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Conserved domains on  [gi|1841866749|ref|XP_034265489|]
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acetyl-CoA acetyltransferase, mitochondrial [Pantherophis guttatus]

Protein Classification

thiolase family protein( domain architecture ID 10091456)

thiolase family protein may catalyze the reversible thiolytic cleavage of 3-ketoacyl-CoA into acyl-CoA and acetyl-CoA, a 2-step reaction involving a covalent intermediate formed with a catalytic cysteine; such as acetyl-CoA acetyltransferase, which catalyzes the transfer of an acetyl group from acetyl-CoA to another molecule of acetyl-CoA to form acetoacetyl-CoA

CATH:  3.40.47.10
EC:  2.3.1.-
Gene Ontology:  GO:0016746|GO:0006635
PubMed:  16356722
SCOP:  4000245

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
thiolase cd00751
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ...
31-414 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: 558.25  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749  31 VIVSAVRTPIGSFQSSLFSLPATNLGSIAIKGAIEKAGIPSQEVKEVYMGNVIQAGEGQAPARQATLGAGLPVSTPCTTV 110
Cdd:cd00751     1 VIVSAVRTPIGRFGGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGEGQNPARQAALLAGLPESVPATTV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 111 NKVCASGMKSIMMAAQSLMCGSQDVMVAGGMESMSNVPYTMTRGTTPY-GGVKLEDLIVKDGLTDVYNKIHMGNCAENTA 189
Cdd:cd00751    81 NRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGrLGLNTLDGMLDDGLTDPFTGLSMGITAENVA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 190 KKFSISREDQDTYAIKSYTKSKEGWESGIFAKEIVPVTISQKGKPDTeVKEDEEYKR-VDFSKVPKLKTVFqKENGTVTA 268
Cdd:cd00751   161 EKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEVPGRKGPVV-VDRDEGPRPdTTLEKLAKLKPAF-KKDGTVTA 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 269 ANASTLNDGAAALVLMTSEAAKRLNVKPLARIVGFADAAVDPIDFPIAPAHAVPKILAQTGLKKEDIKMWEINEAFSVVV 348
Cdd:cd00751   239 GNASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDIDLIEINEAFAAQA 318
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1841866749 349 LANIKMLDIDPQKVNIHGGAVSLGHPIGMSGARIVVHMTHALKQ--GEHGLAGICNGGGGASAILIQK 414
Cdd:cd00751   319 LACLKELGLDPEKVNVNGGAIALGHPLGASGARIVVTLLHELKRrgGRYGLATMCIGGGQGAAMVIER 386
 
Name Accession Description Interval E-value
thiolase cd00751
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ...
31-414 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: 558.25  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749  31 VIVSAVRTPIGSFQSSLFSLPATNLGSIAIKGAIEKAGIPSQEVKEVYMGNVIQAGEGQAPARQATLGAGLPVSTPCTTV 110
Cdd:cd00751     1 VIVSAVRTPIGRFGGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGEGQNPARQAALLAGLPESVPATTV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 111 NKVCASGMKSIMMAAQSLMCGSQDVMVAGGMESMSNVPYTMTRGTTPY-GGVKLEDLIVKDGLTDVYNKIHMGNCAENTA 189
Cdd:cd00751    81 NRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGrLGLNTLDGMLDDGLTDPFTGLSMGITAENVA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 190 KKFSISREDQDTYAIKSYTKSKEGWESGIFAKEIVPVTISQKGKPDTeVKEDEEYKR-VDFSKVPKLKTVFqKENGTVTA 268
Cdd:cd00751   161 EKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEVPGRKGPVV-VDRDEGPRPdTTLEKLAKLKPAF-KKDGTVTA 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 269 ANASTLNDGAAALVLMTSEAAKRLNVKPLARIVGFADAAVDPIDFPIAPAHAVPKILAQTGLKKEDIKMWEINEAFSVVV 348
Cdd:cd00751   239 GNASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDIDLIEINEAFAAQA 318
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1841866749 349 LANIKMLDIDPQKVNIHGGAVSLGHPIGMSGARIVVHMTHALKQ--GEHGLAGICNGGGGASAILIQK 414
Cdd:cd00751   319 LACLKELGLDPEKVNVNGGAIALGHPLGASGARIVVTLLHELKRrgGRYGLATMCIGGGQGAAMVIER 386
PLN02644 PLN02644
acetyl-CoA C-acetyltransferase
29-415 0e+00

acetyl-CoA C-acetyltransferase


Pssm-ID: 215347 [Multi-domain]  Cd Length: 394  Bit Score: 552.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749  29 EVVIVSAVRTPIGSFQSSLFSLPATNLGSIAIKGAIEKAGIPSQEVKEVYMGNVIQAGEGQAPARQATLGAGLPVSTPCT 108
Cdd:PLN02644    2 DVCIVGVARTPIGGFLGSLSSLSATELGSIAIQAALERAGVDPALVQEVFFGNVLSANLGQAPARQAALGAGLPPSTICT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 109 TVNKVCASGMKSIMMAAQSLMCGSQDVMVAGGMESMSNVPYTM--TRGTTPYGGVKLEDLIVKDGLTDVYNKIHMGNCAE 186
Cdd:PLN02644   82 TVNKVCASGMKAVMLAAQSIQLGINDVVVAGGMESMSNAPKYLpeARKGSRLGHDTVVDGMLKDGLWDVYNDFGMGVCAE 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 187 NTAKKFSISREDQDTYAIKSYTKSKEGWESGIFAKEIVPVTISQ-KGKPDTEVKEDEEYKRVDFSKVPKLKTVFQKENGT 265
Cdd:PLN02644  162 LCADQYSISREEQDAYAIQSYERAIAAQEAGAFAWEIVPVEVPGgRGRPSVIVDKDEGLGKFDPAKLRKLRPSFKEDGGS 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 266 VTAANASTLNDGAAALVLMTSEAAKRLNVKPLARIVGFADAAVDPIDFPIAPAHAVPKILAQTGLKKEDIKMWEINEAFS 345
Cdd:PLN02644  242 VTAGNASSISDGAAALVLVSGEKALELGLQVIAKIRGYADAAQAPELFTTAPALAIPKALKHAGLEASQVDYYEINEAFS 321
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1841866749 346 VVVLANIKMLDIDPQKVNIHGGAVSLGHPIGMSGARIVVHMTHALKQ--GEHGLAGICNGGGGASAILIQKL 415
Cdd:PLN02644  322 VVALANQKLLGLDPEKVNVHGGAVSLGHPIGCSGARILVTLLGVLRSknGKYGVAGICNGGGGASAIVVELM 393
PaaJ COG0183
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ...
28-415 0e+00

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


Pssm-ID: 439953 [Multi-domain]  Cd Length: 391  Bit Score: 538.50  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749  28 NEVVIVSAVRTPIGSFQSSLFSLPATNLGSIAIKGAIEKAGIPSQEVKEVYMGNVIQAGEGQAPARQATLGAGLPVSTPC 107
Cdd:COG0183     2 REVVIVDAVRTPFGRFGGALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQAGQGQNPARQAALLAGLPESVPA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 108 TTVNKVCASGMKSIMMAAQSLMCGSQDVMVAGGMESMSNVPYTMTRGTTPYGG-VKLEDLIVKDGLTDVYNKIHMGNCAE 186
Cdd:COG0183    82 VTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMLLPKARWGYRMnAKLVDPMINPGLTDPYTGLSMGETAE 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 187 NTAKKFSISREDQDTYAIKSYTKSKEGWESGIFAKEIVPVTISQKgKPDTEVKEDEEYKR-VDFSKVPKLKTVFqKENGT 265
Cdd:COG0183   162 NVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVEVPDR-KGEVVVDRDEGPRPdTTLEKLAKLKPAF-KKDGT 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 266 VTAANASTLNDGAAALVLMTSEAAKRLNVKPLARIVGFADAAVDPIDFPIAPAHAVPKILAQTGLKKEDIKMWEINEAFS 345
Cdd:COG0183   240 VTAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIGPVPATRKALARAGLTLDDIDLIEINEAFA 319
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1841866749 346 VVVLANIKMLDIDPQKVNIHGGAVSLGHPIGMSGARIVVHMTHALKQ--GEHGLAGICNGGGGASAILIQKL 415
Cdd:COG0183   320 AQVLAVLRELGLDPDKVNVNGGAIALGHPLGASGARILVTLLHELERrgGRYGLATMCIGGGQGIALIIERV 391
AcCoA-C-Actrans TIGR01930
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ...
32-413 5.87e-167

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: 473.25  E-value: 5.87e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749  32 IVSAVRTPIGSFQSSLFSLPATNLGSIAIKGAIEKAGIPSQEVKEVYMGNVIQAGEGQAPARQATLGAGLPVSTPCTTVN 111
Cdd:TIGR01930   1 IVAAARTPIGKFGGSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLQAGEQQNIARQAALLAGLPESVPAYTVN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 112 KVCASGMKSIMMAAQSLMCGSQDVMVAGGMESMSNVPYTMTRGTTP---YGGVKLEDLIVKDgLTDVYNKIHMGNCAENT 188
Cdd:TIGR01930  81 RQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGVPRSLRWgvkPGNAELEDARLKD-LTDANTGLPMGVTAENL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 189 AKKFSISREDQDTYAIKSYTKSKEGWESGIFAKEIVPVTISQKGKPDTEVKEDEEYKRVDFSKVPKLKTVFqKENGTVTA 268
Cdd:TIGR01930 160 AKKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVTVKGRKGPVTVSSDEGIRPNTTLEKLAKLKPAF-DPDGTVTA 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 269 ANASTLNDGAAALVLMTSEAAKRLNVKPLARIVGFADAAVDPIDFPIAPAHAVPKILAQTGLKKEDIKMWEINEAFSVVV 348
Cdd:TIGR01930 239 GNSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALKKAGLSISDIDLFEINEAFAAQV 318
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1841866749 349 LANIKMLDIDPQKVNIHGGAVSLGHPIGMSGARIVVHMTHALKQ--GEHGLAGICNGGGGASAILIQ 413
Cdd:TIGR01930 319 LACIKELGLDLEKVNVNGGAIALGHPLGASGARIVTTLLHELKRrgGRYGLATMCIGGGQGAAVILE 385
Thiolase_N pfam00108
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
30-287 7.84e-114

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: 333.50  E-value: 7.84e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749  30 VVIVSAVRTPIGSFQSSLFSLPATNLGSIAIKGAIEKAGIPSQEVKEVYMGNVIQAGEGQAPARQATLGAGLPVSTPCTT 109
Cdd:pfam00108   1 VVIVSAARTPFGSFGGSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQAGEGQNPARQAALKAGIPDSAPAVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 110 VNKVCASGMKSIMMAAQSLMCGSQDVMVAGGMESMSNVPYTMT---RGTTPYGGVKLEDLIVKDGLTDVYNKIHMGNCAE 186
Cdd:pfam00108  81 INKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALPtdaRSGLKHGDEKKHDLLIPDGLTDAFNGYHMGLTAE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 187 NTAKKFSISREDQDTYAIKSYTKSKEGWESGIFAKEIVPVTISQKGKPDTEVKEDEEYKRVDFSKVPKLKTVFQKEnGTV 266
Cdd:pfam00108 161 NVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDEIVPVTVKGRKGKPTVDKDEGIRPPTTAEPLAKLKPAFDKE-GTV 239
                         250       260
                  ....*....|....*....|.
gi 1841866749 267 TAANASTLNDGAAALVLMTSE 287
Cdd:pfam00108 240 TAGNASPINDGAAAVLLMSES 260
 
Name Accession Description Interval E-value
thiolase cd00751
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ...
31-414 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: 558.25  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749  31 VIVSAVRTPIGSFQSSLFSLPATNLGSIAIKGAIEKAGIPSQEVKEVYMGNVIQAGEGQAPARQATLGAGLPVSTPCTTV 110
Cdd:cd00751     1 VIVSAVRTPIGRFGGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGEGQNPARQAALLAGLPESVPATTV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 111 NKVCASGMKSIMMAAQSLMCGSQDVMVAGGMESMSNVPYTMTRGTTPY-GGVKLEDLIVKDGLTDVYNKIHMGNCAENTA 189
Cdd:cd00751    81 NRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGrLGLNTLDGMLDDGLTDPFTGLSMGITAENVA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 190 KKFSISREDQDTYAIKSYTKSKEGWESGIFAKEIVPVTISQKGKPDTeVKEDEEYKR-VDFSKVPKLKTVFqKENGTVTA 268
Cdd:cd00751   161 EKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEVPGRKGPVV-VDRDEGPRPdTTLEKLAKLKPAF-KKDGTVTA 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 269 ANASTLNDGAAALVLMTSEAAKRLNVKPLARIVGFADAAVDPIDFPIAPAHAVPKILAQTGLKKEDIKMWEINEAFSVVV 348
Cdd:cd00751   239 GNASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDIDLIEINEAFAAQA 318
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1841866749 349 LANIKMLDIDPQKVNIHGGAVSLGHPIGMSGARIVVHMTHALKQ--GEHGLAGICNGGGGASAILIQK 414
Cdd:cd00751   319 LACLKELGLDPEKVNVNGGAIALGHPLGASGARIVVTLLHELKRrgGRYGLATMCIGGGQGAAMVIER 386
PLN02644 PLN02644
acetyl-CoA C-acetyltransferase
29-415 0e+00

acetyl-CoA C-acetyltransferase


Pssm-ID: 215347 [Multi-domain]  Cd Length: 394  Bit Score: 552.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749  29 EVVIVSAVRTPIGSFQSSLFSLPATNLGSIAIKGAIEKAGIPSQEVKEVYMGNVIQAGEGQAPARQATLGAGLPVSTPCT 108
Cdd:PLN02644    2 DVCIVGVARTPIGGFLGSLSSLSATELGSIAIQAALERAGVDPALVQEVFFGNVLSANLGQAPARQAALGAGLPPSTICT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 109 TVNKVCASGMKSIMMAAQSLMCGSQDVMVAGGMESMSNVPYTM--TRGTTPYGGVKLEDLIVKDGLTDVYNKIHMGNCAE 186
Cdd:PLN02644   82 TVNKVCASGMKAVMLAAQSIQLGINDVVVAGGMESMSNAPKYLpeARKGSRLGHDTVVDGMLKDGLWDVYNDFGMGVCAE 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 187 NTAKKFSISREDQDTYAIKSYTKSKEGWESGIFAKEIVPVTISQ-KGKPDTEVKEDEEYKRVDFSKVPKLKTVFQKENGT 265
Cdd:PLN02644  162 LCADQYSISREEQDAYAIQSYERAIAAQEAGAFAWEIVPVEVPGgRGRPSVIVDKDEGLGKFDPAKLRKLRPSFKEDGGS 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 266 VTAANASTLNDGAAALVLMTSEAAKRLNVKPLARIVGFADAAVDPIDFPIAPAHAVPKILAQTGLKKEDIKMWEINEAFS 345
Cdd:PLN02644  242 VTAGNASSISDGAAALVLVSGEKALELGLQVIAKIRGYADAAQAPELFTTAPALAIPKALKHAGLEASQVDYYEINEAFS 321
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1841866749 346 VVVLANIKMLDIDPQKVNIHGGAVSLGHPIGMSGARIVVHMTHALKQ--GEHGLAGICNGGGGASAILIQKL 415
Cdd:PLN02644  322 VVALANQKLLGLDPEKVNVHGGAVSLGHPIGCSGARILVTLLGVLRSknGKYGVAGICNGGGGASAIVVELM 393
PaaJ COG0183
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ...
28-415 0e+00

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


Pssm-ID: 439953 [Multi-domain]  Cd Length: 391  Bit Score: 538.50  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749  28 NEVVIVSAVRTPIGSFQSSLFSLPATNLGSIAIKGAIEKAGIPSQEVKEVYMGNVIQAGEGQAPARQATLGAGLPVSTPC 107
Cdd:COG0183     2 REVVIVDAVRTPFGRFGGALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQAGQGQNPARQAALLAGLPESVPA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 108 TTVNKVCASGMKSIMMAAQSLMCGSQDVMVAGGMESMSNVPYTMTRGTTPYGG-VKLEDLIVKDGLTDVYNKIHMGNCAE 186
Cdd:COG0183    82 VTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMLLPKARWGYRMnAKLVDPMINPGLTDPYTGLSMGETAE 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 187 NTAKKFSISREDQDTYAIKSYTKSKEGWESGIFAKEIVPVTISQKgKPDTEVKEDEEYKR-VDFSKVPKLKTVFqKENGT 265
Cdd:COG0183   162 NVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVEVPDR-KGEVVVDRDEGPRPdTTLEKLAKLKPAF-KKDGT 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 266 VTAANASTLNDGAAALVLMTSEAAKRLNVKPLARIVGFADAAVDPIDFPIAPAHAVPKILAQTGLKKEDIKMWEINEAFS 345
Cdd:COG0183   240 VTAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIGPVPATRKALARAGLTLDDIDLIEINEAFA 319
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1841866749 346 VVVLANIKMLDIDPQKVNIHGGAVSLGHPIGMSGARIVVHMTHALKQ--GEHGLAGICNGGGGASAILIQKL 415
Cdd:COG0183   320 AQVLAVLRELGLDPDKVNVNGGAIALGHPLGASGARILVTLLHELERrgGRYGLATMCIGGGQGIALIIERV 391
PRK05790 PRK05790
putative acyltransferase; Provisional
28-412 2.90e-171

putative acyltransferase; Provisional


Pssm-ID: 180261 [Multi-domain]  Cd Length: 393  Bit Score: 484.66  E-value: 2.90e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749  28 NEVVIVSAVRTPIGSFQSSLFSLPATNLGSIAIKGAIEKAGIPSQEVKEVYMGNVIQAGEGQAPARQATLGAGLPVSTPC 107
Cdd:PRK05790    2 KDVVIVSAARTPIGKFGGALKDVSAVELGAIVIKAALERAGVPPEQVDEVIMGQVLQAGAGQNPARQAALKAGLPVEVPA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 108 TTVNKVCASGMKSIMMAAQSLMCGSQDVMVAGGMESMSNVPYTMT--RGTTPYGGVKLEDLIVKDGLTDVYNKIHMGNCA 185
Cdd:PRK05790   82 LTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQESMSQAPHVLPgsRWGQKMGDVELVDTMIHDGLTDAFNGYHMGITA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 186 ENTAKKFSISREDQDTYAIKSYTKSKEGWESGIFAKEIVPVTISQKGKPDTEVKEDeEYKRVDFS--KVPKLKTVFqKEN 263
Cdd:PRK05790  162 ENLAEQYGITREEQDEFALASQQKAEAAIKAGRFKDEIVPVTIKQRKGDPVVVDTD-EHPRPDTTaeSLAKLRPAF-DKD 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 264 GTVTAANASTLNDGAAALVLMTSEAAKRLNVKPLARIVGFADAAVDPIDFPIAPAHAVPKILAQTGLKKEDIKMWEINEA 343
Cdd:PRK05790  240 GTVTAGNASGINDGAAAVVVMSEAKAKELGLTPLARIVSYAVAGVDPAIMGIGPVPAIRKALEKAGWSLADLDLIEINEA 319
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1841866749 344 FSVVVLANIKMLDIDPQKVNIHGGAVSLGHPIGMSGARIVVHMTHALK--QGEHGLAGICNGGGGASAILI 412
Cdd:PRK05790  320 FAAQALAVEKELGLDPEKVNVNGGAIALGHPIGASGARILVTLLHEMKrrGAKKGLATLCIGGGQGVALIV 390
AcCoA-C-Actrans TIGR01930
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ...
32-413 5.87e-167

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: 473.25  E-value: 5.87e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749  32 IVSAVRTPIGSFQSSLFSLPATNLGSIAIKGAIEKAGIPSQEVKEVYMGNVIQAGEGQAPARQATLGAGLPVSTPCTTVN 111
Cdd:TIGR01930   1 IVAAARTPIGKFGGSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLQAGEQQNIARQAALLAGLPESVPAYTVN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 112 KVCASGMKSIMMAAQSLMCGSQDVMVAGGMESMSNVPYTMTRGTTP---YGGVKLEDLIVKDgLTDVYNKIHMGNCAENT 188
Cdd:TIGR01930  81 RQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGVPRSLRWgvkPGNAELEDARLKD-LTDANTGLPMGVTAENL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 189 AKKFSISREDQDTYAIKSYTKSKEGWESGIFAKEIVPVTISQKGKPDTEVKEDEEYKRVDFSKVPKLKTVFqKENGTVTA 268
Cdd:TIGR01930 160 AKKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVTVKGRKGPVTVSSDEGIRPNTTLEKLAKLKPAF-DPDGTVTA 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 269 ANASTLNDGAAALVLMTSEAAKRLNVKPLARIVGFADAAVDPIDFPIAPAHAVPKILAQTGLKKEDIKMWEINEAFSVVV 348
Cdd:TIGR01930 239 GNSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALKKAGLSISDIDLFEINEAFAAQV 318
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1841866749 349 LANIKMLDIDPQKVNIHGGAVSLGHPIGMSGARIVVHMTHALKQ--GEHGLAGICNGGGGASAILIQ 413
Cdd:TIGR01930 319 LACIKELGLDLEKVNVNGGAIALGHPLGASGARIVTTLLHELKRrgGRYGLATMCIGGGQGAAVILE 385
PRK08235 PRK08235
acetyl-CoA C-acetyltransferase;
29-413 4.10e-154

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181311 [Multi-domain]  Cd Length: 393  Bit Score: 441.07  E-value: 4.10e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749  29 EVVIVSAVRTPIGSFQSSLFSLPATNLGSIAIKGAIEKAGIPSQEVKEVYMGNVIQAGEGQAPARQATLGAGLPVSTPCT 108
Cdd:PRK08235    3 KTVIVSAARTPFGKFGGSLKDVKATELGGIAIKEALERANVSAEDVEEVIMGTVLQGGQGQIPSRQAARAAGIPWEVQTE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 109 TVNKVCASGMKSIMMAAQSLMCGSQDVMVAGGMESMSNVPYTMTRGTTPY--GGVKLEDLIVKDGLTDVYNKIHMGNCAE 186
Cdd:PRK08235   83 TVNKVCASGLRAVTLADQIIRAGDASVIVAGGMESMSNAPYILPGARWGYrmGDNEVIDLMVADGLTCAFSGVHMGVYGG 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 187 NTAKKFSISREDQDTYAIKSYTKSKEGWESGIFAKEIVPVTISQKgKPDTEVKEDEEYKRVDFS--KVPKLKTVFQKEnG 264
Cdd:PRK08235  163 EVAKELGISREAQDEWAYRSHQRAVSAHEEGRFEEEIVPVTIPQR-KGDPIVVAKDEAPRKDTTieKLAKLKPVFDKT-G 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 265 TVTAANASTLNDGAAALVLMTSEAAKRLNVKPLARIVGFADAAVDPIDFPIAPAHAVPKILAQTGLKKEDIKMWEINEAF 344
Cdd:PRK08235  241 TITAGNAPGVNDGAAALVLMSEDRAKQEGRKPLATILAHTAIAVEAKDFPRTPGYAINALLEKTGKTVEDIDLFEINEAF 320
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1841866749 345 SVVVLANIKMLDIDPQKVNIHGGAVSLGHPIGMSGARIVVHMTHALKQ--GEHGLAGICNGGGGASAILIQ 413
Cdd:PRK08235  321 AAVALASTEIAGIDPEKVNVNGGAVALGHPIGASGARIIVTLIHELKRrgGGIGIAAICSGGGQGDAVLIE 391
PRK06954 PRK06954
acetyl-CoA C-acetyltransferase;
28-413 8.30e-131

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180775 [Multi-domain]  Cd Length: 397  Bit Score: 381.93  E-value: 8.30e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749  28 NEVVIVSAVRTPIGSFQSSLFSLPATNLGSIAIKGAIEKAGIPSQEVKEVYMGNVIQAGEGQAPARQATLGAGLPVSTPC 107
Cdd:PRK06954    7 DPIVIASAARTPMAAFQGEFASLTAPQLGAAAIAAAVERAGLKPEQIDEVVMGCVLPAGQGQAPARQAALGAGLPLSVGC 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 108 TTVNKVCASGMKSIMMAAQSLMCGSQDVMVAGGMESMSNVPYTM--TRGTTPYGGVKLEDLIVKDGLTDVYNKIH-MGNC 184
Cdd:PRK06954   87 TTVNKMCGSGMRAAMFAHDMLVAGSVDVIVAGGMESMTNAPYLLpkARGGMRMGHGQVLDHMFLDGLEDAYDKGRlMGTF 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 185 AENTAKKFSISREDQDTYAIKSYTKSKEGWESGIFAKEIVPVTISQKgKPDTEVKEDEEYKRVDFSKVPKLKTVFQKeNG 264
Cdd:PRK06954  167 AEECAGEYGFTREAQDAFAIESLARAKRANEDGSFAWEIAPVTVAGK-KGDTVIDRDEQPFKANPEKIPTLKPAFSK-TG 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 265 TVTAANASTLNDGAAALVLMTSEAAKRLNVKPLARIVGFADAAVDPIDFPIAPAHAVPKILAQTGLKKEDIKMWEINEAF 344
Cdd:PRK06954  245 TVTAANSSSISDGAAALVMMRASTAKRLGLAPLARVVGHSTFAQAPSKFTTAPVGAIRKLFEKNGWRAAEVDLFEINEAF 324
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1841866749 345 SVVVLANIKMLDIDPQKVNIHGGAVSLGHPIGMSGARIVVHMTHALKQ--GEHGLAGICNGGGGASAILIQ 413
Cdd:PRK06954  325 AVVTMAAMKEHGLPHEKVNVNGGACALGHPIGASGARILVTLIGALRArgGKRGVASLCIGGGEATAMGIE 395
PRK09051 PRK09051
beta-ketothiolase BktB;
28-415 6.92e-122

beta-ketothiolase BktB;


Pssm-ID: 181625 [Multi-domain]  Cd Length: 394  Bit Score: 358.89  E-value: 6.92e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749  28 NEVVIVSAVRTPIGSFQSSLFSLPATNLGSIAIKGAIEKAGIPSQEVKEVYMGNVIQAGEGQA-PARQATLGAGLPVSTP 106
Cdd:PRK09051    3 REVVVVSGVRTAIGTFGGSLKDVAPTDLGATVVREALARAGVDPDQVGHVVFGHVIPTEPRDMyLSRVAAINAGVPQETP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 107 CTTVNKVCASGMKSIMMAAQSLMCGSQDVMVAGGMESMSNVPYTMT--RGTTPYGGVKLEDLIVKdGLTDVYNKIHMGNC 184
Cdd:PRK09051   83 AFNVNRLCGSGLQAIVSAAQAILLGDADVAIGGGAESMSRAPYLLPaaRWGARMGDAKLVDMMVG-ALHDPFGTIHMGVT 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 185 AENTAKKFSISREDQDTYAIKSYTKSKEGWESGIFAKEIVPVTISQKgKPDTEVKEDEEYKR-VDFSKVPKLKTVFQKEN 263
Cdd:PRK09051  162 AENVAAKYGISREAQDALALESHRRAAAAIAAGYFKDQIVPVEIKTR-KGEVVFDTDEHVRAdTTLEDLAKLKPVFKKEN 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 264 GTVTAANASTLNDGAAALVLMTSEAAKRLNVKPLARIVGFADAAVDPIDFPIAPAHAVPKILAQTGLKKEDIKMWEINEA 343
Cdd:PRK09051  241 GTVTAGNASGINDGAAAVVLAEADAAEARGLKPLARLVGYAHAGVDPEYMGIGPVPATQKALERAGLTVADLDVIEANEA 320
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1841866749 344 FSVVVLANIKMLDIDPQKVNIHGGAVSLGHPIGMSGARIVVHMTHALK--QGEHGLAGICNGGGGASAILIQKL 415
Cdd:PRK09051  321 FAAQACAVTRELGLDPAKVNPNGSGISLGHPVGATGAIITVKALYELQriGGRYALVTMCIGGGQGIAAIFERL 394
PRK05656 PRK05656
acetyl-CoA C-acetyltransferase;
27-414 6.33e-115

acetyl-CoA C-acetyltransferase;


Pssm-ID: 168156  Cd Length: 393  Bit Score: 341.48  E-value: 6.33e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749  27 LNEVVIVSAVRTPIGSFQSSLFSLPATNLGSIAIKGAIEKAGIPSQEVKEVYMGNVIQAGEGQAPARQATLGAGLPVSTP 106
Cdd:PRK05656    1 MQDVVIVAATRTAIGSFQGSLANIPAVELGAAVIRRLLEQTGLDPAQVDEVILGQVLTAGAGQNPARQAAIKAGLPHSVP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 107 CTTVNKVCASGMKSIMMAAQSLMCGSQDVMVAGGMESMSNVPYTMTRGTT--PYGGVKLEDLIVKDGLTDVYNKIHMGNC 184
Cdd:PRK05656   81 AMTLNKVCGSGLKALHLAAQAIRCGDAEVIIAGGQENMSLAPYVLPGARTglRMGHAQLVDSMITDGLWDAFNDYHMGIT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 185 AENTAKKFSISREDQDTYAIKSYTKSKEGWESGIFAKEIVPVTISQ-KGKPDTEVKEDEEYKRVDFSKVPKLKTVFQKEn 263
Cdd:PRK05656  161 AENLVEKYGISREAQDAFAAASQQKAVAAIEAGRFDDEITPILIPQrKGEPLAFATDEQPRAGTTAESLAKLKPAFKKD- 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 264 GTVTAANASTLNDGAAALVLMTSEAAKRLNVKPLARIVGFADAAVDPIDFPIAPAHAVPKILAQTGLKKEDIKMWEINEA 343
Cdd:PRK05656  240 GSVTAGNASSLNDGAAAVLLMSAAKAKALGLPVLAKIAAYANAGVDPAIMGIGPVSATRRCLDKAGWSLAELDLIEANEA 319
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1841866749 344 FSVVVLANIKMLDIDPQKVNIHGGAVSLGHPIGMSGARIVVHMTHAL--KQGEHGLAGICNGGGGASAILIQK 414
Cdd:PRK05656  320 FAAQSLAVGKELGWDAAKVNVNGGAIALGHPIGASGCRVLVTLLHEMirRDAKKGLATLCIGGGQGVALAIER 392
Thiolase_N pfam00108
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
30-287 7.84e-114

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: 333.50  E-value: 7.84e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749  30 VVIVSAVRTPIGSFQSSLFSLPATNLGSIAIKGAIEKAGIPSQEVKEVYMGNVIQAGEGQAPARQATLGAGLPVSTPCTT 109
Cdd:pfam00108   1 VVIVSAARTPFGSFGGSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQAGEGQNPARQAALKAGIPDSAPAVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 110 VNKVCASGMKSIMMAAQSLMCGSQDVMVAGGMESMSNVPYTMT---RGTTPYGGVKLEDLIVKDGLTDVYNKIHMGNCAE 186
Cdd:pfam00108  81 INKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALPtdaRSGLKHGDEKKHDLLIPDGLTDAFNGYHMGLTAE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 187 NTAKKFSISREDQDTYAIKSYTKSKEGWESGIFAKEIVPVTISQKGKPDTEVKEDEEYKRVDFSKVPKLKTVFQKEnGTV 266
Cdd:pfam00108 161 NVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDEIVPVTVKGRKGKPTVDKDEGIRPPTTAEPLAKLKPAFDKE-GTV 239
                         250       260
                  ....*....|....*....|.
gi 1841866749 267 TAANASTLNDGAAALVLMTSE 287
Cdd:pfam00108 240 TAGNASPINDGAAAVLLMSES 260
PRK09050 PRK09050
beta-ketoadipyl CoA thiolase; Validated
27-415 1.89e-110

beta-ketoadipyl CoA thiolase; Validated


Pssm-ID: 181624 [Multi-domain]  Cd Length: 401  Bit Score: 329.99  E-value: 1.89e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749  27 LNEVVIVSAVRTPIGSFQSSLFSLPATNLGSIAIKGAIEK-AGIPSQEVKEVYMGNVIQAGE-GQAPARQATLGAGLPVS 104
Cdd:PRK09050    1 MTEAFICDAIRTPIGRYGGALSSVRADDLGAVPLKALMARnPGVDWEAVDDVIYGCANQAGEdNRNVARMSALLAGLPVS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 105 TPCTTVNKVCASGMKSIMMAAQSLMCGSQDVMVAGGMESMSNVPYTMTRGTTPYG-GVKLEDL-----IVKDGLTDVYNK 178
Cdd:PRK09050   81 VPGTTINRLCGSGMDAVGTAARAIKAGEAELMIAGGVESMSRAPFVMGKADSAFSrQAEIFDTtigwrFVNPLMKAQYGV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 179 IHMGNCAENTAKKFSISREDQDTYAIKSYTKSKEGWESGIFAKEIVPVTISQKGKPDTEVKEDEeYKRVDFS--KVPKLK 256
Cdd:PRK09050  161 DSMPETAENVAEDYNISRADQDAFALRSQQRAAAAQAAGFLAEEIVPVTIPQKKGDPVVVDRDE-HPRPETTleALAKLK 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 257 TVFqKENGTVTAANASTLNDGAAALVLMTSEAAKRLNVKPLARIVGFADAAVDPIDFPIAPAHAVPKILAQTGLKKEDIK 336
Cdd:PRK09050  240 PVF-RPDGTVTAGNASGVNDGAAALLLASEAAAKKHGLTPRARILGMATAGVEPRIMGIGPAPATRKLLARLGLTIDQFD 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 337 MWEINEAFSVVVLANIKMLDI--DPQKVNIHGGAVSLGHPIGMSGARIVVHMTHALKQ--GEHGLAGICNGGGGASAILI 412
Cdd:PRK09050  319 VIELNEAFAAQGLAVLRQLGLadDDARVNPNGGAIALGHPLGMSGARLVLTALHQLERtgGRYALCTMCIGVGQGIALAI 398

                  ...
gi 1841866749 413 QKL 415
Cdd:PRK09050  399 ERV 401
PRK06366 PRK06366
acetyl-CoA C-acetyltransferase;
27-413 2.32e-109

acetyl-CoA C-acetyltransferase;


Pssm-ID: 102340 [Multi-domain]  Cd Length: 388  Bit Score: 326.97  E-value: 2.32e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749  27 LNEVVIVSAVRTPIGSFQSSLFSLPATNLGSIAIKGAIEKAGIPSQEVKEVYMGNVIQAGEGQAPARQATLGAGLPVSTP 106
Cdd:PRK06366    1 MKDVYIVSAKRTAIGKFGRSFSKIKAPQLGGAAIKAVIDDAKLDPALVQEVIMGNVIQAGVGQNPAGQAAYHAGLPFGVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 107 CTTVNKVCASGMKSIMMAAQSLMCGSQDVMVAGGMESMSNVPYTMTRGTT--P----YGGVKLEDLIVKDGLTDVYNKIH 180
Cdd:PRK06366   81 KYTVNVVCASGMLAVESAAREIMLGERDLVIAGGMENMSNAPFLLPSDLRwgPkhllHKNYKIDDAMLVDGLIDAFYFEH 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 181 MGNCAENTAKKFSISREDQDTYAIKSYTKSKEGWESGIFAKEIVPVtisqkgkpdTEVKEDEEYKRVDFSKVPKLKTVFQ 260
Cdd:PRK06366  161 MGVSAERTARKYGITREMADEYSVQSYERAIRATESGEFRNEIVPF---------NDLDRDEGIRKTTMEDLAKLPPAFD 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 261 KeNGTVTAANASTLNDGAAALVLMTSEAAKRLNVKPLARIVGFADAAVDPIDFPIAPAHAVPKILAQTGLKKEDIKMWEI 340
Cdd:PRK06366  232 K-NGILTAGNSAQLSDGGSALVMASEKAINEYGLKPIARITGYESASLDPLDFVEAPIPATRKLLEKQNKSIDYYDLVEH 310
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1841866749 341 NEAFSVVVLANIKMLDIDPQKVNIHGGAVSLGHPIGMSGARIVVHMTHALKQG--EHGLAGICNGGGGASAILIQ 413
Cdd:PRK06366  311 NEAFSIASIIVRDQLKIDNERFNVNGGAVAIGHPIGNSGSRIIVTLINALKTRhmKTGLATLCHGGGGAHTLTLE 385
PRK06205 PRK06205
acetyl-CoA C-acetyltransferase;
29-410 4.47e-103

acetyl-CoA C-acetyltransferase;


Pssm-ID: 235741 [Multi-domain]  Cd Length: 404  Bit Score: 311.54  E-value: 4.47e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749  29 EVVIVSAVRTPIGSFQSSLFSLPATNLGSIAIKGAIEKAGIPSQEVKEVYMGNVIQAGEGQAPARQATLGAGLPVSTPCT 108
Cdd:PRK06205    3 DAVICEPVRTPVGRFGGAFKDVPAEELAATVIRALVERTGIDPARIDDVIFGQGYPNGEAPAIGRVAALDAGLPVTVPGM 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 109 TVNKVCASGMKSIMMAAQSLMCGSQDVMVAGGMESMSNVPYTMT--RGTTPYGGVKLEDLIVKDGLT---DVYNKIH-MG 182
Cdd:PRK06205   83 QLDRRCGSGLQAVITAAMQVQTGAADVVIAGGAESMSNVEFYTTdmRWGVRGGGVQLHDRLARGRETaggRRFPVPGgMI 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 183 NCAENTAKKFSISREDQDTYAIKSYTKSKEGWESGIFAKEIVPVTISQKGKPDTEVKEDEEYkRVDFS--KVPKLKTVFQ 260
Cdd:PRK06205  163 ETAENLRREYGISREEQDALAVRSHQRAVAAQEAGRFDDEIVPVTVPQRKGDPTVVDRDEHP-RADTTleSLAKLRPIMG 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 261 K--ENGTVTAANASTLNDGAAALVLMTSEAAKRLNVKPLARIVGFADAAVDPIDFPIAPAHAVPKILAQTGLKKEDIKMW 338
Cdd:PRK06205  242 KqdPEATVTAGNASGQNDAAAACLVTTEDKAEELGLRPLARLVSWAVAGVEPSRMGIGPVPATEKALARAGLTLDDIDLI 321
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1841866749 339 EINEAFSVVVLANIKMLDIDPQ---KVNIHGGAVSLGHPIGMSGARIVVHMTHALK--QGEHGLAGICNGGG-GASAI 410
Cdd:PRK06205  322 ELNEAFAAQVLAVLKEWGFGADdeeRLNVNGSGISLGHPVGATGGRILATLLRELQrrQARYGLETMCIGGGqGLAAV 399
PRK06633 PRK06633
acetyl-CoA C-acetyltransferase;
27-413 1.38e-101

acetyl-CoA C-acetyltransferase;


Pssm-ID: 168632 [Multi-domain]  Cd Length: 392  Bit Score: 307.34  E-value: 1.38e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749  27 LNEVVIVSAVRTPIGSFQSSLFSLPATNLGSIAIKGAIEKAGIPSQEVKEVYMGNVIQAGEGQAPARQATLGAGLPVSTP 106
Cdd:PRK06633    2 TKPVYITHAKRTAFGSFMGSLSTTPAPMLAAHLIKDILQNSKIDPALVNEVILGQVITGGSGQNPARQTLIHAGIPKEVP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 107 CTTVNKVCASGMKSIMMAAQSLMCGSQDVMVAGGMESMS-NVPYTMTRGTTPYGGVKLEDLIVKDGLTDVYNKIHMGNCA 185
Cdd:PRK06633   82 GYTINKVCGSGLKSVALAANSIMTGDNEIVIAGGQENMSlGMHGSYIRAGAKFGDIKMVDLMQYDGLTDVFSGVFMGITA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 186 ENTAKKFSISREDQDTYAIKSYTKSKEGWESGIFAKEIVPVTISQKgkPDTEVKEDEEYKRVDFSK--VPKLKTVFQKeN 263
Cdd:PRK06633  162 ENISKQFNISRQEQDEFALSSHKKAAKAQLAGIFKDEILPIEVTIK--KTTSLFDHDETVRPDTSLeiLSKLRPAFDK-N 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 264 GTVTAANASTLNDGAAALVLMTSEAAKRLNVKPLARIVGFADAAVDPIDFPIAPAHAVPKILAQTGLKKEDIKMWEINEA 343
Cdd:PRK06633  239 GVVTAGNASSINDGAACLMVVSEEALKKHNLTPLARIVSYASAGVDPSIMGTAPVPASQKALSKAGWSVNDLEVIEVNEA 318
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1841866749 344 FSVVVLANIKMLDIDPQKVNIHGGAVSLGHPIGMSGARIVVHMTHALK--QGEHGLAGICNGGGGASAILIQ 413
Cdd:PRK06633  319 FAAQSIYVNREMKWDMEKVNINGGAIAIGHPIGASGGRVLITLIHGLRraKAKKGLVTLCIGGGMGMAMCVE 390
PRK06445 PRK06445
acetyl-CoA C-acetyltransferase;
27-414 5.86e-90

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180563 [Multi-domain]  Cd Length: 394  Bit Score: 277.37  E-value: 5.86e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749  27 LNEVVIVSAVRTPIGSF-----QSSLF-SLPATNLGSIAIKGAIEKAGIPSQEVKEVYMGNVIQAGEGQA-PARQATLGA 99
Cdd:PRK06445    1 LEDVYLVDFARTAFSRFrpkdpQKDVFnNIRPEELAAMLINRLIEKTGIKPEEIDDIITGCALQVGENWLyGGRHPIFLA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 100 GLPVSTPCTTVNKVCASGMKSIMMAAQSLMCGSQDVMVAGGMESMSNVPYTMTRGTTPYGGVKLEDLIVKDGLTDVYNki 179
Cdd:PRK06445   81 RLPYNIPAMAVDRQCASSLTTVSIGAMEIATGMADIVIAGGVEHMTRTPMGDNPHIEPNPKLLTDPKYIEYDLTTGYV-- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 180 hMGNCAENTAKKFSISREDQDTYAIKSYTKSKEGWESGIFAKEIVPVTISQKGKPDTeVKEDEEYkRVDFS--KVPKLKT 257
Cdd:PRK06445  159 -MGLTAEKLAEEAGIKREEMDRWSLRSHQLAAKAIQEGYFKDEILPIEVEVEGKKKV-VDVDQSV-RPDTSleKLAKLPP 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 258 VFqKENGTVTAANASTLNDGAAALVLMTSEAAKRLNVKPLARIVGFADAAVDPIDFPIAPAHAVPKILAQTGLKKEDIKM 337
Cdd:PRK06445  236 AF-KPDGVITAGNSSPLNSGASYVLLMSKKAVKKYGLKPMAKIRSFGFAGVPPAIMGKGPVPASKKALEKAGLSVKDIDL 314
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1841866749 338 WEINEAFSVVVLANIKMLDIDPQKVNIHGGAVSLGHPIGMSGARIVVHMTHAL--KQGEHGLAGICNGGGGASAILIQK 414
Cdd:PRK06445  315 WEINEAFAVVVLYAIKELGLDPETVNIKGGAIAIGHPLGATGARIVGTLARQLqiKGKDYGVATLCVGGGQGGAVVLER 393
PRK07801 PRK07801
acetyl-CoA C-acetyltransferase;
29-415 9.06e-90

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181123 [Multi-domain]  Cd Length: 382  Bit Score: 276.59  E-value: 9.06e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749  29 EVVIVSAVRTPIGSFQSSLFSLPATNLGSIAIKGAIEKAGIPSQEVKEVYMGNVIQAGeGQAP--ARQATLGAGLPVSTP 106
Cdd:PRK07801    3 EAYIVDAVRTPVGKRKGGLAGVHPADLGAHVLKGLVDRTGIDPAAVDDVIFGCVDTIG-PQAGniARTSWLAAGLPEEVP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 107 CTTVNKVCASGMKSIMMAAQSLMCGSQDVMVAGGMESMSNVP--YTMTRG-----TTPYGGVKledlivkdGLTDVYNK- 178
Cdd:PRK07801   82 GVTVDRQCGSSQQAIHFAAQAVMSGTQDLVVAGGVQNMSQIPisSAMTAGeqlgfTSPFAESK--------GWLHRYGDq 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 179 -IHMGNCAENTAKKFSISREDQDTYAIKSYTKSKEGWESGIFAKEIVPVTisqkgkpdtEVKEDEEYKRVDFSKVPKLKT 257
Cdd:PRK07801  154 eVSQFRGAELIAEKWGISREEMERFALESHRRAFAAIRAGRFDNEIVPVG---------GVTVDEGPRETSLEKMAGLKP 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 258 VFqkENGTVTAANASTLNDGAAALVLMTSEAAKRLNVKPLARIVGFADAAVDPIDFPIAPAHAVPKILAQTGLKKEDIKM 337
Cdd:PRK07801  225 LV--EGGRLTAAVASQISDGASAVLLASERAVKRHGLTPRARIHHLSVRGDDPVFMLTAPIPATRYALEKTGLSIDDIDV 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 338 WEINEAFSVVVLANIKMLDIDPQKVNIHGGAVSLGHPIGMSGARIVVHMTHALKQ--GEHGLAGICNGGGGASAILIQKL 415
Cdd:PRK07801  303 VEINEAFAPVVLAWLKETGADPAKVNPNGGAIALGHPLGATGAKLMTTLLHELERtgGRYGLQTMCEGGGTANVTIIERL 382
PRK08131 PRK08131
3-oxoadipyl-CoA thiolase;
32-414 9.57e-89

3-oxoadipyl-CoA thiolase;


Pssm-ID: 181242 [Multi-domain]  Cd Length: 401  Bit Score: 274.73  E-value: 9.57e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749  32 IVSAVRTPIGSFQSSLFSLPATNLGSIAIKGAIEKAGIPSQEVKEVYMGNVIQAGE-GQAPARQATLGAGLPVSTPCTTV 110
Cdd:PRK08131    6 IYDGLRSPFGRHAGALASVRPDDLAATVIRRLLEKSGFPGDDIEDVILGCTNQAGEdSRNVARNALLLAGLPVTVPGQTV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 111 NKVCASGMKSIMMAAQSLMCGSQDVMVAGGMESMSNVPYTMTRGTTPYGgvklEDLIVKDG----------LTDVYNKIH 180
Cdd:PRK08131   86 NRLCASGLAAVIDAARAITCGEGDLYLAGGVESMSRAPFVMGKAESAFS----RDAKVFDTtigarfpnpkIVAQYGNDS 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 181 MGNCAENTAKKFSISREDQDTYAIKSYTKSKEGWESGIFAKEIVPVTISQKGK-PDTEVKEDEEYK-RVDFSKVPKLKTV 258
Cdd:PRK08131  162 MPETGDNVAAEFGISREDADRFAAQSQAKYQAAKEEGFFADEITPIEVPQGRKlPPKLVAEDEHPRpSSTVEALTKLKPL 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 259 FqkENGTVTAANASTLNDGAAALVLMTSEAAKRLNVKPLARIVGFADAAVDPIDFPIAPAHAVPKILAQTGLKKEDIKMW 338
Cdd:PRK08131  242 F--EGGVVTAGNASGINDGAAALLIGSRAAGEKYGLKPMARILSSAAAGVEPRIMGIGPVEAIKKALARAGLTLDDMDII 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 339 EINEAFSVVVLANIKMLDI--DPQKVNIHGGAVSLGHPIGMSGARIVVHMTHALK--QGEHGLAGICNGGGGASAILIQK 414
Cdd:PRK08131  320 EINEAFASQVLGCLKGLGVdfDDPRVNPNGGAIAVGHPLGASGARLALTAARELQrrGKRYAVVSLCIGVGQGLAMVIER 399
PRK07108 PRK07108
acetyl-CoA C-acyltransferase;
27-415 2.18e-86

acetyl-CoA C-acyltransferase;


Pssm-ID: 180843 [Multi-domain]  Cd Length: 392  Bit Score: 268.18  E-value: 2.18e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749  27 LNEVVIVSAVRTPIG-SFQSSLFSLPATNLGSIAIKGAIEKAGIPSQEVKEVYMGNVIQAGE-GQAPARQATLGAGLPVS 104
Cdd:PRK07108    1 MTEAVIVSTARTPLAkSWRGAFNMTHGATLGGHVVQHAVERAKLDPAEVEDVIMGCANPEGAtGANIARQIALRAGLPVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 105 TPCTTVNKVCASGMKSIMMAAQSLMCGSQDVMVAGGMESMSNVPYTMTRGttpyggvKLEDLIVKDGLTDVYnkIHMGNC 184
Cdd:PRK07108   81 VPGMTVNRFCSSGLQTIALAAQRVIAGEGDVFVAGGVESISCVQNEMNRH-------MLREGWLVEHKPEIY--WSMLQT 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 185 AENTAKKFSISREDQDTYAIKSYTKSKEGWESGIFAKEIVPVTISQK------GKPDTE---VKEDEEYkRVDFSK--VP 253
Cdd:PRK07108  152 AENVAKRYGISKERQDEYGVQSQQRAAAAQAAGRFDDEIVPITVTAGvadkatGRLFTKevtVSADEGI-RPDTTLegVS 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 254 KLKTVFqkENGTVTAANASTLNDGAAALVLMTSEAAKRLNVKPLARIVGFADAAVDPIDFPIAPAHAVPKILAQTGLKKE 333
Cdd:PRK07108  231 KIRSAL--PGGVITAGNASQFSDGASACVVMNAKVAEREGLQPLGIFRGFAVAGCEPDEMGIGPVFAVPKLLKQAGLKVD 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 334 DIKMWEINEAFSVVVLANIKMLDIDPQKVNIHGGAVSLGHPIGMSGARIVvhmTHALKQGE-----HGLAGICNGGGGAS 408
Cdd:PRK07108  309 DIDLWELNEAFAVQVLYCRDTLGIPMDRLNVNGGAIAVGHPYGVSGARLT---GHALIEGKrrgakYVVVTMCIGGGQGA 385

                  ....*..
gi 1841866749 409 AILIQKL 415
Cdd:PRK07108  386 AGLFEVL 392
PRK07851 PRK07851
acetyl-CoA C-acetyltransferase;
29-415 7.24e-85

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181146 [Multi-domain]  Cd Length: 406  Bit Score: 264.56  E-value: 7.24e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749  29 EVVIVSAVRTPIG-SFQSSLFSLPATNLGSIAIKGAIEKA-GIPSQEVKEVYMGNVIQAGE-GQAPARQATLGAGLPvST 105
Cdd:PRK07851    3 EAVIVSTARSPIGrAFKGSLKDMRPDDLAAQMVRAALDKVpALDPTDIDDLMLGCGLPGGEqGFNMARVVAVLLGYD-FL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 106 PCTTVNKVCASGMKSIMMAAQSLMCGSQDVMVAGGMESMS--------NVPYTM----------TRGTTPYGGVKLEDLI 167
Cdd:PRK07851   82 PGTTVNRYCSSSLQTTRMAFHAIKAGEGDVFISAGVETVSrfakgnsdSLPDTKnplfaeaqarTAARAEGGAEAWHDPR 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 168 VKDGLTDVYnkIHMGNCAENTAKKFSISREDQDTYAIKSYTKSKEGWESGIFAKEIVPVTIsqkgkPDTEV--KEDEEYK 245
Cdd:PRK07851  162 EDGLLPDVY--IAMGQTAENVAQLTGISREEQDEWGVRSQNRAEEAIANGFFEREITPVTL-----PDGTVvsTDDGPRA 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 246 RVDFSKVPKLKTVFqKENGTVTAANASTLNDGAAALVLMTSEAAKRLNVKPLARIVGFADAAVDPIDFPIAPAHAVPKIL 325
Cdd:PRK07851  235 GTTYEKVSQLKPVF-RPDGTVTAGNACPLNDGAAAVVIMSDTKARELGLTPLARIVSTGVSGLSPEIMGLGPVEASKQAL 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 326 AQTGLKKEDIKMWEINEAFSVVVLANIKMLDIDPQKVNIHGGAVSLGHPIGMSGARIVVHMTHALK--QGEHGLAGICNG 403
Cdd:PRK07851  314 ARAGMSIDDIDLVEINEAFAAQVLPSARELGIDEDKLNVSGGAIALGHPFGMTGARITTTLLNNLQthDKTFGLETMCVG 393
                         410
                  ....*....|..
gi 1841866749 404 GGGASAILIQKL 415
Cdd:PRK07851  394 GGQGMAMVLERL 405
PRK09052 PRK09052
acetyl-CoA C-acyltransferase;
27-410 2.32e-84

acetyl-CoA C-acyltransferase;


Pssm-ID: 181626 [Multi-domain]  Cd Length: 399  Bit Score: 263.02  E-value: 2.32e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749  27 LNEVVIVSAVRTPIGSFQSSLF--SLPATNLGSiAIKGAIEKA-GIPSQEVKEVYMGNVIQAGE-GQAPARQATLGAGLP 102
Cdd:PRK09052    5 LQDAYIVAATRTPVGKAPRGMFknTRPDDLLAH-VLRSAVAQVpGLDPKLIEDAIVGCAMPEAEqGLNVARIGALLAGLP 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 103 VSTPCTTVNKVCASGMKSIMMAAQSLMCGSQDVMVAGGMESMSNVP-----YTMTrgttPYGGVKLEDLIVKDGltdvyn 177
Cdd:PRK09052   84 NSVGGVTVNRFCASGLQAVAMAADRIRVGEADVMIAAGVESMSMVPmmgnkPSMS----PAIFARDENVGIAYG------ 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 178 kihMGNCAENTAKKFSISREDQDTYAIKSYTKSKEGWESGIFAKEIVPVTISQKgKPD---------TEVKEDEEYKRVD 248
Cdd:PRK09052  154 ---MGLTAEKVAEQWKVSREDQDAFALESHQKAIAAQQAGEFKDEITPYEITER-FPDlatgevdvkTRTVDLDEGPRAD 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 249 FS--KVPKLKTVFQKEnGTVTAANASTLNDGAAALVLMTSEAAKRLNVKPLARIVGFADAAVDPIDFPIAPAHAVPKILA 326
Cdd:PRK09052  230 TSleGLAKLKPVFANK-GSVTAGNSSQTSDGAGAVILVSEKALKQFNLTPLARFVSFAVAGVPPEIMGIGPIEAIPAALK 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 327 QTGLKKEDIKMWEINEAFSVVVLANIKMLDIDPQKVNIHGGAVSLGHPIGMSGARIVVHMTHAL--KQGEHGLAGICNGG 404
Cdd:PRK09052  309 QAGLKQDDLDWIELNEAFAAQSLAVIRDLGLDPSKVNPLGGAIALGHPLGATGAIRTATVVHGLrrTNLKYGMVTMCVGT 388

                  ....*..
gi 1841866749 405 G-GASAI 410
Cdd:PRK09052  389 GmGAAGI 395
PRK07661 PRK07661
acetyl-CoA C-acetyltransferase;
27-410 2.80e-83

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181072 [Multi-domain]  Cd Length: 391  Bit Score: 260.07  E-value: 2.80e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749  27 LNEVVIVSAVRTPIG-SFQSSLFSLPATNLGSIAIKGAIEKAGIPSQEVKEVYMGNVI-QAGEGQAPARQATLGAGLPVS 104
Cdd:PRK07661    1 MREAVIVAGARTPVGkAKKGSLKTVRPDDLGALVVKETLKRAGNYEGPIDDLIIGCAMpEAEQGLNMARNIGALAGLPYT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 105 TPCTTVNKVCASGMKSIMMAAQSLMCGSQDVMVAGGMESMSNVPYTmtrgttpyGGVKLEDLIVKDGLTDVYnkIHMGNC 184
Cdd:PRK07661   81 VPAITINRYCSSGLQSIAYGAERIMLGHSEAVIAGGAESMSLVPMM--------GHVVRPNPRLVEAAPEYY--MGMGHT 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 185 AENTAKKFSISREDQDTYAIKSYTKSKEGWESGIFAKEIVPVTISQK-----GKPDTE--VKEDEEYKRVDFSK--VPKL 255
Cdd:PRK07661  151 AEQVAVKYGISREDQDAFAVRSHQRAAKALAEGKFADEIVPVDVTLRtvgenNKLQEEtiTFSQDEGVRADTTLeiLGKL 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 256 KTVFQKeNGTVTAANASTLNDGAAALVLMTSEAAKRLNVKPLARIVGFADAAVDPIDFPIAPAHAVPKILAQTGLKKEDI 335
Cdd:PRK07661  231 RPAFNV-KGSVTAGNSSQMSDGAAAVLLMDREKAESDGLKPLAKFRSFAVAGVPPEVMGIGPIAAIPKALKLAGLELSDI 309
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1841866749 336 KMWEINEAFSVVVLANIKMLDIDPQKVNIHGGAVSLGHPIGMSGARIVVHMTHALK-QGEH-GLAGICNGGG-GASAI 410
Cdd:PRK07661  310 GLFELNEAFASQSIQVIRELGLDEEKVNVNGGAIALGHPLGCTGAKLTLSLIHEMKrRNEQfGIVTMCIGGGmGAAGV 387
fadI PRK08963
3-ketoacyl-CoA thiolase; Reviewed
30-411 2.88e-81

3-ketoacyl-CoA thiolase; Reviewed


Pssm-ID: 181597 [Multi-domain]  Cd Length: 428  Bit Score: 256.06  E-value: 2.88e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749  30 VVIVSAVRTPIGSFQSSLFSLPATNLGSIAIKGAIEKAGIPSQEVKEVYMGNVIQAGEGQAPARQATLGAGLPVSTPCTT 109
Cdd:PRK08963    7 IAIVSGLRTPFAKQATAFHGIPAVDLGKMVVGELLARSEIDPELIEQLVFGQVVQMPEAPNIAREIVLGTGMNVHTDAYS 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 110 VNKVCASGMKSIMMAAQSLMCGSQDVMVAGGMESMSNVPY-----------------TMTRGTTPYGGVKLEDLI-VKDG 171
Cdd:PRK08963   87 VSRACATSFQAVANVAESIMAGTIDIGIAGGADSSSVLPIgvskklaralvdlnkarTLGQRLKLFSRLRLRDLLpVPPA 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 172 LTDVYNKIHMGNCAENTAKKFSISREDQDTYAIKSYTKSKEGWESGIFAKEIVPVTISQKGKP---DTEVKEDEeykrvD 248
Cdd:PRK08963  167 VAEYSTGLRMGDTAEQMAKTYGISREEQDALAHRSHQLAAQAWAEGKLDDEVMTAHVPPYKQPleeDNNIRGDS-----T 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 249 FSKVPKLKTVFQKENGTVTAANASTLNDGAAALVLMTSEAAKRLNVKPLARIVGFADAAVDPI-DFPIAPAHAVPKILAQ 327
Cdd:PRK08963  242 LEDYAKLRPAFDRKHGTVTAANSTPLTDGAAAVLLMSESRAKALGLTPLGYLRSYAFAAIDVWqDMLLGPAYATPLALER 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 328 TGLKKEDIKMWEINEAFSVVVLANIKML-----------------DIDPQKVNIHGGAVSLGHPIGMSGARIVVHMTHAL 390
Cdd:PRK08963  322 AGLTLADLTLIDMHEAFAAQTLANLQMFaserfareklgrsqaigEVDMSKFNVLGGSIAYGHPFAATGARMITQTLHEL 401
                         410       420
                  ....*....|....*....|....
gi 1841866749 391 KQ--GEHGLAGICNGGG-GASAIL 411
Cdd:PRK08963  402 RRrgGGLGLTTACAAGGlGAAMVL 425
PRK07850 PRK07850
steroid 3-ketoacyl-CoA thiolase;
29-415 3.78e-79

steroid 3-ketoacyl-CoA thiolase;


Pssm-ID: 181145 [Multi-domain]  Cd Length: 387  Bit Score: 249.25  E-value: 3.78e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749  29 EVVIVSAVRTPIGSFQSSLFSLPATNLGSIAIKGAIEKAGIPSQEVKEVYMGNVIQAGE-GQAPARQATLGAGLPVSTPC 107
Cdd:PRK07850    3 NPVIVEAVRTPIGKRNGWLSGLHAAELLGAVQRAVLDRAGIDPGDVEQVIGGCVTQAGEqSNNITRTAWLHAGLPYHVGA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 108 TTVNKVCASGMKSIMMAAQSLMCGSQDVMVAGGMESMSNVPYTMTRGTTPyGGVKLEDLivkdgltdvynKIHMGN---C 184
Cdd:PRK07850   83 TTIDCQCGSAQQANHLVAGLIAAGAIDVGIACGVEAMSRVPLGANAGPGR-GLPRPDSW-----------DIDMPNqfeA 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 185 AENTAKKFSISREDQDTYAIKSYTKSKEGWESGIFAKEIVPVT---ISQKGKPDTE---VKEDEEYKRVDFSKVPKLKTV 258
Cdd:PRK07850  151 AERIAKRRGITREDVDAFGLRSQRRAAQAWAEGRFDREISPVQapvLDEEGQPTGEtrlVTRDQGLRDTTMEGLAGLKPV 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 259 FqkENGTVTAANASTLNDGAAALVLMTSEAAKRLNVKPLARIVGFADAAVDP---IDFPIapaHAVPKILAQTGLKKEDI 335
Cdd:PRK07850  231 L--EGGIHTAGTSSQISDGAAAVLWMDEDRARALGLRPRARIVAQALVGAEPyyhLDGPV---QATAKVLEKAGMKIGDI 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 336 KMWEINEAFSVVVLANIKMLDIDPQKVNIHGGAVSLGHPIGMSGARIVVHMTHALKQGEHGLAGI--CNGGGGASAILIQ 413
Cdd:PRK07850  306 DLVEINEAFASVVLSWAQVHEPDMDKVNVNGGAIALGHPVGSTGARLITTALHELERTDKSTALItmCAGGALSTGTIIE 385

                  ..
gi 1841866749 414 KL 415
Cdd:PRK07850  386 RI 387
PRK06504 PRK06504
acetyl-CoA C-acetyltransferase;
27-415 7.32e-79

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180595 [Multi-domain]  Cd Length: 390  Bit Score: 248.88  E-value: 7.32e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749  27 LNEVVIVSAVRTPIGSFQSSLFSLPATNLGSIAIKGAIEKAGIPSQEVKEVYMGNVIQAGE-GQAPARQATLGAGLPVST 105
Cdd:PRK06504    1 MAEAYIVAAARTAGGRKGGRLAGWHPADLAAQVLDALVDRSGADPALIEDVIMGCVSQVGEqATNVARNAVLASKLPESV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 106 PCTTVNKVCASGMKSIMMAAQSLMCGSQDVMVAGGMESMSNVPYTMTrGTTPYggvkledlivKDGLTDV--------YN 177
Cdd:PRK06504   81 PGTSIDRQCGSSQQALHFAAQAVMSGTMDIVIAAGVESMTRVPMGSP-STLPA----------KNGLGHYkspgmeerYP 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 178 KIH----MGncAENTAKKFSISREDQDTYAIKSYTKSKEGWESGIFAKEIVPVTISQKgKPDTEVKEDEEYKRVDFS--K 251
Cdd:PRK06504  150 GIQfsqfTG--AEMMAKKYGLSKDQLDEFALQSHQRAIAATQAGKFKAEIVPLEITRA-DGSGEMHTVDEGIRFDATleG 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 252 VPKLKTVfqKENGTVTAANASTLNDGAAALVLMTSEAAKRLNVKPLARIVGFADAAVDPIDFPIAPAHAVPKILAQTGLK 331
Cdd:PRK06504  227 IAGVKLI--AEGGRLTAATASQICDGASGVMVVNERGLKALGVKPLARIHHMTVIGGDPVIMLEAPLPATERALKKAGMK 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 332 KEDIKMWEINEAFSVVVLANIKMLDIDPQKVNIHGGAVSLGHPIGMSGARIVVHMTHALKQ--GEHGLAGICNGGGGASA 409
Cdd:PRK06504  305 IDDIDLYEVNEAFASVPLAWLKATGADPERLNVNGGAIALGHPLGASGTKLMTTLVHALKQrgKRYGLQTMCEGGGMANV 384

                  ....*.
gi 1841866749 410 ILIQKL 415
Cdd:PRK06504  385 TIVERL 390
PLN02287 PLN02287
3-ketoacyl-CoA thiolase
28-411 9.72e-79

3-ketoacyl-CoA thiolase


Pssm-ID: 215161 [Multi-domain]  Cd Length: 452  Bit Score: 250.45  E-value: 9.72e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749  28 NEVVIVSAVRTPI-----GSFQSSLfslPATNLGSIaIKGAIEKAGIPSQEVKEVYMGNVIQAGEGQA-PARQATLGAGL 101
Cdd:PLN02287   46 DDVVIVAAYRTPIckakrGGFKDTY---PDDLLAPV-LKAVVEKTGLNPSEVGDIVVGTVLAPGSQRAnECRMAAFYAGF 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 102 PVSTPCTTVNKVCASGMKSIMMAAQSLMCGSQDVMVAGGMESMSNVPYTMTRGTTPyggvKLEDL-IVKDGLtdvynkIH 180
Cdd:PLN02287  122 PETVPVRTVNRQCSSGLQAVADVAAAIKAGFYDIGIGAGVESMTTNPMAWEGGVNP----RVESFsQAQDCL------LP 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 181 MGNCAENTAKKFSISREDQDTYAIKSYTKSKEGWESGIFAKEIVPVTI------SQKGKPDTEVKEDEEYKRVDFSKVPK 254
Cdd:PLN02287  192 MGITSENVAERFGVTREEQDQAAVESHRKAAAATASGKFKDEIVPVHTkivdpkTGEEKPIVISVDDGIRPNTTLADLAK 271
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 255 LKTVFqKENGTVTAANASTLNDGAAALVLMTSEAAKRLNVKPLARIVGFADAAVDPIDFPIAPAHAVPKILAQTGLKKED 334
Cdd:PLN02287  272 LKPVF-KKNGTTTAGNSSQVSDGAGAVLLMKRSVAMQKGLPILGVFRSFAAVGVDPAVMGIGPAVAIPAAVKAAGLELDD 350
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 335 IKMWEINEAFSVVVLANIKMLDIDPQKVNIHGGAVSLGHPIGMSGARIVVHMTHALKQ----GEHGLAGICNGGG-GASA 409
Cdd:PLN02287  351 IDLFEINEAFASQFVYCCKKLGLDPEKVNVNGGAIALGHPLGATGARCVATLLHEMKRrgkdCRFGVVSMCIGTGmGAAA 430

                  ..
gi 1841866749 410 IL 411
Cdd:PLN02287  431 VF 432
fadA PRK08947
3-ketoacyl-CoA thiolase; Reviewed
28-415 4.11e-78

3-ketoacyl-CoA thiolase; Reviewed


Pssm-ID: 181592 [Multi-domain]  Cd Length: 387  Bit Score: 246.80  E-value: 4.11e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749  28 NEVVIVSAVRTPIGSFQSSLF-SLPATNLGSIAIKGAIEK-AGIPSQEVKEVYMGNVIQAGE-GQAPARQATLGAGLPVS 104
Cdd:PRK08947    2 EDVVIVDAIRTPMGRSKGGAFrNVRAEDLSAHLMRSLLARnPALDPAEIDDIIWGCVQQTLEqGFNIARNAALLAGIPHS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 105 TPCTTVNKVCASGMKSIMMAAQSLMCGSQDVMVAGGMESMSNVPytMTRGTTPYggvkledlivkDGLTDVYNKIH--MG 182
Cdd:PRK08947   82 VPAVTVNRLCGSSMQALHDAARAIMTGDGDVFLIGGVEHMGHVP--MNHGVDFH-----------PGLSKNVAKAAgmMG 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 183 NCAENTAKKFSISREDQDTYAIKSYTKSKEGWESGIFAKEIVPVTisqkGKpdtevKEDEEYKRVDFSKV---------- 252
Cdd:PRK08947  149 LTAEMLGKMHGISREQQDAFAARSHQRAWAATQEGRFKNEIIPTE----GH-----DADGVLKLFDYDEVirpettveal 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 253 PKLKTVFQKENGTVTAANASTLNDGAAALVLMTSEAAKRLNVKPLARIVGFADAAVDPIDFPIAPAHAVPKILAQTGLKK 332
Cdd:PRK08947  220 AALRPAFDPVNGTVTAGTSSALSDGASAMLVMSESRAKELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSI 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 333 EDIKMWEINEAF---SVVVLANIKMLDIDPQKVNIHGGAVSLGHPIGMSGARIVVHMTHALKQ--GEHGLAGICNGGGGA 407
Cdd:PRK08947  300 SDIDVFELNEAFaaqSLPCLKDLGLLDKMDEKVNLNGGAIALGHPLGCSGARISTTLLNLMERkdAQFGLATMCIGLGQG 379

                  ....*...
gi 1841866749 408 SAILIQKL 415
Cdd:PRK08947  380 IATVFERV 387
PRK08170 PRK08170
acetyl-CoA C-acetyltransferase;
73-415 6.84e-78

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181265 [Multi-domain]  Cd Length: 426  Bit Score: 247.24  E-value: 6.84e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749  73 EVKEVYMGNVIQAGEGQAPARQATLGAGLPVSTPCTTVNKVCASGMKSIMMAAQSLMCGSQDVMVAGGMESMSNVPY--- 149
Cdd:PRK08170   48 DLDEVILGCAMPSPDEANIARVVALRLGCGEKVPAWTVQRNCASGMQALDSAAANIALGRADLVLAGGVEAMSHAPLlfs 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 150 -TMTR-----GTTPYGGVKLEDL-------------IVKdGLTDVYNKIHMGNCAENTAKKFSISREDQDTYAIKSYTKS 210
Cdd:PRK08170  128 eKMVRwlagwYAAKSIGQKLAALgklrpsylapvigLLR-GLTDPVVGLNMGQTAEVLAHRFGITREQMDAYAARSHQRL 206
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 211 KEGWESGiFAKEIVPVtISQKGKpdteVKEDEEYKRVDFS--KVPKLKTVFQKENGTVTAANASTLNDGAAALVLMTSEA 288
Cdd:PRK08170  207 AAAQAEG-RLKEVVPL-FDRDGK----FYDHDDGVRPDSSmeKLAKLKPFFDRPYGRVTAGNSSQITDGACWLLLASEEA 280
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 289 AKRLNVKPLARIVGFADAAVDPIDFPIAPAHAVPKILAQTGLKKEDIKMWEINEAFSVVVLANIKMLD------------ 356
Cdd:PRK08170  281 VKKYGLPPLGRIVDSQWAALDPSQMGLGPVHAATPLLQRHGLTLEDLDLWEINEAFAAQVLACLAAWAdeeycreqlgld 360
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1841866749 357 -----IDPQKVNIHGGAVSLGHPIGMSGARIVVHMTHALKQ--GEHGLAGICNGGGGASAILIQKL 415
Cdd:PRK08170  361 galgeLDRERLNVDGGAIALGHPVGASGARIVLHLLHALKRrgTKRGIAAICIGGGQGGAMLLERV 426
PRK08242 PRK08242
acetyl-CoA C-acetyltransferase;
29-415 1.09e-74

acetyl-CoA C-acetyltransferase;


Pssm-ID: 236197 [Multi-domain]  Cd Length: 402  Bit Score: 238.24  E-value: 1.09e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749  29 EVVIVSAVRTPIGSFQS--SLFSLPATNLGSIAIKGAIEKAGIPSQEVKEVYMGNVIQAGE-GQAPARQATLGAGLPVST 105
Cdd:PRK08242    3 EAYIYDAVRTPRGKGKKdgSLHEVKPVRLAAGLLEALRDRNGLDTAAVDDVVLGCVTPVGDqGADIARTAVLAAGLPETV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 106 PCTTVNKVCASGMKSIMMAAQSLMCGSQDVMVAGGMESMSNVPYTMTRGTTPyggvkledliVKDGLTDVYNKIHMGNCA 185
Cdd:PRK08242   83 PGVQINRFCASGLEAVNLAAAKVRSGWDDLVIAGGVESMSRVPMGSDGGAWA----------MDPSTNFPTYFVPQGISA 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 186 ENTAKKFSISREDQDTYAIKSYTKSKEGWESGIFAKEIVPVTiSQKG----------KPDTEVK-------------EDE 242
Cdd:PRK08242  153 DLIATKYGFSREDVDAYAVESQQRAAAAWAEGYFAKSVVPVK-DQNGltildhdehmRPGTTMEslaklkpsfammgEMG 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 243 EYKRVDFSKVPKLKTVfqkeNGTVTAANASTLNDGAAALVLMTSEAAKRLNVKPLARIVGFADAAVDPIDFPIAPAHAVP 322
Cdd:PRK08242  232 GFDAVALQKYPEVERI----NHVHHAGNSSGIVDGAAAVLIGSEEAGKALGLKPRARIVATATIGSDPTIMLTGPVPATR 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 323 KILAQTGLKKEDIKMWEINEAFSVVVLANIKMLDIDPQKVNIHGGAVSLGHPIGMSGARIVVHMTHAL--KQGEHGLAGI 400
Cdd:PRK08242  308 KALAKAGLTVDDIDLFELNEAFASVVLRFMQALDIPHDKVNVNGGAIAMGHPLGATGAMILGTVLDELerRGKRTALITL 387
                         410
                  ....*....|....*
gi 1841866749 401 CNGGGGASAILIQKL 415
Cdd:PRK08242  388 CVGGGMGIATIIERV 402
PRK06690 PRK06690
acetyl-CoA C-acyltransferase;
28-415 2.07e-72

acetyl-CoA C-acyltransferase;


Pssm-ID: 180659 [Multi-domain]  Cd Length: 361  Bit Score: 231.19  E-value: 2.07e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749  28 NEVVIVSAVRTPIGSFQSSLFSLPATNLGSIAIKgaIEKAGIPsQEVKEVYMGNVIqaGEGQAPARQATLGAGLPVSTPC 107
Cdd:PRK06690    1 NRAVIVEAKRTPIGKKNGMLKDYEVQQLAAPLLT--FLSKGME-REIDDVILGNVV--GPGGNVARLSALEAGLGLHIPG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 108 TTVNKVCASGMKSIMMAAQSLMCGSQDVMVAGGMESMSNVPYTMTRGTTPyggvkledlivkdgltDVYNKIHMGNCAEN 187
Cdd:PRK06690   76 VTIDRQCGAGLEAIRTACHFIQGGAGKCYIAGGVESTSTSPFQNRARFSP----------------ETIGDPDMGVAAEY 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 188 TAKKFSISREDQDTYAIKSYTKSKEGWESGIFAKEIVPVTisqkGKPDTEVKEDEEYKRVdfskVPKLKTVFQKeNGTVT 267
Cdd:PRK06690  140 VAERYNITREMQDEYACLSYKRTLQALEKGYIHEEILSFN----GLLDESIKKEMNYERI----IKRTKPAFLH-NGTVT 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 268 AANASTLNDGAAALVLMTSEAAKRLNVKPLARIVGFADAAVDPIDFPIAPAHAVPKILAQTGLKKEDIKMWEINEAFSVV 347
Cdd:PRK06690  211 AGNSCGVNDGACAVLVMEEGQARKLGYKPVLRFVRSAVVGVDPNLPGTGPIFAVNKLLNEMNMKVEDIDYFEINEAFASK 290
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 348 VLANIKMLDIDPQKVNIHGGAVSLGHPIGMSGARIVVHMTHALKQ--GEHGLAGICNGGGGASAILIQKL 415
Cdd:PRK06690  291 VVACAKELQIPYEKLNVNGGAIALGHPYGASGAMLVTRLFYQAKRedMKYGIATLGIGGGIGLALLFEKV 360
PRK06025 PRK06025
acetyl-CoA C-acetyltransferase;
29-415 7.43e-63

acetyl-CoA C-acetyltransferase;


Pssm-ID: 235675 [Multi-domain]  Cd Length: 417  Bit Score: 208.09  E-value: 7.43e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749  29 EVVIVSAVRTP--IGSF-QSSLFSLPATNLGSIAIKGAIEKAGIPSQEVKEVYMGNVIQAG-EGQAPARQATLGAGLPVS 104
Cdd:PRK06025    3 EAYIIDAVRTPrgIGKVgKGALAHLHPQHLAATVLKALAERNGLNTADVDDIIWSTSSQRGkQGGDLGRMAALDAGYDIK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 105 TPCTTVNKVCASGMKSIMMAAQSLMCGSQDVMVAGGMESMS----NVPYTMTRGTTPYGgvkledliVKDG---LTDVYN 177
Cdd:PRK06025   83 ASGVTLDRFCGGGITSVNLAAAQIMSGMEDLVIAGGTEMMSytaaMAAEDMAAGKPPLG--------MGSGnlrLRALHP 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 178 KIHMGNCAENTAKKFSISREDQDTYAIKSYTKSKEGWESGIFAKEIVPVTisqkgKPDTEVKED-EEYKRVDFSK--VPK 254
Cdd:PRK06025  155 QSHQGVCGDAIATMEGITREALDALGLESQRRAARAIKEGRFDKSLVPVY-----RDDGSVALDhEEFPRPQTTAegLAA 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 255 LKTVFQK-------ENGTV------------------TAANASTLNDGAAALVLMTSEAAKRLNVKPLARIVGFADAAVD 309
Cdd:PRK06025  230 LKPAFTAiadypldDKGTTyrglinqkypdleikhvhHAGNSSGVVDGAAALLLASKAYAEKHGLKPRARIVAMANMGDD 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 310 PIDFPIAPAHAVPKILAQTGLKKEDIKMWEINEAFSVVVLANIKMLDIDPQKVNIHGGAVSLGHPIGMSGARIVVHMTHA 389
Cdd:PRK06025  310 PTLMLNAPVPAAKKVLAKAGLTKDDIDLWEINEAFAVVAEKFIRDLDLDRDKVNVNGGAIALGHPIGATGSILIGTVLDE 389
                         410       420
                  ....*....|....*....|....*...
gi 1841866749 390 LKQ--GEHGLAGICNGGGGASAILIQKL 415
Cdd:PRK06025  390 LERrgLKRGLVTMCAAGGMAPAIIIERV 417
Thiolase_C pfam02803
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
294-414 6.60e-57

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: 182.84  E-value: 6.60e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 294 VKPLARIVGFADAAVDPIDFPIAPAHAVPKILAQTGLKKEDIKMWEINEAFSVVVLANIKMLDIDPQKVNIHGGAVSLGH 373
Cdd:pfam02803   1 LKPLARIRSYATAGVDPAIMGIGPAYAIPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGIDPEKVNVNGGAIALGH 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1841866749 374 PIGMSGARIVVHMTHALKQ--GEHGLAGICNGGGGASAILIQK 414
Cdd:pfam02803  81 PLGASGARILVTLLHELKRrgGKYGLASLCIGGGQGVAMIIER 123
PRK09268 PRK09268
acetyl-CoA C-acetyltransferase;
22-411 6.42e-54

acetyl-CoA C-acetyltransferase;


Pssm-ID: 236440 [Multi-domain]  Cd Length: 427  Bit Score: 184.72  E-value: 6.42e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749  22 SSQRGLNEVVIVSAVRTPIGSFQSSLFSLPATNLGSIAIKGAIEKAGIPSQEVKEVYMGNVIQAGEGQAPARQATLGAGL 101
Cdd:PRK09268    1 MTMPTVRRVAILGGNRIPFARSNGAYADASNQDMLTAALDGLVDRFGLQGERLGEVVAGAVLKHSRDFNLTRECVLGSAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 102 PVSTPCTTVNKVCASGMKSIMMAAQSLMCGSQDVMVAGGMESMSNVP-----------YTMTRGTTPYGGVKL------E 164
Cdd:PRK09268   81 SPYTPAYDLQQACGTGLEAAILVANKIALGQIDSGIAGGVDTTSDAPiavneglrkilLELNRAKTTGDRLKAlgklrpK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 165 DLIV--------KDGLTdvynkihMGNCAENTAKKFSISREDQDTYAIKSYTKSKEGWESGIFAKEIVP---VTISQKGK 233
Cdd:PRK09268  161 HLAPeiprngepRTGLS-------MGEHAAITAKEWGISREAQDELAAASHQNLAAAYDRGFFDDLITPflgLTRDNNLR 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 234 PDTEVKedeeykrvdfsKVPKLKTVFQK-ENGTVTAANASTLNDGAAALVLMTSEAAKRLNVKPLARIVGFADAAVDPID 312
Cdd:PRK09268  234 PDSSLE-----------KLAKLKPVFGKgGRATMTAGNSTPLTDGASVVLLASEEWAAEHGLPVLAYLVDAETAAVDFVH 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 313 FP----IAPAHAVPKILAQTGLKKEDIKMWEINEAFSVVVLANIKM------------LD-----IDPQKVNIHGGAVSL 371
Cdd:PRK09268  303 GKegllMAPAYAVPRLLARNGLTLQDFDFYEIHEAFASQVLATLKAwedeeycrerlgLDaplgsIDRSKLNVNGSSLAA 382
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 1841866749 372 GHPIGMSGARIVVHMTHAL--KQGEHGLAGICNGGG-GASAIL 411
Cdd:PRK09268  383 GHPFAATGGRIVATLAKLLaeKGSGRGLISICAAGGqGVTAIL 425
nondecarbox_cond_enzymes cd00826
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ...
33-413 3.09e-52

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: 179.61  E-value: 3.09e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749  33 VSAVRTPIGSF---QSSLFSLPATNLGSIAIKGAIEKAGIPSQEVKEVYMGNVIQAGEGQAPARQATLGAGLPVSTPCTT 109
Cdd:cd00826     1 AGAAMTAFGKFggeNGADANDLAHEAGAKAIAAALEPAGVAAGAVEEACLGQVLGAGEGQNCAQQAAMHAGGLQEAPAIG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 110 VNKVCASGMKSIMMAAQSLMCGSQDVMVAGGMESMS----NVPYTMtrgttpyggvKLEDLIVKDGltdvynkihmgnca 185
Cdd:cd00826    81 MNNLCGSGLRALALAMQLIAGGDANCILAGGFEKMEtsaeNNAKEK----------HIDVLINKYG-------------- 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 186 entakkfsiSREDQDTYAIKSYTKSKEGWESGIFAKEIVPVTIsqKGKPDTEVKEDEEYKR----VDFSKVPKLKTVFQK 261
Cdd:cd00826   137 ---------MRACPDAFALAGQAGAEAAEKDGRFKDEFAKFGV--KGRKGDIHSDADEYIQfgdeASLDEIAKLRPAFDK 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 262 EnGTVTAANASTLNDGAAALVLMTSEAA-------KRLNVKPLARIVGFADAAVDPIDFPIA----PAHAVPKILAQTGL 330
Cdd:cd00826   206 E-DFLTAGNACGLNDGAAAAILMSEAEAqkhglqsKAREIQALEMITDMASTFEDKKVIKMVggdgPIEAARKALEKAGL 284
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 331 KKEDIKMWEINEAFSVVVLANIKMLDIDPQK------------------VNIHGGAVSLGHPIGMSGARIVVHMTHALKQ 392
Cdd:cd00826   285 GIGDLDLIEAHDAFAANACATNEALGLCPEGqggalvdrgdntyggksiINPNGGAIAIGHPIGASGAAICAELCFELKG 364
                         410       420
                  ....*....|....*....|....*...
gi 1841866749 393 -------GEHGLAGICNGGGGASAILIQ 413
Cdd:cd00826   365 eagkrqgAGAGLALLCIGGGGGAAMCIE 392
SCP-x_thiolase cd00829
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ...
59-409 2.67e-19

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: 88.86  E-value: 2.67e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749  59 AIKGAIEKAGIPSQEVKEVYMGNVIQAGEGQAPARQATLGAGLPVsTPCTTVNKVCASGMKSIMMAAQSLMCGSQDVMVA 138
Cdd:cd00829    23 AARAALDDAGLEPADIDAVVVGNAAGGRFQSFPGALIAEYLGLLG-KPATRVEAAGASGSAAVRAAAAAIASGLADVVLV 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 139 GGMESMSNVPYTMTRGTTPyGGVKLEDLIVKDGLT--DVYNKI---HMgncaentaKKFSISREDqdtyaiksytkskeg 213
Cdd:cd00829   102 VGAEKMSDVPTGDEAGGRA-SDLEWEGPEPPGGLTppALYALAarrYM--------HRYGTTRED--------------- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 214 wesgiFAKeiVPVTI---------SQKGKPDTEvkedEEYKRvdfSKV---PklktvfqkengtVTAANASTLNDGAAAL 281
Cdd:cd00829   158 -----LAK--VAVKNhrnaarnpyAQFRKPITV----EDVLN---SRMiadP------------LRLLDCCPVSDGAAAV 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 282 VLMTSEAAKRLnVKPLARIVGFADA-------AVDPIDFPIAPAHAVPKILAQTGLKKEDIKMWEINEAFSVVVLANIKM 354
Cdd:cd00829   212 VLASEERAREL-TDRPVWILGVGAAsdtpslsERDDFLSLDAARLAARRAYKMAGITPDDIDVAELYDCFTIAELLALED 290
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 355 L---------------DIDPQ---KVNIHGGAVSLGHPIGMSGARIVVHMTHALKqGEHG--------LAGICNGGGGAS 408
Cdd:cd00829   291 LgfcekgeggklvregDTAIGgdlPVNTSGGLLSKGHPLGATGLAQAVEAVRQLR-GEAGarqvpgarVGLAHNIGGTGS 369

                  .
gi 1841866749 409 A 409
Cdd:cd00829   370 A 370
cond_enzymes cd00327
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ...
52-412 1.26e-14

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


Pssm-ID: 238201 [Multi-domain]  Cd Length: 254  Bit Score: 73.25  E-value: 1.26e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749  52 ATNLGSIAIKGAIEKAGIPSQEVKEVYMGNVIQAGEGQAPARQATLGAGLPvSTPCTTVNKVCASGMKSIMMAAQSLMCG 131
Cdd:cd00327     7 ASELGFEAAEQAIADAGLSKGPIVGVIVGTTGGSGEFSGAAGQLAYHLGIS-GGPAYSVNQACATGLTALALAVQQVQNG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 132 SQDVMVAGGMESmsnvpytmtrgttpyggvkledlivkdgltdvynkihmgncaentakkfsisredqdtyaiksytksk 211
Cdd:cd00327    86 KADIVLAGGSEE-------------------------------------------------------------------- 97
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 212 egwesgifakeivpvtisqkgkpdtevkedeeykrvdfskvpklktvfqkengtvtaanaSTLNDGAAALVLMTSEAAKR 291
Cdd:cd00327    98 ------------------------------------------------------------FVFGDGAAAAVVESEEHALR 117
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 292 LNVKPLARIVGFADAAVDPIDFPI----APAHAVPKILAQTGLKKEDIKMWEINEAFSVVVLANIKMLDIDPQKV---NI 364
Cdd:cd00327   118 RGAHPQAEIVSTAATFDGASMVPAvsgeGLARAARKALEGAGLTPSDIDYVEAHGTGTPIGDAVELALGLDPDGVrspAV 197
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 365 HGGAVSLGHPIGMSGARIVVhmtHALKQGEH------------GLAGICNGGGGASAILI 412
Cdd:cd00327   198 SATLIMTGHPLGAAGLAILD---ELLLMLEHefipptpreprtVLLLGFGLGGTNAAVVL 254
PRK06064 PRK06064
thiolase domain-containing protein;
59-392 2.29e-10

thiolase domain-containing protein;


Pssm-ID: 235688 [Multi-domain]  Cd Length: 389  Bit Score: 61.84  E-value: 2.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749  59 AIKGAIEKAGIPSQEVKEVYMGNVIQAGEGQAPARQATLG--AGLPvSTPCTTVNKVCASGMKSIMMAAQSLMCGSQDVM 136
Cdd:PRK06064   29 AGLEALEDAGIDGKDIDAMYVGNMSAGLFVSQEHIAALIAdyAGLA-PIPATRVEAACASGGAALRQAYLAVASGEADVV 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 137 VAGGMESMSNVPYTMTRGTTPYGGVKLEDLIVkdGLTDV-----YNKIHMgncaentaKKFSISREDQDTYAIKS-YTKS 210
Cdd:PRK06064  108 LAAGVEKMTDVPTPDATEAIARAGDYEWEEFF--GATFPglyalIARRYM--------HKYGTTEEDLALVAVKNhYNGS 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 211 KEGWESgiFAKEIvpvtisqkgkpdtevkedeeykrvdfskvpklkTVFQKENGTVTAA-----NASTLNDGAAALVLMT 285
Cdd:PRK06064  178 KNPYAQ--FQKEI---------------------------------TVEQVLNSPPVADplkllDCSPITDGAAAVILAS 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 286 SEAAKRLNVKPLaRIVGFADAAvDPI------DFPI--APAHAVPKILAQTGLKKEDIKMWEINEAFSVVVLANIKML-- 355
Cdd:PRK06064  223 EEKAKEYTDTPV-WIKASGQAS-DTIalhdrkDFTTldAAVVAAEKAYKMAGIEPKDIDVAEVHDCFTIAEILAYEDLgf 300
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1841866749 356 -------------------DIdpqKVNIHGGAVSLGHPIGMSGARIVVHMTHALKQ 392
Cdd:PRK06064  301 akkgeggklaregqtyiggDI---PVNPSGGLKAKGHPVGATGVSQAVEIVWQLRG 353
PTZ00455 PTZ00455
3-ketoacyl-CoA thiolase; Provisional
59-400 1.27e-08

3-ketoacyl-CoA thiolase; Provisional


Pssm-ID: 240424 [Multi-domain]  Cd Length: 438  Bit Score: 56.44  E-value: 1.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749  59 AIKGAIEKAGIPSQE--VKEVYMGNVIqageGQAPARQATLGAGLPVST------------PCTTVNKVCASGMKSIMMA 124
Cdd:PTZ00455   55 AIQGTLENTGLDGKAalVDKVVVGNFL----GELFSSQGHLGPAAVGSLgqsgasnallykPAMRVEGACASGGLAVQSA 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 125 AQSLMCGSQDVMVAGGMESMSNVpytmtrgTTPYGG---VKLEDLIVKDGLTDVYNKIHMGNCAENTAKKFSISREDQDT 201
Cdd:PTZ00455  131 WEALLAGTSDIALVVGVEVQTTV-------SARVGGdylARAADYRRQRKLDDFTFPCLFAKRMKYIQEHGHFTMEDTAR 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 202 YAIKSYTKSKEGWESGIFAKEIVPVTISQKGKPDTEVKEDEEYKrvdfskvPKLKTvfqkengtvtaANASTLNDGAAAL 281
Cdd:PTZ00455  204 VAAKAYANGNKNPLAHMHTRKLSLEFCTGASDKNPKFLGNETYK-------PFLRM-----------TDCSQVSDGGAGL 265
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 282 VLMTSEAAKRLNVKP----LARIVGFADAA----VDPIDFP--IAPAHAVPKILAQTGLKKEDIKMWEINEAFSVVVLAN 351
Cdd:PTZ00455  266 VLASEEGLQKMGLSPndsrLVEIKSLACASgnlyEDPPDATrmFTSRAAAQKALSMAGVKPSDLQVAEVHDCFTIAELLM 345
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1841866749 352 IKMLDI-DPQK-----------------VNIHGGAVSLGHPIGMSGARIVVHMTHALKQ--GEHGLAGI 400
Cdd:PTZ00455  346 YEALGIaEYGHakdlirngatalegripVNTGGGLLSFGHPVGATGVKQIMEVYRQMKGqcGEYQMKNI 414
PRK06289 PRK06289
acetyl-CoA acetyltransferase; Provisional
59-392 6.38e-08

acetyl-CoA acetyltransferase; Provisional


Pssm-ID: 235771 [Multi-domain]  Cd Length: 403  Bit Score: 54.31  E-value: 6.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749  59 AIKGAIEKAGIPSQEVKEVYMGNVIqageGQAPARQATLGaGLPVS-------TPCTTVNKVCASGMKSIMMAAQSLMCG 131
Cdd:PRK06289   33 VVDGTLAAAGVDADDIEVVHVGNFF----GELFAGQGHLG-AMPATvhpalwgVPASRHEAACASGSVATLAAMADLRAG 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 132 SQDVMVAGGMESMSNVP---YTMTRGTTPYGGVKLEDliVKDGLTDVYNKIhmgncAENTAKKFSISREDQDTYAIKSYT 208
Cdd:PRK06289  108 RYDVALVVGVELMKTVPgdvAAEHLGAAAWTGHEGQD--ARFPWPSMFARV-----ADEYDRRYGLDEEHLRAIAEINFA 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 209 KSK-------EGWESgifakeivpvtisqkgkPDTEVKEDEEYKRVDFSKVPKLktvfqkengtvtaaNASTLNDGAAAL 281
Cdd:PRK06289  181 NARrnpnaqtRGWAF-----------------PDEATNDDDATNPVVEGRLRRQ--------------DCSQVTDGGAGV 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 282 VLMTSEAAKRL-NVKPLARIVGF-------------ADAAVDPIDFPiapaH---AVPKILAQTGLKKEDIKMWEINEAF 344
Cdd:PRK06289  230 VLASDAYLRDYaDARPIPRIKGWghrtaplgleqklDRSAGDPYVLP----HvrqAVLDAYRRAGVGLDDLDGFEVHDCF 305
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1841866749 345 SVVVLANIKML---------------DIDP---QKVNIHGGAVSLGHPIGMSGARIvvhMTHALKQ 392
Cdd:PRK06289  306 TPSEYLAIDHIgltgpgeswkaiengEIAIggrLPINPSGGLIGGGHPVGASGVRM---LLDAAKQ 368
PRK06157 PRK06157
acetyl-CoA acetyltransferase; Validated
59-399 1.37e-07

acetyl-CoA acetyltransferase; Validated


Pssm-ID: 180433 [Multi-domain]  Cd Length: 398  Bit Score: 53.11  E-value: 1.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749  59 AIKGAIEKAGIPSQEVKEVYMGNVIQAgegqaparQATLGAGLPVST-------PCTTVNKVCASGMKSIMMAAQSLMCG 131
Cdd:PRK06157   34 AFLEALADAGIEPKDIDAAWFGTHYDE--------IGSGKSGTPLSRalrlpniPVTRVENFCATGSEAFRGAVYAVASG 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 132 SQDVMVAGGMESMSNvpytmtrgtTPYGGVKLEDlivKDGLTDVYNkihmgncAENTAkkfsisredqdtyaiksytksk 211
Cdd:PRK06157  106 AYDIALALGVEKLKD---------TGYGGLPVAN---PGTLADMTM-------PNVTA---------------------- 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 212 egweSGIFAkEIVPVTISQKGKPDTEVKEDEEYKRV----DFSKVPKLKtvFQKENGTVTAANA------------STLN 275
Cdd:PRK06157  145 ----PGNFA-QLASAYAAKYGVSREDLKRAMAHVSVkshaNGARNPKAH--LRKAVTEEQVLKApmiagplglfdcCGVS 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 276 DGAAALVLMTSEAAKRLN------VKPLARIVGFADAAVDP-IDFPIAPA--HAVPKILAQTGLK--KEDIKMWEINEAF 344
Cdd:PRK06157  218 DGAAAAIVTTPEIARALGkkdpvyVKALQLAVSNGWELQYNgWDGSYFPTtrIAARKAYREAGITdpREELSMAEVHDCF 297
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1841866749 345 SVVVLANIKMLDIDPQ------------------KVNIHGGAVSLGHPIGMSGARIVVHMTHALkqgeHGLAG 399
Cdd:PRK06157  298 SITELVTMEDLGLSERgqawrdvldgffdadgglPCQIDGGLKCFGHPIGASGLRMLYEMYLQL----LGRAG 366
PRK07516 PRK07516
thiolase domain-containing protein;
272-409 1.92e-06

thiolase domain-containing protein;


Pssm-ID: 181013 [Multi-domain]  Cd Length: 389  Bit Score: 49.56  E-value: 1.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 272 STLNDGAAALVLMTSEAAKRLNvkplaRIVGFADAA----------VDPIDFPiAPAHAVPKILAQTGLKKEDIKMWEIN 341
Cdd:PRK07516  213 SLVSDGAAALVLADAETARALQ-----RAVRFRARAhvndflplsrRDPLAFE-GPRRAWQRALAQAGVTLDDLSFVETH 286
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 342 EAFSVVVLANIKMLDIDPQ------------------KVNIHGGAVSLGHPIGMSGarivVHMtHALK----QGEHG--- 396
Cdd:PRK07516  287 DCFTIAELIEYEAMGLAPPgqgarairegwtakdgklPVNPSGGLKAKGHPIGATG----VSM-HVLAamqlTGEAGgmq 361
                         170
                  ....*....|....*...
gi 1841866749 397 -----LAGICNGGGGASA 409
Cdd:PRK07516  362 ipgakLAGVFNMGGAAVA 379
PRK05952 PRK05952
beta-ketoacyl-ACP synthase;
274-392 6.66e-06

beta-ketoacyl-ACP synthase;


Pssm-ID: 235653 [Multi-domain]  Cd Length: 381  Bit Score: 47.74  E-value: 6.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 274 LNDGAAALVLMTSEAAKRLNVKPLARIVGF---ADA----AVDPiDFPIAPAhAVPKILAQTGLKKEDIKM-------WE 339
Cdd:PRK05952  208 LGEGGAILVLESAELAQKRGAKIYGQILGFgltCDAyhmsAPEP-DGKSAIA-AIQQCLARSGLTPEDIDYihahgtaTR 285
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1841866749 340 INEAFSVVVlanIKMLdiDPQKVNIHGGAVSLGHPIGMSGARIVVHMTHALKQ 392
Cdd:PRK05952  286 LNDQREANL---IQAL--FPHRVAVSSTKGATGHTLGASGALGVAFSLLALRH 333
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
90-146 9.06e-06

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


Pssm-ID: 238430 [Multi-domain]  Cd Length: 406  Bit Score: 47.53  E-value: 9.06e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1841866749  90 APARQATLGAGL--PVSTPCTTvnkvCASGMKSIMMAAQSLMCGSQDVMVAGGMESMSN 146
Cdd:cd00834   139 MAAGQVAIRLGLrgPNYTVSTA----CASGAHAIGDAARLIRLGRADVVIAGGAEALIT 193
FabB COG0304
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...
106-151 2.37e-05

3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism]; 3-oxoacyl-(acyl-carrier-protein) synthase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440073 [Multi-domain]  Cd Length: 409  Bit Score: 46.24  E-value: 2.37e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1841866749 106 PCTTVNKVCASGMKSIMMAAQSLMCGSQDVMVAGGMESMSNvPYTM 151
Cdd:COG0304   153 PNYTVSTACASGAHAIGEAYRLIRRGRADVMIAGGAEAAIT-PLGL 197
PRK07314 PRK07314
beta-ketoacyl-ACP synthase II;
106-143 6.59e-05

beta-ketoacyl-ACP synthase II;


Pssm-ID: 235987 [Multi-domain]  Cd Length: 411  Bit Score: 44.78  E-value: 6.59e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1841866749 106 PCTTVNKVCASGMKSIMMAAQSLMCGSQDVMVAGGMES 143
Cdd:PRK07314  154 PNHSIVTACATGAHAIGDAARLIAYGDADVMVAGGAEA 191
PRK08256 PRK08256
lipid-transfer protein; Provisional
49-144 8.70e-05

lipid-transfer protein; Provisional


Pssm-ID: 181327 [Multi-domain]  Cd Length: 391  Bit Score: 44.50  E-value: 8.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749  49 SLPATNLGSIAIKGAIEKAGIPSQEVKEVYMGNViqAGE---GQAPARQATLgAGLPVstpcTTVNKVCASGMKSIMMAA 125
Cdd:PRK08256   19 SWDYPDMAAEAGRAALADAGIDYDAVQQAYVGYV--YGDstsGQRALYEVGM-TGIPI----VNVNNNCSTGSTALFLAR 91
                          90
                  ....*....|....*....
gi 1841866749 126 QSLMCGSQDVMVAGGMESM 144
Cdd:PRK08256   92 QAVRSGAADCALALGFEQM 110
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
63-144 1.38e-04

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


Pssm-ID: 425468 [Multi-domain]  Cd Length: 251  Bit Score: 43.01  E-value: 1.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749  63 AIEKAGIPSQEVKEVYMGNVIQAGEGQAPARQATLGAGLPVST------------------------PCTTVNKVCASGM 118
Cdd:pfam00109  98 ALEDAGITPDSLDGSRTGVFIGSGIGDYAALLLLDEDGGPRRGspfavgtmpsviagrisyflglrgPSVTVDTACSSSL 177
                          90       100
                  ....*....|....*....|....*.
gi 1841866749 119 KSIMMAAQSLMCGSQDVMVAGGMESM 144
Cdd:pfam00109 178 VAIHAAVQSIRSGEADVALAGGVNLL 203
PRK12578 PRK12578
thiolase domain-containing protein;
59-396 2.23e-04

thiolase domain-containing protein;


Pssm-ID: 183606 [Multi-domain]  Cd Length: 385  Bit Score: 43.30  E-value: 2.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749  59 AIKGAIEKAGIPSQEVKEVYMGNVIQAGEGQAPARQATLGAGLPVSTPcTTVNKVCASGMKSIMMAAQSLMCGSQDVMVA 138
Cdd:PRK12578   28 SIKEALNDAGVSQTDIELVVVGSTAYRGIELYPAPIVAEYSGLTGKVP-LRVEAMCATGLAASLTAYTAVASGLVDMAIA 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 139 GGMESMSNVPYTMTRGTTPYGGVKLEDLIVKDGLTDVYNKIHmgncAENTAKKFSISREDQDTYAIKSYtKSKEGWESGI 218
Cdd:PRK12578  107 VGVDKMTEVDTSTSLAIGGRGGNYQWEYHFYGTTFPTYYALY----ATRHMAVYGTTEEQMALVSVKAH-KYGAMNPKAH 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 219 FAKeivPVTIsqkgkpdtevkEDEEYKRVdFSKVPKLktvfqkengtvtaANASTLNDGAAALVLMTSEAAKRLNVKPLA 298
Cdd:PRK12578  182 FQK---PVTV-----------EEVLKSRA-ISWPIKL-------------LDSCPISDGSATAIFASEEKVKELKIDSPV 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 299 RI--VGFA-DAA-----VDPIDFPiAPAHAVPKILAQTGLKKEDIKMWEINEAFSVVVLANIKMLDI------------- 357
Cdd:PRK12578  234 WItgIGYAnDYAyvarrGEWVGFK-ATQLAARQAYNMAKVTPNDIEVATVHDAFTIAEIMGYEDLGFtekgkggkfieeg 312
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1841866749 358 DPQK-----VNIHGGAVSLGHPIGMSGARIVVHMTHALKqGEHG 396
Cdd:PRK12578  313 QSEKggkvgVNLFGGLKAKGHPLGATGLSMIYEITKQLR-DEAG 355
PRK08142 PRK08142
thiolase domain-containing protein;
276-349 5.70e-04

thiolase domain-containing protein;


Pssm-ID: 236164 [Multi-domain]  Cd Length: 388  Bit Score: 42.00  E-value: 5.70e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1841866749 276 DGAAALVLMTSEAAKRLNvKPLARIVGFADAAVDPIDFPI-----APAHAVPKILAQTGLKKEDIKMWEINEAFSVVVL 349
Cdd:PRK08142  212 DGGGALVVVRPEIARSLK-RPLVKVLGAGEAIKGQMGGKVdltysGAAWSGPAAFAEAGVTPADIKYASIYDSFTITVL 289
elong_cond_enzymes cd00828
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ...
79-145 4.12e-03

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


Pssm-ID: 238424 [Multi-domain]  Cd Length: 407  Bit Score: 39.34  E-value: 4.12e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1841866749  79 MGNVIQAGEGQAPARQATLGAGLPVST-PCTTVNKVCASGMKSIMMAAQSLMCGSQDVMVAGGMESMS 145
Cdd:cd00828   126 NPYVSPKWMLSPNTVAGWVNILLLSSHgPIKTPVGACATALEALDLAVEAIRSGKADIVVVGGVEDPL 193
FabB COG0304
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...
277-335 5.83e-03

3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism]; 3-oxoacyl-(acyl-carrier-protein) synthase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440073 [Multi-domain]  Cd Length: 409  Bit Score: 38.54  E-value: 5.83e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1841866749 277 GAAALVLMTSEAAKRLNVKPLARIVGFA---DAA--VDPIDFPIAPAHAVPKILAQTGLKKEDI 335
Cdd:COG0304   232 GAGVLVLEELEHAKARGAKIYAEVVGYGassDAYhiTAPAPDGEGAARAMRAALKDAGLSPEDI 295
PRK08257 PRK08257
acetyl-CoA acetyltransferase; Validated
276-359 9.13e-03

acetyl-CoA acetyltransferase; Validated


Pssm-ID: 236204 [Multi-domain]  Cd Length: 498  Bit Score: 38.36  E-value: 9.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841866749 276 DGAAALVLMTSEAAKRLNVkPLARIV---GFADaAVDPI------DFPIAPA--HAVPKILAQTGLKKEDIKMWEINEAF 344
Cdd:PRK08257  244 DQGAAVLLTSVAKARRLGV-PEDRWVylhGGAD-AHDPYdilerpDLHRSPAirAAGRRALALAGLGIDDIDAFDLYSCF 321
                          90
                  ....*....|....*
gi 1841866749 345 SVVVLANIKMLDIDP 359
Cdd:PRK08257  322 PSAVQVAARELGLDL 336
 
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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