolase_N pfam00108
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
37-294 2.88e-117

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: 342.75  E-value: 2.88e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314   37 VVIVSAIRTPIGSFLGSLSSLPATKLGSIAIQGAIEKAGIPKEEVKEAYMGNVLQGGEGQAPTRQAVLGAGLPISTPCTT 116
Cdd:pfam00108   1 VVIVSAARTPFGSFGGSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQAGEGQNPARQAALKAGIPDSAPAVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314  117 INKVCASGMKAIMMASQNLMCGHQDVMVAGGMESMSNVPYVMN---RGATPYGGVKLEDLIVKDGLTDVYNKIHMGNCAE 193
Cdd:pfam00108  81 INKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALPtdaRSGLKHGDEKKHDLLIPDGLTDAFNGYHMGLTAE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314  194 NTAKKLNITREEQDTYALNSYTRSKAAWEAGRFGNEVVPVTITVKGKPDVVVKEDEEYKRVDFSKIPKLKTVFQREnGTV 273
Cdd:pfam00108 161 NVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDEIVPVTVKGRKGKPTVDKDEGIRPPTTAEPLAKLKPAFDKE-GTV 239
                         250       260
                  ....*....|....*....|.
gi 296480314  274 TAANASTLNDGAAAVVLMTAD 294
Cdd:pfam00108 240 TAGNASPINDGAAAVLLMSES 260
 
Name Accession Description Interval E-value
thiolase cd00751
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ...
38-421 0e+00

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


Pssm-ID: 238383 [Multi-domain]  Cd Length: 386  Bit Score: 547.85  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314  38 VIVSAIRTPIGSFLGSLSSLPATKLGSIAIQGAIEKAGIPKEEVKEAYMGNVLQGGEGQAPTRQAVLGAGLPISTPCTTI 117
Cdd:cd00751    1 VIVSAVRTPIGRFGGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGEGQNPARQAALLAGLPESVPATTV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 118 NKVCASGMKAIMMASQNLMCGHQDVMVAGGMESMSNVPYVMNRGATPY-GGVKLEDLIVKDGLTDVYNKIHMGNCAENTA 196
Cdd:cd00751   81 NRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGrLGLNTLDGMLDDGLTDPFTGLSMGITAENVA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 197 KKLNITREEQDTYALNSYTRSKAAWEAGRFGNEVVPVTITVKGKPdVVVKEDEEYKR-VDFSKIPKLKTVFqRENGTVTA 275
Cdd:cd00751  161 EKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEVPGRKGP-VVVDRDEGPRPdTTLEKLAKLKPAF-KKDGTVTA 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 276 ANASTLNDGAAAVVLMTADAAKRLNVKPLARIAAFADAAVEPIDFPLAPAYAVPKVLKDAGLKKEDITMWEVNEAFSVVV 355
Cdd:cd00751  239 GNASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDIDLIEINEAFAAQA 318
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 296480314 356 LANIKMLEMDPQKVNINGGAVSLGHPIGMSGARIVVHLAHALKQ--GEYGLASICNGGGGASAMLIQK 421
Cdd:cd00751  319 LACLKELGLDPEKVNVNGGAIALGHPLGASGARIVVTLLHELKRrgGRYGLATMCIGGGQGAAMVIER 386
PaaJ COG0183
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ...
35-422 0e+00

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


Pssm-ID: 439953 [Multi-domain]  Cd Length: 391  Bit Score: 523.86  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314  35 NEVVIVSAIRTPIGSFLGSLSSLPATKLGSIAIQGAIEKAGIPKEEVKEAYMGNVLQGGEGQAPTRQAVLGAGLPISTPC 114
Cdd:COG0183    2 REVVIVDAVRTPFGRFGGALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQAGQGQNPARQAALLAGLPESVPA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 115 TTINKVCASGMKAIMMASQNLMCGHQDVMVAGGMESMSNVPYVMNRGATPYGG-VKLEDLIVKDGLTDVYNKIHMGNCAE 193
Cdd:COG0183   82 VTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMLLPKARWGYRMnAKLVDPMINPGLTDPYTGLSMGETAE 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 194 NTAKKLNITREEQDTYALNSYTRSKAAWEAGRFGNEVVPVTITVKgKPDVVVKEDEEYKR-VDFSKIPKLKTVFqRENGT 272
Cdd:COG0183  162 NVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVEVPDR-KGEVVVDRDEGPRPdTTLEKLAKLKPAF-KKDGT 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 273 VTAANASTLNDGAAAVVLMTADAAKRLNVKPLARIAAFADAAVEPIDFPLAPAYAVPKVLKDAGLKKEDITMWEVNEAFS 352
Cdd:COG0183  240 VTAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIGPVPATRKALARAGLTLDDIDLIEINEAFA 319
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 296480314 353 VVVLANIKMLEMDPQKVNINGGAVSLGHPIGMSGARIVVHLAHALKQ--GEYGLASICNGGGGASAMLIQKL 422
Cdd:COG0183  320 AQVLAVLRELGLDPDKVNVNGGAIALGHPLGASGARILVTLLHELERrgGRYGLATMCIGGGQGIALIIERV 391
PLN02644 PLN02644
acetyl-CoA C-acetyltransferase
36-422 0e+00

acetyl-CoA C-acetyltransferase


Pssm-ID: 215347 [Multi-domain]  Cd Length: 394  Bit Score: 521.96  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314  36 EVVIVSAIRTPIGSFLGSLSSLPATKLGSIAIQGAIEKAGIPKEEVKEAYMGNVLQGGEGQAPTRQAVLGAGLPISTPCT 115
Cdd:PLN02644   2 DVCIVGVARTPIGGFLGSLSSLSATELGSIAIQAALERAGVDPALVQEVFFGNVLSANLGQAPARQAALGAGLPPSTICT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 116 TINKVCASGMKAIMMASQNLMCGHQDVMVAGGMESMSNVPYVM--NRGATPYGGVKLEDLIVKDGLTDVYNKIHMGNCAE 193
Cdd:PLN02644  82 TVNKVCASGMKAVMLAAQSIQLGINDVVVAGGMESMSNAPKYLpeARKGSRLGHDTVVDGMLKDGLWDVYNDFGMGVCAE 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 194 NTAKKLNITREEQDTYALNSYTRSKAAWEAGRFGNEVVPVTITV-KGKPDVVVKEDEEYKRVDFSKIPKLKTVFQRENGT 272
Cdd:PLN02644 162 LCADQYSISREEQDAYAIQSYERAIAAQEAGAFAWEIVPVEVPGgRGRPSVIVDKDEGLGKFDPAKLRKLRPSFKEDGGS 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 273 VTAANASTLNDGAAAVVLMTADAAKRLNVKPLARIAAFADAAVEPIDFPLAPAYAVPKVLKDAGLKKEDITMWEVNEAFS 352
Cdd:PLN02644 242 VTAGNASSISDGAAALVLVSGEKALELGLQVIAKIRGYADAAQAPELFTTAPALAIPKALKHAGLEASQVDYYEINEAFS 321
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 296480314 353 VVVLANIKMLEMDPQKVNINGGAVSLGHPIGMSGARIVVHLAHALKQ--GEYGLASICNGGGGASAMLIQKL 422
Cdd:PLN02644 322 VVALANQKLLGLDPEKVNVHGGAVSLGHPIGCSGARILVTLLGVLRSknGKYGVAGICNGGGGASAIVVELM 393
PRK05790 PRK05790
putative acyltransferase; Provisional
35-419 1.54e-170

putative acyltransferase; Provisional


Pssm-ID: 180261 [Multi-domain]  Cd Length: 393  Bit Score: 483.11  E-value: 1.54e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314  35 NEVVIVSAIRTPIGSFLGSLSSLPATKLGSIAIQGAIEKAGIPKEEVKEAYMGNVLQGGEGQAPTRQAVLGAGLPISTPC 114
Cdd:PRK05790   2 KDVVIVSAARTPIGKFGGALKDVSAVELGAIVIKAALERAGVPPEQVDEVIMGQVLQAGAGQNPARQAALKAGLPVEVPA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 115 TTINKVCASGMKAIMMASQNLMCGHQDVMVAGGMESMSNVPYVMN--RGATPYGGVKLEDLIVKDGLTDVYNKIHMGNCA 192
Cdd:PRK05790  82 LTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQESMSQAPHVLPgsRWGQKMGDVELVDTMIHDGLTDAFNGYHMGITA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 193 ENTAKKLNITREEQDTYALNSYTRSKAAWEAGRFGNEVVPVTITVKGKPDVVVKEDeEYKRVDFS--KIPKLKTVFqREN 270
Cdd:PRK05790 162 ENLAEQYGITREEQDEFALASQQKAEAAIKAGRFKDEIVPVTIKQRKGDPVVVDTD-EHPRPDTTaeSLAKLRPAF-DKD 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 271 GTVTAANASTLNDGAAAVVLMTADAAKRLNVKPLARIAAFADAAVEPIDFPLAPAYAVPKVLKDAGLKKEDITMWEVNEA 350
Cdd:PRK05790 240 GTVTAGNASGINDGAAAVVVMSEAKAKELGLTPLARIVSYAVAGVDPAIMGIGPVPAIRKALEKAGWSLADLDLIEINEA 319
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 296480314 351 FSVVVLANIKMLEMDPQKVNINGGAVSLGHPIGMSGARIVVHLAHALK--QGEYGLASICNGGGGASAMLI 419
Cdd:PRK05790 320 FAAQALAVEKELGLDPEKVNVNGGAIALGHPIGASGARILVTLLHEMKrrGAKKGLATLCIGGGQGVALIV 390
AcCoA-C-Actrans TIGR01930
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ...
39-420 7.38e-166

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: 470.94  E-value: 7.38e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314   39 IVSAIRTPIGSFLGSLSSLPATKLGSIAIQGAIEKAGIPKEEVKEAYMGNVLQGGEGQAPTRQAVLGAGLPISTPCTTIN 118
Cdd:TIGR01930   1 IVAAARTPIGKFGGSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLQAGEQQNIARQAALLAGLPESVPAYTVN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314  119 KVCASGMKAIMMASQNLMCGHQDVMVAGGMESMSNVPYVMNRGATP---YGGVKLEDLIVKDgLTDVYNKIHMGNCAENT 195
Cdd:TIGR01930  81 RQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGVPRSLRWgvkPGNAELEDARLKD-LTDANTGLPMGVTAENL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314  196 AKKLNITREEQDTYALNSYTRSKAAWEAGRFGNEVVPVTITVKGKPDVVVKEDEEYKRVDFSKIPKLKTVFqRENGTVTA 275
Cdd:TIGR01930 160 AKKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVTVKGRKGPVTVSSDEGIRPNTTLEKLAKLKPAF-DPDGTVTA 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314  276 ANASTLNDGAAAVVLMTADAAKRLNVKPLARIAAFADAAVEPIDFPLAPAYAVPKVLKDAGLKKEDITMWEVNEAFSVVV 355
Cdd:TIGR01930 239 GNSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALKKAGLSISDIDLFEINEAFAAQV 318
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 296480314  356 LANIKMLEMDPQKVNINGGAVSLGHPIGMSGARIVVHLAHALKQ--GEYGLASICNGGGGASAMLIQ 420
Cdd:TIGR01930 319 LACIKELGLDLEKVNVNGGAIALGHPLGASGARIVTTLLHELKRrgGRYGLATMCIGGGQGAAVILE 385
PRK08235 PRK08235
acetyl-CoA C-acetyltransferase;
36-420 3.50e-153

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181311 [Multi-domain]  Cd Length: 393  Bit Score: 439.15  E-value: 3.50e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314  36 EVVIVSAIRTPIGSFLGSLSSLPATKLGSIAIQGAIEKAGIPKEEVKEAYMGNVLQGGEGQAPTRQAVLGAGLPISTPCT 115
Cdd:PRK08235   3 KTVIVSAARTPFGKFGGSLKDVKATELGGIAIKEALERANVSAEDVEEVIMGTVLQGGQGQIPSRQAARAAGIPWEVQTE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 116 TINKVCASGMKAIMMASQNLMCGHQDVMVAGGMESMSNVPYVMNRGATPY--GGVKLEDLIVKDGLTDVYNKIHMGNCAE 193
Cdd:PRK08235  83 TVNKVCASGLRAVTLADQIIRAGDASVIVAGGMESMSNAPYILPGARWGYrmGDNEVIDLMVADGLTCAFSGVHMGVYGG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 194 NTAKKLNITREEQDTYALNSYTRSKAAWEAGRFGNEVVPVTIT-VKGKPDVVVKEDEEYKRVDFSKIPKLKTVFQREnGT 272
Cdd:PRK08235 163 EVAKELGISREAQDEWAYRSHQRAVSAHEEGRFEEEIVPVTIPqRKGDPIVVAKDEAPRKDTTIEKLAKLKPVFDKT-GT 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 273 VTAANASTLNDGAAAVVLMTADAAKRLNVKPLARIAAFADAAVEPIDFPLAPAYAVPKVLKDAGLKKEDITMWEVNEAFS 352
Cdd:PRK08235 242 ITAGNAPGVNDGAAALVLMSEDRAKQEGRKPLATILAHTAIAVEAKDFPRTPGYAINALLEKTGKTVEDIDLFEINEAFA 321
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 353 VVVLANIKMLEMDPQKVNINGGAVSLGHPIGMSGARIVVHLAHALKQ--GEYGLASICNGGGGASAMLIQ 420
Cdd:PRK08235 322 AVALASTEIAGIDPEKVNVNGGAVALGHPIGASGARIIVTLIHELKRrgGGIGIAAICSGGGQGDAVLIE 391
PRK06954 PRK06954
acetyl-CoA C-acetyltransferase;
35-420 1.12e-124

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180775 [Multi-domain]  Cd Length: 397  Bit Score: 366.52  E-value: 1.12e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314  35 NEVVIVSAIRTPIGSFLGSLSSLPATKLGSIAIQGAIEKAGIPKEEVKEAYMGNVLQGGEGQAPTRQAVLGAGLPISTPC 114
Cdd:PRK06954   7 DPIVIASAARTPMAAFQGEFASLTAPQLGAAAIAAAVERAGLKPEQIDEVVMGCVLPAGQGQAPARQAALGAGLPLSVGC 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 115 TTINKVCASGMKAIMMASQNLMCGHQDVMVAGGMESMSNVPYVM--NRGATPYGGVKLEDLIVKDGLTDVYNKIH-MGNC 191
Cdd:PRK06954  87 TTVNKMCGSGMRAAMFAHDMLVAGSVDVIVAGGMESMTNAPYLLpkARGGMRMGHGQVLDHMFLDGLEDAYDKGRlMGTF 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 192 AENTAKKLNITREEQDTYALNSYTRSKAAWEAGRFGNEVVPVTITVKgKPDVVVKEDEEYKRVDFSKIPKLKTVFQReNG 271
Cdd:PRK06954 167 AEECAGEYGFTREAQDAFAIESLARAKRANEDGSFAWEIAPVTVAGK-KGDTVIDRDEQPFKANPEKIPTLKPAFSK-TG 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 272 TVTAANASTLNDGAAAVVLMTADAAKRLNVKPLARIAAFADAAVEPIDFPLAPAYAVPKVLKDAGLKKEDITMWEVNEAF 351
Cdd:PRK06954 245 TVTAANSSSISDGAAALVMMRASTAKRLGLAPLARVVGHSTFAQAPSKFTTAPVGAIRKLFEKNGWRAAEVDLFEINEAF 324
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 296480314 352 SVVVLANIKMLEMDPQKVNINGGAVSLGHPIGMSGARIVVHLAHALKQ--GEYGLASICNGGGGASAMLIQ 420
Cdd:PRK06954 325 AVVTMAAMKEHGLPHEKVNVNGGACALGHPIGASGARILVTLIGALRArgGKRGVASLCIGGGEATAMGIE 395
PRK09051 PRK09051
beta-ketothiolase BktB;
35-422 6.62e-118

beta-ketothiolase BktB;


Pssm-ID: 181625 [Multi-domain]  Cd Length: 394  Bit Score: 349.26  E-value: 6.62e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314  35 NEVVIVSAIRTPIGSFLGSLSSLPATKLGSIAIQGAIEKAGIPKEEVKEAYMGNVLqggegqaPT--------RQAVLGA 106
Cdd:PRK09051   3 REVVVVSGVRTAIGTFGGSLKDVAPTDLGATVVREALARAGVDPDQVGHVVFGHVI-------PTeprdmylsRVAAINA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 107 GLPISTPCTTINKVCASGMKAIMMASQNLMCGHQDVMVAGGMESMSNVPYVM--NRGATPYGGVKLEDLIVKdGLTDVYN 184
Cdd:PRK09051  76 GVPQETPAFNVNRLCGSGLQAIVSAAQAILLGDADVAIGGGAESMSRAPYLLpaARWGARMGDAKLVDMMVG-ALHDPFG 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 185 KIHMGNCAENTAKKLNITREEQDTYALNSYTRSKAAWEAGRFGNEVVPVTITVKgKPDVVVKEDEEYKR-VDFSKIPKLK 263
Cdd:PRK09051 155 TIHMGVTAENVAAKYGISREAQDALALESHRRAAAAIAAGYFKDQIVPVEIKTR-KGEVVFDTDEHVRAdTTLEDLAKLK 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 264 TVFQRENGTVTAANASTLNDGAAAVVLMTADAAKRLNVKPLARIAAFADAAVEPIDFPLAPAYAVPKVLKDAGLKKEDIT 343
Cdd:PRK09051 234 PVFKKENGTVTAGNASGINDGAAAVVLAEADAAEARGLKPLARLVGYAHAGVDPEYMGIGPVPATQKALERAGLTVADLD 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 344 MWEVNEAFSVVVLANIKMLEMDPQKVNINGGAVSLGHPIGMSGARIVVHLAHALK--QGEYGLASICNGGGGASAMLIQK 421
Cdd:PRK09051 314 VIEANEAFAAQACAVTRELGLDPAKVNPNGSGISLGHPVGATGAIITVKALYELQriGGRYALVTMCIGGGQGIAAIFER 393

                 .
gi 296480314 422 L 422
Cdd:PRK09051 394 L 394
Thiolase_N pfam00108
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
37-294 2.88e-117

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: 342.75  E-value: 2.88e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314   37 VVIVSAIRTPIGSFLGSLSSLPATKLGSIAIQGAIEKAGIPKEEVKEAYMGNVLQGGEGQAPTRQAVLGAGLPISTPCTT 116
Cdd:pfam00108   1 VVIVSAARTPFGSFGGSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQAGEGQNPARQAALKAGIPDSAPAVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314  117 INKVCASGMKAIMMASQNLMCGHQDVMVAGGMESMSNVPYVMN---RGATPYGGVKLEDLIVKDGLTDVYNKIHMGNCAE 193
Cdd:pfam00108  81 INKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALPtdaRSGLKHGDEKKHDLLIPDGLTDAFNGYHMGLTAE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314  194 NTAKKLNITREEQDTYALNSYTRSKAAWEAGRFGNEVVPVTITVKGKPDVVVKEDEEYKRVDFSKIPKLKTVFQREnGTV 273
Cdd:pfam00108 161 NVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDEIVPVTVKGRKGKPTVDKDEGIRPPTTAEPLAKLKPAFDKE-GTV 239
                         250       260
                  ....*....|....*....|.
gi 296480314  274 TAANASTLNDGAAAVVLMTAD 294
Cdd:pfam00108 240 TAGNASPINDGAAAVLLMSES 260
PRK05656 PRK05656
acetyl-CoA C-acetyltransferase;
34-421 1.99e-110

acetyl-CoA C-acetyltransferase;


Pssm-ID: 168156  Cd Length: 393  Bit Score: 330.31  E-value: 1.99e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314  34 LNEVVIVSAIRTPIGSFLGSLSSLPATKLGSIAIQGAIEKAGIPKEEVKEAYMGNVLQGGEGQAPTRQAVLGAGLPISTP 113
Cdd:PRK05656   1 MQDVVIVAATRTAIGSFQGSLANIPAVELGAAVIRRLLEQTGLDPAQVDEVILGQVLTAGAGQNPARQAAIKAGLPHSVP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 114 CTTINKVCASGMKAIMMASQNLMCGHQDVMVAGGMESMSNVPYVM--NRGATPYGGVKLEDLIVKDGLTDVYNKIHMGNC 191
Cdd:PRK05656  81 AMTLNKVCGSGLKALHLAAQAIRCGDAEVIIAGGQENMSLAPYVLpgARTGLRMGHAQLVDSMITDGLWDAFNDYHMGIT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 192 AENTAKKLNITREEQDTYALNSYTRSKAAWEAGRFGNEVVPVTI-TVKGKPDVVVKEDEEYKRVDFSKIPKLKTVFqREN 270
Cdd:PRK05656 161 AENLVEKYGISREAQDAFAAASQQKAVAAIEAGRFDDEITPILIpQRKGEPLAFATDEQPRAGTTAESLAKLKPAF-KKD 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 271 GTVTAANASTLNDGAAAVVLMTADAAKRLNVKPLARIAAFADAAVEPIDFPLAPAYAVPKVLKDAGLKKEDITMWEVNEA 350
Cdd:PRK05656 240 GSVTAGNASSLNDGAAAVLLMSAAKAKALGLPVLAKIAAYANAGVDPAIMGIGPVSATRRCLDKAGWSLAELDLIEANEA 319
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 296480314 351 FSVVVLANIKMLEMDPQKVNINGGAVSLGHPIGMSGARIVVHLAHAL--KQGEYGLASICNGGGGASAMLIQK 421
Cdd:PRK05656 320 FAAQSLAVGKELGWDAAKVNVNGGAIALGHPIGASGCRVLVTLLHEMirRDAKKGLATLCIGGGQGVALAIER 392
PRK06366 PRK06366
acetyl-CoA C-acetyltransferase;
34-420 2.55e-100

acetyl-CoA C-acetyltransferase;


Pssm-ID: 102340 [Multi-domain]  Cd Length: 388  Bit Score: 304.24  E-value: 2.55e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314  34 LNEVVIVSAIRTPIGSFLGSLSSLPATKLGSIAIQGAIEKAGIPKEEVKEAYMGNVLQGGEGQAPTRQAVLGAGLPISTP 113
Cdd:PRK06366   1 MKDVYIVSAKRTAIGKFGRSFSKIKAPQLGGAAIKAVIDDAKLDPALVQEVIMGNVIQAGVGQNPAGQAAYHAGLPFGVT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 114 CTTINKVCASGMKAIMMASQNLMCGHQDVMVAGGMESMSNVPYVMNRGAT--P----YGGVKLEDLIVKDGLTDVYNKIH 187
Cdd:PRK06366  81 KYTVNVVCASGMLAVESAAREIMLGERDLVIAGGMENMSNAPFLLPSDLRwgPkhllHKNYKIDDAMLVDGLIDAFYFEH 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 188 MGNCAENTAKKLNITREEQDTYALNSYTRSKAAWEAGRFGNEVVPVTitvkgkpdvVVKEDEEYKRVDFSKIPKLKTVFQ 267
Cdd:PRK06366 161 MGVSAERTARKYGITREMADEYSVQSYERAIRATESGEFRNEIVPFN---------DLDRDEGIRKTTMEDLAKLPPAFD 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 268 ReNGTVTAANASTLNDGAAAVVLMTADAAKRLNVKPLARIAAFADAAVEPIDFPLAPAYAVPKVLKDAGLKKEDITMWEV 347
Cdd:PRK06366 232 K-NGILTAGNSAQLSDGGSALVMASEKAINEYGLKPIARITGYESASLDPLDFVEAPIPATRKLLEKQNKSIDYYDLVEH 310
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 296480314 348 NEAFSVVVLANIKMLEMDPQKVNINGGAVSLGHPIGMSGARIVVHLAHALKQG--EYGLASICNGGGGASAMLIQ 420
Cdd:PRK06366 311 NEAFSIASIIVRDQLKIDNERFNVNGGAVAIGHPIGNSGSRIIVTLINALKTRhmKTGLATLCHGGGGAHTLTLE 385
PRK09050 PRK09050
beta-ketoadipyl CoA thiolase; Validated
34-422 9.92e-100

beta-ketoadipyl CoA thiolase; Validated


Pssm-ID: 181624 [Multi-domain]  Cd Length: 401  Bit Score: 303.03  E-value: 9.92e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314  34 LNEVVIVSAIRTPIGSFLGSLSSLPATKLGSIAIQGAIEK-AGIPKEEVKEAYMGNVLQGGE-GQAPTRQAVLGAGLPIS 111
Cdd:PRK09050   1 MTEAFICDAIRTPIGRYGGALSSVRADDLGAVPLKALMARnPGVDWEAVDDVIYGCANQAGEdNRNVARMSALLAGLPVS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 112 TPCTTINKVCASGMKAIMMASQNLMCGHQDVMVAGGMESMSNVPYVMNRGATPYG-GVKLEDL-----IVKDGLTDVYNK 185
Cdd:PRK09050  81 VPGTTINRLCGSGMDAVGTAARAIKAGEAELMIAGGVESMSRAPFVMGKADSAFSrQAEIFDTtigwrFVNPLMKAQYGV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 186 IHMGNCAENTAKKLNITREEQDTYALNSYTRSKAAWEAGRFGNEVVPVTITVKGKPDVVVKEDEeYKRVDFS--KIPKLK 263
Cdd:PRK09050 161 DSMPETAENVAEDYNISRADQDAFALRSQQRAAAAQAAGFLAEEIVPVTIPQKKGDPVVVDRDE-HPRPETTleALAKLK 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 264 TVFqRENGTVTAANASTLNDGAAAVVLMTADAAKRLNVKPLARIAAFADAAVEPIDFPLAPAYAVPKVLKDAGLKKEDIT 343
Cdd:PRK09050 240 PVF-RPDGTVTAGNASGVNDGAAALLLASEAAAKKHGLTPRARILGMATAGVEPRIMGIGPAPATRKLLARLGLTIDQFD 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 344 MWEVNEAFSVVVLANIKMLEM--DPQKVNINGGAVSLGHPIGMSGARIVVHLAHALKQ--GEYGLASICNGGGGASAMLI 419
Cdd:PRK09050 319 VIELNEAFAAQGLAVLRQLGLadDDARVNPNGGAIALGHPLGMSGARLVLTALHQLERtgGRYALCTMCIGVGQGIALAI 398

                 ...
gi 296480314 420 QKL 422
Cdd:PRK09050 399 ERV 401
PRK06633 PRK06633
acetyl-CoA C-acetyltransferase;
34-420 1.30e-97

acetyl-CoA C-acetyltransferase;


Pssm-ID: 168632 [Multi-domain]  Cd Length: 392  Bit Score: 297.33  E-value: 1.30e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314  34 LNEVVIVSAIRTPIGSFLGSLSSLPATKLGSIAIQGAIEKAGIPKEEVKEAYMGNVLQGGEGQAPTRQAVLGAGLPISTP 113
Cdd:PRK06633   2 TKPVYITHAKRTAFGSFMGSLSTTPAPMLAAHLIKDILQNSKIDPALVNEVILGQVITGGSGQNPARQTLIHAGIPKEVP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 114 CTTINKVCASGMKAIMMASQNLMCGHQDVMVAGGMESMS---NVPYVmnRGATPYGGVKLEDLIVKDGLTDVYNKIHMGN 190
Cdd:PRK06633  82 GYTINKVCGSGLKSVALAANSIMTGDNEIVIAGGQENMSlgmHGSYI--RAGAKFGDIKMVDLMQYDGLTDVFSGVFMGI 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 191 CAENTAKKLNITREEQDTYALNSYTRSKAAWEAGRFGNEVVPVTITVKgKPDVVVKEDEEYK-RVDFSKIPKLKTVFQRe 269
Cdd:PRK06633 160 TAENISKQFNISRQEQDEFALSSHKKAAKAQLAGIFKDEILPIEVTIK-KTTSLFDHDETVRpDTSLEILSKLRPAFDK- 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 270 NGTVTAANASTLNDGAAAVVLMTADAAKRLNVKPLARIAAFADAAVEPIDFPLAPAYAVPKVLKDAGLKKEDITMWEVNE 349
Cdd:PRK06633 238 NGVVTAGNASSINDGAACLMVVSEEALKKHNLTPLARIVSYASAGVDPSIMGTAPVPASQKALSKAGWSVNDLEVIEVNE 317
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 296480314 350 AFSVVVLANIKMLEMDPQKVNINGGAVSLGHPIGMSGARIVVHLAHALK--QGEYGLASICNGGGGASAMLIQ 420
Cdd:PRK06633 318 AFAAQSIYVNREMKWDMEKVNINGGAIAIGHPIGASGGRVLITLIHGLRraKAKKGLVTLCIGGGMGMAMCVE 390
PRK06205 PRK06205
acetyl-CoA C-acetyltransferase;
36-421 4.78e-97

acetyl-CoA C-acetyltransferase;


Pssm-ID: 235741 [Multi-domain]  Cd Length: 404  Bit Score: 296.13  E-value: 4.78e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314  36 EVVIVSAIRTPIGSFLGSLSSLPATKLGSIAIQGAIEKAGIPKEEVKEAYMGNVLQGGEGQAPTRQAVLGAGLPISTPCT 115
Cdd:PRK06205   3 DAVICEPVRTPVGRFGGAFKDVPAEELAATVIRALVERTGIDPARIDDVIFGQGYPNGEAPAIGRVAALDAGLPVTVPGM 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 116 TINKVCASGMKAIMMASQNLMCGHQDVMVAGGMESMSNVPYVMN--RGATPYGGVKLEDLIVKDGLT---DVYNKIH-MG 189
Cdd:PRK06205  83 QLDRRCGSGLQAVITAAMQVQTGAADVVIAGGAESMSNVEFYTTdmRWGVRGGGVQLHDRLARGRETaggRRFPVPGgMI 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 190 NCAENTAKKLNITREEQDTYALNSYTRSKAAWEAGRFGNEVVPVTITVKGKPDVVVKEDEEYkRVDFS--KIPKLKTVFQ 267
Cdd:PRK06205 163 ETAENLRREYGISREEQDALAVRSHQRAVAAQEAGRFDDEIVPVTVPQRKGDPTVVDRDEHP-RADTTleSLAKLRPIMG 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 268 R--ENGTVTAANASTLNDGAAAVVLMTADAAKRLNVKPLARIAAFADAAVEPIDFPLAPAYAVPKVLKDAGLKKEDITMW 345
Cdd:PRK06205 242 KqdPEATVTAGNASGQNDAAAACLVTTEDKAEELGLRPLARLVSWAVAGVEPSRMGIGPVPATEKALARAGLTLDDIDLI 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 346 EVNEAFSVVVLANIKMLEMDPQ---KVNINGGAVSLGHPIGMSGARIVVHLAHALK--QGEYGLASICNGGGGASAMLIQ 420
Cdd:PRK06205 322 ELNEAFAAQVLAVLKEWGFGADdeeRLNVNGSGISLGHPVGATGGRILATLLRELQrrQARYGLETMCIGGGQGLAAVFE 401

                 .
gi 296480314 421 K 421
Cdd:PRK06205 402 R 402
PRK07108 PRK07108
acetyl-CoA C-acyltransferase;
34-422 1.21e-87

acetyl-CoA C-acyltransferase;


Pssm-ID: 180843 [Multi-domain]  Cd Length: 392  Bit Score: 271.64  E-value: 1.21e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314  34 LNEVVIVSAIRTPIG-SFLGSLSSLPATKLGSIAIQGAIEKAGIPKEEVKEAYMGNVL-QGGEGQAPTRQAVLGAGLPIS 111
Cdd:PRK07108   1 MTEAVIVSTARTPLAkSWRGAFNMTHGATLGGHVVQHAVERAKLDPAEVEDVIMGCANpEGATGANIARQIALRAGLPVT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 112 TPCTTINKVCASGMKAIMMASQNLMCGHQDVMVAGGMESMSNVPYVMNRGatpyggvKLEDLIVKDGLTDVYnkIHMGNC 191
Cdd:PRK07108  81 VPGMTVNRFCSSGLQTIALAAQRVIAGEGDVFVAGGVESISCVQNEMNRH-------MLREGWLVEHKPEIY--WSMLQT 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 192 AENTAKKLNITREEQDTYALNSYTRSKAAWEAGRFGNEVVPVTITVK---------GKPDVVVKEDEEYkRVDFSK--IP 260
Cdd:PRK07108 152 AENVAKRYGISKERQDEYGVQSQQRAAAAQAAGRFDDEIVPITVTAGvadkatgrlFTKEVTVSADEGI-RPDTTLegVS 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 261 KLKTVFqrENGTVTAANASTLNDGAAAVVLMTADAAKRLNVKPLARIAAFADAAVEPIDFPLAPAYAVPKVLKDAGLKKE 340
Cdd:PRK07108 231 KIRSAL--PGGVITAGNASQFSDGASACVVMNAKVAEREGLQPLGIFRGFAVAGCEPDEMGIGPVFAVPKLLKQAGLKVD 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 341 DITMWEVNEAFSVVVLANIKMLEMDPQKVNINGGAVSLGHPIGMSGARIVvhlAHALKQGE-----YGLASICNGGGGAS 415
Cdd:PRK07108 309 DIDLWELNEAFAVQVLYCRDTLGIPMDRLNVNGGAIAVGHPYGVSGARLT---GHALIEGKrrgakYVVVTMCIGGGQGA 385

                 ....*..
gi 296480314 416 AMLIQKL 422
Cdd:PRK07108 386 AGLFEVL 392
PRK07801 PRK07801
acetyl-CoA C-acetyltransferase;
36-422 3.82e-85

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181123 [Multi-domain]  Cd Length: 382  Bit Score: 265.03  E-value: 3.82e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314  36 EVVIVSAIRTPIGSFLGSLSSLPATKLGSIAIQGAIEKAGIPKEEVKEAYMGNVLQGGeGQAP--TRQAVLGAGLPISTP 113
Cdd:PRK07801   3 EAYIVDAVRTPVGKRKGGLAGVHPADLGAHVLKGLVDRTGIDPAAVDDVIFGCVDTIG-PQAGniARTSWLAAGLPEEVP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 114 CTTINKVCASGMKAIMMASQNLMCGHQDVMVAGGMESMSNVPYVMNRGA-------TPYGGVKledlivkdGLTDVYNK- 185
Cdd:PRK07801  82 GVTVDRQCGSSQQAIHFAAQAVMSGTQDLVVAGGVQNMSQIPISSAMTAgeqlgftSPFAESK--------GWLHRYGDq 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 186 -IHMGNCAENTAKKLNITREEQDTYALNSYTRSKAAWEAGRFGNEVVPVTitvkgkpDVVVkeDEEYKRVDFSKIPKLKT 264
Cdd:PRK07801 154 eVSQFRGAELIAEKWGISREEMERFALESHRRAFAAIRAGRFDNEIVPVG-------GVTV--DEGPRETSLEKMAGLKP 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 265 VfqRENGTVTAANASTLNDGAAAVVLMTADAAKRLNVKPLARIAAFADAAVEPIDFPLAPAYAVPKVLKDAGLKKEDITM 344
Cdd:PRK07801 225 L--VEGGRLTAAVASQISDGASAVLLASERAVKRHGLTPRARIHHLSVRGDDPVFMLTAPIPATRYALEKTGLSIDDIDV 302
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 345 WEVNEAFSVVVLANIKMLEMDPQKVNINGGAVSLGHPIGMSGARIVVHLAHALKQ--GEYGLASICNGGGGASAMLIQKL 422
Cdd:PRK07801 303 VEINEAFAPVVLAWLKETGADPAKVNPNGGAIALGHPLGATGAKLMTTLLHELERtgGRYGLQTMCEGGGTANVTIIERL 382
PRK06445 PRK06445
acetyl-CoA C-acetyltransferase;
34-421 6.79e-83

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180563 [Multi-domain]  Cd Length: 394  Bit Score: 259.65  E-value: 6.79e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314  34 LNEVVIVSAIRTPIGSFLGS------LSSLPATKLGSIAIQGAIEKAGIPKEEVKEAYMGNVLQGGEGQA-PTRQAVLGA 106
Cdd:PRK06445   1 LEDVYLVDFARTAFSRFRPKdpqkdvFNNIRPEELAAMLINRLIEKTGIKPEEIDDIITGCALQVGENWLyGGRHPIFLA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 107 GLPISTPCTTINKVCASGMKAIMMASQNLMCGHQDVMVAGGMESMSNVPYVMNRGATPYGGVKLEDLIVKDGLTDVYNki 186
Cdd:PRK06445  81 RLPYNIPAMAVDRQCASSLTTVSIGAMEIATGMADIVIAGGVEHMTRTPMGDNPHIEPNPKLLTDPKYIEYDLTTGYV-- 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 187 hMGNCAENTAKKLNITREEQDTYALNSYTRSKAAWEAGRFGNEVVPVTITVKGKPDVVVKEDEEYKRVDFSKIPKLKTVF 266
Cdd:PRK06445 159 -MGLTAEKLAEEAGIKREEMDRWSLRSHQLAAKAIQEGYFKDEILPIEVEVEGKKKVVDVDQSVRPDTSLEKLAKLPPAF 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 267 qRENGTVTAANASTLNDGAAAVVLMTADAAKRLNVKPLARIAAFADAAVEPIDFPLAPAYAVPKVLKDAGLKKEDITMWE 346
Cdd:PRK06445 238 -KPDGVITAGNSSPLNSGASYVLLMSKKAVKKYGLKPMAKIRSFGFAGVPPAIMGKGPVPASKKALEKAGLSVKDIDLWE 316
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 296480314 347 VNEAFSVVVLANIKMLEMDPQKVNINGGAVSLGHPIGMSGARIVVHLAHAL--KQGEYGLASICNGGGGASAMLIQK 421
Cdd:PRK06445 317 INEAFAVVVLYAIKELGLDPETVNIKGGAIAIGHPLGATGARIVGTLARQLqiKGKDYGVATLCVGGGQGGAVVLER 393
PRK08131 PRK08131
3-oxoadipyl-CoA thiolase;
39-421 9.83e-83

3-oxoadipyl-CoA thiolase;


Pssm-ID: 181242 [Multi-domain]  Cd Length: 401  Bit Score: 259.32  E-value: 9.83e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314  39 IVSAIRTPIGSFLGSLSSLPATKLGSIAIQGAIEKAGIPKEEVKEAYMGNVLQGGE-GQAPTRQAVLGAGLPISTPCTTI 117
Cdd:PRK08131   6 IYDGLRSPFGRHAGALASVRPDDLAATVIRRLLEKSGFPGDDIEDVILGCTNQAGEdSRNVARNALLLAGLPVTVPGQTV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 118 NKVCASGMKAIMMASQNLMCGHQDVMVAGGMESMSNVPYVMNRGATPYGgvklEDLIVKDG----------LTDVYNKIH 187
Cdd:PRK08131  86 NRLCASGLAAVIDAARAITCGEGDLYLAGGVESMSRAPFVMGKAESAFS----RDAKVFDTtigarfpnpkIVAQYGNDS 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 188 MGNCAENTAKKLNITREEQDTYALNSYTRSKAAWEAGRFGNEVVPVTITVKGK-PDVVVKEDEEYK-RVDFSKIPKLKTV 265
Cdd:PRK08131 162 MPETGDNVAAEFGISREDADRFAAQSQAKYQAAKEEGFFADEITPIEVPQGRKlPPKLVAEDEHPRpSSTVEALTKLKPL 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 266 FqrENGTVTAANASTLNDGAAAVVLMTADAAKRLNVKPLARIAAFADAAVEPIDFPLAPAYAVPKVLKDAGLKKEDITMW 345
Cdd:PRK08131 242 F--EGGVVTAGNASGINDGAAALLIGSRAAGEKYGLKPMARILSSAAAGVEPRIMGIGPVEAIKKALARAGLTLDDMDII 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 346 EVNEAFSVVVLANIKMLEM--DPQKVNINGGAVSLGHPIGMSGARIVVHLAHALK--QGEYGLASICNGGGGASAMLIQK 421
Cdd:PRK08131 320 EINEAFASQVLGCLKGLGVdfDDPRVNPNGGAIAVGHPLGASGARLALTAARELQrrGKRYAVVSLCIGVGQGLAMVIER 399
PRK06504 PRK06504
acetyl-CoA C-acetyltransferase;
34-422 7.29e-82

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180595 [Multi-domain]  Cd Length: 390  Bit Score: 256.58  E-value: 7.29e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314  34 LNEVVIVSAIRTPIGSFLGSLSSLPATKLGSIAIQGAIEKAGIPKEEVKEAYMGNVLQGGEgQAPT--RQAVLGAGLPIS 111
Cdd:PRK06504   1 MAEAYIVAAARTAGGRKGGRLAGWHPADLAAQVLDALVDRSGADPALIEDVIMGCVSQVGE-QATNvaRNAVLASKLPES 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 112 TPCTTINKVCASGMKAIMMASQNLMCGHQDVMVAGGMESMSNVPyvMNRGATpyggvkledLIVKDGLTDV--------Y 183
Cdd:PRK06504  80 VPGTSIDRQCGSSQQALHFAAQAVMSGTMDIVIAAGVESMTRVP--MGSPST---------LPAKNGLGHYkspgmeerY 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 184 NKIH----MGncAENTAKKLNITREEQDTYALNSYTRSKAAWEAGRFGNEVVPVTITVKGKPDVVVKEDEEYkRVDFS-- 257
Cdd:PRK06504 149 PGIQfsqfTG--AEMMAKKYGLSKDQLDEFALQSHQRAIAATQAGKFKAEIVPLEITRADGSGEMHTVDEGI-RFDATle 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 258 KIPKLKTVfqRENGTVTAANASTLNDGAAAVVLMTADAAKRLNVKPLARIAAFADAAVEPIDFPLAPAYAVPKVLKDAGL 337
Cdd:PRK06504 226 GIAGVKLI--AEGGRLTAATASQICDGASGVMVVNERGLKALGVKPLARIHHMTVIGGDPVIMLEAPLPATERALKKAGM 303
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 338 KKEDITMWEVNEAFSVVVLANIKMLEMDPQKVNINGGAVSLGHPIGMSGARIVVHLAHALKQ--GEYGLASICNGGGGAS 415
Cdd:PRK06504 304 KIDDIDLYEVNEAFASVPLAWLKATGADPERLNVNGGAIALGHPLGASGTKLMTTLVHALKQrgKRYGLQTMCEGGGMAN 383

                 ....*..
gi 296480314 416 AMLIQKL 422
Cdd:PRK06504 384 VTIVERL 390
PLN02287 PLN02287
3-ketoacyl-CoA thiolase
35-418 7.59e-82

3-ketoacyl-CoA thiolase


Pssm-ID: 215161 [Multi-domain]  Cd Length: 452  Bit Score: 258.54  E-value: 7.59e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314  35 NEVVIVSAIRTPI-GSFLGSLSSLPATKLGSIAIQGAIEKAGIPKEEVKEAYMGNVLQGGEGQA-PTRQAVLGAGLPIST 112
Cdd:PLN02287  46 DDVVIVAAYRTPIcKAKRGGFKDTYPDDLLAPVLKAVVEKTGLNPSEVGDIVVGTVLAPGSQRAnECRMAAFYAGFPETV 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 113 PCTTINKVCASGMKAIMMASQNLMCGHQDVMVAGGMESMSNVPYVMNRGATPyggvKLEDL-IVKDGLtdvynkIHMGNC 191
Cdd:PLN02287 126 PVRTVNRQCSSGLQAVADVAAAIKAGFYDIGIGAGVESMTTNPMAWEGGVNP----RVESFsQAQDCL------LPMGIT 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 192 AENTAKKLNITREEQDTYALNSYTRSKAAWEAGRFGNEVVPVTI------TVKGKPDVVVKEDEEYKRVDFSKIPKLKTV 265
Cdd:PLN02287 196 SENVAERFGVTREEQDQAAVESHRKAAAATASGKFKDEIVPVHTkivdpkTGEEKPIVISVDDGIRPNTTLADLAKLKPV 275
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 266 FqRENGTVTAANASTLNDGAAAVVLMTADAAKRLNVKPLARIAAFADAAVEPIDFPLAPAYAVPKVLKDAGLKKEDITMW 345
Cdd:PLN02287 276 F-KKNGTTTAGNSSQVSDGAGAVLLMKRSVAMQKGLPILGVFRSFAAVGVDPAVMGIGPAVAIPAAVKAAGLELDDIDLF 354
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 296480314 346 EVNEAFSVVVLANIKMLEMDPQKVNINGGAVSLGHPIGMSGARIVVHLAHALKQ----GEYGLASICNGGG-GASAML 418
Cdd:PLN02287 355 EINEAFASQFVYCCKKLGLDPEKVNVNGGAIALGHPLGATGARCVATLLHEMKRrgkdCRFGVVSMCIGTGmGAAAVF 432
PRK07661 PRK07661
acetyl-CoA C-acetyltransferase;
34-416 4.75e-81

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181072 [Multi-domain]  Cd Length: 391  Bit Score: 254.67  E-value: 4.75e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314  34 LNEVVIVSAIRTPIG-SFLGSLSSLPATKLGSIAIQGAIEKAGIPKEEVKEAYMGNVLQGGE-GQAPTRQAVLGAGLPIS 111
Cdd:PRK07661   1 MREAVIVAGARTPVGkAKKGSLKTVRPDDLGALVVKETLKRAGNYEGPIDDLIIGCAMPEAEqGLNMARNIGALAGLPYT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 112 TPCTTINKVCASGMKAIMMASQNLMCGHQDVMVAGGMESMSNVPYVmnrgatpyGGVKLEDLIVKDGLTDVYnkIHMGNC 191
Cdd:PRK07661  81 VPAITINRYCSSGLQSIAYGAERIMLGHSEAVIAGGAESMSLVPMM--------GHVVRPNPRLVEAAPEYY--MGMGHT 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 192 AENTAKKLNITREEQDTYALNSYTRSKAAWEAGRFGNEVVPVTITVK-----GKP---DVVVKEDEEYkRVDFSK--IPK 261
Cdd:PRK07661 151 AEQVAVKYGISREDQDAFAVRSHQRAAKALAEGKFADEIVPVDVTLRtvgenNKLqeeTITFSQDEGV-RADTTLeiLGK 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 262 LKTVFQReNGTVTAANASTLNDGAAAVVLMTADAAKRLNVKPLARIAAFADAAVEPIDFPLAPAYAVPKVLKDAGLKKED 341
Cdd:PRK07661 230 LRPAFNV-KGSVTAGNSSQMSDGAAAVLLMDREKAESDGLKPLAKFRSFAVAGVPPEVMGIGPIAAIPKALKLAGLELSD 308
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 296480314 342 ITMWEVNEAFSVVVLANIKMLEMDPQKVNINGGAVSLGHPIGMSGARIVVHLAHALK-QGE-YGLASICNGGGGASA 416
Cdd:PRK07661 309 IGLFELNEAFASQSIQVIRELGLDEEKVNVNGGAIALGHPLGCTGAKLTLSLIHEMKrRNEqFGIVTMCIGGGMGAA 385
PRK07850 PRK07850
steroid 3-ketoacyl-CoA thiolase;
36-422 3.14e-79

steroid 3-ketoacyl-CoA thiolase;


Pssm-ID: 181145 [Multi-domain]  Cd Length: 387  Bit Score: 250.02  E-value: 3.14e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314  36 EVVIVSAIRTPIGSFLGSLSSLPATKLGSIAIQGAIEKAGIPKEEVKEAYMGNVLQGGE-GQAPTRQAVLGAGLPISTPC 114
Cdd:PRK07850   3 NPVIVEAVRTPIGKRNGWLSGLHAAELLGAVQRAVLDRAGIDPGDVEQVIGGCVTQAGEqSNNITRTAWLHAGLPYHVGA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 115 TTINKVCASGMKAIMMASQNLMCGHQDVMVAGGMESMSNVPYVMNRG---ATPYggvkledlivkdglTDVYNkIHMGN- 190
Cdd:PRK07850  83 TTIDCQCGSAQQANHLVAGLIAAGAIDVGIACGVEAMSRVPLGANAGpgrGLPR--------------PDSWD-IDMPNq 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 191 --CAENTAKKLNITREEQDTYALNSYTRSKAAWEAGRFGNEVVPVTITV---KGKP---DVVVKEDEEYKRVDFSKIPKL 262
Cdd:PRK07850 148 feAAERIAKRRGITREDVDAFGLRSQRRAAQAWAEGRFDREISPVQAPVldeEGQPtgeTRLVTRDQGLRDTTMEGLAGL 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 263 KTVfqRENGTVTAANASTLNDGAAAVVLMTADAAKRLNVKPLARIAAFADAAVEPiDFPL-APAYAVPKVLKDAGLKKED 341
Cdd:PRK07850 228 KPV--LEGGIHTAGTSSQISDGAAAVLWMDEDRARALGLRPRARIVAQALVGAEP-YYHLdGPVQATAKVLEKAGMKIGD 304
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 342 ITMWEVNEAFSVVVLANIKMLEMDPQKVNINGGAVSLGHPIGMSGARIVVHLAHALKQ--GEYGLASICNGGGGASAMLI 419
Cdd:PRK07850 305 IDLVEINEAFASVVLSWAQVHEPDMDKVNVNGGAIALGHPVGSTGARLITTALHELERtdKSTALITMCAGGALSTGTII 384

                 ...
gi 296480314 420 QKL 422
Cdd:PRK07850 385 ERI 387
PRK07851 PRK07851
acetyl-CoA C-acetyltransferase;
36-422 3.41e-79

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181146 [Multi-domain]  Cd Length: 406  Bit Score: 250.31  E-value: 3.41e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314  36 EVVIVSAIRTPIG-SFLGSLSSLPATKLGSIAIQGAIEKA-GIPKEEVKEAYMGNVLQGGE-GQAPTRQAVLGAGLPiST 112
Cdd:PRK07851   3 EAVIVSTARSPIGrAFKGSLKDMRPDDLAAQMVRAALDKVpALDPTDIDDLMLGCGLPGGEqGFNMARVVAVLLGYD-FL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 113 PCTTINKVCASGMKAIMMASQNLMCGHQDVMVAGGMESMS--------NVPYVMN---------------RGATPYGGVK 169
Cdd:PRK07851  82 PGTTVNRYCSSSLQTTRMAFHAIKAGEGDVFISAGVETVSrfakgnsdSLPDTKNplfaeaqartaaraeGGAEAWHDPR 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 170 LEDLivkdgLTDVYnkIHMGNCAENTAKKLNITREEQDTYALNSYTRSKAAWEAGRFGNEVVPVTItvkgkPD--VVVKE 247
Cdd:PRK07851 162 EDGL-----LPDVY--IAMGQTAENVAQLTGISREEQDEWGVRSQNRAEEAIANGFFEREITPVTL-----PDgtVVSTD 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 248 DEEYKRVDFSKIPKLKTVFqRENGTVTAANASTLNDGAAAVVLMTADAAKRLNVKPLARIAAFADAAVEPIDFPLAPAYA 327
Cdd:PRK07851 230 DGPRAGTTYEKVSQLKPVF-RPDGTVTAGNACPLNDGAAAVVIMSDTKARELGLTPLARIVSTGVSGLSPEIMGLGPVEA 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 328 VPKVLKDAGLKKEDITMWEVNEAFSVVVLANIKMLEMDPQKVNINGGAVSLGHPIGMSGARIVVHLAHALK--QGEYGLA 405
Cdd:PRK07851 309 SKQALARAGMSIDDIDLVEINEAFAAQVLPSARELGIDEDKLNVSGGAIALGHPFGMTGARITTTLLNNLQthDKTFGLE 388
                        410
                 ....*....|....*..
gi 296480314 406 SICNGGGGASAMLIQKL 422
Cdd:PRK07851 389 TMCVGGGQGMAMVLERL 405
fadI PRK08963
3-ketoacyl-CoA thiolase; Reviewed
37-420 7.06e-79

3-ketoacyl-CoA thiolase; Reviewed


Pssm-ID: 181597 [Multi-domain]  Cd Length: 428  Bit Score: 250.29  E-value: 7.06e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314  37 VVIVSAIRTPIGSFLGSLSSLPATKLGSIAIQGAIEKAGIPKEEVKEAYMGNVLQGGEGQAPTRQAVLGAGLPISTPCTT 116
Cdd:PRK08963   7 IAIVSGLRTPFAKQATAFHGIPAVDLGKMVVGELLARSEIDPELIEQLVFGQVVQMPEAPNIAREIVLGTGMNVHTDAYS 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 117 INKVCASGMKAIMMASQNLMCGHQDVMVAGGMESMSNVP-----------YVMNRGAT------PYGGVKLEDLI-VKDG 178
Cdd:PRK08963  87 VSRACATSFQAVANVAESIMAGTIDIGIAGGADSSSVLPigvskklaralVDLNKARTlgqrlkLFSRLRLRDLLpVPPA 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 179 LTDVYNKIHMGNCAENTAKKLNITREEQDTYALNSYTRSKAAWEAGRFGNEVVPVTITVKGKP---DVVVKEDEeykrvD 255
Cdd:PRK08963 167 VAEYSTGLRMGDTAEQMAKTYGISREEQDALAHRSHQLAAQAWAEGKLDDEVMTAHVPPYKQPleeDNNIRGDS-----T 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 256 FSKIPKLKTVFQRENGTVTAANASTLNDGAAAVVLMTADAAKRLNVKPLARIAAFADAAVEPI-DFPLAPAYAVPKVLKD 334
Cdd:PRK08963 242 LEDYAKLRPAFDRKHGTVTAANSTPLTDGAAAVLLMSESRAKALGLTPLGYLRSYAFAAIDVWqDMLLGPAYATPLALER 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 335 AGLKKEDITMWEVNEAFSVVVLANIKML-----------------EMDPQKVNINGGAVSLGHPIGMSGARIVVHLAHAL 397
Cdd:PRK08963 322 AGLTLADLTLIDMHEAFAAQTLANLQMFaserfareklgrsqaigEVDMSKFNVLGGSIAYGHPFAATGARMITQTLHEL 401
                        410       420
                 ....*....|....*....|....*
gi 296480314 398 KQ--GEYGLASICNGGGGASAMLIQ 420
Cdd:PRK08963 402 RRrgGGLGLTTACAAGGLGAAMVLE 426
PRK09052 PRK09052
acetyl-CoA C-acyltransferase;
34-422 3.22e-78

acetyl-CoA C-acyltransferase;


Pssm-ID: 181626 [Multi-domain]  Cd Length: 399  Bit Score: 247.61  E-value: 3.22e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314  34 LNEVVIVSAIRTPIG-SFLGSLSSLPATKLGSIAIQGAIEKA-GIPKEEVKEAYMGNVLQGGE-GQAPTRQAVLGAGLPI 110
Cdd:PRK09052   5 LQDAYIVAATRTPVGkAPRGMFKNTRPDDLLAHVLRSAVAQVpGLDPKLIEDAIVGCAMPEAEqGLNVARIGALLAGLPN 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 111 STPCTTINKVCASGMKAIMMASQNLMCGHQDVMVAGGMESMSNVPYVMNRGA-TPYGGVKLEDLIVKDGltdvynkihMG 189
Cdd:PRK09052  85 SVGGVTVNRFCASGLQAVAMAADRIRVGEADVMIAAGVESMSMVPMMGNKPSmSPAIFARDENVGIAYG---------MG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 190 NCAENTAKKLNITREEQDTYALNSYTRSKAAWEAGRFGNEVVPVTITVKgKPD-----VVVKEDE----EYKRVDFS--K 258
Cdd:PRK09052 156 LTAEKVAEQWKVSREDQDAFALESHQKAIAAQQAGEFKDEITPYEITER-FPDlatgeVDVKTRTvdldEGPRADTSleG 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 259 IPKLKTVFqRENGTVTAANASTLNDGAAAVVLMTADAAKRLNVKPLARIAAFADAAVEPIDFPLAPAYAVPKVLKDAGLK 338
Cdd:PRK09052 235 LAKLKPVF-ANKGSVTAGNSSQTSDGAGAVILVSEKALKQFNLTPLARFVSFAVAGVPPEIMGIGPIEAIPAALKQAGLK 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 339 KEDITMWEVNEAFSVVVLANIKMLEMDPQKVNINGGAVSLGHPIGMSGARIVVHLAHAL--KQGEYGLASICNGGGGASA 416
Cdd:PRK09052 314 QDDLDWIELNEAFAAQSLAVIRDLGLDPSKVNPLGGAIALGHPLGATGAIRTATVVHGLrrTNLKYGMVTMCVGTGMGAA 393

                 ....*.
gi 296480314 417 MLIQKL 422
Cdd:PRK09052 394 GIFERL 399
PRK08170 PRK08170
acetyl-CoA C-acetyltransferase;
79-422 5.13e-74

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181265 [Multi-domain]  Cd Length: 426  Bit Score: 237.61  E-value: 5.13e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314  79 EEVKEAYMGNVLQGGEGQAPTRQAVLGAGLPISTPCTTINKVCASGMKAIMMASQNLMCGHQDVMVAGGMESMSNVPYVM 158
Cdd:PRK08170  47 DDLDEVILGCAMPSPDEANIARVVALRLGCGEKVPAWTVQRNCASGMQALDSAAANIALGRADLVLAGGVEAMSHAPLLF 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 159 NRGATPY---------GGVKLEDL-------------IVKdGLTDVYNKIHMGNCAENTAKKLNITREEQDTYALNSYTR 216
Cdd:PRK08170 127 SEKMVRWlagwyaaksIGQKLAALgklrpsylapvigLLR-GLTDPVVGLNMGQTAEVLAHRFGITREQMDAYAARSHQR 205
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 217 SKAAWEAGRFGnEVVPVtITVKGKpdvvVKEDEEYKRVDFS--KIPKLKTVFQRENGTVTAANASTLNDGAAAVVLMTAD 294
Cdd:PRK08170 206 LAAAQAEGRLK-EVVPL-FDRDGK----FYDHDDGVRPDSSmeKLAKLKPFFDRPYGRVTAGNSSQITDGACWLLLASEE 279
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 295 AAKRLNVKPLARIAAFADAAVEPIDFPLAPAYAVPKVLKDAGLKKEDITMWEVNEAFSVVVLANIKML------------ 362
Cdd:PRK08170 280 AVKKYGLPPLGRIVDSQWAALDPSQMGLGPVHAATPLLQRHGLTLEDLDLWEINEAFAAQVLACLAAWadeeycreqlgl 359
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 296480314 363 -----EMDPQKVNINGGAVSLGHPIGMSGARIVVHLAHALKQ--GEYGLASICNGGGGASAMLIQKL 422
Cdd:PRK08170 360 dgalgELDRERLNVDGGAIALGHPVGASGARIVLHLLHALKRrgTKRGIAAICIGGGQGGAMLLERV 426
fadA PRK08947
3-ketoacyl-CoA thiolase; Reviewed
35-422 1.00e-73

3-ketoacyl-CoA thiolase; Reviewed


Pssm-ID: 181592 [Multi-domain]  Cd Length: 387  Bit Score: 235.63  E-value: 1.00e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314  35 NEVVIVSAIRTPIG-SFLGSLSSLPATKLGSIAIQGAIEK-AGIPKEEVKEAYMGNVLQGGE-GQAPTRQAVLGAGLPIS 111
Cdd:PRK08947   2 EDVVIVDAIRTPMGrSKGGAFRNVRAEDLSAHLMRSLLARnPALDPAEIDDIIWGCVQQTLEqGFNIARNAALLAGIPHS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 112 TPCTTINKVCASGMKAIMMASQNLMCGHQDVMVAGGMESMSNVPyvMNRGATPYggvkledlivkDGLTDVYNKIH--MG 189
Cdd:PRK08947  82 VPAVTVNRLCGSSMQALHDAARAIMTGDGDVFLIGGVEHMGHVP--MNHGVDFH-----------PGLSKNVAKAAgmMG 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 190 NCAENTAKKLNITREEQDTYALNSYTRSKAAWEAGRFGNEVVPVTitvkGKpdvvvKEDEEYKRVDFSKI---------- 259
Cdd:PRK08947 149 LTAEMLGKMHGISREQQDAFAARSHQRAWAATQEGRFKNEIIPTE----GH-----DADGVLKLFDYDEVirpettveal 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 260 PKLKTVFQRENGTVTAANASTLNDGAAAVVLMTADAAKRLNVKPLARIAAFADAAVEPIDFPLAPAYAVPKVLKDAGLKK 339
Cdd:PRK08947 220 AALRPAFDPVNGTVTAGTSSALSDGASAMLVMSESRAKELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSI 299
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 340 EDITMWEVNEAF---SVVVLANIKMLEMDPQKVNINGGAVSLGHPIGMSGARIVVHLAHALKQ--GEYGLASICNGGGGA 414
Cdd:PRK08947 300 SDIDVFELNEAFaaqSLPCLKDLGLLDKMDEKVNLNGGAIALGHPLGCSGARISTTLLNLMERkdAQFGLATMCIGLGQG 379

                 ....*...
gi 296480314 415 SAMLIQKL 422
Cdd:PRK08947 380 IATVFERV 387
PRK08242 PRK08242
acetyl-CoA C-acetyltransferase;
36-422 2.23e-69

acetyl-CoA C-acetyltransferase;


Pssm-ID: 236197 [Multi-domain]  Cd Length: 402  Bit Score: 224.76  E-value: 2.23e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314  36 EVVIVSAIRTPIGSFL--GSLSSLPATKLGSIAIQGAIEKAGIPKEEVKEAYMGNVLQGGE-GQAPTRQAVLGAGLPIST 112
Cdd:PRK08242   3 EAYIYDAVRTPRGKGKkdGSLHEVKPVRLAAGLLEALRDRNGLDTAAVDDVVLGCVTPVGDqGADIARTAVLAAGLPETV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 113 PCTTINKVCASGMKAIMMASQNLMCGHQDVMVAGGMESMSNVPYVMNRGATPyggvkledliVKDGLTDVYNKIHMGNCA 192
Cdd:PRK08242  83 PGVQINRFCASGLEAVNLAAAKVRSGWDDLVIAGGVESMSRVPMGSDGGAWA----------MDPSTNFPTYFVPQGISA 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 193 ENTAKKLNITREEQDTYALNSYTRSKAAWEAGRFGNEVVPVtitvKGKPDVVVKEDEEYKR--VDFSKIPKLKTVFQ--- 267
Cdd:PRK08242 153 DLIATKYGFSREDVDAYAVESQQRAAAAWAEGYFAKSVVPV----KDQNGLTILDHDEHMRpgTTMESLAKLKPSFAmmg 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 268 -----------------RENGTVTAANASTLNDGAAAVVLMTADAAKRLNVKPLARIAAFADAAVEPIDFPLAPAYAVPK 330
Cdd:PRK08242 229 emggfdavalqkypeveRINHVHHAGNSSGIVDGAAAVLIGSEEAGKALGLKPRARIVATATIGSDPTIMLTGPVPATRK 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 331 VLKDAGLKKEDITMWEVNEAFSVVVLANIKMLEMDPQKVNINGGAVSLGHPIGMSGARIVVHLAHAL--KQGEYGLASIC 408
Cdd:PRK08242 309 ALAKAGLTVDDIDLFELNEAFASVVLRFMQALDIPHDKVNVNGGAIAMGHPLGATGAMILGTVLDELerRGKRTALITLC 388
                        410
                 ....*....|....
gi 296480314 409 NGGGGASAMLIQKL 422
Cdd:PRK08242 389 VGGGMGIATIIERV 402
PRK06690 PRK06690
acetyl-CoA C-acyltransferase;
35-422 1.28e-68

acetyl-CoA C-acyltransferase;


Pssm-ID: 180659 [Multi-domain]  Cd Length: 361  Bit Score: 221.56  E-value: 1.28e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314  35 NEVVIVSAIRTPIGSFLGSLSSLPATKLGSIAIQgaIEKAGIPkEEVKEAYMGNVLQGGEGQAptRQAVLGAGLPISTPC 114
Cdd:PRK06690   1 NRAVIVEAKRTPIGKKNGMLKDYEVQQLAAPLLT--FLSKGME-REIDDVILGNVVGPGGNVA--RLSALEAGLGLHIPG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 115 TTINKVCASGMKAIMMASQNLMCGHQDVMVAGGMESMSNVPYVMNRGATPyggvkledlivkdgltDVYNKIHMGNCAEN 194
Cdd:PRK06690  76 VTIDRQCGAGLEAIRTACHFIQGGAGKCYIAGGVESTSTSPFQNRARFSP----------------ETIGDPDMGVAAEY 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 195 TAKKLNITREEQDTYALNSYTRSKAAWEAGRFGNEVVPVTitvkGKPDVVVKEDEEYKRVdfskIPKLKTVFQReNGTVT 274
Cdd:PRK06690 140 VAERYNITREMQDEYACLSYKRTLQALEKGYIHEEILSFN----GLLDESIKKEMNYERI----IKRTKPAFLH-NGTVT 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 275 AANASTLNDGAAAVVLMTADAAKRLNVKPLARIAAFADAAVEPIDFPLAPAYAVPKVLKDAGLKKEDITMWEVNEAFSVV 354
Cdd:PRK06690 211 AGNSCGVNDGACAVLVMEEGQARKLGYKPVLRFVRSAVVGVDPNLPGTGPIFAVNKLLNEMNMKVEDIDYFEINEAFASK 290
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 355 VLANIKMLEMDPQKVNINGGAVSLGHPIGMSGARIVVHLAHALKQ--GEYGLASICNGGGGASAMLIQKL 422
Cdd:PRK06690 291 VVACAKELQIPYEKLNVNGGAIALGHPYGASGAMLVTRLFYQAKRedMKYGIATLGIGGGIGLALLFEKV 360
PRK06025 PRK06025
acetyl-CoA C-acetyltransferase;
36-422 2.49e-56

acetyl-CoA C-acetyltransferase;


Pssm-ID: 235675 [Multi-domain]  Cd Length: 417  Bit Score: 191.14  E-value: 2.49e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314  36 EVVIVSAIRTP--IGSF-LGSLSSLPATKLGSIAIQGAIEKAGIPKEEVKEAYMGNVLQ-GGEGQAPTRQAVLGAGLPIS 111
Cdd:PRK06025   3 EAYIIDAVRTPrgIGKVgKGALAHLHPQHLAATVLKALAERNGLNTADVDDIIWSTSSQrGKQGGDLGRMAALDAGYDIK 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 112 TPCTTINKVCASGMKAIMMASQNLMCGHQDVMVAGGMESMS----NVPYVMNRGATPYGgvkledliVKDG---LTDVYN 184
Cdd:PRK06025  83 ASGVTLDRFCGGGITSVNLAAAQIMSGMEDLVIAGGTEMMSytaaMAAEDMAAGKPPLG--------MGSGnlrLRALHP 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 185 KIHMGNCAENTAKKLNITREEQDTYALNSYTRSKAAWEAGRFGNEVVPVTitvkgKPDVVVKED-EEYKRVDFSK--IPK 261
Cdd:PRK06025 155 QSHQGVCGDAIATMEGITREALDALGLESQRRAARAIKEGRFDKSLVPVY-----RDDGSVALDhEEFPRPQTTAegLAA 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 262 LKTVFQR-------ENGTVT------------------AANASTLNDGAAAVVLMTADAAKRLNVKPLARIAAFADAAVE 316
Cdd:PRK06025 230 LKPAFTAiadypldDKGTTYrglinqkypdleikhvhhAGNSSGVVDGAAALLLASKAYAEKHGLKPRARIVAMANMGDD 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 317 PIDFPLAPAYAVPKVLKDAGLKKEDITMWEVNEAFSVVVLANIKMLEMDPQKVNINGGAVSLGHPIGMSGARIVVHLAHA 396
Cdd:PRK06025 310 PTLMLNAPVPAAKKVLAKAGLTKDDIDLWEINEAFAVVAEKFIRDLDLDRDKVNVNGGAIALGHPIGATGSILIGTVLDE 389
                        410       420
                 ....*....|....*....|....*...
gi 296480314 397 LKQ--GEYGLASICNGGGGASAMLIQKL 422
Cdd:PRK06025 390 LERrgLKRGLVTMCAAGGMAPAIIIERV 417
Thiolase_C pfam02803
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
301-421 7.24e-54

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: 175.14  E-value: 7.24e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314  301 VKPLARIAAFADAAVEPIDFPLAPAYAVPKVLKDAGLKKEDITMWEVNEAFSVVVLANIKMLEMDPQKVNINGGAVSLGH 380
Cdd:pfam02803   1 LKPLARIRSYATAGVDPAIMGIGPAYAIPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGIDPEKVNVNGGAIALGH 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 296480314  381 PIGMSGARIVVHLAHALKQ--GEYGLASICNGGGGASAMLIQK 421
Cdd:pfam02803  81 PLGASGARILVTLLHELKRrgGKYGLASLCIGGGQGVAMIIER 123
nondecarbox_cond_enzymes cd00826
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ...
40-420 9.18e-53

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


Pssm-ID: 238422 [Multi-domain]  Cd Length: 393  Bit Score: 181.15  E-value: 9.18e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314  40 VSAIRTPIGSFLGSLSSL---PATKLGSIAIQGAIEKAGIPKEEVKEAYMGNVLQGGEGQAPTRQAVLGAGLPISTPCTT 116
Cdd:cd00826    1 AGAAMTAFGKFGGENGADandLAHEAGAKAIAAALEPAGVAAGAVEEACLGQVLGAGEGQNCAQQAAMHAGGLQEAPAIG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 117 INKVCASGMKAIMMASQNLMCGHQDVMVAGGMESMSNVPyvmnrgatpyggvklEDLIVKDGLTDVYNKIHMgncaenta 196
Cdd:cd00826   81 MNNLCGSGLRALALAMQLIAGGDANCILAGGFEKMETSA---------------ENNAKEKHIDVLINKYGM-------- 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 197 kklnitREEQDTYALNSYTRSKAAWEAGRFGNEVVPvtITVKGKPDVVVKEDEEYKR----VDFSKIPKLKTVFQREnGT 272
Cdd:cd00826  138 ------RACPDAFALAGQAGAEAAEKDGRFKDEFAK--FGVKGRKGDIHSDADEYIQfgdeASLDEIAKLRPAFDKE-DF 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 273 VTAANASTLNDGAAAVVLMTADAA-------KRLNVKPLARIAAFADAAVEPIDFPLA----PAYAVPKVLKDAGLKKED 341
Cdd:cd00826  209 LTAGNACGLNDGAAAAILMSEAEAqkhglqsKAREIQALEMITDMASTFEDKKVIKMVggdgPIEAARKALEKAGLGIGD 288
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 342 ITMWEVNEAFSVVVLANIKMLEMDPQK------------------VNINGGAVSLGHPIGMSGARIVVHLAHALKQGEY- 402
Cdd:cd00826  289 LDLIEAHDAFAANACATNEALGLCPEGqggalvdrgdntyggksiINPNGGAIAIGHPIGASGAAICAELCFELKGEAGk 368
                        410       420
                 ....*....|....*....|....
gi 296480314 403 ------GLASICNGGGGASAMLIQ 420
Cdd:cd00826  369 rqgagaGLALLCIGGGGGAAMCIE 392
PRK09268 PRK09268
acetyl-CoA C-acetyltransferase;
32-421 2.76e-52

acetyl-CoA C-acetyltransferase;


Pssm-ID: 236440 [Multi-domain]  Cd Length: 427  Bit Score: 180.87  E-value: 2.76e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314  32 PTLNEVVIVSAIRTPIGSFLGSLSSLPATKLGSIAIQGAIEKAGIPKEEVKEAYMGNVLQGGEGQAPTRQAVLGAGLPIS 111
Cdd:PRK09268   4 PTVRRVAILGGNRIPFARSNGAYADASNQDMLTAALDGLVDRFGLQGERLGEVVAGAVLKHSRDFNLTRECVLGSALSPY 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 112 TPCTTINKVCASGMKAIMMASQNLMCGHQDVMVAGGMESMSNVPYV-----------MNRGATPYGGVKL------EDLI 174
Cdd:PRK09268  84 TPAYDLQQACGTGLEAAILVANKIALGQIDSGIAGGVDTTSDAPIAvneglrkilleLNRAKTTGDRLKAlgklrpKHLA 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 175 V--------KDGLTdvynkihMGNCAENTAKKLNITREEQDTYALNSYTRSKAAWEAGRFGNEVVPvtitVKGkpdvvVK 246
Cdd:PRK09268 164 PeiprngepRTGLS-------MGEHAAITAKEWGISREAQDELAAASHQNLAAAYDRGFFDDLITP----FLG-----LT 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 247 EDEEYkRVDFS--KIPKLKTVFQR-ENGTVTAANASTLNDGAAAVVLMTADAAKRLNVKPLARIAAFADAAVEPIDFP-- 321
Cdd:PRK09268 228 RDNNL-RPDSSleKLAKLKPVFGKgGRATMTAGNSTPLTDGASVVLLASEEWAAEHGLPVLAYLVDAETAAVDFVHGKeg 306
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 322 --LAPAYAVPKVLKDAGLKKEDITMWEVNEAFSVVVLANIKMLE-----------------MDPQKVNINGGAVSLGHPI 382
Cdd:PRK09268 307 llMAPAYAVPRLLARNGLTLQDFDFYEIHEAFASQVLATLKAWEdeeycrerlgldaplgsIDRSKLNVNGSSLAAGHPF 386
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 296480314 383 GMSGARIVVHLAHAL--KQGEYGLASICNGGGGASAMLIQK 421
Cdd:PRK09268 387 AATGGRIVATLAKLLaeKGSGRGLISICAAGGQGVTAILER 427
SCP-x_thiolase cd00829
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ...
66-416 2.25e-16

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: 80.00  E-value: 2.25e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314  66 AIQGAIEKAGIPKEEVKEAYMGNVLQGGEGQAPTRQAVLGAGLPIsTPCTTINKVCASGMKAIMMASQNLMCGHQDVMVA 145
Cdd:cd00829   23 AARAALDDAGLEPADIDAVVVGNAAGGRFQSFPGALIAEYLGLLG-KPATRVEAAGASGSAAVRAAAAAIASGLADVVLV 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 146 GGMESMSNVPYVMNRGATPyGGVKLEDLIVKDGLT--DVYnkihmGNCAENTAKKLNITREEQDTYA--------LNSYt 215
Cdd:cd00829  102 VGAEKMSDVPTGDEAGGRA-SDLEWEGPEPPGGLTppALY-----ALAARRYMHRYGTTREDLAKVAvknhrnaaRNPY- 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 216 rskaAWEAGrfgnevvPVTI-TVKGKPDVVvkedEEYKRVDFSKIpklktvfqrengtvtaanastlNDGAAAVVLMTAD 294
Cdd:cd00829  175 ----AQFRK-------PITVeDVLNSRMIA----DPLRLLDCCPV----------------------SDGAAAVVLASEE 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 295 AAKRLNVKPL----ARIAAFADAAVEPIDFPLAPA--YAVPKVLKDAGLKKEDITMWEVNEAFSVVVLANIKML------ 362
Cdd:cd00829  218 RARELTDRPVwilgVGAASDTPSLSERDDFLSLDAarLAARRAYKMAGITPDDIDVAELYDCFTIAELLALEDLgfcekg 297
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 296480314 363 -------EMDPQK-----VNINGGAVSLGHPIGMSGARIVVHL---------AHALKQGEYGLASicNGGGGASA 416
Cdd:cd00829  298 eggklvrEGDTAIggdlpVNTSGGLLSKGHPLGATGLAQAVEAvrqlrgeagARQVPGARVGLAH--NIGGTGSA 370
PRK06064 PRK06064
thiolase domain-containing protein;
66-416 3.50e-13

thiolase domain-containing protein;


Pssm-ID: 235688 [Multi-domain]  Cd Length: 389  Bit Score: 70.70  E-value: 3.50e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314  66 AIQGAIEKAGIPKEEVKEAYMGNVLQGGEGQAPTRQAVLG--AGL-PIstPCTTINKVCASGMKAIMMASQNLMCGHQDV 142
Cdd:PRK06064  29 AGLEALEDAGIDGKDIDAMYVGNMSAGLFVSQEHIAALIAdyAGLaPI--PATRVEAACASGGAALRQAYLAVASGEADV 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 143 MVAGGMESMSNVP---------------YVMNRGATPyggvkledlivkDGLTDVYNKIHMgncaentaKKLNITREEQD 207
Cdd:PRK06064 107 VLAAGVEKMTDVPtpdateaiaragdyeWEEFFGATF------------PGLYALIARRYM--------HKYGTTEEDLA 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 208 TYALNSY---TRSKAAweagRFGNEvvpvtITVkgkpdvvvkedEEYKRVDFSKIPkLKtVFqrengtvtaaNASTLNDG 284
Cdd:PRK06064 167 LVAVKNHyngSKNPYA----QFQKE-----ITV-----------EQVLNSPPVADP-LK-LL----------DCSPITDG 214
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 285 AAAVVLMTADAAKRLNVKPLARIAAFADAAV------EPIDFPLAPAYAVPKVLKDAGLKKEDITMWEVNEAFSVVVLAN 358
Cdd:PRK06064 215 AAAVILASEEKAKEYTDTPVWIKASGQASDTialhdrKDFTTLDAAVVAAEKAYKMAGIEPKDIDVAEVHDCFTIAEILA 294
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 359 I------------KMLEMDPQK------VNINGGAVSLGHPIGMSGARIVVHLAHALKQG-----------EYGLASicN 409
Cdd:PRK06064 295 YedlgfakkgeggKLAREGQTYiggdipVNPSGGLKAKGHPVGATGVSQAVEIVWQLRGEaekgrqqvigaGYGLTH--N 372

                 ....*...
gi 296480314 410 -GGGGASA 416
Cdd:PRK06064 373 vGGTGHTA 380
cond_enzymes cd00327
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ...
59-419 5.10e-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: 68.62  E-value: 5.10e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314  59 ATKLGSIAIQGAIEKAGIPKEEVKEAYMGNVLQGGEGQAPTRQAVLGAGLPiSTPCTTINKVCASGMKAIMMASQNLMCG 138
Cdd:cd00327    7 ASELGFEAAEQAIADAGLSKGPIVGVIVGTTGGSGEFSGAAGQLAYHLGIS-GGPAYSVNQACATGLTALALAVQQVQNG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 139 HQDVMVAGGMESmsnvpyvmnrgatpyggvkledlivkdgltdvynkihmgncaentakklnitreeqdtyalnsytrsk 218
Cdd:cd00327   86 KADIVLAGGSEE-------------------------------------------------------------------- 97
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 219 aaweagrfgnevvpvtitvkgkpdvvvkedeeykrvdfskipklktvfqrengtvtaanaSTLNDGAAAVVLMTADAAKR 298
Cdd:cd00327   98 ------------------------------------------------------------FVFGDGAAAAVVESEEHALR 117
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 299 LNVKPLARIAAFADAAVEPIDFPL----APAYAVPKVLKDAGLKKEDITMWEVNEAFSVVVLANIKMLEMDPQKV---NI 371
Cdd:cd00327  118 RGAHPQAEIVSTAATFDGASMVPAvsgeGLARAARKALEGAGLTPSDIDYVEAHGTGTPIGDAVELALGLDPDGVrspAV 197
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 296480314 372 NGGAVSLGHPIGMSGARIVVHLAHALKQGEY---------GLASICNGGGGASAMLI 419
Cdd:cd00327  198 SATLIMTGHPLGAAGLAILDELLLMLEHEFIpptpreprtVLLLGFGLGGTNAAVVL 254
PRK06289 PRK06289
acetyl-CoA acetyltransferase; Provisional
66-402 3.67e-08

acetyl-CoA acetyltransferase; Provisional


Pssm-ID: 235771 [Multi-domain]  Cd Length: 403  Bit Score: 55.08  E-value: 3.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314  66 AIQGAIEKAGIPKEEVKEAYMGNVLqggeGQAPTRQAVLGaGLPIS-------TPCTTINKVCASGMKAIMMASQNLMCG 138
Cdd:PRK06289  33 VVDGTLAAAGVDADDIEVVHVGNFF----GELFAGQGHLG-AMPATvhpalwgVPASRHEAACASGSVATLAAMADLRAG 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 139 HQDVMVAGGMESMSNVP---YVMNRGATPYGGVKLEDL-----IVKDGLTDVYNK------IHMGNCAEntakkLNITRE 204
Cdd:PRK06289 108 RYDVALVVGVELMKTVPgdvAAEHLGAAAWTGHEGQDArfpwpSMFARVADEYDRrygldeEHLRAIAE-----INFANA 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 205 EQDTyalNSYTRSkaaWeagRFgnevvpvtitvkgkPDVVVKEDEEYKRVDFSKIPKLktvfqrengtvtaaNASTLNDG 284
Cdd:PRK06289 183 RRNP---NAQTRG---W---AF--------------PDEATNDDDATNPVVEGRLRRQ--------------DCSQVTDG 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 285 AAAVVLMTADAAKRL--------------NVKPLARIAAFADAAVEPIDFPLAPAyAVPKVLKDAGLKKEDITMWEVNEA 350
Cdd:PRK06289 226 GAGVVLASDAYLRDYadarpiprikgwghRTAPLGLEQKLDRSAGDPYVLPHVRQ-AVLDAYRRAGVGLDDLDGFEVHDC 304
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 296480314 351 FSVVVLANIKML-----------------EMDPQK-VNINGGAVSLGHPIGMSGARIVVHLAHAL--KQGEY 402
Cdd:PRK06289 305 FTPSEYLAIDHIgltgpgeswkaiengeiAIGGRLpINPSGGLIGGGHPVGASGVRMLLDAAKQVtgTAGDY 376
PRK06157 PRK06157
acetyl-CoA acetyltransferase; Validated
66-390 2.72e-07

acetyl-CoA acetyltransferase; Validated


Pssm-ID: 180433 [Multi-domain]  Cd Length: 398  Bit Score: 52.34  E-value: 2.72e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314  66 AIQGAIEKAGIPKEEVKEAYMGNVLQggegqaptRQAVLGAGLPIST-------PCTTINKVCASGMKAIMMASQNLMCG 138
Cdd:PRK06157  34 AFLEALADAGIEPKDIDAAWFGTHYD--------EIGSGKSGTPLSRalrlpniPVTRVENFCATGSEAFRGAVYAVASG 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 139 HQDVMVAGGMESMSNVPY----VMNRG-------------------ATPYG---GVKLEDLivKDGLTDVYNKIHmGNCA 192
Cdd:PRK06157 106 AYDIALALGVEKLKDTGYgglpVANPGtladmtmpnvtapgnfaqlASAYAakyGVSREDL--KRAMAHVSVKSH-ANGA 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 193 ENTAKKLN--ITREEQDtyalnsytrsKAAWEAGRFGnevvpvtitvkgkpdvvvkedeeykrvdfskipklktVFqren 270
Cdd:PRK06157 183 RNPKAHLRkaVTEEQVL----------KAPMIAGPLG-------------------------------------LF---- 211
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 271 gtvtaaNASTLNDGAAAVVLMTADAAKRLN------VKPLARIAAFADAAVEP-IDFPLAPA--YAVPKVLKDAGLK--K 339
Cdd:PRK06157 212 ------DCCGVSDGAAAAIVTTPEIARALGkkdpvyVKALQLAVSNGWELQYNgWDGSYFPTtrIAARKAYREAGITdpR 285
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 296480314 340 EDITMWEVNEAFSVVVLANIKMLEMDPQ------------------KVNINGGAVSLGHPIGMSGARIV 390
Cdd:PRK06157 286 EELSMAEVHDCFSITELVTMEDLGLSERgqawrdvldgffdadgglPCQIDGGLKCFGHPIGASGLRML 354
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
102-153 6.91e-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: 47.92  E-value: 6.91e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 296480314 102 AVLGAGLPISTPCTTINKVCASGMKAIMMASQNLMCGHQDVMVAGGMESMSN 153
Cdd:cd00834  142 GQVAIRLGLRGPNYTVSTACASGAHAIGDAARLIRLGRADVVIAGGAEALIT 193
PRK07314 PRK07314
beta-ketoacyl-ACP synthase II;
113-150 2.46e-05

beta-ketoacyl-ACP synthase II;


Pssm-ID: 235987 [Multi-domain]  Cd Length: 411  Bit Score: 46.32  E-value: 2.46e-05
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 296480314 113 PCTTINKVCASGMKAIMMASQNLMCGHQDVMVAGGMES 150
Cdd:PRK07314 154 PNHSIVTACATGAHAIGDAARLIAYGDADVMVAGGAEA 191
FabB COG0304
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...
113-158 3.82e-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: 3.82e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 296480314 113 PCTTINKVCASGMKAIMMASQNLMCGHQDVMVAGGMESMSNvPYVM 158
Cdd:COG0304  153 PNYTVSTACASGAHAIGEAYRLIRRGRADVMIAGGAEAAIT-PLGL 197
PTZ00455 PTZ00455
3-ketoacyl-CoA thiolase; Provisional
66-407 5.43e-05

3-ketoacyl-CoA thiolase; Provisional


Pssm-ID: 240424 [Multi-domain]  Cd Length: 438  Bit Score: 45.27  E-value: 5.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314  66 AIQGAIEKAGIPKEE--VKEAYMGNVL------QGGEGQAPT-RQAVLGAGLP-ISTPCTTINKVCASGMKAIMMASQNL 135
Cdd:PTZ00455  55 AIQGTLENTGLDGKAalVDKVVVGNFLgelfssQGHLGPAAVgSLGQSGASNAlLYKPAMRVEGACASGGLAVQSAWEAL 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 136 MCGHQDVMVAGGMEsmsnvpyVMNRGATPYGG---VKLEDLIVKDGLTDVYNKIHMGNCAENTAKKLNITREEQDTYALN 212
Cdd:PTZ00455 135 LAGTSDIALVVGVE-------VQTTVSARVGGdylARAADYRRQRKLDDFTFPCLFAKRMKYIQEHGHFTMEDTARVAAK 207
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 213 SYTRSKAAWEAGRFGNEVVPVTITVKGKPDVVVKEDEEYKrvdfskiPKLKTvfqrengtvtaANASTLNDGAAAVVLMT 292
Cdd:PTZ00455 208 AYANGNKNPLAHMHTRKLSLEFCTGASDKNPKFLGNETYK-------PFLRM-----------TDCSQVSDGGAGLVLAS 269
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 293 ADAAKRLNVKP--------LARIAAFADAAVEPIDFP--LAPAYAVPKVLKDAGLKKEDITMWEVNEAFSVvvlANIKML 362
Cdd:PTZ00455 270 EEGLQKMGLSPndsrlveiKSLACASGNLYEDPPDATrmFTSRAAAQKALSMAGVKPSDLQVAEVHDCFTI---AELLMY 346
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 296480314 363 EM----DPQK-----------------VNINGGAVSLGHPIGMSGARIVVHLAHALKQ--GEYGLASI 407
Cdd:PTZ00455 347 EAlgiaEYGHakdlirngatalegripVNTGGGLLSFGHPVGATGVKQIMEVYRQMKGqcGEYQMKNI 414
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
70-151 3.38e-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: 41.85  E-value: 3.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314   70 AIEKAGIPKEEVKEAYMGnVLQG------GEGQAPTRQAVLGAGLPISTPCT-------------------TINKVCASG 124
Cdd:pfam00109  98 ALEDAGITPDSLDGSRTG-VFIGsgigdyAALLLLDEDGGPRRGSPFAVGTMpsviagrisyflglrgpsvTVDTACSSS 176
                          90       100
                  ....*....|....*....|....*..
gi 296480314  125 MKAIMMASQNLMCGHQDVMVAGGMESM 151
Cdd:pfam00109 177 LVAIHAAVQSIRSGEADVALAGGVNLL 203
PRK08256 PRK08256
lipid-transfer protein; Provisional
55-151 3.43e-04

lipid-transfer protein; Provisional


Pssm-ID: 181327 [Multi-domain]  Cd Length: 391  Bit Score: 42.58  E-value: 3.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314  55 SSLPATKLGSIAIQGAIEKAGIPKEEVKEAYMGNVLqgGE---GQAptrqAVLGAGLpISTPCTTINKVCASGMKAIMMA 131
Cdd:PRK08256  18 ASWDYPDMAAEAGRAALADAGIDYDAVQQAYVGYVY--GDstsGQR----ALYEVGM-TGIPIVNVNNNCSTGSTALFLA 90
                         90       100
                 ....*....|....*....|
gi 296480314 132 SQNLMCGHQDVMVAGGMESM 151
Cdd:PRK08256  91 RQAVRSGAADCALALGFEQM 110
PRK12578 PRK12578
thiolase domain-containing protein;
66-154 1.45e-03

thiolase domain-containing protein;


Pssm-ID: 183606 [Multi-domain]  Cd Length: 385  Bit Score: 40.60  E-value: 1.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314  66 AIQGAIEKAGIPKEEVKEAYMGNvlqggegqAPTRQAVLGAGLPISTPCTTINKV-------CASGMKAIMMASQNLMCG 138
Cdd:PRK12578  28 SIKEALNDAGVSQTDIELVVVGS--------TAYRGIELYPAPIVAEYSGLTGKVplrveamCATGLAASLTAYTAVASG 99
                         90
                 ....*....|....*.
gi 296480314 139 HQDVMVAGGMESMSNV 154
Cdd:PRK12578 100 LVDMAIAVGVDKMTEV 115
PRK07516 PRK07516
thiolase domain-containing protein;
279-416 3.57e-03

thiolase domain-containing protein;


Pssm-ID: 181013 [Multi-domain]  Cd Length: 389  Bit Score: 39.16  E-value: 3.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 279 STLNDGAAAVVLMTADAAKRLN-------------VKPLARIaafadaavEPIDFPlAPAYAVPKVLKDAGLKKEDITMW 345
Cdd:PRK07516 213 SLVSDGAAALVLADAETARALQravrfrarahvndFLPLSRR--------DPLAFE-GPRRAWQRALAQAGVTLDDLSFV 283
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296480314 346 EVNEAFSVVVLANIKMLEMDPQ------------------KVNINGGAVSLGHPIGMSG-------ARIVVHLAHALKQG 400
Cdd:PRK07516 284 ETHDCFTIAELIEYEAMGLAPPgqgarairegwtakdgklPVNPSGGLKAKGHPIGATGvsmhvlaAMQLTGEAGGMQIP 363
                        170
                 ....*....|....*.
gi 296480314 401 EYGLASICNGGGGASA 416
Cdd:PRK07516 364 GAKLAGVFNMGGAAVA 379
elong_cond_enzymes cd00828
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ...
82-152 3.87e-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: 39.34  E-value: 3.87e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 296480314  82 KEAYMGNVLQGGEGQAPTRQAVLGAGLPIST-PCTTINKVCASGMKAIMMASQNLMCGHQDVMVAGGMESMS 152
Cdd:cd00828  122 ARAVNPYVSPKWMLSPNTVAGWVNILLLSSHgPIKTPVGACATALEALDLAVEAIRSGKADIVVVGGVEDPL 193
 
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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