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Conserved domains on  [gi|61651654|dbj|BAD91166|]
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50-kDa brain acyl-CoA hydrolase [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; belongs to the Hotdog fold superfamily

CATH:  3.10.129.10
EC:  3.1.2.-
Gene Ontology:  GO:0016790|GO:0016787
PubMed:  15307895

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];
221-363 1.32e-48

Acyl-CoA hydrolase [Lipid transport and metabolism];


:

Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 161.12  E-value: 1.32e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61651654 221 TVSYSQSSLIHLVGPSDCTLHGFVHGGVTMKLMDEVAGIVAARHCKTNIVTASVDAINFHDKIRKGCVITISGRMTFTSN 300
Cdd:COG1607   1 PLPDSELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGR 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 61651654 301 KSMEIEVLVDADPVvdNSQKRYRAASAFFTYVSLNQEGKPMPVPQLVPETEDEKKRFEEGKGR 363
Cdd:COG1607  81 TSMEVGVEVWAEDL--RTGERRLVTEAYFTFVAVDEDGKPRPVPPLIPETEEEKRLFEEALRR 141
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
57-202 5.75e-31

Acyl-CoA hydrolase [Lipid transport and metabolism];


:

Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 114.89  E-value: 5.75e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61651654  57 RIMRPDDANVAGNVHGGTILKMIEEAGAIISTRHCNSqngeRCVAalARVERTDFLSPMCIGEVAHVSAEITYTSKHSVE 136
Cdd:COG1607  11 ELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARG----RVVT--ASVDSVDFLRPVRVGDIVELYARVVRVGRTSME 84

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 61651654 137 VQVHVMSENILTGTKKLTNKATLWYVplslkNVD---KVLEVPPIVylrqEQEEEGRKRYEAQKLERME 202
Cdd:COG1607  85 VGVEVWAEDLRTGERRLVTEAYFTFV-----AVDedgKPRPVPPLI----PETEEEKRLFEEALRRREL 144
 
Name Accession Description Interval E-value
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
221-363 1.32e-48

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 161.12  E-value: 1.32e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61651654 221 TVSYSQSSLIHLVGPSDCTLHGFVHGGVTMKLMDEVAGIVAARHCKTNIVTASVDAINFHDKIRKGCVITISGRMTFTSN 300
Cdd:COG1607   1 PLPDSELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGR 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 61651654 301 KSMEIEVLVDADPVvdNSQKRYRAASAFFTYVSLNQEGKPMPVPQLVPETEDEKKRFEEGKGR 363
Cdd:COG1607  81 TSMEVGVEVWAEDL--RTGERRLVTEAYFTFVAVDEDGKPRPVPPLIPETEEEKRLFEEALRR 141
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 221-344 8.32e-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: 140.01  E-value: 8.32e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61651654 221 TVSYSQSSLIHLVGPSDCTLHGFVHGGVTMKLMDEVAGIVAARHCKTNIVTASVDAINFHDKIRKGCVITISGRMTFTSN 300
Cdd:cd03442   2 PMEDTELSTRELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGGRVVTASVDRIDFLKPVRVGDVVELSARVVYTGR 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 61651654 301 KSMEIEVLVDAdpVVDNSQKRYRAASAFFTYVSLNQEGKPMPVP 344
Cdd:cd03442  82 TSMEVGVEVEA--EDPLTGERRLVTSAYFTFVALDEDGKPRPVP 123
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
57-202 5.75e-31

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 114.89  E-value: 5.75e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61651654  57 RIMRPDDANVAGNVHGGTILKMIEEAGAIISTRHCNSqngeRCVAalARVERTDFLSPMCIGEVAHVSAEITYTSKHSVE 136
Cdd:COG1607  11 ELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARG----RVVT--ASVDSVDFLRPVRVGDIVELYARVVRVGRTSME 84

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 61651654 137 VQVHVMSENILTGTKKLTNKATLWYVplslkNVD---KVLEVPPIVylrqEQEEEGRKRYEAQKLERME 202
Cdd:COG1607  85 VGVEVWAEDLRTGERRLVTEAYFTFV-----AVDedgKPRPVPPLI----PETEEEKRLFEEALRRREL 144
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 57-162 2.25e-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: 112.66  E-value: 2.25e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61651654  57 RIMRPDDANVAGNVHGGTILKMIEEAGAIISTRHCNSqngeRCVaaLARVERTDFLSPMCIGEVAHVSAEITYTSKHSVE 136
Cdd:cd03442  12 ELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGG----RVV--TASVDRIDFLKPVRVGDVVELSARVVYTGRTSME 85

                        90       100
                ....*....|....*....|....*.
gi 61651654 137 VQVHVMSENILTGTKKLTNKATLWYV 162
Cdd:cd03442  86 VGVEVEAEDPLTGERRLVTSAYFTFV 111
PLN02647 PLN02647
acyl-CoA thioesterase
 247-376 3.08e-16

acyl-CoA thioesterase


Pssm-ID: 215349 [Multi-domain]  Cd Length: 437  Bit Score: 79.83  E-value: 3.08e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61651654  247 GVTMKLMDEVAGIVAARHCKTN--------IVTASVDAINFHDKIRKGCVITISGRMTFTSNKSMEIEVLVDADPVVDNS 318
Cdd:PLN02647 114 GKLLEDLDALAGTISVKHCSDDdsttrpllLVTASVDKIVLKKPIRVDVDLKIVGAVTWVGRSSMEIQLEVIQPTKDESN 193

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 61651654  319 QKRYRAASAFFTYVSLN-QEGKPMPVPQLVPETEDEKKRFEEGKGRYLQMKAKRQGHTE 376
Cdd:PLN02647 194 TSDSVALTANFTFVARDsKTGKSAPVNRLSPETEEEKLLFEEAEARNKLRKKKRGEQKR 252
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 241-309 6.04e-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: 69.21  E-value: 6.04e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61651654   241 HGFVHGGVTMKLMDEVAGIVAARHCKTNI-VTASVDAINFHDKIRKGCVITISGRMTFTSNKSMEIEVLV 309
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSQQvVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEV 70
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 68-149 5.80e-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: 63.81  E-value: 5.80e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61651654    68 GNVHGGTILKMIEEAGAIISTRHCNSQngercVAALARVERTDFLSPMCIGEVAHVSAEITYTSKHSVEVQVHVMSENIL 147
Cdd:pfam03061   2 GVVHGGVYLALADEAAGAAARRLGGSQ-----QVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDEDGR 76


                  ..
gi 61651654   148 TG 149
Cdd:pfam03061  77 LV 78
 
Name Accession Description Interval E-value
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
221-363 1.32e-48

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 161.12  E-value: 1.32e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61651654 221 TVSYSQSSLIHLVGPSDCTLHGFVHGGVTMKLMDEVAGIVAARHCKTNIVTASVDAINFHDKIRKGCVITISGRMTFTSN 300
Cdd:COG1607   1 PLPDSELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGR 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 61651654 301 KSMEIEVLVDADPVvdNSQKRYRAASAFFTYVSLNQEGKPMPVPQLVPETEDEKKRFEEGKGR 363
Cdd:COG1607  81 TSMEVGVEVWAEDL--RTGERRLVTEAYFTFVAVDEDGKPRPVPPLIPETEEEKRLFEEALRR 141
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 221-344 8.32e-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: 140.01  E-value: 8.32e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61651654 221 TVSYSQSSLIHLVGPSDCTLHGFVHGGVTMKLMDEVAGIVAARHCKTNIVTASVDAINFHDKIRKGCVITISGRMTFTSN 300
Cdd:cd03442   2 PMEDTELSTRELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGGRVVTASVDRIDFLKPVRVGDVVELSARVVYTGR 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 61651654 301 KSMEIEVLVDAdpVVDNSQKRYRAASAFFTYVSLNQEGKPMPVP 344
Cdd:cd03442  82 TSMEVGVEVEA--EDPLTGERRLVTSAYFTFVALDEDGKPRPVP 123
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
57-202 5.75e-31

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 114.89  E-value: 5.75e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61651654  57 RIMRPDDANVAGNVHGGTILKMIEEAGAIISTRHCNSqngeRCVAalARVERTDFLSPMCIGEVAHVSAEITYTSKHSVE 136
Cdd:COG1607  11 ELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARG----RVVT--ASVDSVDFLRPVRVGDIVELYARVVRVGRTSME 84

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 61651654 137 VQVHVMSENILTGTKKLTNKATLWYVplslkNVD---KVLEVPPIVylrqEQEEEGRKRYEAQKLERME 202
Cdd:COG1607  85 VGVEVWAEDLRTGERRLVTEAYFTFV-----AVDedgKPRPVPPLI----PETEEEKRLFEEALRRREL 144
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 57-162 2.25e-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: 112.66  E-value: 2.25e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61651654  57 RIMRPDDANVAGNVHGGTILKMIEEAGAIISTRHCNSqngeRCVaaLARVERTDFLSPMCIGEVAHVSAEITYTSKHSVE 136
Cdd:cd03442  12 ELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGG----RVV--TASVDRIDFLKPVRVGDVVELSARVVYTGRTSME 85

                        90       100
                ....*....|....*....|....*.
gi 61651654 137 VQVHVMSENILTGTKKLTNKATLWYV 162
Cdd:cd03442  86 VGVEVEAEDPLTGERRLVTSAYFTFV 111
PLN02647 PLN02647
acyl-CoA thioesterase
 247-376 3.08e-16

acyl-CoA thioesterase


Pssm-ID: 215349 [Multi-domain]  Cd Length: 437  Bit Score: 79.83  E-value: 3.08e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61651654  247 GVTMKLMDEVAGIVAARHCKTN--------IVTASVDAINFHDKIRKGCVITISGRMTFTSNKSMEIEVLVDADPVVDNS 318
Cdd:PLN02647 114 GKLLEDLDALAGTISVKHCSDDdsttrpllLVTASVDKIVLKKPIRVDVDLKIVGAVTWVGRSSMEIQLEVIQPTKDESN 193

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 61651654  319 QKRYRAASAFFTYVSLN-QEGKPMPVPQLVPETEDEKKRFEEGKGRYLQMKAKRQGHTE 376
Cdd:PLN02647 194 TSDSVALTANFTFVARDsKTGKSAPVNRLSPETEEEKLLFEEAEARNKLRKKKRGEQKR 252
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 241-309 6.04e-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: 69.21  E-value: 6.04e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61651654   241 HGFVHGGVTMKLMDEVAGIVAARHCKTNI-VTASVDAINFHDKIRKGCVITISGRMTFTSNKSMEIEVLV 309
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSQQvVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEV 70
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 68-149 5.80e-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: 63.81  E-value: 5.80e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61651654    68 GNVHGGTILKMIEEAGAIISTRHCNSQngercVAALARVERTDFLSPMCIGEVAHVSAEITYTSKHSVEVQVHVMSENIL 147
Cdd:pfam03061   2 GVVHGGVYLALADEAAGAAARRLGGSQ-----QVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDEDGR 76


                  ..
gi 61651654   148 TG 149
Cdd:pfam03061  77 LV 78
PRK10694 PRK10694
acyl-CoA thioester hydrolase YciA;
232-345 2.99e-12

acyl-CoA thioester hydrolase YciA;


Pssm-ID: 236736 [Multi-domain]  Cd Length: 133  Bit Score: 63.34  E-value: 2.99e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61651654  232 LVGPSDCTLHGFVHGGVTMKLMDEVAGIVAARHCKTNIVTASVDAINFHDKIRKGCVITISGRMTFTSNKSMEIEV---- 307
Cdd:PRK10694  17 LAMPADTNANGDIFGGWLMSQMDIGGAILAKEIAHGRVVTVRVEGMTFLRPVAVGDVVCCYARCVKTGTTSISINIevwv 96

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 61651654  308 -LVDADPVvdnsQKRYRAASAFFTYVSLNQEGKPMPVPQ 345
Cdd:PRK10694  97 kKVASEPI----GQRYKATEALFTYVAVDPEGKPRALPV 131
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 228-332 2.37e-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: 57.10  E-value: 2.37e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61651654 228 SLIHLVGPSDCTLHGFVHGGVTMKLMDEVAGIVAARHCKTNIVTASVDA-INFHDKIRKGCVITISGRMTFTSNKSMEIE 306
Cdd:cd03440   2 VLRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLGGRGLGAVTLSLdVRFLRPVRPGDTLTVEAEVVRVGRSSVTVE 81

                        90       100
                ....*....|....*....|....*.
gi 61651654 307 VLvdadpVVDNSQKryRAASAFFTYV 332
Cdd:cd03440  82 VE-----VRNEDGK--LVATATATFV 100
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 57-162 6.03e-08

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: 50.17  E-value: 6.03e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61651654  57 RIMRPDDANVAGNVHGGTILKMIEEAGAIISTRHCnsqnGERCVAALARVErTDFLSPMCIGEVAHVSAEITYTSKHSVE 136
Cdd:cd03440   5 LTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLG----GRGLGAVTLSLD-VRFLRPVRPGDTLTVEAEVVRVGRSSVT 79

                        90       100
                ....*....|....*....|....*.
gi 61651654 137 VQVHVMSEniltgTKKLTNKATLWYV 162
Cdd:cd03440  80 VEVEVRNE-----DGKLVATATATFV 100
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 241-312 8.22e-08

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 50.71  E-value: 8.22e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 61651654 241 HGFVHGGVTMKLMDEVAGIVAARHCKTNIVTASVDA-INFHDKIRKGCVITISGRMTFTSNKSMEIEV-LVDAD 312
Cdd:COG2050  47 PGTVHGGALAALADSAAGLAANSALPPGRRAVTIELnINFLRPARLGDRLTAEARVVRRGRRLAVVEVeVTDED 120
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 241-315 1.66e-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: 46.40  E-value: 1.66e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61651654 241 HGFVHGGVTMKLMDEVAGIVAARHCKTNIVTASVD-AINFHDKIRKGCVITIS------GRMTFTsnksmEIEVLVDADP 313
Cdd:cd03443  28 GGIVHGGAIATLADTAGGLAALSALPPGALAVTVDlNVNYLRPARGGDLTARArvvklgRRLAVV-----EVEVTDEDGK 102


                ..
gi 61651654 314 VV 315
Cdd:cd03443 103 LV 104
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 59-145 1.39e-03

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 38.77  E-value: 1.39e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61651654  59 MRPDDANVAGNVHGGTILKMIEEAGAIISTRHCNsqNGERCVAALARVertDFLSPMCIGEVAHVSAEITYTSKHSVEVQ 138
Cdd:COG2050  39 VRPEHLNPPGTVHGGALAALADSAAGLAANSALP--PGRRAVTIELNI---NFLRPARLGDRLTAEARVVRRGRRLAVVE 113


                ....*..
gi 61651654 139 VHVMSEN 145
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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