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Conserved domains on  [gi|2113560739|ref|XP_044138075|]
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cytosolic acyl coenzyme A thioester hydrolase isoform X2 [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];
184-322 1.07e-46

Acyl-CoA hydrolase [Lipid transport and metabolism];


:

Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 154.95  E-value: 1.07e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113560739 184 SQSSLIHLVGPSDCTLHGYVHGGVTMKLMDEVAGIVAARHCKTNIVTASVDAINFHRKIQKGCIITVSGRMTFTSNKSME 263
Cdd:COG1607     5 SELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGRTSME 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2113560739 264 IEVFVDADTLvgDTQEQYRAVSAFFTYVSLSKDAKPLPVPQLVIETEEEKKRFEEGKGR 322
Cdd:COG1607    85 VGVEVWAEDL--RTGERRLVTEAYFTFVAVDEDGKPRPVPPLIPETEEEKRLFEEALRR 141
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
6-159 4.75e-30

Acyl-CoA hydrolase [Lipid transport and metabolism];


:

Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 111.81  E-value: 4.75e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113560739   6 DPAASALQICRIMRPDDANIAGNVHGGTILKMIEEAGAIISTRHCNSqsgeKCVgTlARVERTDFLSPMCIGEVGHVSAE 85
Cdd:COG1607     1 PLPDSELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARG----RVV-T-ASVDSVDFLRPVRVGDIVELYAR 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2113560739  86 ISYTSKHSVEVQVNVMAENILTGANRLTNRATLWYVplsltNVD---KVIQVPPIqyeKPEQEDEgRKRYESQKLER 159
Cdd:COG1607    75 VVRVGRTSMEVGVEVWAEDLRTGERRLVTEAYFTFV-----AVDedgKPRPVPPL---IPETEEE-KRLFEEALRRR 142
 
Name Accession Description Interval E-value
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
184-322 1.07e-46

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 154.95  E-value: 1.07e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113560739 184 SQSSLIHLVGPSDCTLHGYVHGGVTMKLMDEVAGIVAARHCKTNIVTASVDAINFHRKIQKGCIITVSGRMTFTSNKSME 263
Cdd:COG1607     5 SELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGRTSME 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2113560739 264 IEVFVDADTLvgDTQEQYRAVSAFFTYVSLSKDAKPLPVPQLVIETEEEKKRFEEGKGR 322
Cdd:COG1607    85 VGVEVWAEDL--RTGERRLVTEAYFTFVAVDEDGKPRPVPPLIPETEEEKRLFEEALRR 141
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 179-303 1.18e-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: 138.86  E-value: 1.18e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113560739 179 YTVGYSQSSLIHLVGPSDCTLHGYVHGGVTMKLMDEVAGIVAARHCKTNIVTASVDAINFHRKIQKGCIITVSGRMTFTS 258
Cdd:cd03442     1 VPMEDTELSTRELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGGRVVTASVDRIDFLKPVRVGDVVELSARVVYTG 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2113560739 259 NKSMeiEVFVDADTLVGDTQEQYRAVSAFFTYVSLSKDAKPLPVP 303
Cdd:cd03442    81 RTSM--EVGVEVEAEDPLTGERRLVTSAYFTFVALDEDGKPRPVP 123
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
6-159 4.75e-30

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 111.81  E-value: 4.75e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113560739   6 DPAASALQICRIMRPDDANIAGNVHGGTILKMIEEAGAIISTRHCNSqsgeKCVgTlARVERTDFLSPMCIGEVGHVSAE 85
Cdd:COG1607     1 PLPDSELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARG----RVV-T-ASVDSVDFLRPVRVGDIVELYAR 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2113560739  86 ISYTSKHSVEVQVNVMAENILTGANRLTNRATLWYVplsltNVD---KVIQVPPIqyeKPEQEDEgRKRYESQKLER 159
Cdd:COG1607    75 VVRVGRTSMEVGVEVWAEDLRTGERRLVTEAYFTFV-----AVDedgKPRPVPPL---IPETEEE-KRLFEEALRRR 142
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 7-121 3.11e-29

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: 108.81  E-value: 3.11e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113560739   7 PAASALQICRIMRPDDANIAGNVHGGTILKMIEEAGAIISTRHCNSqsgeKCVgtLARVERTDFLSPMCIGEVGHVSAEI 86
Cdd:cd03442     3 MEDTELSTRELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGG----RVV--TASVDRIDFLKPVRVGDVVELSARV 76

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2113560739  87 SYTSKHSVEVQVNVMAENILTGANRLTNRATLWYV 121
Cdd:cd03442    77 VYTGRTSMEVGVEVEAEDPLTGERRLVTSAYFTFV 111
PLN02647 PLN02647
acyl-CoA thioesterase
 210-340 4.85e-16

acyl-CoA thioesterase


Pssm-ID: 215349 [Multi-domain]  Cd Length: 437  Bit Score: 78.68  E-value: 4.85e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113560739 210 KLM---DEVAGIVAARHCKTN--------IVTASVDAINFHRKIQKGCIITVSGRMTFTSNKSMEIEVFVDADTLVGDTQ 278
Cdd:PLN02647  115 KLLedlDALAGTISVKHCSDDdsttrpllLVTASVDKIVLKKPIRVDVDLKIVGAVTWVGRSSMEIQLEVIQPTKDESNT 194

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2113560739 279 EQYRAVSAFFTYVSL-SKDAKPLPVPQLVIETEEEKKRFEEGKGRYLQTKAKRQTNSQSLTQQ 340
Cdd:PLN02647  195 SDSVALTANFTFVARdSKTGKSAPVNRLSPETEEEKLLFEEAEARNKLRKKKRGEQKREFENG 257
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 200-268 2.86e-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: 69.98  E-value: 2.86e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113560739 200 HGYVHGGVTMKLMDEVAGIVAARHCKTNI-VTASVDAINFHRKIQKGCIITVSGRMTFTSNKSMEIEVFV 268
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSQQvVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEV 70
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 27-109 1.30e-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: 1.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113560739  27 GNVHGGTILKMIEEAGAIISTRHCNSQsgekcVGTLARVERTDFLSPMCIGEVGHVSAEISYTSKHSVEVQVNVMAENIL 106
Cdd:pfam03061   2 GVVHGGVYLALADEAAGAAARRLGGSQ-----QVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDEDGR 76


                  ...
gi 2113560739 107 TGA 109
Cdd:pfam03061  77 LVA 79
 
Name Accession Description Interval E-value
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
184-322 1.07e-46

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 154.95  E-value: 1.07e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113560739 184 SQSSLIHLVGPSDCTLHGYVHGGVTMKLMDEVAGIVAARHCKTNIVTASVDAINFHRKIQKGCIITVSGRMTFTSNKSME 263
Cdd:COG1607     5 SELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGRTSME 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2113560739 264 IEVFVDADTLvgDTQEQYRAVSAFFTYVSLSKDAKPLPVPQLVIETEEEKKRFEEGKGR 322
Cdd:COG1607    85 VGVEVWAEDL--RTGERRLVTEAYFTFVAVDEDGKPRPVPPLIPETEEEKRLFEEALRR 141
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 179-303 1.18e-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: 138.86  E-value: 1.18e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113560739 179 YTVGYSQSSLIHLVGPSDCTLHGYVHGGVTMKLMDEVAGIVAARHCKTNIVTASVDAINFHRKIQKGCIITVSGRMTFTS 258
Cdd:cd03442     1 VPMEDTELSTRELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGGRVVTASVDRIDFLKPVRVGDVVELSARVVYTG 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2113560739 259 NKSMeiEVFVDADTLVGDTQEQYRAVSAFFTYVSLSKDAKPLPVP 303
Cdd:cd03442    81 RTSM--EVGVEVEAEDPLTGERRLVTSAYFTFVALDEDGKPRPVP 123
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
6-159 4.75e-30

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 111.81  E-value: 4.75e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113560739   6 DPAASALQICRIMRPDDANIAGNVHGGTILKMIEEAGAIISTRHCNSqsgeKCVgTlARVERTDFLSPMCIGEVGHVSAE 85
Cdd:COG1607     1 PLPDSELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARG----RVV-T-ASVDSVDFLRPVRVGDIVELYAR 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2113560739  86 ISYTSKHSVEVQVNVMAENILTGANRLTNRATLWYVplsltNVD---KVIQVPPIqyeKPEQEDEgRKRYESQKLER 159
Cdd:COG1607    75 VVRVGRTSMEVGVEVWAEDLRTGERRLVTEAYFTFV-----AVDedgKPRPVPPL---IPETEEE-KRLFEEALRRR 142
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 7-121 3.11e-29

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: 108.81  E-value: 3.11e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113560739   7 PAASALQICRIMRPDDANIAGNVHGGTILKMIEEAGAIISTRHCNSqsgeKCVgtLARVERTDFLSPMCIGEVGHVSAEI 86
Cdd:cd03442     3 MEDTELSTRELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGG----RVV--TASVDRIDFLKPVRVGDVVELSARV 76

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2113560739  87 SYTSKHSVEVQVNVMAENILTGANRLTNRATLWYV 121
Cdd:cd03442    77 VYTGRTSMEVGVEVEAEDPLTGERRLVTSAYFTFV 111
PLN02647 PLN02647
acyl-CoA thioesterase
 210-340 4.85e-16

acyl-CoA thioesterase


Pssm-ID: 215349 [Multi-domain]  Cd Length: 437  Bit Score: 78.68  E-value: 4.85e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113560739 210 KLM---DEVAGIVAARHCKTN--------IVTASVDAINFHRKIQKGCIITVSGRMTFTSNKSMEIEVFVDADTLVGDTQ 278
Cdd:PLN02647  115 KLLedlDALAGTISVKHCSDDdsttrpllLVTASVDKIVLKKPIRVDVDLKIVGAVTWVGRSSMEIQLEVIQPTKDESNT 194

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2113560739 279 EQYRAVSAFFTYVSL-SKDAKPLPVPQLVIETEEEKKRFEEGKGRYLQTKAKRQTNSQSLTQQ 340
Cdd:PLN02647  195 SDSVALTANFTFVARdSKTGKSAPVNRLSPETEEEKLLFEEAEARNKLRKKKRGEQKREFENG 257
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 200-268 2.86e-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: 69.98  E-value: 2.86e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113560739 200 HGYVHGGVTMKLMDEVAGIVAARHCKTNI-VTASVDAINFHRKIQKGCIITVSGRMTFTSNKSMEIEVFV 268
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSQQvVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEV 70
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 27-109 1.30e-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: 1.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113560739  27 GNVHGGTILKMIEEAGAIISTRHCNSQsgekcVGTLARVERTDFLSPMCIGEVGHVSAEISYTSKHSVEVQVNVMAENIL 106
Cdd:pfam03061   2 GVVHGGVYLALADEAAGAAARRLGGSQ-----QVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDEDGR 76


                  ...
gi 2113560739 107 TGA 109
Cdd:pfam03061  77 LVA 79
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 187-274 5.77e-11

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: 58.64  E-value: 5.77e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113560739 187 SLIHLVGPSDCTLHGYVHGGVTMKLMDEVAGIVAARHCKTNIVTASVDA-INFHRKIQKGCIITVSGRMTFTSNKSM--E 263
Cdd:cd03440     2 VLRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLGGRGLGAVTLSLdVRFLRPVRPGDTLTVEAEVVRVGRSSVtvE 81

                          90
                  ....*....|.
gi 2113560739 264 IEVFVDADTLV 274
Cdd:cd03440    82 VEVRNEDGKLV 92
PRK10694 PRK10694
acyl-CoA thioester hydrolase YciA;
191-304 7.03e-11

acyl-CoA thioester hydrolase YciA;


Pssm-ID: 236736 [Multi-domain]  Cd Length: 133  Bit Score: 59.10  E-value: 7.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113560739 191 LVGPSDCTLHGYVHGGVTMKLMDEVAGIVAARHCKTNIVTASVDAINFHRKIQKGCIITVSGRMTFTSNKSM--EIEVFV 268
Cdd:PRK10694   17 LAMPADTNANGDIFGGWLMSQMDIGGAILAKEIAHGRVVTVRVEGMTFLRPVAVGDVVCCYARCVKTGTTSIsiNIEVWV 96

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2113560739 269 D--ADTLVGdtqEQYRAVSAFFTYVSLSKDAKPLPVPQ 304
Cdd:PRK10694   97 KkvASEPIG---QRYKATEALFTYVAVDPEGKPRALPV 131
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 200-274 2.56e-10

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 57.65  E-value: 2.56e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2113560739 200 HGYVHGGVTMKLMDEVAGIVAARHCKTNIVTASVDA-INFHRKIQKGCIITVSGRMTFTSNKS--MEIEVFVDADTLV 274
Cdd:COG2050    47 PGTVHGGALAALADSAAGLAANSALPPGRRAVTIELnINFLRPARLGDRLTAEARVVRRGRRLavVEVEVTDEDGKLV 124
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 200-274 1.59e-09

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: 54.87  E-value: 1.59e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113560739 200 HGYVHGGVTMKLMDEVAGIVAARHCKTNIVTASVD-AINFHRKIQKGCIITVS------GRMTFTsnksmEIEVFVDADT 272
Cdd:cd03443    28 GGIVHGGAIATLADTAGGLAALSALPPGALAVTVDlNVNYLRPARGGDLTARArvvklgRRLAVV-----EVEVTDEDGK 102


                  ..
gi 2113560739 273 LV 274
Cdd:cd03443   103 LV 104
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 16-121 1.86e-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: 45.93  E-value: 1.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113560739  16 RIMRPDDANIAGNVHGGTILKMIEEAGAIISTRHCnsqsGEKCVGTLARVErTDFLSPMCIGEVGHVSAEISYTSKHSVE 95
Cdd:cd03440     5 LTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLG----GRGLGAVTLSLD-VRFLRPVRPGDTLTVEAEVVRVGRSSVT 79

                          90       100
                  ....*....|....*....|....*.
gi 2113560739  96 VQVNVMAENiltgaNRLTNRATLWYV 121
Cdd:cd03440    80 VEVEVRNED-----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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