NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1084963442|gb|OGR77919|]
View 

hypothetical protein A2X40_09145 [Elusimicrobia bacterium GWC2_65_9]

Protein Classification

thioesterase family protein( domain architecture ID 10002786)

thioesterase family protein such as 1,4-dihydroxy-2-naphthoyl-CoA (DHNA-CoA) hydrolase, which catalyzes the hydrolysis of DHNA-CoA to form 1,4-dihydroxy-2-naphthoate (DHNA)

EC:  3.1.2.-

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
1-62 1.19e-08

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: 47.59  E-value: 1.19e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1084963442   1 MRTWIAELGRASVVFECDVLDRELGaKVVARGYSRHALVD-DLWRIARMPDDLRGLMAPFVGR 62
Cdd:COG0824    78 VETRVVRLGGSSLTFEYEIFRADDG-ELLATGETVLVFVDlETGRPVPLPDELRAALEALLAA 139
 
Name Accession Description Interval E-value
FadM COG0824
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ...
1-62 1.19e-08

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: 47.59  E-value: 1.19e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1084963442   1 MRTWIAELGRASVVFECDVLDRELGaKVVARGYSRHALVD-DLWRIARMPDDLRGLMAPFVGR 62
Cdd:COG0824    78 VETRVVRLGGSSLTFEYEIFRADDG-ELLATGETVLVFVDlETGRPVPLPDELRAALEALLAA 139
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
1-40 4.51e-04

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: 35.27  E-value: 4.51e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1084963442   1 MRTWIAELGRASVVFECDVLDRElgAKVVARGYSRHALVD 40
Cdd:cd00586    73 VETRVLRLGRKSFTFEQEIFRED--GELLATAETVLVCVD 110
 
Name Accession Description Interval E-value
FadM COG0824
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ...
1-62 1.19e-08

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: 47.59  E-value: 1.19e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1084963442   1 MRTWIAELGRASVVFECDVLDRELGaKVVARGYSRHALVD-DLWRIARMPDDLRGLMAPFVGR 62
Cdd:COG0824    78 VETRVVRLGGSSLTFEYEIFRADDG-ELLATGETVLVFVDlETGRPVPLPDELRAALEALLAA 139
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
1-40 4.51e-04

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: 35.27  E-value: 4.51e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1084963442   1 MRTWIAELGRASVVFECDVLDRElgAKVVARGYSRHALVD 40
Cdd:cd00586    73 VETRVLRLGRKSFTFEQEIFRED--GELLATAETVLVCVD 110
 
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