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Conserved domains on  [gi|1672687034|ref|WP_138328841|]
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MULTISPECIES: thioesterase family protein [Rhizobium]

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 ...
 11-128 1.55e-11

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: 57.60  E-value: 1.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672687034  11 EIRVPFRDVDMNGQMFLASYISYAESVLAGFWSSR----PDVDDEPVYSP-SKVSCMLHRPLHYDEPATFTATVDKIGMH 85
Cdd:COG0824     9 PIRVRFGDTDAMGHVNNANYLRYFEEARTEFLRALglsyAELEEEGIGLVvVEAEIDYLRPARYGDELTVETRVVRLGGS 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1672687034  86 SIGFLVSI--DTGEERAAEVEIIWQARTREDQLPASLPEETRDWL 128
Cdd:COG0824    89 SLTFEYEIfrADDGELLATGETVLVFVDLETGRPVPLPDELRAAL 133
 
Name Accession Description Interval E-value
FadM COG0824
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ...
 11-128 1.55e-11

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: 57.60  E-value: 1.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672687034  11 EIRVPFRDVDMNGQMFLASYISYAESVLAGFWSSR----PDVDDEPVYSP-SKVSCMLHRPLHYDEPATFTATVDKIGMH 85
Cdd:COG0824     9 PIRVRFGDTDAMGHVNNANYLRYFEEARTEFLRALglsyAELEEEGIGLVvVEAEIDYLRPARYGDELTVETRVVRLGGS 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1672687034  86 SIGFLVSI--DTGEERAAEVEIIWQARTREDQLPASLPEETRDWL 128
Cdd:COG0824    89 SLTFEYEIfrADDGELLATGETVLVFVDLETGRPVPLPDELRAAL 133
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
 11-107 4.23e-09

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: 50.68  E-value: 4.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672687034  11 EIRVPFRDVDMNGQMFLASYISYAESVLAGFWS----SRPDVDDEPVYSP-SKVSCMLHRPLHYDEPATFTATVDKIGMH 85
Cdd:cd00586     4 EIRVRFGDTDAAGHVNNARYLRYFEEAREEFLRelglGYDELEEQGLGLVvVELEIDYLRPLRLGDRLTVETRVLRLGRK 83

                          90       100
                  ....*....|....*....|...
gi 1672687034  86 SIGFLVSI-DTGEERAAEVEIIW 107
Cdd:cd00586    84 SFTFEQEIfREDGELLATAETVL 106
4HBT_2 pfam13279
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ...
 14-128 8.93e-03

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: 33.85  E-value: 8.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672687034  14 VPFRDVDMNGQMFLASYISYAESVLAGFWsSRPDVDDEPVYSpSKVSCML-------HRPLHYDEPATFTATVDKIG--- 83
Cdd:pfam13279   1 VRPGDIDANGHMNNARYLRYFEEARDRFL-ERLGLDLAYREA-LGIGLILaeahvryRRELKLGDELTVETRLIDWDakr 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1672687034  84 MHSIGFLVSIDtGEERA-AEVEIIW-QARTREdqlPASLPEETRDWL 128
Cdd:pfam13279  79 FHLEHRFLSPD-GKLVAtAETRLVFvDYETRK---PAPIPEELLEAL 121
 
Name Accession Description Interval E-value
FadM COG0824
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ...
 11-128 1.55e-11

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: 57.60  E-value: 1.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672687034  11 EIRVPFRDVDMNGQMFLASYISYAESVLAGFWSSR----PDVDDEPVYSP-SKVSCMLHRPLHYDEPATFTATVDKIGMH 85
Cdd:COG0824     9 PIRVRFGDTDAMGHVNNANYLRYFEEARTEFLRALglsyAELEEEGIGLVvVEAEIDYLRPARYGDELTVETRVVRLGGS 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1672687034  86 SIGFLVSI--DTGEERAAEVEIIWQARTREDQLPASLPEETRDWL 128
Cdd:COG0824    89 SLTFEYEIfrADDGELLATGETVLVFVDLETGRPVPLPDELRAAL 133
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
 11-107 4.23e-09

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: 50.68  E-value: 4.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672687034  11 EIRVPFRDVDMNGQMFLASYISYAESVLAGFWS----SRPDVDDEPVYSP-SKVSCMLHRPLHYDEPATFTATVDKIGMH 85
Cdd:cd00586     4 EIRVRFGDTDAAGHVNNARYLRYFEEAREEFLRelglGYDELEEQGLGLVvVELEIDYLRPLRLGDRLTVETRVLRLGRK 83

                          90       100
                  ....*....|....*....|...
gi 1672687034  86 SIGFLVSI-DTGEERAAEVEIIW 107
Cdd:cd00586    84 SFTFEQEIfREDGELLATAETVL 106
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 8-107 9.76e-06

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: 41.69  E-value: 9.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672687034   8 DVAEIRVPFRDVDMNGQMFLASYISYAESVLAGFWSSRPDVDDEPVYspSKVSCMLHRPLHYDEPATFTATVDKIGMHSI 87
Cdd:cd03440     1 FVLRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLGGRGLGAVT--LSLDVRFLRPVRPGDTLTVEAEVVRVGRSSV 78

                          90       100
                  ....*....|....*....|.
gi 1672687034  88 GFLVSI-DTGEERAAEVEIIW 107
Cdd:cd03440    79 TVEVEVrNEDGKLVATATATF 99
4HBT_2 pfam13279
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ...
 14-128 8.93e-03

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: 33.85  E-value: 8.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672687034  14 VPFRDVDMNGQMFLASYISYAESVLAGFWsSRPDVDDEPVYSpSKVSCML-------HRPLHYDEPATFTATVDKIG--- 83
Cdd:pfam13279   1 VRPGDIDANGHMNNARYLRYFEEARDRFL-ERLGLDLAYREA-LGIGLILaeahvryRRELKLGDELTVETRLIDWDakr 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1672687034  84 MHSIGFLVSIDtGEERA-AEVEIIW-QARTREdqlPASLPEETRDWL 128
Cdd:pfam13279  79 FHLEHRFLSPD-GKLVAtAETRLVFvDYETRK---PAPIPEELLEAL 121
 
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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