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Conserved domains on  [gi|225690628|ref|NP_001139533|]
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cytosolic acyl coenzyme A thioester hydrolase isoform 1 [Rattus norvegicus]

Protein Classification

BFIT_BACH domain-containing protein( domain architecture ID 10855570)

BFIT_BACH domain-containing protein

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];
223-365 4.49e-48

Acyl-CoA hydrolase [Lipid transport and metabolism];


:

Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 159.96  E-value: 4.49e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225690628 223 TVSYSQSSLIHLVGPSDCTLHGFVHGGVTMKLMDEVAGIVAARHCKTNIVTASVDAINFHDKIRKGCVITISGRMTFTSN 302
Cdd:COG1607    1 PLPDSELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGR 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 225690628 303 KSMEIEVLVDADPVvdNSQKRYRAASAFFTYVSLNQEGKPLPVPQLVPETEDEKKRFEEGKGR 365
Cdd:COG1607   81 TSMEVGVEVWAEDL--RTGERRLVTEAYFTFVAVDEDGKPRPVPPLIPETEEEKRLFEEALRR 141
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 59-164 8.12e-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: 111.12  E-value: 8.12e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225690628  59 RIMRPDDANVAGNVHGGTILKMIEEAGVIISTRHCNSqngeRCVaaLARVERTDFLSPMCIGEVAHVSAEITYTSKHSVE 138
Cdd:cd03442   12 ELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGG----RVV--TASVDRIDFLKPVRVGDVVELSARVVYTGRTSME 85

                         90       100
                 ....*....|....*....|....*.
gi 225690628 139 VQVHVLSENILTGTKKLTNKATLWYV 164
Cdd:cd03442   86 VGVEVEAEDPLTGERRLVTSAYFTFV 111
 
Name Accession Description Interval E-value
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
223-365 4.49e-48

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 159.96  E-value: 4.49e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225690628 223 TVSYSQSSLIHLVGPSDCTLHGFVHGGVTMKLMDEVAGIVAARHCKTNIVTASVDAINFHDKIRKGCVITISGRMTFTSN 302
Cdd:COG1607    1 PLPDSELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGR 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 225690628 303 KSMEIEVLVDADPVvdNSQKRYRAASAFFTYVSLNQEGKPLPVPQLVPETEDEKKRFEEGKGR 365
Cdd:COG1607   81 TSMEVGVEVWAEDL--RTGERRLVTEAYFTFVAVDEDGKPRPVPPLIPETEEEKRLFEEALRR 141
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 223-346 4.45e-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: 140.78  E-value: 4.45e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225690628 223 TVSYSQSSLIHLVGPSDCTLHGFVHGGVTMKLMDEVAGIVAARHCKTNIVTASVDAINFHDKIRKGCVITISGRMTFTSN 302
Cdd:cd03442    2 PMEDTELSTRELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGGRVVTASVDRIDFLKPVRVGDVVELSARVVYTGR 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 225690628 303 KSMEIEVLVDAdpVVDNSQKRYRAASAFFTYVSLNQEGKPLPVP 346
Cdd:cd03442   82 TSMEVGVEVEA--EDPLTGERRLVTSAYFTFVALDEDGKPRPVP 123
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 59-164 8.12e-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: 111.12  E-value: 8.12e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225690628  59 RIMRPDDANVAGNVHGGTILKMIEEAGVIISTRHCNSqngeRCVaaLARVERTDFLSPMCIGEVAHVSAEITYTSKHSVE 138
Cdd:cd03442   12 ELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGG----RVV--TASVDRIDFLKPVRVGDVVELSARVVYTGRTSME 85

                         90       100
                 ....*....|....*....|....*.
gi 225690628 139 VQVHVLSENILTGTKKLTNKATLWYV 164
Cdd:cd03442   86 VGVEVEAEDPLTGERRLVTSAYFTFV 111
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
59-204 3.01e-29

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 110.27  E-value: 3.01e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225690628  59 RIMRPDDANVAGNVHGGTILKMIEEAGVIISTRHCNSqngeRCVAalARVERTDFLSPMCIGEVAHVSAEITYTSKHSVE 138
Cdd:COG1607   11 ELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARG----RVVT--ASVDSVDFLRPVRVGDIVELYARVVRVGRTSME 84

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 225690628 139 VQVHVLSENILTGTKKLTNKATLWYVplslkNVD---KVLEVPPIVylrqEQEEEGRKRYEAQKLERME 204
Cdd:COG1607   85 VGVEVWAEDLRTGERRLVTEAYFTFV-----AVDedgKPRPVPPLI----PETEEEKRLFEEALRRREL 144
PLN02647 PLN02647
acyl-CoA thioesterase
 253-378 2.84e-16

acyl-CoA thioesterase


Pssm-ID: 215349 [Multi-domain]  Cd Length: 437  Bit Score: 79.83  E-value: 2.84e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225690628 253 KLM---DEVAGIVAARHCKTN--------IVTASVDAINFHDKIRKGCVITISGRMTFTSNKSMEIEVLVDADPVVDNSQ 321
Cdd:PLN02647 115 KLLedlDALAGTISVKHCSDDdsttrpllLVTASVDKIVLKKPIRVDVDLKIVGAVTWVGRSSMEIQLEVIQPTKDESNT 194

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 225690628 322 KRYRAASAFFTYVSLN-QEGKPLPVPQLVPETEDEKKRFEEGKGRYLQMKAKRQGHTE 378
Cdd:PLN02647 195 SDSVALTANFTFVARDsKTGKSAPVNRLSPETEEEKLLFEEAEARNKLRKKKRGEQKR 252
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 243-311 2.08e-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: 67.67  E-value: 2.08e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225690628  243 HGFVHGGVTMKLMDEVAGIVAARHCKTNI-VTASVDAINFHDKIRKGCVITISGRMTFTSNKSMEIEVLV 311
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSQQvVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEV 70
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 70-151 1.15e-11

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: 59.96  E-value: 1.15e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225690628   70 GNVHGGTILKMIEEAGVIISTRHCNSQngercVAALARVERTDFLSPMCIGEVAHVSAEITYTSKHSVEVQVHVLSENIL 149
Cdd:pfam03061   2 GVVHGGVYLALADEAAGAAARRLGGSQ-----QVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDEDGR 76


                  ..
gi 225690628  150 TG 151
Cdd:pfam03061  77 LV 78
 
Name Accession Description Interval E-value
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
223-365 4.49e-48

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 159.96  E-value: 4.49e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225690628 223 TVSYSQSSLIHLVGPSDCTLHGFVHGGVTMKLMDEVAGIVAARHCKTNIVTASVDAINFHDKIRKGCVITISGRMTFTSN 302
Cdd:COG1607    1 PLPDSELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGR 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 225690628 303 KSMEIEVLVDADPVvdNSQKRYRAASAFFTYVSLNQEGKPLPVPQLVPETEDEKKRFEEGKGR 365
Cdd:COG1607   81 TSMEVGVEVWAEDL--RTGERRLVTEAYFTFVAVDEDGKPRPVPPLIPETEEEKRLFEEALRR 141
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 223-346 4.45e-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: 140.78  E-value: 4.45e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225690628 223 TVSYSQSSLIHLVGPSDCTLHGFVHGGVTMKLMDEVAGIVAARHCKTNIVTASVDAINFHDKIRKGCVITISGRMTFTSN 302
Cdd:cd03442    2 PMEDTELSTRELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGGRVVTASVDRIDFLKPVRVGDVVELSARVVYTGR 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 225690628 303 KSMEIEVLVDAdpVVDNSQKRYRAASAFFTYVSLNQEGKPLPVP 346
Cdd:cd03442   82 TSMEVGVEVEA--EDPLTGERRLVTSAYFTFVALDEDGKPRPVP 123
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 59-164 8.12e-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: 111.12  E-value: 8.12e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225690628  59 RIMRPDDANVAGNVHGGTILKMIEEAGVIISTRHCNSqngeRCVaaLARVERTDFLSPMCIGEVAHVSAEITYTSKHSVE 138
Cdd:cd03442   12 ELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGG----RVV--TASVDRIDFLKPVRVGDVVELSARVVYTGRTSME 85

                         90       100
                 ....*....|....*....|....*.
gi 225690628 139 VQVHVLSENILTGTKKLTNKATLWYV 164
Cdd:cd03442   86 VGVEVEAEDPLTGERRLVTSAYFTFV 111
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
59-204 3.01e-29

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 110.27  E-value: 3.01e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225690628  59 RIMRPDDANVAGNVHGGTILKMIEEAGVIISTRHCNSqngeRCVAalARVERTDFLSPMCIGEVAHVSAEITYTSKHSVE 138
Cdd:COG1607   11 ELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARG----RVVT--ASVDSVDFLRPVRVGDIVELYARVVRVGRTSME 84

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 225690628 139 VQVHVLSENILTGTKKLTNKATLWYVplslkNVD---KVLEVPPIVylrqEQEEEGRKRYEAQKLERME 204
Cdd:COG1607   85 VGVEVWAEDLRTGERRLVTEAYFTFV-----AVDedgKPRPVPPLI----PETEEEKRLFEEALRRREL 144
PLN02647 PLN02647
acyl-CoA thioesterase
 253-378 2.84e-16

acyl-CoA thioesterase


Pssm-ID: 215349 [Multi-domain]  Cd Length: 437  Bit Score: 79.83  E-value: 2.84e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225690628 253 KLM---DEVAGIVAARHCKTN--------IVTASVDAINFHDKIRKGCVITISGRMTFTSNKSMEIEVLVDADPVVDNSQ 321
Cdd:PLN02647 115 KLLedlDALAGTISVKHCSDDdsttrpllLVTASVDKIVLKKPIRVDVDLKIVGAVTWVGRSSMEIQLEVIQPTKDESNT 194

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 225690628 322 KRYRAASAFFTYVSLN-QEGKPLPVPQLVPETEDEKKRFEEGKGRYLQMKAKRQGHTE 378
Cdd:PLN02647 195 SDSVALTANFTFVARDsKTGKSAPVNRLSPETEEEKLLFEEAEARNKLRKKKRGEQKR 252
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 243-311 2.08e-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: 67.67  E-value: 2.08e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225690628  243 HGFVHGGVTMKLMDEVAGIVAARHCKTNI-VTASVDAINFHDKIRKGCVITISGRMTFTSNKSMEIEVLV 311
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSQQvVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEV 70
PRK10694 PRK10694
acyl-CoA thioester hydrolase YciA;
234-347 2.76e-12

acyl-CoA thioester hydrolase YciA;


Pssm-ID: 236736 [Multi-domain]  Cd Length: 133  Bit Score: 63.34  E-value: 2.76e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225690628 234 LVGPSDCTLHGFVHGGVTMKLMDEVAGIVAARHCKTNIVTASVDAINFHDKIRKGCVITISGRMTFTSNKSMEIEV---- 309
Cdd:PRK10694  17 LAMPADTNANGDIFGGWLMSQMDIGGAILAKEIAHGRVVTVRVEGMTFLRPVAVGDVVCCYARCVKTGTTSISINIevwv 96

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 225690628 310 -LVDADPVvdnsQKRYRAASAFFTYVSLNQEGKPLPVPQ 347
Cdd:PRK10694  97 kKVASEPI----GQRYKATEALFTYVAVDPEGKPRALPV 131
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 70-151 1.15e-11

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: 59.96  E-value: 1.15e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225690628   70 GNVHGGTILKMIEEAGVIISTRHCNSQngercVAALARVERTDFLSPMCIGEVAHVSAEITYTSKHSVEVQVHVLSENIL 149
Cdd:pfam03061   2 GVVHGGVYLALADEAAGAAARRLGGSQ-----QVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDEDGR 76


                  ..
gi 225690628  150 TG 151
Cdd:pfam03061  77 LV 78
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 230-334 1.17e-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: 55.17  E-value: 1.17e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225690628 230 SLIHLVGPSDCTLHGFVHGGVTMKLMDEVAGIVAARHCKTNIVTASVDA-INFHDKIRKGCVITISGRMTFTSNKSMEIE 308
Cdd:cd03440    2 VLRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLGGRGLGAVTLSLdVRFLRPVRPGDTLTVEAEVVRVGRSSVTVE 81

                         90       100
                 ....*....|....*....|....*.
gi 225690628 309 VLVDAdpvvdnsQKRYRAASAFFTYV 334
Cdd:cd03440   82 VEVRN-------EDGKLVATATATFV 100
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 243-314 9.94e-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: 9.94e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 225690628 243 HGFVHGGVTMKLMDEVAGIVAARHCKTNIVTASVDA-INFHDKIRKGCVITISGRMTFTSNKSMEIEV-LVDAD 314
Cdd:COG2050   47 PGTVHGGALAALADSAAGLAANSALPPGRRAVTIELnINFLRPARLGDRLTAEARVVRRGRRLAVVEVeVTDED 120
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 59-164 2.26e-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: 48.63  E-value: 2.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225690628  59 RIMRPDDANVAGNVHGGTILKMIEEAGVIISTRHCnsqnGERCVAALARVErTDFLSPMCIGEVAHVSAEITYTSKHSVE 138
Cdd:cd03440    5 LTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLG----GRGLGAVTLSLD-VRFLRPVRPGDTLTVEAEVVRVGRSSVT 79

                         90       100
                 ....*....|....*....|....*.
gi 225690628 139 VQVHVLSEniltgTKKLTNKATLWYV 164
Cdd:cd03440   80 VEVEVRNE-----DGKLVATATATFV 100
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 243-317 2.51e-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: 46.01  E-value: 2.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225690628 243 HGFVHGGVTMKLMDEVAGIVAARHCKTNIVTASVD-AINFHDKIRKGCVITIS------GRMTFTsnksmEIEVLVDADP 315
Cdd:cd03443   28 GGIVHGGAIATLADTAGGLAALSALPPGALAVTVDlNVNYLRPARGGDLTARArvvklgRRLAVV-----EVEVTDEDGK 102


                 ..
gi 225690628 316 VV 317
Cdd:cd03443  103 LV 104
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 39-147 3.86e-04

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 40.31  E-value: 3.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225690628  39 MRAVRTRAVHHKPGHCIAMGRImRPDDANVAGNVHGGTILKMIEEAGVIISTRHCNsqNGERCVAALARVertDFLSPMC 118
Cdd:COG2050   18 AELLGIELVEVEPGRAVLRLPV-RPEHLNPPGTVHGGALAALADSAAGLAANSALP--PGRRAVTIELNI---NFLRPAR 91

                         90       100
                 ....*....|....*....|....*....
gi 225690628 119 IGEVAHVSAEITYTSKHSVEVQVHVLSEN 147
Cdd:COG2050   92 LGDRLTAEARVVRRGRRLAVVEVEVTDED 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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