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Conserved domains on  [gi|568931880|ref|XP_006539232|]
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cytosolic acyl coenzyme A thioester hydrolase isoform X2 [Mus musculus]

Protein Classification

acyl-CoA thioesterase( domain architecture ID 10787832)

acyl-CoA thioesterase catalyzes the hydrolysis of acyl-CoA esters to the free fatty acid and CoA

EC:  3.1.2.20
Gene Ontology:  GO:0047617

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
163-305 6.29e-49

Acyl-CoA hydrolase [Lipid transport and metabolism];


:

Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 160.35  E-value: 6.29e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931880 163 TVSYSQSSLIHLVGPSDCTLHGFVHGGVTMKLMDEVAGIVAARHCKTNIVTASVDAINFHDKIRKGCVITISGRMTFTSN 242
Cdd:COG1607    1 PLPDSELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGR 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568931880 243 KSMEIEVLVDADPVvdNSQKRYRAASAFFTYVSLNQEGKPMPVPQLVPETEDEKKRFEEGKGR 305
Cdd:COG1607   81 TSMEVGVEVWAEDL--RTGERRLVTEAYFTFVAVDEDGKPRPVPPLIPETEEEKRLFEEALRR 141
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
1-144 1.74e-30

Acyl-CoA hydrolase [Lipid transport and metabolism];


:

Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 112.58  E-value: 1.74e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931880   1 MRPDDANVAGNVHGGTILKMIEEAGAIISTRHCNSqngeRCVAalARVERTDFLSPMCIGEVAHVSAEITYTSKHSVEVQ 80
Cdd:COG1607   13 VMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARG----RVVT--ASVDSVDFLRPVRVGDIVELYARVVRVGRTSMEVG 86

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568931880  81 VHVMSENILTGTKKLTNKATLWYVplslkNVD---KVLEVPPIVylrqEQEEEGRKRYEAQKLERME 144
Cdd:COG1607   87 VEVWAEDLRTGERRLVTEAYFTFV-----AVDedgKPRPVPPLI----PETEEEKRLFEEALRRREL 144
 
Name Accession Description Interval E-value
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
163-305 6.29e-49

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 160.35  E-value: 6.29e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931880 163 TVSYSQSSLIHLVGPSDCTLHGFVHGGVTMKLMDEVAGIVAARHCKTNIVTASVDAINFHDKIRKGCVITISGRMTFTSN 242
Cdd:COG1607    1 PLPDSELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGR 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568931880 243 KSMEIEVLVDADPVvdNSQKRYRAASAFFTYVSLNQEGKPMPVPQLVPETEDEKKRFEEGKGR 305
Cdd:COG1607   81 TSMEVGVEVWAEDL--RTGERRLVTEAYFTFVAVDEDGKPRPVPPLIPETEEEKRLFEEALRR 141
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 163-286 2.69e-41

Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes deacylate long-chain fatty acids by hydrolyzing acyl-CoA thioesters to free fatty acids and CoA-SH. Eukaryotic members of this family are expressed in brain, testis, and brown adipose tissues. The archeal and eukaryotic members of this family have two tandem copies of the conserved hot dog fold, while most bacterial members have only one copy.


Pssm-ID: 239526 [Multi-domain]  Cd Length: 123  Bit Score: 139.63  E-value: 2.69e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931880 163 TVSYSQSSLIHLVGPSDCTLHGFVHGGVTMKLMDEVAGIVAARHCKTNIVTASVDAINFHDKIRKGCVITISGRMTFTSN 242
Cdd:cd03442    2 PMEDTELSTRELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGGRVVTASVDRIDFLKPVRVGDVVELSARVVYTGR 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 568931880 243 KSMEIEVLVDAdpVVDNSQKRYRAASAFFTYVSLNQEGKPMPVP 286
Cdd:cd03442   82 TSMEVGVEVEA--EDPLTGERRLVTSAYFTFVALDEDGKPRPVP 123
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
1-144 1.74e-30

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 112.58  E-value: 1.74e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931880   1 MRPDDANVAGNVHGGTILKMIEEAGAIISTRHCNSqngeRCVAalARVERTDFLSPMCIGEVAHVSAEITYTSKHSVEVQ 80
Cdd:COG1607   13 VMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARG----RVVT--ASVDSVDFLRPVRVGDIVELYARVVRVGRTSMEVG 86

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568931880  81 VHVMSENILTGTKKLTNKATLWYVplslkNVD---KVLEVPPIVylrqEQEEEGRKRYEAQKLERME 144
Cdd:COG1607   87 VEVWAEDLRTGERRLVTEAYFTFV-----AVDedgKPRPVPPLI----PETEEEKRLFEEALRRREL 144
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 1-104 6.51e-30

Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes deacylate long-chain fatty acids by hydrolyzing acyl-CoA thioesters to free fatty acids and CoA-SH. Eukaryotic members of this family are expressed in brain, testis, and brown adipose tissues. The archeal and eukaryotic members of this family have two tandem copies of the conserved hot dog fold, while most bacterial members have only one copy.


Pssm-ID: 239526 [Multi-domain]  Cd Length: 123  Bit Score: 110.35  E-value: 6.51e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931880   1 MRPDDANVAGNVHGGTILKMIEEAGAIISTRHCNSqngeRCVaaLARVERTDFLSPMCIGEVAHVSAEITYTSKHSVEVQ 80
Cdd:cd03442   14 VLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGG----RVV--TASVDRIDFLKPVRVGDVVELSARVVYTGRTSMEVG 87

                         90       100
                 ....*....|....*....|....
gi 568931880  81 VHVMSENILTGTKKLTNKATLWYV 104
Cdd:cd03442   88 VEVEAEDPLTGERRLVTSAYFTFV 111
PLN02647 PLN02647
acyl-CoA thioesterase
 189-318 1.48e-16

acyl-CoA thioesterase


Pssm-ID: 215349 [Multi-domain]  Cd Length: 437  Bit Score: 79.83  E-value: 1.48e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931880 189 GVTMKLMDEVAGIVAARHCKTN--------IVTASVDAINFHDKIRKGCVITISGRMTFTSNKSMEIEVLVDADPVVDNS 260
Cdd:PLN02647 114 GKLLEDLDALAGTISVKHCSDDdsttrpllLVTASVDKIVLKKPIRVDVDLKIVGAVTWVGRSSMEIQLEVIQPTKDESN 193

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568931880 261 QKRYRAASAFFTYVSLN-QEGKPMPVPQLVPETEDEKKRFEEGKGRYLQMKAKRQGHTE 318
Cdd:PLN02647 194 TSDSVALTANFTFVARDsKTGKSAPVNRLSPETEEEKLLFEEAEARNKLRKKKRGEQKR 252
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 183-251 7.12e-15

Thioesterase superfamily; This family contains a wide variety of enzymes, principally thioesterases. This family includes 4HBT (EC 3.1.2.23) which catalyzes the final step in the biosynthesis of 4-hydroxybenzoate from 4-chlorobenzoate in the soil dwelling microbe Pseudomonas CBS-3. This family includes various cytosolic long-chain acyl-CoA thioester hydrolases. Long-chain acyl-CoA hydrolases hydrolyse palmitoyl-CoA to CoA and palmitate, they also catalyze the hydrolysis of other long chain fatty acyl-CoA thioesters.


Pssm-ID: 427116 [Multi-domain]  Cd Length: 79  Bit Score: 68.44  E-value: 7.12e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931880  183 HGFVHGGVTMKLMDEVAGIVAARHCKTNI-VTASVDAINFHDKIRKGCVITISGRMTFTSNKSMEIEVLV 251
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSQQvVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEV 70
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 10-91 7.54e-13

Thioesterase superfamily; This family contains a wide variety of enzymes, principally thioesterases. This family includes 4HBT (EC 3.1.2.23) which catalyzes the final step in the biosynthesis of 4-hydroxybenzoate from 4-chlorobenzoate in the soil dwelling microbe Pseudomonas CBS-3. This family includes various cytosolic long-chain acyl-CoA thioester hydrolases. Long-chain acyl-CoA hydrolases hydrolyse palmitoyl-CoA to CoA and palmitate, they also catalyze the hydrolysis of other long chain fatty acyl-CoA thioesters.


Pssm-ID: 427116 [Multi-domain]  Cd Length: 79  Bit Score: 63.04  E-value: 7.54e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931880   10 GNVHGGTILKMIEEAGAIISTRHCNSQngercVAALARVERTDFLSPMCIGEVAHVSAEITYTSKHSVEVQVHVMSENIL 89
Cdd:pfam03061   2 GVVHGGVYLALADEAAGAAARRLGGSQ-----QVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDEDGR 76


                  ..
gi 568931880   90 TG 91
Cdd:pfam03061  77 LV 78
 
Name Accession Description Interval E-value
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
163-305 6.29e-49

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 160.35  E-value: 6.29e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931880 163 TVSYSQSSLIHLVGPSDCTLHGFVHGGVTMKLMDEVAGIVAARHCKTNIVTASVDAINFHDKIRKGCVITISGRMTFTSN 242
Cdd:COG1607    1 PLPDSELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGR 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568931880 243 KSMEIEVLVDADPVvdNSQKRYRAASAFFTYVSLNQEGKPMPVPQLVPETEDEKKRFEEGKGR 305
Cdd:COG1607   81 TSMEVGVEVWAEDL--RTGERRLVTEAYFTFVAVDEDGKPRPVPPLIPETEEEKRLFEEALRR 141
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 163-286 2.69e-41

Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes deacylate long-chain fatty acids by hydrolyzing acyl-CoA thioesters to free fatty acids and CoA-SH. Eukaryotic members of this family are expressed in brain, testis, and brown adipose tissues. The archeal and eukaryotic members of this family have two tandem copies of the conserved hot dog fold, while most bacterial members have only one copy.


Pssm-ID: 239526 [Multi-domain]  Cd Length: 123  Bit Score: 139.63  E-value: 2.69e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931880 163 TVSYSQSSLIHLVGPSDCTLHGFVHGGVTMKLMDEVAGIVAARHCKTNIVTASVDAINFHDKIRKGCVITISGRMTFTSN 242
Cdd:cd03442    2 PMEDTELSTRELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGGRVVTASVDRIDFLKPVRVGDVVELSARVVYTGR 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 568931880 243 KSMEIEVLVDAdpVVDNSQKRYRAASAFFTYVSLNQEGKPMPVP 286
Cdd:cd03442   82 TSMEVGVEVEA--EDPLTGERRLVTSAYFTFVALDEDGKPRPVP 123
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
1-144 1.74e-30

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 112.58  E-value: 1.74e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931880   1 MRPDDANVAGNVHGGTILKMIEEAGAIISTRHCNSqngeRCVAalARVERTDFLSPMCIGEVAHVSAEITYTSKHSVEVQ 80
Cdd:COG1607   13 VMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARG----RVVT--ASVDSVDFLRPVRVGDIVELYARVVRVGRTSMEVG 86

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568931880  81 VHVMSENILTGTKKLTNKATLWYVplslkNVD---KVLEVPPIVylrqEQEEEGRKRYEAQKLERME 144
Cdd:COG1607   87 VEVWAEDLRTGERRLVTEAYFTFV-----AVDedgKPRPVPPLI----PETEEEKRLFEEALRRREL 144
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 1-104 6.51e-30

Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes deacylate long-chain fatty acids by hydrolyzing acyl-CoA thioesters to free fatty acids and CoA-SH. Eukaryotic members of this family are expressed in brain, testis, and brown adipose tissues. The archeal and eukaryotic members of this family have two tandem copies of the conserved hot dog fold, while most bacterial members have only one copy.


Pssm-ID: 239526 [Multi-domain]  Cd Length: 123  Bit Score: 110.35  E-value: 6.51e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931880   1 MRPDDANVAGNVHGGTILKMIEEAGAIISTRHCNSqngeRCVaaLARVERTDFLSPMCIGEVAHVSAEITYTSKHSVEVQ 80
Cdd:cd03442   14 VLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGG----RVV--TASVDRIDFLKPVRVGDVVELSARVVYTGRTSMEVG 87

                         90       100
                 ....*....|....*....|....
gi 568931880  81 VHVMSENILTGTKKLTNKATLWYV 104
Cdd:cd03442   88 VEVEAEDPLTGERRLVTSAYFTFV 111
PLN02647 PLN02647
acyl-CoA thioesterase
 189-318 1.48e-16

acyl-CoA thioesterase


Pssm-ID: 215349 [Multi-domain]  Cd Length: 437  Bit Score: 79.83  E-value: 1.48e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931880 189 GVTMKLMDEVAGIVAARHCKTN--------IVTASVDAINFHDKIRKGCVITISGRMTFTSNKSMEIEVLVDADPVVDNS 260
Cdd:PLN02647 114 GKLLEDLDALAGTISVKHCSDDdsttrpllLVTASVDKIVLKKPIRVDVDLKIVGAVTWVGRSSMEIQLEVIQPTKDESN 193

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568931880 261 QKRYRAASAFFTYVSLN-QEGKPMPVPQLVPETEDEKKRFEEGKGRYLQMKAKRQGHTE 318
Cdd:PLN02647 194 TSDSVALTANFTFVARDsKTGKSAPVNRLSPETEEEKLLFEEAEARNKLRKKKRGEQKR 252
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 183-251 7.12e-15

Thioesterase superfamily; This family contains a wide variety of enzymes, principally thioesterases. This family includes 4HBT (EC 3.1.2.23) which catalyzes the final step in the biosynthesis of 4-hydroxybenzoate from 4-chlorobenzoate in the soil dwelling microbe Pseudomonas CBS-3. This family includes various cytosolic long-chain acyl-CoA thioester hydrolases. Long-chain acyl-CoA hydrolases hydrolyse palmitoyl-CoA to CoA and palmitate, they also catalyze the hydrolysis of other long chain fatty acyl-CoA thioesters.


Pssm-ID: 427116 [Multi-domain]  Cd Length: 79  Bit Score: 68.44  E-value: 7.12e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931880  183 HGFVHGGVTMKLMDEVAGIVAARHCKTNI-VTASVDAINFHDKIRKGCVITISGRMTFTSNKSMEIEVLV 251
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSQQvVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEV 70
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 10-91 7.54e-13

Thioesterase superfamily; This family contains a wide variety of enzymes, principally thioesterases. This family includes 4HBT (EC 3.1.2.23) which catalyzes the final step in the biosynthesis of 4-hydroxybenzoate from 4-chlorobenzoate in the soil dwelling microbe Pseudomonas CBS-3. This family includes various cytosolic long-chain acyl-CoA thioester hydrolases. Long-chain acyl-CoA hydrolases hydrolyse palmitoyl-CoA to CoA and palmitate, they also catalyze the hydrolysis of other long chain fatty acyl-CoA thioesters.


Pssm-ID: 427116 [Multi-domain]  Cd Length: 79  Bit Score: 63.04  E-value: 7.54e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931880   10 GNVHGGTILKMIEEAGAIISTRHCNSQngercVAALARVERTDFLSPMCIGEVAHVSAEITYTSKHSVEVQVHVMSENIL 89
Cdd:pfam03061   2 GVVHGGVYLALADEAAGAAARRLGGSQ-----QVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDEDGR 76


                  ..
gi 568931880   90 TG 91
Cdd:pfam03061  77 LV 78
PRK10694 PRK10694
acyl-CoA thioester hydrolase YciA;
174-287 1.56e-12

acyl-CoA thioester hydrolase YciA;


Pssm-ID: 236736 [Multi-domain]  Cd Length: 133  Bit Score: 63.72  E-value: 1.56e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931880 174 LVGPSDCTLHGFVHGGVTMKLMDEVAGIVAARHCKTNIVTASVDAINFHDKIRKGCVITISGRMTFTSNKSMEIEV---- 249
Cdd:PRK10694  17 LAMPADTNANGDIFGGWLMSQMDIGGAILAKEIAHGRVVTVRVEGMTFLRPVAVGDVVCCYARCVKTGTTSISINIevwv 96

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 568931880 250 -LVDADPVvdnsQKRYRAASAFFTYVSLNQEGKPMPVPQ 287
Cdd:PRK10694  97 kKVASEPI----GQRYKATEALFTYVAVDPEGKPRALPV 131
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 170-274 3.09e-10

The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl carrier protein (ACP)-dehydratase) structure and subsequently in 4HBT (4-hydroxybenzoyl-CoA thioesterase) from Pseudomonas. A number of other seemingly unrelated proteins also share the hotdog fold. These proteins have related, but distinct, catalytic activities that include metabolic roles such as thioester hydrolysis in fatty acid metabolism, and degradation of phenylacetic acid and the environmental pollutant 4-chlorobenzoate. This superfamily also includes the PaaI-like protein FapR, a non-catalytic bacterial homolog involved in transcriptional regulation of fatty acid biosynthesis.


Pssm-ID: 239524 [Multi-domain]  Cd Length: 100  Bit Score: 56.33  E-value: 3.09e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931880 170 SLIHLVGPSDCTLHGFVHGGVTMKLMDEVAGIVAARHCKTNIVTASVDA-INFHDKIRKGCVITISGRMTFTSNKSMEIE 248
Cdd:cd03440    2 VLRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLGGRGLGAVTLSLdVRFLRPVRPGDTLTVEAEVVRVGRSSVTVE 81

                         90       100
                 ....*....|....*....|....*.
gi 568931880 249 VLvdadpVVDNSQKryRAASAFFTYV 274
Cdd:cd03440   82 VE-----VRNEDGK--LVATATATFV 100
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 183-254 5.24e-08

Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 51.10  E-value: 5.24e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568931880 183 HGFVHGGVTMKLMDEVAGIVAARHCKTNIVTASVDA-INFHDKIRKGCVITISGRMTFTSNKSMEIEV-LVDAD 254
Cdd:COG2050   47 PGTVHGGALAALADSAAGLAANSALPPGRRAVTIELnINFLRPARLGDRLTAEARVVRRGRRLAVVEVeVTDED 120
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 2-104 1.29e-07

The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl carrier protein (ACP)-dehydratase) structure and subsequently in 4HBT (4-hydroxybenzoyl-CoA thioesterase) from Pseudomonas. A number of other seemingly unrelated proteins also share the hotdog fold. These proteins have related, but distinct, catalytic activities that include metabolic roles such as thioester hydrolysis in fatty acid metabolism, and degradation of phenylacetic acid and the environmental pollutant 4-chlorobenzoate. This superfamily also includes the PaaI-like protein FapR, a non-catalytic bacterial homolog involved in transcriptional regulation of fatty acid biosynthesis.


Pssm-ID: 239524 [Multi-domain]  Cd Length: 100  Bit Score: 49.01  E-value: 1.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931880   2 RPDDANVAGNVHGGTILKMIEEAGAIISTRHCnsqnGERCVAALARVErTDFLSPMCIGEVAHVSAEITYTSKHSVEVQV 81
Cdd:cd03440    8 TPEDIDGGGIVHGGLLLALADEAAGAAAARLG----GRGLGAVTLSLD-VRFLRPVRPGDTLTVEAEVVRVGRSSVTVEV 82

                         90       100
                 ....*....|....*....|...
gi 568931880  82 HVMSEniltgTKKLTNKATLWYV 104
Cdd:cd03440   83 EVRNE-----DGKLVATATATFV 100
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 183-257 1.15e-06

PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several proteins responsible for phenylacetic acid (PA) degradation in bacteria. Although orthologs of PaaI exist in archaea and eukaryotes, their function has not been determined. Sequence similarity between PaaI, E. coli medium chain acyl-CoA thioesterase II, and human thioesterase III suggests they all belong to the same thioesterase superfamily. The conserved fold present in these thioesterases is referred to as an asymmetric hot dog fold, similar to those of 4-hydroxybenzoyl-CoA thioesterase (4HBT) and the beta-hydroxydecanoyl-ACP dehydratases (FabA/FabZ).


Pssm-ID: 239527 [Multi-domain]  Cd Length: 113  Bit Score: 46.78  E-value: 1.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931880 183 HGFVHGGVTMKLMDEVAGIVAARHCKTNIVTASVD-AINFHDKIRKGCVITIS------GRMTFTsnksmEIEVLVDADP 255
Cdd:cd03443   28 GGIVHGGAIATLADTAGGLAALSALPPGALAVTVDlNVNYLRPARGGDLTARArvvklgRRLAVV-----EVEVTDEDGK 102


                 ..
gi 568931880 256 VV 257
Cdd:cd03443  103 LV 104
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 1-87 9.62e-04

Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 38.77  E-value: 9.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931880   1 MRPDDANVAGNVHGGTILKMIEEAGAIISTRHCNsqNGERCVAALARVertDFLSPMCIGEVAHVSAEITYTSKHSVEVQ 80
Cdd:COG2050   39 VRPEHLNPPGTVHGGALAALADSAAGLAANSALP--PGRRAVTIELNI---NFLRPARLGDRLTAEARVVRRGRRLAVVE 113


                 ....*..
gi 568931880  81 VHVMSEN 87
Cdd:COG2050  114 VEVTDED 120
 
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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