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Conserved domains on  [gi|665390158|ref|NP_001284987|]
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Acetyl-CoA acetyltransferase 1, isoform B [Drosophila melanogaster]

Protein Classification

thiolase family protein( domain architecture ID 10091456)

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

CATH:  3.40.47.10
EC:  2.3.1.-
Gene Ontology:  GO:0016746|GO:0006635
PubMed:  16356722

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 ...
26-409 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: 534.37  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158  26 VVVSAARTPIGSFQSQLAPLTATQLGARAIEAAIEKAGIAKTDVQEVIMGNVVSAGLGQAPARQAAIFAGLPTNVCCTTV 105
Cdd:cd00751    1 VIVSAVRTPIGRFGGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGEGQNPARQAALLAGLPESVPATTV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 106 NKVCSSGMKAVMLGAQSLMLGYADVVVAGGMESMSNVPYYLKRGATPY-GGVNLTDGIVFDGLWDVYNKFHMGNCAENTA 184
Cdd:cd00751   81 NRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGrLGLNTLDGMLDDGLTDPFTGLSMGITAENVA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 185 KKLEITRQQQDDFAIESYKRSAAAWANKVFQDEIAPVKIQQkRKPEIVISEDEEYKR-VNFDKFGQLATVFqRENGTVTA 263
Cdd:cd00751  161 EKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEVPG-RKGPVVVDRDEGPRPdTTLEKLAKLKPAF-KKDGTVTA 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 264 GNASTLNDGGAAVVLMSAEAAQKAGIKPLARIVAFQDAETDPIDFPIAPALAIPKLLKRAGVRKEDVAMWEVNEAFSLVV 343
Cdd:cd00751  239 GNASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDIDLIEINEAFAAQA 318
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665390158 344 LANIKKLDVDPAKVNVHGGAVSIGHPIGMSGARLVAHLSHSLKK--GELGCASICNGGGGASSILIEK 409
Cdd:cd00751  319 LACLKELGLDPEKVNVNGGAIALGHPLGASGARIVVTLLHELKRrgGRYGLATMCIGGGQGAAMVIER 386
 
Name Accession Description Interval E-value
thiolase cd00751
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ...
26-409 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: 534.37  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158  26 VVVSAARTPIGSFQSQLAPLTATQLGARAIEAAIEKAGIAKTDVQEVIMGNVVSAGLGQAPARQAAIFAGLPTNVCCTTV 105
Cdd:cd00751    1 VIVSAVRTPIGRFGGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGEGQNPARQAALLAGLPESVPATTV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 106 NKVCSSGMKAVMLGAQSLMLGYADVVVAGGMESMSNVPYYLKRGATPY-GGVNLTDGIVFDGLWDVYNKFHMGNCAENTA 184
Cdd:cd00751   81 NRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGrLGLNTLDGMLDDGLTDPFTGLSMGITAENVA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 185 KKLEITRQQQDDFAIESYKRSAAAWANKVFQDEIAPVKIQQkRKPEIVISEDEEYKR-VNFDKFGQLATVFqRENGTVTA 263
Cdd:cd00751  161 EKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEVPG-RKGPVVVDRDEGPRPdTTLEKLAKLKPAF-KKDGTVTA 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 264 GNASTLNDGGAAVVLMSAEAAQKAGIKPLARIVAFQDAETDPIDFPIAPALAIPKLLKRAGVRKEDVAMWEVNEAFSLVV 343
Cdd:cd00751  239 GNASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDIDLIEINEAFAAQA 318
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665390158 344 LANIKKLDVDPAKVNVHGGAVSIGHPIGMSGARLVAHLSHSLKK--GELGCASICNGGGGASSILIEK 409
Cdd:cd00751  319 LACLKELGLDPEKVNVNGGAIALGHPLGASGARIVVTLLHELKRrgGRYGLATMCIGGGQGAAMVIER 386
PLN02644 PLN02644
acetyl-CoA C-acetyltransferase
24-410 0e+00

acetyl-CoA C-acetyltransferase


Pssm-ID: 215347 [Multi-domain]  Cd Length: 394  Bit Score: 534.29  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158  24 EVVVVSAARTPIGSFQSQLAPLTATQLGARAIEAAIEKAGIAKTDVQEVIMGNVVSAGLGQAPARQAAIFAGLPTNVCCT 103
Cdd:PLN02644   2 DVCIVGVARTPIGGFLGSLSSLSATELGSIAIQAALERAGVDPALVQEVFFGNVLSANLGQAPARQAALGAGLPPSTICT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 104 TVNKVCSSGMKAVMLGAQSLMLGYADVVVAGGMESMSNVPYYL--KRGATPYGGVNLTDGIVFDGLWDVYNKFHMGNCAE 181
Cdd:PLN02644  82 TVNKVCASGMKAVMLAAQSIQLGINDVVVAGGMESMSNAPKYLpeARKGSRLGHDTVVDGMLKDGLWDVYNDFGMGVCAE 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 182 NTAKKLEITRQQQDDFAIESYKRSAAAWANKVFQDEIAPVKIQQKR-KPEIVISEDEEYKRVNFDKFGQLATVFQRENGT 260
Cdd:PLN02644 162 LCADQYSISREEQDAYAIQSYERAIAAQEAGAFAWEIVPVEVPGGRgRPSVIVDKDEGLGKFDPAKLRKLRPSFKEDGGS 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 261 VTAGNASTLNDGGAAVVLMSAEAAQKAGIKPLARIVAFQDAETDPIDFPIAPALAIPKLLKRAGVRKEDVAMWEVNEAFS 340
Cdd:PLN02644 242 VTAGNASSISDGAAALVLVSGEKALELGLQVIAKIRGYADAAQAPELFTTAPALAIPKALKHAGLEASQVDYYEINEAFS 321
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665390158 341 LVVLANIKKLDVDPAKVNVHGGAVSIGHPIGMSGARLVAHLSHSLKK--GELGCASICNGGGGASSILIEKL 410
Cdd:PLN02644 322 VVALANQKLLGLDPEKVNVHGGAVSLGHPIGCSGARILVTLLGVLRSknGKYGVAGICNGGGGASAIVVELM 393
PaaJ COG0183
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ...
24-410 7.56e-180

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: 506.14  E-value: 7.56e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158  24 EVVVVSAARTPIGSFQSQLAPLTATQLGARAIEAAIEKAGIAKTDVQEVIMGNVVSAGLGQAPARQAAIFAGLPTNVCCT 103
Cdd:COG0183    3 EVVIVDAVRTPFGRFGGALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQAGQGQNPARQAALLAGLPESVPAV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 104 TVNKVCSSGMKAVMLGAQSLMLGYADVVVAGGMESMSNVPYYLKRGATPYGG-VNLTDGIVFDGLWDVYNKFHMGNCAEN 182
Cdd:COG0183   83 TVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMLLPKARWGYRMnAKLVDPMINPGLTDPYTGLSMGETAEN 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 183 TAKKLEITRQQQDDFAIESYKRSAAAWANKVFQDEIAPVKIQQkRKPEIVISEDEEYKR-VNFDKFGQLATVFqRENGTV 261
Cdd:COG0183  163 VAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVEVPD-RKGEVVVDRDEGPRPdTTLEKLAKLKPAF-KKDGTV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 262 TAGNASTLNDGGAAVVLMSAEAAQKAGIKPLARIVAFQDAETDPIDFPIAPALAIPKLLKRAGVRKEDVAMWEVNEAFSL 341
Cdd:COG0183  241 TAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIGPVPATRKALARAGLTLDDIDLIEINEAFAA 320
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665390158 342 VVLANIKKLDVDPAKVNVHGGAVSIGHPIGMSGARLVAHLSHSLKK--GELGCASICNGGGGASSILIEKL 410
Cdd:COG0183  321 QVLAVLRELGLDPDKVNVNGGAIALGHPLGASGARILVTLLHELERrgGRYGLATMCIGGGQGIALIIERV 391
AcCoA-C-Actrans TIGR01930
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ...
27-408 4.10e-161

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: 458.23  E-value: 4.10e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158   27 VVSAARTPIGSFQSQLAPLTATQLGARAIEAAIEKAGIAKTDVQEVIMGNVVSAGLGQAPARQAAIFAGLPTNVCCTTVN 106
Cdd:TIGR01930   1 IVAAARTPIGKFGGSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLQAGEQQNIARQAALLAGLPESVPAYTVN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158  107 KVCSSGMKAVMLGAQSLMLGYADVVVAGGMESMSNVPYYLKRGatPYGGVNLTDGIVFDG----LWDVYNKFHMGNCAEN 182
Cdd:TIGR01930  81 RQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGVPRS--LRWGVKPGNAELEDArlkdLTDANTGLPMGVTAEN 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158  183 TAKKLEITRQQQDDFAIESYKRSAAAWANKVFQDEIAPVKIQQKRKPEIVISEDEEYKRVNFDKFGQLATVFqRENGTVT 262
Cdd:TIGR01930 159 LAKKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVTVKGRKGPVTVSSDEGIRPNTTLEKLAKLKPAF-DPDGTVT 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158  263 AGNASTLNDGGAAVVLMSAEAAQKAGIKPLARIVAFQDAETDPIDFPIAPALAIPKLLKRAGVRKEDVAMWEVNEAFSLV 342
Cdd:TIGR01930 238 AGNSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALKKAGLSISDIDLFEINEAFAAQ 317
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665390158  343 VLANIKKLDVDPAKVNVHGGAVSIGHPIGMSGARLVAHLSHSLKK--GELGCASICNGGGGASSILIE 408
Cdd:TIGR01930 318 VLACIKELGLDLEKVNVNGGAIALGHPLGASGARIVTTLLHELKRrgGRYGLATMCIGGGQGAAVILE 385
Thiolase_N pfam00108
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
25-282 2.09e-103

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: 306.92  E-value: 2.09e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158   25 VVVVSAARTPIGSFQSQLAPLTATQLGARAIEAAIEKAGIAKTDVQEVIMGNVVSAGLGQAPARQAAIFAGLPTNVCCTT 104
Cdd:pfam00108   1 VVIVSAARTPFGSFGGSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQAGEGQNPARQAALKAGIPDSAPAVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158  105 VNKVCSSGMKAVMLGAQSLMLGYADVVVAGGMESMSNVPYYLK---RGATPYGGVNLTDGIVFDGLWDVYNKFHMGNCAE 181
Cdd:pfam00108  81 INKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALPtdaRSGLKHGDEKKHDLLIPDGLTDAFNGYHMGLTAE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158  182 NTAKKLEITRQQQDDFAIESYKRSAAAWANKVFQDEIAPVKIQQKRKPEIVISEDEEYKRVNFDKFGQLATVFQREnGTV 261
Cdd:pfam00108 161 NVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDEIVPVTVKGRKGKPTVDKDEGIRPPTTAEPLAKLKPAFDKE-GTV 239
                         250       260
                  ....*....|....*....|.
gi 665390158  262 TAGNASTLNDGGAAVVLMSAE 282
Cdd:pfam00108 240 TAGNASPINDGAAAVLLMSES 260
 
Name Accession Description Interval E-value
thiolase cd00751
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ...
26-409 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: 534.37  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158  26 VVVSAARTPIGSFQSQLAPLTATQLGARAIEAAIEKAGIAKTDVQEVIMGNVVSAGLGQAPARQAAIFAGLPTNVCCTTV 105
Cdd:cd00751    1 VIVSAVRTPIGRFGGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGEGQNPARQAALLAGLPESVPATTV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 106 NKVCSSGMKAVMLGAQSLMLGYADVVVAGGMESMSNVPYYLKRGATPY-GGVNLTDGIVFDGLWDVYNKFHMGNCAENTA 184
Cdd:cd00751   81 NRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGrLGLNTLDGMLDDGLTDPFTGLSMGITAENVA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 185 KKLEITRQQQDDFAIESYKRSAAAWANKVFQDEIAPVKIQQkRKPEIVISEDEEYKR-VNFDKFGQLATVFqRENGTVTA 263
Cdd:cd00751  161 EKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEVPG-RKGPVVVDRDEGPRPdTTLEKLAKLKPAF-KKDGTVTA 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 264 GNASTLNDGGAAVVLMSAEAAQKAGIKPLARIVAFQDAETDPIDFPIAPALAIPKLLKRAGVRKEDVAMWEVNEAFSLVV 343
Cdd:cd00751  239 GNASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDIDLIEINEAFAAQA 318
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665390158 344 LANIKKLDVDPAKVNVHGGAVSIGHPIGMSGARLVAHLSHSLKK--GELGCASICNGGGGASSILIEK 409
Cdd:cd00751  319 LACLKELGLDPEKVNVNGGAIALGHPLGASGARIVVTLLHELKRrgGRYGLATMCIGGGQGAAMVIER 386
PLN02644 PLN02644
acetyl-CoA C-acetyltransferase
24-410 0e+00

acetyl-CoA C-acetyltransferase


Pssm-ID: 215347 [Multi-domain]  Cd Length: 394  Bit Score: 534.29  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158  24 EVVVVSAARTPIGSFQSQLAPLTATQLGARAIEAAIEKAGIAKTDVQEVIMGNVVSAGLGQAPARQAAIFAGLPTNVCCT 103
Cdd:PLN02644   2 DVCIVGVARTPIGGFLGSLSSLSATELGSIAIQAALERAGVDPALVQEVFFGNVLSANLGQAPARQAALGAGLPPSTICT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 104 TVNKVCSSGMKAVMLGAQSLMLGYADVVVAGGMESMSNVPYYL--KRGATPYGGVNLTDGIVFDGLWDVYNKFHMGNCAE 181
Cdd:PLN02644  82 TVNKVCASGMKAVMLAAQSIQLGINDVVVAGGMESMSNAPKYLpeARKGSRLGHDTVVDGMLKDGLWDVYNDFGMGVCAE 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 182 NTAKKLEITRQQQDDFAIESYKRSAAAWANKVFQDEIAPVKIQQKR-KPEIVISEDEEYKRVNFDKFGQLATVFQRENGT 260
Cdd:PLN02644 162 LCADQYSISREEQDAYAIQSYERAIAAQEAGAFAWEIVPVEVPGGRgRPSVIVDKDEGLGKFDPAKLRKLRPSFKEDGGS 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 261 VTAGNASTLNDGGAAVVLMSAEAAQKAGIKPLARIVAFQDAETDPIDFPIAPALAIPKLLKRAGVRKEDVAMWEVNEAFS 340
Cdd:PLN02644 242 VTAGNASSISDGAAALVLVSGEKALELGLQVIAKIRGYADAAQAPELFTTAPALAIPKALKHAGLEASQVDYYEINEAFS 321
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665390158 341 LVVLANIKKLDVDPAKVNVHGGAVSIGHPIGMSGARLVAHLSHSLKK--GELGCASICNGGGGASSILIEKL 410
Cdd:PLN02644 322 VVALANQKLLGLDPEKVNVHGGAVSLGHPIGCSGARILVTLLGVLRSknGKYGVAGICNGGGGASAIVVELM 393
PaaJ COG0183
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ...
24-410 7.56e-180

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: 506.14  E-value: 7.56e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158  24 EVVVVSAARTPIGSFQSQLAPLTATQLGARAIEAAIEKAGIAKTDVQEVIMGNVVSAGLGQAPARQAAIFAGLPTNVCCT 103
Cdd:COG0183    3 EVVIVDAVRTPFGRFGGALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQAGQGQNPARQAALLAGLPESVPAV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 104 TVNKVCSSGMKAVMLGAQSLMLGYADVVVAGGMESMSNVPYYLKRGATPYGG-VNLTDGIVFDGLWDVYNKFHMGNCAEN 182
Cdd:COG0183   83 TVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMLLPKARWGYRMnAKLVDPMINPGLTDPYTGLSMGETAEN 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 183 TAKKLEITRQQQDDFAIESYKRSAAAWANKVFQDEIAPVKIQQkRKPEIVISEDEEYKR-VNFDKFGQLATVFqRENGTV 261
Cdd:COG0183  163 VAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVEVPD-RKGEVVVDRDEGPRPdTTLEKLAKLKPAF-KKDGTV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 262 TAGNASTLNDGGAAVVLMSAEAAQKAGIKPLARIVAFQDAETDPIDFPIAPALAIPKLLKRAGVRKEDVAMWEVNEAFSL 341
Cdd:COG0183  241 TAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIGPVPATRKALARAGLTLDDIDLIEINEAFAA 320
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665390158 342 VVLANIKKLDVDPAKVNVHGGAVSIGHPIGMSGARLVAHLSHSLKK--GELGCASICNGGGGASSILIEKL 410
Cdd:COG0183  321 QVLAVLRELGLDPDKVNVNGGAIALGHPLGASGARILVTLLHELERrgGRYGLATMCIGGGQGIALIIERV 391
PRK05790 PRK05790
putative acyltransferase; Provisional
24-410 8.02e-166

putative acyltransferase; Provisional


Pssm-ID: 180261 [Multi-domain]  Cd Length: 393  Bit Score: 470.40  E-value: 8.02e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158  24 EVVVVSAARTPIGSFQSQLAPLTATQLGARAIEAAIEKAGIAKTDVQEVIMGNVVSAGLGQAPARQAAIFAGLPTNVCCT 103
Cdd:PRK05790   3 DVVIVSAARTPIGKFGGALKDVSAVELGAIVIKAALERAGVPPEQVDEVIMGQVLQAGAGQNPARQAALKAGLPVEVPAL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 104 TVNKVCSSGMKAVMLGAQSLMLGYADVVVAGGMESMSNVPYYLK--RGATPYGGVNLTDGIVFDGLWDVYNKFHMGNCAE 181
Cdd:PRK05790  83 TINKVCGSGLKAVALAAQAIRAGDADIVVAGGQESMSQAPHVLPgsRWGQKMGDVELVDTMIHDGLTDAFNGYHMGITAE 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 182 NTAKKLEITRQQQDDFAIESYKRSAAAWANKVFQDEIAPVKIQQKRKPEIVISEDeEYKR--VNFDKFGQLATVFqRENG 259
Cdd:PRK05790 163 NLAEQYGITREEQDEFALASQQKAEAAIKAGRFKDEIVPVTIKQRKGDPVVVDTD-EHPRpdTTAESLAKLRPAF-DKDG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 260 TVTAGNASTLNDGGAAVVLMSAEAAQKAGIKPLARIVAFQDAETDPIDFPIAPALAIPKLLKRAGVRKEDVAMWEVNEAF 339
Cdd:PRK05790 241 TVTAGNASGINDGAAAVVVMSEAKAKELGLTPLARIVSYAVAGVDPAIMGIGPVPAIRKALEKAGWSLADLDLIEINEAF 320
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 665390158 340 SLVVLANIKKLDVDPAKVNVHGGAVSIGHPIGMSGARLVAHLSHSLKK--GELGCASICNGGGGASSILIEKL 410
Cdd:PRK05790 321 AAQALAVEKELGLDPEKVNVNGGAIALGHPIGASGARILVTLLHEMKRrgAKKGLATLCIGGGQGVALIVERP 393
AcCoA-C-Actrans TIGR01930
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ...
27-408 4.10e-161

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: 458.23  E-value: 4.10e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158   27 VVSAARTPIGSFQSQLAPLTATQLGARAIEAAIEKAGIAKTDVQEVIMGNVVSAGLGQAPARQAAIFAGLPTNVCCTTVN 106
Cdd:TIGR01930   1 IVAAARTPIGKFGGSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLQAGEQQNIARQAALLAGLPESVPAYTVN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158  107 KVCSSGMKAVMLGAQSLMLGYADVVVAGGMESMSNVPYYLKRGatPYGGVNLTDGIVFDG----LWDVYNKFHMGNCAEN 182
Cdd:TIGR01930  81 RQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGVPRS--LRWGVKPGNAELEDArlkdLTDANTGLPMGVTAEN 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158  183 TAKKLEITRQQQDDFAIESYKRSAAAWANKVFQDEIAPVKIQQKRKPEIVISEDEEYKRVNFDKFGQLATVFqRENGTVT 262
Cdd:TIGR01930 159 LAKKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVTVKGRKGPVTVSSDEGIRPNTTLEKLAKLKPAF-DPDGTVT 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158  263 AGNASTLNDGGAAVVLMSAEAAQKAGIKPLARIVAFQDAETDPIDFPIAPALAIPKLLKRAGVRKEDVAMWEVNEAFSLV 342
Cdd:TIGR01930 238 AGNSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALKKAGLSISDIDLFEINEAFAAQ 317
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665390158  343 VLANIKKLDVDPAKVNVHGGAVSIGHPIGMSGARLVAHLSHSLKK--GELGCASICNGGGGASSILIE 408
Cdd:TIGR01930 318 VLACIKELGLDLEKVNVNGGAIALGHPLGASGARIVTTLLHELKRrgGRYGLATMCIGGGQGAAVILE 385
PRK08235 PRK08235
acetyl-CoA C-acetyltransferase;
22-408 1.55e-148

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181311 [Multi-domain]  Cd Length: 393  Bit Score: 426.82  E-value: 1.55e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158  22 IAEVVVVSAARTPIGSFQSQLAPLTATQLGARAIEAAIEKAGIAKTDVQEVIMGNVVSAGLGQAPARQAAIFAGLPTNVC 101
Cdd:PRK08235   1 MSKTVIVSAARTPFGKFGGSLKDVKATELGGIAIKEALERANVSAEDVEEVIMGTVLQGGQGQIPSRQAARAAGIPWEVQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 102 CTTVNKVCSSGMKAVMLGAQSLMLGYADVVVAGGMESMSNVPYYLKRGATPY--GGVNLTDGIVFDGLWDVYNKFHMGNC 179
Cdd:PRK08235  81 TETVNKVCASGLRAVTLADQIIRAGDASVIVAGGMESMSNAPYILPGARWGYrmGDNEVIDLMVADGLTCAFSGVHMGVY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 180 AENTAKKLEITRQQQDDFAIESYKRSAAAWANKVFQDEIAPVKIQQKRKPEIVISEDEEYKR-VNFDKFGQLATVFQREn 258
Cdd:PRK08235 161 GGEVAKELGISREAQDEWAYRSHQRAVSAHEEGRFEEEIVPVTIPQRKGDPIVVAKDEAPRKdTTIEKLAKLKPVFDKT- 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 259 GTVTAGNASTLNDGGAAVVLMSAEAAQKAGIKPLARIVAFQDAETDPIDFPIAPALAIPKLLKRAGVRKEDVAMWEVNEA 338
Cdd:PRK08235 240 GTITAGNAPGVNDGAAALVLMSEDRAKQEGRKPLATILAHTAIAVEAKDFPRTPGYAINALLEKTGKTVEDIDLFEINEA 319
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665390158 339 FSLVVLANIKKLDVDPAKVNVHGGAVSIGHPIGMSGARLVAHLSHSLKK--GELGCASICNGGGGASSILIE 408
Cdd:PRK08235 320 FAAVALASTEIAGIDPEKVNVNGGAVALGHPIGASGARIIVTLIHELKRrgGGIGIAAICSGGGQGDAVLIE 391
PRK06954 PRK06954
acetyl-CoA C-acetyltransferase;
24-408 3.25e-123

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180775 [Multi-domain]  Cd Length: 397  Bit Score: 362.29  E-value: 3.25e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158  24 EVVVVSAARTPIGSFQSQLAPLTATQLGARAIEAAIEKAGIAKTDVQEVIMGNVVSAGLGQAPARQAAIFAGLPTNVCCT 103
Cdd:PRK06954   8 PIVIASAARTPMAAFQGEFASLTAPQLGAAAIAAAVERAGLKPEQIDEVVMGCVLPAGQGQAPARQAALGAGLPLSVGCT 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 104 TVNKVCSSGMKAVMLGAQSLMLGYADVVVAGGMESMSNVPYYL--KRGATPYGGVNLTDGIVFDGLWDVYNKFH-MGNCA 180
Cdd:PRK06954  88 TVNKMCGSGMRAAMFAHDMLVAGSVDVIVAGGMESMTNAPYLLpkARGGMRMGHGQVLDHMFLDGLEDAYDKGRlMGTFA 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 181 ENTAKKLEITRQQQDDFAIESYKRSAAAWANKVFQDEIAPVKIQQKrKPEIVISEDEEYKRVNFDKFGQLATVFQReNGT 260
Cdd:PRK06954 168 EECAGEYGFTREAQDAFAIESLARAKRANEDGSFAWEIAPVTVAGK-KGDTVIDRDEQPFKANPEKIPTLKPAFSK-TGT 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 261 VTAGNASTLNDGGAAVVLMSAEAAQKAGIKPLARIVAFQDAETDPIDFPIAPALAIPKLLKRAGVRKEDVAMWEVNEAFS 340
Cdd:PRK06954 246 VTAANSSSISDGAAALVMMRASTAKRLGLAPLARVVGHSTFAQAPSKFTTAPVGAIRKLFEKNGWRAAEVDLFEINEAFA 325
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 341 LVVLANIKKLDVDPAKVNVHGGAVSIGHPIGMSGARLVAHLSHSLKK--GELGCASICNGGGGASSILIE 408
Cdd:PRK06954 326 VVTMAAMKEHGLPHEKVNVNGGACALGHPIGASGARILVTLIGALRArgGKRGVASLCIGGGEATAMGIE 395
PRK09051 PRK09051
beta-ketothiolase BktB;
24-410 5.04e-113

beta-ketothiolase BktB;


Pssm-ID: 181625 [Multi-domain]  Cd Length: 394  Bit Score: 336.16  E-value: 5.04e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158  24 EVVVVSAARTPIGSFQSQLAPLTATQLGARAIEAAIEKAGIAKTDVQEVIMGNVVSAGLGQA-PARQAAIFAGLPTNVCC 102
Cdd:PRK09051   4 EVVVVSGVRTAIGTFGGSLKDVAPTDLGATVVREALARAGVDPDQVGHVVFGHVIPTEPRDMyLSRVAAINAGVPQETPA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 103 TTVNKVCSSGMKAVMLGAQSLMLGYADVVVAGGMESMSNVPYYLK--RGATPYGGVNLTDGIVfDGLWDVYNKFHMGNCA 180
Cdd:PRK09051  84 FNVNRLCGSGLQAIVSAAQAILLGDADVAIGGGAESMSRAPYLLPaaRWGARMGDAKLVDMMV-GALHDPFGTIHMGVTA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 181 ENTAKKLEITRQQQDDFAIESYKRSAAAWANKVFQDEIAPVKIQQkRKPEIVISEDEEYKR-VNFDKFGQLATVFQRENG 259
Cdd:PRK09051 163 ENVAAKYGISREAQDALALESHRRAAAAIAAGYFKDQIVPVEIKT-RKGEVVFDTDEHVRAdTTLEDLAKLKPVFKKENG 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 260 TVTAGNASTLNDGGAAVVLMSAEAAQKAGIKPLARIVAFQDAETDPIDFPIAPALAIPKLLKRAGVRKEDVAMWEVNEAF 339
Cdd:PRK09051 242 TVTAGNASGINDGAAAVVLAEADAAEARGLKPLARLVGYAHAGVDPEYMGIGPVPATQKALERAGLTVADLDVIEANEAF 321
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 665390158 340 SLVVLANIKKLDVDPAKVNVHGGAVSIGHPIGMSGARLVAHLSHSLKK--GELGCASICNGGGGASSILIEKL 410
Cdd:PRK09051 322 AAQACAVTRELGLDPAKVNPNGSGISLGHPVGATGAIITVKALYELQRigGRYALVTMCIGGGQGIAAIFERL 394
PRK05656 PRK05656
acetyl-CoA C-acetyltransferase;
24-409 1.66e-111

acetyl-CoA C-acetyltransferase;


Pssm-ID: 168156  Cd Length: 393  Bit Score: 332.24  E-value: 1.66e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158  24 EVVVVSAARTPIGSFQSQLAPLTATQLGARAIEAAIEKAGIAKTDVQEVIMGNVVSAGLGQAPARQAAIFAGLPTNVCCT 103
Cdd:PRK05656   3 DVVIVAATRTAIGSFQGSLANIPAVELGAAVIRRLLEQTGLDPAQVDEVILGQVLTAGAGQNPARQAAIKAGLPHSVPAM 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 104 TVNKVCSSGMKAVMLGAQSLMLGYADVVVAGGMESMSNVPYYL--KRGATPYGGVNLTDGIVFDGLWDVYNKFHMGNCAE 181
Cdd:PRK05656  83 TLNKVCGSGLKALHLAAQAIRCGDAEVIIAGGQENMSLAPYVLpgARTGLRMGHAQLVDSMITDGLWDAFNDYHMGITAE 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 182 NTAKKLEITRQQQDDFAIESYKRSAAAWANKVFQDEIAPVKIQQKRKPEIVISEDEEYKR-VNFDKFGQLATVFqRENGT 260
Cdd:PRK05656 163 NLVEKYGISREAQDAFAAASQQKAVAAIEAGRFDDEITPILIPQRKGEPLAFATDEQPRAgTTAESLAKLKPAF-KKDGS 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 261 VTAGNASTLNDGGAAVVLMSAEAAQKAGIKPLARIVAFQDAETDPIDFPIAPALAIPKLLKRAGVRKEDVAMWEVNEAFS 340
Cdd:PRK05656 242 VTAGNASSLNDGAAAVLLMSAAKAKALGLPVLAKIAAYANAGVDPAIMGIGPVSATRRCLDKAGWSLAELDLIEANEAFA 321
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665390158 341 LVVLANIKKLDVDPAKVNVHGGAVSIGHPIGMSGARLVAHLSHSLKKGEL--GCASICNGGGGASSILIEK 409
Cdd:PRK05656 322 AQSLAVGKELGWDAAKVNVNGGAIALGHPIGASGCRVLVTLLHEMIRRDAkkGLATLCIGGGQGVALAIER 392
PRK06366 PRK06366
acetyl-CoA C-acetyltransferase;
24-408 1.63e-106

acetyl-CoA C-acetyltransferase;


Pssm-ID: 102340 [Multi-domain]  Cd Length: 388  Bit Score: 319.65  E-value: 1.63e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158  24 EVVVVSAARTPIGSFQSQLAPLTATQLGARAIEAAIEKAGIAKTDVQEVIMGNVVSAGLGQAPARQAAIFAGLPTNVCCT 103
Cdd:PRK06366   3 DVYIVSAKRTAIGKFGRSFSKIKAPQLGGAAIKAVIDDAKLDPALVQEVIMGNVIQAGVGQNPAGQAAYHAGLPFGVTKY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 104 TVNKVCSSGMKAVMLGAQSLMLGYADVVVAGGMESMSNVPYYL----KRGATP--YGGVNLTDGIVFDGLWDVYNKFHMG 177
Cdd:PRK06366  83 TVNVVCASGMLAVESAAREIMLGERDLVIAGGMENMSNAPFLLpsdlRWGPKHllHKNYKIDDAMLVDGLIDAFYFEHMG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 178 NCAENTAKKLEITRQQQDDFAIESYKRSAAAWANKVFQDEIAPVKiqqkrkpeiVISEDEEYKRVNFDKFGQLATVFQRe 257
Cdd:PRK06366 163 VSAERTARKYGITREMADEYSVQSYERAIRATESGEFRNEIVPFN---------DLDRDEGIRKTTMEDLAKLPPAFDK- 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 258 NGTVTAGNASTLNDGGAAVVLMSAEAAQKAGIKPLARIVAFQDAETDPIDFPIAPALAIPKLLKRAGVRKEDVAMWEVNE 337
Cdd:PRK06366 233 NGILTAGNSAQLSDGGSALVMASEKAINEYGLKPIARITGYESASLDPLDFVEAPIPATRKLLEKQNKSIDYYDLVEHNE 312
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 665390158 338 AFSLVVLANIKKLDVDPAKVNVHGGAVSIGHPIGMSGARLVAHLSHSLKKGEL--GCASICNGGGGASSILIE 408
Cdd:PRK06366 313 AFSIASIIVRDQLKIDNERFNVNGGAVAIGHPIGNSGSRIIVTLINALKTRHMktGLATLCHGGGGAHTLTLE 385
Thiolase_N pfam00108
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
25-282 2.09e-103

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: 306.92  E-value: 2.09e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158   25 VVVVSAARTPIGSFQSQLAPLTATQLGARAIEAAIEKAGIAKTDVQEVIMGNVVSAGLGQAPARQAAIFAGLPTNVCCTT 104
Cdd:pfam00108   1 VVIVSAARTPFGSFGGSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQAGEGQNPARQAALKAGIPDSAPAVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158  105 VNKVCSSGMKAVMLGAQSLMLGYADVVVAGGMESMSNVPYYLK---RGATPYGGVNLTDGIVFDGLWDVYNKFHMGNCAE 181
Cdd:pfam00108  81 INKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALPtdaRSGLKHGDEKKHDLLIPDGLTDAFNGYHMGLTAE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158  182 NTAKKLEITRQQQDDFAIESYKRSAAAWANKVFQDEIAPVKIQQKRKPEIVISEDEEYKRVNFDKFGQLATVFQREnGTV 261
Cdd:pfam00108 161 NVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDEIVPVTVKGRKGKPTVDKDEGIRPPTTAEPLAKLKPAFDKE-GTV 239
                         250       260
                  ....*....|....*....|.
gi 665390158  262 TAGNASTLNDGGAAVVLMSAE 282
Cdd:pfam00108 240 TAGNASPINDGAAAVLLMSES 260
PRK06633 PRK06633
acetyl-CoA C-acetyltransferase;
22-408 2.42e-98

acetyl-CoA C-acetyltransferase;


Pssm-ID: 168632 [Multi-domain]  Cd Length: 392  Bit Score: 298.87  E-value: 2.42e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158  22 IAEVVVVSAARTPIGSFQSQLAPLTATQLGARAIEAAIEKAGIAKTDVQEVIMGNVVSAGLGQAPARQAAIFAGLPTNVC 101
Cdd:PRK06633   2 TKPVYITHAKRTAFGSFMGSLSTTPAPMLAAHLIKDILQNSKIDPALVNEVILGQVITGGSGQNPARQTLIHAGIPKEVP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 102 CTTVNKVCSSGMKAVMLGAQSLMLGYADVVVAGGMESMSNVPY--YLKRGATpYGGVNLTDGIVFDGLWDVYNKFHMGNC 179
Cdd:PRK06633  82 GYTINKVCGSGLKSVALAANSIMTGDNEIVIAGGQENMSLGMHgsYIRAGAK-FGDIKMVDLMQYDGLTDVFSGVFMGIT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 180 AENTAKKLEITRQQQDDFAIESYKRSAAAWANKVFQDEIAPVKIQQKRKPEIVISEDEEYKRVNFDKFGQLATVFQReNG 259
Cdd:PRK06633 161 AENISKQFNISRQEQDEFALSSHKKAAKAQLAGIFKDEILPIEVTIKKTTSLFDHDETVRPDTSLEILSKLRPAFDK-NG 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 260 TVTAGNASTLNDGGAAVVLMSAEAAQKAGIKPLARIVAFQDAETDPIDFPIAPALAIPKLLKRAGVRKEDVAMWEVNEAF 339
Cdd:PRK06633 240 VVTAGNASSINDGAACLMVVSEEALKKHNLTPLARIVSYASAGVDPSIMGTAPVPASQKALSKAGWSVNDLEVIEVNEAF 319
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665390158 340 SLVVLANIKKLDVDPAKVNVHGGAVSIGHPIGMSGARLVAHLSHSLK--KGELGCASICNGGGGASSILIE 408
Cdd:PRK06633 320 AAQSIYVNREMKWDMEKVNINGGAIAIGHPIGASGGRVLITLIHGLRraKAKKGLVTLCIGGGMGMAMCVE 390
PRK06205 PRK06205
acetyl-CoA C-acetyltransferase;
24-400 4.09e-94

acetyl-CoA C-acetyltransferase;


Pssm-ID: 235741 [Multi-domain]  Cd Length: 404  Bit Score: 288.43  E-value: 4.09e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158  24 EVVVVSAARTPIGSFQSQLAPLTATQLGARAIEAAIEKAGIAKTDVQEVIMGNvvSAGLGQAPA--RQAAIFAGLPTNVC 101
Cdd:PRK06205   3 DAVICEPVRTPVGRFGGAFKDVPAEELAATVIRALVERTGIDPARIDDVIFGQ--GYPNGEAPAigRVAALDAGLPVTVP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 102 CTTVNKVCSSGMKAVMLGAQSLMLGYADVVVAGGMESMSNVPYYLK--RGATPYGGVNLTDGI-------------VFDG 166
Cdd:PRK06205  81 GMQLDRRCGSGLQAVITAAMQVQTGAADVVIAGGAESMSNVEFYTTdmRWGVRGGGVQLHDRLargretaggrrfpVPGG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 167 lwdvynkfhMGNCAENTAKKLEITRQQQDDFAIESYKRSAAAWANKVFQDEIAPVKIQQKRKPEIVISEDEEYKR-VNFD 245
Cdd:PRK06205 161 ---------MIETAENLRREYGISREEQDALAVRSHQRAVAAQEAGRFDDEIVPVTVPQRKGDPTVVDRDEHPRAdTTLE 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 246 KFGQLATVFQR--ENGTVTAGNASTLNDGGAAVVLMSAEAAQKAGIKPLARIVAFQDAETDPIDFPIAPALAIPKLLKRA 323
Cdd:PRK06205 232 SLAKLRPIMGKqdPEATVTAGNASGQNDAAAACLVTTEDKAEELGLRPLARLVSWAVAGVEPSRMGIGPVPATEKALARA 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 324 GVRKEDVAMWEVNEAFSLVVLANIKKL---DVDPAKVNVHGGAVSIGHPIGMSGARLVAHLSHSLK--KGELGCASICNG 398
Cdd:PRK06205 312 GLTLDDIDLIELNEAFAAQVLAVLKEWgfgADDEERLNVNGSGISLGHPVGATGGRILATLLRELQrrQARYGLETMCIG 391

                 ..
gi 665390158 399 GG 400
Cdd:PRK06205 392 GG 393
PRK06445 PRK06445
acetyl-CoA C-acetyltransferase;
24-409 2.45e-90

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180563 [Multi-domain]  Cd Length: 394  Bit Score: 278.14  E-value: 2.45e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158  24 EVVVVSAARTPIGSFQSQ------LAPLTATQLGARAIEAAIEKAGIAKTDVQEVIMGNVVSAGLGQAPARQAAIF-AGL 96
Cdd:PRK06445   3 DVYLVDFARTAFSRFRPKdpqkdvFNNIRPEELAAMLINRLIEKTGIKPEEIDDIITGCALQVGENWLYGGRHPIFlARL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158  97 PTNVCCTTVNKVCSSGMKAVMLGAQSLMLGYADVVVAGGMESMSNVPYYlkrgATPYGGVN---LTDGIVFDglWDVYNK 173
Cdd:PRK06445  83 PYNIPAMAVDRQCASSLTTVSIGAMEIATGMADIVIAGGVEHMTRTPMG----DNPHIEPNpklLTDPKYIE--YDLTTG 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 174 FHMGNCAENTAKKLEITRQQQDDFAIESYKRSAAAWANKVFQDEIAPVKIQQKRKPEIVISEDEEYKRVNFDKFGQLATV 253
Cdd:PRK06445 157 YVMGLTAEKLAEEAGIKREEMDRWSLRSHQLAAKAIQEGYFKDEILPIEVEVEGKKKVVDVDQSVRPDTSLEKLAKLPPA 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 254 FqRENGTVTAGNASTLNDGGAAVVLMSAEAAQKAGIKPLARIVAFQDAETDPIDFPIAPALAIPKLLKRAGVRKEDVAMW 333
Cdd:PRK06445 237 F-KPDGVITAGNSSPLNSGASYVLLMSKKAVKKYGLKPMAKIRSFGFAGVPPAIMGKGPVPASKKALEKAGLSVKDIDLW 315
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665390158 334 EVNEAFSLVVLANIKKLDVDPAKVNVHGGAVSIGHPIGMSGARLVAHLSHSL--KKGELGCASICNGGGGASSILIEK 409
Cdd:PRK06445 316 EINEAFAVVVLYAIKELGLDPETVNIKGGAIAIGHPLGATGARIVGTLARQLqiKGKDYGVATLCVGGGQGGAVVLER 393
PRK09050 PRK09050
beta-ketoadipyl CoA thiolase; Validated
23-410 1.30e-88

beta-ketoadipyl CoA thiolase; Validated


Pssm-ID: 181624 [Multi-domain]  Cd Length: 401  Bit Score: 274.14  E-value: 1.30e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158  23 AEVVVVSAARTPIGSFQSQLAPLTATQLGARAIEAAIEK-AGIAKTDVQEVIMGNVVSAGL-GQAPARQAAIFAGLPTNV 100
Cdd:PRK09050   2 TEAFICDAIRTPIGRYGGALSSVRADDLGAVPLKALMARnPGVDWEAVDDVIYGCANQAGEdNRNVARMSALLAGLPVSV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 101 CCTTVNKVCSSGMKAVMLGAQSLMLGYADVVVAGGMESMSNVPYYLKRGATPYGgvnlTDGIVFDGL--WDVYNKF---- 174
Cdd:PRK09050  82 PGTTINRLCGSGMDAVGTAARAIKAGEAELMIAGGVESMSRAPFVMGKADSAFS----RQAEIFDTTigWRFVNPLmkaq 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 175 ----HMGNCAENTAKKLEITRQQQDDFAIESYKRSAAAWANKVFQDEIAPVKIQQKRKPEIVISEDEEYKR-VNFDKFGQ 249
Cdd:PRK09050 158 ygvdSMPETAENVAEDYNISRADQDAFALRSQQRAAAAQAAGFLAEEIVPVTIPQKKGDPVVVDRDEHPRPeTTLEALAK 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 250 LATVFqRENGTVTAGNASTLNDGGAAVVLMSAEAAQKAGIKPLARIVAFQDAETDPIDFPIAPALAIPKLLKRAGVRKED 329
Cdd:PRK09050 238 LKPVF-RPDGTVTAGNASGVNDGAAALLLASEAAAKKHGLTPRARILGMATAGVEPRIMGIGPAPATRKLLARLGLTIDQ 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 330 VAMWEVNEAFSLVVLANIKKLDV--DPAKVNVHGGAVSIGHPIGMSGARLVAHLSHSLKK--GELGCASICNGGGGASSI 405
Cdd:PRK09050 317 FDVIELNEAFAAQGLAVLRQLGLadDDARVNPNGGAIALGHPLGMSGARLVLTALHQLERtgGRYALCTMCIGVGQGIAL 396

                 ....*
gi 665390158 406 LIEKL 410
Cdd:PRK09050 397 AIERV 401
PLN02287 PLN02287
3-ketoacyl-CoA thiolase
24-406 4.02e-85

3-ketoacyl-CoA thiolase


Pssm-ID: 215161 [Multi-domain]  Cd Length: 452  Bit Score: 266.63  E-value: 4.02e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158  24 EVVVVSAARTPI-----GSFQSQLApltaTQLGARAIEAAIEKAGIAKTDVQEVIMGNVVSAGLGQA-PARQAAIFAGLP 97
Cdd:PLN02287  47 DVVIVAAYRTPIckakrGGFKDTYP----DDLLAPVLKAVVEKTGLNPSEVGDIVVGTVLAPGSQRAnECRMAAFYAGFP 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158  98 TNVCCTTVNKVCSSGMKAVMLGAQSLMLGYADVVVAGGMESMSNVPYYLKRGATPYggVNLtdgivFDGLWDVYnkFHMG 177
Cdd:PLN02287 123 ETVPVRTVNRQCSSGLQAVADVAAAIKAGFYDIGIGAGVESMTTNPMAWEGGVNPR--VES-----FSQAQDCL--LPMG 193
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 178 NCAENTAKKLEITRQQQDDFAIESYKRSAAAWANKVFQDEIAPVKIQ-----QKRKPEIVISEDEEYK-RVNFDKFGQLA 251
Cdd:PLN02287 194 ITSENVAERFGVTREEQDQAAVESHRKAAAATASGKFKDEIVPVHTKivdpkTGEEKPIVISVDDGIRpNTTLADLAKLK 273
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 252 TVFqRENGTVTAGNASTLNDGGAAVVLMSAEAAQKAGIKPLARIVAFQDAETDPIDFPIAPALAIPKLLKRAGVRKEDVA 331
Cdd:PLN02287 274 PVF-KKNGTTTAGNSSQVSDGAGAVLLMKRSVAMQKGLPILGVFRSFAAVGVDPAVMGIGPAVAIPAAVKAAGLELDDID 352
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 332 MWEVNEAFSLVVLANIKKLDVDPAKVNVHGGAVSIGHPIGMSGARLVAHLSHSLKK----GELGCASICNGGG-GASSIL 406
Cdd:PLN02287 353 LFEINEAFASQFVYCCKKLGLDPEKVNVNGGAIALGHPLGATGARCVATLLHEMKRrgkdCRFGVVSMCIGTGmGAAAVF 432
PRK07108 PRK07108
acetyl-CoA C-acyltransferase;
24-410 2.62e-84

acetyl-CoA C-acyltransferase;


Pssm-ID: 180843 [Multi-domain]  Cd Length: 392  Bit Score: 262.78  E-value: 2.62e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158  24 EVVVVSAARTPIG-SFQSQLAPLTATQLGARAIEAAIEKAGIAKTDVQEVIMGNVVSAG-LGQAPARQAAIFAGLPTNVC 101
Cdd:PRK07108   3 EAVIVSTARTPLAkSWRGAFNMTHGATLGGHVVQHAVERAKLDPAEVEDVIMGCANPEGaTGANIARQIALRAGLPVTVP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 102 CTTVNKVCSSGMKAVMLGAQSLMLGYADVVVAGGMESMSNVPYYLKRGAtpyggvnLTDGIVFDGLWDVYnkFHMGNCAE 181
Cdd:PRK07108  83 GMTVNRFCSSGLQTIALAAQRVIAGEGDVFVAGGVESISCVQNEMNRHM-------LREGWLVEHKPEIY--WSMLQTAE 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 182 NTAKKLEITRQQQDDFAIESYKRSAAAWANKVFQDEIAPV----KIQQK-----RKPEIVISEDEEYKR-VNFDKFGQLA 251
Cdd:PRK07108 154 NVAKRYGISKERQDEYGVQSQQRAAAAQAAGRFDDEIVPItvtaGVADKatgrlFTKEVTVSADEGIRPdTTLEGVSKIR 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 252 TVFqrENGTVTAGNASTLNDGGAAVVLMSAEAAQKAGIKPLARIVAFQDAETDPIDFPIAPALAIPKLLKRAGVRKEDVA 331
Cdd:PRK07108 234 SAL--PGGVITAGNASQFSDGASACVVMNAKVAEREGLQPLGIFRGFAVAGCEPDEMGIGPVFAVPKLLKQAGLKVDDID 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 332 MWEVNEAFSLVVLANIKKLDVDPAKVNVHGGAVSIGHPIGMSGARLVAH-LSHSLKKG-ELGCASICNGGGGASSILIEK 409
Cdd:PRK07108 312 LWELNEAFAVQVLYCRDTLGIPMDRLNVNGGAIAVGHPYGVSGARLTGHaLIEGKRRGaKYVVVTMCIGGGQGAAGLFEV 391

                 .
gi 665390158 410 L 410
Cdd:PRK07108 392 L 392
PRK07661 PRK07661
acetyl-CoA C-acetyltransferase;
24-405 1.37e-83

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181072 [Multi-domain]  Cd Length: 391  Bit Score: 260.84  E-value: 1.37e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158  24 EVVVVSAARTPIG-SFQSQLAPLTATQLGARAIEAAIEKAGIAKTDVQEVIMGNVV-SAGLGQAPARQAAIFAGLPTNVC 101
Cdd:PRK07661   3 EAVIVAGARTPVGkAKKGSLKTVRPDDLGALVVKETLKRAGNYEGPIDDLIIGCAMpEAEQGLNMARNIGALAGLPYTVP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 102 CTTVNKVCSSGMKAVMLGAQSLMLGYADVVVAGGMESMSNVPYYlkrgatpyGGVNLTDGIVFDGLWDVYnkFHMGNCAE 181
Cdd:PRK07661  83 AITINRYCSSGLQSIAYGAERIMLGHSEAVIAGGAESMSLVPMM--------GHVVRPNPRLVEAAPEYY--MGMGHTAE 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 182 NTAKKLEITRQQQDDFAIESYKRSAAAWANKVFQDEIAPVKIQQK--------RKPEIVISEDEEYK-RVNFDKFGQLAT 252
Cdd:PRK07661 153 QVAVKYGISREDQDAFAVRSHQRAAKALAEGKFADEIVPVDVTLRtvgennklQEETITFSQDEGVRaDTTLEILGKLRP 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 253 VFQReNGTVTAGNASTLNDGGAAVVLMSAEAAQKAGIKPLARIVAFQDAETDPIDFPIAPALAIPKLLKRAGVRKEDVAM 332
Cdd:PRK07661 233 AFNV-KGSVTAGNSSQMSDGAAAVLLMDREKAESDGLKPLAKFRSFAVAGVPPEVMGIGPIAAIPKALKLAGLELSDIGL 311
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665390158 333 WEVNEAFSLVVLANIKKLDVDPAKVNVHGGAVSIGHPIGMSGARLVAHLSHSLKK--GELGCASICNGGG-GASSI 405
Cdd:PRK07661 312 FELNEAFASQSIQVIRELGLDEEKVNVNGGAIALGHPLGCTGAKLTLSLIHEMKRrnEQFGIVTMCIGGGmGAAGV 387
PRK07801 PRK07801
acetyl-CoA C-acetyltransferase;
23-410 2.11e-82

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181123 [Multi-domain]  Cd Length: 382  Bit Score: 257.33  E-value: 2.11e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158  23 AEVVVVSAARTPIGSFQSQLAPLTATQLGARAIEAAIEKAGIAKTDVQEVIMGNVVSAGlGQAP--ARQAAIFAGLPTNV 100
Cdd:PRK07801   2 AEAYIVDAVRTPVGKRKGGLAGVHPADLGAHVLKGLVDRTGIDPAAVDDVIFGCVDTIG-PQAGniARTSWLAAGLPEEV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 101 CCTTVNKVCSSGMKAVMLGAQSLMLGYADVVVAGGMESMSNVPYYLKR-GATPYGgvnLTDGIVFDGLWDV------YNK 173
Cdd:PRK07801  81 PGVTVDRQCGSSQQAIHFAAQAVMSGTQDLVVAGGVQNMSQIPISSAMtAGEQLG---FTSPFAESKGWLHrygdqeVSQ 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 174 FHmgnCAENTAKKLEITRQQQDDFAIESYKRSAAAWANKVFQDEIAPVKiqqkrkpeiVISEDEEYKRVNFDKFGQLATV 253
Cdd:PRK07801 158 FR---GAELIAEKWGISREEMERFALESHRRAFAAIRAGRFDNEIVPVG---------GVTVDEGPRETSLEKMAGLKPL 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 254 fqRENGTVTAGNASTLNDGGAAVVLMSAEAAQKAGIKPLARIVAFQDAETDPIDFPIAPALAIPKLLKRAGVRKEDVAMW 333
Cdd:PRK07801 226 --VEGGRLTAAVASQISDGASAVLLASERAVKRHGLTPRARIHHLSVRGDDPVFMLTAPIPATRYALEKTGLSIDDIDVV 303
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665390158 334 EVNEAFSLVVLANIKKLDVDPAKVNVHGGAVSIGHPIGMSGARLVAHLSHSLKK--GELGCASICNGGGGASSILIEKL 410
Cdd:PRK07801 304 EINEAFAPVVLAWLKETGADPAKVNPNGGAIALGHPLGATGAKLMTTLLHELERtgGRYGLQTMCEGGGTANVTIIERL 382
PRK08131 PRK08131
3-oxoadipyl-CoA thiolase;
32-409 6.10e-79

3-oxoadipyl-CoA thiolase;


Pssm-ID: 181242 [Multi-domain]  Cd Length: 401  Bit Score: 249.31  E-value: 6.10e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158  32 RTPIGSFQSQLAPLTATQLGARAIEAAIEKAGIAKTDVQEVIMGNVVSAGL-GQAPARQAAIFAGLPTNVCCTTVNKVCS 110
Cdd:PRK08131  11 RSPFGRHAGALASVRPDDLAATVIRRLLEKSGFPGDDIEDVILGCTNQAGEdSRNVARNALLLAGLPVTVPGQTVNRLCA 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 111 SGMKAVMLGAQSLMLGYADVVVAGGMESMSNVPYYLKRGATPYGgvnlTDGIVFDG----------LWDVYNKFHMGNCA 180
Cdd:PRK08131  91 SGLAAVIDAARAITCGEGDLYLAGGVESMSRAPFVMGKAESAFS----RDAKVFDTtigarfpnpkIVAQYGNDSMPETG 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 181 ENTAKKLEITRQQQDDFAIESYKRSAAAWANKVFQDEIAPVKIQQ-KRKPEIVISEDEEYK-RVNFDKFGQLATVFqrEN 258
Cdd:PRK08131 167 DNVAAEFGISREDADRFAAQSQAKYQAAKEEGFFADEITPIEVPQgRKLPPKLVAEDEHPRpSSTVEALTKLKPLF--EG 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 259 GTVTAGNASTLNDGGAAVVLMSAEAAQKAGIKPLARIVAFQDAETDPIDFPIAPALAIPKLLKRAGVRKEDVAMWEVNEA 338
Cdd:PRK08131 245 GVVTAGNASGINDGAAALLIGSRAAGEKYGLKPMARILSSAAAGVEPRIMGIGPVEAIKKALARAGLTLDDMDIIEINEA 324
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665390158 339 FSLVVLANIKKLDV--DPAKVNVHGGAVSIGHPIGMSGARLVAHLSHSLKK--GELGCASICNGGGGASSILIEK 409
Cdd:PRK08131 325 FASQVLGCLKGLGVdfDDPRVNPNGGAIAVGHPLGASGARLALTAARELQRrgKRYAVVSLCIGVGQGLAMVIER 399
PRK09052 PRK09052
acetyl-CoA C-acyltransferase;
19-410 3.29e-78

acetyl-CoA C-acyltransferase;


Pssm-ID: 181626 [Multi-domain]  Cd Length: 399  Bit Score: 247.22  E-value: 3.29e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158  19 SSKIAEVVVVSAARTPIG-SFQSQLAPLTATQLGARAIEAAIEKA-GIAKTDVQEVIMGNVV-SAGLGQAPARQAAIFAG 95
Cdd:PRK09052   2 SKQLQDAYIVAATRTPVGkAPRGMFKNTRPDDLLAHVLRSAVAQVpGLDPKLIEDAIVGCAMpEAEQGLNVARIGALLAG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158  96 LPTNVCCTTVNKVCSSGMKAVMLGAQSLMLGYADVVVAGGMESMSNVPYylkrgatpyGG--VNLTDGIvFDGLWDVYNK 173
Cdd:PRK09052  82 LPNSVGGVTVNRFCASGLQAVAMAADRIRVGEADVMIAAGVESMSMVPM---------MGnkPSMSPAI-FARDENVGIA 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 174 FHMGNCAENTAKKLEITRQQQDDFAIESYKRSAAAWANKVFQDEIAPVKIQQkRKP----------EIVISEDEEYKR-V 242
Cdd:PRK09052 152 YGMGLTAEKVAEQWKVSREDQDAFALESHQKAIAAQQAGEFKDEITPYEITE-RFPdlatgevdvkTRTVDLDEGPRAdT 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 243 NFDKFGQLATVFqRENGTVTAGNASTLNDGGAAVVLMSAEAAQKAGIKPLARIVAFQDAETDPIDFPIAPALAIPKLLKR 322
Cdd:PRK09052 231 SLEGLAKLKPVF-ANKGSVTAGNSSQTSDGAGAVILVSEKALKQFNLTPLARFVSFAVAGVPPEIMGIGPIEAIPAALKQ 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 323 AGVRKEDVAMWEVNEAFSLVVLANIKKLDVDPAKVNVHGGAVSIGHPIGMSGARLVAHLSHSL--KKGELGCASICNGGG 400
Cdd:PRK09052 310 AGLKQDDLDWIELNEAFAAQSLAVIRDLGLDPSKVNPLGGAIALGHPLGATGAIRTATVVHGLrrTNLKYGMVTMCVGTG 389
                        410
                 ....*....|.
gi 665390158 401 -GASSIlIEKL 410
Cdd:PRK09052 390 mGAAGI-FERL 399
PRK06504 PRK06504
acetyl-CoA C-acetyltransferase;
22-410 5.97e-75

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180595 [Multi-domain]  Cd Length: 390  Bit Score: 238.47  E-value: 5.97e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158  22 IAEVVVVSAARTPIGSFQSQLAPLTATQLGARAIEAAIEKAGIAKTDVQEVIMGNVVSAG-LGQAPARQAAIFAGLPTNV 100
Cdd:PRK06504   1 MAEAYIVAAARTAGGRKGGRLAGWHPADLAAQVLDALVDRSGADPALIEDVIMGCVSQVGeQATNVARNAVLASKLPESV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 101 CCTTVNKVCSSGMKAVMLGAQSLMLGYADVVVAGGMESMSNVPYYL------KRGATPYGGVNLT---DGIVFdglwdvy 171
Cdd:PRK06504  81 PGTSIDRQCGSSQQALHFAAQAVMSGTMDIVIAAGVESMTRVPMGSpstlpaKNGLGHYKSPGMEeryPGIQF------- 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 172 NKFhMGncAENTAKKLEITRQQQDDFAIESYKRSAAAWANKVFQDEIAPVKIQQKRKPEIVISEDEEYK-RVNFDKFGQL 250
Cdd:PRK06504 154 SQF-TG--AEMMAKKYGLSKDQLDEFALQSHQRAIAATQAGKFKAEIVPLEITRADGSGEMHTVDEGIRfDATLEGIAGV 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 251 ATVfqRENGTVTAGNASTLNDGGAAVVLMSAEAAQKAGIKPLARIVAFQDAETDPIDFPIAPALAIPKLLKRAGVRKEDV 330
Cdd:PRK06504 231 KLI--AEGGRLTAATASQICDGASGVMVVNERGLKALGVKPLARIHHMTVIGGDPVIMLEAPLPATERALKKAGMKIDDI 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 331 AMWEVNEAFSLVVLANIKKLDVDPAKVNVHGGAVSIGHPIGMSGARLVAHLSHSLKK--GELGCASICNGGGGASSILIE 408
Cdd:PRK06504 309 DLYEVNEAFASVPLAWLKATGADPERLNVNGGAIALGHPLGASGTKLMTTLVHALKQrgKRYGLQTMCEGGGMANVTIVE 388

                 ..
gi 665390158 409 KL 410
Cdd:PRK06504 389 RL 390
PRK07851 PRK07851
acetyl-CoA C-acetyltransferase;
24-410 3.32e-74

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181146 [Multi-domain]  Cd Length: 406  Bit Score: 237.21  E-value: 3.32e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158  24 EVVVVSAARTPIG-SFQSQLAPLTATQLGARAIEAAIEKA-GIAKTDVQEVIMGNVVSAG-LGQAPARQAAIFAGLPTnV 100
Cdd:PRK07851   3 EAVIVSTARSPIGrAFKGSLKDMRPDDLAAQMVRAALDKVpALDPTDIDDLMLGCGLPGGeQGFNMARVVAVLLGYDF-L 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 101 CCTTVNKVCSSGMKAVMLGAQSLMLGYADVVVAGGMESMSNV-------------PYY-------LKRGATpyGGVNLTD 160
Cdd:PRK07851  82 PGTTVNRYCSSSLQTTRMAFHAIKAGEGDVFISAGVETVSRFakgnsdslpdtknPLFaeaqartAARAEG--GAEAWHD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 161 GIVFDGLWDVYnkFHMGNCAENTAKKLEITRQQQDDFAIESYKRSAAAWANKVFQDEIAPVKIqqkrkPE-IVISEDEEY 239
Cdd:PRK07851 160 PREDGLLPDVY--IAMGQTAENVAQLTGISREEQDEWGVRSQNRAEEAIANGFFEREITPVTL-----PDgTVVSTDDGP 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 240 KR-VNFDKFGQLATVFqRENGTVTAGNASTLNDGGAAVVLMSAEAAQKAGIKPLARIVAFQDAETDPIDFPIAPALAIPK 318
Cdd:PRK07851 233 RAgTTYEKVSQLKPVF-RPDGTVTAGNACPLNDGAAAVVIMSDTKARELGLTPLARIVSTGVSGLSPEIMGLGPVEASKQ 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 319 LLKRAGVRKEDVAMWEVNEAFSLVVLANIKKLDVDPAKVNVHGGAVSIGHPIGMSGARLVAHLSHSLK--KGELGCASIC 396
Cdd:PRK07851 312 ALARAGMSIDDIDLVEINEAFAAQVLPSARELGIDEDKLNVSGGAIALGHPFGMTGARITTTLLNNLQthDKTFGLETMC 391
                        410
                 ....*....|....
gi 665390158 397 NGGGGASSILIEKL 410
Cdd:PRK07851 392 VGGGQGMAMVLERL 405
PRK07850 PRK07850
steroid 3-ketoacyl-CoA thiolase;
23-410 5.60e-73

steroid 3-ketoacyl-CoA thiolase;


Pssm-ID: 181145 [Multi-domain]  Cd Length: 387  Bit Score: 233.46  E-value: 5.60e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158  23 AEVVVVSAARTPIGSFQSQLAPLTATQLGARAIEAAIEKAGIAKTDVQEVIMGNVVSAG-LGQAPARQAAIFAGLPTNVC 101
Cdd:PRK07850   2 GNPVIVEAVRTPIGKRNGWLSGLHAAELLGAVQRAVLDRAGIDPGDVEQVIGGCVTQAGeQSNNITRTAWLHAGLPYHVG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 102 CTTVNKVCSSGMKAVMLGAQSLMLGYADVVVAGGMESMSNVPyyLKRGATPYGGVNLTDgivfDGLWDVYNKFhmgNCAE 181
Cdd:PRK07850  82 ATTIDCQCGSAQQANHLVAGLIAAGAIDVGIACGVEAMSRVP--LGANAGPGRGLPRPD----SWDIDMPNQF---EAAE 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 182 NTAKKLEITRQQQDDFAIESYKRSAAAWANKVFQDEIAPVK---IQQKRKPE---IVISEDEEYKRVNFDKFGQLATVfq 255
Cdd:PRK07850 153 RIAKRRGITREDVDAFGLRSQRRAAQAWAEGRFDREISPVQapvLDEEGQPTgetRLVTRDQGLRDTTMEGLAGLKPV-- 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 256 RENGTVTAGNASTLNDGGAAVVLMSAEAAQKAGIKPLARIVAFQDAETDP---IDFPIApalAIPKLLKRAGVRKEDVAM 332
Cdd:PRK07850 231 LEGGIHTAGTSSQISDGAAAVLWMDEDRARALGLRPRARIVAQALVGAEPyyhLDGPVQ---ATAKVLEKAGMKIGDIDL 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 333 WEVNEAFSLVVLANIKKLDVDPAKVNVHGGAVSIGHPIGMSGARLVAHLSHSLKK--GELGCASICNGGGGASSILIEKL 410
Cdd:PRK07850 308 VEINEAFASVVLSWAQVHEPDMDKVNVNGGAIALGHPVGSTGARLITTALHELERtdKSTALITMCAGGALSTGTIIERI 387
PRK08170 PRK08170
acetyl-CoA C-acetyltransferase;
25-410 7.88e-73

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181265 [Multi-domain]  Cd Length: 426  Bit Score: 234.14  E-value: 7.88e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158  25 VVVVSAARTPIGSFQSQLAPLTATQLGARAIEAAIEKAGIAKTDVQEVIMGNVVSAGLGQAPARQAAIFAGLPTNVCCTT 104
Cdd:PRK08170   5 VYIVDGARTPFLKARGGPGPFSASDLAVAAGRALLNRQPFAPDDLDEVILGCAMPSPDEANIARVVALRLGCGEKVPAWT 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 105 VNKVCSSGMKAVMLGAQSLMLGYADVVVAGGMESMSNVPYYLKR-GATPYGGVNLTDGIV-------------------- 163
Cdd:PRK08170  85 VQRNCASGMQALDSAAANIALGRADLVLAGGVEAMSHAPLLFSEkMVRWLAGWYAAKSIGqklaalgklrpsylapvigl 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 164 FDGLWDVYNKFHMGNCAENTAKKLEITRQQQDDFAIESYKRSAAAWANKVFQdEIAPVkIQQKRKpeiVISEDEEYKR-V 242
Cdd:PRK08170 165 LRGLTDPVVGLNMGQTAEVLAHRFGITREQMDAYAARSHQRLAAAQAEGRLK-EVVPL-FDRDGK---FYDHDDGVRPdS 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 243 NFDKFGQLATVFQRENGTVTAGNASTLNDGGAAVVLMSAEAAQKAGIKPLARIVAFQDAETDPIDFPIAPALAIPKLLKR 322
Cdd:PRK08170 240 SMEKLAKLKPFFDRPYGRVTAGNSSQITDGACWLLLASEEAVKKYGLPPLGRIVDSQWAALDPSQMGLGPVHAATPLLQR 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 323 AGVRKEDVAMWEVNEAFSLVVLANIKKLD-----------------VDPAKVNVHGGAVSIGHPIGMSGARLVAHLSHSL 385
Cdd:PRK08170 320 HGLTLEDLDLWEINEAFAAQVLACLAAWAdeeycreqlgldgalgeLDRERLNVDGGAIALGHPVGASGARIVLHLLHAL 399
                        410       420
                 ....*....|....*....|....*..
gi 665390158 386 KKGEL--GCASICNGGGGASSILIEKL 410
Cdd:PRK08170 400 KRRGTkrGIAAICIGGGQGGAMLLERV 426
fadA PRK08947
3-ketoacyl-CoA thiolase; Reviewed
24-410 1.25e-70

3-ketoacyl-CoA thiolase; Reviewed


Pssm-ID: 181592 [Multi-domain]  Cd Length: 387  Bit Score: 227.16  E-value: 1.25e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158  24 EVVVVSAARTPIG-SFQSQLAPLTATQLGARAIEAAIEK-AGIAKTDVQEVIMGnVVSAGLGQA--PARQAAIFAGLPTN 99
Cdd:PRK08947   3 DVVIVDAIRTPMGrSKGGAFRNVRAEDLSAHLMRSLLARnPALDPAEIDDIIWG-CVQQTLEQGfnIARNAALLAGIPHS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 100 VCCTTVNKVCSSGMKAVMLGAQSLMLGYADVVVAGGMESMSNVPyylkrgatpyggvnLTDGIVFD-GLWDVYNK--FHM 176
Cdd:PRK08947  82 VPAVTVNRLCGSSMQALHDAARAIMTGDGDVFLIGGVEHMGHVP--------------MNHGVDFHpGLSKNVAKaaGMM 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 177 GNCAENTAKKLEITRQQQDDFAIESYKRSAAAWANKVFQDEIAPVKIQQKRKPEIVISEDEEYK-RVNFDKFGQLATVFQ 255
Cdd:PRK08947 148 GLTAEMLGKMHGISREQQDAFAARSHQRAWAATQEGRFKNEIIPTEGHDADGVLKLFDYDEVIRpETTVEALAALRPAFD 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 256 RENGTVTAGNASTLNDGGAAVVLMSAEAAQKAGIKPLARIVAFQDAETDPIDFPIAPALAIPKLLKRAGVRKEDVAMWEV 335
Cdd:PRK08947 228 PVNGTVTAGTSSALSDGASAMLVMSESRAKELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISDIDVFEL 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 336 NEAF---SLVVLANIKKLDVDPAKVNVHGGAVSIGHPIGMSGARLVAHLSHSL--KKGELGCASICNGGGGASSILIEKL 410
Cdd:PRK08947 308 NEAFaaqSLPCLKDLGLLDKMDEKVNLNGGAIALGHPLGCSGARISTTLLNLMerKDAQFGLATMCIGLGQGIATVFERV 387
PRK08242 PRK08242
acetyl-CoA C-acetyltransferase;
24-410 3.87e-68

acetyl-CoA C-acetyltransferase;


Pssm-ID: 236197 [Multi-domain]  Cd Length: 402  Bit Score: 221.30  E-value: 3.87e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158  24 EVVVVSAARTPIGSFQSQ--LAPLTATQLGARAIEAAIEKAGIAKTDVQEVIMGNVVSAG-LGQAPARQAAIFAGLPTNV 100
Cdd:PRK08242   3 EAYIYDAVRTPRGKGKKDgsLHEVKPVRLAAGLLEALRDRNGLDTAAVDDVVLGCVTPVGdQGADIARTAVLAAGLPETV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 101 CCTTVNKVCSSGMKAVMLGAQSLMLGYADVVVAGGMESMSNVPYYLKRGATPYG-GVNLTDGIVFDGLwdvynkfhmgnC 179
Cdd:PRK08242  83 PGVQINRFCASGLEAVNLAAAKVRSGWDDLVIAGGVESMSRVPMGSDGGAWAMDpSTNFPTYFVPQGI-----------S 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 180 AENTAKKLEITRQQQDDFAIESYKRSAAAWANKVFQDEIAPVKIQQKrkpeIVISEDEEYKRVN--FDKFGQLATVFQ-- 255
Cdd:PRK08242 152 ADLIATKYGFSREDVDAYAVESQQRAAAAWAEGYFAKSVVPVKDQNG----LTILDHDEHMRPGttMESLAKLKPSFAmm 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 256 ------------------RENGTVTAGNASTLNDGGAAVVLMSAEAAQKAGIKPLARIVAFQDAETDPIDFPIAPALAIP 317
Cdd:PRK08242 228 gemggfdavalqkypeveRINHVHHAGNSSGIVDGAAAVLIGSEEAGKALGLKPRARIVATATIGSDPTIMLTGPVPATR 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 318 KLLKRAGVRKEDVAMWEVNEAFSLVVLANIKKLDVDPAKVNVHGGAVSIGHPIGMSGARLVAHLSHSLKK--GELGCASI 395
Cdd:PRK08242 308 KALAKAGLTVDDIDLFELNEAFASVVLRFMQALDIPHDKVNVNGGAIAMGHPLGATGAMILGTVLDELERrgKRTALITL 387
                        410
                 ....*....|....*
gi 665390158 396 CNGGGGASSILIEKL 410
Cdd:PRK08242 388 CVGGGMGIATIIERV 402
fadI PRK08963
3-ketoacyl-CoA thiolase; Reviewed
25-406 1.30e-63

3-ketoacyl-CoA thiolase; Reviewed


Pssm-ID: 181597 [Multi-domain]  Cd Length: 428  Bit Score: 210.23  E-value: 1.30e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158  25 VVVVSAARTPIGSFQSQLAPLTATQLGARAIEAAIEKAGIAKTDVQEVIMGNVVSagLGQAP--ARQAAIFAGLPTNVCC 102
Cdd:PRK08963   7 IAIVSGLRTPFAKQATAFHGIPAVDLGKMVVGELLARSEIDPELIEQLVFGQVVQ--MPEAPniAREIVLGTGMNVHTDA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 103 TTVNKVCSSGMKAVMLGAQSLMLGYADVVVAGGMESMSNVPYY-----------LKRGATPYGGVNLTDGIVFDGLWDV- 170
Cdd:PRK08963  85 YSVSRACATSFQAVANVAESIMAGTIDIGIAGGADSSSVLPIGvskklaralvdLNKARTLGQRLKLFSRLRLRDLLPVp 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 171 -----YNK-FHMGNCAENTAKKLEITRQQQDDFAIESYKRSAAAWANKVFQDEIAPVKIQQKRKPeivISEDEEYKR-VN 243
Cdd:PRK08963 165 pavaeYSTgLRMGDTAEQMAKTYGISREEQDALAHRSHQLAAQAWAEGKLDDEVMTAHVPPYKQP---LEEDNNIRGdST 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 244 FDKFGQLATVFQRENGTVTAGNASTLNDGGAAVVLMSAEAAQKAGIKPLARIVAFQDAETDPI-DFPIAPALAIPKLLKR 322
Cdd:PRK08963 242 LEDYAKLRPAFDRKHGTVTAANSTPLTDGAAAVLLMSESRAKALGLTPLGYLRSYAFAAIDVWqDMLLGPAYATPLALER 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 323 AGVRKEDVAMWEVNEAFSLVVLANIKKL-----------------DVDPAKVNVHGGAVSIGHPIGMSGARLVAHLSHSL 385
Cdd:PRK08963 322 AGLTLADLTLIDMHEAFAAQTLANLQMFaserfareklgrsqaigEVDMSKFNVLGGSIAYGHPFAATGARMITQTLHEL 401
                        410       420
                 ....*....|....*....|....
gi 665390158 386 KK--GELGCASICNGGG-GASSIL 406
Cdd:PRK08963 402 RRrgGGLGLTTACAAGGlGAAMVL 425
PRK06690 PRK06690
acetyl-CoA C-acyltransferase;
24-410 4.57e-63

acetyl-CoA C-acyltransferase;


Pssm-ID: 180659 [Multi-domain]  Cd Length: 361  Bit Score: 206.93  E-value: 4.57e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158  24 EVVVVSAARTPIGSFQSQLAPLTATQLGA---RAIEAAIEKagiaktDVQEVIMGNVVsaGLGQAPARQAAIFAGLPTNV 100
Cdd:PRK06690   2 RAVIVEAKRTPIGKKNGMLKDYEVQQLAApllTFLSKGMER------EIDDVILGNVV--GPGGNVARLSALEAGLGLHI 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 101 CCTTVNKVCSSGMKAVMLGAQSLMLGYADVVVAGGMESMSNVPYYLKRGATPyggvnltdgivfdglwDVYNKFHMGNCA 180
Cdd:PRK06690  74 PGVTIDRQCGAGLEAIRTACHFIQGGAGKCYIAGGVESTSTSPFQNRARFSP----------------ETIGDPDMGVAA 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 181 ENTAKKLEITRQQQDDFAIESYKRSAAAWANKVFQDEIAPVKIQqkrkpeivisEDEEYKRV-NFDKFGQLAT-VFQReN 258
Cdd:PRK06690 138 EYVAERYNITREMQDEYACLSYKRTLQALEKGYIHEEILSFNGL----------LDESIKKEmNYERIIKRTKpAFLH-N 206
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 259 GTVTAGNASTLNDGGAAVVLMSAEAAQKAGIKPLARIVAFQDAETDPIDFPIAPALAIPKLLKRAGVRKEDVAMWEVNEA 338
Cdd:PRK06690 207 GTVTAGNSCGVNDGACAVLVMEEGQARKLGYKPVLRFVRSAVVGVDPNLPGTGPIFAVNKLLNEMNMKVEDIDYFEINEA 286
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665390158 339 FSLVVLANIKKLDVDPAKVNVHGGAVSIGHPIGMSGARLVAHLSHSLKK--GELGCASICNGGGGASSILIEKL 410
Cdd:PRK06690 287 FASKVVACAKELQIPYEKLNVNGGAIALGHPYGASGAMLVTRLFYQAKRedMKYGIATLGIGGGIGLALLFEKV 360
PRK06025 PRK06025
acetyl-CoA C-acetyltransferase;
22-410 4.36e-59

acetyl-CoA C-acetyltransferase;


Pssm-ID: 235675 [Multi-domain]  Cd Length: 417  Bit Score: 198.08  E-value: 4.36e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158  22 IAEVVVVSAARTP--IGSF-QSQLAPLTATQLGARAIEAAIEKAGIAKTDVQEVIMGNVVSAGL-GQAPARQAAIFAGLP 97
Cdd:PRK06025   1 MAEAYIIDAVRTPrgIGKVgKGALAHLHPQHLAATVLKALAERNGLNTADVDDIIWSTSSQRGKqGGDLGRMAALDAGYD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158  98 TNVCCTTVNKVCSSGMKAVMLGAQSLMLGYADVVVAGGMESMSnvpyYLKRGATPYGGVNLTDGIVFDG---LWDVYNKF 174
Cdd:PRK06025  81 IKASGVTLDRFCGGGITSVNLAAAQIMSGMEDLVIAGGTEMMS----YTAAMAAEDMAAGKPPLGMGSGnlrLRALHPQS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 175 HMGNCAENTAKKLEITRQQQDDFAIESYKRSAAAWANKVFQDEIAPVKiqqkRKPEIVISEDEEYKR--VNFDKFGQLAT 252
Cdd:PRK06025 157 HQGVCGDAIATMEGITREALDALGLESQRRAARAIKEGRFDKSLVPVY----RDDGSVALDHEEFPRpqTTAEGLAALKP 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 253 VFQR-------ENGTV------------------TAGNASTLNDGGAAVVLMSAEAAQKAGIKPLARIVAFQDAETDPID 307
Cdd:PRK06025 233 AFTAiadypldDKGTTyrglinqkypdleikhvhHAGNSSGVVDGAAALLLASKAYAEKHGLKPRARIVAMANMGDDPTL 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 308 FPIAPALAIPKLLKRAGVRKEDVAMWEVNEAFSLVVLANIKKLDVDPAKVNVHGGAVSIGHPIGMSGARLVAHLSHSLKK 387
Cdd:PRK06025 313 MLNAPVPAAKKVLAKAGLTKDDIDLWEINEAFAVVAEKFIRDLDLDRDKVNVNGGAIALGHPIGATGSILIGTVLDELER 392
                        410       420
                 ....*....|....*....|....*
gi 665390158 388 --GELGCASICNGGGGASSILIEKL 410
Cdd:PRK06025 393 rgLKRGLVTMCAAGGMAPAIIIERV 417
nondecarbox_cond_enzymes cd00826
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ...
28-408 1.96e-56

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: 190.40  E-value: 1.96e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158  28 VSAARTPIGSF---QSQLAPLTATQLGARAIEAAIEKAGIAKTDVQEVIMGNVVSAGLGQAPARQAAIFAGLPTNVCCTT 104
Cdd:cd00826    1 AGAAMTAFGKFggeNGADANDLAHEAGAKAIAAALEPAGVAAGAVEEACLGQVLGAGEGQNCAQQAAMHAGGLQEAPAIG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 105 VNKVCSSGMKAVMLGAQSLMLGYADVVVAGGMESMS----NVPYYLKrgatpyggvnltdgivfdgLWDVYNKFHMGNCa 180
Cdd:cd00826   81 MNNLCGSGLRALALAMQLIAGGDANCILAGGFEKMEtsaeNNAKEKH-------------------IDVLINKYGMRAC- 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 181 entakkleitrqqQDDFAIESYKRSAAAWANKVFQDEIAPVkIQQKRKPEIVISEDEeYKR----VNFDKFGQLATVFQR 256
Cdd:cd00826  141 -------------PDAFALAGQAGAEAAEKDGRFKDEFAKF-GVKGRKGDIHSDADE-YIQfgdeASLDEIAKLRPAFDK 205
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 257 EnGTVTAGNASTLNDGGAAVVLMSAEAAQKAG-------IKPLARIVAFQDAETDPIDFPIA----PALAIPKLLKRAGV 325
Cdd:cd00826  206 E-DFLTAGNACGLNDGAAAAILMSEAEAQKHGlqskareIQALEMITDMASTFEDKKVIKMVggdgPIEAARKALEKAGL 284
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 326 RKEDVAMWEVNEAFSLVVLANIKKLDVDPAK------------------VNVHGGAVSIGHPIGMSGARLVAHLSHSLKK 387
Cdd:cd00826  285 GIGDLDLIEAHDAFAANACATNEALGLCPEGqggalvdrgdntyggksiINPNGGAIAIGHPIGASGAAICAELCFELKG 364
                        410       420
                 ....*....|....*....|....*...
gi 665390158 388 GEL-------GCASICNGGGGASSILIE 408
Cdd:cd00826  365 EAGkrqgagaGLALLCIGGGGGAAMCIE 392
Thiolase_C pfam02803
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
290-409 6.06e-52

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: 169.75  E-value: 6.06e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158  290 KPLARIVAFQDAETDPIDFPIAPALAIPKLLKRAGVRKEDVAMWEVNEAFSLVVLANIKKLDVDPAKVNVHGGAVSIGHP 369
Cdd:pfam02803   2 KPLARIRSYATAGVDPAIMGIGPAYAIPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGIDPEKVNVNGGAIALGHP 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 665390158  370 IGMSGARLVAHLSHSLKK--GELGCASICNGGGGASSILIEK 409
Cdd:pfam02803  82 LGASGARILVTLLHELKRrgGKYGLASLCIGGGQGVAMIIER 123
PRK09268 PRK09268
acetyl-CoA C-acetyltransferase;
25-406 3.83e-42

acetyl-CoA C-acetyltransferase;


Pssm-ID: 236440 [Multi-domain]  Cd Length: 427  Bit Score: 153.13  E-value: 3.83e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158  25 VVVVSAARTPIGSFQSQLAPLTATQLGARAIEAAIEKAGIAKTDVQEVIMGNVVSAGLGQAPARQAAIFAGLPTNVCCTT 104
Cdd:PRK09268   9 VAILGGNRIPFARSNGAYADASNQDMLTAALDGLVDRFGLQGERLGEVVAGAVLKHSRDFNLTRECVLGSALSPYTPAYD 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 105 VNKVCSSGMKAVMLGAQSLMLGYADVVVAGGMESMSNVP-----------YYLKRGATPYGGVNLTDGIvfdglwdvyNK 173
Cdd:PRK09268  89 LQQACGTGLEAAILVANKIALGQIDSGIAGGVDTTSDAPiavneglrkilLELNRAKTTGDRLKALGKL---------RP 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 174 FH----------------MGNCAENTAKKLEITRQQQDDFAIESYKRSAAAWANKVFQDEIAP---VKIQQKRKPEIVIs 234
Cdd:PRK09268 160 KHlapeiprngeprtglsMGEHAAITAKEWGISREAQDELAAASHQNLAAAYDRGFFDDLITPflgLTRDNNLRPDSSL- 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 235 edeeykrvnfDKFGQLATVFQR-ENGTVTAGNASTLNDGGAAVVLMSAEAAQKAGIKPLARIVafqDAETDPIDFP---- 309
Cdd:PRK09268 239 ----------EKLAKLKPVFGKgGRATMTAGNSTPLTDGASVVLLASEEWAAEHGLPVLAYLV---DAETAAVDFVhgke 305
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 310 ---IAPALAIPKLLKRAGVRKEDVAMWEVNEAFSLVVLANIKK------------LD-----VDPAKVNVHGGAVSIGHP 369
Cdd:PRK09268 306 gllMAPAYAVPRLLARNGLTLQDFDFYEIHEAFASQVLATLKAwedeeycrerlgLDaplgsIDRSKLNVNGSSLAAGHP 385
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|
gi 665390158 370 IGMSGARLVAHLSHSL--KKGELGCASICNGGG-GASSIL 406
Cdd:PRK09268 386 FAATGGRIVATLAKLLaeKGSGRGLISICAAGGqGVTAIL 425
SCP-x_thiolase cd00829
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ...
49-391 9.50e-24

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: 101.57  E-value: 9.50e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158  49 QLGARAIEAAIEKAGIAKTDVQEVIMGNVVSAGLGQAPARQAAIFAGLpTNVCCTTVNKVCSSGMKAVMLGAQSLMLGYA 128
Cdd:cd00829   18 ELAAEAARAALDDAGLEPADIDAVVVGNAAGGRFQSFPGALIAEYLGL-LGKPATRVEAAGASGSAAVRAAAAAIASGLA 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 129 DVVVAGGMESMSNVPY----------YLKRGATPYGGVNLTDgivFDGLwdvYNKFHMgncaentaKKLEITRqqqDDFA 198
Cdd:cd00829   97 DVVLVVGAEKMSDVPTgdeaggrasdLEWEGPEPPGGLTPPA---LYAL---AARRYM--------HRYGTTR---EDLA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 199 IESYKRSAAAWANK--VFQDEIAPVKIQQKRkpeiVISEDeeykrvnfdkfgqlatvfqrengtVTAGNASTLNDGGAAV 276
Cdd:cd00829  160 KVAVKNHRNAARNPyaQFRKPITVEDVLNSR----MIADP------------------------LRLLDCCPVSDGAAAV 211
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 277 VLMSAEAAQKAGIKPlARIVAFQDAE-----TDPIDFPIAPA--LAIPKLLKRAGVRKEDVAMWEVNEAFSLVVLANI-- 347
Cdd:cd00829  212 VLASEERARELTDRP-VWILGVGAASdtpslSERDDFLSLDAarLAARRAYKMAGITPDDIDVAELYDCFTIAELLALed 290
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 348 ---------KKLDVDPA-------KVNVHGGAVSIGHPIGMSGARLVAHLSHSLkKGELG 391
Cdd:cd00829  291 lgfcekgegGKLVREGDtaiggdlPVNTSGGLLSKGHPLGATGLAQAVEAVRQL-RGEAG 349
cond_enzymes cd00327
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ...
46-407 1.13e-16

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: 79.03  E-value: 1.13e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158  46 TATQLGARAIEAAIEKAGIAKTDVQEVIMGNVVSAGLGQAPARQAAIFAGLPtNVCCTTVNKVCSSGMKAVMLGAQSLML 125
Cdd:cd00327    6 TASELGFEAAEQAIADAGLSKGPIVGVIVGTTGGSGEFSGAAGQLAYHLGIS-GGPAYSVNQACATGLTALALAVQQVQN 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 126 GYADVVVAGGMESmsnvpyylkrgatpyggvnltdgivfdglwdvynkfhmgncaentakkleitrqqqddfaiesykrs 205
Cdd:cd00327   85 GKADIVLAGGSEE------------------------------------------------------------------- 97
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 206 aaawankvfqdeiapvkiqqkrkpeivisedeeykrvnfdkfgqlatvfqrengtvtagnaSTLNDGGAAVVLMSAEAAQ 285
Cdd:cd00327   98 -------------------------------------------------------------FVFGDGAAAAVVESEEHAL 116
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 286 KAGIKPLARIVA----FQDAETDPIDFPIAPALAIPKLLKRAGVRKEDVAMWEVNEAFSLVVLANIKKLDVDPAKV---N 358
Cdd:cd00327  117 RRGAHPQAEIVStaatFDGASMVPAVSGEGLARAARKALEGAGLTPSDIDYVEAHGTGTPIGDAVELALGLDPDGVrspA 196
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 665390158 359 VHGGAVSIGHPIGMSGARLVAHLSHSLKKGE---------LGCASICNGGGGASSILI 407
Cdd:cd00327  197 VSATLIMTGHPLGAAGLAILDELLLMLEHEFipptpreprTVLLLGFGLGGTNAAVVL 254
PRK06064 PRK06064
thiolase domain-containing protein;
25-386 4.02e-15

thiolase domain-containing protein;


Pssm-ID: 235688 [Multi-domain]  Cd Length: 389  Bit Score: 76.47  E-value: 4.02e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158  25 VVVVSAARTPIG-----SFQSqlapltatqLGARAIEAAIEKAGIAKTDVQEVIMGNVvSAGL--GQA-PARQAAIFAGL 96
Cdd:PRK06064   4 VAIIGVGQTKFGelwdvSLRD---------LAVEAGLEALEDAGIDGKDIDAMYVGNM-SAGLfvSQEhIAALIADYAGL 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158  97 pTNVCCTTVNKVCSSGMKAVMLGAQSLMLGYADVVVAGGMESMSNVPyylKRGATPYGGV------NLTDGIVFDGLWDV 170
Cdd:PRK06064  74 -APIPATRVEAACASGGAALRQAYLAVASGEADVVLAAGVEKMTDVP---TPDATEAIARagdyewEEFFGATFPGLYAL 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 171 YNKFHMgncaentaKKLEITRQQQDDFAIESYKrSAAAWANKVFQDEIapvkiqqkrkpeivisedeeykrvnfdkfgql 250
Cdd:PRK06064 150 IARRYM--------HKYGTTEEDLALVAVKNHY-NGSKNPYAQFQKEI-------------------------------- 188
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 251 aTVFQRENGTVTAG-----NASTLNDGGAAVVLMSAEAAQKAGIKPLaRIVAFQDAeTDPI------DFPI--APALAIP 317
Cdd:PRK06064 189 -TVEQVLNSPPVADplkllDCSPITDGAAAVILASEEKAKEYTDTPV-WIKASGQA-SDTIalhdrkDFTTldAAVVAAE 265
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 318 KLLKRAGVRKEDVAMWEVNEAFSLVVLANIKKLDVdpAK--------------------VNVHGGAVSIGHPIGMSGARL 377
Cdd:PRK06064 266 KAYKMAGIEPKDIDVAEVHDCFTIAEILAYEDLGF--AKkgeggklaregqtyiggdipVNPSGGLKAKGHPVGATGVSQ 343

                 ....*....
gi 665390158 378 VAHLSHSLK 386
Cdd:PRK06064 344 AVEIVWQLR 352
PTZ00455 PTZ00455
3-ketoacyl-CoA thiolase; Provisional
46-400 3.54e-10

3-ketoacyl-CoA thiolase; Provisional


Pssm-ID: 240424 [Multi-domain]  Cd Length: 438  Bit Score: 61.45  E-value: 3.54e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158  46 TATQLGARAIEAAIEKAGI-AKTD-VQEVIMGNVVSAGLG-QAPARQAAIFAGLPTNVCCTTVNK-------VCSSGMKA 115
Cdd:PTZ00455  47 TLEELLATAIQGTLENTGLdGKAAlVDKVVVGNFLGELFSsQGHLGPAAVGSLGQSGASNALLYKpamrvegACASGGLA 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 116 VMLGAQSLMLGYADVVVAGGMESMSNVPY-----YLKRGATpYGGVNLTDGIVFDGLWdvynkfhmgncaentAKKLEIT 190
Cdd:PTZ00455 127 VQSAWEALLAGTSDIALVVGVEVQTTVSArvggdYLARAAD-YRRQRKLDDFTFPCLF---------------AKRMKYI 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 191 rQQQDDFAIESYKRSAA-AWANkvfqDEIAPVKIQQKRKPEIVISEDEEYKRVNFdkfgqLATVFQRENGTVTagNASTL 269
Cdd:PTZ00455 191 -QEHGHFTMEDTARVAAkAYAN----GNKNPLAHMHTRKLSLEFCTGASDKNPKF-----LGNETYKPFLRMT--DCSQV 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 270 NDGGAAVVLMSAEAAQKAGIKP--------LARIVAFQDAETDPIDFP--IAPALAIPKLLKRAGVRKEDVAMWEVNEAF 339
Cdd:PTZ00455 259 SDGGAGLVLASEEGLQKMGLSPndsrlveiKSLACASGNLYEDPPDATrmFTSRAAAQKALSMAGVKPSDLQVAEVHDCF 338
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 340 SLVVLANIKKLDV-DPAK-----------------VNVHGGAVSIGHPIGMSGARLVAHLSHSLK--------KGELGCA 393
Cdd:PTZ00455 339 TIAELLMYEALGIaEYGHakdlirngatalegripVNTGGGLLSFGHPVGATGVKQIMEVYRQMKgqcgeyqmKNIPALG 418

                 ....*..
gi 665390158 394 SICNGGG 400
Cdd:PTZ00455 419 ATLNMGG 425
PRK12578 PRK12578
thiolase domain-containing protein;
45-391 1.55e-09

thiolase domain-containing protein;


Pssm-ID: 183606 [Multi-domain]  Cd Length: 385  Bit Score: 59.09  E-value: 1.55e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158  45 LTATQLGARAIEAAIEKAGIAKTDVQEVIMGNVVSAGLGQAPARQAAIFAGLpTNVCCTTVNKVCSSGMKAVMLGAQSLM 124
Cdd:PRK12578  19 VSVQELAWESIKEALNDAGVSQTDIELVVVGSTAYRGIELYPAPIVAEYSGL-TGKVPLRVEAMCATGLAASLTAYTAVA 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 125 LGYADVVVAGGMESMSNVPYYLKRGATPYGGVNLTD----GIVFDGLWDVYNKFHMGncaentakKLEITRQQQDDFAIE 200
Cdd:PRK12578  98 SGLVDMAIAVGVDKMTEVDTSTSLAIGGRGGNYQWEyhfyGTTFPTYYALYATRHMA--------VYGTTEEQMALVSVK 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 201 SYKrSAAAWANKVFQDEIAPVKIQQKRkpeiVISedeeYKRVNFDkfgqlatvfqrengtvtagnASTLNDGGAAVVLMS 280
Cdd:PRK12578 170 AHK-YGAMNPKAHFQKPVTVEEVLKSR----AIS----WPIKLLD--------------------SCPISDGSATAIFAS 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 281 AEAAQKAGIKPLARI--------VAFQDAETDPIDFPiAPALAIPKLLKRAGVRKEDVAMWEVNEAFSLVVLANIKKLD- 351
Cdd:PRK12578 221 EEKVKELKIDSPVWItgigyandYAYVARRGEWVGFK-ATQLAARQAYNMAKVTPNDIEVATVHDAFTIAEIMGYEDLGf 299
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 665390158 352 VDPAK-----------------VNVHGGAVSIGHPIGMSGARLVAHLSHSLkKGELG 391
Cdd:PRK12578 300 TEKGKggkfieegqsekggkvgVNLFGGLKAKGHPLGATGLSMIYEITKQL-RDEAG 355
PRK08256 PRK08256
lipid-transfer protein; Provisional
48-381 4.90e-09

lipid-transfer protein; Provisional


Pssm-ID: 181327 [Multi-domain]  Cd Length: 391  Bit Score: 57.60  E-value: 4.90e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158  48 TQLGARAIEAAIEKAGIAKTDVQEVIMGNVvsagLGQAPARQAAIF-AGLpTNVCCTTVNKVCSSGMKAVMLGAQSLMLG 126
Cdd:PRK08256  23 PDMAAEAGRAALADAGIDYDAVQQAYVGYV----YGDSTSGQRALYeVGM-TGIPIVNVNNNCSTGSTALFLARQAVRSG 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 127 YADVVVAGGMESMSnvPYYLKRGAT----PYGG-VNLTDGIV-FDGLWDVYNKFhmGNCAENTAKKLEITRQQqddFAIE 200
Cdd:PRK08256  98 AADCALALGFEQMQ--PGALGSVWDdrpsPLERfDKALAELQgFDPAPPALRMF--GGAGREHMEKYGTTAET---FAKI 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 201 SYKRSAAAWAN--KVFQDEiapvkiqqkrkpeivISEDEeykrVNFDKfgqlaTVFqrenGTVTAGNASTLNDGGAAVVL 278
Cdd:PRK08256 171 GVKARRHAANNpyAQFRDE---------------YTLED----VLASP-----MIW----GPLTRLQCCPPTCGAAAAIV 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 279 MSAEAAQKAGIKPLARIVAfQDAETD---------PID---FPIAPAlAIPKLLKRAGVRKEDVAMWEVNEAFS------ 340
Cdd:PRK08256 223 CSEEFARKHGLDRAVEIVA-QAMTTDtpstfdgrsMIDlvgYDMTRA-AAQQVYEQAGIGPEDIDVVELHDCFSanellt 300
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 665390158 341 -----LVVLANIKKLDVDPAK-------VNVHGGAVSIGHPIGMSG----ARLVAHL 381
Cdd:PRK08256 301 yealgLCPEGEAEKFIDDGDNtyggrwvVNPSGGLLSKGHPLGATGlaqcAELTWQL 357
PRK06157 PRK06157
acetyl-CoA acetyltransferase; Validated
54-379 2.95e-07

acetyl-CoA acetyltransferase; Validated


Pssm-ID: 180433 [Multi-domain]  Cd Length: 398  Bit Score: 52.34  E-value: 2.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158  54 AIEAAIEKAGIAKTDVQEVIMG---NVVSAGLGQAPARQAAIFAGLPtnvcCTTVNKVCSSGMKAVMLGAQSLMLGYADV 130
Cdd:PRK06157  34 AFLEALADAGIEPKDIDAAWFGthyDEIGSGKSGTPLSRALRLPNIP----VTRVENFCATGSEAFRGAVYAVASGAYDI 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 131 VVAGGMESMSNvpyylkrgaTPYGGVNLTD-GIVFDGLW-DVYNKFHMGNCAENTAKKLEITRQQqddfaiesYKRSAA- 207
Cdd:PRK06157 110 ALALGVEKLKD---------TGYGGLPVANpGTLADMTMpNVTAPGNFAQLASAYAAKYGVSRED--------LKRAMAh 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 208 -AWANkvfQDEIAPVKIQQKRKPeivISEDeeykrvnfdkfgqlatvfQRENGTVTAGN-----ASTLNDGGAAVVLMSA 281
Cdd:PRK06157 173 vSVKS---HANGARNPKAHLRKA---VTEE------------------QVLKAPMIAGPlglfdCCGVSDGAAAAIVTTP 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 282 EAAQKAGIKPLARIVAFQDA------ETDP-IDFPIAPALAIP--KLLKRAGVR--KEDVAMWEVNEAFSLVVLANIKKL 350
Cdd:PRK06157 229 EIARALGKKDPVYVKALQLAvsngweLQYNgWDGSYFPTTRIAarKAYREAGITdpREELSMAEVHDCFSITELVTMEDL 308
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 665390158 351 -----------------DVDPA-KVNVHGGAVSIGHPIGMSGARLVA 379
Cdd:PRK06157 309 glsergqawrdvldgffDADGGlPCQIDGGLKCFGHPIGASGLRMLY 355
PRK07516 PRK07516
thiolase domain-containing protein;
25-374 5.88e-07

thiolase domain-containing protein;


Pssm-ID: 181013 [Multi-domain]  Cd Length: 389  Bit Score: 51.10  E-value: 5.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158  25 VVVVSAARTPIGsfqsQLAPLTATQLGARAIEAAIEKAGIAKTDVQEVIMGNVVSAGLGQA-PARQAAIFAGLPTNVCCT 103
Cdd:PRK07516   4 ASIVGWAHTPFG----KLDAETLESLIVRVAREALAHAGIAAGDVDGIFLGHFNAGFSPQDfPASLVLQADPALRFKPAT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 104 TVNKVCSSGMKAVMLGAQSLMLGYADVVVAGGMESMSNVPY-----------YLKRGATPYGGvnltdgivFDGLWdvyn 172
Cdd:PRK07516  80 RVENACATGSAAVYAALDAIEAGRARIVLVVGAEKMTATPTaevgdillgasYLKEEGDTPGG--------FAGVF---- 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 173 kfhmGNCAENTAKKLeitRQQQDDFAIESYKRSAAAWANkvfqdeiapvKIQQKRKPeivisEDEEYKRVNFDKFGQLAT 252
Cdd:PRK07516 148 ----GRIAQAYFQRY---GDQSDALAMIAAKNHANGVAN----------PYAQMRKD-----LGFEFCRTVSEKNPLVAG 205
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 253 VFQREngtvtagNASTLNDGGAAVVLMSAEAAQKagikpLARIVAF------QD----AETDPIDFPiAPALAIPKLLKR 322
Cdd:PRK07516 206 PLRRT-------DCSLVSDGAAALVLADAETARA-----LQRAVRFrarahvNDflplSRRDPLAFE-GPRRAWQRALAQ 272
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 323 AGVRKEDVAMWEVNEAFSLVVLANIKKLDVDPA------------------KVNVHGGAVSIGHPIGMSG 374
Cdd:PRK07516 273 AGVTLDDLSFVETHDCFTIAELIEYEAMGLAPPgqgarairegwtakdgklPVNPSGGLKAKGHPIGATG 342
PRK06289 PRK06289
acetyl-CoA acetyltransferase; Provisional
50-378 9.13e-07

acetyl-CoA acetyltransferase; Provisional


Pssm-ID: 235771 [Multi-domain]  Cd Length: 403  Bit Score: 50.46  E-value: 9.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158  50 LGARAIEAAIEKAGIAKTDVQEVIMGNVVS---AGLGQAPARQAAI---FAGLPTnvccTTVNKVCSSGMKAVMLGAQSL 123
Cdd:PRK06289  29 LTREVVDGTLAAAGVDADDIEVVHVGNFFGelfAGQGHLGAMPATVhpaLWGVPA----SRHEAACASGSVATLAAMADL 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 124 MLGYADVVVAGGMESMSNVPyylkrgaTPYGGVNLtdgivfdglwdvynkfhmgncaentakkleitrqqqddfaiesyk 203
Cdd:PRK06289 105 RAGRYDVALVVGVELMKTVP-------GDVAAEHL--------------------------------------------- 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 204 rSAAAWANKVFQDE-------IAPVKIQQKRKPEIVISEDEEYKRVNFDK-------------FGQLATVFQRENGTVTA 263
Cdd:PRK06289 133 -GAAAWTGHEGQDArfpwpsmFARVADEYDRRYGLDEEHLRAIAEINFANarrnpnaqtrgwaFPDEATNDDDATNPVVE 211
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 264 G-----NASTLNDGGAAVVLMSAEAAQK-AGIKPLARIVAF-------------QDAETDPIDFPIAPAlAIPKLLKRAG 324
Cdd:PRK06289 212 GrlrrqDCSQVTDGGAGVVLASDAYLRDyADARPIPRIKGWghrtaplgleqklDRSAGDPYVLPHVRQ-AVLDAYRRAG 290
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665390158 325 VRKEDVAMWEVNEAFSLVVLANIKKL---------------DVDPA---KVNVHGGAVSIGHPIGMSGARLV 378
Cdd:PRK06289 291 VGLDDLDGFEVHDCFTPSEYLAIDHIgltgpgeswkaiengEIAIGgrlPINPSGGLIGGGHPVGASGVRML 362
FabB COG0304
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...
47-141 3.49e-06

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: 48.94  E-value: 3.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158  47 ATQLGARAIEAAIEKAGIAKTDVQEVIMGNVVSAGLGQ------------------------------APARQAAIFAGL 96
Cdd:COG0304   71 FTQYALAAAREALADAGLDLDEVDPDRTGVIIGSGIGGldtleeayrallekgprrvspffvpmmmpnMAAGHVSIRFGL 150
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 665390158  97 pTNVCCTTVNKvCSSGMKAVMLGAQSLMLGYADVVVAGGMESMSN 141
Cdd:COG0304  151 -KGPNYTVSTA-CASGAHAIGEAYRLIRRGRADVMIAGGAEAAIT 193
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
17-141 6.34e-06

Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible for the elongation steps in fatty acid biosynthesis. KASIII catalyses the initial condensation and KAS I and II catalyze further elongation steps by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP.


Pssm-ID: 238430 [Multi-domain]  Cd Length: 406  Bit Score: 47.92  E-value: 6.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158  17 NYSSKIAEVVVVSAARTPIgsFQSQLAPLT-ATQLGARAIEAAIEKAGIAKTDVQEVIMGNVVSAGLGQ----------- 84
Cdd:cd00834   42 GFPSRIAGEVPDFDPEDYL--DRKELRRMDrFAQFALAAAEEALADAGLDPEELDPERIGVVIGSGIGGlatieeayral 119
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665390158  85 -------------------APARQAAIFAGLpTNVCCTTVNkVCSSGMKAVMLGAQSLMLGYADVVVAGGMESMSN 141
Cdd:cd00834  120 lekgprrvspffvpmalpnMAAGQVAIRLGL-RGPNYTVST-ACASGAHAIGDAARLIRLGRADVVIAGGAEALIT 193
PRK05952 PRK05952
beta-ketoacyl-ACP synthase;
244-379 6.70e-06

beta-ketoacyl-ACP synthase;


Pssm-ID: 235653 [Multi-domain]  Cd Length: 381  Bit Score: 47.74  E-value: 6.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 244 FDKFGQLATV----F--QREnGTVtagnastLNDGGAAVVLMSAEAAQKAGIKPLARIVAF---QDAE---TDPIDFPIA 311
Cdd:PRK05952 185 FQQMGALAKTgaypFdrQRE-GLV-------LGEGGAILVLESAELAQKRGAKIYGQILGFgltCDAYhmsAPEPDGKSA 256
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665390158 312 pALAIPKLLKRAGVRKEDV-------AMWEVNEAFSLVVLANIKkldvdPAKVNVHGGAVSIGHPIGMSGARLVA 379
Cdd:PRK05952 257 -IAAIQQCLARSGLTPEDIdyihahgTATRLNDQREANLIQALF-----PHRVAVSSTKGATGHTLGASGALGVA 325
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
104-139 1.01e-03

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: 40.70  E-value: 1.01e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 665390158  104 TVNKVCSSGMKAVMLGAQSLMLGYADVVVAGGMESM 139
Cdd:pfam00109 168 TVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLL 203
PRK06059 PRK06059
lipid-transfer protein; Provisional
24-139 2.74e-03

lipid-transfer protein; Provisional


Pssm-ID: 180373 [Multi-domain]  Cd Length: 399  Bit Score: 39.75  E-value: 2.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158  24 EVVVVSAARTPIGSFqsqlaPLTATQLGARAIEAAIEKAGIAKTDVQEVIMGNVVSAG----LGQAPARQAAIFAGLPtn 99
Cdd:PRK06059   5 PVYILGAGMHPWGKW-----GRDFVEYGVVAARAALADAGLDWRDVQLVVGADTIRNGypgfVAGATFAQALGWNGAP-- 77
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 665390158 100 vcCTTVNKVCSSGMKAVMLGAQSLMLGYADVVVAGGMESM 139
Cdd:PRK06059  78 --VSSSYAACASGSQALQSARAQILAGLCDVALVVGADTT 115
PRK08313 PRK08313
thiolase domain-containing protein;
271-374 4.27e-03

thiolase domain-containing protein;


Pssm-ID: 181378 [Multi-domain]  Cd Length: 386  Bit Score: 38.94  E-value: 4.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 271 DGGAAVVLMSAEAAQKAGIKPLARIVAfQDAETDPIDF-------PIAPALAIPKLLKRAGV---RKE-DVA-------- 331
Cdd:PRK08313 210 DGACAVVIGDEEAADAAAGRPVAWIHG-TAMRTEPLAFagrdqvnPQAGRDAAAALWKAAGItdpRDEiDVAeiyvpfsw 288
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 665390158 332 ---MWEVNEAFS------LVVLANIKKLDVDpAKVNVHGGAVSiGHPIGMSG 374
Cdd:PRK08313 289 fepMWLENLGFApegegwKLTEAGETAIGGR-LPVNPSGGVLS-SNPIGASG 338
PRK07314 PRK07314
beta-ketoacyl-ACP synthase II;
102-138 7.99e-03

beta-ketoacyl-ACP synthase II;


Pssm-ID: 235987 [Multi-domain]  Cd Length: 411  Bit Score: 38.23  E-value: 7.99e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 665390158 102 CTTVNKVCSSGMKAVMLGAQSLMLGYADVVVAGGMES 138
Cdd:PRK07314 155 NHSIVTACATGAHAIGDAARLIAYGDADVMVAGGAEA 191
FabH COG0332
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl- ...
46-142 8.59e-03

3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl-[acyl-carrier-protein] synthase III is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440101 [Multi-domain]  Cd Length: 323  Bit Score: 37.78  E-value: 8.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158  46 TATQLGARAIEAAIEKAGIAKTDVQEVI------------MGNVVSAGLGqapARQAAIFaglptnvcctTVNKVCSSGM 113
Cdd:COG0332   50 TTSDLAVEAARKALEAAGIDPEDIDLIIvatvtpdylfpsTACLVQHKLG---AKNAAAF----------DINAACSGFV 116
                         90       100       110
                 ....*....|....*....|....*....|
gi 665390158 114 KAVMLGAQSLMLGYAD-VVVAGGmESMSNV 142
Cdd:COG0332  117 YALSVAAALIRSGQAKnVLVVGA-ETLSRI 145
PRK06519 PRK06519
beta-ketoacyl-ACP synthase;
248-333 8.81e-03

beta-ketoacyl-ACP synthase;


Pssm-ID: 235819 [Multi-domain]  Cd Length: 398  Bit Score: 38.01  E-value: 8.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390158 248 GQLATVFQRENGtvtAGNASTLNDGGAAVVLMSAEAAQKAGIKPLARIVAFQDAETDPIDFPIAPALAipKLLKRAGVRK 327
Cdd:PRK06519 223 GGWAPVWSRGGE---DGGGFILGSGGAFLVLESREHAEARGARPYARISGVESDRARRAPGDLEASLE--RLLKPAGGLA 297

                 ....*.
gi 665390158 328 EDVAMW 333
Cdd:PRK06519 298 APTAVI 303
 
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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