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Conserved domains on  [gi|2148409036|ref|XP_006050863|]
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acyl-coenzyme A thioesterase THEM5 [Bubalus bubalis]

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 ...
 136-237 1.62e-08

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: 51.40  E-value: 1.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2148409036 136 SEKKSVCLFQPGPSLEGVPGFTHGGSLAALIDETFSKTAYLS---GEGLLTVNFNIRFKNLIPLGSLaVLNVNVEKIEDQ 212
Cdd:cd03443    10 GPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSAlppGALAVTVDLNVNYLRPARGGDL-TARARVVKLGRR 88

                          90       100
                  ....*....|....*....|....*.
gi 2148409036 213 KMYLSC-VTQsrDQQTVYAKASGTFL 237
Cdd:cd03443    89 LAVVEVeVTD--EDGKLVATARGTFA 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 ...
 136-237 1.62e-08

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: 51.40  E-value: 1.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2148409036 136 SEKKSVCLFQPGPSLEGVPGFTHGGSLAALIDETFSKTAYLS---GEGLLTVNFNIRFKNLIPLGSLaVLNVNVEKIEDQ 212
Cdd:cd03443    10 GPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSAlppGALAVTVDLNVNYLRPARGGDL-TARARVVKLGRR 88

                          90       100
                  ....*....|....*....|....*.
gi 2148409036 213 KMYLSC-VTQsrDQQTVYAKASGTFL 237
Cdd:cd03443    89 LAVVEVeVTD--EDGKLVATARGTFA 112
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 136-239 3.12e-08

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 51.10  E-value: 3.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2148409036 136 SEKKSVCLFQPGPSLEGVPGFTHGGSLAALIDETFSKTAYLS---GEGLLTVNFNIRFKNLIPLGSLAVLNVNVEKIEDQ 212
Cdd:COG2050    29 EPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSAlppGRRAVTIELNINFLRPARLGDRLTAEARVVRRGRR 108

                          90       100
                  ....*....|....*....|....*...
gi 2148409036 213 KMYLSC-VTQsrDQQTVYAKASGTFLQM 239
Cdd:COG2050   109 LAVVEVeVTD--EDGKLVATATGTFAVL 134
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 155-218 1.91e-03

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: 36.08  E-value: 1.91e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2148409036 155 GFTHGGSLAALIDETFSKTAYLSGEG---LLTVNFNIRFKNLIPLGSLAVLNVNVEKIEDQKMYLSC 218
Cdd:pfam03061   2 GVVHGGVYLALADEAAGAAARRLGGSqqvVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEV 68
 
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 ...
 136-237 1.62e-08

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: 51.40  E-value: 1.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2148409036 136 SEKKSVCLFQPGPSLEGVPGFTHGGSLAALIDETFSKTAYLS---GEGLLTVNFNIRFKNLIPLGSLaVLNVNVEKIEDQ 212
Cdd:cd03443    10 GPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSAlppGALAVTVDLNVNYLRPARGGDL-TARARVVKLGRR 88

                          90       100
                  ....*....|....*....|....*.
gi 2148409036 213 KMYLSC-VTQsrDQQTVYAKASGTFL 237
Cdd:cd03443    89 LAVVEVeVTD--EDGKLVATARGTFA 112
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 136-239 3.12e-08

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 51.10  E-value: 3.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2148409036 136 SEKKSVCLFQPGPSLEGVPGFTHGGSLAALIDETFSKTAYLS---GEGLLTVNFNIRFKNLIPLGSLAVLNVNVEKIEDQ 212
Cdd:COG2050    29 EPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSAlppGRRAVTIELNINFLRPARLGDRLTAEARVVRRGRR 108

                          90       100
                  ....*....|....*....|....*...
gi 2148409036 213 KMYLSC-VTQsrDQQTVYAKASGTFLQM 239
Cdd:COG2050   109 LAVVEVeVTD--EDGKLVATATGTFAVL 134
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 155-237 5.18e-04

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: 38.23  E-value: 5.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2148409036 155 GFTHGGSLAALIDETFSKTAYLSGE---GLLTVNFNIRFKNLIPLGSLAVLNVNVEKIEDQKMYLSCVTQSRDQQTVyAK 231
Cdd:cd03440    16 GIVHGGLLLALADEAAGAAAARLGGrglGAVTLSLDVRFLRPVRPGDTLTVEAEVVRVGRSSVTVEVEVRNEDGKLV-AT 94


                  ....*.
gi 2148409036 232 ASGTFL 237
Cdd:cd03440    95 ATATFV 100
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 155-218 1.91e-03

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: 36.08  E-value: 1.91e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2148409036 155 GFTHGGSLAALIDETFSKTAYLSGEG---LLTVNFNIRFKNLIPLGSLAVLNVNVEKIEDQKMYLSC 218
Cdd:pfam03061   2 GVVHGGVYLALADEAAGAAARRLGGSqqvVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEV 68
 
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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