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Conserved domains on  [gi|1032718762|ref|WP_064293249|]
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MULTISPECIES: thioesterase family protein [Aerococcus]

Protein Classification

thioesterase family protein( domain architecture ID 10009353)

thioesterase family protein such as Streptomyces cattleya fluoroacetyl-CoA thioesterase that catalyzes the hydrolysis of fluoroacetyl-coenzyme A, preventing it from metabolizing to 4-hydroxy-trans-aconitate, a lethal inhibitor of the tricarboxylic acid cycle

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG5496 COG5496
Predicted thioesterase [General function prediction only];
5-117 1.43e-37

Predicted thioesterase [General function prediction only];


:

Pssm-ID: 444247  Cd Length: 129  Bit Score: 123.37  E-value: 1.43e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718762   5 FTVLPHQLANQVGSGSLEVLSSPWLLGYFENAAVRFLKDYLAEDETTVGTNAQLEHLAPSLLNEEIRIHCELVDHDDRHY 84
Cdd:COG5496    12 FTVTEEDTAAALGSGDVPVLATPAMIALMEWAAREALDPHLPEGETTVGTEVDVKHLAPTPVGMTVTVTAELTEVDGRRL 91

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1032718762  85 HFQMQAYCQDQLIGRLDHRRVKVNKESFMKKTQ 117
Cdd:COG5496    92 TFEVEAFDEAGLIGEGTHERFIVNKEKFMAKAA 124
 
Name Accession Description Interval E-value
COG5496 COG5496
Predicted thioesterase [General function prediction only];
5-117 1.43e-37

Predicted thioesterase [General function prediction only];


Pssm-ID: 444247  Cd Length: 129  Bit Score: 123.37  E-value: 1.43e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718762   5 FTVLPHQLANQVGSGSLEVLSSPWLLGYFENAAVRFLKDYLAEDETTVGTNAQLEHLAPSLLNEEIRIHCELVDHDDRHY 84
Cdd:COG5496    12 FTVTEEDTAAALGSGDVPVLATPAMIALMEWAAREALDPHLPEGETTVGTEVDVKHLAPTPVGMTVTVTAELTEVDGRRL 91

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1032718762  85 HFQMQAYCQDQLIGRLDHRRVKVNKESFMKKTQ 117
Cdd:COG5496    92 TFEVEAFDEAGLIGEGTHERFIVNKEKFMAKAA 124
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
 29-95 1.38e-03

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: 35.66  E-value: 1.38e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1032718762  29 LLGYFENAAVRFLK----DYLAEDETTVG---TNAQLEHLAPSLLNEEIRIHCELVDHDDRHYHFQMQAYCQDQ 95
Cdd:cd00586    23 YLRYFEEAREEFLRelglGYDELEEQGLGlvvVELEIDYLRPLRLGDRLTVETRVLRLGRKSFTFEQEIFREDG 96
4HBT_2 pfam13279
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ...
 29-95 1.47e-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: 35.78  E-value: 1.47e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1032718762  29 LLGYFENAAVRFLK------DYLAEDETTVGT-NAQLEHLAPSLLNEEIRIHCELVDHDDRHYHFQMQAYCQDQ 95
Cdd:pfam13279  17 YLRYFEEARDRFLErlgldlAYREALGIGLILaEAHVRYRRELKLGDELTVETRLIDWDAKRFHLEHRFLSPDG 90
 
Name Accession Description Interval E-value
COG5496 COG5496
Predicted thioesterase [General function prediction only];
5-117 1.43e-37

Predicted thioesterase [General function prediction only];


Pssm-ID: 444247  Cd Length: 129  Bit Score: 123.37  E-value: 1.43e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718762   5 FTVLPHQLANQVGSGSLEVLSSPWLLGYFENAAVRFLKDYLAEDETTVGTNAQLEHLAPSLLNEEIRIHCELVDHDDRHY 84
Cdd:COG5496    12 FTVTEEDTAAALGSGDVPVLATPAMIALMEWAAREALDPHLPEGETTVGTEVDVKHLAPTPVGMTVTVTAELTEVDGRRL 91

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1032718762  85 HFQMQAYCQDQLIGRLDHRRVKVNKESFMKKTQ 117
Cdd:COG5496    92 TFEVEAFDEAGLIGEGTHERFIVNKEKFMAKAA 124
FadM COG0824
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ...
 30-112 4.86e-04

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: 37.18  E-value: 4.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032718762  30 LGYFENAAVRFLK----DYLAEDETTVGT---NAQLEHLAPSLLNEEIRIHCELVDHDDRHYHFQMQAYCQD--QLIGRL 100
Cdd:COG0824    29 LRYFEEARTEFLRalglSYAELEEEGIGLvvvEAEIDYLRPARYGDELTVETRVVRLGGSSLTFEYEIFRADdgELLATG 108

                          90
                  ....*....|..
gi 1032718762 101 DHRRVKVNKESF 112
Cdd:COG0824   109 ETVLVFVDLETG 120
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
 29-95 1.38e-03

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: 35.66  E-value: 1.38e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1032718762  29 LLGYFENAAVRFLK----DYLAEDETTVG---TNAQLEHLAPSLLNEEIRIHCELVDHDDRHYHFQMQAYCQDQ 95
Cdd:cd00586    23 YLRYFEEAREEFLRelglGYDELEEQGLGlvvVELEIDYLRPLRLGDRLTVETRVLRLGRKSFTFEQEIFREDG 96
4HBT_2 pfam13279
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ...
 29-95 1.47e-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: 35.78  E-value: 1.47e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1032718762  29 LLGYFENAAVRFLK------DYLAEDETTVGT-NAQLEHLAPSLLNEEIRIHCELVDHDDRHYHFQMQAYCQDQ 95
Cdd:pfam13279  17 YLRYFEEARDRFLErlgldlAYREALGIGLILaEAHVRYRRELKLGDELTVETRLIDWDAKRFHLEHRFLSPDG 90
 
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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