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Conserved domains on  [gi|568963838|ref|XP_006512179|]
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3-ketoacyl-CoA thiolase B, peroxisomal isoform X3 [Mus musculus]

Protein Classification

3-ketoacyl-CoA thiolase( domain architecture ID 1004030)

3-ketoacyl-CoA thiolase is responsible for the thiolytic cleavage of straight chain 3-keto fatty acyl-CoAs (3-oxoacyl-CoAs)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02287 super family cl30635
3-ketoacyl-CoA thiolase
 1-209 1.87e-86

3-ketoacyl-CoA thiolase


The actual alignment was detected with superfamily member PLN02287:

Pssm-ID: 215161 [Multi-domain]  Cd Length: 452  Bit Score: 263.55  E-value: 1.87e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963838   1 MHRLQVVLGHLAGRPESSSALQAAPCSAGFLQASAS------DVVVVHGRRTPIGRASRGCFKDTTPDELLSAVLTAVLQ 74
Cdd:PLN02287   5 INRQRVLLRHLRPSSSEPSSLSASACAAGDSAAYHRttafgdDVVIVAAYRTPICKAKRGGFKDTYPDDLLAPVLKAVVE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963838  75 DVKLKPEQLGDISVGNVLQPGAG-AIMARIAQFLSGIPETVPLSTVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESM 153
Cdd:PLN02287  85 KTGLNPSEVGDIVVGTVLAPGSQrANECRMAAFYAGFPETVPVRTVNRQCSSGLQAVADVAAAIKAGFYDIGIGAGVESM 164

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568963838 154 TLSQRGNHGNISSRLLENEKARDCLIPMGITSENVAERFGVSRQKQDAFALASQQK 209
Cdd:PLN02287 165 TTNPMAWEGGVNPRVESFSQAQDCLLPMGITSENVAERFGVTREEQDQAAVESHRK 220
 
Name Accession Description Interval E-value
PLN02287 PLN02287
3-ketoacyl-CoA thiolase
 1-209 1.87e-86

3-ketoacyl-CoA thiolase


Pssm-ID: 215161 [Multi-domain]  Cd Length: 452  Bit Score: 263.55  E-value: 1.87e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963838   1 MHRLQVVLGHLAGRPESSSALQAAPCSAGFLQASAS------DVVVVHGRRTPIGRASRGCFKDTTPDELLSAVLTAVLQ 74
Cdd:PLN02287   5 INRQRVLLRHLRPSSSEPSSLSASACAAGDSAAYHRttafgdDVVIVAAYRTPICKAKRGGFKDTYPDDLLAPVLKAVVE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963838  75 DVKLKPEQLGDISVGNVLQPGAG-AIMARIAQFLSGIPETVPLSTVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESM 153
Cdd:PLN02287  85 KTGLNPSEVGDIVVGTVLAPGSQrANECRMAAFYAGFPETVPVRTVNRQCSSGLQAVADVAAAIKAGFYDIGIGAGVESM 164

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568963838 154 TLSQRGNHGNISSRLLENEKARDCLIPMGITSENVAERFGVSRQKQDAFALASQQK 209
Cdd:PLN02287 165 TTNPMAWEGGVNPRVESFSQAQDCLLPMGITSENVAERFGVTREEQDQAAVESHRK 220
Thiolase_N pfam00108
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
 38-209 1.10e-68

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: 211.78  E-value: 1.10e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963838   38 VVVVHGRRTPIGRaSRGCFKDTTPDELLSAVLTAVLQDVKLKPEQLGDISVGNVLQPGAGAIMARIAQFLSGIPETVPLS 117
Cdd:pfam00108   1 VVIVSAARTPFGS-FGGSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQAGEGQNPARQAALKAGIPDSAPAV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963838  118 TVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMTLSQRG-NHGNISSRLLENEKARDCLIP-----------MGITS 185
Cdd:pfam00108  80 TINKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYAlPTDARSGLKHGDEKKHDLLIPdgltdafngyhMGLTA 159

                         170       180
                  ....*....|....*....|....
gi 568963838  186 ENVAERFGVSRQKQDAFALASQQK 209
Cdd:pfam00108 160 ENVAKKYGISREEQDAFAVKSHQK 183
thiolase cd00751
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ...
 39-209 2.83e-66

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: 209.64  E-value: 2.83e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963838  39 VVVHGRRTPIGRAsRGCFKDTTPDELLSAVLTAVLQDVKLKPEQLGDISVGNVLQPGAGAIMARIAQFLSGIPETVPLST 118
Cdd:cd00751    1 VIVSAVRTPIGRF-GGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGEGQNPARQAALLAGLPESVPATT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963838 119 VNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMTLS----------QRGNHGNISSRLLENEKARDCLIPMGITSENV 188
Cdd:cd00751   80 VNRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRApyllpkarrgGRLGLNTLDGMLDDGLTDPFTGLSMGITAENV 159

                        170       180
                 ....*....|....*....|.
gi 568963838 189 AERFGVSRQKQDAFALASQQK 209
Cdd:cd00751  160 AEKYGISREEQDEFALRSHQR 180
PaaJ COG0183
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ...
 36-209 3.96e-58

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: 188.74  E-value: 3.96e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963838  36 SDVVVVHGRRTPIGRAsRGCFKDTTPDELLSAVLTAVLQDVKLKPEQLGDISVGNVLQPGAGAIMARIAQFLSGIPETVP 115
Cdd:COG0183    2 REVVIVDAVRTPFGRF-GGALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQAGQGQNPARQAALLAGLPESVP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963838 116 LSTVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMTLS----------QRGNHGNISSRLLENEKARDCLIPMGITS 185
Cdd:COG0183   81 AVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRApmllpkarwgYRMNAKLVDPMINPGLTDPYTGLSMGETA 160

                        170       180
                 ....*....|....*....|....
gi 568963838 186 ENVAERFGVSRQKQDAFALASQQK 209
Cdd:COG0183  161 ENVAERYGISREEQDAFALRSHQR 184
AcCoA-C-Actrans TIGR01930
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ...
 40-209 9.46e-53

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: 174.72  E-value: 9.46e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963838   40 VVHGRRTPIGRAsRGCFKDTTPDELLSAVLTAVLQDVKLKPEQLGDISVGNVLQPGAGAIMARIAQFLSGIPETVPLSTV 119
Cdd:TIGR01930   1 IVAAARTPIGKF-GGSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLQAGEQQNIARQAALLAGLPESVPAYTV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963838  120 NRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMT----LSQRGNHGNISSRLLENEKAR-------DCLIPMGITSENV 188
Cdd:TIGR01930  80 NRQCASGLQAVILAAQLIRAGEADVVVAGGVESMSrvpyGVPRSLRWGVKPGNAELEDARlkdltdaNTGLPMGVTAENL 159

                         170       180
                  ....*....|....*....|.
gi 568963838  189 AERFGVSRQKQDAFALASQQK 209
Cdd:TIGR01930 160 AKKYGISREEQDEYALRSHQR 180
 
Name Accession Description Interval E-value
PLN02287 PLN02287
3-ketoacyl-CoA thiolase
 1-209 1.87e-86

3-ketoacyl-CoA thiolase


Pssm-ID: 215161 [Multi-domain]  Cd Length: 452  Bit Score: 263.55  E-value: 1.87e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963838   1 MHRLQVVLGHLAGRPESSSALQAAPCSAGFLQASAS------DVVVVHGRRTPIGRASRGCFKDTTPDELLSAVLTAVLQ 74
Cdd:PLN02287   5 INRQRVLLRHLRPSSSEPSSLSASACAAGDSAAYHRttafgdDVVIVAAYRTPICKAKRGGFKDTYPDDLLAPVLKAVVE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963838  75 DVKLKPEQLGDISVGNVLQPGAG-AIMARIAQFLSGIPETVPLSTVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESM 153
Cdd:PLN02287  85 KTGLNPSEVGDIVVGTVLAPGSQrANECRMAAFYAGFPETVPVRTVNRQCSSGLQAVADVAAAIKAGFYDIGIGAGVESM 164

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568963838 154 TLSQRGNHGNISSRLLENEKARDCLIPMGITSENVAERFGVSRQKQDAFALASQQK 209
Cdd:PLN02287 165 TTNPMAWEGGVNPRVESFSQAQDCLLPMGITSENVAERFGVTREEQDQAAVESHRK 220
Thiolase_N pfam00108
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
 38-209 1.10e-68

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: 211.78  E-value: 1.10e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963838   38 VVVVHGRRTPIGRaSRGCFKDTTPDELLSAVLTAVLQDVKLKPEQLGDISVGNVLQPGAGAIMARIAQFLSGIPETVPLS 117
Cdd:pfam00108   1 VVIVSAARTPFGS-FGGSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQAGEGQNPARQAALKAGIPDSAPAV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963838  118 TVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMTLSQRG-NHGNISSRLLENEKARDCLIP-----------MGITS 185
Cdd:pfam00108  80 TINKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYAlPTDARSGLKHGDEKKHDLLIPdgltdafngyhMGLTA 159

                         170       180
                  ....*....|....*....|....
gi 568963838  186 ENVAERFGVSRQKQDAFALASQQK 209
Cdd:pfam00108 160 ENVAKKYGISREEQDAFAVKSHQK 183
thiolase cd00751
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ...
 39-209 2.83e-66

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: 209.64  E-value: 2.83e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963838  39 VVVHGRRTPIGRAsRGCFKDTTPDELLSAVLTAVLQDVKLKPEQLGDISVGNVLQPGAGAIMARIAQFLSGIPETVPLST 118
Cdd:cd00751    1 VIVSAVRTPIGRF-GGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGEGQNPARQAALLAGLPESVPATT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963838 119 VNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMTLS----------QRGNHGNISSRLLENEKARDCLIPMGITSENV 188
Cdd:cd00751   80 VNRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRApyllpkarrgGRLGLNTLDGMLDDGLTDPFTGLSMGITAENV 159

                        170       180
                 ....*....|....*....|.
gi 568963838 189 AERFGVSRQKQDAFALASQQK 209
Cdd:cd00751  160 AEKYGISREEQDEFALRSHQR 180
PaaJ COG0183
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ...
 36-209 3.96e-58

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: 188.74  E-value: 3.96e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963838  36 SDVVVVHGRRTPIGRAsRGCFKDTTPDELLSAVLTAVLQDVKLKPEQLGDISVGNVLQPGAGAIMARIAQFLSGIPETVP 115
Cdd:COG0183    2 REVVIVDAVRTPFGRF-GGALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQAGQGQNPARQAALLAGLPESVP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963838 116 LSTVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMTLS----------QRGNHGNISSRLLENEKARDCLIPMGITS 185
Cdd:COG0183   81 AVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRApmllpkarwgYRMNAKLVDPMINPGLTDPYTGLSMGETA 160

                        170       180
                 ....*....|....*....|....
gi 568963838 186 ENVAERFGVSRQKQDAFALASQQK 209
Cdd:COG0183  161 ENVAERYGISREEQDAFALRSHQR 184
AcCoA-C-Actrans TIGR01930
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ...
 40-209 9.46e-53

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: 174.72  E-value: 9.46e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963838   40 VVHGRRTPIGRAsRGCFKDTTPDELLSAVLTAVLQDVKLKPEQLGDISVGNVLQPGAGAIMARIAQFLSGIPETVPLSTV 119
Cdd:TIGR01930   1 IVAAARTPIGKF-GGSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLQAGEQQNIARQAALLAGLPESVPAYTV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963838  120 NRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMT----LSQRGNHGNISSRLLENEKAR-------DCLIPMGITSENV 188
Cdd:TIGR01930  80 NRQCASGLQAVILAAQLIRAGEADVVVAGGVESMSrvpyGVPRSLRWGVKPGNAELEDARlkdltdaNTGLPMGVTAENL 159

                         170       180
                  ....*....|....*....|.
gi 568963838  189 AERFGVSRQKQDAFALASQQK 209
Cdd:TIGR01930 160 AKKYGISREEQDEYALRSHQR 180
PRK05790 PRK05790
putative acyltransferase; Provisional
 36-209 5.70e-48

putative acyltransferase; Provisional


Pssm-ID: 180261 [Multi-domain]  Cd Length: 393  Bit Score: 162.63  E-value: 5.70e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963838  36 SDVVVVHGRRTPIGRASrGCFKDTTPDELLSAVLTAVLQDVKLKPEQLGDISVGNVLQPGAGAIMARIAQFLSGIPETVP 115
Cdd:PRK05790   2 KDVVIVSAARTPIGKFG-GALKDVSAVELGAIVIKAALERAGVPPEQVDEVIMGQVLQAGAGQNPARQAALKAGLPVEVP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963838 116 LSTVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMTLS------QRGNH--GNISsrlLENEKARDCL------IPM 181
Cdd:PRK05790  81 ALTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQESMSQAphvlpgSRWGQkmGDVE---LVDTMIHDGLtdafngYHM 157

                        170       180
                 ....*....|....*....|....*...
gi 568963838 182 GITSENVAERFGVSRQKQDAFALASQQK 209
Cdd:PRK05790 158 GITAENLAEQYGITREEQDEFALASQQK 185
PRK09052 PRK09052
acetyl-CoA C-acyltransferase;
37-211 4.22e-47

acetyl-CoA C-acyltransferase;


Pssm-ID: 181626 [Multi-domain]  Cd Length: 399  Bit Score: 160.55  E-value: 4.22e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963838  37 DVVVVHGRRTPIGRASRGCFKDTTPDELLSAVLTAVLQDVK-LKPEQLGDISVGNVLqPGA--GAIMARIAQFLSGIPET 113
Cdd:PRK09052   7 DAYIVAATRTPVGKAPRGMFKNTRPDDLLAHVLRSAVAQVPgLDPKLIEDAIVGCAM-PEAeqGLNVARIGALLAGLPNS 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963838 114 VPLSTVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMTL-SQRGNHGNISSRLLENEKARDCLIPMGITSENVAERF 192
Cdd:PRK09052  86 VGGVTVNRFCASGLQAVAMAADRIRVGEADVMIAAGVESMSMvPMMGNKPSMSPAIFARDENVGIAYGMGLTAEKVAEQW 165

                        170
                 ....*....|....*....
gi 568963838 193 GVSRQKQDAFALASQQKEC 211
Cdd:PRK09052 166 KVSREDQDAFALESHQKAI 184
PRK09051 PRK09051
beta-ketothiolase BktB;
34-209 1.27e-34

beta-ketothiolase BktB;


Pssm-ID: 181625 [Multi-domain]  Cd Length: 394  Bit Score: 127.38  E-value: 1.27e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963838  34 SASDVVVVHGRRTPIGrASRGCFKDTTPDELLSAVLTAVLQDVKLKPEQLGDISVGNVLQPGA-GAIMARIAQFLSGIPE 112
Cdd:PRK09051   1 MMREVVVVSGVRTAIG-TFGGSLKDVAPTDLGATVVREALARAGVDPDQVGHVVFGHVIPTEPrDMYLSRVAAINAGVPQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963838 113 TVPLSTVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMTlsqRGNHGNISSRL---LENEKARDCL----------I 179
Cdd:PRK09051  80 ETPAFNVNRLCGSGLQAIVSAAQAILLGDADVAIGGGAESMS---RAPYLLPAARWgarMGDAKLVDMMvgalhdpfgtI 156

                        170       180       190
                 ....*....|....*....|....*....|
gi 568963838 180 PMGITSENVAERFGVSRQKQDAFALASQQK 209
Cdd:PRK09051 157 HMGVTAENVAAKYGISREAQDALALESHRR 186
PRK07661 PRK07661
acetyl-CoA C-acetyltransferase;
39-209 7.02e-34

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181072 [Multi-domain]  Cd Length: 391  Bit Score: 125.63  E-value: 7.02e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963838  39 VVVHGRRTPIGRASRGCFKDTTPDELLSAVLTAVLQDVKLKPEQLGDISVGNVLqPGA--GAIMARIAQFLSGIPETVPL 116
Cdd:PRK07661   5 VIVAGARTPVGKAKKGSLKTVRPDDLGALVVKETLKRAGNYEGPIDDLIIGCAM-PEAeqGLNMARNIGALAGLPYTVPA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963838 117 STVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMTLSQRGNH-GNISSRLLENekARDCLIPMGITSENVAERFGVS 195
Cdd:PRK07661  84 ITINRYCSSGLQSIAYGAERIMLGHSEAVIAGGAESMSLVPMMGHvVRPNPRLVEA--APEYYMGMGHTAEQVAVKYGIS 161

                        170
                 ....*....|....
gi 568963838 196 RQKQDAFALASQQK 209
Cdd:PRK07661 162 REDQDAFAVRSHQR 175
PRK06205 PRK06205
acetyl-CoA C-acetyltransferase;
36-209 6.88e-29

acetyl-CoA C-acetyltransferase;


Pssm-ID: 235741 [Multi-domain]  Cd Length: 404  Bit Score: 112.39  E-value: 6.88e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963838  36 SDVVVVHGRRTPIGRASrGCFKDTTPDELLSAVLTAVLQDVKLKPEQLGDISVGNVLQPGAGAIMARIAQFLSGIPETVP 115
Cdd:PRK06205   2 RDAVICEPVRTPVGRFG-GAFKDVPAEELAATVIRALVERTGIDPARIDDVIFGQGYPNGEAPAIGRVAALDAGLPVTVP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963838 116 LSTVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESM------TLSQR--GNHGNIS-----SRLLENEKARDCLIPMG 182
Cdd:PRK06205  81 GMQLDRRCGSGLQAVITAAMQVQTGAADVVIAGGAESMsnvefyTTDMRwgVRGGGVQlhdrlARGRETAGGRRFPVPGG 160

                        170       180
                 ....*....|....*....|....*....
gi 568963838 183 I--TSENVAERFGVSRQKQDAFALASQQK 209
Cdd:PRK06205 161 MieTAENLRREYGISREEQDALAVRSHQR 189
PRK05656 PRK05656
acetyl-CoA C-acetyltransferase;
37-209 1.43e-28

acetyl-CoA C-acetyltransferase;


Pssm-ID: 168156  Cd Length: 393  Bit Score: 111.13  E-value: 1.43e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963838  37 DVVVVHGRRTPIGrASRGCFKDTTPDELLSAVLTAVLQDVKLKPEQLGDISVGNVLQPGAGAIMARIAQFLSGIPETVPL 116
Cdd:PRK05656   3 DVVIVAATRTAIG-SFQGSLANIPAVELGAAVIRRLLEQTGLDPAQVDEVILGQVLTAGAGQNPARQAAIKAGLPHSVPA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963838 117 STVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMTLS----------QRGNHGNISSRLLEN---EKARDclIPMGI 183
Cdd:PRK05656  82 MTLNKVCGSGLKALHLAAQAIRCGDAEVIIAGGQENMSLApyvlpgartgLRMGHAQLVDSMITDglwDAFND--YHMGI 159

                        170       180
                 ....*....|....*....|....*.
gi 568963838 184 TSENVAERFGVSRQKQDAFALASQQK 209
Cdd:PRK05656 160 TAENLVEKYGISREAQDAFAAASQQK 185
PRK06633 PRK06633
acetyl-CoA C-acetyltransferase;
38-209 3.49e-28

acetyl-CoA C-acetyltransferase;


Pssm-ID: 168632 [Multi-domain]  Cd Length: 392  Bit Score: 110.12  E-value: 3.49e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963838  38 VVVVHGRRTPIGraSRGCFKDTTPDELLSAVLTA-VLQDVKLKPEQLGDISVGNVLQPGAGAIMARIAQFLSGIPETVPL 116
Cdd:PRK06633   5 VYITHAKRTAFG--SFMGSLSTTPAPMLAAHLIKdILQNSKIDPALVNEVILGQVITGGSGQNPARQTLIHAGIPKEVPG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963838 117 STVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMTLSQRGNH-------GNISS-RLLENEKARDCL--IPMGITSE 186
Cdd:PRK06633  83 YTINKVCGSGLKSVALAANSIMTGDNEIVIAGGQENMSLGMHGSYiragakfGDIKMvDLMQYDGLTDVFsgVFMGITAE 162

                        170       180
                 ....*....|....*....|...
gi 568963838 187 NVAERFGVSRQKQDAFALASQQK 209
Cdd:PRK06633 163 NISKQFNISRQEQDEFALSSHKK 185
PRK07851 PRK07851
acetyl-CoA C-acetyltransferase;
37-208 3.71e-28

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181146 [Multi-domain]  Cd Length: 406  Bit Score: 110.48  E-value: 3.71e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963838  37 DVVVVHGRRTPIGRASRGCFKDTTPDELLSAVLTAVLQDV-KLKPEQLGDISVGnVLQPG--AGAIMARIAQFLSGIPeT 113
Cdd:PRK07851   3 EAVIVSTARSPIGRAFKGSLKDMRPDDLAAQMVRAALDKVpALDPTDIDDLMLG-CGLPGgeQGFNMARVVAVLLGYD-F 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963838 114 VPLSTVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMTLSQRGNHGNISSR---LLENEKAR--------------- 175
Cdd:PRK07851  81 LPGTTVNRYCSSSLQTTRMAFHAIKAGEGDVFISAGVETVSRFAKGNSDSLPDTknpLFAEAQARtaaraeggaeawhdp 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 568963838 176 -------DCLIPMGITSENVAERFGVSRQKQDAFALASQQ 208
Cdd:PRK07851 161 redgllpDVYIAMGQTAENVAQLTGISREEQDEWGVRSQN 200
PRK07108 PRK07108
acetyl-CoA C-acyltransferase;
36-211 4.06e-28

acetyl-CoA C-acyltransferase;


Pssm-ID: 180843 [Multi-domain]  Cd Length: 392  Bit Score: 109.86  E-value: 4.06e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963838  36 SDVVVVHGRRTPIGRASRGCFKDTTPDELLSAVLTAVLQDVKLKPEQLGDISVGNVLQPGA-GAIMARIAQFLSGIPETV 114
Cdd:PRK07108   2 TEAVIVSTARTPLAKSWRGAFNMTHGATLGGHVVQHAVERAKLDPAEVEDVIMGCANPEGAtGANIARQIALRAGLPVTV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963838 115 PLSTVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMTLSQR-GNHGNISSRLLENEKArDCLIPMGITSENVAERFG 193
Cdd:PRK07108  82 PGMTVNRFCSSGLQTIALAAQRVIAGEGDVFVAGGVESISCVQNeMNRHMLREGWLVEHKP-EIYWSMLQTAENVAKRYG 160

                        170
                 ....*....|....*...
gi 568963838 194 VSRQKQDAFALASQQKEC 211
Cdd:PRK07108 161 ISKERQDEYGVQSQQRAA 178
fadA PRK08947
3-ketoacyl-CoA thiolase; Reviewed
 37-209 2.46e-27

3-ketoacyl-CoA thiolase; Reviewed


Pssm-ID: 181592 [Multi-domain]  Cd Length: 387  Bit Score: 107.74  E-value: 2.46e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963838  37 DVVVVHGRRTPIGRASRGCFKDTTPDELLSAVLTAVL-QDVKLKPEQLGDISVGNVLQPG-AGAIMARIAQFLSGIPETV 114
Cdd:PRK08947   3 DVVIVDAIRTPMGRSKGGAFRNVRAEDLSAHLMRSLLaRNPALDPAEIDDIIWGCVQQTLeQGFNIARNAALLAGIPHSV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963838 115 PLSTVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMtlsqrG----NHG-NISSRLLEN-EKARDClipMGITSENV 188
Cdd:PRK08947  83 PAVTVNRLCGSSMQALHDAARAIMTGDGDVFLIGGVEHM-----GhvpmNHGvDFHPGLSKNvAKAAGM---MGLTAEML 154

                        170       180
                 ....*....|....*....|.
gi 568963838 189 AERFGVSRQKQDAFALASQQK 209
Cdd:PRK08947 155 GKMHGISREQQDAFAARSHQR 175
PRK09050 PRK09050
beta-ketoadipyl CoA thiolase; Validated
 36-209 1.33e-26

beta-ketoadipyl CoA thiolase; Validated


Pssm-ID: 181624 [Multi-domain]  Cd Length: 401  Bit Score: 105.81  E-value: 1.33e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963838  36 SDVVVVHGRRTPIGRASrGCFKDTTPDELLSAVLTAVLQ-DVKLKPEQLGDISVGNVLQPGA-GAIMARIAQFLSGIPET 113
Cdd:PRK09050   2 TEAFICDAIRTPIGRYG-GALSSVRADDLGAVPLKALMArNPGVDWEAVDDVIYGCANQAGEdNRNVARMSALLAGLPVS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963838 114 VPLSTVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMTlsqRGNH--GNISSRLLENEKARDCLI------------ 179
Cdd:PRK09050  81 VPGTTINRLCGSGMDAVGTAARAIKAGEAELMIAGGVESMS---RAPFvmGKADSAFSRQAEIFDTTIgwrfvnplmkaq 157

                        170       180       190
                 ....*....|....*....|....*....|....
gi 568963838 180 ----PMGITSENVAERFGVSRQKQDAFALASQQK 209
Cdd:PRK09050 158 ygvdSMPETAENVAEDYNISRADQDAFALRSQQR 191
PRK08242 PRK08242
acetyl-CoA C-acetyltransferase;
45-209 1.64e-24

acetyl-CoA C-acetyltransferase;


Pssm-ID: 236197 [Multi-domain]  Cd Length: 402  Bit Score: 100.34  E-value: 1.64e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963838  45 RTPIGRA-SRGCFKDTTPDELLSAVLTAVLQDVKLKPEQLGDISVGNVLQPG-AGAIMARIAQFLSGIPETVPLSTVNRQ 122
Cdd:PRK08242  11 RTPRGKGkKDGSLHEVKPVRLAAGLLEALRDRNGLDTAAVDDVVLGCVTPVGdQGADIARTAVLAAGLPETVPGVQINRF 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963838 123 CSSGLQAVANIAGGIRNGSYDIGMACGVESMTLSQRGNHG---------NISSRllenekardcLIPMGITSENVAERFG 193
Cdd:PRK08242  91 CASGLEAVNLAAAKVRSGWDDLVIAGGVESMSRVPMGSDGgawamdpstNFPTY----------FVPQGISADLIATKYG 160

                        170
                 ....*....|....*.
gi 568963838 194 VSRQKQDAFALASQQK 209
Cdd:PRK08242 161 FSREDVDAYAVESQQR 176
PLN02644 PLN02644
acetyl-CoA C-acetyltransferase
 37-209 8.06e-24

acetyl-CoA C-acetyltransferase


Pssm-ID: 215347 [Multi-domain]  Cd Length: 394  Bit Score: 98.24  E-value: 8.06e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963838  37 DVVVVHGRRTPIGrASRGCFKDTTPDELLSAVLTAVLQDVKLKPEQLGDISVGNVLQPGAGAIMARIAQFLSGIPETVPL 116
Cdd:PLN02644   2 DVCIVGVARTPIG-GFLGSLSSLSATELGSIAIQAALERAGVDPALVQEVFFGNVLSANLGQAPARQAALGAGLPPSTIC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963838 117 STVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMT----------LSQRGNHGNISSRLLenekaRDCL------IP 180
Cdd:PLN02644  81 TTVNKVCASGMKAVMLAAQSIQLGINDVVVAGGMESMSnapkylpearKGSRLGHDTVVDGML-----KDGLwdvyndFG 155

                        170       180
                 ....*....|....*....|....*....
gi 568963838 181 MGITSENVAERFGVSRQKQDAFALASQQK 209
Cdd:PLN02644 156 MGVCAELCADQYSISREEQDAYAIQSYER 184
PRK06954 PRK06954
acetyl-CoA C-acetyltransferase;
38-206 1.25e-23

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180775 [Multi-domain]  Cd Length: 397  Bit Score: 97.66  E-value: 1.25e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963838  38 VVVVHGRRTPIGrASRGCFKDTTPDELLSAVLTAVLQDVKLKPEQLGDISVGNVLQPGAGAIMARIAQFLSGIPETVPLS 117
Cdd:PRK06954   9 IVIASAARTPMA-AFQGEFASLTAPQLGAAAIAAAVERAGLKPEQIDEVVMGCVLPAGQGQAPARQAALGAGLPLSVGCT 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963838 118 TVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMTLS----------QRGNHGNISSRLLEN--EKARDCLIPMGITS 185
Cdd:PRK06954  88 TVNKMCGSGMRAAMFAHDMLVAGSVDVIVAGGMESMTNApyllpkarggMRMGHGQVLDHMFLDglEDAYDKGRLMGTFA 167

                        170       180
                 ....*....|....*....|.
gi 568963838 186 ENVAERFGVSRQKQDAFALAS 206
Cdd:PRK06954 168 EECAGEYGFTREAQDAFAIES 188
PRK07850 PRK07850
steroid 3-ketoacyl-CoA thiolase;
39-209 3.36e-23

steroid 3-ketoacyl-CoA thiolase;


Pssm-ID: 181145 [Multi-domain]  Cd Length: 387  Bit Score: 96.33  E-value: 3.36e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963838  39 VVVHGRRTPIGRaSRGCFKDTTPDELLSAVLTAVLQDVKLKPEQLGDISVGNVLQPGAGAI-MARIAQFLSGIPETVPLS 117
Cdd:PRK07850   5 VIVEAVRTPIGK-RNGWLSGLHAAELLGAVQRAVLDRAGIDPGDVEQVIGGCVTQAGEQSNnITRTAWLHAGLPYHVGAT 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963838 118 TVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMT---LSQRGNHGnissrlLENEKARDCLIPMG---ITSENVAER 191
Cdd:PRK07850  84 TIDCQCGSAQQANHLVAGLIAAGAIDVGIACGVEAMSrvpLGANAGPG------RGLPRPDSWDIDMPnqfEAAERIAKR 157

                        170
                 ....*....|....*...
gi 568963838 192 FGVSRQKQDAFALASQQK 209
Cdd:PRK07850 158 RGITREDVDAFGLRSQRR 175
PRK08235 PRK08235
acetyl-CoA C-acetyltransferase;
39-209 4.78e-23

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181311 [Multi-domain]  Cd Length: 393  Bit Score: 95.93  E-value: 4.78e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963838  39 VVVHGRRTPIGRASrGCFKDTTPDELLSAVLTAVLQDVKLKPEQLGDISVGNVLQPGAGAIMARIAQFLSGIPETVPLST 118
Cdd:PRK08235   5 VIVSAARTPFGKFG-GSLKDVKATELGGIAIKEALERANVSAEDVEEVIMGTVLQGGQGQIPSRQAARAAGIPWEVQTET 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963838 119 VNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMT----LSQRGNHGNissRLLENEkARDCLI-----------PMGI 183
Cdd:PRK08235  84 VNKVCASGLRAVTLADQIIRAGDASVIVAGGMESMSnapyILPGARWGY---RMGDNE-VIDLMVadgltcafsgvHMGV 159

                        170       180
                 ....*....|....*....|....*.
gi 568963838 184 TSENVAERFGVSRQKQDAFALASQQK 209
Cdd:PRK08235 160 YGGEVAKELGISREAQDEWAYRSHQR 185
PRK06366 PRK06366
acetyl-CoA C-acetyltransferase;
37-209 1.63e-22

acetyl-CoA C-acetyltransferase;


Pssm-ID: 102340 [Multi-domain]  Cd Length: 388  Bit Score: 94.69  E-value: 1.63e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963838  37 DVVVVHGRRTPIGRASRGCFKDTTPdELLSAVLTAVLQDVKLKPEQLGDISVGNVLQPGAGAIMARIAQFLSGIPETVPL 116
Cdd:PRK06366   3 DVYIVSAKRTAIGKFGRSFSKIKAP-QLGGAAIKAVIDDAKLDPALVQEVIMGNVIQAGVGQNPAGQAAYHAGLPFGVTK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963838 117 STVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMTLSQRGNHGNI----SSRLLENEKARDCLIP-----------M 181
Cdd:PRK06366  82 YTVNVVCASGMLAVESAAREIMLGERDLVIAGGMENMSNAPFLLPSDLrwgpKHLLHKNYKIDDAMLVdglidafyfehM 161

                        170       180
                 ....*....|....*....|....*...
gi 568963838 182 GITSENVAERFGVSRQKQDAFALASQQK 209
Cdd:PRK06366 162 GVSAERTARKYGITREMADEYSVQSYER 189
PRK06690 PRK06690
acetyl-CoA C-acyltransferase;
39-209 7.84e-22

acetyl-CoA C-acyltransferase;


Pssm-ID: 180659 [Multi-domain]  Cd Length: 361  Bit Score: 92.52  E-value: 7.84e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963838  39 VVVHGRRTPIGRASrGCFKDTTPDELLSAVLTAVLQDVklkPEQLGDISVGNVLQPGAGaiMARIAQFLSGIPETVPLST 118
Cdd:PRK06690   4 VIVEAKRTPIGKKN-GMLKDYEVQQLAAPLLTFLSKGM---EREIDDVILGNVVGPGGN--VARLSALEAGLGLHIPGVT 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963838 119 VNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMTLSQRGNHGNISSRLLENEKardclipMGITSENVAERFGVSRQK 198
Cdd:PRK06690  78 IDRQCGAGLEAIRTACHFIQGGAGKCYIAGGVESTSTSPFQNRARFSPETIGDPD-------MGVAAEYVAERYNITREM 150

                        170
                 ....*....|.
gi 568963838 199 QDAFALASQQK 209
Cdd:PRK06690 151 QDEYACLSYKR 161
PRK08131 PRK08131
3-oxoadipyl-CoA thiolase;
37-209 1.17e-21

3-oxoadipyl-CoA thiolase;


Pssm-ID: 181242 [Multi-domain]  Cd Length: 401  Bit Score: 92.15  E-value: 1.17e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963838  37 DVVVVHGRRTPIGRASrGCFKDTTPDELLSAVLTAVLQDVKLKPEQLGDISVGNVLQPGAGAI-MARIAQFLSGIPETVP 115
Cdd:PRK08131   3 DAYIYDGLRSPFGRHA-GALASVRPDDLAATVIRRLLEKSGFPGDDIEDVILGCTNQAGEDSRnVARNALLLAGLPVTVP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963838 116 LSTVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMT------------LSQRGN--HGNISSRL----LENEKARDc 177
Cdd:PRK08131  82 GQTVNRLCASGLAAVIDAARAITCGEGDLYLAGGVESMSrapfvmgkaesaFSRDAKvfDTTIGARFpnpkIVAQYGND- 160

                        170       180       190
                 ....*....|....*....|....*....|..
gi 568963838 178 liPMGITSENVAERFGVSRQKQDAFALASQQK 209
Cdd:PRK08131 161 --SMPETGDNVAAEFGISREDADRFAAQSQAK 190
PRK06504 PRK06504
acetyl-CoA C-acetyltransferase;
40-209 8.94e-19

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180595 [Multi-domain]  Cd Length: 390  Bit Score: 84.01  E-value: 8.94e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963838  40 VVHGRRTPIGRASrGCFKDTTPDELLSAVLTAVLQDVKLKPEQLGDISVGNVLQPGAGAI-MARIAQFLSGIPETVPLST 118
Cdd:PRK06504   6 IVAAARTAGGRKG-GRLAGWHPADLAAQVLDALVDRSGADPALIEDVIMGCVSQVGEQATnVARNAVLASKLPESVPGTS 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963838 119 VNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMT---------LSQRGNHGNISSRLLEnEKARDCLIPMGITSENVA 189
Cdd:PRK06504  85 IDRQCGSSQQALHFAAQAVMSGTMDIVIAAGVESMTrvpmgspstLPAKNGLGHYKSPGME-ERYPGIQFSQFTGAEMMA 163

                        170       180
                 ....*....|....*....|
gi 568963838 190 ERFGVSRQKQDAFALASQQK 209
Cdd:PRK06504 164 KKYGLSKDQLDEFALQSHQR 183
PRK07801 PRK07801
acetyl-CoA C-acetyltransferase;
36-209 1.36e-17

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181123 [Multi-domain]  Cd Length: 382  Bit Score: 80.52  E-value: 1.36e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963838  36 SDVVVVHGRRTPIGRaSRGCFKDTTPDELLSAVLTAVLQDVKLKPEQLGDISVGNVLQ--PGAGAImARIAQFLSGIPET 113
Cdd:PRK07801   2 AEAYIVDAVRTPVGK-RKGGLAGVHPADLGAHVLKGLVDRTGIDPAAVDDVIFGCVDTigPQAGNI-ARTSWLAAGLPEE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963838 114 VPLSTVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMTL------SQRGNHGNISSRLLENEKAR----DCLIPMGI 183
Cdd:PRK07801  80 VPGVTVDRQCGSSQQAIHFAAQAVMSGTQDLVVAGGVQNMSQipissaMTAGEQLGFTSPFAESKGWLhrygDQEVSQFR 159

                        170       180
                 ....*....|....*....|....*.
gi 568963838 184 TSENVAERFGVSRQKQDAFALASQQK 209
Cdd:PRK07801 160 GAELIAEKWGISREEMERFALESHRR 185
nondecarbox_cond_enzymes cd00826
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ...
 45-203 3.72e-10

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: 59.04  E-value: 3.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963838  45 RTPIGR--ASRGCFKDTTPDELLSAVLTAVLQDVKLKPEQLGDISVGNVLQPGAGAIMARIAQFLSGIPETVPLSTVNRQ 122
Cdd:cd00826    5 MTAFGKfgGENGADANDLAHEAGAKAIAAALEPAGVAAGAVEEACLGQVLGAGEGQNCAQQAAMHAGGLQEAPAIGMNNL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963838 123 CSSGLQAVANIAGGIRNGSYDIGMACGVESMTLSQRGNHGNISSRLLENE-KARDCLIPMGITSENVAERFGVSRQKQDA 201
Cdd:cd00826   85 CGSGLRALALAMQLIAGGDANCILAGGFEKMETSAENNAKEKHIDVLINKyGMRACPDAFALAGQAGAEAAEKDGRFKDE 164


                 ..
gi 568963838 202 FA 203
Cdd:cd00826  165 FA 166
SCP-x_thiolase cd00829
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ...
 46-161 1.05e-07

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: 51.88  E-value: 1.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963838  46 TPIGRASrgcfkDTTPDELLSAVLTAVLQDVKLKPEQLGDISVGNVL-QPGAGAIMARIAQFLSGIPetVPLSTVNRQCS 124
Cdd:cd00829    6 TPFGRRS-----DRSPLELAAEAARAALDDAGLEPADIDAVVVGNAAgGRFQSFPGALIAEYLGLLG--KPATRVEAAGA 78

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 568963838 125 SGLQAVANIAGGIRNGSYDIGMACGVESMTLSQRGNH 161
Cdd:cd00829   79 SGSAAVRAAAAAIASGLADVVLVVGAEKMSDVPTGDE 115
PRK06157 PRK06157
acetyl-CoA acetyltransferase; Validated
 54-151 2.16e-04

acetyl-CoA acetyltransferase; Validated


Pssm-ID: 180433 [Multi-domain]  Cd Length: 398  Bit Score: 41.94  E-value: 2.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963838  54 GCFK-----DTTPDELLSAVLTAVLQDVKLKPEQLGDISVG---NVLQPGAGAIMARIAQFLSGIPETvplsTVNRQCSS 125
Cdd:PRK06157  15 GCTKfgerwDAGAEDLMVEAFLEALADAGIEPKDIDAAWFGthyDEIGSGKSGTPLSRALRLPNIPVT----RVENFCAT 90

                         90       100
                 ....*....|....*....|....*.
gi 568963838 126 GLQAVANIAGGIRNGSYDIGMACGVE 151
Cdd:PRK06157  91 GSEAFRGAVYAVASGAYDIALALGVE 116
PRK06064 PRK06064
thiolase domain-containing protein;
36-154 2.50e-04

thiolase domain-containing protein;


Pssm-ID: 235688 [Multi-domain]  Cd Length: 389  Bit Score: 41.42  E-value: 2.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963838  36 SDVVVVHGRRTPIGRASRGCFKDTtpdeLLSAVLTAvLQDVKLKPEQLGDISVGNVL------QPGAGAIMARIAQfLSG 109
Cdd:PRK06064   2 RDVAIIGVGQTKFGELWDVSLRDL----AVEAGLEA-LEDAGIDGKDIDAMYVGNMSaglfvsQEHIAALIADYAG-LAP 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 568963838 110 IPETvplsTVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMT 154
Cdd:PRK06064  76 IPAT----RVEAACASGGAALRQAYLAVASGEADVVLAAGVEKMT 116
PRK06289 PRK06289
acetyl-CoA acetyltransferase; Provisional
 63-153 2.62e-04

acetyl-CoA acetyltransferase; Provisional


Pssm-ID: 235771 [Multi-domain]  Cd Length: 403  Bit Score: 41.60  E-value: 2.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963838  63 ELLSAVLTAVLQDVKLKPEQLGDISVGNVlqpgAGAIMARIAQfLSGIPETV-------PLSTVNRQCSSGLQAVANIAG 135
Cdd:PRK06289  28 DLTREVVDGTLAAAGVDADDIEVVHVGNF----FGELFAGQGH-LGAMPATVhpalwgvPASRHEAACASGSVATLAAMA 102

                         90
                 ....*....|....*...
gi 568963838 136 GIRNGSYDIGMACGVESM 153
Cdd:PRK06289 103 DLRAGRYDVALVVGVELM 120
cond_enzymes cd00327
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ...
 59-152 1.28e-03

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: 38.96  E-value: 1.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963838  59 TTPDELLSAVLTAVLQDVKLKPEQLGDISVGNVLQPGAGAIMARIAQFLSGIPEtVPLSTVNRQCSSGLQAVANIAGGIR 138
Cdd:cd00327    5 ITASELGFEAAEQAIADAGLSKGPIVGVIVGTTGGSGEFSGAAGQLAYHLGISG-GPAYSVNQACATGLTALALAVQQVQ 83

                         90
                 ....*....|....
gi 568963838 139 NGSYDIGMACGVES 152
Cdd:cd00327   84 NGKADIVLAGGSEE 97
PRK12578 PRK12578
thiolase domain-containing protein;
48-154 2.05e-03

thiolase domain-containing protein;


Pssm-ID: 183606 [Multi-domain]  Cd Length: 385  Bit Score: 38.67  E-value: 2.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963838  48 IGRASRGCFKDTTPDELLSAVLTAVLQDVKLKPEQLGDISVGNVLQPGAGAIMARIAQFLSGIPETVPLStVNRQCSSGL 127
Cdd:PRK12578   8 VGNSKFGRRDDVSVQELAWESIKEALNDAGVSQTDIELVVVGSTAYRGIELYPAPIVAEYSGLTGKVPLR-VEAMCATGL 86

                         90       100
                 ....*....|....*....|....*..
gi 568963838 128 QAVANIAGGIRNGSYDIGMACGVESMT 154
Cdd:PRK12578  87 AASLTAYTAVASGLVDMAIAVGVDKMT 113
 
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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