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Conserved domains on  [gi|980525743|gb|KWI02654|]
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4-hydroxybenzoyl-CoA thioesterase [Burkholderia stagnalis]

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 ...
 27-157 9.22e-12

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: 59.14  E-value: 9.22e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 980525743  27 SKKTFHHVIDIYLKDSNAFMNTYFARYFEWQGVTRERWFHEC--IHDNLLAAGGSFVTKRAHQEYIQETFPFQRVDCYLN 104
Cdd:COG0824    2 TLFTFETPIRVRFGDTDAMGHVNNANYLRYFEEARTEFLRALglSYAELEEEGIGLVVVEAEIDYLRPARYGDELTVETR 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 980525743 105 TWQVRQCSAYLLFRFC--IDGRPVSLGYQQIIFAGTDK-RIRRFPAGIVERVKEYE 157
Cdd:COG0824   82 VVRLGGSSLTFEYEIFraDDGELLATGETVLVFVDLETgRPVPLPDELRAALEALL 137
 
Name Accession Description Interval E-value
FadM COG0824
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ...
 27-157 9.22e-12

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: 59.14  E-value: 9.22e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 980525743  27 SKKTFHHVIDIYLKDSNAFMNTYFARYFEWQGVTRERWFHEC--IHDNLLAAGGSFVTKRAHQEYIQETFPFQRVDCYLN 104
Cdd:COG0824    2 TLFTFETPIRVRFGDTDAMGHVNNANYLRYFEEARTEFLRALglSYAELEEEGIGLVVVEAEIDYLRPARYGDELTVETR 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 980525743 105 TWQVRQCSAYLLFRFC--IDGRPVSLGYQQIIFAGTDK-RIRRFPAGIVERVKEYE 157
Cdd:COG0824   82 VVRLGGSSLTFEYEIFraDDGELLATGETVLVFVDLETgRPVPLPDELRAALEALL 137
4HBT_2 pfam13279
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ...
 41-153 6.06e-08

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: 48.49  E-value: 6.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 980525743   41 DSNAFMNtyFARYFEWQGVTRERWFHE--CIHDNLLAAGGSFVTKRAHQEYIQETFPFQRVDCYLNTWQVRQCSAYLLFR 118
Cdd:pfam13279   7 DANGHMN--NARYLRYFEEARDRFLERlgLDLAYREALGIGLILAEAHVRYRRELKLGDELTVETRLIDWDAKRFHLEHR 84

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 980525743  119 F-CIDGRPVSLGYQQIIFAGTDKRIR-RFPAGIVERV 153
Cdd:pfam13279  85 FlSPDGKLVATAETRLVFVDYETRKPaPIPEELLEAL 121
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
 31-135 1.96e-07

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: 46.83  E-value: 1.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 980525743  31 FHHVIDIYLKDSNAFMNTYFARYFEWQGVTRERWFHEC--IHDNLLAAGGSFVTKRAHQEYIQETFPFQRVDCYLNTWQV 108
Cdd:cd00586    1 FTLEIRVRFGDTDAAGHVNNARYLRYFEEAREEFLRELglGYDELEEQGLGLVVVELEIDYLRPLRLGDRLTVETRVLRL 80

                         90       100
                 ....*....|....*....|....*...
gi 980525743 109 RQCSAYLLFRFCI-DGRPVSLGYQQIIF 135
Cdd:cd00586   81 GRKSFTFEQEIFReDGELLATAETVLVC 108
 
Name Accession Description Interval E-value
FadM COG0824
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ...
 27-157 9.22e-12

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: 59.14  E-value: 9.22e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 980525743  27 SKKTFHHVIDIYLKDSNAFMNTYFARYFEWQGVTRERWFHEC--IHDNLLAAGGSFVTKRAHQEYIQETFPFQRVDCYLN 104
Cdd:COG0824    2 TLFTFETPIRVRFGDTDAMGHVNNANYLRYFEEARTEFLRALglSYAELEEEGIGLVVVEAEIDYLRPARYGDELTVETR 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 980525743 105 TWQVRQCSAYLLFRFC--IDGRPVSLGYQQIIFAGTDK-RIRRFPAGIVERVKEYE 157
Cdd:COG0824   82 VVRLGGSSLTFEYEIFraDDGELLATGETVLVFVDLETgRPVPLPDELRAALEALL 137
4HBT_2 pfam13279
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ...
 41-153 6.06e-08

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: 48.49  E-value: 6.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 980525743   41 DSNAFMNtyFARYFEWQGVTRERWFHE--CIHDNLLAAGGSFVTKRAHQEYIQETFPFQRVDCYLNTWQVRQCSAYLLFR 118
Cdd:pfam13279   7 DANGHMN--NARYLRYFEEARDRFLERlgLDLAYREALGIGLILAEAHVRYRRELKLGDELTVETRLIDWDAKRFHLEHR 84

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 980525743  119 F-CIDGRPVSLGYQQIIFAGTDKRIR-RFPAGIVERV 153
Cdd:pfam13279  85 FlSPDGKLVATAETRLVFVDYETRKPaPIPEELLEAL 121
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
 31-135 1.96e-07

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: 46.83  E-value: 1.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 980525743  31 FHHVIDIYLKDSNAFMNTYFARYFEWQGVTRERWFHEC--IHDNLLAAGGSFVTKRAHQEYIQETFPFQRVDCYLNTWQV 108
Cdd:cd00586    1 FTLEIRVRFGDTDAAGHVNNARYLRYFEEAREEFLRELglGYDELEEQGLGLVVVELEIDYLRPLRLGDRLTVETRVLRL 80

                         90       100
                 ....*....|....*....|....*...
gi 980525743 109 RQCSAYLLFRFCI-DGRPVSLGYQQIIF 135
Cdd:cd00586   81 GRKSFTFEQEIFReDGELLATAETVLVC 108
 
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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