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Conserved domains on  [gi|1603768531|ref|NP_001356203|]
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cytosolic acyl coenzyme A thioester hydrolase isoform 5 [Mus musculus]

Protein Classification

acyl-CoA thioesterase( domain architecture ID 10787833)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 180-303 3.10e-40

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: 137.32  E-value: 3.10e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768531 180 TVSYSQSSLIHLVGPSDCTLHGFVHGGVTMKLMDEVAGIVAARHCKTNIVTASVDAINFHDKIRKGCVITISGRMTFTSN 259
Cdd:cd03442     2 PMEDTELSTRELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGGRVVTASVDRIDFLKPVRVGDVVELSARVVYTGR 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1603768531 260 KSMEIEVLVDAdpVVDNSQKRYRAASAFFTYVSLNQEGKPMPVP 303
Cdd:cd03442    82 TSMEVGVEVEA--EDPLTGERRLVTSAYFTFVALDEDGKPRPVP 123
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
16-161 1.91e-30

Acyl-CoA hydrolase [Lipid transport and metabolism];


:

Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 112.58  E-value: 1.91e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768531  16 RIMRPDDANVAGNVHGGTILKMIEEAGAIISTRHCNSqngeRCVAalARVERTDFLSPMCIGEVAHVSAEITYTSKHSVE 95
Cdd:COG1607    11 ELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARG----RVVT--ASVDSVDFLRPVRVGDIVELYARVVRVGRTSME 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1603768531  96 VQVHVMSENILTGTKKLTNKATLWYVplslkNVD---KVLEVPPIVylrqEQEEEGRKRYEAQKLERME 161
Cdd:COG1607    85 VGVEVWAEDLRTGERRLVTEAYFTFV-----AVDedgKPRPVPPLI----PETEEEKRLFEEALRRREL 144
 
Name Accession Description Interval E-value
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 180-303 3.10e-40

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: 137.32  E-value: 3.10e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768531 180 TVSYSQSSLIHLVGPSDCTLHGFVHGGVTMKLMDEVAGIVAARHCKTNIVTASVDAINFHDKIRKGCVITISGRMTFTSN 259
Cdd:cd03442     2 PMEDTELSTRELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGGRVVTASVDRIDFLKPVRVGDVVELSARVVYTGR 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1603768531 260 KSMEIEVLVDAdpVVDNSQKRYRAASAFFTYVSLNQEGKPMPVP 303
Cdd:cd03442    82 TSMEVGVEVEA--EDPLTGERRLVTSAYFTFVALDEDGKPRPVP 123
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
180-312 9.38e-40

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 136.85  E-value: 9.38e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768531 180 TVSYSQSSLIHLVGPSDCTLHGFVHGGVTMKLMDEVAGIVAARHCKTNIVTASVDAINFHDKIRKGCVITISGRMTFTSN 259
Cdd:COG1607     1 PLPDSELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGR 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1603768531 260 KSMEIEVLVDADPVvdNSQKRYRAASAFFTYVSLNQEGKPMPVPQLV--------------RRRMRR 312
Cdd:COG1607    81 TSMEVGVEVWAEDL--RTGERRLVTEAYFTFVAVDEDGKPRPVPPLIpeteeekrlfeealRRRELR 145
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
16-161 1.91e-30

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 112.58  E-value: 1.91e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768531  16 RIMRPDDANVAGNVHGGTILKMIEEAGAIISTRHCNSqngeRCVAalARVERTDFLSPMCIGEVAHVSAEITYTSKHSVE 95
Cdd:COG1607    11 ELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARG----RVVT--ASVDSVDFLRPVRVGDIVELYARVVRVGRTSME 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1603768531  96 VQVHVMSENILTGTKKLTNKATLWYVplslkNVD---KVLEVPPIVylrqEQEEEGRKRYEAQKLERME 161
Cdd:COG1607    85 VGVEVWAEDLRTGERRLVTEAYFTFV-----AVDedgKPRPVPPLI----PETEEEKRLFEEALRRREL 144
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 16-121 7.78e-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: 109.97  E-value: 7.78e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768531  16 RIMRPDDANVAGNVHGGTILKMIEEAGAIISTRHCNSqngeRCVaaLARVERTDFLSPMCIGEVAHVSAEITYTSKHSVE 95
Cdd:cd03442    12 ELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGG----RVV--TASVDRIDFLKPVRVGDVVELSARVVYTGRTSME 85

                          90       100
                  ....*....|....*....|....*.
gi 1603768531  96 VQVHVMSENILTGTKKLTNKATLWYV 121
Cdd:cd03442    86 VGVEVEAEDPLTGERRLVTSAYFTFV 111
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 200-268 2.06e-14

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: 67.28  E-value: 2.06e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768531 200 HGFVHGGVTMKLMDEVAGIVAARHCKTNI-VTASVDAINFHDKIRKGCVITISGRMTFTSNKSMEIEVLV 268
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSQQvVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEV 70
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 27-108 1.97e-12

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: 61.89  E-value: 1.97e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768531  27 GNVHGGTILKMIEEAGAIISTRHCNSQngercVAALARVERTDFLSPMCIGEVAHVSAEITYTSKHSVEVQVHVMSENIL 106
Cdd:pfam03061   2 GVVHGGVYLALADEAAGAAARRLGGSQ-----QVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDEDGR 76


                  ..
gi 1603768531 107 TG 108
Cdd:pfam03061  77 LV 78
PRK10694 PRK10694
acyl-CoA thioester hydrolase YciA;
191-304 3.18e-12

acyl-CoA thioester hydrolase YciA;


Pssm-ID: 236736 [Multi-domain]  Cd Length: 133  Bit Score: 62.95  E-value: 3.18e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768531 191 LVGPSDCTLHGFVHGGVTMKLMDEVAGIVAARHCKTNIVTASVDAINFHDKIRKGCVITISGRMTFTSNKSMEIEV---- 266
Cdd:PRK10694   17 LAMPADTNANGDIFGGWLMSQMDIGGAILAKEIAHGRVVTVRVEGMTFLRPVAVGDVVCCYARCVKTGTTSISINIevwv 96

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1603768531 267 -LVDADPVvdnsQKRYRAASAFFTYVSLNQEGKPMPVPQ 304
Cdd:PRK10694   97 kKVASEPI----GQRYKATEALFTYVAVDPEGKPRALPV 131
 
Name Accession Description Interval E-value
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 180-303 3.10e-40

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: 137.32  E-value: 3.10e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768531 180 TVSYSQSSLIHLVGPSDCTLHGFVHGGVTMKLMDEVAGIVAARHCKTNIVTASVDAINFHDKIRKGCVITISGRMTFTSN 259
Cdd:cd03442     2 PMEDTELSTRELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGGRVVTASVDRIDFLKPVRVGDVVELSARVVYTGR 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1603768531 260 KSMEIEVLVDAdpVVDNSQKRYRAASAFFTYVSLNQEGKPMPVP 303
Cdd:cd03442    82 TSMEVGVEVEA--EDPLTGERRLVTSAYFTFVALDEDGKPRPVP 123
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
180-312 9.38e-40

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 136.85  E-value: 9.38e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768531 180 TVSYSQSSLIHLVGPSDCTLHGFVHGGVTMKLMDEVAGIVAARHCKTNIVTASVDAINFHDKIRKGCVITISGRMTFTSN 259
Cdd:COG1607     1 PLPDSELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGR 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1603768531 260 KSMEIEVLVDADPVvdNSQKRYRAASAFFTYVSLNQEGKPMPVPQLV--------------RRRMRR 312
Cdd:COG1607    81 TSMEVGVEVWAEDL--RTGERRLVTEAYFTFVAVDEDGKPRPVPPLIpeteeekrlfeealRRRELR 145
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
16-161 1.91e-30

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 112.58  E-value: 1.91e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768531  16 RIMRPDDANVAGNVHGGTILKMIEEAGAIISTRHCNSqngeRCVAalARVERTDFLSPMCIGEVAHVSAEITYTSKHSVE 95
Cdd:COG1607    11 ELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARG----RVVT--ASVDSVDFLRPVRVGDIVELYARVVRVGRTSME 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1603768531  96 VQVHVMSENILTGTKKLTNKATLWYVplslkNVD---KVLEVPPIVylrqEQEEEGRKRYEAQKLERME 161
Cdd:COG1607    85 VGVEVWAEDLRTGERRLVTEAYFTFV-----AVDedgKPRPVPPLI----PETEEEKRLFEEALRRREL 144
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 16-121 7.78e-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: 109.97  E-value: 7.78e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768531  16 RIMRPDDANVAGNVHGGTILKMIEEAGAIISTRHCNSqngeRCVaaLARVERTDFLSPMCIGEVAHVSAEITYTSKHSVE 95
Cdd:cd03442    12 ELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGG----RVV--TASVDRIDFLKPVRVGDVVELSARVVYTGRTSME 85

                          90       100
                  ....*....|....*....|....*.
gi 1603768531  96 VQVHVMSENILTGTKKLTNKATLWYV 121
Cdd:cd03442    86 VGVEVEAEDPLTGERRLVTSAYFTFV 111
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 200-268 2.06e-14

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: 67.28  E-value: 2.06e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768531 200 HGFVHGGVTMKLMDEVAGIVAARHCKTNI-VTASVDAINFHDKIRKGCVITISGRMTFTSNKSMEIEVLV 268
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSQQvVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEV 70
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 27-108 1.97e-12

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: 61.89  E-value: 1.97e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768531  27 GNVHGGTILKMIEEAGAIISTRHCNSQngercVAALARVERTDFLSPMCIGEVAHVSAEITYTSKHSVEVQVHVMSENIL 106
Cdd:pfam03061   2 GVVHGGVYLALADEAAGAAARRLGGSQ-----QVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDEDGR 76


                  ..
gi 1603768531 107 TG 108
Cdd:pfam03061  77 LV 78
PRK10694 PRK10694
acyl-CoA thioester hydrolase YciA;
191-304 3.18e-12

acyl-CoA thioester hydrolase YciA;


Pssm-ID: 236736 [Multi-domain]  Cd Length: 133  Bit Score: 62.95  E-value: 3.18e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768531 191 LVGPSDCTLHGFVHGGVTMKLMDEVAGIVAARHCKTNIVTASVDAINFHDKIRKGCVITISGRMTFTSNKSMEIEV---- 266
Cdd:PRK10694   17 LAMPADTNANGDIFGGWLMSQMDIGGAILAKEIAHGRVVTVRVEGMTFLRPVAVGDVVCCYARCVKTGTTSISINIevwv 96

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1603768531 267 -LVDADPVvdnsQKRYRAASAFFTYVSLNQEGKPMPVPQ 304
Cdd:PRK10694   97 kKVASEPI----GQRYKATEALFTYVAVDPEGKPRALPV 131
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 187-291 1.41e-09

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: 54.40  E-value: 1.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768531 187 SLIHLVGPSDCTLHGFVHGGVTMKLMDEVAGIVAARHCKTNIVTASVDA-INFHDKIRKGCVITISGRMTFTSNKSMEIE 265
Cdd:cd03440     2 VLRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLGGRGLGAVTLSLdVRFLRPVRPGDTLTVEAEVVRVGRSSVTVE 81

                          90       100
                  ....*....|....*....|....*.
gi 1603768531 266 VLVDAdpvvdnsQKRYRAASAFFTYV 291
Cdd:cd03440    82 VEVRN-------EDGKLVATATATFV 100
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 200-271 1.33e-07

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 49.94  E-value: 1.33e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1603768531 200 HGFVHGGVTMKLMDEVAGIVAARHCKTNIVTASVDA-INFHDKIRKGCVITISGRMTFTSNKSMEIEV-LVDAD 271
Cdd:COG2050    47 PGTVHGGALAALADSAAGLAANSALPPGRRAVTIELnINFLRPARLGDRLTAEARVVRRGRRLAVVEVeVTDED 120
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 16-121 3.38e-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: 47.86  E-value: 3.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768531  16 RIMRPDDANVAGNVHGGTILKMIEEAGAIISTRHCnsqnGERCVAALARVErTDFLSPMCIGEVAHVSAEITYTSKHSVE 95
Cdd:cd03440     5 LTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLG----GRGLGAVTLSLD-VRFLRPVRPGDTLTVEAEVVRVGRSSVT 79

                          90       100
                  ....*....|....*....|....*.
gi 1603768531  96 VQVHVMSEniltgTKKLTNKATLWYV 121
Cdd:cd03440    80 VEVEVRNE-----DGKLVATATATFV 100
PLN02647 PLN02647
acyl-CoA thioesterase
 206-306 7.26e-07

acyl-CoA thioesterase


Pssm-ID: 215349 [Multi-domain]  Cd Length: 437  Bit Score: 50.56  E-value: 7.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768531 206 GVTMKLMDEVAGIVAARHCKTN--------IVTASVDAINFHDKIRKGCVITISGRMTFTSNKSMEIEVLVDADPVVDNS 277
Cdd:PLN02647  114 GKLLEDLDALAGTISVKHCSDDdsttrpllLVTASVDKIVLKKPIRVDVDLKIVGAVTWVGRSSMEIQLEVIQPTKDESN 193

                          90       100       110
                  ....*....|....*....|....*....|
gi 1603768531 278 QKRYRAASAFFTYVSLN-QEGKPMPVPQLV 306
Cdd:PLN02647  194 TSDSVALTANFTFVARDsKTGKSAPVNRLS 223
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 200-274 3.38e-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: 45.24  E-value: 3.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768531 200 HGFVHGGVTMKLMDEVAGIVAARHCKTNIVTASVD-AINFHDKIRKGCVITIS------GRMTFTsnksmEIEVLVDADP 272
Cdd:cd03443    28 GGIVHGGAIATLADTAGGLAALSALPPGALAVTVDlNVNYLRPARGGDLTARArvvklgRRLAVV-----EVEVTDEDGK 102


                  ..
gi 1603768531 273 VV 274
Cdd:cd03443   103 LV 104
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 18-104 1.97e-03

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 38.00  E-value: 1.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603768531  18 MRPDDANVAGNVHGGTILKMIEEAGAIISTRHCNsqNGERCVAALARVertDFLSPMCIGEVAHVSAEITYTSKHSVEVQ 97
Cdd:COG2050    39 VRPEHLNPPGTVHGGALAALADSAAGLAANSALP--PGRRAVTIELNI---NFLRPARLGDRLTAEARVVRRGRRLAVVE 113


                  ....*..
gi 1603768531  98 VHVMSEN 104
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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