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Conserved domains on  [gi|2113560743|ref|XP_044138077|]
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cytosolic acyl coenzyme A thioester hydrolase isoform X4 [Bufo gargarizans]

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];
182-295 1.06e-37

Acyl-CoA hydrolase [Lipid transport and metabolism];


:

Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 131.07  E-value: 1.06e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113560743 182 MKLMDEVAGIVAARHCKTNIVTASVDAINFHRKIQKGCIITVSGRMTFTSNKSMEIEVFVDADTLvgDTQEQYRAVSAFF 261
Cdd:COG1607    30 LSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGRTSMEVGVEVWAEDL--RTGERRLVTEAYF 107

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2113560743 262 TYVSLSKDAKPLPVPQLVIETEEEKKRFEEGKGR 295
Cdd:COG1607   108 TFVAVDEDGKPRPVPPLIPETEEEKRLFEEALRR 141
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
11-161 6.86e-29

Acyl-CoA hydrolase [Lipid transport and metabolism];


:

Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 107.96  E-value: 6.86e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113560743  11 EGLLFHSRIMRPDDANIAGNVHGGTILKMIEEAGAIISTRHCNSqsgeKCVgtLARVERTDFLSPMCIGEVGHVSAEISY 90
Cdd:COG1607     4 DSELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARG----RVV--TASVDSVDFLRPVRVGDIVELYARVVR 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2113560743  91 TSKHSVEVQVNVMAENILTGANRLTNRATLWYVplsltNVD---KVIQVPPIqyeKPEQEDEgRKRYESQKLER 161
Cdd:COG1607    78 VGRTSMEVGVEVWAEDLRTGERRLVTEAYFTFV-----AVDedgKPRPVPPL---IPETEEE-KRLFEEALRRR 142
 
Name Accession Description Interval E-value
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
182-295 1.06e-37

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 131.07  E-value: 1.06e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113560743 182 MKLMDEVAGIVAARHCKTNIVTASVDAINFHRKIQKGCIITVSGRMTFTSNKSMEIEVFVDADTLvgDTQEQYRAVSAFF 261
Cdd:COG1607    30 LSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGRTSMEVGVEVWAEDL--RTGERRLVTEAYF 107

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2113560743 262 TYVSLSKDAKPLPVPQLVIETEEEKKRFEEGKGR 295
Cdd:COG1607   108 TFVAVDEDGKPRPVPPLIPETEEEKRLFEEALRR 141
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 182-276 8.10e-32

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: 114.97  E-value: 8.10e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113560743 182 MKLMDEVAGIVAARHCKTNIVTASVDAINFHRKIQKGCIITVSGRMTFTSNKSMeiEVFVDADTLVGDTQEQYRAVSAFF 261
Cdd:cd03442    31 LEWMDELAGIAAYRHAGGRVVTASVDRIDFLKPVRVGDVVELSARVVYTGRTSM--EVGVEVEAEDPLTGERRLVTSAYF 108

                          90
                  ....*....|....*
gi 2113560743 262 TYVSLSKDAKPLPVP 276
Cdd:cd03442   109 TFVALDEDGKPRPVP 123
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
11-161 6.86e-29

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 107.96  E-value: 6.86e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113560743  11 EGLLFHSRIMRPDDANIAGNVHGGTILKMIEEAGAIISTRHCNSqsgeKCVgtLARVERTDFLSPMCIGEVGHVSAEISY 90
Cdd:COG1607     4 DSELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARG----RVV--TASVDSVDFLRPVRVGDIVELYARVVR 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2113560743  91 TSKHSVEVQVNVMAENILTGANRLTNRATLWYVplsltNVD---KVIQVPPIqyeKPEQEDEgRKRYESQKLER 161
Cdd:COG1607    78 VGRTSMEVGVEVWAEDLRTGERRLVTEAYFTFV-----AVDedgKPRPVPPL---IPETEEE-KRLFEEALRRR 142
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 17-123 1.56e-28

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: 106.50  E-value: 1.56e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113560743  17 SRIMRPDDANIAGNVHGGTILKMIEEAGAIISTRHCNSqsgeKCVgtLARVERTDFLSPMCIGEVGHVSAEISYTSKHSV 96
Cdd:cd03442    11 RELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGG----RVV--TASVDRIDFLKPVRVGDVVELSARVVYTGRTSM 84

                          90       100
                  ....*....|....*....|....*..
gi 2113560743  97 EVQVNVMAENILTGANRLTNRATLWYV 123
Cdd:cd03442    85 EVGVEVEAEDPLTGERRLVTSAYFTFV 111
PLN02647 PLN02647
acyl-CoA thioesterase
 185-313 7.44e-16

acyl-CoA thioesterase


Pssm-ID: 215349 [Multi-domain]  Cd Length: 437  Bit Score: 77.52  E-value: 7.44e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113560743 185 MDEVAGIVAARHCKTN--------IVTASVDAINFHRKIQKGCIITVSGRMTFTSNKSMEIEVFVDADTLVGDTQEQYRA 256
Cdd:PLN02647  120 LDALAGTISVKHCSDDdsttrpllLVTASVDKIVLKKPIRVDVDLKIVGAVTWVGRSSMEIQLEVIQPTKDESNTSDSVA 199

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2113560743 257 VSAFFTYVSL-SKDAKPLPVPQLVIETEEEKKRFEEGKGRYLQTKAKRQTNSQSLTQQ 313
Cdd:PLN02647  200 LTANFTFVARdSKTGKSAPVNRLSPETEEEKLLFEEAEARNKLRKKKRGEQKREFENG 257
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 29-111 1.35e-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: 59.58  E-value: 1.35e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113560743  29 GNVHGGTILKMIEEAGAIISTRHCNSQsgekcVGTLARVERTDFLSPMCIGEVGHVSAEISYTSKHSVEVQVNVMAENIL 108
Cdd:pfam03061   2 GVVHGGVYLALADEAAGAAARRLGGSQ-----QVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDEDGR 76


                  ...
gi 2113560743 109 TGA 111
Cdd:pfam03061  77 LVA 79
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 175-241 7.24e-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: 57.26  E-value: 7.24e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2113560743 175 VVNPSVTMKLMDEVAGIVAARHCKTNI-VTASVDAINFHRKIQKGCIITVSGRMTFTSNKSMEIEVFV 241
Cdd:pfam03061   3 VVHGGVYLALADEAAGAAARRLGGSQQvVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEV 70
 
Name Accession Description Interval E-value
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
182-295 1.06e-37

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 131.07  E-value: 1.06e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113560743 182 MKLMDEVAGIVAARHCKTNIVTASVDAINFHRKIQKGCIITVSGRMTFTSNKSMEIEVFVDADTLvgDTQEQYRAVSAFF 261
Cdd:COG1607    30 LSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGRTSMEVGVEVWAEDL--RTGERRLVTEAYF 107

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2113560743 262 TYVSLSKDAKPLPVPQLVIETEEEKKRFEEGKGR 295
Cdd:COG1607   108 TFVAVDEDGKPRPVPPLIPETEEEKRLFEEALRR 141
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 182-276 8.10e-32

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: 114.97  E-value: 8.10e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113560743 182 MKLMDEVAGIVAARHCKTNIVTASVDAINFHRKIQKGCIITVSGRMTFTSNKSMeiEVFVDADTLVGDTQEQYRAVSAFF 261
Cdd:cd03442    31 LEWMDELAGIAAYRHAGGRVVTASVDRIDFLKPVRVGDVVELSARVVYTGRTSM--EVGVEVEAEDPLTGERRLVTSAYF 108

                          90
                  ....*....|....*
gi 2113560743 262 TYVSLSKDAKPLPVP 276
Cdd:cd03442   109 TFVALDEDGKPRPVP 123
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
11-161 6.86e-29

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 107.96  E-value: 6.86e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113560743  11 EGLLFHSRIMRPDDANIAGNVHGGTILKMIEEAGAIISTRHCNSqsgeKCVgtLARVERTDFLSPMCIGEVGHVSAEISY 90
Cdd:COG1607     4 DSELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARG----RVV--TASVDSVDFLRPVRVGDIVELYARVVR 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2113560743  91 TSKHSVEVQVNVMAENILTGANRLTNRATLWYVplsltNVD---KVIQVPPIqyeKPEQEDEgRKRYESQKLER 161
Cdd:COG1607    78 VGRTSMEVGVEVWAEDLRTGERRLVTEAYFTFV-----AVDedgKPRPVPPL---IPETEEE-KRLFEEALRRR 142
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 17-123 1.56e-28

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: 106.50  E-value: 1.56e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113560743  17 SRIMRPDDANIAGNVHGGTILKMIEEAGAIISTRHCNSqsgeKCVgtLARVERTDFLSPMCIGEVGHVSAEISYTSKHSV 96
Cdd:cd03442    11 RELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGG----RVV--TASVDRIDFLKPVRVGDVVELSARVVYTGRTSM 84

                          90       100
                  ....*....|....*....|....*..
gi 2113560743  97 EVQVNVMAENILTGANRLTNRATLWYV 123
Cdd:cd03442    85 EVGVEVEAEDPLTGERRLVTSAYFTFV 111
PLN02647 PLN02647
acyl-CoA thioesterase
 185-313 7.44e-16

acyl-CoA thioesterase


Pssm-ID: 215349 [Multi-domain]  Cd Length: 437  Bit Score: 77.52  E-value: 7.44e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113560743 185 MDEVAGIVAARHCKTN--------IVTASVDAINFHRKIQKGCIITVSGRMTFTSNKSMEIEVFVDADTLVGDTQEQYRA 256
Cdd:PLN02647  120 LDALAGTISVKHCSDDdsttrpllLVTASVDKIVLKKPIRVDVDLKIVGAVTWVGRSSMEIQLEVIQPTKDESNTSDSVA 199

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2113560743 257 VSAFFTYVSL-SKDAKPLPVPQLVIETEEEKKRFEEGKGRYLQTKAKRQTNSQSLTQQ 313
Cdd:PLN02647  200 LTANFTFVARdSKTGKSAPVNRLSPETEEEKLLFEEAEARNKLRKKKRGEQKREFENG 257
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 29-111 1.35e-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: 59.58  E-value: 1.35e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113560743  29 GNVHGGTILKMIEEAGAIISTRHCNSQsgekcVGTLARVERTDFLSPMCIGEVGHVSAEISYTSKHSVEVQVNVMAENIL 108
Cdd:pfam03061   2 GVVHGGVYLALADEAAGAAARRLGGSQ-----QVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDEDGR 76


                  ...
gi 2113560743 109 TGA 111
Cdd:pfam03061  77 LVA 79
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 175-241 7.24e-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: 57.26  E-value: 7.24e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2113560743 175 VVNPSVTMKLMDEVAGIVAARHCKTNI-VTASVDAINFHRKIQKGCIITVSGRMTFTSNKSMEIEVFV 241
Cdd:pfam03061   3 VVHGGVYLALADEAAGAAARRLGGSQQvVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEV 70
PRK10694 PRK10694
acyl-CoA thioester hydrolase YciA;
182-277 8.24e-08

acyl-CoA thioester hydrolase YciA;


Pssm-ID: 236736 [Multi-domain]  Cd Length: 133  Bit Score: 50.24  E-value: 8.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113560743 182 MKLMDEVAGIVAARHCKTNIVTASVDAINFHRKIQKGCIITVSGRMTFTSNKSM--EIEVFVD--ADTLVGdtqEQYRAV 257
Cdd:PRK10694   35 MSQMDIGGAILAKEIAHGRVVTVRVEGMTFLRPVAVGDVVCCYARCVKTGTTSIsiNIEVWVKkvASEPIG---QRYKAT 111

                          90       100
                  ....*....|....*....|
gi 2113560743 258 SAFFTYVSLSKDAKPLPVPQ 277
Cdd:PRK10694  112 EALFTYVAVDPEGKPRALPV 131
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 174-247 2.39e-06

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: 45.54  E-value: 2.39e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2113560743 174 PVVNPSVTMKLMDEVAGIVAARHCKTNIVTASVDA-INFHRKIQKGCIITVSGRMTFTSNKSM--EIEVFVDADTLV 247
Cdd:cd03440    16 GIVHGGLLLALADEAAGAAAARLGGRGLGAVTLSLdVRFLRPVRPGDTLTVEAEVVRVGRSSVtvEVEVRNEDGKLV 92
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 17-123 2.83e-06

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: 45.16  E-value: 2.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113560743  17 SRIMRPDDANIAGNVHGGTILKMIEEAGAIISTRHCnsqsGEKCVGTLARVErTDFLSPMCIGEVGHVSAEISYTSKHSV 96
Cdd:cd03440     4 RLTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLG----GRGLGAVTLSLD-VRFLRPVRPGDTLTVEAEVVRVGRSSV 78

                          90       100
                  ....*....|....*....|....*..
gi 2113560743  97 EVQVNVMAENiltgaNRLTNRATLWYV 123
Cdd:cd03440    79 TVEVEVRNED-----GKLVATATATFV 100
 
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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