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Conserved domains on  [gi|18402093|ref|NP_565683|]
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Thioesterase superfamily protein [Arabidopsis thaliana]

Protein Classification

PaaI family thioesterase( domain architecture ID 10130874)

PaaI family thioesterase is a member of the broader hot dog-fold acyl-CoA thioesterase family that catalyzes the conversion of acyl-CoAs back to free fatty acids and coenzyme A, similar to 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|GO:0016790
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 ...
 42-151 5.56e-14

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: 64.12  E-value: 5.56e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402093  42 GIRVNRVEPGFISCSFKVPLRLTDRDKNLANGAIANLVDEVGG--ALVHGEGLPMSVSVDMSIAFLSKAKLGeELEITSR 119
Cdd:cd03443   3 GIRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGlaALSALPPGALAVTVDLNVNYLRPARGG-DLTARAR 81

                        90       100       110
                ....*....|....*....|....*....|....*
gi 18402093 120 LLGErggyKGTIVVVRNKMT---GEIIAEGRHSMF 151
Cdd:cd03443  82 VVKL----GRRLAVVEVEVTdedGKLVATARGTFA 112
 
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 ...
 42-151 5.56e-14

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: 64.12  E-value: 5.56e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402093  42 GIRVNRVEPGFISCSFKVPLRLTDRDKNLANGAIANLVDEVGG--ALVHGEGLPMSVSVDMSIAFLSKAKLGeELEITSR 119
Cdd:cd03443   3 GIRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGlaALSALPPGALAVTVDLNVNYLRPARGG-DLTARAR 81

                        90       100       110
                ....*....|....*....|....*....|....*
gi 18402093 120 LLGErggyKGTIVVVRNKMT---GEIIAEGRHSMF 151
Cdd:cd03443  82 VVKL----GRRLAVVEVEVTdedGKLVATARGTFA 112
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 42-147 2.55e-09

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 52.64  E-value: 2.55e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402093  42 GIRVNRVEPGFISCSFKVPLRLTDRDKNLANGAIANLVDEVGGALVH---GEGLPMsVSVDMSIAFLSKAKLGEELEITS 118
Cdd:COG2050  22 GIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANsalPPGRRA-VTIELNINFLRPARLGDRLTAEA 100

                        90       100       110
                ....*....|....*....|....*....|..
gi 18402093 119 RLLgERGgykGTIVVVRNKMT---GEIIAEGR 147
Cdd:COG2050 101 RVV-RRG---RRLAVVEVEVTdedGKLVATAT 128
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 69-121 7.13e-06

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: 41.86  E-value: 7.13e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 18402093    69 NLANGAIANLVDEVGGALV--HGEGLPMSVSVDMSIAFLSKAKLGEELEITSRLL 121
Cdd:pfam03061   3 VVHGGVYLALADEAAGAAArrLGGSQQVVVVVELSIDFLRPARLGDRLTVEARVV 57
 
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 ...
 42-151 5.56e-14

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: 64.12  E-value: 5.56e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402093  42 GIRVNRVEPGFISCSFKVPLRLTDRDKNLANGAIANLVDEVGG--ALVHGEGLPMSVSVDMSIAFLSKAKLGeELEITSR 119
Cdd:cd03443   3 GIRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGlaALSALPPGALAVTVDLNVNYLRPARGG-DLTARAR 81

                        90       100       110
                ....*....|....*....|....*....|....*
gi 18402093 120 LLGErggyKGTIVVVRNKMT---GEIIAEGRHSMF 151
Cdd:cd03443  82 VVKL----GRRLAVVEVEVTdedGKLVATARGTFA 112
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 42-147 2.55e-09

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 52.64  E-value: 2.55e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402093  42 GIRVNRVEPGFISCSFKVPLRLTDRDKNLANGAIANLVDEVGGALVH---GEGLPMsVSVDMSIAFLSKAKLGEELEITS 118
Cdd:COG2050  22 GIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANsalPPGRRA-VTIELNINFLRPARLGDRLTAEA 100

                        90       100       110
                ....*....|....*....|....*....|..
gi 18402093 119 RLLgERGgykGTIVVVRNKMT---GEIIAEGR 147
Cdd:COG2050 101 RVV-RRG---RRLAVVEVEVTdedGKLVATAT 128
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 69-121 7.13e-06

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: 41.86  E-value: 7.13e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 18402093    69 NLANGAIANLVDEVGGALV--HGEGLPMSVSVDMSIAFLSKAKLGEELEITSRLL 121
Cdd:pfam03061   3 VVHGGVYLALADEAAGAAArrLGGSQQVVVVVELSIDFLRPARLGDRLTVEARVV 57
 
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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