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Conserved domains on  [gi|13385260|ref|NP_080066|]
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acyl-coenzyme A thioesterase 13 [Mus musculus]

Protein Classification

PaaI family thioesterase( domain architecture ID 10130874)

PaaI family thioesterase such as Arthrobacter sp. hot-dog fold enzyme hydroxybenzoyl-CoA thioesterase, a member of the broader acyl-CoA thioesterase family that catalyzes the conversion of acyl-CoAs back to free fatty acids and coenzyme A, and human acyl-coenzyme A thioesterase THEM5, which plays an important role in mitochondrial fatty acid metabolism, and in remodeling of the mitochondrial lipid cardiolipin

EC:  3.1.2.-
Gene Ontology:  GO:0047617
PubMed:  15307895|16464851
TCDB:  9.B.371

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 28-138 3.05e-31

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: 107.64  E-value: 3.05e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385260  28 VTLVSAAPEKLICEMKVEEQHTNKLGTLHGGLTATLVDSISTMALMCT-ERGAPGVSVDMNITYMSPAKIGeEIVITAHI 106
Cdd:cd03443   4 IRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSAlPPGALAVTVDLNVNYLRPARGG-DLTARARV 82

                        90       100       110
                ....*....|....*....|....*....|..
gi 13385260 107 LKQGKTLAFASVDLTNKtTGKLIAQGRHTKHL 138
Cdd:cd03443  83 VKLGRRLAVVEVEVTDE-DGKLVATARGTFAV 113
 
Name Accession Description Interval E-value
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 28-138 3.05e-31

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: 107.64  E-value: 3.05e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385260  28 VTLVSAAPEKLICEMKVEEQHTNKLGTLHGGLTATLVDSISTMALMCT-ERGAPGVSVDMNITYMSPAKIGeEIVITAHI 106
Cdd:cd03443   4 IRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSAlPPGALAVTVDLNVNYLRPARGG-DLTARARV 82

                        90       100       110
                ....*....|....*....|....*....|..
gi 13385260 107 LKQGKTLAFASVDLTNKtTGKLIAQGRHTKHL 138
Cdd:cd03443  83 VKLGRRLAVVEVEVTDE-DGKLVATARGTFAV 113
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 4-133 5.88e-29

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 102.71  E-value: 5.88e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385260   4 MTQNLREVMKVMFKVPgFDRVLeKVTLVSAAPEKLICEMKVEEQHTNKLGTLHGGLTATLVDSISTMALM-CTERGAPGV 82
Cdd:COG2050   1 MSDPLERLEGFLAANP-FAELL-GIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANsALPPGRRAV 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 13385260  83 SVDMNITYMSPAKIGEEIVITAHILKQGKTLAFASVDLTNKtTGKLIAQGR 133
Cdd:COG2050  79 TIELNINFLRPARLGDRLTAEARVVRRGRRLAVVEVEVTDE-DGKLVATAT 128
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 52-129 2.71e-16

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: 68.44  E-value: 2.71e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13385260    52 LGTLHGGLTATLVDSISTMALM-CTERGAPGVSVDMNITYMSPAKIGEEIVITAHILKQGKTLAFASVDLTNKTTGKLI 129
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARrLGGSQQVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDEDGRLVA 79
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 36-137 3.65e-14

uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a single copy of this domain. A protein from C. elegans consists of two tandem copies of the domain. The domain is also found as the N-terminal region of an apparent initiation factor eIF-2B alpha subunit of Aquifex aeolicus. The function of the domain is unknown.


Pssm-ID: 161843 [Multi-domain]  Cd Length: 117  Bit Score: 64.29  E-value: 3.65e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385260    36 EKLICEMKVEEQHTNKLGTLHGGLTATLVDSISTMA-LMCTERGAPGVSVDMNITYMSPAKIGeEIVITAHILKQGKTLA 114
Cdd:TIGR00369  16 GFLEATMPVDERTLQPFGSLHGGVSAALADTAGSAAgYLCNSGGQAVVGLELNANHLRPAREG-KVRAIAQVVHLGRQTG 94

                          90       100
                  ....*....|....*....|...
gi 13385260   115 FASVDLTNKtTGKLIAQGRHTKH 137
Cdd:TIGR00369  95 VAEIEIVDE-QGRLCALSRGTTA 116
PRK10254 PRK10254
proofreading thioesterase EntH;
38-98 5.57e-03

proofreading thioesterase EntH;


Pssm-ID: 182337  Cd Length: 137  Bit Score: 34.96  E-value: 5.57e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13385260   38 LICEMKVEEQHTNKLGTLHGGLTATLVDSISTMA-LMCTERGAPGVSVDMNITYMSPAKIGE 98
Cdd:PRK10254  36 LEAEMPVDTRTHQPFGLLHGGASAALAETLGSMAgFLMTRDGQCVVGTELNATHHRPVSEGK 97
 
Name Accession Description Interval E-value
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 28-138 3.05e-31

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: 107.64  E-value: 3.05e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385260  28 VTLVSAAPEKLICEMKVEEQHTNKLGTLHGGLTATLVDSISTMALMCT-ERGAPGVSVDMNITYMSPAKIGeEIVITAHI 106
Cdd:cd03443   4 IRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSAlPPGALAVTVDLNVNYLRPARGG-DLTARARV 82

                        90       100       110
                ....*....|....*....|....*....|..
gi 13385260 107 LKQGKTLAFASVDLTNKtTGKLIAQGRHTKHL 138
Cdd:cd03443  83 VKLGRRLAVVEVEVTDE-DGKLVATARGTFAV 113
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 4-133 5.88e-29

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 102.71  E-value: 5.88e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385260   4 MTQNLREVMKVMFKVPgFDRVLeKVTLVSAAPEKLICEMKVEEQHTNKLGTLHGGLTATLVDSISTMALM-CTERGAPGV 82
Cdd:COG2050   1 MSDPLERLEGFLAANP-FAELL-GIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANsALPPGRRAV 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 13385260  83 SVDMNITYMSPAKIGEEIVITAHILKQGKTLAFASVDLTNKtTGKLIAQGR 133
Cdd:COG2050  79 TIELNINFLRPARLGDRLTAEARVVRRGRRLAVVEVEVTDE-DGKLVATAT 128
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 38-135 1.76e-16

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: 69.81  E-value: 1.76e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385260  38 LICEMKVEEQHTNKLGTLHGGLTATLVDSISTMALM-CTERGAPGVSVDMNITYMSPAKIGEEIVITAHILKQGKTLAFA 116
Cdd:cd03440   1 FVLRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAArLGGRGLGAVTLSLDVRFLRPVRPGDTLTVEAEVVRVGRSSVTV 80

                        90
                ....*....|....*....
gi 13385260 117 SVDLTNKtTGKLIAQGRHT 135
Cdd:cd03440  81 EVEVRNE-DGKLVATATAT 98
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 52-129 2.71e-16

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: 68.44  E-value: 2.71e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13385260    52 LGTLHGGLTATLVDSISTMALM-CTERGAPGVSVDMNITYMSPAKIGEEIVITAHILKQGKTLAFASVDLTNKTTGKLI 129
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARrLGGSQQVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDEDGRLVA 79
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 36-137 3.65e-14

uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a single copy of this domain. A protein from C. elegans consists of two tandem copies of the domain. The domain is also found as the N-terminal region of an apparent initiation factor eIF-2B alpha subunit of Aquifex aeolicus. The function of the domain is unknown.


Pssm-ID: 161843 [Multi-domain]  Cd Length: 117  Bit Score: 64.29  E-value: 3.65e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385260    36 EKLICEMKVEEQHTNKLGTLHGGLTATLVDSISTMA-LMCTERGAPGVSVDMNITYMSPAKIGeEIVITAHILKQGKTLA 114
Cdd:TIGR00369  16 GFLEATMPVDERTLQPFGSLHGGVSAALADTAGSAAgYLCNSGGQAVVGLELNANHLRPAREG-KVRAIAQVVHLGRQTG 94

                          90       100
                  ....*....|....*....|...
gi 13385260   115 FASVDLTNKtTGKLIAQGRHTKH 137
Cdd:TIGR00369  95 VAEIEIVDE-QGRLCALSRGTTA 116
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
48-112 1.90e-06

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 44.40  E-value: 1.90e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13385260  48 HTNKLGTLHGGLTATLVDSIstmALMCTERGAPG----VSVDmNITYMSPAKIGEEIVITAHILKQGKT 112
Cdd:COG1607  17 DTNHHGTLFGGWLLSWMDEA---AAIAAARHARGrvvtASVD-SVDFLRPVRVGDIVELYARVVRVGRT 81
FadM COG0824
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ...
 76-135 1.37e-04

Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440586 [Multi-domain]  Cd Length: 139  Bit Score: 39.11  E-value: 1.37e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13385260  76 ERGAPGVSVDMNITYMSPAKIGEEIVITAHILK-QGKTLAFAsVDLTNKTTGKLIAQGRHT 135
Cdd:COG0824  52 EEGIGLVVVEAEIDYLRPARYGDELTVETRVVRlGGSSLTFE-YEIFRADDGELLATGETV 111
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 44-112 1.87e-04

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: 38.70  E-value: 1.87e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13385260  44 VEEQHTNKLGTLHGGLTATLVDSIstmALMCTERGAPG----VSVDmNITYMSPAKIGEEIVITAHILKQGKT 112
Cdd:cd03442  14 VLPEDTNHHGTIFGGWLLEWMDEL---AGIAAYRHAGGrvvtASVD-RIDFLKPVRVGDVVELSARVVYTGRT 82
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
 75-135 5.22e-04

4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate degradation pathway in which 4-chlorobenzoate is converted to 4-hydroxybenzoate in certain soil-dwelling bacteria. 4HBT forms a homotetramer with four active sites. There is no evidence to suggest that 4HBT is related to the type I thioesterases functioning in primary or secondary metabolic pathways. Each subunit of the 4HBT tetramer adopts a so-called hot-dog fold similar to those of beta-hydroxydecanoyl-ACP dehydratase, (R)-specific enoyl-CoA hydratase, and type II, thioesterase (TEII).


Pssm-ID: 238329 [Multi-domain]  Cd Length: 110  Bit Score: 37.20  E-value: 5.22e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13385260  75 TERGAPGVSVDMNITYMSPAKIGEEIVITAHILKQGKTLAFASVDLTNKtTGKLIAQGRHT 135
Cdd:cd00586  46 EEQGLGLVVVELEIDYLRPLRLGDRLTVETRVLRLGRKSFTFEQEIFRE-DGELLATAETV 105
PRK10254 PRK10254
proofreading thioesterase EntH;
38-98 5.57e-03

proofreading thioesterase EntH;


Pssm-ID: 182337  Cd Length: 137  Bit Score: 34.96  E-value: 5.57e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13385260   38 LICEMKVEEQHTNKLGTLHGGLTATLVDSISTMA-LMCTERGAPGVSVDMNITYMSPAKIGE 98
Cdd:PRK10254  36 LEAEMPVDTRTHQPFGLLHGGASAALAETLGSMAgFLMTRDGQCVVGTELNATHHRPVSEGK 97
PRK11688 PRK11688
thioesterase family protein;
55-132 8.42e-03

thioesterase family protein;


Pssm-ID: 183276  Cd Length: 154  Bit Score: 34.44  E-value: 8.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385260   55 LHGGLTATLVDsisTMA-LMCT----------------ERGAPGVSVDMNITYMSPAkIGEEIVITAHILKQGKTLAFAS 117
Cdd:PRK11688  58 LHGGVIASVLD---VAGgLVCVggilarhediseeelrQRLSRLGTIDLRVDYLRPG-RGERFTATSSVLRAGNKVAVAR 133

                         90
                 ....*....|....*
gi 13385260  118 VDLTNKtTGKLIAQG 132
Cdd:PRK11688 134 MELHNE-QGVHIASG 147
Glyco_hydro_47 pfam01532
Glycosyl hydrolase family 47; Members of this family are alpha-mannosidases that catalyze the ...
 57-73 8.95e-03

Glycosyl hydrolase family 47; Members of this family are alpha-mannosidases that catalyze the hydrolysis of the terminal 1,2-linked alpha-D-mannose residues in the oligo-mannose oligosaccharide Man(9)(GlcNAc)(2).


Pssm-ID: 460241  Cd Length: 453  Bit Score: 35.23  E-value: 8.95e-03
                          10
                  ....*....|....*..
gi 13385260    57 GGLTATLVDSISTMALM 73
Cdd:pfam01532  31 GGWGATIVDSLDTLIIM 47
 
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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