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Conserved domains on  [gi|262077353|gb|ACY13322|]
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4-hydroxybenzoyl-CoA thioesterase [Haliangium ochraceum DSM 14365]

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 ...
4-136 5.45e-21

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: 82.25  E-value: 5.45e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262077353   4 YEYRHVIGLEETNLVGNVYFVNHLRWQGRCREFFLRDHAPGVMEALKRDLVLVTTRCACDYFAELAPFDEITVRMRLGDM 83
Cdd:COG0824    6 FETPIRVRFGDTDAMGHVNNANYLRYFEEARTEFLRALGLSYAELEEEGIGLVVVEAEIDYLRPARYGDELTVETRVVRL 85
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 262077353  84 AQNRITMLFEYVRG--GEVVARGEQQIACMHRlPEGHLLPIsvPDELHDALTPFR 136
Cdd:COG0824   86 GGSSLTFEYEIFRAddGELLATGETVLVFVDL-ETGRPVPL--PDELRAALEALL 137
 
Name Accession Description Interval E-value
FadM COG0824
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ...
4-136 5.45e-21

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: 82.25  E-value: 5.45e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262077353   4 YEYRHVIGLEETNLVGNVYFVNHLRWQGRCREFFLRDHAPGVMEALKRDLVLVTTRCACDYFAELAPFDEITVRMRLGDM 83
Cdd:COG0824    6 FETPIRVRFGDTDAMGHVNNANYLRYFEEARTEFLRALGLSYAELEEEGIGLVVVEAEIDYLRPARYGDELTVETRVVRL 85
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 262077353  84 AQNRITMLFEYVRG--GEVVARGEQQIACMHRlPEGHLLPIsvPDELHDALTPFR 136
Cdd:COG0824   86 GGSSLTFEYEIFRAddGELLATGETVLVFVDL-ETGRPVPL--PDELRAALEALL 137
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
4-111 6.47e-20

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: 78.42  E-value: 6.47e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262077353   4 YEYRHVIGLEETNLVGNVYFVNHLRWQGRCREFFLRDHAPGVMEALKRDLVLVTTRCACDYFAELAPFDEITVRMRLGDM 83
Cdd:cd00586    1 FTLEIRVRFGDTDAAGHVNNARYLRYFEEAREEFLRELGLGYDELEEQGLGLVVVELEIDYLRPLRLGDRLTVETRVLRL 80
                         90       100
                 ....*....|....*....|....*....
gi 262077353  84 AQNRITMLFEYVRG-GEVVARGEQQIACM 111
Cdd:cd00586   81 GRKSFTFEQEIFREdGELLATAETVLVCV 109
4HBT_2 pfam13279
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ...
10-111 1.87e-09

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: 51.96  E-value: 1.87e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262077353   10 IGLEETNLVGNVYFVNHLRWQGRCREFFLRDHapGVMEALKRDL--VLVTTRCACDYFAELAPFDEITVRMRLGDMAQNR 87
Cdd:pfam13279   1 VRPGDIDANGHMNNARYLRYFEEARDRFLERL--GLDLAYREALgiGLILAEAHVRYRRELKLGDELTVETRLIDWDAKR 78
                          90       100
                  ....*....|....*....|....*
gi 262077353   88 ITMLFE-YVRGGEVVARGEQQIACM 111
Cdd:pfam13279  79 FHLEHRfLSPDGKLVATAETRLVFV 103
TIGR00051 TIGR00051
acyl-CoA thioester hydrolase, YbgC/YbaW family; This model describes a subset of related ...
13-95 4.92e-06

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: 42.79  E-value: 4.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262077353   13 EETNLVGNVYFVNHLRWQGRCREFFLRDHA--PGVMEALKRDLVLVTTrcACDYFAELAPFDEITVRMRLGDMaqNRITM 90
Cdd:TIGR00051   7 EDTDAQGIVYHANYLRYCERARTEFLRSLGfpQSVLRAEGVAFVVVNI--NIEYKKPARLDDVLEIRTQIEEL--NGFSF 82

                  ....*
gi 262077353   91 LFEYV 95
Cdd:TIGR00051  83 VFSQE 87
 
Name Accession Description Interval E-value
FadM COG0824
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ...
4-136 5.45e-21

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: 82.25  E-value: 5.45e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262077353   4 YEYRHVIGLEETNLVGNVYFVNHLRWQGRCREFFLRDHAPGVMEALKRDLVLVTTRCACDYFAELAPFDEITVRMRLGDM 83
Cdd:COG0824    6 FETPIRVRFGDTDAMGHVNNANYLRYFEEARTEFLRALGLSYAELEEEGIGLVVVEAEIDYLRPARYGDELTVETRVVRL 85
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 262077353  84 AQNRITMLFEYVRG--GEVVARGEQQIACMHRlPEGHLLPIsvPDELHDALTPFR 136
Cdd:COG0824   86 GGSSLTFEYEIFRAddGELLATGETVLVFVDL-ETGRPVPL--PDELRAALEALL 137
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
4-111 6.47e-20

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: 78.42  E-value: 6.47e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262077353   4 YEYRHVIGLEETNLVGNVYFVNHLRWQGRCREFFLRDHAPGVMEALKRDLVLVTTRCACDYFAELAPFDEITVRMRLGDM 83
Cdd:cd00586    1 FTLEIRVRFGDTDAAGHVNNARYLRYFEEAREEFLRELGLGYDELEEQGLGLVVVELEIDYLRPLRLGDRLTVETRVLRL 80
                         90       100
                 ....*....|....*....|....*....
gi 262077353  84 AQNRITMLFEYVRG-GEVVARGEQQIACM 111
Cdd:cd00586   81 GRKSFTFEQEIFREdGELLATAETVLVCV 109
4HBT_2 pfam13279
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ...
10-111 1.87e-09

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: 51.96  E-value: 1.87e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262077353   10 IGLEETNLVGNVYFVNHLRWQGRCREFFLRDHapGVMEALKRDL--VLVTTRCACDYFAELAPFDEITVRMRLGDMAQNR 87
Cdd:pfam13279   1 VRPGDIDANGHMNNARYLRYFEEARDRFLERL--GLDLAYREALgiGLILAEAHVRYRRELKLGDELTVETRLIDWDAKR 78
                          90       100
                  ....*....|....*....|....*
gi 262077353   88 ITMLFE-YVRGGEVVARGEQQIACM 111
Cdd:pfam13279  79 FHLEHRfLSPDGKLVATAETRLVFV 103
TIGR00051 TIGR00051
acyl-CoA thioester hydrolase, YbgC/YbaW family; This model describes a subset of related ...
13-95 4.92e-06

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: 42.79  E-value: 4.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262077353   13 EETNLVGNVYFVNHLRWQGRCREFFLRDHA--PGVMEALKRDLVLVTTrcACDYFAELAPFDEITVRMRLGDMaqNRITM 90
Cdd:TIGR00051   7 EDTDAQGIVYHANYLRYCERARTEFLRSLGfpQSVLRAEGVAFVVVNI--NIEYKKPARLDDVLEIRTQIEEL--NGFSF 82

                  ....*
gi 262077353   91 LFEYV 95
Cdd:TIGR00051  83 VFSQE 87
 
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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