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Conserved domains on  [gi|1519315147|ref|NP_872384|]
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acyl-coenzyme A thioesterase THEM5 [Homo sapiens]

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 ...
 141-237 1.46e-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: 54.10  E-value: 1.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315147 141 VCLFQPGSYLEGPPGFAHGGSLAAMMDETFS---KTAFLAGEGLFTLSLNIRFKNLIPVDSLVVmDVELDKIEDQKLYMS 217
Cdd:cd03443    15 VLRLPVRPRHLNPGGIVHGGAIATLADTAGGlaaLSALPPGALAVTVDLNVNYLRPARGGDLTA-RARVVKLGRRLAVVE 93

                          90       100
                  ....*....|....*....|
gi 1519315147 218 CIAHSRDQQTVyAKSSGVFL 237
Cdd:cd03443    94 VEVTDEDGKLV-ATARGTFA 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 ...
 141-237 1.46e-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: 54.10  E-value: 1.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315147 141 VCLFQPGSYLEGPPGFAHGGSLAAMMDETFS---KTAFLAGEGLFTLSLNIRFKNLIPVDSLVVmDVELDKIEDQKLYMS 217
Cdd:cd03443    15 VLRLPVRPRHLNPGGIVHGGAIATLADTAGGlaaLSALPPGALAVTVDLNVNYLRPARGGDLTA-RARVVKLGRRLAVVE 93

                          90       100
                  ....*....|....*....|
gi 1519315147 218 CIAHSRDQQTVyAKSSGVFL 237
Cdd:cd03443    94 VEVTDEDGKLV-ATARGTFA 112
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 141-237 1.59e-08

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 51.87  E-value: 1.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315147 141 VCLFQPGSYLEGPPGFAHGGSLAAMMDETFSKTAFLA---GEGLFTLSLNIRFKNLIPVDSLVVMDVELDKIEDQKLYMS 217
Cdd:COG2050    34 VLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSAlppGRRAVTIELNINFLRPARLGDRLTAEARVVRRGRRLAVVE 113

                          90       100
                  ....*....|....*....|
gi 1519315147 218 CIAHSrDQQTVYAKSSGVFL 237
Cdd:COG2050   114 VEVTD-EDGKLVATATGTFA 132
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 155-228 1.37e-05

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: 42.24  E-value: 1.37e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1519315147 155 GFAHGGSLAAMMDETFSKTAFLAGEG---LFTLSLNIRFKNLIPVDSLVVMDVELDKIEDQKLYMSCIAHSRDQQTV 228
Cdd:pfam03061   2 GVVHGGVYLALADEAAGAAARRLGGSqqvVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDEDGRLV 78
 
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 ...
 141-237 1.46e-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: 54.10  E-value: 1.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315147 141 VCLFQPGSYLEGPPGFAHGGSLAAMMDETFS---KTAFLAGEGLFTLSLNIRFKNLIPVDSLVVmDVELDKIEDQKLYMS 217
Cdd:cd03443    15 VLRLPVRPRHLNPGGIVHGGAIATLADTAGGlaaLSALPPGALAVTVDLNVNYLRPARGGDLTA-RARVVKLGRRLAVVE 93

                          90       100
                  ....*....|....*....|
gi 1519315147 218 CIAHSRDQQTVyAKSSGVFL 237
Cdd:cd03443    94 VEVTDEDGKLV-ATARGTFA 112
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 141-237 1.59e-08

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 51.87  E-value: 1.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315147 141 VCLFQPGSYLEGPPGFAHGGSLAAMMDETFSKTAFLA---GEGLFTLSLNIRFKNLIPVDSLVVMDVELDKIEDQKLYMS 217
Cdd:COG2050    34 VLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSAlppGRRAVTIELNINFLRPARLGDRLTAEARVVRRGRRLAVVE 113

                          90       100
                  ....*....|....*....|
gi 1519315147 218 CIAHSrDQQTVYAKSSGVFL 237
Cdd:COG2050   114 VEVTD-EDGKLVATATGTFA 132
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 153-237 1.66e-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: 48.24  E-value: 1.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315147 153 PPGFAHGGSLAAMMDETFSKTAFLAGE---GLFTLSLNIRFKNLIPVDSLVVMDVELDKIEDQKLYMSCIAHSRDQQTVy 229
Cdd:cd03440    14 GGGIVHGGLLLALADEAAGAAAARLGGrglGAVTLSLDVRFLRPVRPGDTLTVEAEVVRVGRSSVTVEVEVRNEDGKLV- 92


                  ....*...
gi 1519315147 230 AKSSGVFL 237
Cdd:cd03440    93 ATATATFV 100
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 155-228 1.37e-05

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: 42.24  E-value: 1.37e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1519315147 155 GFAHGGSLAAMMDETFSKTAFLAGEG---LFTLSLNIRFKNLIPVDSLVVMDVELDKIEDQKLYMSCIAHSRDQQTV 228
Cdd:pfam03061   2 GVVHGGVYLALADEAAGAAARRLGGSqqvVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDEDGRLV 78
 
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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