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Conserved domains on  [gi|32528282|ref|NP_863654|]
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cytosolic acyl coenzyme A thioester hydrolase isoform hBACHb [Homo sapiens]

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];
222-364 2.98e-46

Acyl-CoA hydrolase [Lipid transport and metabolism];


:

Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 154.95  E-value: 2.98e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528282 222 TVSYSQSSLIHLVGPSDCTLHGFVHGGVTMKLMDEVAGIVAARHCKTNIVTASVDAINFHDKIRKGCVITISGRMTFTSN 301
Cdd:COG1607   1 PLPDSELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGR 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32528282 302 KSMEIEVLVDADPVvdSSQKRYRAASAFFTYVSLSQEGRSLPVPQLVPETEDEKKRFEEGKGR 364
Cdd:COG1607  81 TSMEVGVEVWAEDL--RTGERRLVTEAYFTFVAVDEDGKPRPVPPLIPETEEEKRLFEEALRR 141
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
49-203 2.07e-30

Acyl-CoA hydrolase [Lipid transport and metabolism];


:

Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 113.35  E-value: 2.07e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528282  49 PPCGACITGRIMRPDDANVAGNVHGGTILKMIEEAGAIISTRHCNSqngeRCVAalARVERTDFLSPMCIGEVAHVSAEI 128
Cdd:COG1607   2 LPDSELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARG----RVVT--ASVDSVDFLRPVRVGDIVELYARV 75

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 32528282 129 TYTSKHSVEVQVNVMSENILTGAKKLTNKATLWYVplslkNVD---KVLEVPPVVysrqEQEEEGRKRYEAQKLERME 203
Cdd:COG1607  76 VRVGRTSMEVGVEVWAEDLRTGERRLVTEAYFTFV-----AVDedgKPRPVPPLI----PETEEEKRLFEEALRRREL 144
 
Name Accession Description Interval E-value
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
222-364 2.98e-46

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 154.95  E-value: 2.98e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528282 222 TVSYSQSSLIHLVGPSDCTLHGFVHGGVTMKLMDEVAGIVAARHCKTNIVTASVDAINFHDKIRKGCVITISGRMTFTSN 301
Cdd:COG1607   1 PLPDSELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGR 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32528282 302 KSMEIEVLVDADPVvdSSQKRYRAASAFFTYVSLSQEGRSLPVPQLVPETEDEKKRFEEGKGR 364
Cdd:COG1607  81 TSMEVGVEVWAEDL--RTGERRLVTEAYFTFVAVDEDGKPRPVPPLIPETEEEKRLFEEALRR 141
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 222-345 6.13e-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: 137.70  E-value: 6.13e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528282 222 TVSYSQSSLIHLVGPSDCTLHGFVHGGVTMKLMDEVAGIVAARHCKTNIVTASVDAINFHDKIRKGCVITISGRMTFTSN 301
Cdd:cd03442   2 PMEDTELSTRELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGGRVVTASVDRIDFLKPVRVGDVVELSARVVYTGR 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 32528282 302 KSMEIEVLVDAdpVVDSSQKRYRAASAFFTYVSLSQEGRSLPVP 345
Cdd:cd03442  82 TSMEVGVEVEA--EDPLTGERRLVTSAYFTFVALDEDGKPRPVP 123
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
49-203 2.07e-30

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 113.35  E-value: 2.07e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528282  49 PPCGACITGRIMRPDDANVAGNVHGGTILKMIEEAGAIISTRHCNSqngeRCVAalARVERTDFLSPMCIGEVAHVSAEI 128
Cdd:COG1607   2 LPDSELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARG----RVVT--ASVDSVDFLRPVRVGDIVELYARV 75

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 32528282 129 TYTSKHSVEVQVNVMSENILTGAKKLTNKATLWYVplslkNVD---KVLEVPPVVysrqEQEEEGRKRYEAQKLERME 203
Cdd:COG1607  76 VRVGRTSMEVGVEVWAEDLRTGERRLVTEAYFTFV-----AVDedgKPRPVPPLI----PETEEEKRLFEEALRRREL 144
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 48-163 4.51e-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: 111.89  E-value: 4.51e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528282  48 LPPCGACITGRIMRPDDANVAGNVHGGTILKMIEEAGAIISTRHCNSqngeRCVaaLARVERTDFLSPMCIGEVAHVSAE 127
Cdd:cd03442   2 PMEDTELSTRELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGG----RVV--TASVDRIDFLKPVRVGDVVELSAR 75

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 32528282 128 ITYTSKHSVEVQVNVMSENILTGAKKLTNKATLWYV 163
Cdd:cd03442  76 VVYTGRTSMEVGVEVEAEDPLTGERRLVTSAYFTFV 111
PLN02647 PLN02647
acyl-CoA thioesterase
 248-377 4.26e-17

acyl-CoA thioesterase


Pssm-ID: 215349 [Multi-domain]  Cd Length: 437  Bit Score: 82.14  E-value: 4.26e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528282  248 GVTMKLMDEVAGIVAARHCKTN--------IVTASVDAINFHDKIRKGCVITISGRMTFTSNKSMEIEVLVDADPVVDSS 319
Cdd:PLN02647 114 GKLLEDLDALAGTISVKHCSDDdsttrpllLVTASVDKIVLKKPIRVDVDLKIVGAVTWVGRSSMEIQLEVIQPTKDESN 193

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 32528282  320 QKRYRAASAFFTYVSL-SQEGRSLPVPQLVPETEDEKKRFEEGKGRYLQMKAKRQGHAE 377
Cdd:PLN02647 194 TSDSVALTANFTFVARdSKTGKSAPVNRLSPETEEEKLLFEEAEARNKLRKKKRGEQKR 252
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 242-310 1.75e-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: 68.05  E-value: 1.75e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528282   242 HGFVHGGVTMKLMDEVAGIVAARHCKTNI-VTASVDAINFHDKIRKGCVITISGRMTFTSNKSMEIEVLV 310
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSQQvVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEV 70
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 69-151 8.63e-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: 8.63e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528282    69 GNVHGGTILKMIEEAGAIISTRHCNSQngercVAALARVERTDFLSPMCIGEVAHVSAEITYTSKHSVEVQVNVMSENIL 148
Cdd:pfam03061   2 GVVHGGVYLALADEAAGAAARRLGGSQ-----QVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDEDGR 76


                  ...
gi 32528282   149 TGA 151
Cdd:pfam03061  77 LVA 79
 
Name Accession Description Interval E-value
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
222-364 2.98e-46

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 154.95  E-value: 2.98e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528282 222 TVSYSQSSLIHLVGPSDCTLHGFVHGGVTMKLMDEVAGIVAARHCKTNIVTASVDAINFHDKIRKGCVITISGRMTFTSN 301
Cdd:COG1607   1 PLPDSELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGR 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32528282 302 KSMEIEVLVDADPVvdSSQKRYRAASAFFTYVSLSQEGRSLPVPQLVPETEDEKKRFEEGKGR 364
Cdd:COG1607  81 TSMEVGVEVWAEDL--RTGERRLVTEAYFTFVAVDEDGKPRPVPPLIPETEEEKRLFEEALRR 141
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 222-345 6.13e-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: 137.70  E-value: 6.13e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528282 222 TVSYSQSSLIHLVGPSDCTLHGFVHGGVTMKLMDEVAGIVAARHCKTNIVTASVDAINFHDKIRKGCVITISGRMTFTSN 301
Cdd:cd03442   2 PMEDTELSTRELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGGRVVTASVDRIDFLKPVRVGDVVELSARVVYTGR 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 32528282 302 KSMEIEVLVDAdpVVDSSQKRYRAASAFFTYVSLSQEGRSLPVP 345
Cdd:cd03442  82 TSMEVGVEVEA--EDPLTGERRLVTSAYFTFVALDEDGKPRPVP 123
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
49-203 2.07e-30

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 113.35  E-value: 2.07e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528282  49 PPCGACITGRIMRPDDANVAGNVHGGTILKMIEEAGAIISTRHCNSqngeRCVAalARVERTDFLSPMCIGEVAHVSAEI 128
Cdd:COG1607   2 LPDSELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARG----RVVT--ASVDSVDFLRPVRVGDIVELYARV 75

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 32528282 129 TYTSKHSVEVQVNVMSENILTGAKKLTNKATLWYVplslkNVD---KVLEVPPVVysrqEQEEEGRKRYEAQKLERME 203
Cdd:COG1607  76 VRVGRTSMEVGVEVWAEDLRTGERRLVTEAYFTFV-----AVDedgKPRPVPPLI----PETEEEKRLFEEALRRREL 144
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 48-163 4.51e-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: 111.89  E-value: 4.51e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528282  48 LPPCGACITGRIMRPDDANVAGNVHGGTILKMIEEAGAIISTRHCNSqngeRCVaaLARVERTDFLSPMCIGEVAHVSAE 127
Cdd:cd03442   2 PMEDTELSTRELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGG----RVV--TASVDRIDFLKPVRVGDVVELSAR 75

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 32528282 128 ITYTSKHSVEVQVNVMSENILTGAKKLTNKATLWYV 163
Cdd:cd03442  76 VVYTGRTSMEVGVEVEAEDPLTGERRLVTSAYFTFV 111
PLN02647 PLN02647
acyl-CoA thioesterase
 248-377 4.26e-17

acyl-CoA thioesterase


Pssm-ID: 215349 [Multi-domain]  Cd Length: 437  Bit Score: 82.14  E-value: 4.26e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528282  248 GVTMKLMDEVAGIVAARHCKTN--------IVTASVDAINFHDKIRKGCVITISGRMTFTSNKSMEIEVLVDADPVVDSS 319
Cdd:PLN02647 114 GKLLEDLDALAGTISVKHCSDDdsttrpllLVTASVDKIVLKKPIRVDVDLKIVGAVTWVGRSSMEIQLEVIQPTKDESN 193

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 32528282  320 QKRYRAASAFFTYVSL-SQEGRSLPVPQLVPETEDEKKRFEEGKGRYLQMKAKRQGHAE 377
Cdd:PLN02647 194 TSDSVALTANFTFVARdSKTGKSAPVNRLSPETEEEKLLFEEAEARNKLRKKKRGEQKR 252
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 242-310 1.75e-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: 68.05  E-value: 1.75e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528282   242 HGFVHGGVTMKLMDEVAGIVAARHCKTNI-VTASVDAINFHDKIRKGCVITISGRMTFTSNKSMEIEVLV 310
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSQQvVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEV 70
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 69-151 8.63e-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: 8.63e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528282    69 GNVHGGTILKMIEEAGAIISTRHCNSQngercVAALARVERTDFLSPMCIGEVAHVSAEITYTSKHSVEVQVNVMSENIL 148
Cdd:pfam03061   2 GVVHGGVYLALADEAAGAAARRLGGSQ-----QVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDEDGR 76


                  ...
gi 32528282   149 TGA 151
Cdd:pfam03061  77 LVA 79
PRK10694 PRK10694
acyl-CoA thioester hydrolase YciA;
233-346 1.21e-10

acyl-CoA thioester hydrolase YciA;


Pssm-ID: 236736 [Multi-domain]  Cd Length: 133  Bit Score: 58.72  E-value: 1.21e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528282  233 LVGPSDCTLHGFVHGGVTMKLMDEVAGIVAARHCKTNIVTASVDAINFHDKIRKGCVITISGRMTFTSNKSMEIEVLVDA 312
Cdd:PRK10694  17 LAMPADTNANGDIFGGWLMSQMDIGGAILAKEIAHGRVVTVRVEGMTFLRPVAVGDVVCCYARCVKTGTTSISINIEVWV 96

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 32528282  313 DPVV-DSSQKRYRAASAFFTYVSLSQEGRSLPVPQ 346
Cdd:PRK10694  97 KKVAsEPIGQRYKATEALFTYVAVDPEGKPRALPV 131
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 229-333 4.26e-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: 4.26e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528282 229 SLIHLVGPSDCTLHGFVHGGVTMKLMDEVAGIVAARHCKTNIVTASVDA-INFHDKIRKGCVITISGRMTFTSNKSMEIE 307
Cdd:cd03440   2 VLRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLGGRGLGAVTLSLdVRFLRPVRPGDTLTVEAEVVRVGRSSVTVE 81

                        90       100
                ....*....|....*....|....*.
gi 32528282 308 VLVdadpvvdSSQKRYRAASAFFTYV 333
Cdd:cd03440  82 VEV-------RNEDGKLVATATATFV 100
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 242-313 1.14e-07

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 50.33  E-value: 1.14e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32528282 242 HGFVHGGVTMKLMDEVAGIVAARHCKTNIVTASVDA-INFHDKIRKGCVITISGRMTFTSNKSMEIEV-LVDAD 313
Cdd:COG2050  47 PGTVHGGALAALADSAAGLAANSALPPGRRAVTIELnINFLRPARLGDRLTAEARVVRRGRRLAVVEVeVTDED 120
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 54-163 4.05e-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: 4.05e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528282  54 CITGRIMRPDDANVAGNVHGGTILKMIEEAGAIISTRHCnsqnGERCVAALARVErTDFLSPMCIGEVAHVSAEITYTSK 133
Cdd:cd03440   1 FVLRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLG----GRGLGAVTLSLD-VRFLRPVRPGDTLTVEAEVVRVGR 75

                        90       100       110
                ....*....|....*....|....*....|
gi 32528282 134 HSVEVQVNVMSENiltgaKKLTNKATLWYV 163
Cdd:cd03440  76 SSVTVEVEVRNED-----GKLVATATATFV 100
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 242-316 3.13e-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: 45.63  E-value: 3.13e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528282 242 HGFVHGGVTMKLMDEVAGIVAARHCKTNIVTASVD-AINFHDKIRKGCVITIS------GRMTFTsnksmEIEVLVDADP 314
Cdd:cd03443  28 GGIVHGGAIATLADTAGGLAALSALPPGALAVTVDlNVNYLRPARGGDLTARArvvklgRRLAVV-----EVEVTDEDGK 102


                ..
gi 32528282 315 VV 316
Cdd:cd03443 103 LV 104
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 60-146 2.26e-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: 2.26e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528282  60 MRPDDANVAGNVHGGTILKMIEEAGAIISTRHCNsqNGERCVAALARVertDFLSPMCIGEVAHVSAEITYTSKHSVEVQ 139
Cdd:COG2050  39 VRPEHLNPPGTVHGGALAALADSAAGLAANSALP--PGRRAVTIELNI---NFLRPARLGDRLTAEARVVRRGRRLAVVE 113


                ....*..
gi 32528282 140 VNVMSEN 146
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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