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Conserved domains on  [gi|490442108|ref|WP_004313074|]
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MULTISPECIES: thioesterase family protein [Bacteroidaceae]

Protein Classification

acyl-CoA thioesterase( domain architecture ID 10002786)

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
FadM COG0824
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ...
 6-138 1.67e-34

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: 116.92  E-value: 1.67e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442108   6 FHHTLPIQLRFNDVDKFGHVNNTVYFSFYDLGKTEYFASVCPGVDW---EKIGIVVVHIEADFVKQIFASDHIAVQTAVS 82
Cdd:COG0824    4 FTFETPIRVRFGDTDAMGHVNNANYLRYFEEARTEFLRALGLSYAEleeEGIGLVVVEAEIDYLRPARYGDELTVETRVV 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 490442108  83 KIGTKSFHLIQRVIDTETNEVKCICKSVMVTFDLERHESMPLTEEWIEAICKYEER 138
Cdd:COG0824   84 RLGGSSLTFEYEIFRADDGELLATGETVLVFVDLETGRPVPLPDELRAALEALLAA 139
 
Name Accession Description Interval E-value
FadM COG0824
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ...
 6-138 1.67e-34

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: 116.92  E-value: 1.67e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442108   6 FHHTLPIQLRFNDVDKFGHVNNTVYFSFYDLGKTEYFASVCPGVDW---EKIGIVVVHIEADFVKQIFASDHIAVQTAVS 82
Cdd:COG0824    4 FTFETPIRVRFGDTDAMGHVNNANYLRYFEEARTEFLRALGLSYAEleeEGIGLVVVEAEIDYLRPARYGDELTVETRVV 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 490442108  83 KIGTKSFHLIQRVIDTETNEVKCICKSVMVTFDLERHESMPLTEEWIEAICKYEER 138
Cdd:COG0824   84 RLGGSSLTFEYEIFRADDGELLATGETVLVFVDLETGRPVPLPDELRAALEALLAA 139
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
 8-115 1.31e-26

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: 95.75  E-value: 1.31e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442108   8 HTLPIQLRFNDVDKFGHVNNTVYFSFYDLGKTEYFASVCPGVDW---EKIGIVVVHIEADFVKQIFASDHIAVQTAVSKI 84
Cdd:cd00586    1 FTLEIRVRFGDTDAAGHVNNARYLRYFEEAREEFLRELGLGYDEleeQGLGLVVVELEIDYLRPLRLGDRLTVETRVLRL 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 490442108  85 GTKSFHLIQRVIDtETNEVKCICKSVMVTFD 115
Cdd:cd00586   81 GRKSFTFEQEIFR-EDGELLATAETVLVCVD 110
4HBT_2 pfam13279
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ...
 15-132 6.14e-19

Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally thioesterases. These enzymes are part of the Hotdog fold superfamily.


Pssm-ID: 463826  Cd Length: 121  Bit Score: 76.61  E-value: 6.14e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442108   15 RFNDVDKFGHVNNTVYFSFYDLGKTEYFASVcpGVDWE-----KIGIVVVHIEADFVKQIFASDHIAVQTAVSKIGTKSF 89
Cdd:pfam13279   2 RPGDIDANGHMNNARYLRYFEEARDRFLERL--GLDLAyrealGIGLILAEAHVRYRRELKLGDELTVETRLIDWDAKRF 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 490442108   90 HLIQRVIDTETNEVkCICKSVMVTFDLERHESMPLTEEWIEAI 132
Cdd:pfam13279  80 HLEHRFLSPDGKLV-ATAETRLVFVDYETRKPAPIPEELLEAL 121
TIGR00051 TIGR00051
acyl-CoA thioester hydrolase, YbgC/YbaW family; This model describes a subset of related ...
 11-95 3.34e-07

acyl-CoA thioester hydrolase, YbgC/YbaW family; This model describes a subset of related acyl-CoA thioesterases that include several at least partially characterized proteins. YbgC is an acyl-CoA thioesterase associated with the Tol-Pal system. YbaW is part of the FadM regulon. [Unknown function, General]


Pssm-ID: 129161 [Multi-domain]  Cd Length: 117  Bit Score: 45.87  E-value: 3.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442108   11 PIQLRFNDVDKFGHVNNTVYFSFYDLGKTEYF-ASVCPGVDWEKIGI--VVVHIEADFVKQIFASDHIAVQTAVSKIGTK 87
Cdd:TIGR00051   1 PVRVYYEDTDAQGIVYHANYLRYCERARTEFLrSLGFPQSVLRAEGVafVVVNINIEYKKPARLDDVLEIRTQIEELNGF 80


                  ....*...
gi 490442108   88 SFHLIQRV 95
Cdd:TIGR00051  81 SFVFSQEI 88
 
Name Accession Description Interval E-value
FadM COG0824
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ...
 6-138 1.67e-34

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: 116.92  E-value: 1.67e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442108   6 FHHTLPIQLRFNDVDKFGHVNNTVYFSFYDLGKTEYFASVCPGVDW---EKIGIVVVHIEADFVKQIFASDHIAVQTAVS 82
Cdd:COG0824    4 FTFETPIRVRFGDTDAMGHVNNANYLRYFEEARTEFLRALGLSYAEleeEGIGLVVVEAEIDYLRPARYGDELTVETRVV 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 490442108  83 KIGTKSFHLIQRVIDTETNEVKCICKSVMVTFDLERHESMPLTEEWIEAICKYEER 138
Cdd:COG0824   84 RLGGSSLTFEYEIFRADDGELLATGETVLVFVDLETGRPVPLPDELRAALEALLAA 139
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
 8-115 1.31e-26

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: 95.75  E-value: 1.31e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442108   8 HTLPIQLRFNDVDKFGHVNNTVYFSFYDLGKTEYFASVCPGVDW---EKIGIVVVHIEADFVKQIFASDHIAVQTAVSKI 84
Cdd:cd00586    1 FTLEIRVRFGDTDAAGHVNNARYLRYFEEAREEFLRELGLGYDEleeQGLGLVVVELEIDYLRPLRLGDRLTVETRVLRL 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 490442108  85 GTKSFHLIQRVIDtETNEVKCICKSVMVTFD 115
Cdd:cd00586   81 GRKSFTFEQEIFR-EDGELLATAETVLVCVD 110
4HBT_2 pfam13279
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ...
 15-132 6.14e-19

Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally thioesterases. These enzymes are part of the Hotdog fold superfamily.


Pssm-ID: 463826  Cd Length: 121  Bit Score: 76.61  E-value: 6.14e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442108   15 RFNDVDKFGHVNNTVYFSFYDLGKTEYFASVcpGVDWE-----KIGIVVVHIEADFVKQIFASDHIAVQTAVSKIGTKSF 89
Cdd:pfam13279   2 RPGDIDANGHMNNARYLRYFEEARDRFLERL--GLDLAyrealGIGLILAEAHVRYRRELKLGDELTVETRLIDWDAKRF 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 490442108   90 HLIQRVIDTETNEVkCICKSVMVTFDLERHESMPLTEEWIEAI 132
Cdd:pfam13279  80 HLEHRFLSPDGKLV-ATAETRLVFVDYETRKPAPIPEELLEAL 121
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 8-112 3.23e-09

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: 50.94  E-value: 3.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442108   8 HTLPIQLRFNDVDKFGHVNNTVYFSFYDLGKTEYFASVCPgvdwEKIGIVVVHIEADFVKQIFASDHIAVQTAVSKIGTK 87
Cdd:cd03440    1 FVLRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLGG----RGLGAVTLSLDVRFLRPVRPGDTLTVEAEVVRVGRS 76

                         90       100
                 ....*....|....*....|....*
gi 490442108  88 SFHLIQRVIDtETNEVKCICKSVMV 112
Cdd:cd03440   77 SVTVEVEVRN-EDGKLVATATATFV 100
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 22-104 5.89e-09

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: 49.56  E-value: 5.89e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442108   22 FGHVNNTVYFSFYDLGKTEYFASVCPGvdweKIGIVVVHIEADFVKQIFASDHIAVQTAVSKIGTKSFHLIQRVIDTETN 101
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGS----QQVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDEDGR 76


                  ...
gi 490442108  102 EVK 104
Cdd:pfam03061  77 LVA 79
TIGR00051 TIGR00051
acyl-CoA thioester hydrolase, YbgC/YbaW family; This model describes a subset of related ...
 11-95 3.34e-07

acyl-CoA thioester hydrolase, YbgC/YbaW family; This model describes a subset of related acyl-CoA thioesterases that include several at least partially characterized proteins. YbgC is an acyl-CoA thioesterase associated with the Tol-Pal system. YbaW is part of the FadM regulon. [Unknown function, General]


Pssm-ID: 129161 [Multi-domain]  Cd Length: 117  Bit Score: 45.87  E-value: 3.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442108   11 PIQLRFNDVDKFGHVNNTVYFSFYDLGKTEYF-ASVCPGVDWEKIGI--VVVHIEADFVKQIFASDHIAVQTAVSKIGTK 87
Cdd:TIGR00051   1 PVRVYYEDTDAQGIVYHANYLRYCERARTEFLrSLGFPQSVLRAEGVafVVVNINIEYKKPARLDDVLEIRTQIEELNGF 80


                  ....*...
gi 490442108   88 SFHLIQRV 95
Cdd:TIGR00051  81 SFVFSQEI 88
FatA COG3884
Acyl-ACP thioesterase [Lipid transport and metabolism];
6-111 1.27e-06

Acyl-ACP thioesterase [Lipid transport and metabolism];


Pssm-ID: 443092 [Multi-domain]  Cd Length: 242  Bit Score: 46.10  E-value: 1.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442108   6 FHHTLPIQLRFNDVDKFGHVNNTVYFSFYDlgktEYFAsvcpgVDWEKiGIVVVHIEADFVKQIFASDHIAVQTAVSKIG 85
Cdd:COG3884  148 DEEEKEFTVRYSDIDTNGHVNNARYLEWAL----DALP-----LEFLK-NHRLKRLEINYLKEVRLGDTVEVRSARDEDG 217

                         90       100
                 ....*....|....*....|....*.
gi 490442108  86 tksfHLIQRVIDTETNEVKCICKSVM 111
Cdd:COG3884  218 ----RTLHRIVGDDDGKELARARIEW 239
 
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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