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Conserved domains on  [gi|2264345237|gb|UTB60282|]
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acetyl-coenzyme A acetyltransferase, partial [Staphylococcus lugdunensis]

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 ...
 1-177 9.41e-85

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: 254.33  E-value: 9.41e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237   1 RYKGKLRDYSAVELGTAALKAAVEAIDIDPSTIQQVIFGNVLQSGVGQNPARQIAIKAGLPNTTPAMTINEVCGSGLKAI 80
Cdd:cd00751    12 RFGGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGEGQNPARQAALLAGLPESVPATTVNRVCGSGLQAV 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237  81 ILGKQLIQLGEAKVVAVGGVESMTNAPQLI------LKEGQDPVESFMHDGLTDAFHYVPMGVTAENIAEKYHISREMQD 154
Cdd:cd00751    92 ALAAQSIAAGEADVVVAGGVESMSRAPYLLpkarrgGRLGLNTLDGMLDDGLTDPFTGLSMGITAENVAEKYGISREEQD 171

                         170       180
                  ....*....|....*....|...
gi 2264345237 155 AFANQSQQKAHQATINGKFNNEI 177
Cdd:cd00751   172 EFALRSHQRAAAAQEAGRFKDEI 194
 
Name Accession Description Interval E-value
thiolase cd00751
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ...
 1-177 9.41e-85

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: 254.33  E-value: 9.41e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237   1 RYKGKLRDYSAVELGTAALKAAVEAIDIDPSTIQQVIFGNVLQSGVGQNPARQIAIKAGLPNTTPAMTINEVCGSGLKAI 80
Cdd:cd00751    12 RFGGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGEGQNPARQAALLAGLPESVPATTVNRVCGSGLQAV 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237  81 ILGKQLIQLGEAKVVAVGGVESMTNAPQLI------LKEGQDPVESFMHDGLTDAFHYVPMGVTAENIAEKYHISREMQD 154
Cdd:cd00751    92 ALAAQSIAAGEADVVVAGGVESMSRAPYLLpkarrgGRLGLNTLDGMLDDGLTDPFTGLSMGITAENVAEKYGISREEQD 171

                         170       180
                  ....*....|....*....|...
gi 2264345237 155 AFANQSQQKAHQATINGKFNNEI 177
Cdd:cd00751   172 EFALRSHQRAAAAQEAGRFKDEI 194
PRK05790 PRK05790
putative acyltransferase; Provisional
 1-177 9.42e-85

putative acyltransferase; Provisional


Pssm-ID: 180261 [Multi-domain]  Cd Length: 393  Bit Score: 254.69  E-value: 9.42e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237   1 RYKGKLRDYSAVELGTAALKAAVEAIDIDPSTIQQVIFGNVLQSGVGQNPARQIAIKAGLPNTTPAMTINEVCGSGLKAI 80
Cdd:PRK05790   16 KFGGALKDVSAVELGAIVIKAALERAGVPPEQVDEVIMGQVLQAGAGQNPARQAALKAGLPVEVPALTINKVCGSGLKAV 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237  81 ILGKQLIQLGEAKVVAVGGVESMTNAPQLI--LKEGQ-----DPVESFMHDGLTDAFHYVPMGVTAENIAEKYHISREMQ 153
Cdd:PRK05790   96 ALAAQAIRAGDADIVVAGGQESMSQAPHVLpgSRWGQkmgdvELVDTMIHDGLTDAFNGYHMGITAENLAEQYGITREEQ 175

                         170       180
                  ....*....|....*....|....
gi 2264345237 154 DAFANQSQQKAHQATINGKFNNEI 177
Cdd:PRK05790  176 DEFALASQQKAEAAIKAGRFKDEI 199
PaaJ COG0183
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ...
 1-177 4.08e-81

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: 245.36  E-value: 4.08e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237   1 RYKGKLRDYSAVELGTAALKAAVEAIDIDPSTIQQVIFGNVLQSGVGQNPARQIAIKAGLPNTTPAMTINEVCGSGLKAI 80
Cdd:COG0183    16 RFGGALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQAGQGQNPARQAALLAGLPESVPAVTVNRVCGSGLQAV 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237  81 ILGKQLIQLGEAKVVAVGGVESMTNAPQLI------LKEGQDPVESFMHDGLTDAFHYVPMGVTAENIAEKYHISREMQD 154
Cdd:COG0183    96 ALAAQAIAAGDADVVIAGGVESMSRAPMLLpkarwgYRMNAKLVDPMINPGLTDPYTGLSMGETAENVAERYGISREEQD 175

                         170       180
                  ....*....|....*....|...
gi 2264345237 155 AFANQSQQKAHQATINGKFNNEI 177
Cdd:COG0183   176 AFALRSHQRAAAAIAAGRFDDEI 198
Thiolase_N pfam00108
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
 1-177 9.12e-71

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: 214.47  E-value: 9.12e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237   1 RYKGKLRDYSAVELGTAALKAAVEAIDIDPSTIQQVIFGNVLQSGVGQNPARQIAIKAGLPNTTPAMTINEVCGSGLKAI 80
Cdd:pfam00108  13 SFGGSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQAGEGQNPARQAALKAGIPDSAPAVTINKVCGSGLKAV 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237  81 ILGKQLIQLGEAKVVAVGGVESMTNAPQLI-------LKEGQDPVESFM-HDGLTDAFHYVPMGVTAENIAEKYHISREM 152
Cdd:pfam00108  93 YLAAQSIASGDADVVLAGGVESMSHAPYALptdarsgLKHGDEKKHDLLiPDGLTDAFNGYHMGLTAENVAKKYGISREE 172

                         170       180
                  ....*....|....*....|....*
gi 2264345237 153 QDAFANQSQQKAHQATINGKFNNEI 177
Cdd:pfam00108 173 QDAFAVKSHQKAAAAPKAGKFKDEI 197
AcCoA-C-Actrans TIGR01930
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ...
 1-177 9.90e-66

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: 205.54  E-value: 9.90e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237   1 RYKGKLRDYSAVELGTAALKAAVEAIDIDPSTIQQVIFGNVLQSGVGQNPARQIAIKAGLPNTTPAMTINEVCGSGLKAI 80
Cdd:TIGR01930  11 KFGGSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLQAGEQQNIARQAALLAGLPESVPAYTVNRQCASGLQAV 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237  81 ILGKQLIQLGEAKVVAVGGVESMTNAPQLI---LKEGQDP----VESFMHDGLTDAFHYVPMGVTAENIAEKYHISREMQ 153
Cdd:TIGR01930  91 ILAAQLIRAGEADVVVAGGVESMSRVPYGVprsLRWGVKPgnaeLEDARLKDLTDANTGLPMGVTAENLAKKYGISREEQ 170

                         170       180
                  ....*....|....*....|....
gi 2264345237 154 DAFANQSQQKAHQATINGKFNNEI 177
Cdd:TIGR01930 171 DEYALRSHQRAAKAWEEGLFKDEI 194
 
Name Accession Description Interval E-value
thiolase cd00751
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ...
 1-177 9.41e-85

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: 254.33  E-value: 9.41e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237   1 RYKGKLRDYSAVELGTAALKAAVEAIDIDPSTIQQVIFGNVLQSGVGQNPARQIAIKAGLPNTTPAMTINEVCGSGLKAI 80
Cdd:cd00751    12 RFGGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGEGQNPARQAALLAGLPESVPATTVNRVCGSGLQAV 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237  81 ILGKQLIQLGEAKVVAVGGVESMTNAPQLI------LKEGQDPVESFMHDGLTDAFHYVPMGVTAENIAEKYHISREMQD 154
Cdd:cd00751    92 ALAAQSIAAGEADVVVAGGVESMSRAPYLLpkarrgGRLGLNTLDGMLDDGLTDPFTGLSMGITAENVAEKYGISREEQD 171

                         170       180
                  ....*....|....*....|...
gi 2264345237 155 AFANQSQQKAHQATINGKFNNEI 177
Cdd:cd00751   172 EFALRSHQRAAAAQEAGRFKDEI 194
PRK05790 PRK05790
putative acyltransferase; Provisional
 1-177 9.42e-85

putative acyltransferase; Provisional


Pssm-ID: 180261 [Multi-domain]  Cd Length: 393  Bit Score: 254.69  E-value: 9.42e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237   1 RYKGKLRDYSAVELGTAALKAAVEAIDIDPSTIQQVIFGNVLQSGVGQNPARQIAIKAGLPNTTPAMTINEVCGSGLKAI 80
Cdd:PRK05790   16 KFGGALKDVSAVELGAIVIKAALERAGVPPEQVDEVIMGQVLQAGAGQNPARQAALKAGLPVEVPALTINKVCGSGLKAV 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237  81 ILGKQLIQLGEAKVVAVGGVESMTNAPQLI--LKEGQ-----DPVESFMHDGLTDAFHYVPMGVTAENIAEKYHISREMQ 153
Cdd:PRK05790   96 ALAAQAIRAGDADIVVAGGQESMSQAPHVLpgSRWGQkmgdvELVDTMIHDGLTDAFNGYHMGITAENLAEQYGITREEQ 175

                         170       180
                  ....*....|....*....|....
gi 2264345237 154 DAFANQSQQKAHQATINGKFNNEI 177
Cdd:PRK05790  176 DEFALASQQKAEAAIKAGRFKDEI 199
PaaJ COG0183
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ...
 1-177 4.08e-81

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: 245.36  E-value: 4.08e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237   1 RYKGKLRDYSAVELGTAALKAAVEAIDIDPSTIQQVIFGNVLQSGVGQNPARQIAIKAGLPNTTPAMTINEVCGSGLKAI 80
Cdd:COG0183    16 RFGGALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQAGQGQNPARQAALLAGLPESVPAVTVNRVCGSGLQAV 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237  81 ILGKQLIQLGEAKVVAVGGVESMTNAPQLI------LKEGQDPVESFMHDGLTDAFHYVPMGVTAENIAEKYHISREMQD 154
Cdd:COG0183    96 ALAAQAIAAGDADVVIAGGVESMSRAPMLLpkarwgYRMNAKLVDPMINPGLTDPYTGLSMGETAENVAERYGISREEQD 175

                         170       180
                  ....*....|....*....|...
gi 2264345237 155 AFANQSQQKAHQATINGKFNNEI 177
Cdd:COG0183   176 AFALRSHQRAAAAIAAGRFDDEI 198
Thiolase_N pfam00108
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
 1-177 9.12e-71

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: 214.47  E-value: 9.12e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237   1 RYKGKLRDYSAVELGTAALKAAVEAIDIDPSTIQQVIFGNVLQSGVGQNPARQIAIKAGLPNTTPAMTINEVCGSGLKAI 80
Cdd:pfam00108  13 SFGGSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQAGEGQNPARQAALKAGIPDSAPAVTINKVCGSGLKAV 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237  81 ILGKQLIQLGEAKVVAVGGVESMTNAPQLI-------LKEGQDPVESFM-HDGLTDAFHYVPMGVTAENIAEKYHISREM 152
Cdd:pfam00108  93 YLAAQSIASGDADVVLAGGVESMSHAPYALptdarsgLKHGDEKKHDLLiPDGLTDAFNGYHMGLTAENVAKKYGISREE 172

                         170       180
                  ....*....|....*....|....*
gi 2264345237 153 QDAFANQSQQKAHQATINGKFNNEI 177
Cdd:pfam00108 173 QDAFAVKSHQKAAAAPKAGKFKDEI 197
AcCoA-C-Actrans TIGR01930
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ...
 1-177 9.90e-66

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: 205.54  E-value: 9.90e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237   1 RYKGKLRDYSAVELGTAALKAAVEAIDIDPSTIQQVIFGNVLQSGVGQNPARQIAIKAGLPNTTPAMTINEVCGSGLKAI 80
Cdd:TIGR01930  11 KFGGSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLQAGEQQNIARQAALLAGLPESVPAYTVNRQCASGLQAV 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237  81 ILGKQLIQLGEAKVVAVGGVESMTNAPQLI---LKEGQDP----VESFMHDGLTDAFHYVPMGVTAENIAEKYHISREMQ 153
Cdd:TIGR01930  91 ILAAQLIRAGEADVVVAGGVESMSRVPYGVprsLRWGVKPgnaeLEDARLKDLTDANTGLPMGVTAENLAKKYGISREEQ 170

                         170       180
                  ....*....|....*....|....
gi 2264345237 154 DAFANQSQQKAHQATINGKFNNEI 177
Cdd:TIGR01930 171 DEYALRSHQRAAKAWEEGLFKDEI 194
PLN02644 PLN02644
acetyl-CoA C-acetyltransferase
 2-177 3.86e-61

acetyl-CoA C-acetyltransferase


Pssm-ID: 215347 [Multi-domain]  Cd Length: 394  Bit Score: 194.16  E-value: 3.86e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237   2 YKGKLRDYSAVELGTAALKAAVEAIDIDPSTIQQVIFGNVLQSGVGQNPARQIAIKAGLPNTTPAMTINEVCGSGLKAII 81
Cdd:PLN02644   16 FLGSLSSLSATELGSIAIQAALERAGVDPALVQEVFFGNVLSANLGQAPARQAALGAGLPPSTICTTVNKVCASGMKAVM 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237  82 LGKQLIQLGEAKVVAVGGVESMTNAPQLI------LKEGQDP-VESFMHDGLTDAFHYVPMGVTAENIAEKYHISREMQD 154
Cdd:PLN02644   96 LAAQSIQLGINDVVVAGGMESMSNAPKYLpearkgSRLGHDTvVDGMLKDGLWDVYNDFGMGVCAELCADQYSISREEQD 175

                         170       180
                  ....*....|....*....|...
gi 2264345237 155 AFANQSQQKAHQATINGKFNNEI 177
Cdd:PLN02644  176 AYAIQSYERAIAAQEAGAFAWEI 198
PRK05656 PRK05656
acetyl-CoA C-acetyltransferase;
2-177 1.06e-56

acetyl-CoA C-acetyltransferase;


Pssm-ID: 168156  Cd Length: 393  Bit Score: 182.78  E-value: 1.06e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237   2 YKGKLRDYSAVELGTAALKAAVEAIDIDPSTIQQVIFGNVLQSGVGQNPARQIAIKAGLPNTTPAMTINEVCGSGLKAII 81
Cdd:PRK05656   17 FQGSLANIPAVELGAAVIRRLLEQTGLDPAQVDEVILGQVLTAGAGQNPARQAAIKAGLPHSVPAMTLNKVCGSGLKALH 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237  82 LGKQLIQLGEAKVVAVGGVESMTNAPQLI------LKEGQDP-VESFMHDGLTDAFHYVPMGVTAENIAEKYHISREMQD 154
Cdd:PRK05656   97 LAAQAIRCGDAEVIIAGGQENMSLAPYVLpgartgLRMGHAQlVDSMITDGLWDAFNDYHMGITAENLVEKYGISREAQD 176

                         170       180
                  ....*....|....*....|...
gi 2264345237 155 AFANQSQQKAHQATINGKFNNEI 177
Cdd:PRK05656  177 AFAAASQQKAVAAIEAGRFDDEI 199
PRK08235 PRK08235
acetyl-CoA C-acetyltransferase;
1-177 5.12e-53

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181311 [Multi-domain]  Cd Length: 393  Bit Score: 173.36  E-value: 5.12e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237   1 RYKGKLRDYSAVELGTAALKAAVEAIDIDPSTIQQVIFGNVLQSGVGQNPARQIAIKAGLPNTTPAMTINEVCGSGLKAI 80
Cdd:PRK08235   16 KFGGSLKDVKATELGGIAIKEALERANVSAEDVEEVIMGTVLQGGQGQIPSRQAARAAGIPWEVQTETVNKVCASGLRAV 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237  81 ILGKQLIQLGEAKVVAVGGVESMTNAPQLI------LKEGQDPVESFM-HDGLTDAFHYVPMGVTAENIAEKYHISREMQ 153
Cdd:PRK08235   96 TLADQIIRAGDASVIVAGGMESMSNAPYILpgarwgYRMGDNEVIDLMvADGLTCAFSGVHMGVYGGEVAKELGISREAQ 175

                         170       180
                  ....*....|....*....|....
gi 2264345237 154 DAFANQSQQKAHQATINGKFNNEI 177
Cdd:PRK08235  176 DEWAYRSHQRAVSAHEEGRFEEEI 199
PRK09051 PRK09051
beta-ketothiolase BktB;
2-177 9.63e-50

beta-ketothiolase BktB;


Pssm-ID: 181625 [Multi-domain]  Cd Length: 394  Bit Score: 164.75  E-value: 9.63e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237   2 YKGKLRDYSAVELGTAALKAAVEAIDIDPSTIQQVIFGNVLQSGvgqnP-----ARQIAIKAGLPNTTPAMTINEVCGSG 76
Cdd:PRK09051   18 FGGSLKDVAPTDLGATVVREALARAGVDPDQVGHVVFGHVIPTE----PrdmylSRVAAINAGVPQETPAFNVNRLCGSG 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237  77 LKAIILGKQLIQLGEAKVVAVGGVESMTNAPQLIL------KEGQDPVESFMHDGLTDAFHYVPMGVTAENIAEKYHISR 150
Cdd:PRK09051   94 LQAIVSAAQAILLGDADVAIGGGAESMSRAPYLLPaarwgaRMGDAKLVDMMVGALHDPFGTIHMGVTAENVAAKYGISR 173

                         170       180
                  ....*....|....*....|....*..
gi 2264345237 151 EMQDAFANQSQQKAHQATINGKFNNEI 177
Cdd:PRK09051  174 EAQDALALESHRRAAAAIAAGYFKDQI 200
PRK06366 PRK06366
acetyl-CoA C-acetyltransferase;
11-177 1.83e-49

acetyl-CoA C-acetyltransferase;


Pssm-ID: 102340 [Multi-domain]  Cd Length: 388  Bit Score: 164.03  E-value: 1.83e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237  11 AVELGTAALKAAVEAIDIDPSTIQQVIFGNVLQSGVGQNPARQIAIKAGLPNTTPAMTINEVCGSGLKAIILGKQLIQLG 90
Cdd:PRK06366   26 APQLGGAAIKAVIDDAKLDPALVQEVIMGNVIQAGVGQNPAGQAAYHAGLPFGVTKYTVNVVCASGMLAVESAAREIMLG 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237  91 EAKVVAVGGVESMTNAPQL-----------ILKEGQDPVESFMHDGLTDAFHYVPMGVTAENIAEKYHISREMQDAFANQ 159
Cdd:PRK06366  106 ERDLVIAGGMENMSNAPFLlpsdlrwgpkhLLHKNYKIDDAMLVDGLIDAFYFEHMGVSAERTARKYGITREMADEYSVQ 185

                         170
                  ....*....|....*...
gi 2264345237 160 SQQKAHQATINGKFNNEI 177
Cdd:PRK06366  186 SYERAIRATESGEFRNEI 203
PRK06954 PRK06954
acetyl-CoA C-acetyltransferase;
2-177 3.97e-42

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180775 [Multi-domain]  Cd Length: 397  Bit Score: 145.03  E-value: 3.97e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237   2 YKGKLRDYSAVELGTAALKAAVEAIDIDPSTIQQVIFGNVLQSGVGQNPARQIAIKAGLPNTTPAMTINEVCGSGLKAII 81
Cdd:PRK06954   22 FQGEFASLTAPQLGAAAIAAAVERAGLKPEQIDEVVMGCVLPAGQGQAPARQAALGAGLPLSVGCTTVNKMCGSGMRAAM 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237  82 LGKQLIQLGEAKVVAVGGVESMTNAPQLILK--------EGQdPVESFMHDGLTDAFHY-VPMGVTAENIAEKYHISREM 152
Cdd:PRK06954  102 FAHDMLVAGSVDVIVAGGMESMTNAPYLLPKarggmrmgHGQ-VLDHMFLDGLEDAYDKgRLMGTFAEECAGEYGFTREA 180

                         170       180
                  ....*....|....*....|....*
gi 2264345237 153 QDAFANQSQQKAHQATINGKFNNEI 177
Cdd:PRK06954  181 QDAFAIESLARAKRANEDGSFAWEI 205
PRK06205 PRK06205
acetyl-CoA C-acetyltransferase;
1-177 8.90e-42

acetyl-CoA C-acetyltransferase;


Pssm-ID: 235741 [Multi-domain]  Cd Length: 404  Bit Score: 144.36  E-value: 8.90e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237   1 RYKGKLRDYSAVELGTAALKAAVEAIDIDPSTIQQVIFGNVLQSGvgQNPA--RQIAIKAGLPNTTPAMTINEVCGSGLK 78
Cdd:PRK06205   16 RFGGAFKDVPAEELAATVIRALVERTGIDPARIDDVIFGQGYPNG--EAPAigRVAALDAGLPVTVPGMQLDRRCGSGLQ 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237  79 AIILGKQLIQLGEAKVVAVGGVESMTNAP--QLILKEGQDPVESFMHDGLTDA-------FHYVPMGV--TAENIAEKYH 147
Cdd:PRK06205   94 AVITAAMQVQTGAADVVIAGGAESMSNVEfyTTDMRWGVRGGGVQLHDRLARGretaggrRFPVPGGMieTAENLRREYG 173

                         170       180       190
                  ....*....|....*....|....*....|
gi 2264345237 148 ISREMQDAFANQSQQKAHQATINGKFNNEI 177
Cdd:PRK06205  174 ISREEQDALAVRSHQRAVAAQEAGRFDDEI 203
PRK06633 PRK06633
acetyl-CoA C-acetyltransferase;
2-177 2.87e-41

acetyl-CoA C-acetyltransferase;


Pssm-ID: 168632 [Multi-domain]  Cd Length: 392  Bit Score: 142.86  E-value: 2.87e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237   2 YKGKLRDYSAVELGTAALKAAVEAIDIDPSTIQQVIFGNVLQSGVGQNPARQIAIKAGLPNTTPAMTINEVCGSGLKAII 81
Cdd:PRK06633   18 FMGSLSTTPAPMLAAHLIKDILQNSKIDPALVNEVILGQVITGGSGQNPARQTLIHAGIPKEVPGYTINKVCGSGLKSVA 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237  82 LGKQLIQLGEAKVVAVGGVESMTNAPQ-LILKEGQ-----DPVESFMHDGLTDAFHYVPMGVTAENIAEKYHISREMQDA 155
Cdd:PRK06633   98 LAANSIMTGDNEIVIAGGQENMSLGMHgSYIRAGAkfgdiKMVDLMQYDGLTDVFSGVFMGITAENISKQFNISRQEQDE 177

                         170       180
                  ....*....|....*....|..
gi 2264345237 156 FANQSQQKAHQATINGKFNNEI 177
Cdd:PRK06633  178 FALSSHKKAAKAQLAGIFKDEI 199
fadA PRK08947
3-ketoacyl-CoA thiolase; Reviewed
 27-177 1.26e-36

3-ketoacyl-CoA thiolase; Reviewed


Pssm-ID: 181592 [Multi-domain]  Cd Length: 387  Bit Score: 130.47  E-value: 1.26e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237  27 DIDPSTIQQVIFGNVLQSG-VGQNPARQIAIKAGLPNTTPAMTINEVCGSGLKAIILGKQLIQLGEAKVVAVGGVESMTN 105
Cdd:PRK08947   44 ALDPAEIDDIIWGCVQQTLeQGFNIARNAALLAGIPHSVPAVTVNRLCGSSMQALHDAARAIMTGDGDVFLIGGVEHMGH 123

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2264345237 106 APqliLKEGQDPvesfmHDGLTdafHYVP-----MGVTAENIAEKYHISREMQDAFANQSQQKAHQATINGKFNNEI 177
Cdd:PRK08947  124 VP---MNHGVDF-----HPGLS---KNVAkaagmMGLTAEMLGKMHGISREQQDAFAARSHQRAWAATQEGRFKNEI 189
PRK09050 PRK09050
beta-ketoadipyl CoA thiolase; Validated
 1-177 2.18e-36

beta-ketoadipyl CoA thiolase; Validated


Pssm-ID: 181624 [Multi-domain]  Cd Length: 401  Bit Score: 130.07  E-value: 2.18e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237   1 RYKGKLRDYSAVELGTAALKAAVEA-IDIDPSTIQQVIFGNVLQSGV-GQNPARQIAIKAGLPNTTPAMTINEVCGSGLK 78
Cdd:PRK09050   16 RYGGALSSVRADDLGAVPLKALMARnPGVDWEAVDDVIYGCANQAGEdNRNVARMSALLAGLPVSVPGTTINRLCGSGMD 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237  79 AIILGKQLIQLGEAKVVAVGGVESMTNAPQLILKEGqdpvESF-----MHDG---------LTDAFHYV-PMGVTAENIA 143
Cdd:PRK09050   96 AVGTAARAIKAGEAELMIAGGVESMSRAPFVMGKAD----SAFsrqaeIFDTtigwrfvnpLMKAQYGVdSMPETAENVA 171

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2264345237 144 EKYHISREMQDAFANQSQQKAHQATINGKFNNEI 177
Cdd:PRK09050  172 EDYNISRADQDAFALRSQQRAAAAQAAGFLAEEI 205
PRK07108 PRK07108
acetyl-CoA C-acyltransferase;
2-177 2.97e-36

acetyl-CoA C-acyltransferase;


Pssm-ID: 180843 [Multi-domain]  Cd Length: 392  Bit Score: 129.50  E-value: 2.97e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237   2 YKGKLRDYSAVELGTAALKAAVEAIDIDPSTIQQVIFGNVLQSG-VGQNPARQIAIKAGLPNTTPAMTINEVCGSGLKAI 80
Cdd:PRK07108   18 WRGAFNMTHGATLGGHVVQHAVERAKLDPAEVEDVIMGCANPEGaTGANIARQIALRAGLPVTVPGMTVNRFCSSGLQTI 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237  81 ILGKQLIQLGEAKVVAVGGVESMTNApqlilkegQDPVESFMHDGLTDAFH----YVPMGVTAENIAEKYHISREMQDAF 156
Cdd:PRK07108   98 ALAAQRVIAGEGDVFVAGGVESISCV--------QNEMNRHMLREGWLVEHkpeiYWSMLQTAENVAKRYGISKERQDEY 169

                         170       180
                  ....*....|....*....|.
gi 2264345237 157 ANQSQQKAHQATINGKFNNEI 177
Cdd:PRK07108  170 GVQSQQRAAAAQAAGRFDDEI 190
PRK09052 PRK09052
acetyl-CoA C-acyltransferase;
3-177 1.89e-34

acetyl-CoA C-acyltransferase;


Pssm-ID: 181626 [Multi-domain]  Cd Length: 399  Bit Score: 124.73  E-value: 1.89e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237   3 KGKLRDYSAVELGTAALKAAV-EAIDIDPSTIQQVIFGNVLQSG-VGQNPARQIAIKAGLPNTTPAMTINEVCGSGLKAI 80
Cdd:PRK09052   23 RGMFKNTRPDDLLAHVLRSAVaQVPGLDPKLIEDAIVGCAMPEAeQGLNVARIGALLAGLPNSVGGVTVNRFCASGLQAV 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237  81 ILGKQLIQLGEAKVVAVGGVESMTNAPQLILKEGQDPvESFMHDGlTDAFHYvPMGVTAENIAEKYHISREMQDAFANQS 160
Cdd:PRK09052  103 AMAADRIRVGEADVMIAAGVESMSMVPMMGNKPSMSP-AIFARDE-NVGIAY-GMGLTAEKVAEQWKVSREDQDAFALES 179

                         170
                  ....*....|....*..
gi 2264345237 161 QQKAHQATINGKFNNEI 177
Cdd:PRK09052  180 HQKAIAAQQAGEFKDEI 196
PRK07661 PRK07661
acetyl-CoA C-acetyltransferase;
3-177 3.03e-34

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181072 [Multi-domain]  Cd Length: 391  Bit Score: 124.09  E-value: 3.03e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237   3 KGKLRDYSAVELGTAALKAAVEAIDIDPSTIQQVIFGNVL-QSGVGQNPARQIAIKAGLPNTTPAMTINEVCGSGLKAII 81
Cdd:PRK07661   19 KGSLKTVRPDDLGALVVKETLKRAGNYEGPIDDLIIGCAMpEAEQGLNMARNIGALAGLPYTVPAITINRYCSSGLQSIA 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237  82 LGKQLIQLGEAKVVAVGGVESMTNAPQL--ILKEGQDPVEsfmhdglTDAFHYVPMGVTAENIAEKYHISREMQDAFANQ 159
Cdd:PRK07661   99 YGAERIMLGHSEAVIAGGAESMSLVPMMghVVRPNPRLVE-------AAPEYYMGMGHTAEQVAVKYGISREDQDAFAVR 171

                         170
                  ....*....|....*...
gi 2264345237 160 SQQKAHQATINGKFNNEI 177
Cdd:PRK07661  172 SHQRAAKALAEGKFADEI 189
PLN02287 PLN02287
3-ketoacyl-CoA thiolase
 3-177 1.22e-33

3-ketoacyl-CoA thiolase


Pssm-ID: 215161 [Multi-domain]  Cd Length: 452  Bit Score: 123.34  E-value: 1.22e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237   3 KGKLRDYSAVELGTAALKAAVEAIDIDPSTIQQVIFGNVLQSGVGQ-NPARQIAIKAGLPNTTPAMTINEVCGSGLKAII 81
Cdd:PLN02287   63 RGGFKDTYPDDLLAPVLKAVVEKTGLNPSEVGDIVVGTVLAPGSQRaNECRMAAFYAGFPETVPVRTVNRQCSSGLQAVA 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237  82 LGKQLIQLGEAKVVAVGGVESMTNAPqlILKEGQDP--VESF--MHDGLtdafhyVPMGVTAENIAEKYHISREMQDAFA 157
Cdd:PLN02287  143 DVAAAIKAGFYDIGIGAGVESMTTNP--MAWEGGVNprVESFsqAQDCL------LPMGITSENVAERFGVTREEQDQAA 214

                         170       180
                  ....*....|....*....|
gi 2264345237 158 NQSQQKAHQATINGKFNNEI 177
Cdd:PLN02287  215 VESHRKAAAATASGKFKDEI 234
PRK08242 PRK08242
acetyl-CoA C-acetyltransferase;
1-177 4.23e-33

acetyl-CoA C-acetyltransferase;


Pssm-ID: 236197 [Multi-domain]  Cd Length: 402  Bit Score: 121.14  E-value: 4.23e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237   1 RYKGK----LRDYSAVELGTAALKAAVEAIDIDPSTIQQVIFGNVLQSG-VGQNPARQIAIKAGLPNTTPAMTINEVCGS 75
Cdd:PRK08242   14 RGKGKkdgsLHEVKPVRLAAGLLEALRDRNGLDTAAVDDVVLGCVTPVGdQGADIARTAVLAAGLPETVPGVQINRFCAS 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237  76 GLKAIILGKQLIQLGEAKVVAVGGVESMTNAPQlilkeGQDPVESFMHDGLTDAFHYVPMGVTAENIAEKYHISREMQDA 155
Cdd:PRK08242   94 GLEAVNLAAAKVRSGWDDLVIAGGVESMSRVPM-----GSDGGAWAMDPSTNFPTYFVPQGISADLIATKYGFSREDVDA 168

                         170       180
                  ....*....|....*....|..
gi 2264345237 156 FANQSQQKAHQATINGKFNNEI 177
Cdd:PRK08242  169 YAVESQQRAAAAWAEGYFAKSV 190
PRK07801 PRK07801
acetyl-CoA C-acetyltransferase;
1-177 1.78e-29

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181123 [Multi-domain]  Cd Length: 382  Bit Score: 111.34  E-value: 1.78e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237   1 RYKGKLRDYSAVELGTAALKAAVEAIDIDPSTIQQVIFGNVLQSGvGQ--NPARQIAIKAGLPNTTPAMTINEVCGSGLK 78
Cdd:PRK07801   16 KRKGGLAGVHPADLGAHVLKGLVDRTGIDPAAVDDVIFGCVDTIG-PQagNIARTSWLAAGLPEEVPGVTVDRQCGSSQQ 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237  79 AIILGKQLIQLGEAKVVAVGGVESMTnapqlilkegQDPVESFM----HDGLTDAFHYVPMGVT------------AENI 142
Cdd:PRK07801   95 AIHFAAQAVMSGTQDLVVAGGVQNMS----------QIPISSAMtageQLGFTSPFAESKGWLHrygdqevsqfrgAELI 164

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2264345237 143 AEKYHISREMQDAFANQSQQKAHQATINGKFNNEI 177
Cdd:PRK07801  165 AEKWGISREEMERFALESHRRAFAAIRAGRFDNEI 199
PRK06504 PRK06504
acetyl-CoA C-acetyltransferase;
1-177 5.83e-29

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180595 [Multi-domain]  Cd Length: 390  Bit Score: 109.82  E-value: 5.83e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237   1 RYKGKLRDYSAVELGTAALKAAVEAIDIDPSTIQQVIFGNVLQSG-VGQNPARQIAIKAGLPNTTPAMTINEVCGSGLKA 79
Cdd:PRK06504   16 RKGGRLAGWHPADLAAQVLDALVDRSGADPALIEDVIMGCVSQVGeQATNVARNAVLASKLPESVPGTSIDRQCGSSQQA 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237  80 IILGKQLIQLGEAKVVAVGGVESMTNAP-----QLILKEGqdpVESFMHDGLTDAFHYVP----MGvtAENIAEKYHISR 150
Cdd:PRK06504   96 LHFAAQAVMSGTMDIVIAAGVESMTRVPmgspsTLPAKNG---LGHYKSPGMEERYPGIQfsqfTG--AEMMAKKYGLSK 170

                         170       180
                  ....*....|....*....|....*..
gi 2264345237 151 EMQDAFANQSQQKAHQATINGKFNNEI 177
Cdd:PRK06504  171 DQLDEFALQSHQRAIAATQAGKFKAEI 197
PRK08131 PRK08131
3-oxoadipyl-CoA thiolase;
1-177 6.19e-27

3-oxoadipyl-CoA thiolase;


Pssm-ID: 181242 [Multi-domain]  Cd Length: 401  Bit Score: 104.86  E-value: 6.19e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237   1 RYKGKLRDYSAVELGTAALKAAVEAIDIDPSTIQQVIFGNVLQSGV-GQNPARQIAIKAGLPNTTPAMTINEVCGSGLKA 79
Cdd:PRK08131   16 RHAGALASVRPDDLAATVIRRLLEKSGFPGDDIEDVILGCTNQAGEdSRNVARNALLLAGLPVTVPGQTVNRLCASGLAA 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237  80 IILGKQLIQLGEAKVVAVGGVESMTNAPqLILKEGQDPVE------------SFMHDGLTDAFHYVPMGVTAENIAEKYH 147
Cdd:PRK08131   96 VIDAARAITCGEGDLYLAGGVESMSRAP-FVMGKAESAFSrdakvfdttigaRFPNPKIVAQYGNDSMPETGDNVAAEFG 174

                         170       180       190
                  ....*....|....*....|....*....|
gi 2264345237 148 ISREMQDAFANQSQQKAHQATINGKFNNEI 177
Cdd:PRK08131  175 ISREDADRFAAQSQAKYQAAKEEGFFADEI 204
PRK08170 PRK08170
acetyl-CoA C-acetyltransferase;
9-174 9.79e-26

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181265 [Multi-domain]  Cd Length: 426  Bit Score: 101.63  E-value: 9.79e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237   9 YSAVELGTAALKAAVEAIDIDPSTIQQVIFGNVLQSGVGQNPARQIAIKAGLPNTTPAMTINEVCGSGLKAIILGKQLIQ 88
Cdd:PRK08170   25 FSASDLAVAAGRALLNRQPFAPDDLDEVILGCAMPSPDEANIARVVALRLGCGEKVPAWTVQRNCASGMQALDSAAANIA 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237  89 LGEAKVVAVGGVESMTNAPQLILKEGQD---------------------------PVESFMHdGLTDAFHYVPMGVTAEN 141
Cdd:PRK08170  105 LGRADLVLAGGVEAMSHAPLLFSEKMVRwlagwyaaksigqklaalgklrpsylaPVIGLLR-GLTDPVVGLNMGQTAEV 183

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2264345237 142 IAEKYHISREMQDAFANQSQQKAHQATINGKFN 174
Cdd:PRK08170  184 LAHRFGITREQMDAYAARSHQRLAAAQAEGRLK 216
fadI PRK08963
3-ketoacyl-CoA thiolase; Reviewed
 6-177 2.02e-25

3-ketoacyl-CoA thiolase; Reviewed


Pssm-ID: 181597 [Multi-domain]  Cd Length: 428  Bit Score: 100.83  E-value: 2.02e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237   6 LRDYSAVELGTAALKAAVEAIDIDPSTIQQVIFGNVLQSGVGQNPARQIAIKAGLPNTTPAMTINEVCGSGLKAIILGKQ 85
Cdd:PRK08963   24 FHGIPAVDLGKMVVGELLARSEIDPELIEQLVFGQVVQMPEAPNIAREIVLGTGMNVHTDAYSVSRACATSFQAVANVAE 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237  86 LIQLGEAKVVAVGGVESMTNAPQLILKegqdPVESFMHD-----------------GLTDAFHYVP----------MGVT 138
Cdd:PRK08963  104 SIMAGTIDIGIAGGADSSSVLPIGVSK----KLARALVDlnkartlgqrlklfsrlRLRDLLPVPPavaeystglrMGDT 179

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2264345237 139 AENIAEKYHISREMQDAFANQSQQKAHQATINGKFNNEI 177
Cdd:PRK08963  180 AEQMAKTYGISREEQDALAHRSHQLAAQAWAEGKLDDEV 218
PRK06690 PRK06690
acetyl-CoA C-acyltransferase;
4-177 1.70e-24

acetyl-CoA C-acyltransferase;


Pssm-ID: 180659 [Multi-domain]  Cd Length: 361  Bit Score: 97.53  E-value: 1.70e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237   4 GKLRDYSAVELGTAALKAAVEAIdidPSTIQQVIFGNVLqsGVGQNPARQIAIKAGLPNTTPAMTINEVCGSGLKAIILG 83
Cdd:PRK06690   18 GMLKDYEVQQLAAPLLTFLSKGM---EREIDDVILGNVV--GPGGNVARLSALEAGLGLHIPGVTIDRQCGAGLEAIRTA 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237  84 KQLIQLGEAKVVAVGGVESMTNAPqliLKEGQdpveSFMHDGLTDAfhyvPMGVTAENIAEKYHISREMQDAFANQSQQK 163
Cdd:PRK06690   93 CHFIQGGAGKCYIAGGVESTSTSP---FQNRA----RFSPETIGDP----DMGVAAEYVAERYNITREMQDEYACLSYKR 161

                         170
                  ....*....|....
gi 2264345237 164 AHQATINGKFNNEI 177
Cdd:PRK06690  162 TLQALEKGYIHEEI 175
PRK07851 PRK07851
acetyl-CoA C-acetyltransferase;
2-177 3.40e-23

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181146 [Multi-domain]  Cd Length: 406  Bit Score: 94.30  E-value: 3.40e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237   2 YKGKLRDYSAVELGTAALKAAVEAI-DIDPSTIQQVIFGNVLQSG-VGQNPARQIAIKAGLPnTTPAMTINEVCGSGLKA 79
Cdd:PRK07851   18 FKGSLKDMRPDDLAAQMVRAALDKVpALDPTDIDDLMLGCGLPGGeQGFNMARVVAVLLGYD-FLPGTTVNRYCSSSLQT 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237  80 IILGKQLIQLGEAKVVAVGGVES-----MTNAPQLilKEGQDPV-------ESFMHDGLTDAFH-----------YVPMG 136
Cdd:PRK07851   97 TRMAFHAIKAGEGDVFISAGVETvsrfaKGNSDSL--PDTKNPLfaeaqarTAARAEGGAEAWHdpredgllpdvYIAMG 174

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2264345237 137 VTAENIAEKYHISREMQDAFANQSQQKAHQATINGKFNNEI 177
Cdd:PRK07851  175 QTAENVAQLTGISREEQDEWGVRSQNRAEEAIANGFFEREI 215
PRK07850 PRK07850
steroid 3-ketoacyl-CoA thiolase;
1-177 9.17e-23

steroid 3-ketoacyl-CoA thiolase;


Pssm-ID: 181145 [Multi-domain]  Cd Length: 387  Bit Score: 93.25  E-value: 9.17e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237   1 RYKGKLRDYSAVELGTAALKAAVEAIDIDPSTIQQVIFGNVLQSGV-GQNPARQIAIKAGLPNTTPAMTINEVCGSGLKA 79
Cdd:PRK07850   16 KRNGWLSGLHAAELLGAVQRAVLDRAGIDPGDVEQVIGGCVTQAGEqSNNITRTAWLHAGLPYHVGATTIDCQCGSAQQA 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237  80 IILGKQLIQLGEAKVVAVGGVESMTNAPqLILKEGQDP----VESFMHDgLTDAFhyvpmgVTAENIAEKYHISREMQDA 155
Cdd:PRK07850   96 NHLVAGLIAAGAIDVGIACGVEAMSRVP-LGANAGPGRglprPDSWDID-MPNQF------EAAERIAKRRGITREDVDA 167

                         170       180
                  ....*....|....*....|..
gi 2264345237 156 FANQSQQKAHQATINGKFNNEI 177
Cdd:PRK07850  168 FGLRSQRRAAQAWAEGRFDREI 189
PRK06445 PRK06445
acetyl-CoA C-acetyltransferase;
13-177 9.25e-23

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180563 [Multi-domain]  Cd Length: 394  Bit Score: 93.25  E-value: 9.25e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237  13 ELGTAALKAAVEAIDIDPSTIQQVIFGNVLQsgVGQN---PARQIAIKAGLPNTTPAMTINEVCGSGLKAIILGKQLIQL 89
Cdd:PRK06445   34 ELAAMLINRLIEKTGIKPEEIDDIITGCALQ--VGENwlyGGRHPIFLARLPYNIPAMAVDRQCASSLTTVSIGAMEIAT 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237  90 GEAKVVAVGGVESMTNAPqliLKEGQ--DPVESFMHDglTDAFHY-----VPMGVTAENIAEKYHISREMQDAFANQSQQ 162
Cdd:PRK06445  112 GMADIVIAGGVEHMTRTP---MGDNPhiEPNPKLLTD--PKYIEYdlttgYVMGLTAEKLAEEAGIKREEMDRWSLRSHQ 186

                         170
                  ....*....|....*
gi 2264345237 163 KAHQATINGKFNNEI 177
Cdd:PRK06445  187 LAAKAIQEGYFKDEI 201
nondecarbox_cond_enzymes cd00826
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ...
 7-177 1.01e-22

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: 93.33  E-value: 1.01e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237   7 RDYS--AVELGTAALKAAVEAIDIDPSTIQQVIFGNVLQSGVGQNPARQIAIKAGLPNTTPAMTINEVCGSGLKAIILGK 84
Cdd:cd00826    17 ADANdlAHEAGAKAIAAALEPAGVAAGAVEEACLGQVLGAGEGQNCAQQAAMHAGGLQEAPAIGMNNLCGSGLRALALAM 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237  85 QLIQLGEAKVVAVGGVESMTnapqlilkegqdpvesfmhdgltdafhyvpmgVTAENIAEKYHI--------SREMQDAF 156
Cdd:cd00826    97 QLIAGGDANCILAGGFEKME--------------------------------TSAENNAKEKHIdvlinkygMRACPDAF 144

                         170       180
                  ....*....|....*....|.
gi 2264345237 157 ANQSQQKAHQATINGKFNNEI 177
Cdd:cd00826   145 ALAGQAGAEAAEKDGRFKDEF 165
SCP-x_thiolase cd00829
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ...
 4-107 1.18e-16

Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; SCP-2 has multiple roles in intracellular lipid circulation and metabolism. The N-terminal presequence in the SCP-x isoform represents a peroxisomal 3-ketacyl-Coa thiolase specific for branched-chain acyl CoAs, which is proteolytically cleaved from the sterol carrier protein.


Pssm-ID: 238425 [Multi-domain]  Cd Length: 375  Bit Score: 76.15  E-value: 1.18e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237   4 GKLRDYSAVELGTAALKAAVEAIDIDPSTIQQVIFGNVLQSGVGQNPARQIAIKAGLPNTtPAMTINEVCGSGLKAIILG 83
Cdd:cd00829     9 GRRSDRSPLELAAEAARAALDDAGLEPADIDAVVVGNAAGGRFQSFPGALIAEYLGLLGK-PATRVEAAGASGSAAVRAA 87

                          90       100
                  ....*....|....*....|....
gi 2264345237  84 KQLIQLGEAKVVAVGGVESMTNAP 107
Cdd:cd00829    88 AAAIASGLADVVLVVGAEKMSDVP 111
cond_enzymes cd00327
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ...
 16-102 5.44e-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: 67.47  E-value: 5.44e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237  16 TAALKAAVEAID---IDPSTIQQVIFGNVLQSGVGQNPARQIAIKAGLPNTtPAMTINEVCGSGLKAIILGKQLIQLGEA 92
Cdd:cd00327     9 ELGFEAAEQAIAdagLSKGPIVGVIVGTTGGSGEFSGAAGQLAYHLGISGG-PAYSVNQACATGLTALALAVQQVQNGKA 87

                          90
                  ....*....|
gi 2264345237  93 KVVAVGGVES 102
Cdd:cd00327    88 DIVLAGGSEE 97
PRK09268 PRK09268
acetyl-CoA C-acetyltransferase;
10-174 1.80e-11

acetyl-CoA C-acetyltransferase;


Pssm-ID: 236440 [Multi-domain]  Cd Length: 427  Bit Score: 61.45  E-value: 1.80e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237  10 SAVELGTAALKAAVEAIDIDPSTIQQVIFGNVLQSGVGQNPARQIAIKAGLPNTTPAMTINEVCGSGLKAIILGKQLIQL 89
Cdd:PRK09268   30 SNQDMLTAALDGLVDRFGLQGERLGEVVAGAVLKHSRDFNLTRECVLGSALSPYTPAYDLQQACGTGLEAAILVANKIAL 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237  90 GEAKVVAVGGVESMTNAP--------QLIL-----KEGQDPVESFmhdGLTDAFHYVP-------------MGVTAENIA 143
Cdd:PRK09268  110 GQIDSGIAGGVDTTSDAPiavneglrKILLelnraKTTGDRLKAL---GKLRPKHLAPeiprngeprtglsMGEHAAITA 186

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2264345237 144 EKYHISREMQDAFANQSQQKAHQATINGKFN 174
Cdd:PRK09268  187 KEWGISREAQDELAAASHQNLAAAYDRGFFD 217
PRK06064 PRK06064
thiolase domain-containing protein;
4-107 1.57e-10

thiolase domain-containing protein;


Pssm-ID: 235688 [Multi-domain]  Cd Length: 389  Bit Score: 58.75  E-value: 1.57e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237   4 GKLRDYSAVELGTAALKAAVEAIDIDPSTIQQVIFGNVLQSG-VGQ-NPARQIAIKAGLPNTtPAMTINEVCGSGLKAII 81
Cdd:PRK06064   15 GELWDVSLRDLAVEAGLEALEDAGIDGKDIDAMYVGNMSAGLfVSQeHIAALIADYAGLAPI-PATRVEAACASGGAALR 93

                          90       100
                  ....*....|....*....|....*.
gi 2264345237  82 LGKQLIQLGEAKVVAVGGVESMTNAP 107
Cdd:PRK06064   94 QAYLAVASGEADVVLAAGVEKMTDVP 119
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
 50-105 6.32e-09

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: 54.08  E-value: 6.32e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2264345237  50 PARQIAIKAGLpnTTPAMTINEVCGSGLKAIILGKQLIQLGEAKVVAVGGVESMTN 105
Cdd:cd00834   140 AAGQVAIRLGL--RGPNYTVSTACASGAHAIGDAARLIRLGRADVVIAGGAEALIT 193
FabH COG0332
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl- ...
 8-104 3.51e-08

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


Pssm-ID: 440101 [Multi-domain]  Cd Length: 323  Bit Score: 51.65  E-value: 3.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237   8 DYSAVELGTAALKAAVEAIDIDPSTIQQVIFGNVLQSGVGQNPARQIAIKAGLPNtTPAMTINEVCGSGLKAIILGKQLI 87
Cdd:COG0332    48 DETTSDLAVEAARKALEAAGIDPEDIDLIIVATVTPDYLFPSTACLVQHKLGAKN-AAAFDINAACSGFVYALSVAAALI 126

                          90
                  ....*....|....*..
gi 2264345237  88 QLGEAKVVAVGGVESMT 104
Cdd:COG0332   127 RSGQAKNVLVVGAETLS 143
FabB COG0304
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...
 15-105 8.89e-08

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: 50.48  E-value: 8.89e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237  15 GTAALKAAVEAID------IDPSTIQQVIFGNvlqsgvgqnPARQIAIKAGLPNttPAMTINEVCGSGLKAIILGKQLIQ 88
Cdd:COG0304   108 GLDTLEEAYRALLekgprrVSPFFVPMMMPNM---------AAGHVSIRFGLKG--PNYTVSTACASGAHAIGEAYRLIR 176

                          90
                  ....*....|....*..
gi 2264345237  89 LGEAKVVAVGGVESMTN 105
Cdd:COG0304   177 RGRADVMIAGGAEAAIT 193
PRK12578 PRK12578
thiolase domain-containing protein;
4-104 2.83e-06

thiolase domain-containing protein;


Pssm-ID: 183606 [Multi-domain]  Cd Length: 385  Bit Score: 46.38  E-value: 2.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237   4 GKLRDYSAVELGTAALKAAVEAIDIDPSTIQQVIFGNVLQSGVGQNPARQIAIKAGLPNTTPaMTINEVCGSGLKAIILG 83
Cdd:PRK12578   14 GRRDDVSVQELAWESIKEALNDAGVSQTDIELVVVGSTAYRGIELYPAPIVAEYSGLTGKVP-LRVEAMCATGLAASLTA 92

                          90       100
                  ....*....|....*....|.
gi 2264345237  84 KQLIQLGEAKVVAVGGVESMT 104
Cdd:PRK12578   93 YTAVASGLVDMAIAVGVDKMT 113
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
 34-105 1.47e-05

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: 43.78  E-value: 1.47e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2264345237  34 QQVIFGNVLQSGVGQN--PARqIAIKAGLpnTTPAMTINEVCGSGLKAIILGKQLIQLGEAKVVAVGGVESMTN 105
Cdd:pfam00109 135 GGPRRGSPFAVGTMPSviAGR-ISYFLGL--RGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLT 205
PRK09185 PRK09185
beta-ketoacyl-ACP synthase;
49-102 4.40e-05

beta-ketoacyl-ACP synthase;


Pssm-ID: 236398 [Multi-domain]  Cd Length: 392  Bit Score: 42.52  E-value: 4.40e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2264345237  49 NPARQIAIKAGLpnTTPAMTINEVCGSGLKAIILGKQLIQLGEAKVVAVGGVES 102
Cdd:PRK09185  138 SLADFLRAYLGL--SGPAYTISTACSSSAKVFASARRLLEAGLCDAAIVGGVDS 189
PRK07516 PRK07516
thiolase domain-containing protein;
4-107 2.19e-04

thiolase domain-containing protein;


Pssm-ID: 181013 [Multi-domain]  Cd Length: 389  Bit Score: 40.70  E-value: 2.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237   4 GKLRDYSAVELGTAALKAAVEAIDIDPSTIQQVIFGnVLQSG-VGQNPARQIAIKA--GLPNTtPAMTINEVCGSGLKAI 80
Cdd:PRK07516   15 GKLDAETLESLIVRVAREALAHAGIAAGDVDGIFLG-HFNAGfSPQDFPASLVLQAdpALRFK-PATRVENACATGSAAV 92

                          90       100
                  ....*....|....*....|....*..
gi 2264345237  81 ILGKQLIQLGEAKVVAVGGVESMTNAP 107
Cdd:PRK07516   93 YAALDAIEAGRARIVLVVGAEKMTATP 119
init_cond_enzymes cd00827
"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ...
 8-99 2.86e-04

"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, including beta-ketoacyl [ACP] synthase, type III and polyketide synthases, type III, which include chalcone synthase and related enzymes. They are characterized by the utlization of CoA substrate primers, as well as the nature of their active site residues.


Pssm-ID: 238423 [Multi-domain]  Cd Length: 324  Bit Score: 40.11  E-value: 2.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237   8 DYSAVELGTAALKAAVEAIDIDPSTIQQVIFGNVLQSGVGQNPARQIAIKAGLPNTTPAMTINeVCGSGLKAIILGKQLI 87
Cdd:cd00827    45 DEDVPTMAVEAARRALERAGIDPDDIGLLIVATESPIDKGKSAATYLAELLGLTNAEAFDLKQ-ACYGGTAALQLAANLV 123

                          90
                  ....*....|...
gi 2264345237  88 QLGE-AKVVAVGG 99
Cdd:cd00827   124 ESGPwRYALVVAS 136
elong_cond_enzymes cd00828
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ...
 65-150 3.83e-04

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


Pssm-ID: 238424 [Multi-domain]  Cd Length: 407  Bit Score: 40.11  E-value: 3.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237  65 PAMTINEVCGSGLKAIILGKQLIQLGEAKVVAVGGVESMTnapqlilkegqdpVESfmhdgltdAFHYVPMGVTAENIAE 144
Cdd:cd00828   154 PIKTPVGACATALEALDLAVEAIRSGKADIVVVGGVEDPL-------------EEG--------LSGFANMGALSTAEEE 212


                  ....*.
gi 2264345237 145 KYHISR 150
Cdd:cd00828   213 PEEMSR 218
PRK07314 PRK07314
beta-ketoacyl-ACP synthase II;
18-102 1.30e-03

beta-ketoacyl-ACP synthase II;


Pssm-ID: 235987 [Multi-domain]  Cd Length: 411  Bit Score: 38.23  E-value: 1.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237  18 ALKAAVEAID---IDPSTIQQVIFGNVLQSGVG--------------QNPAR----------------QIAIKAGL--PN 62
Cdd:PRK07314   76 GIAAAKQAVEdagLEITEENADRIGVIIGSGIGgletieeqhitlleKGPRRvspffvpmaiinmaagHVSIRYGAkgPN 155

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2264345237  63 TTpamtINEVCGSGLKAIILGKQLIQLGEAKVVAVGGVES 102
Cdd:PRK07314  156 HS----IVTACATGAHAIGDAARLIAYGDADVMVAGGAEA 191
decarbox_cond_enzymes cd00825
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ...
 53-120 1.39e-03

decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new carbon-carbon bond by a decarboxylating Claisen-like condensation reaction. Members are involved in the synthesis of fatty acids and polyketides, a diverse group of natural products. Both pathways are an iterative series of additions of small carbon units, usually acetate, to a nascent acyl group. There are 2 classes of decarboxylating condensing enzymes, which can be distinguished by sequence similarity, type of active site residues and type of primer units (acetyl CoA or acyl carrier protein (ACP) linked units).


Pssm-ID: 238421 [Multi-domain]  Cd Length: 332  Bit Score: 38.39  E-value: 1.39e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2264345237  53 QIAIKAGLpnTTPAMTINEVCGSGLKAIILGKQLIQLGEAKVVAVGGVESMTnAPQLILKEGQDPVES 120
Cdd:cd00825    78 QIATPLGI--HGPAYDVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEELA-APMDCEFDAMGALST 142
KAS_III cd00830
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty ...
 10-105 2.06e-03

Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty acid synthase systems. It is found in bacteria and plants. Elongation of fatty acids in the type II systems occurs by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP. KASIII initiates this process by specifically using acetyl-CoA over acyl-CoA.


Pssm-ID: 238426 [Multi-domain]  Cd Length: 320  Bit Score: 37.52  E-value: 2.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237  10 SAVELGTAALKAAVEAIDIDPSTIQQVIFGNVlqSGVGQNPAR--QIAIKAGLPNtTPAMTINEVCGSGLKAIILGKQLI 87
Cdd:cd00830    49 TTSDLAVEAAKKALEDAGIDADDIDLIIVATS--TPDYLFPATacLVQARLGAKN-AAAFDINAACSGFLYGLSTAAGLI 125

                          90
                  ....*....|....*...
gi 2264345237  88 QLGEAKVVAVGGVESMTN 105
Cdd:cd00830   126 RSGGAKNVLVVGAETLSR 143
PRK09352 PRK09352
beta-ketoacyl-ACP synthase 3;
10-104 5.74e-03

beta-ketoacyl-ACP synthase 3;


Pssm-ID: 236475 [Multi-domain]  Cd Length: 319  Bit Score: 36.20  E-value: 5.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264345237  10 SAVELGTAALKAAVEAIDIDPSTIQQVIFGNVLQSGVGQNPARQIAIKAGLPNTtPAMTINEVCgSG-LKAIILGKQLIQ 88
Cdd:PRK09352   51 TTSDLATEAAKKALEAAGIDPEDIDLIIVATTTPDYAFPSTACLVQARLGAKNA-AAFDLSAAC-SGfVYALSTADQFIR 128

                          90
                  ....*....|....*.
gi 2264345237  89 LGEAKVVAVGGVESMT 104
Cdd:PRK09352  129 SGAYKNVLVIGAEKLS 144
 
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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