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Conserved domains on  [gi|401461805|ref|NP_058771|]
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acetyl-CoA acetyltransferase, mitochondrial precursor [Rattus norvegicus]

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 ...
40-423 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: 537.45  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805  40 VIVSATRTPIGSFLGSLASQPATKLGTIAIQGAIEKAGIPKEEVKEVYMGNVIQGGEGQAPTRQATLGAGLPIATPCTTV 119
Cdd:cd00751    1 VIVSAVRTPIGRFGGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGEGQNPARQAALLAGLPESVPATTV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 120 NKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMSRGATPY-GGVKLEDLIVKDGLTDVYNKIHMGNCAENTA 198
Cdd:cd00751   81 NRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGrLGLNTLDGMLDDGLTDPFTGLSMGITAENVA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 199 KKLSISREEQDKYAIGSYTRSKEAWDAGKFANEITPITISVKGKPdVVVKEDEEYKR-VDFSKVPKLKTVFqKENGTVTA 277
Cdd:cd00751  161 EKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEVPGRKGP-VVVDRDEGPRPdTTLEKLAKLKPAF-KKDGTVTA 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 278 ANASTLNDGAAAVVLMTAEAAQRLKVKPLARIAAFADAAVDPIDFPLAPAYAVPKVLKYAGLKKEDIAMWEVNEAFSVVV 357
Cdd:cd00751  239 GNASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDIDLIEINEAFAAQA 318
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 401461805 358 LANIKMLEIDPQKVNVHGGAVSLGHPIGMSGARIVVHLAHALKQ--GEFGLASICNGGGGASAVLIEK 423
Cdd:cd00751  319 LACLKELGLDPEKVNVNGGAIALGHPLGASGARIVVTLLHELKRrgGRYGLATMCIGGGQGAAMVIER 386
 
Name Accession Description Interval E-value
thiolase cd00751
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ...
40-423 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: 537.45  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805  40 VIVSATRTPIGSFLGSLASQPATKLGTIAIQGAIEKAGIPKEEVKEVYMGNVIQGGEGQAPTRQATLGAGLPIATPCTTV 119
Cdd:cd00751    1 VIVSAVRTPIGRFGGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGEGQNPARQAALLAGLPESVPATTV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 120 NKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMSRGATPY-GGVKLEDLIVKDGLTDVYNKIHMGNCAENTA 198
Cdd:cd00751   81 NRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGrLGLNTLDGMLDDGLTDPFTGLSMGITAENVA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 199 KKLSISREEQDKYAIGSYTRSKEAWDAGKFANEITPITISVKGKPdVVVKEDEEYKR-VDFSKVPKLKTVFqKENGTVTA 277
Cdd:cd00751  161 EKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEVPGRKGP-VVVDRDEGPRPdTTLEKLAKLKPAF-KKDGTVTA 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 278 ANASTLNDGAAAVVLMTAEAAQRLKVKPLARIAAFADAAVDPIDFPLAPAYAVPKVLKYAGLKKEDIAMWEVNEAFSVVV 357
Cdd:cd00751  239 GNASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDIDLIEINEAFAAQA 318
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 401461805 358 LANIKMLEIDPQKVNVHGGAVSLGHPIGMSGARIVVHLAHALKQ--GEFGLASICNGGGGASAVLIEK 423
Cdd:cd00751  319 LACLKELGLDPEKVNVNGGAIALGHPLGASGARIVVTLLHELKRrgGRYGLATMCIGGGQGAAMVIER 386
PLN02644 PLN02644
acetyl-CoA C-acetyltransferase
38-424 0e+00

acetyl-CoA C-acetyltransferase


Pssm-ID: 215347 [Multi-domain]  Cd Length: 394  Bit Score: 524.66  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805  38 DVVIVSATRTPIGSFLGSLASQPATKLGTIAIQGAIEKAGIPKEEVKEVYMGNVIQGGEGQAPTRQATLGAGLPIATPCT 117
Cdd:PLN02644   2 DVCIVGVARTPIGGFLGSLSSLSATELGSIAIQAALERAGVDPALVQEVFFGNVLSANLGQAPARQAALGAGLPPSTICT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 118 TVNKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVM--SRGATPYGGVKLEDLIVKDGLTDVYNKIHMGNCAE 195
Cdd:PLN02644  82 TVNKVCASGMKAVMLAAQSIQLGINDVVVAGGMESMSNAPKYLpeARKGSRLGHDTVVDGMLKDGLWDVYNDFGMGVCAE 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 196 NTAKKLSISREEQDKYAIGSYTRSKEAWDAGKFANEITPITISV-KGKPDVVVKEDEEYKRVDFSKVPKLKTVFQKENGT 274
Cdd:PLN02644 162 LCADQYSISREEQDAYAIQSYERAIAAQEAGAFAWEIVPVEVPGgRGRPSVIVDKDEGLGKFDPAKLRKLRPSFKEDGGS 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 275 VTAANASTLNDGAAAVVLMTAEAAQRLKVKPLARIAAFADAAVDPIDFPLAPAYAVPKVLKYAGLKKEDIAMWEVNEAFS 354
Cdd:PLN02644 242 VTAGNASSISDGAAALVLVSGEKALELGLQVIAKIRGYADAAQAPELFTTAPALAIPKALKHAGLEASQVDYYEINEAFS 321
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 401461805 355 VVVLANIKMLEIDPQKVNVHGGAVSLGHPIGMSGARIVVHLAHALKQ--GEFGLASICNGGGGASAVLIEKL 424
Cdd:PLN02644 322 VVALANQKLLGLDPEKVNVHGGAVSLGHPIGCSGARILVTLLGVLRSknGKYGVAGICNGGGGASAIVVELM 393
PaaJ COG0183
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ...
37-424 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: 515.39  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805  37 NDVVIVSATRTPIGSFLGSLASQPATKLGTIAIQGAIEKAGIPKEEVKEVYMGNVIQGGEGQAPTRQATLGAGLPIATPC 116
Cdd:COG0183    2 REVVIVDAVRTPFGRFGGALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQAGQGQNPARQAALLAGLPESVPA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 117 TTVNKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMSRGATPYGG-VKLEDLIVKDGLTDVYNKIHMGNCAE 195
Cdd:COG0183   82 VTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMLLPKARWGYRMnAKLVDPMINPGLTDPYTGLSMGETAE 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 196 NTAKKLSISREEQDKYAIGSYTRSKEAWDAGKFANEITPITIsVKGKPDVVVKEDEEYKR-VDFSKVPKLKTVFqKENGT 274
Cdd:COG0183  162 NVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVEV-PDRKGEVVVDRDEGPRPdTTLEKLAKLKPAF-KKDGT 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 275 VTAANASTLNDGAAAVVLMTAEAAQRLKVKPLARIAAFADAAVDPIDFPLAPAYAVPKVLKYAGLKKEDIAMWEVNEAFS 354
Cdd:COG0183  240 VTAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIGPVPATRKALARAGLTLDDIDLIEINEAFA 319
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 401461805 355 VVVLANIKMLEIDPQKVNVHGGAVSLGHPIGMSGARIVVHLAHALKQ--GEFGLASICNGGGGASAVLIEKL 424
Cdd:COG0183  320 AQVLAVLRELGLDPDKVNVNGGAIALGHPLGASGARILVTLLHELERrgGRYGLATMCIGGGQGIALIIERV 391
AcCoA-C-Actrans TIGR01930
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ...
41-422 9.13e-162

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: 460.54  E-value: 9.13e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805   41 IVSATRTPIGSFLGSLASQPATKLGTIAIQGAIEKAGIPKEEVKEVYMGNVIQGGEGQAPTRQATLGAGLPIATPCTTVN 120
Cdd:TIGR01930   1 IVAAARTPIGKFGGSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLQAGEQQNIARQAALLAGLPESVPAYTVN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805  121 KVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMSRGATP---YGGVKLEDLIVKDgLTDVYNKIHMGNCAENT 197
Cdd:TIGR01930  81 RQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGVPRSLRWgvkPGNAELEDARLKD-LTDANTGLPMGVTAENL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805  198 AKKLSISREEQDKYAIGSYTRSKEAWDAGKFANEITPITISVKGKPDVVVKEDEEYKRVDFSKVPKLKTVFqKENGTVTA 277
Cdd:TIGR01930 160 AKKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVTVKGRKGPVTVSSDEGIRPNTTLEKLAKLKPAF-DPDGTVTA 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805  278 ANASTLNDGAAAVVLMTAEAAQRLKVKPLARIAAFADAAVDPIDFPLAPAYAVPKVLKYAGLKKEDIAMWEVNEAFSVVV 357
Cdd:TIGR01930 239 GNSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALKKAGLSISDIDLFEINEAFAAQV 318
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 401461805  358 LANIKMLEIDPQKVNVHGGAVSLGHPIGMSGARIVVHLAHALKQ--GEFGLASICNGGGGASAVLIE 422
Cdd:TIGR01930 319 LACIKELGLDLEKVNVNGGAIALGHPLGASGARIVTTLLHELKRrgGRYGLATMCIGGGQGAAVILE 385
Thiolase_N pfam00108
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
39-296 5.63e-115

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: 336.97  E-value: 5.63e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805   39 VVIVSATRTPIGSFLGSLASQPATKLGTIAIQGAIEKAGIPKEEVKEVYMGNVIQGGEGQAPTRQATLGAGLPIATPCTT 118
Cdd:pfam00108   1 VVIVSAARTPFGSFGGSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQAGEGQNPARQAALKAGIPDSAPAVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805  119 VNKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMS---RGATPYGGVKLEDLIVKDGLTDVYNKIHMGNCAE 195
Cdd:pfam00108  81 INKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALPtdaRSGLKHGDEKKHDLLIPDGLTDAFNGYHMGLTAE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805  196 NTAKKLSISREEQDKYAIGSYTRSKEAWDAGKFANEITPITISVKGKPDVVVKEDEEYKRVDFSKVPKLKTVFQKEnGTV 275
Cdd:pfam00108 161 NVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDEIVPVTVKGRKGKPTVDKDEGIRPPTTAEPLAKLKPAFDKE-GTV 239
                         250       260
                  ....*....|....*....|.
gi 401461805  276 TAANASTLNDGAAAVVLMTAE 296
Cdd:pfam00108 240 TAGNASPINDGAAAVLLMSES 260
 
Name Accession Description Interval E-value
thiolase cd00751
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ...
40-423 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: 537.45  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805  40 VIVSATRTPIGSFLGSLASQPATKLGTIAIQGAIEKAGIPKEEVKEVYMGNVIQGGEGQAPTRQATLGAGLPIATPCTTV 119
Cdd:cd00751    1 VIVSAVRTPIGRFGGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGEGQNPARQAALLAGLPESVPATTV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 120 NKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMSRGATPY-GGVKLEDLIVKDGLTDVYNKIHMGNCAENTA 198
Cdd:cd00751   81 NRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGrLGLNTLDGMLDDGLTDPFTGLSMGITAENVA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 199 KKLSISREEQDKYAIGSYTRSKEAWDAGKFANEITPITISVKGKPdVVVKEDEEYKR-VDFSKVPKLKTVFqKENGTVTA 277
Cdd:cd00751  161 EKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEVPGRKGP-VVVDRDEGPRPdTTLEKLAKLKPAF-KKDGTVTA 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 278 ANASTLNDGAAAVVLMTAEAAQRLKVKPLARIAAFADAAVDPIDFPLAPAYAVPKVLKYAGLKKEDIAMWEVNEAFSVVV 357
Cdd:cd00751  239 GNASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDIDLIEINEAFAAQA 318
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 401461805 358 LANIKMLEIDPQKVNVHGGAVSLGHPIGMSGARIVVHLAHALKQ--GEFGLASICNGGGGASAVLIEK 423
Cdd:cd00751  319 LACLKELGLDPEKVNVNGGAIALGHPLGASGARIVVTLLHELKRrgGRYGLATMCIGGGQGAAMVIER 386
PLN02644 PLN02644
acetyl-CoA C-acetyltransferase
38-424 0e+00

acetyl-CoA C-acetyltransferase


Pssm-ID: 215347 [Multi-domain]  Cd Length: 394  Bit Score: 524.66  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805  38 DVVIVSATRTPIGSFLGSLASQPATKLGTIAIQGAIEKAGIPKEEVKEVYMGNVIQGGEGQAPTRQATLGAGLPIATPCT 117
Cdd:PLN02644   2 DVCIVGVARTPIGGFLGSLSSLSATELGSIAIQAALERAGVDPALVQEVFFGNVLSANLGQAPARQAALGAGLPPSTICT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 118 TVNKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVM--SRGATPYGGVKLEDLIVKDGLTDVYNKIHMGNCAE 195
Cdd:PLN02644  82 TVNKVCASGMKAVMLAAQSIQLGINDVVVAGGMESMSNAPKYLpeARKGSRLGHDTVVDGMLKDGLWDVYNDFGMGVCAE 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 196 NTAKKLSISREEQDKYAIGSYTRSKEAWDAGKFANEITPITISV-KGKPDVVVKEDEEYKRVDFSKVPKLKTVFQKENGT 274
Cdd:PLN02644 162 LCADQYSISREEQDAYAIQSYERAIAAQEAGAFAWEIVPVEVPGgRGRPSVIVDKDEGLGKFDPAKLRKLRPSFKEDGGS 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 275 VTAANASTLNDGAAAVVLMTAEAAQRLKVKPLARIAAFADAAVDPIDFPLAPAYAVPKVLKYAGLKKEDIAMWEVNEAFS 354
Cdd:PLN02644 242 VTAGNASSISDGAAALVLVSGEKALELGLQVIAKIRGYADAAQAPELFTTAPALAIPKALKHAGLEASQVDYYEINEAFS 321
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 401461805 355 VVVLANIKMLEIDPQKVNVHGGAVSLGHPIGMSGARIVVHLAHALKQ--GEFGLASICNGGGGASAVLIEKL 424
Cdd:PLN02644 322 VVALANQKLLGLDPEKVNVHGGAVSLGHPIGCSGARILVTLLGVLRSknGKYGVAGICNGGGGASAIVVELM 393
PaaJ COG0183
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ...
37-424 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: 515.39  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805  37 NDVVIVSATRTPIGSFLGSLASQPATKLGTIAIQGAIEKAGIPKEEVKEVYMGNVIQGGEGQAPTRQATLGAGLPIATPC 116
Cdd:COG0183    2 REVVIVDAVRTPFGRFGGALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQAGQGQNPARQAALLAGLPESVPA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 117 TTVNKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMSRGATPYGG-VKLEDLIVKDGLTDVYNKIHMGNCAE 195
Cdd:COG0183   82 VTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMLLPKARWGYRMnAKLVDPMINPGLTDPYTGLSMGETAE 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 196 NTAKKLSISREEQDKYAIGSYTRSKEAWDAGKFANEITPITIsVKGKPDVVVKEDEEYKR-VDFSKVPKLKTVFqKENGT 274
Cdd:COG0183  162 NVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVEV-PDRKGEVVVDRDEGPRPdTTLEKLAKLKPAF-KKDGT 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 275 VTAANASTLNDGAAAVVLMTAEAAQRLKVKPLARIAAFADAAVDPIDFPLAPAYAVPKVLKYAGLKKEDIAMWEVNEAFS 354
Cdd:COG0183  240 VTAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIGPVPATRKALARAGLTLDDIDLIEINEAFA 319
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 401461805 355 VVVLANIKMLEIDPQKVNVHGGAVSLGHPIGMSGARIVVHLAHALKQ--GEFGLASICNGGGGASAVLIEKL 424
Cdd:COG0183  320 AQVLAVLRELGLDPDKVNVNGGAIALGHPLGASGARILVTLLHELERrgGRYGLATMCIGGGQGIALIIERV 391
PRK05790 PRK05790
putative acyltransferase; Provisional
37-424 3.29e-167

putative acyltransferase; Provisional


Pssm-ID: 180261 [Multi-domain]  Cd Length: 393  Bit Score: 474.64  E-value: 3.29e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805  37 NDVVIVSATRTPIGSFLGSLASQPATKLGTIAIQGAIEKAGIPKEEVKEVYMGNVIQGGEGQAPTRQATLGAGLPIATPC 116
Cdd:PRK05790   2 KDVVIVSAARTPIGKFGGALKDVSAVELGAIVIKAALERAGVPPEQVDEVIMGQVLQAGAGQNPARQAALKAGLPVEVPA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 117 TTVNKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVM--SRGATPYGGVKLEDLIVKDGLTDVYNKIHMGNCA 194
Cdd:PRK05790  82 LTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQESMSQAPHVLpgSRWGQKMGDVELVDTMIHDGLTDAFNGYHMGITA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 195 ENTAKKLSISREEQDKYAIGSYTRSKEAWDAGKFANEITPITISVKGKPDVVVKEDeEYKRVDFS--KVPKLKTVFqKEN 272
Cdd:PRK05790 162 ENLAEQYGITREEQDEFALASQQKAEAAIKAGRFKDEIVPVTIKQRKGDPVVVDTD-EHPRPDTTaeSLAKLRPAF-DKD 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 273 GTVTAANASTLNDGAAAVVLMTAEAAQRLKVKPLARIAAFADAAVDPIDFPLAPAYAVPKVLKYAGLKKEDIAMWEVNEA 352
Cdd:PRK05790 240 GTVTAGNASGINDGAAAVVVMSEAKAKELGLTPLARIVSYAVAGVDPAIMGIGPVPAIRKALEKAGWSLADLDLIEINEA 319
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 401461805 353 FSVVVLANIKMLEIDPQKVNVHGGAVSLGHPIGMSGARIVVHLAHALK--QGEFGLASICNGGGGASAVLIEKL 424
Cdd:PRK05790 320 FAAQALAVEKELGLDPEKVNVNGGAIALGHPIGASGARILVTLLHEMKrrGAKKGLATLCIGGGQGVALIVERP 393
AcCoA-C-Actrans TIGR01930
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ...
41-422 9.13e-162

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: 460.54  E-value: 9.13e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805   41 IVSATRTPIGSFLGSLASQPATKLGTIAIQGAIEKAGIPKEEVKEVYMGNVIQGGEGQAPTRQATLGAGLPIATPCTTVN 120
Cdd:TIGR01930   1 IVAAARTPIGKFGGSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLQAGEQQNIARQAALLAGLPESVPAYTVN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805  121 KVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMSRGATP---YGGVKLEDLIVKDgLTDVYNKIHMGNCAENT 197
Cdd:TIGR01930  81 RQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGVPRSLRWgvkPGNAELEDARLKD-LTDANTGLPMGVTAENL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805  198 AKKLSISREEQDKYAIGSYTRSKEAWDAGKFANEITPITISVKGKPDVVVKEDEEYKRVDFSKVPKLKTVFqKENGTVTA 277
Cdd:TIGR01930 160 AKKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVTVKGRKGPVTVSSDEGIRPNTTLEKLAKLKPAF-DPDGTVTA 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805  278 ANASTLNDGAAAVVLMTAEAAQRLKVKPLARIAAFADAAVDPIDFPLAPAYAVPKVLKYAGLKKEDIAMWEVNEAFSVVV 357
Cdd:TIGR01930 239 GNSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALKKAGLSISDIDLFEINEAFAAQV 318
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 401461805  358 LANIKMLEIDPQKVNVHGGAVSLGHPIGMSGARIVVHLAHALKQ--GEFGLASICNGGGGASAVLIE 422
Cdd:TIGR01930 319 LACIKELGLDLEKVNVNGGAIALGHPLGASGARIVTTLLHELKRrgGRYGLATMCIGGGQGAAVILE 385
PRK08235 PRK08235
acetyl-CoA C-acetyltransferase;
40-422 6.19e-149

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181311 [Multi-domain]  Cd Length: 393  Bit Score: 428.36  E-value: 6.19e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805  40 VIVSATRTPIGSFLGSLASQPATKLGTIAIQGAIEKAGIPKEEVKEVYMGNVIQGGEGQAPTRQATLGAGLPIATPCTTV 119
Cdd:PRK08235   5 VIVSAARTPFGKFGGSLKDVKATELGGIAIKEALERANVSAEDVEEVIMGTVLQGGQGQIPSRQAARAAGIPWEVQTETV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 120 NKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMSRGATPY--GGVKLEDLIVKDGLTDVYNKIHMGNCAENT 197
Cdd:PRK08235  85 NKVCASGLRAVTLADQIIRAGDASVIVAGGMESMSNAPYILPGARWGYrmGDNEVIDLMVADGLTCAFSGVHMGVYGGEV 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 198 AKKLSISREEQDKYAIGSYTRSKEAWDAGKFANEITPITI-SVKGKPDVVVKEDEEYKRVDFSKVPKLKTVFQKEnGTVT 276
Cdd:PRK08235 165 AKELGISREAQDEWAYRSHQRAVSAHEEGRFEEEIVPVTIpQRKGDPIVVAKDEAPRKDTTIEKLAKLKPVFDKT-GTIT 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 277 AANASTLNDGAAAVVLMTAEAAQRLKVKPLARIAAFADAAVDPIDFPLAPAYAVPKVLKYAGLKKEDIAMWEVNEAFSVV 356
Cdd:PRK08235 244 AGNAPGVNDGAAALVLMSEDRAKQEGRKPLATILAHTAIAVEAKDFPRTPGYAINALLEKTGKTVEDIDLFEINEAFAAV 323
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 401461805 357 VLANIKMLEIDPQKVNVHGGAVSLGHPIGMSGARIVVHLAHALKQ--GEFGLASICNGGGGASAVLIE 422
Cdd:PRK08235 324 ALASTEIAGIDPEKVNVNGGAVALGHPIGASGARIIVTLIHELKRrgGGIGIAAICSGGGQGDAVLIE 391
PRK06954 PRK06954
acetyl-CoA C-acetyltransferase;
39-422 2.89e-121

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180775 [Multi-domain]  Cd Length: 397  Bit Score: 358.05  E-value: 2.89e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805  39 VVIVSATRTPIGSFLGSLASQPATKLGTIAIQGAIEKAGIPKEEVKEVYMGNVIQGGEGQAPTRQATLGAGLPIATPCTT 118
Cdd:PRK06954   9 IVIASAARTPMAAFQGEFASLTAPQLGAAAIAAAVERAGLKPEQIDEVVMGCVLPAGQGQAPARQAALGAGLPLSVGCTT 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 119 VNKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVM--SRGATPYGGVKLEDLIVKDGLTDVYNKIH-MGNCAE 195
Cdd:PRK06954  89 VNKMCGSGMRAAMFAHDMLVAGSVDVIVAGGMESMTNAPYLLpkARGGMRMGHGQVLDHMFLDGLEDAYDKGRlMGTFAE 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 196 NTAKKLSISREEQDKYAIGSYTRSKEAWDAGKFANEITPITISVKgKPDVVVKEDEEYKRVDFSKVPKLKTVFQKeNGTV 275
Cdd:PRK06954 169 ECAGEYGFTREAQDAFAIESLARAKRANEDGSFAWEIAPVTVAGK-KGDTVIDRDEQPFKANPEKIPTLKPAFSK-TGTV 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 276 TAANASTLNDGAAAVVLMTAEAAQRLKVKPLARIAAFADAAVDPIDFPLAPAYAVPKVLKYAGLKKEDIAMWEVNEAFSV 355
Cdd:PRK06954 247 TAANSSSISDGAAALVMMRASTAKRLGLAPLARVVGHSTFAQAPSKFTTAPVGAIRKLFEKNGWRAAEVDLFEINEAFAV 326
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 401461805 356 VVLANIKMLEIDPQKVNVHGGAVSLGHPIGMSGARIVVHLAHALKQ--GEFGLASICNGGGGASAVLIE 422
Cdd:PRK06954 327 VTMAAMKEHGLPHEKVNVNGGACALGHPIGASGARILVTLIGALRArgGKRGVASLCIGGGEATAMGIE 395
PRK09051 PRK09051
beta-ketothiolase BktB;
37-424 4.21e-116

beta-ketothiolase BktB;


Pssm-ID: 181625 [Multi-domain]  Cd Length: 394  Bit Score: 344.64  E-value: 4.21e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805  37 NDVVIVSATRTPIGSFLGSLASQPATKLGTIAIQGAIEKAGIPKEEVKEVYMGNVIqggegqaPT--------RQATLGA 108
Cdd:PRK09051   3 REVVVVSGVRTAIGTFGGSLKDVAPTDLGATVVREALARAGVDPDQVGHVVFGHVI-------PTeprdmylsRVAAINA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 109 GLPIATPCTTVNKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVM--SRGATPYGGVKLEDLIVKdGLTDVYN 186
Cdd:PRK09051  76 GVPQETPAFNVNRLCGSGLQAIVSAAQAILLGDADVAIGGGAESMSRAPYLLpaARWGARMGDAKLVDMMVG-ALHDPFG 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 187 KIHMGNCAENTAKKLSISREEQDKYAIGSYTRSKEAWDAGKFANEITPITISVKgKPDVVVKEDEEYKR-VDFSKVPKLK 265
Cdd:PRK09051 155 TIHMGVTAENVAAKYGISREAQDALALESHRRAAAAIAAGYFKDQIVPVEIKTR-KGEVVFDTDEHVRAdTTLEDLAKLK 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 266 TVFQKENGTVTAANASTLNDGAAAVVLMTAEAAQRLKVKPLARIAAFADAAVDPIDFPLAPAYAVPKVLKYAGLKKEDIA 345
Cdd:PRK09051 234 PVFKKENGTVTAGNASGINDGAAAVVLAEADAAEARGLKPLARLVGYAHAGVDPEYMGIGPVPATQKALERAGLTVADLD 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 346 MWEVNEAFSVVVLANIKMLEIDPQKVNVHGGAVSLGHPIGMSGARIVVHLAHALK--QGEFGLASICNGGGGASAVLIEK 423
Cdd:PRK09051 314 VIEANEAFAAQACAVTRELGLDPAKVNPNGSGISLGHPVGATGAIITVKALYELQriGGRYALVTMCIGGGQGIAAIFER 393

                 .
gi 401461805 424 L 424
Cdd:PRK09051 394 L 394
Thiolase_N pfam00108
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
39-296 5.63e-115

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: 336.97  E-value: 5.63e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805   39 VVIVSATRTPIGSFLGSLASQPATKLGTIAIQGAIEKAGIPKEEVKEVYMGNVIQGGEGQAPTRQATLGAGLPIATPCTT 118
Cdd:pfam00108   1 VVIVSAARTPFGSFGGSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQAGEGQNPARQAALKAGIPDSAPAVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805  119 VNKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMS---RGATPYGGVKLEDLIVKDGLTDVYNKIHMGNCAE 195
Cdd:pfam00108  81 INKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALPtdaRSGLKHGDEKKHDLLIPDGLTDAFNGYHMGLTAE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805  196 NTAKKLSISREEQDKYAIGSYTRSKEAWDAGKFANEITPITISVKGKPDVVVKEDEEYKRVDFSKVPKLKTVFQKEnGTV 275
Cdd:pfam00108 161 NVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDEIVPVTVKGRKGKPTVDKDEGIRPPTTAEPLAKLKPAFDKE-GTV 239
                         250       260
                  ....*....|....*....|.
gi 401461805  276 TAANASTLNDGAAAVVLMTAE 296
Cdd:pfam00108 240 TAGNASPINDGAAAVLLMSES 260
PRK05656 PRK05656
acetyl-CoA C-acetyltransferase;
36-423 4.32e-111

acetyl-CoA C-acetyltransferase;


Pssm-ID: 168156  Cd Length: 393  Bit Score: 331.85  E-value: 4.32e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805  36 LNDVVIVSATRTPIGSFLGSLASQPATKLGTIAIQGAIEKAGIPKEEVKEVYMGNVIQGGEGQAPTRQATLGAGLPIATP 115
Cdd:PRK05656   1 MQDVVIVAATRTAIGSFQGSLANIPAVELGAAVIRRLLEQTGLDPAQVDEVILGQVLTAGAGQNPARQAAIKAGLPHSVP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 116 CTTVNKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVM--SRGATPYGGVKLEDLIVKDGLTDVYNKIHMGNC 193
Cdd:PRK05656  81 AMTLNKVCGSGLKALHLAAQAIRCGDAEVIIAGGQENMSLAPYVLpgARTGLRMGHAQLVDSMITDGLWDAFNDYHMGIT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 194 AENTAKKLSISREEQDKYAIGSYTRSKEAWDAGKFANEITPITI-SVKGKPDVVVKEDEEYKRVDFSKVPKLKTVFQKEn 272
Cdd:PRK05656 161 AENLVEKYGISREAQDAFAAASQQKAVAAIEAGRFDDEITPILIpQRKGEPLAFATDEQPRAGTTAESLAKLKPAFKKD- 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 273 GTVTAANASTLNDGAAAVVLMTAEAAQRLKVKPLARIAAFADAAVDPIDFPLAPAYAVPKVLKYAGLKKEDIAMWEVNEA 352
Cdd:PRK05656 240 GSVTAGNASSLNDGAAAVLLMSAAKAKALGLPVLAKIAAYANAGVDPAIMGIGPVSATRRCLDKAGWSLAELDLIEANEA 319
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 401461805 353 FSVVVLANIKMLEIDPQKVNVHGGAVSLGHPIGMSGARIVVHLAHAL--KQGEFGLASICNGGGGASAVLIEK 423
Cdd:PRK05656 320 FAAQSLAVGKELGWDAAKVNVNGGAIALGHPIGASGCRVLVTLLHEMirRDAKKGLATLCIGGGQGVALAIER 392
PRK06366 PRK06366
acetyl-CoA C-acetyltransferase;
36-422 8.06e-102

acetyl-CoA C-acetyltransferase;


Pssm-ID: 102340 [Multi-domain]  Cd Length: 388  Bit Score: 308.09  E-value: 8.06e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805  36 LNDVVIVSATRTPIGSFLGSLASQPATKLGTIAIQGAIEKAGIPKEEVKEVYMGNVIQGGEGQAPTRQATLGAGLPIATP 115
Cdd:PRK06366   1 MKDVYIVSAKRTAIGKFGRSFSKIKAPQLGGAAIKAVIDDAKLDPALVQEVIMGNVIQAGVGQNPAGQAAYHAGLPFGVT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 116 CTTVNKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMSRGAT--P----YGGVKLEDLIVKDGLTDVYNKIH 189
Cdd:PRK06366  81 KYTVNVVCASGMLAVESAAREIMLGERDLVIAGGMENMSNAPFLLPSDLRwgPkhllHKNYKIDDAMLVDGLIDAFYFEH 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 190 MGNCAENTAKKLSISREEQDKYAIGSYTRSKEAWDAGKFANEITPITisvkgkpdvVVKEDEEYKRVDFSKVPKLKTVFQ 269
Cdd:PRK06366 161 MGVSAERTARKYGITREMADEYSVQSYERAIRATESGEFRNEIVPFN---------DLDRDEGIRKTTMEDLAKLPPAFD 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 270 KeNGTVTAANASTLNDGAAAVVLMTAEAAQRLKVKPLARIAAFADAAVDPIDFPLAPAYAVPKVLKYAGLKKEDIAMWEV 349
Cdd:PRK06366 232 K-NGILTAGNSAQLSDGGSALVMASEKAINEYGLKPIARITGYESASLDPLDFVEAPIPATRKLLEKQNKSIDYYDLVEH 310
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 401461805 350 NEAFSVVVLANIKMLEIDPQKVNVHGGAVSLGHPIGMSGARIVVHLAHALKQGEF--GLASICNGGGGASAVLIE 422
Cdd:PRK06366 311 NEAFSIASIIVRDQLKIDNERFNVNGGAVAIGHPIGNSGSRIIVTLINALKTRHMktGLATLCHGGGGAHTLTLE 385
PRK06205 PRK06205
acetyl-CoA C-acetyltransferase;
38-423 4.06e-95

acetyl-CoA C-acetyltransferase;


Pssm-ID: 235741 [Multi-domain]  Cd Length: 404  Bit Score: 291.51  E-value: 4.06e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805  38 DVVIVSATRTPIGSFLGSLASQPATKLGTIAIQGAIEKAGIPKEEVKEVYMGNVIQGGEGQAPTRQATLGAGLPIATPCT 117
Cdd:PRK06205   3 DAVICEPVRTPVGRFGGAFKDVPAEELAATVIRALVERTGIDPARIDDVIFGQGYPNGEAPAIGRVAALDAGLPVTVPGM 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 118 TVNKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMS--RGATPYGGVKLEDLIVKDGLT---DVYNKIH-MG 191
Cdd:PRK06205  83 QLDRRCGSGLQAVITAAMQVQTGAADVVIAGGAESMSNVEFYTTdmRWGVRGGGVQLHDRLARGRETaggRRFPVPGgMI 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 192 NCAENTAKKLSISREEQDKYAIGSYTRSKEAWDAGKFANEITPITISVKGKPDVVVKEDEEYkRVDFS--KVPKLKTVFQ 269
Cdd:PRK06205 163 ETAENLRREYGISREEQDALAVRSHQRAVAAQEAGRFDDEIVPVTVPQRKGDPTVVDRDEHP-RADTTleSLAKLRPIMG 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 270 K--ENGTVTAANASTLNDGAAAVVLMTAEAAQRLKVKPLARIAAFADAAVDPIDFPLAPAYAVPKVLKYAGLKKEDIAMW 347
Cdd:PRK06205 242 KqdPEATVTAGNASGQNDAAAACLVTTEDKAEELGLRPLARLVSWAVAGVEPSRMGIGPVPATEKALARAGLTLDDIDLI 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 348 EVNEAFSVVVLANIKMLEIDPQ---KVNVHGGAVSLGHPIGMSGARIVVHLAHALK--QGEFGLASICNGGGGASAVLIE 422
Cdd:PRK06205 322 ELNEAFAAQVLAVLKEWGFGADdeeRLNVNGSGISLGHPVGATGGRILATLLRELQrrQARYGLETMCIGGGQGLAAVFE 401

                 .
gi 401461805 423 K 423
Cdd:PRK06205 402 R 402
PRK06633 PRK06633
acetyl-CoA C-acetyltransferase;
39-422 1.23e-94

acetyl-CoA C-acetyltransferase;


Pssm-ID: 168632 [Multi-domain]  Cd Length: 392  Bit Score: 289.62  E-value: 1.23e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805  39 VVIVSATRTPIGSFLGSLASQPATKLGTIAIQGAIEKAGIPKEEVKEVYMGNVIQGGEGQAPTRQATLGAGLPIATPCTT 118
Cdd:PRK06633   5 VYITHAKRTAFGSFMGSLSTTPAPMLAAHLIKDILQNSKIDPALVNEVILGQVITGGSGQNPARQTLIHAGIPKEVPGYT 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 119 VNKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMS---NVPYVmsRGATPYGGVKLEDLIVKDGLTDVYNKIHMGNCAE 195
Cdd:PRK06633  85 INKVCGSGLKSVALAANSIMTGDNEIVIAGGQENMSlgmHGSYI--RAGAKFGDIKMVDLMQYDGLTDVFSGVFMGITAE 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 196 NTAKKLSISREEQDKYAIGSYTRSKEAWDAGKFANEITPITISVKgKPDVVVKEDEEYK-RVDFSKVPKLKTVFQKeNGT 274
Cdd:PRK06633 163 NISKQFNISRQEQDEFALSSHKKAAKAQLAGIFKDEILPIEVTIK-KTTSLFDHDETVRpDTSLEILSKLRPAFDK-NGV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 275 VTAANASTLNDGAAAVVLMTAEAAQRLKVKPLARIAAFADAAVDPIDFPLAPAYAVPKVLKYAGLKKEDIAMWEVNEAFS 354
Cdd:PRK06633 241 VTAGNASSINDGAACLMVVSEEALKKHNLTPLARIVSYASAGVDPSIMGTAPVPASQKALSKAGWSVNDLEVIEVNEAFA 320
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 355 VVVLANIKMLEIDPQKVNVHGGAVSLGHPIGMSGARIVVHLAHALKQGEF--GLASICNGGGGASAVLIE 422
Cdd:PRK06633 321 AQSIYVNREMKWDMEKVNINGGAIAIGHPIGASGGRVLITLIHGLRRAKAkkGLVTLCIGGGMGMAMCVE 390
PRK09050 PRK09050
beta-ketoadipyl CoA thiolase; Validated
36-424 2.57e-94

beta-ketoadipyl CoA thiolase; Validated


Pssm-ID: 181624 [Multi-domain]  Cd Length: 401  Bit Score: 289.16  E-value: 2.57e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805  36 LNDVVIVSATRTPIGSFLGSLASQPATKLGTIAIQGAIEK-AGIPKEEVKEVYMGNVIQGGE-GQAPTRQATLGAGLPIA 113
Cdd:PRK09050   1 MTEAFICDAIRTPIGRYGGALSSVRADDLGAVPLKALMARnPGVDWEAVDDVIYGCANQAGEdNRNVARMSALLAGLPVS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 114 TPCTTVNKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMSRGATPYG-GVKLEDL-----IVKDGLTDVYNK 187
Cdd:PRK09050  81 VPGTTINRLCGSGMDAVGTAARAIKAGEAELMIAGGVESMSRAPFVMGKADSAFSrQAEIFDTtigwrFVNPLMKAQYGV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 188 IHMGNCAENTAKKLSISREEQDKYAIGSYTRSKEAWDAGKFANEITPITISVKGKPDVVVKEDEeYKRVDFS--KVPKLK 265
Cdd:PRK09050 161 DSMPETAENVAEDYNISRADQDAFALRSQQRAAAAQAAGFLAEEIVPVTIPQKKGDPVVVDRDE-HPRPETTleALAKLK 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 266 TVFqKENGTVTAANASTLNDGAAAVVLMTAEAAQRLKVKPLARIAAFADAAVDPIDFPLAPAYAVPKVLKYAGLKKEDIA 345
Cdd:PRK09050 240 PVF-RPDGTVTAGNASGVNDGAAALLLASEAAAKKHGLTPRARILGMATAGVEPRIMGIGPAPATRKLLARLGLTIDQFD 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 346 MWEVNEAFSVVVLANIKMLEI--DPQKVNVHGGAVSLGHPIGMSGARIVVHLAHALKQ--GEFGLASICNGGGGASAVLI 421
Cdd:PRK09050 319 VIELNEAFAAQGLAVLRQLGLadDDARVNPNGGAIALGHPLGMSGARLVLTALHQLERtgGRYALCTMCIGVGQGIALAI 398

                 ...
gi 401461805 422 EKL 424
Cdd:PRK09050 399 ERV 401
PRK08131 PRK08131
3-oxoadipyl-CoA thiolase;
38-423 1.68e-83

3-oxoadipyl-CoA thiolase;


Pssm-ID: 181242 [Multi-domain]  Cd Length: 401  Bit Score: 261.25  E-value: 1.68e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805  38 DVVIVSATRTPIGSFLGSLASQPATKLGTIAIQGAIEKAGIPKEEVKEVYMGNVIQGGE-GQAPTRQATLGAGLPIATPC 116
Cdd:PRK08131   3 DAYIYDGLRSPFGRHAGALASVRPDDLAATVIRRLLEKSGFPGDDIEDVILGCTNQAGEdSRNVARNALLLAGLPVTVPG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 117 TTVNKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMSRGATPYGgvklEDLIVKDG----------LTDVYN 186
Cdd:PRK08131  83 QTVNRLCASGLAAVIDAARAITCGEGDLYLAGGVESMSRAPFVMGKAESAFS----RDAKVFDTtigarfpnpkIVAQYG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 187 KIHMGNCAENTAKKLSISREEQDKYAIGSYTRSKEAWDAGKFANEITPITISVKGK-PDVVVKEDEEYK-RVDFSKVPKL 264
Cdd:PRK08131 159 NDSMPETGDNVAAEFGISREDADRFAAQSQAKYQAAKEEGFFADEITPIEVPQGRKlPPKLVAEDEHPRpSSTVEALTKL 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 265 KTVFqkENGTVTAANASTLNDGAAAVVLMTAEAAQRLKVKPLARIAAFADAAVDPIDFPLAPAYAVPKVLKYAGLKKEDI 344
Cdd:PRK08131 239 KPLF--EGGVVTAGNASGINDGAAALLIGSRAAGEKYGLKPMARILSSAAAGVEPRIMGIGPVEAIKKALARAGLTLDDM 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 345 AMWEVNEAFSVVVLANIKMLEI--DPQKVNVHGGAVSLGHPIGMSGARIVVHLAHALK--QGEFGLASICNGGGGASAVL 420
Cdd:PRK08131 317 DIIEINEAFASQVLGCLKGLGVdfDDPRVNPNGGAIAVGHPLGASGARLALTAARELQrrGKRYAVVSLCIGVGQGLAMV 396

                 ...
gi 401461805 421 IEK 423
Cdd:PRK08131 397 IER 399
PRK07108 PRK07108
acetyl-CoA C-acyltransferase;
36-424 2.08e-83

acetyl-CoA C-acyltransferase;


Pssm-ID: 180843 [Multi-domain]  Cd Length: 392  Bit Score: 260.86  E-value: 2.08e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805  36 LNDVVIVSATRTPIG-SFLGSLASQPATKLGTIAIQGAIEKAGIPKEEVKEVYMGNVI-QGGEGQAPTRQATLGAGLPIA 113
Cdd:PRK07108   1 MTEAVIVSTARTPLAkSWRGAFNMTHGATLGGHVVQHAVERAKLDPAEVEDVIMGCANpEGATGANIARQIALRAGLPVT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 114 TPCTTVNKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMSRGatpyggvKLEDLIVKDGLTDVYnkIHMGNC 193
Cdd:PRK07108  81 VPGMTVNRFCSSGLQTIALAAQRVIAGEGDVFVAGGVESISCVQNEMNRH-------MLREGWLVEHKPEIY--WSMLQT 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 194 AENTAKKLSISREEQDKYAIGSYTRSKEAWDAGKFANEITPITISVK---------GKPDVVVKEDEEYkRVDFSK--VP 262
Cdd:PRK07108 152 AENVAKRYGISKERQDEYGVQSQQRAAAAQAAGRFDDEIVPITVTAGvadkatgrlFTKEVTVSADEGI-RPDTTLegVS 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 263 KLKTVFqkENGTVTAANASTLNDGAAAVVLMTAEAAQRLKVKPLARIAAFADAAVDPIDFPLAPAYAVPKVLKYAGLKKE 342
Cdd:PRK07108 231 KIRSAL--PGGVITAGNASQFSDGASACVVMNAKVAEREGLQPLGIFRGFAVAGCEPDEMGIGPVFAVPKLLKQAGLKVD 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 343 DIAMWEVNEAFSVVVLANIKMLEIDPQKVNVHGGAVSLGHPIGMSGARIVvhlAHALKQGE-----FGLASICNGGGGAS 417
Cdd:PRK07108 309 DIDLWELNEAFAVQVLYCRDTLGIPMDRLNVNGGAIAVGHPYGVSGARLT---GHALIEGKrrgakYVVVTMCIGGGQGA 385

                 ....*..
gi 401461805 418 AVLIEKL 424
Cdd:PRK07108 386 AGLFEVL 392
PRK06445 PRK06445
acetyl-CoA C-acetyltransferase;
36-423 2.96e-83

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180563 [Multi-domain]  Cd Length: 394  Bit Score: 260.42  E-value: 2.96e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805  36 LNDVVIVSATRTPigsFLGSLASQPAT---------KLGTIAIQGAIEKAGIPKEEVKEVYMGNVIQGGEGQA-PTRQAT 105
Cdd:PRK06445   1 LEDVYLVDFARTA---FSRFRPKDPQKdvfnnirpeELAAMLINRLIEKTGIKPEEIDDIITGCALQVGENWLyGGRHPI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 106 LGAGLPIATPCTTVNKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMSRGATPYGGVKLEDLIVKDGLTDVY 185
Cdd:PRK06445  78 FLARLPYNIPAMAVDRQCASSLTTVSIGAMEIATGMADIVIAGGVEHMTRTPMGDNPHIEPNPKLLTDPKYIEYDLTTGY 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 186 NkihMGNCAENTAKKLSISREEQDKYAIGSYTRSKEAWDAGKFANEITPITISVKGKPDVVVKEDEEYKRVDFSKVPKLK 265
Cdd:PRK06445 158 V---MGLTAEKLAEEAGIKREEMDRWSLRSHQLAAKAIQEGYFKDEILPIEVEVEGKKKVVDVDQSVRPDTSLEKLAKLP 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 266 TVFqKENGTVTAANASTLNDGAAAVVLMTAEAAQRLKVKPLARIAAFADAAVDPIDFPLAPAYAVPKVLKYAGLKKEDIA 345
Cdd:PRK06445 235 PAF-KPDGVITAGNSSPLNSGASYVLLMSKKAVKKYGLKPMAKIRSFGFAGVPPAIMGKGPVPASKKALEKAGLSVKDID 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 346 MWEVNEAFSVVVLANIKMLEIDPQKVNVHGGAVSLGHPIGMSGARIVVHLAHAL--KQGEFGLASICNGGGGASAVLIEK 423
Cdd:PRK06445 314 LWEINEAFAVVVLYAIKELGLDPETVNIKGGAIAIGHPLGATGARIVGTLARQLqiKGKDYGVATLCVGGGQGGAVVLER 393
PRK07851 PRK07851
acetyl-CoA C-acetyltransferase;
38-424 1.17e-81

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181146 [Multi-domain]  Cd Length: 406  Bit Score: 256.85  E-value: 1.17e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805  38 DVVIVSATRTPIG-SFLGSLASQPATKLGTIAIQGAIEKA-GIPKEEVKEVYMGNVIQGGE-GQAPTRQATLGAGLPiAT 114
Cdd:PRK07851   3 EAVIVSTARSPIGrAFKGSLKDMRPDDLAAQMVRAALDKVpALDPTDIDDLMLGCGLPGGEqGFNMARVVAVLLGYD-FL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 115 PCTTVNKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMSRG------------------ATPYGGVKLEDLI 176
Cdd:PRK07851  82 PGTTVNRYCSSSLQTTRMAFHAIKAGEGDVFISAGVETVSRFAKGNSDSlpdtknplfaeaqartaaRAEGGAEAWHDPR 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 177 VKDGLTDVYnkIHMGNCAENTAKKLSISREEQDKYAIGSYTRSKEAWDAGKFANEITPITIsvkgkPD--VVVKEDEEYK 254
Cdd:PRK07851 162 EDGLLPDVY--IAMGQTAENVAQLTGISREEQDEWGVRSQNRAEEAIANGFFEREITPVTL-----PDgtVVSTDDGPRA 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 255 RVDFSKVPKLKTVFqKENGTVTAANASTLNDGAAAVVLMTAEAAQRLKVKPLARIAAFADAAVDPIDFPLAPAYAVPKVL 334
Cdd:PRK07851 235 GTTYEKVSQLKPVF-RPDGTVTAGNACPLNDGAAAVVIMSDTKARELGLTPLARIVSTGVSGLSPEIMGLGPVEASKQAL 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 335 KYAGLKKEDIAMWEVNEAFSVVVLANIKMLEIDPQKVNVHGGAVSLGHPIGMSGARIVVHLAHALK--QGEFGLASICNG 412
Cdd:PRK07851 314 ARAGMSIDDIDLVEINEAFAAQVLPSARELGIDEDKLNVSGGAIALGHPFGMTGARITTTLLNNLQthDKTFGLETMCVG 393
                        410
                 ....*....|..
gi 401461805 413 GGGASAVLIEKL 424
Cdd:PRK07851 394 GGQGMAMVLERL 405
PLN02287 PLN02287
3-ketoacyl-CoA thiolase
37-420 6.12e-81

3-ketoacyl-CoA thiolase


Pssm-ID: 215161 [Multi-domain]  Cd Length: 452  Bit Score: 256.23  E-value: 6.12e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805  37 NDVVIVSATRTPI-GSFLGSLASQPATKLGTIAIQGAIEKAGIPKEEVKEVYMGNVIQGGEGQA-PTRQATLGAGLPIAT 114
Cdd:PLN02287  46 DDVVIVAAYRTPIcKAKRGGFKDTYPDDLLAPVLKAVVEKTGLNPSEVGDIVVGTVLAPGSQRAnECRMAAFYAGFPETV 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 115 PCTTVNKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMSRGATPyggvKLEDL-IVKDGLtdvynkIHMGNC 193
Cdd:PLN02287 126 PVRTVNRQCSSGLQAVADVAAAIKAGFYDIGIGAGVESMTTNPMAWEGGVNP----RVESFsQAQDCL------LPMGIT 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 194 AENTAKKLSISREEQDKYAIGSYTRSKEAWDAGKFANEITPITISVK------GKPDVVVKEDEEYKRVDFSKVPKLKTV 267
Cdd:PLN02287 196 SENVAERFGVTREEQDQAAVESHRKAAAATASGKFKDEIVPVHTKIVdpktgeEKPIVISVDDGIRPNTTLADLAKLKPV 275
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 268 FqKENGTVTAANASTLNDGAAAVVLMTAEAAQRLKVKPLARIAAFADAAVDPIDFPLAPAYAVPKVLKYAGLKKEDIAMW 347
Cdd:PLN02287 276 F-KKNGTTTAGNSSQVSDGAGAVLLMKRSVAMQKGLPILGVFRSFAAVGVDPAVMGIGPAVAIPAAVKAAGLELDDIDLF 354
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 401461805 348 EVNEAFSVVVLANIKMLEIDPQKVNVHGGAVSLGHPIGMSGARIVVHLAHALKQ----GEFGLASICNGGG-GASAVL 420
Cdd:PLN02287 355 EINEAFASQFVYCCKKLGLDPEKVNVNGGAIALGHPLGATGARCVATLLHEMKRrgkdCRFGVVSMCIGTGmGAAAVF 432
PRK07801 PRK07801
acetyl-CoA C-acetyltransferase;
41-424 1.39e-80

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181123 [Multi-domain]  Cd Length: 382  Bit Score: 253.09  E-value: 1.39e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805  41 IVSATRTPIGSFLGSLASQPATKLGTIAIQGAIEKAGIPKEEVKEVYMGNVIQGGeGQAP--TRQATLGAGLPIATPCTT 118
Cdd:PRK07801   6 IVDAVRTPVGKRKGGLAGVHPADLGAHVLKGLVDRTGIDPAAVDDVIFGCVDTIG-PQAGniARTSWLAAGLPEEVPGVT 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 119 VNKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMSRGA-------TPYGGVKledlivkdGLTDVYNK--IH 189
Cdd:PRK07801  85 VDRQCGSSQQAIHFAAQAVMSGTQDLVVAGGVQNMSQIPISSAMTAgeqlgftSPFAESK--------GWLHRYGDqeVS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 190 MGNCAENTAKKLSISREEQDKYAIGSYTRSKEAWDAGKFANEITPITisvkgkpDVVVkeDEEYKRVDFSKVPKLKTVFq 269
Cdd:PRK07801 157 QFRGAELIAEKWGISREEMERFALESHRRAFAAIRAGRFDNEIVPVG-------GVTV--DEGPRETSLEKMAGLKPLV- 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 270 kENGTVTAANASTLNDGAAAVVLMTAEAAQRLKVKPLARIAAFADAAVDPIDFPLAPAYAVPKVLKYAGLKKEDIAMWEV 349
Cdd:PRK07801 227 -EGGRLTAAVASQISDGASAVLLASERAVKRHGLTPRARIHHLSVRGDDPVFMLTAPIPATRYALEKTGLSIDDIDVVEI 305
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 401461805 350 NEAFSVVVLANIKMLEIDPQKVNVHGGAVSLGHPIGMSGARIVVHLAHALKQ--GEFGLASICNGGGGASAVLIEKL 424
Cdd:PRK07801 306 NEAFAPVVLAWLKETGADPAKVNPNGGAIALGHPLGATGAKLMTTLLHELERtgGRYGLQTMCEGGGTANVTIIERL 382
PRK07661 PRK07661
acetyl-CoA C-acetyltransferase;
36-419 5.98e-80

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181072 [Multi-domain]  Cd Length: 391  Bit Score: 251.98  E-value: 5.98e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805  36 LNDVVIVSATRTPIG-SFLGSLASQPATKLGTIAIQGAIEKAGIPKEEVKEVYMGNVIQGGE-GQAPTRQATLGAGLPIA 113
Cdd:PRK07661   1 MREAVIVAGARTPVGkAKKGSLKTVRPDDLGALVVKETLKRAGNYEGPIDDLIIGCAMPEAEqGLNMARNIGALAGLPYT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 114 TPCTTVNKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVmsrgatpyGGVKLEDLIVKDGLTDVYnkIHMGNC 193
Cdd:PRK07661  81 VPAITINRYCSSGLQSIAYGAERIMLGHSEAVIAGGAESMSLVPMM--------GHVVRPNPRLVEAAPEYY--MGMGHT 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 194 AENTAKKLSISREEQDKYAIGSYTRSKEAWDAGKFANEITPITISVK-----GKP---DVVVKEDEEYkRVDFSK--VPK 263
Cdd:PRK07661 151 AEQVAVKYGISREDQDAFAVRSHQRAAKALAEGKFADEIVPVDVTLRtvgenNKLqeeTITFSQDEGV-RADTTLeiLGK 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 264 LKTVFQKeNGTVTAANASTLNDGAAAVVLMTAEAAQRLKVKPLARIAAFADAAVDPIDFPLAPAYAVPKVLKYAGLKKED 343
Cdd:PRK07661 230 LRPAFNV-KGSVTAGNSSQMSDGAAAVLLMDREKAESDGLKPLAKFRSFAVAGVPPEVMGIGPIAAIPKALKLAGLELSD 308
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 401461805 344 IAMWEVNEAFSVVVLANIKMLEIDPQKVNVHGGAVSLGHPIGMSGARIVVHLAHALK-QGE-FGLASICNGGG-GASAV 419
Cdd:PRK07661 309 IGLFELNEAFASQSIQVIRELGLDEEKVNVNGGAIALGHPLGCTGAKLTLSLIHEMKrRNEqFGIVTMCIGGGmGAAGV 387
PRK09052 PRK09052
acetyl-CoA C-acyltransferase;
36-424 5.69e-77

acetyl-CoA C-acyltransferase;


Pssm-ID: 181626 [Multi-domain]  Cd Length: 399  Bit Score: 244.53  E-value: 5.69e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805  36 LNDVVIVSATRTPIG-SFLGSLASQPATKLGTIAIQGAIEKA-GIPKEEVKEVYMGNVIQGGE-GQAPTRQATLGAGLPI 112
Cdd:PRK09052   5 LQDAYIVAATRTPVGkAPRGMFKNTRPDDLLAHVLRSAVAQVpGLDPKLIEDAIVGCAMPEAEqGLNVARIGALLAGLPN 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 113 ATPCTTVNKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMSRGA-TPYGGVKLEDLIVKDGltdvynkihMG 191
Cdd:PRK09052  85 SVGGVTVNRFCASGLQAVAMAADRIRVGEADVMIAAGVESMSMVPMMGNKPSmSPAIFARDENVGIAYG---------MG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 192 NCAENTAKKLSISREEQDKYAIGSYTRSKEAWDAGKFANEITPITISVKgKPD-----VVVKEDE----EYKRVDFS--K 260
Cdd:PRK09052 156 LTAEKVAEQWKVSREDQDAFALESHQKAIAAQQAGEFKDEITPYEITER-FPDlatgeVDVKTRTvdldEGPRADTSleG 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 261 VPKLKTVFQKEnGTVTAANASTLNDGAAAVVLMTAEAAQRLKVKPLARIAAFADAAVDPIDFPLAPAYAVPKVLKYAGLK 340
Cdd:PRK09052 235 LAKLKPVFANK-GSVTAGNSSQTSDGAGAVILVSEKALKQFNLTPLARFVSFAVAGVPPEIMGIGPIEAIPAALKQAGLK 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 341 KEDIAMWEVNEAFSVVVLANIKMLEIDPQKVNVHGGAVSLGHPIGMSGARIVVHLAHAL--KQGEFGLASICNGGGGASA 418
Cdd:PRK09052 314 QDDLDWIELNEAFAAQSLAVIRDLGLDPSKVNPLGGAIALGHPLGATGAIRTATVVHGLrrTNLKYGMVTMCVGTGMGAA 393

                 ....*.
gi 401461805 419 VLIEKL 424
Cdd:PRK09052 394 GIFERL 399
PRK06504 PRK06504
acetyl-CoA C-acetyltransferase;
41-424 1.64e-76

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180595 [Multi-domain]  Cd Length: 390  Bit Score: 243.10  E-value: 1.64e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805  41 IVSATRTPIGSFLGSLASQPATKLGTIAIQGAIEKAGIPKEEVKEVYMGNVIQGGEgQAPT--RQATLGAGLPIATPCTT 118
Cdd:PRK06504   6 IVAAARTAGGRKGGRLAGWHPADLAAQVLDALVDRSGADPALIEDVIMGCVSQVGE-QATNvaRNAVLASKLPESVPGTS 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 119 VNKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPyvMSRGATpyggvkledLIVKDGLTDV--------YNKIH- 189
Cdd:PRK06504  85 IDRQCGSSQQALHFAAQAVMSGTMDIVIAAGVESMTRVP--MGSPST---------LPAKNGLGHYkspgmeerYPGIQf 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 190 ---MGncAENTAKKLSISREEQDKYAIGSYTRSKEAWDAGKFANEITPITISVKGKPDVVVKEDEEYkRVDFS--KVPKL 264
Cdd:PRK06504 154 sqfTG--AEMMAKKYGLSKDQLDEFALQSHQRAIAATQAGKFKAEIVPLEITRADGSGEMHTVDEGI-RFDATleGIAGV 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 265 KTVfqKENGTVTAANASTLNDGAAAVVLMTAEAAQRLKVKPLARIAAFADAAVDPIDFPLAPAYAVPKVLKYAGLKKEDI 344
Cdd:PRK06504 231 KLI--AEGGRLTAATASQICDGASGVMVVNERGLKALGVKPLARIHHMTVIGGDPVIMLEAPLPATERALKKAGMKIDDI 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 345 AMWEVNEAFSVVVLANIKMLEIDPQKVNVHGGAVSLGHPIGMSGARIVVHLAHALKQ--GEFGLASICNGGGGASAVLIE 422
Cdd:PRK06504 309 DLYEVNEAFASVPLAWLKATGADPERLNVNGGAIALGHPLGASGTKLMTTLVHALKQrgKRYGLQTMCEGGGMANVTIVE 388

                 ..
gi 401461805 423 KL 424
Cdd:PRK06504 389 RL 390
fadI PRK08963
3-ketoacyl-CoA thiolase; Reviewed
39-420 2.79e-75

3-ketoacyl-CoA thiolase; Reviewed


Pssm-ID: 181597 [Multi-domain]  Cd Length: 428  Bit Score: 241.04  E-value: 2.79e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805  39 VVIVSATRTPIGSFLGSLASQPATKLGTIAIQGAIEKAGIPKEEVKEVYMGNVIQGGEGQAPTRQATLGAGLPIATPCTT 118
Cdd:PRK08963   7 IAIVSGLRTPFAKQATAFHGIPAVDLGKMVVGELLARSEIDPELIEQLVFGQVVQMPEAPNIAREIVLGTGMNVHTDAYS 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 119 VNKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMSRG-----------------ATPYGGVKLEDLI-VKDG 180
Cdd:PRK08963  87 VSRACATSFQAVANVAESIMAGTIDIGIAGGADSSSVLPIGVSKKlaralvdlnkartlgqrLKLFSRLRLRDLLpVPPA 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 181 LTDVYNKIHMGNCAENTAKKLSISREEQDKYAIGSYTRSKEAWDAGKFANEITPITISVKGKP---DVVVKEDEeykrvD 257
Cdd:PRK08963 167 VAEYSTGLRMGDTAEQMAKTYGISREEQDALAHRSHQLAAQAWAEGKLDDEVMTAHVPPYKQPleeDNNIRGDS-----T 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 258 FSKVPKLKTVFQKENGTVTAANASTLNDGAAAVVLMTAEAAQRLKVKPLARIAAFADAAVDPI-DFPLAPAYAVPKVLKY 336
Cdd:PRK08963 242 LEDYAKLRPAFDRKHGTVTAANSTPLTDGAAAVLLMSESRAKALGLTPLGYLRSYAFAAIDVWqDMLLGPAYATPLALER 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 337 AGLKKEDIAMWEVNEAFSVVVLANIKML-----------------EIDPQKVNVHGGAVSLGHPIGMSGARIVVHLAHAL 399
Cdd:PRK08963 322 AGLTLADLTLIDMHEAFAAQTLANLQMFaserfareklgrsqaigEVDMSKFNVLGGSIAYGHPFAATGARMITQTLHEL 401
                        410       420
                 ....*....|....*....|....
gi 401461805 400 KQ--GEFGLASICNGGG-GASAVL 420
Cdd:PRK08963 402 RRrgGGLGLTTACAAGGlGAAMVL 425
PRK07850 PRK07850
steroid 3-ketoacyl-CoA thiolase;
40-424 1.12e-74

steroid 3-ketoacyl-CoA thiolase;


Pssm-ID: 181145 [Multi-domain]  Cd Length: 387  Bit Score: 238.08  E-value: 1.12e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805  40 VIVSATRTPIGSFLGSLASQPATKLGTIAIQGAIEKAGIPKEEVKEVYMGNVIQGGE-GQAPTRQATLGAGLPIATPCTT 118
Cdd:PRK07850   5 VIVEAVRTPIGKRNGWLSGLHAAELLGAVQRAVLDRAGIDPGDVEQVIGGCVTQAGEqSNNITRTAWLHAGLPYHVGATT 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 119 VNKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPyvMSRGATPYGGvkledlivkDGLTDVYNkIHMGN---CAE 195
Cdd:PRK07850  85 IDCQCGSAQQANHLVAGLIAAGAIDVGIACGVEAMSRVP--LGANAGPGRG---------LPRPDSWD-IDMPNqfeAAE 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 196 NTAKKLSISREEQDKYAIGSYTRSKEAWDAGKFANEITPITISV---KGKP---DVVVKEDEEYKRVDFSKVPKLKTVFq 269
Cdd:PRK07850 153 RIAKRRGITREDVDAFGLRSQRRAAQAWAEGRFDREISPVQAPVldeEGQPtgeTRLVTRDQGLRDTTMEGLAGLKPVL- 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 270 kENGTVTAANASTLNDGAAAVVLMTAEAAQRLKVKPLARIAAFADAAVDPIDFPLAPAYAVPKVLKYAGLKKEDIAMWEV 349
Cdd:PRK07850 232 -EGGIHTAGTSSQISDGAAAVLWMDEDRARALGLRPRARIVAQALVGAEPYYHLDGPVQATAKVLEKAGMKIGDIDLVEI 310
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 401461805 350 NEAFSVVVLANIKMLEIDPQKVNVHGGAVSLGHPIGMSGARIVVHLAHALKQ--GEFGLASICNGGGGASAVLIEKL 424
Cdd:PRK07850 311 NEAFASVVLSWAQVHEPDMDKVNVNGGAIALGHPVGSTGARLITTALHELERtdKSTALITMCAGGALSTGTIIERI 387
fadA PRK08947
3-ketoacyl-CoA thiolase; Reviewed
37-424 2.34e-74

3-ketoacyl-CoA thiolase; Reviewed


Pssm-ID: 181592 [Multi-domain]  Cd Length: 387  Bit Score: 237.17  E-value: 2.34e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805  37 NDVVIVSATRTPIG-SFLGSLASQPATKLGTIAIQGAIEK-AGIPKEEVKEVYMGNVIQGGE-GQAPTRQATLGAGLPIA 113
Cdd:PRK08947   2 EDVVIVDAIRTPMGrSKGGAFRNVRAEDLSAHLMRSLLARnPALDPAEIDDIIWGCVQQTLEqGFNIARNAALLAGIPHS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 114 TPCTTVNKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPyvMSRGATPYggvkledlivkDGLTDVYNKIH--MG 191
Cdd:PRK08947  82 VPAVTVNRLCGSSMQALHDAARAIMTGDGDVFLIGGVEHMGHVP--MNHGVDFH-----------PGLSKNVAKAAgmMG 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 192 NCAENTAKKLSISREEQDKYAIGSYTRSKEAWDAGKFANEITPITisvkGKpdvvvKEDEEYKRVDFSKV---------- 261
Cdd:PRK08947 149 LTAEMLGKMHGISREQQDAFAARSHQRAWAATQEGRFKNEIIPTE----GH-----DADGVLKLFDYDEVirpettveal 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 262 PKLKTVFQKENGTVTAANASTLNDGAAAVVLMTAEAAQRLKVKPLARIAAFADAAVDPIDFPLAPAYAVPKVLKYAGLKK 341
Cdd:PRK08947 220 AALRPAFDPVNGTVTAGTSSALSDGASAMLVMSESRAKELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSI 299
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 342 EDIAMWEVNEAF---SVVVLANIKMLEIDPQKVNVHGGAVSLGHPIGMSGARIVVHLAHALKQ--GEFGLASICNGGGGA 416
Cdd:PRK08947 300 SDIDVFELNEAFaaqSLPCLKDLGLLDKMDEKVNLNGGAIALGHPLGCSGARISTTLLNLMERkdAQFGLATMCIGLGQG 379

                 ....*...
gi 401461805 417 SAVLIEKL 424
Cdd:PRK08947 380 IATVFERV 387
PRK08170 PRK08170
acetyl-CoA C-acetyltransferase;
38-424 2.20e-73

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181265 [Multi-domain]  Cd Length: 426  Bit Score: 236.07  E-value: 2.20e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805  38 DVVIVSATRTP-------IGSFLGS-LASQPATKLgtiaiqgaIEKAGIPKEEVKEVYMGNVIQGGEGQAPTRQATLGAG 109
Cdd:PRK08170   4 PVYIVDGARTPflkarggPGPFSASdLAVAAGRAL--------LNRQPFAPDDLDEVILGCAMPSPDEANIARVVALRLG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 110 LPIATPCTTVNKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMSRGATPY---------GGVKLEDL----- 175
Cdd:PRK08170  76 CGEKVPAWTVQRNCASGMQALDSAAANIALGRADLVLAGGVEAMSHAPLLFSEKMVRWlagwyaaksIGQKLAALgklrp 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 176 --------IVKdGLTDVYNKIHMGNCAENTAKKLSISREEQDKYAIGSYTRSKEAWDAGKFAnEITPItISVKGKpdvvV 247
Cdd:PRK08170 156 sylapvigLLR-GLTDPVVGLNMGQTAEVLAHRFGITREQMDAYAARSHQRLAAAQAEGRLK-EVVPL-FDRDGK----F 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 248 KEDEEYKRVDFS--KVPKLKTVFQKENGTVTAANASTLNDGAAAVVLMTAEAAQRLKVKPLARIAAFADAAVDPIDFPLA 325
Cdd:PRK08170 229 YDHDDGVRPDSSmeKLAKLKPFFDRPYGRVTAGNSSQITDGACWLLLASEEAVKKYGLPPLGRIVDSQWAALDPSQMGLG 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 326 PAYAVPKVLKYAGLKKEDIAMWEVNEAFSVVVLANIKML-----------------EIDPQKVNVHGGAVSLGHPIGMSG 388
Cdd:PRK08170 309 PVHAATPLLQRHGLTLEDLDLWEINEAFAAQVLACLAAWadeeycreqlgldgalgELDRERLNVDGGAIALGHPVGASG 388
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 401461805 389 ARIVVHLAHALKQ--GEFGLASICNGGGGASAVLIEKL 424
Cdd:PRK08170 389 ARIVLHLLHALKRrgTKRGIAAICIGGGQGGAMLLERV 426
PRK06690 PRK06690
acetyl-CoA C-acyltransferase;
37-424 4.31e-69

acetyl-CoA C-acyltransferase;


Pssm-ID: 180659 [Multi-domain]  Cd Length: 361  Bit Score: 222.72  E-value: 4.31e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805  37 NDVVIVSATRTPIGSFLGSLASQPATKLGTIAIQgaIEKAGIPkEEVKEVYMGNVIQGGEGQAptRQATLGAGLPIATPC 116
Cdd:PRK06690   1 NRAVIVEAKRTPIGKKNGMLKDYEVQQLAAPLLT--FLSKGME-REIDDVILGNVVGPGGNVA--RLSALEAGLGLHIPG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 117 TTVNKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMSRGATPyggvkledlivkdgltDVYNKIHMGNCAEN 196
Cdd:PRK06690  76 VTIDRQCGAGLEAIRTACHFIQGGAGKCYIAGGVESTSTSPFQNRARFSP----------------ETIGDPDMGVAAEY 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 197 TAKKLSISREEQDKYAIGSYTRSKEAWDAGKFANEITPITisvkGKPDVVVKEDEEYKRVdfskVPKLKTVFQKeNGTVT 276
Cdd:PRK06690 140 VAERYNITREMQDEYACLSYKRTLQALEKGYIHEEILSFN----GLLDESIKKEMNYERI----IKRTKPAFLH-NGTVT 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 277 AANASTLNDGAAAVVLMTAEAAQRLKVKPLARIAAFADAAVDPIDFPLAPAYAVPKVLKYAGLKKEDIAMWEVNEAFSVV 356
Cdd:PRK06690 211 AGNSCGVNDGACAVLVMEEGQARKLGYKPVLRFVRSAVVGVDPNLPGTGPIFAVNKLLNEMNMKVEDIDYFEINEAFASK 290
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 357 VLANIKMLEIDPQKVNVHGGAVSLGHPIGMSGARIVVHLAHALKQ--GEFGLASICNGGGGASAVLIEKL 424
Cdd:PRK06690 291 VVACAKELQIPYEKLNVNGGAIALGHPYGASGAMLVTRLFYQAKRedMKYGIATLGIGGGIGLALLFEKV 360
PRK08242 PRK08242
acetyl-CoA C-acetyltransferase;
38-424 3.65e-64

acetyl-CoA C-acetyltransferase;


Pssm-ID: 236197 [Multi-domain]  Cd Length: 402  Bit Score: 211.28  E-value: 3.65e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805  38 DVVIVSATRTPIGSFL--GSLASQPATKLGTIAIQGAIEKAGIPKEEVKEVYMGNVIQGGE-GQAPTRQATLGAGLPIAT 114
Cdd:PRK08242   3 EAYIYDAVRTPRGKGKkdGSLHEVKPVRLAAGLLEALRDRNGLDTAAVDDVVLGCVTPVGDqGADIARTAVLAAGLPETV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 115 PCTTVNKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMSRGATPyggvkledliVKDGLTDVYNKIHMGNCA 194
Cdd:PRK08242  83 PGVQINRFCASGLEAVNLAAAKVRSGWDDLVIAGGVESMSRVPMGSDGGAWA----------MDPSTNFPTYFVPQGISA 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 195 ENTAKKLSISREEQDKYAIGSYTRSKEAWDAGKFANEITPitisVKGKPDVVVKEDEEYKR--VDFSKVPKLKTVFQ--- 269
Cdd:PRK08242 153 DLIATKYGFSREDVDAYAVESQQRAAAAWAEGYFAKSVVP----VKDQNGLTILDHDEHMRpgTTMESLAKLKPSFAmmg 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 270 -----------------KENGTVTAANASTLNDGAAAVVLMTAEAAQRLKVKPLARIAAFADAAVDPIDFPLAPAYAVPK 332
Cdd:PRK08242 229 emggfdavalqkypeveRINHVHHAGNSSGIVDGAAAVLIGSEEAGKALGLKPRARIVATATIGSDPTIMLTGPVPATRK 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 333 VLKYAGLKKEDIAMWEVNEAFSVVVLANIKMLEIDPQKVNVHGGAVSLGHPIGMSGARIVVHLAHAL--KQGEFGLASIC 410
Cdd:PRK08242 309 ALAKAGLTVDDIDLFELNEAFASVVLRFMQALDIPHDKVNVNGGAIAMGHPLGATGAMILGTVLDELerRGKRTALITLC 388
                        410
                 ....*....|....
gi 401461805 411 NGGGGASAVLIEKL 424
Cdd:PRK08242 389 VGGGMGIATIIERV 402
PRK09268 PRK09268
acetyl-CoA C-acetyltransferase;
34-423 3.50e-55

acetyl-CoA C-acetyltransferase;


Pssm-ID: 236440 [Multi-domain]  Cd Length: 427  Bit Score: 188.57  E-value: 3.50e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805  34 PTLNDVVIVSATRTPIGSFLGSLASQPATKLGTIAIQGAIEKAGIPKEEVKEVYMGNVIQGGEGQAPTRQATLGAGLPIA 113
Cdd:PRK09268   4 PTVRRVAILGGNRIPFARSNGAYADASNQDMLTAALDGLVDRFGLQGERLGEVVAGAVLKHSRDFNLTRECVLGSALSPY 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 114 TPCTTVNKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMS-----------RGATPYGGVKL------EDLI 176
Cdd:PRK09268  84 TPAYDLQQACGTGLEAAILVANKIALGQIDSGIAGGVDTTSDAPIAVNeglrkillelnRAKTTGDRLKAlgklrpKHLA 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 177 V--------KDGLTdvynkihMGNCAENTAKKLSISREEQDKYAIGSYTRSKEAWDAGKFANEITPItisvKGkpdvvVK 248
Cdd:PRK09268 164 PeiprngepRTGLS-------MGEHAAITAKEWGISREAQDELAAASHQNLAAAYDRGFFDDLITPF----LG-----LT 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 249 EDEEYkRVDFS--KVPKLKTVFQK-ENGTVTAANASTLNDGAAAVVLMTAEAAQRLKVKPLARIAAFADAAVDPIDFP-- 323
Cdd:PRK09268 228 RDNNL-RPDSSleKLAKLKPVFGKgGRATMTAGNSTPLTDGASVVLLASEEWAAEHGLPVLAYLVDAETAAVDFVHGKeg 306
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 324 --LAPAYAVPKVLKYAGLKKEDIAMWEVNEAFSVVVLANIKMLE-----------------IDPQKVNVHGGAVSLGHPI 384
Cdd:PRK09268 307 llMAPAYAVPRLLARNGLTLQDFDFYEIHEAFASQVLATLKAWEdeeycrerlgldaplgsIDRSKLNVNGSSLAAGHPF 386
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 401461805 385 GMSGARIVVHLAHAL--KQGEFGLASICNGGGGASAVLIEK 423
Cdd:PRK09268 387 AATGGRIVATLAKLLaeKGSGRGLISICAAGGQGVTAILER 427
Thiolase_C pfam02803
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
303-423 2.46e-53

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: 173.98  E-value: 2.46e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805  303 VKPLARIAAFADAAVDPIDFPLAPAYAVPKVLKYAGLKKEDIAMWEVNEAFSVVVLANIKMLEIDPQKVNVHGGAVSLGH 382
Cdd:pfam02803   1 LKPLARIRSYATAGVDPAIMGIGPAYAIPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGIDPEKVNVNGGAIALGH 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 401461805  383 PIGMSGARIVVHLAHALKQ--GEFGLASICNGGGGASAVLIEK 423
Cdd:pfam02803  81 PLGASGARILVTLLHELKRrgGKYGLASLCIGGGQGVAMIIER 123
PRK06025 PRK06025
acetyl-CoA C-acetyltransferase;
38-424 1.07e-51

acetyl-CoA C-acetyltransferase;


Pssm-ID: 235675 [Multi-domain]  Cd Length: 417  Bit Score: 178.82  E-value: 1.07e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805  38 DVVIVSATRTP--IGSF-LGSLASQPATKLGTIAIQGAIEKAGIPKEEVKEVYMGNVIQ-GGEGQAPTRQATLGAGLPIA 113
Cdd:PRK06025   3 EAYIIDAVRTPrgIGKVgKGALAHLHPQHLAATVLKALAERNGLNTADVDDIIWSTSSQrGKQGGDLGRMAALDAGYDIK 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 114 TPCTTVNKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMS----NVPYVMSRGATPYGgvkledliVKDG---LTDVYN 186
Cdd:PRK06025  83 ASGVTLDRFCGGGITSVNLAAAQIMSGMEDLVIAGGTEMMSytaaMAAEDMAAGKPPLG--------MGSGnlrLRALHP 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 187 KIHMGNCAENTAKKLSISREEQDKYAIGSYTRSKEAWDAGKFANEITPITisvkgKPDVVVKED-EEYKRVDFSK--VPK 263
Cdd:PRK06025 155 QSHQGVCGDAIATMEGITREALDALGLESQRRAARAIKEGRFDKSLVPVY-----RDDGSVALDhEEFPRPQTTAegLAA 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 264 LKTVFQK-------ENGTV------------------TAANASTLNDGAAAVVLMTAEAAQRLKVKPLARIAAFADAAVD 318
Cdd:PRK06025 230 LKPAFTAiadypldDKGTTyrglinqkypdleikhvhHAGNSSGVVDGAAALLLASKAYAEKHGLKPRARIVAMANMGDD 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 319 PIDFPLAPAYAVPKVLKYAGLKKEDIAMWEVNEAFSVVVLANIKMLEIDPQKVNVHGGAVSLGHPIGMSGARIVVHLAHA 398
Cdd:PRK06025 310 PTLMLNAPVPAAKKVLAKAGLTKDDIDLWEINEAFAVVAEKFIRDLDLDRDKVNVNGGAIALGHPIGATGSILIGTVLDE 389
                        410       420
                 ....*....|....*....|....*...
gi 401461805 399 LKQ--GEFGLASICNGGGGASAVLIEKL 424
Cdd:PRK06025 390 LERrgLKRGLVTMCAAGGMAPAIIIERV 417
nondecarbox_cond_enzymes cd00826
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ...
42-422 3.08e-51

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: 177.30  E-value: 3.08e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805  42 VSATRTPIGSF---LGSLASQPATKLGTIAIQGAIEKAGIPKEEVKEVYMGNVIQGGEGQAPTRQATLGAGLPIATPCTT 118
Cdd:cd00826    1 AGAAMTAFGKFggeNGADANDLAHEAGAKAIAAALEPAGVAAGAVEEACLGQVLGAGEGQNCAQQAAMHAGGLQEAPAIG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 119 VNKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSnvpYVMSRGATPYggvKLEDLIVKDGltdvynkihmgncaenta 198
Cdd:cd00826   81 MNNLCGSGLRALALAMQLIAGGDANCILAGGFEKME---TSAENNAKEK---HIDVLINKYG------------------ 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 199 kklsiSREEQDKYAIGSYTRSKEAWDAGKFANEITPITisVKGKPDVVVKEDEEYKR----VDFSKVPKLKTVFQKEnGT 274
Cdd:cd00826  137 -----MRACPDAFALAGQAGAEAAEKDGRFKDEFAKFG--VKGRKGDIHSDADEYIQfgdeASLDEIAKLRPAFDKE-DF 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 275 VTAANASTLNDGAAAVVLMTAEAAQ-------RLKVKPLARIAAFADAAVDPIDFPLA----PAYAVPKVLKYAGLKKED 343
Cdd:cd00826  209 LTAGNACGLNDGAAAAILMSEAEAQkhglqskAREIQALEMITDMASTFEDKKVIKMVggdgPIEAARKALEKAGLGIGD 288
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 344 IAMWEVNEAFSVVVLANIKMLEIDPQK------------------VNVHGGAVSLGHPIGMSGARIVVHLAHALKQGEF- 404
Cdd:cd00826  289 LDLIEAHDAFAANACATNEALGLCPEGqggalvdrgdntyggksiINPNGGAIAIGHPIGASGAAICAELCFELKGEAGk 368
                        410       420
                 ....*....|....*....|....
gi 401461805 405 ------GLASICNGGGGASAVLIE 422
Cdd:cd00826  369 rqgagaGLALLCIGGGGGAAMCIE 392
SCP-x_thiolase cd00829
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ...
64-419 1.90e-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: 80.39  E-value: 1.90e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805  64 LGTIAIQGAIEKAGIPKEEVKEVYMGNVIQGGEGQAPTRQATLGAGLPIAtPCTTVNKVCASGMKAIMMASQSLMCGHQD 143
Cdd:cd00829   19 LAAEAARAALDDAGLEPADIDAVVVGNAAGGRFQSFPGALIAEYLGLLGK-PATRVEAAGASGSAAVRAAAAAIASGLAD 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 144 VMVAGGMESMSNVPYVMSRGATPyGGVKLEDLIVKDGLT--DVYnkihmGNCAENTAKKLSISREEQDKYAIGSY---TR 218
Cdd:cd00829   98 VVLVVGAEKMSDVPTGDEAGGRA-SDLEWEGPEPPGGLTppALY-----ALAARRYMHRYGTTREDLAKVAVKNHrnaAR 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 219 SKEAWdagkFANEITPitisvkgkpdvvvkedEEYKrvdfsKVPKLktvfqkeNGTVTAANASTLNDGAAAVVLMTAEAA 298
Cdd:cd00829  172 NPYAQ----FRKPITV----------------EDVL-----NSRMI-------ADPLRLLDCCPVSDGAAAVVLASEERA 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 299 QRLKVKPL----ARIAAFADAAVDPIDFPLAPA--YAVPKVLKYAGLKKEDIAMWEVNEAFSVVVLANIKML-------- 364
Cdd:cd00829  220 RELTDRPVwilgVGAASDTPSLSERDDFLSLDAarLAARRAYKMAGITPDDIDVAELYDCFTIAELLALEDLgfcekgeg 299
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 401461805 365 -------EIDPQ---KVNVHGGAVSLGHPIGMSGARIVVHL---------AHALKQGEFGLASicNGGGGASAV 419
Cdd:cd00829  300 gklvregDTAIGgdlPVNTSGGLLSKGHPLGATGLAQAVEAvrqlrgeagARQVPGARVGLAH--NIGGTGSAA 371
PRK06064 PRK06064
thiolase domain-containing protein;
36-421 8.90e-13

thiolase domain-containing protein;


Pssm-ID: 235688 [Multi-domain]  Cd Length: 389  Bit Score: 69.16  E-value: 8.90e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805  36 LNDVVIVSATRTPIGSF----LGSLASQpatklgtiAIQGAIEKAGIPKEEVKEVYMGNVIQGGEGQAPTRQATLG--AG 109
Cdd:PRK06064   1 MRDVAIIGVGQTKFGELwdvsLRDLAVE--------AGLEALEDAGIDGKDIDAMYVGNMSAGLFVSQEHIAALIAdyAG 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 110 L-PIatPCTTVNKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPY-----VMSR----------GATPyggvkle 173
Cdd:PRK06064  73 LaPI--PATRVEAACASGGAALRQAYLAVASGEADVVLAAGVEKMTDVPTpdateAIARagdyeweeffGATF------- 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 174 dlivkDGLTDVYNKIHMgncaentaKKLSISREEQDKYAIGSYTRSKEAWDAgKFANEITpitisvkgkPDVVVKEdeey 253
Cdd:PRK06064 144 -----PGLYALIARRYM--------HKYGTTEEDLALVAVKNHYNGSKNPYA-QFQKEIT---------VEQVLNS---- 196
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 254 krvdfSKVPKLKTVFqkengtvtaaNASTLNDGAAAVVLMTAEAAQRLKVKPLARIAAFADAavDPI------DFPL--A 325
Cdd:PRK06064 197 -----PPVADPLKLL----------DCSPITDGAAAVILASEEKAKEYTDTPVWIKASGQAS--DTIalhdrkDFTTldA 259
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 326 PAYAVPKVLKYAGLKKEDIAMWEVNEAFSVVVLANIKML-----------------EIDPQ-KVNVHGGAVSLGHPIGMS 387
Cdd:PRK06064 260 AVVAAEKAYKMAGIEPKDIDVAEVHDCFTIAEILAYEDLgfakkgeggklaregqtYIGGDiPVNPSGGLKAKGHPVGAT 339
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 401461805 388 GARIVVHLAHALKQG-----------EFGLASICNGGGGASAVLI 421
Cdd:PRK06064 340 GVSQAVEIVWQLRGEaekgrqqvigaGYGLTHNVGGTGHTAVVHI 384
cond_enzymes cd00327
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ...
61-421 6.41e-12

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: 65.16  E-value: 6.41e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805  61 ATKLGTIAIQGAIEKAGIPKEEVKEVYMGNVIQGGEGQAPTRQATLGAGLPIAtPCTTVNKVCASGMKAIMMASQSLMCG 140
Cdd:cd00327    7 ASELGFEAAEQAIADAGLSKGPIVGVIVGTTGGSGEFSGAAGQLAYHLGISGG-PAYSVNQACATGLTALALAVQQVQNG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 141 HQDVMVAGGMESmsnvpyvmsrgatpyggvkledlivkdgltdvynkihmgncaentakklsisreeqdkyaigsytrsk 220
Cdd:cd00327   86 KADIVLAGGSEE-------------------------------------------------------------------- 97
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 221 eawdagkfaneitpitisvkgkpdvvvkedeeykrvdfskvpklktvfqkengtvtaanaSTLNDGAAAVVLMTAEAAQR 300
Cdd:cd00327   98 ------------------------------------------------------------FVFGDGAAAAVVESEEHALR 117
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 301 LKVKPLARIAAFADAAVDPIDFPL----APAYAVPKVLKYAGLKKEDIAMWEVNEAFSVVVLANIKMLEIDPQKV---NV 373
Cdd:cd00327  118 RGAHPQAEIVSTAATFDGASMVPAvsgeGLARAARKALEGAGLTPSDIDYVEAHGTGTPIGDAVELALGLDPDGVrspAV 197
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 401461805 374 HGGAVSLGHPIGMSGARIVVHLAHALKQGEF---------GLASICNGGGGASAVLI 421
Cdd:cd00327  198 SATLIMTGHPLGAAGLAILDELLLMLEHEFIpptpreprtVLLLGFGLGGTNAAVVL 254
PRK06157 PRK06157
acetyl-CoA acetyltransferase; Validated
68-392 1.72e-07

acetyl-CoA acetyltransferase; Validated


Pssm-ID: 180433 [Multi-domain]  Cd Length: 398  Bit Score: 53.11  E-value: 1.72e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805  68 AIQGAIEKAGIPKEEVKEVYMGNVIQggegqaptRQATLGAGLPIAT-------PCTTVNKVCASGMKAIMMASQSLMCG 140
Cdd:PRK06157  34 AFLEALADAGIEPKDIDAAWFGTHYD--------EIGSGKSGTPLSRalrlpniPVTRVENFCATGSEAFRGAVYAVASG 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 141 HQDVMVAGGMESMSNvpyvmsrgaTPYGGVKLEDlivKDGLTDVYNkihmgncaentakkLSISREEQDKYAIGSYtRSK 220
Cdd:PRK06157 106 AYDIALALGVEKLKD---------TGYGGLPVAN---PGTLADMTM--------------PNVTAPGNFAQLASAY-AAK 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 221 EAWDAGKFANEITpiTISVKgkpdvvvkedeeyKRVDFSKVPKLKtvFQKENGTVTAANA------------STLNDGAA 288
Cdd:PRK06157 159 YGVSREDLKRAMA--HVSVK-------------SHANGARNPKAH--LRKAVTEEQVLKApmiagplglfdcCGVSDGAA 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 289 AVVLMTAEAAQRLK------VKPLARIAAFADAAVDP-IDFPLAPA--YAVPKVLKYAGLK--KEDIAMWEVNEAFSVVV 357
Cdd:PRK06157 222 AAIVTTPEIARALGkkdpvyVKALQLAVSNGWELQYNgWDGSYFPTtrIAARKAYREAGITdpREELSMAEVHDCFSITE 301
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 401461805 358 LANIKMLEIDPQ------------------KVNVHGGAVSLGHPIGMSGARIV 392
Cdd:PRK06157 302 LVTMEDLGLSERgqawrdvldgffdadgglPCQIDGGLKCFGHPIGASGLRML 354
PTZ00455 PTZ00455
3-ketoacyl-CoA thiolase; Provisional
68-400 2.27e-07

3-ketoacyl-CoA thiolase; Provisional


Pssm-ID: 240424 [Multi-domain]  Cd Length: 438  Bit Score: 52.59  E-value: 2.27e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805  68 AIQGAIEKAGIPKEE--VKEVYMGNVI------QGGEGQAPTR---QATLGAGLpIATPCTTVNKVCASGMKAIMMASQS 136
Cdd:PTZ00455  55 AIQGTLENTGLDGKAalVDKVVVGNFLgelfssQGHLGPAAVGslgQSGASNAL-LYKPAMRVEGACASGGLAVQSAWEA 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 137 LMCGHQDVMVAGGMESMSNVPyvmSRGATPYGGvKLEDLIVKDGLTDVYNKIHMGNCAENTAKKLSISREEQDKYAIGSY 216
Cdd:PTZ00455 134 LLAGTSDIALVVGVEVQTTVS---ARVGGDYLA-RAADYRRQRKLDDFTFPCLFAKRMKYIQEHGHFTMEDTARVAAKAY 209
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 217 TRSKEAWDAGKFANEITPITISVKGKPDVVVKEDEEYKrvdfskvPKLKTvfqkengtvtaANASTLNDGAAAVVLMTAE 296
Cdd:PTZ00455 210 ANGNKNPLAHMHTRKLSLEFCTGASDKNPKFLGNETYK-------PFLRM-----------TDCSQVSDGGAGLVLASEE 271
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 297 AAQRLKVKP--------LARIAAFADAAVDPIDFP--LAPAYAVPKVLKYAGLKKEDIAMWEVNEAFSVVVLANIKMLEI 366
Cdd:PTZ00455 272 GLQKMGLSPndsrlveiKSLACASGNLYEDPPDATrmFTSRAAAQKALSMAGVKPSDLQVAEVHDCFTIAELLMYEALGI 351
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 401461805 367 -DPQK-----------------VNVHGGAVSLGHPIGMSGARIVVHLAHALK 400
Cdd:PTZ00455 352 aEYGHakdlirngatalegripVNTGGGLLSFGHPVGATGVKQIMEVYRQMK 403
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
60-153 3.12e-06

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: 48.40  E-value: 3.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805   60 PATKLGTIAIQGAIEKAGIPKEEVKE----VYMGNVIQG-GEGQAPTRQATLGAGLPIATPCT----------------- 117
Cdd:pfam00109  86 PQQRLLLEAAWEALEDAGITPDSLDGsrtgVFIGSGIGDyAALLLLDEDGGPRRGSPFAVGTMpsviagrisyflglrgp 165
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 401461805  118 --TVNKVCASGMKAIMMASQSLMCGHQDVMVAGGMESM 153
Cdd:pfam00109 166 svTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLL 203
PRK06289 PRK06289
acetyl-CoA acetyltransferase; Provisional
68-397 4.58e-06

acetyl-CoA acetyltransferase; Provisional


Pssm-ID: 235771 [Multi-domain]  Cd Length: 403  Bit Score: 48.53  E-value: 4.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805  68 AIQGAIEKAGIPKEEVKEVYMGNVIqggeGQAPTRQATLGAGLPIA------TPCTTVNKVCASGMKAIMMASQSLMCGH 141
Cdd:PRK06289  33 VVDGTLAAAGVDADDIEVVHVGNFF----GELFAGQGHLGAMPATVhpalwgVPASRHEAACASGSVATLAAMADLRAGR 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 142 QDVMVAGGMESMSNVPYVMSR---GATPYGGVKLEDL-----IVKDGLTDVYNK------IHMGNCAENT---AKK--LS 202
Cdd:PRK06289 109 YDVALVVGVELMKTVPGDVAAehlGAAAWTGHEGQDArfpwpSMFARVADEYDRrygldeEHLRAIAEINfanARRnpNA 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 203 ISReeqdkyaigSYTRSKEAWDAGKFANEItpitisVKGKpdvvvkedeeYKRVDFSKVpklktvfqkengtvtaanast 282
Cdd:PRK06289 189 QTR---------GWAFPDEATNDDDATNPV------VEGR----------LRRQDCSQV--------------------- 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 283 lNDGAAAVVLMTAEAAQRL--------------KVKPLARIAAFADAAVDPIDFPLAPAyAVPKVLKYAGLKKEDIAMWE 348
Cdd:PRK06289 223 -TDGGAGVVLASDAYLRDYadarpiprikgwghRTAPLGLEQKLDRSAGDPYVLPHVRQ-AVLDAYRRAGVGLDDLDGFE 300
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 401461805 349 VNEAFSVVVLANIKML---------------EIDP---QKVNVHGGAVSLGHPIGMSGARIVVHLAH 397
Cdd:PRK06289 301 VHDCFTPSEYLAIDHIgltgpgeswkaiengEIAIggrLPINPSGGLIGGGHPVGASGVRMLLDAAK 367
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
60-155 8.23e-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: 47.53  E-value: 8.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805  60 PATKLGTIAIQGAIEKAGIPKEEVKEVYMGNVIQGGEGQAPTRQ----------------------------ATLGAGLP 111
Cdd:cd00834   70 RFAQFALAAAEEALADAGLDPEELDPERIGVVIGSGIGGLATIEeayrallekgprrvspffvpmalpnmaaGQVAIRLG 149
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 401461805 112 IATPCTTVNKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSN 155
Cdd:cd00834  150 LRGPNYTVSTACASGAHAIGDAARLIRLGRADVVIAGGAEALIT 193
FabB COG0304
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...
60-160 1.74e-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: 46.63  E-value: 1.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805  60 PATKLGTIAIQGAIEKAGIPKEEVKE----VYMGNviqGGEGQAPTRQA--TLGAGLP-------------------IAT 114
Cdd:COG0304   70 RFTQYALAAAREALADAGLDLDEVDPdrtgVIIGS---GIGGLDTLEEAyrALLEKGPrrvspffvpmmmpnmaaghVSI 146
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 401461805 115 ------PCTTVNKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNvPYVM 160
Cdd:COG0304  147 rfglkgPNYTVSTACASGAHAIGEAYRLIRRGRADVMIAGGAEAAIT-PLGL 197
PRK07314 PRK07314
beta-ketoacyl-ACP synthase II;
115-152 6.36e-05

beta-ketoacyl-ACP synthase II;


Pssm-ID: 235987 [Multi-domain]  Cd Length: 411  Bit Score: 44.78  E-value: 6.36e-05
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 401461805 115 PCTTVNKVCASGMKAIMMASQSLMCGHQDVMVAGGMES 152
Cdd:PRK07314 154 PNHSIVTACATGAHAIGDAARLIAYGDADVMVAGGAEA 191
PRK08256 PRK08256
lipid-transfer protein; Provisional
57-153 1.67e-04

lipid-transfer protein; Provisional


Pssm-ID: 181327 [Multi-domain]  Cd Length: 391  Bit Score: 43.73  E-value: 1.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805  57 ASQPATKLGTIAIQGAIEKAGIPKEEVKEVYMGNVIqgGE---GQAPTRQATLgAGLPIatpcTTVNKVCASGMKAIMMA 133
Cdd:PRK08256  18 ASWDYPDMAAEAGRAALADAGIDYDAVQQAYVGYVY--GDstsGQRALYEVGM-TGIPI----VNVNNNCSTGSTALFLA 90
                         90       100
                 ....*....|....*....|
gi 401461805 134 SQSLMCGHQDVMVAGGMESM 153
Cdd:PRK08256  91 RQAVRSGAADCALALGFEQM 110
PRK12578 PRK12578
thiolase domain-containing protein;
68-156 2.51e-04

thiolase domain-containing protein;


Pssm-ID: 183606 [Multi-domain]  Cd Length: 385  Bit Score: 42.91  E-value: 2.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805  68 AIQGAIEKAGIPKEEVKEVYMGNviqggegqAPTRQATLGAGLPIATPCTTVNKV-------CASGMKAIMMASQSLMCG 140
Cdd:PRK12578  28 SIKEALNDAGVSQTDIELVVVGS--------TAYRGIELYPAPIVAEYSGLTGKVplrveamCATGLAASLTAYTAVASG 99
                         90
                 ....*....|....*.
gi 401461805 141 HQDVMVAGGMESMSNV 156
Cdd:PRK12578 100 LVDMAIAVGVDKMTEV 115
elong_cond_enzymes cd00828
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ...
27-154 5.48e-04

"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: 42.04  E-value: 5.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805  27 GRSYASKPTLNDV--VIVSATRTPIGSFLGSLASQ-----PATKLGTIAIQGAIEKAGIPKEEVKEVY------------ 87
Cdd:cd00828   31 GRSGIAPVARLKSrfDRGVAGQIPTGDIPGWDAKRtgivdRTTLLALVATEEALADAGITDPYEVHPSevgvvvgsgmgg 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805  88 ---------------MGNVIQGGEGQAPTRQATLGAGLPIAT-PCTTVNKVCASGMKAIMMASQSLMCGHQDVMVAGGME 151
Cdd:cd00828  111 lrflrrggkldaravNPYVSPKWMLSPNTVAGWVNILLLSSHgPIKTPVGACATALEALDLAVEAIRSGKADIVVVGGVE 190

                 ...
gi 401461805 152 SMS 154
Cdd:cd00828  191 DPL 193
PRK07516 PRK07516
thiolase domain-containing protein;
37-168 1.46e-03

thiolase domain-containing protein;


Pssm-ID: 181013 [Multi-domain]  Cd Length: 389  Bit Score: 40.70  E-value: 1.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805  37 NDVVIVSATRTPIGSF----LGSLASQPATklgtiaiqGAIEKAGIPKEEVKEVYMGNVIQGGEGQAPTRQATLGAGLPI 112
Cdd:PRK07516   2 MTASIVGWAHTPFGKLdaetLESLIVRVAR--------EALAHAGIAAGDVDGIFLGHFNAGFSPQDFPASLVLQADPAL 73
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 401461805 113 A-TPCTTVNKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVP------------YVMSRGATPYG 168
Cdd:PRK07516  74 RfKPATRVENACATGSAAVYAALDAIEAGRARIVLVVGAEKMTATPtaevgdillgasYLKEEGDTPGG 142
PKS cd00833
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ...
72-149 4.25e-03

polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different products, called polyketides, by successive decarboxylating Claisen condensations. PKSs can be divided into 2 groups, modular type I PKSs consisting of one or more large multifunctional proteins and iterative type II PKSs, complexes of several monofunctional subunits.


Pssm-ID: 238429 [Multi-domain]  Cd Length: 421  Bit Score: 39.08  E-value: 4.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805  72 AIEKAGIPKEEVKE----VYMGN------VIQGGEGQAPTRQATLGAGLPIAT-----------PCTTVNKVCASGMKAI 130
Cdd:cd00833   98 ALEDAGYSPESLAGsrtgVFVGAsssdylELLARDPDEIDAYAATGTSRAFLAnrisyffdlrgPSLTVDTACSSSLVAL 177
                         90
                 ....*....|....*....
gi 401461805 131 MMASQSLMCGHQDVMVAGG 149
Cdd:cd00833  178 HLACQSLRSGECDLALVGG 196
PRK07516 PRK07516
thiolase domain-containing protein;
281-418 6.88e-03

thiolase domain-containing protein;


Pssm-ID: 181013 [Multi-domain]  Cd Length: 389  Bit Score: 38.39  E-value: 6.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 281 STLNDGAAAVVLMTAEAAQRLKvKPLARIAAFADAAV------DPIDFPlAPAYAVPKVLKYAGLKKEDIAMWEVNEAFS 354
Cdd:PRK07516 213 SLVSDGAAALVLADAETARALQ-RAVRFRARAHVNDFlplsrrDPLAFE-GPRRAWQRALAQAGVTLDDLSFVETHDCFT 290
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461805 355 VVVLANIKMLEIDPQ------------------KVNVHGGAVSLGHPIGMSG-------ARIVVHLAHALKQGEFGLASI 409
Cdd:PRK07516 291 IAELIEYEAMGLAPPgqgarairegwtakdgklPVNPSGGLKAKGHPIGATGvsmhvlaAMQLTGEAGGMQIPGAKLAGV 370

                 ....*....
gi 401461805 410 CNGGGGASA 418
Cdd:PRK07516 371 FNMGGAAVA 379
 
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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