NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|627945168|gb|KCV67298|]
View 

hypothetical protein H696_06281 [Fonticula alba]

Protein Classification

thioesterase family protein( domain architecture ID 10594194)

thioesterase family protein belonging to the Hotdog fold superfamily, similar to 1,4-dihydroxy-2-naphthoyl-CoA hydrolase, which catalyzes the hydrolysis of 1,4-dihydroxy-2-naphthoyl-CoA (DHNA-CoA) to 1,4-dihydroxy-2-naphthoate (DHNA) during the synthesis of menaquinones and phylloquinone (vitamin K1)

CATH:  3.10.129.10
Gene Ontology:  GO:0016790
PubMed:  15307895
SCOP:  3000149

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
4HBT_2 pfam13279
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ...
77-186 4.19e-16

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: 71.99  E-value: 4.19e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627945168   77 VGFDSMDYNFHMNNGTYCRIADYGRAALL--LPVVLGAARRNGWKVANGGVTMVFRRELMVGSAYTATTRVRSFDDKWFV 154
Cdd:pfam13279   1 VRPGDIDANGHMNNARYLRYFEEARDRFLerLGLDLAYREALGIGLILAEAHVRYRRELKLGDELTVETRLIDWDAKRFH 80
                          90       100       110
                  ....*....|....*....|....*....|...
gi 627945168  155 LEHKFIS-GGRVVAIGVCRMVIKERSGRTLPPV 186
Cdd:pfam13279  81 LEHRFLSpDGKLVATAETRLVFVDYETRKPAPI 113
 
Name Accession Description Interval E-value
4HBT_2 pfam13279
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ...
77-186 4.19e-16

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: 71.99  E-value: 4.19e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627945168   77 VGFDSMDYNFHMNNGTYCRIADYGRAALL--LPVVLGAARRNGWKVANGGVTMVFRRELMVGSAYTATTRVRSFDDKWFV 154
Cdd:pfam13279   1 VRPGDIDANGHMNNARYLRYFEEARDRFLerLGLDLAYREALGIGLILAEAHVRYRRELKLGDELTVETRLIDWDAKRFH 80
                          90       100       110
                  ....*....|....*....|....*....|...
gi 627945168  155 LEHKFIS-GGRVVAIGVCRMVIKERSGRTLPPV 186
Cdd:pfam13279  81 LEHRFLSpDGKLVATAETRLVFVDYETRKPAPI 113
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
72-174 9.16e-12

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: 59.93  E-value: 9.16e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627945168  72 TTSHRVGFDSMDYNFHMNNGTYCRIADYGRAALLLPVVLGAA--RRNGWKVANGGVTMVFRRELMVGSAYTATTRVRSFD 149
Cdd:cd00586    2 TLEIRVRFGDTDAAGHVNNARYLRYFEEAREEFLRELGLGYDelEEQGLGLVVVELEIDYLRPLRLGDRLTVETRVLRLG 81
                         90       100
                 ....*....|....*....|....*.
gi 627945168 150 DKWFVLEHKFISG-GRVVAIGVCRMV 174
Cdd:cd00586   82 RKSFTFEQEIFREdGELLATAETVLV 107
FadM COG0824
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ...
72-174 2.53e-10

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: 56.83  E-value: 2.53e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627945168  72 TTSHRVGFDSMDYNFHMNNGTYCRIADYGRAALL--LPVVLGAARRNGWKVANGGVTMVFRRELMVGSAYTATTRVRSFD 149
Cdd:COG0824    7 ETPIRVRFGDTDAMGHVNNANYLRYFEEARTEFLraLGLSYAELEEEGIGLVVVEAEIDYLRPARYGDELTVETRVVRLG 86
                         90       100
                 ....*....|....*....|....*..
gi 627945168 150 DKWFVLEHKFI--SGGRVVAIGVCRMV 174
Cdd:COG0824   87 GSSLTFEYEIFraDDGELLATGETVLV 113
 
Name Accession Description Interval E-value
4HBT_2 pfam13279
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ...
77-186 4.19e-16

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: 71.99  E-value: 4.19e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627945168   77 VGFDSMDYNFHMNNGTYCRIADYGRAALL--LPVVLGAARRNGWKVANGGVTMVFRRELMVGSAYTATTRVRSFDDKWFV 154
Cdd:pfam13279   1 VRPGDIDANGHMNNARYLRYFEEARDRFLerLGLDLAYREALGIGLILAEAHVRYRRELKLGDELTVETRLIDWDAKRFH 80
                          90       100       110
                  ....*....|....*....|....*....|...
gi 627945168  155 LEHKFIS-GGRVVAIGVCRMVIKERSGRTLPPV 186
Cdd:pfam13279  81 LEHRFLSpDGKLVATAETRLVFVDYETRKPAPI 113
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
72-174 9.16e-12

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: 59.93  E-value: 9.16e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627945168  72 TTSHRVGFDSMDYNFHMNNGTYCRIADYGRAALLLPVVLGAA--RRNGWKVANGGVTMVFRRELMVGSAYTATTRVRSFD 149
Cdd:cd00586    2 TLEIRVRFGDTDAAGHVNNARYLRYFEEAREEFLRELGLGYDelEEQGLGLVVVELEIDYLRPLRLGDRLTVETRVLRLG 81
                         90       100
                 ....*....|....*....|....*.
gi 627945168 150 DKWFVLEHKFISG-GRVVAIGVCRMV 174
Cdd:cd00586   82 RKSFTFEQEIFREdGELLATAETVLV 107
FadM COG0824
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ...
72-174 2.53e-10

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: 56.83  E-value: 2.53e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627945168  72 TTSHRVGFDSMDYNFHMNNGTYCRIADYGRAALL--LPVVLGAARRNGWKVANGGVTMVFRRELMVGSAYTATTRVRSFD 149
Cdd:COG0824    7 ETPIRVRFGDTDAMGHVNNANYLRYFEEARTEFLraLGLSYAELEEEGIGLVVVEAEIDYLRPARYGDELTVETRVVRLG 86
                         90       100
                 ....*....|....*....|....*..
gi 627945168 150 DKWFVLEHKFI--SGGRVVAIGVCRMV 174
Cdd:COG0824   87 GSSLTFEYEIFraDDGELLATGETVLV 113
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
71-174 1.30e-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: 39.77  E-value: 1.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627945168  71 ITTSHRVGFDSMDYNFHMNNGTYCRIADYGRAALLLPVVLGaarrnGWKVANGGVTMVFRRELMVGSAYTATTRVRSFDD 150
Cdd:cd03440    1 FVLRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLGGR-----GLGAVTLSLDVRFLRPVRPGDTLTVEAEVVRVGR 75
                         90       100
                 ....*....|....*....|....*
gi 627945168 151 KWFVLEHKFISG-GRVVAIGVCRMV 174
Cdd:cd03440   76 SSVTVEVEVRNEdGKLVATATATFV 100
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH