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Conserved domains on  [gi|1524589160|gb|RQO30802|]
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thioesterase [Taibaiella sp. KBW10]

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 ...
 1-136 2.03e-32

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: 111.53  E-value: 2.03e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524589160   1 MFVHETKIRVRYGETDQMGYLYYGYYALYYEQGRGDAMRSLGFTYKELEEQGTIMPVASMHCEYLRPAHYDDLITVKTIL 80
Cdd:COG0824     3 LFTFETPIRVRFGDTDAMGHVNNANYLRYFEEARTEFLRALGLSYAELEEEGIGLVVVEAEIDYLRPARYGDELTVETRV 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1524589160  81 KELpDGHFTTFHSELYNEA-GKLINRGSVTLAFFDPLAKRKTKLPEVLRNVLAPYFK 136
Cdd:COG0824    83 VRL-GGSSLTFEYEIFRADdGELLATGETVLVFVDLETGRPVPLPDELRAALEALLA 138
 
Name Accession Description Interval E-value
FadM COG0824
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ...
 1-136 2.03e-32

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: 111.53  E-value: 2.03e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524589160   1 MFVHETKIRVRYGETDQMGYLYYGYYALYYEQGRGDAMRSLGFTYKELEEQGTIMPVASMHCEYLRPAHYDDLITVKTIL 80
Cdd:COG0824     3 LFTFETPIRVRFGDTDAMGHVNNANYLRYFEEARTEFLRALGLSYAELEEEGIGLVVVEAEIDYLRPARYGDELTVETRV 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1524589160  81 KELpDGHFTTFHSELYNEA-GKLINRGSVTLAFFDPLAKRKTKLPEVLRNVLAPYFK 136
Cdd:COG0824    83 VRL-GGSSLTFEYEIFRADdGELLATGETVLVFVDLETGRPVPLPDELRAALEALLA 138
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
 4-114 4.00e-26

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: 94.60  E-value: 4.00e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524589160   4 HETKIRVRYGETDQMGYLYYGYYALYYEQGRGDAMRSLGFTYKELEEQGTIMPVASMHCEYLRPAHYDDLITVKTILKEL 83
Cdd:cd00586     1 FTLEIRVRFGDTDAAGHVNNARYLRYFEEAREEFLRELGLGYDELEEQGLGLVVVELEIDYLRPLRLGDRLTVETRVLRL 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1524589160  84 pDGHFTTFHSELYNEAGKLINRGSVTLAFFD 114
Cdd:cd00586    81 -GRKSFTFEQEIFREDGELLATAETVLVCVD 110
TIGR00051 TIGR00051
acyl-CoA thioester hydrolase, YbgC/YbaW family; This model describes a subset of related ...
 7-124 3.38e-18

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: 74.38  E-value: 3.38e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524589160   7 KIRVRYGETDQMGYLYYGYYALYYEQGRGDAMRSLGFTYKELEEQGTIMPVASMHCEYLRPAHYDDLITVKTILKELpDG 86
Cdd:TIGR00051   1 PVRVYYEDTDAQGIVYHANYLRYCERARTEFLRSLGFPQSVLRAEGVAFVVVNINIEYKKPARLDDVLEIRTQIEEL-NG 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1524589160  87 HFTTFHSELYNEAGKLINRGSVTLAFFDPLAKRKTKLP 124
Cdd:TIGR00051  80 FSFVFSQEIFNEDEALLKAATVIVVCVDPKKQKPVAIP 117
4HBT_2 pfam13279
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ...
 31-131 3.17e-11

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: 56.58  E-value: 3.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524589160  31 EQGRGDAMRSLGFTYKELEEQGTIMPVASMHCEYLRPAHYDDLITVKTILKELPDGHFTTFHsELYNEAGKLINRGSVTL 110
Cdd:pfam13279  22 EEARDRFLERLGLDLAYREALGIGLILAEAHVRYRRELKLGDELTVETRLIDWDAKRFHLEH-RFLSPDGKLVATAETRL 100

                          90       100
                  ....*....|....*....|.
gi 1524589160 111 AFFDPLAKRKTKLPEVLRNVL 131
Cdd:pfam13279 101 VFVDYETRKPAPIPEELLEAL 121
PRK10800 PRK10800
acyl-CoA thioesterase YbgC; Provisional
 8-124 9.12e-08

acyl-CoA thioesterase YbgC; Provisional


Pssm-ID: 182742  Cd Length: 130  Bit Score: 47.82  E-value: 9.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524589160   8 IRVRYGETDQMGYLYYGYYALYYEQGRGDAMRSLGFTYKELEEQGTIMPVASMHCEYLRPAHYDDLITVKTILKELpDGH 87
Cdd:PRK10800    7 VRVYYEDTDAGGVVYHASYVAFYERARTEMLRHHHFSQQALLAERVAFVVRKMTVEYYAPARLDDMLEVQSEITSM-RGT 85

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1524589160  88 FTTFHSELYNEAGKLINRGSVTLAFFDPLAKRKTKLP 124
Cdd:PRK10800   86 SLTFTQRIVNAEGTLLNEAEVLIVCVDPLKMKPRALP 122
 
Name Accession Description Interval E-value
FadM COG0824
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ...
 1-136 2.03e-32

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: 111.53  E-value: 2.03e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524589160   1 MFVHETKIRVRYGETDQMGYLYYGYYALYYEQGRGDAMRSLGFTYKELEEQGTIMPVASMHCEYLRPAHYDDLITVKTIL 80
Cdd:COG0824     3 LFTFETPIRVRFGDTDAMGHVNNANYLRYFEEARTEFLRALGLSYAELEEEGIGLVVVEAEIDYLRPARYGDELTVETRV 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1524589160  81 KELpDGHFTTFHSELYNEA-GKLINRGSVTLAFFDPLAKRKTKLPEVLRNVLAPYFK 136
Cdd:COG0824    83 VRL-GGSSLTFEYEIFRADdGELLATGETVLVFVDLETGRPVPLPDELRAALEALLA 138
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
 4-114 4.00e-26

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: 94.60  E-value: 4.00e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524589160   4 HETKIRVRYGETDQMGYLYYGYYALYYEQGRGDAMRSLGFTYKELEEQGTIMPVASMHCEYLRPAHYDDLITVKTILKEL 83
Cdd:cd00586     1 FTLEIRVRFGDTDAAGHVNNARYLRYFEEAREEFLRELGLGYDELEEQGLGLVVVELEIDYLRPLRLGDRLTVETRVLRL 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1524589160  84 pDGHFTTFHSELYNEAGKLINRGSVTLAFFD 114
Cdd:cd00586    81 -GRKSFTFEQEIFREDGELLATAETVLVCVD 110
TIGR00051 TIGR00051
acyl-CoA thioester hydrolase, YbgC/YbaW family; This model describes a subset of related ...
 7-124 3.38e-18

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: 74.38  E-value: 3.38e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524589160   7 KIRVRYGETDQMGYLYYGYYALYYEQGRGDAMRSLGFTYKELEEQGTIMPVASMHCEYLRPAHYDDLITVKTILKELpDG 86
Cdd:TIGR00051   1 PVRVYYEDTDAQGIVYHANYLRYCERARTEFLRSLGFPQSVLRAEGVAFVVVNINIEYKKPARLDDVLEIRTQIEEL-NG 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1524589160  87 HFTTFHSELYNEAGKLINRGSVTLAFFDPLAKRKTKLP 124
Cdd:TIGR00051  80 FSFVFSQEIFNEDEALLKAATVIVVCVDPKKQKPVAIP 117
4HBT_2 pfam13279
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ...
 31-131 3.17e-11

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: 56.58  E-value: 3.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524589160  31 EQGRGDAMRSLGFTYKELEEQGTIMPVASMHCEYLRPAHYDDLITVKTILKELPDGHFTTFHsELYNEAGKLINRGSVTL 110
Cdd:pfam13279  22 EEARDRFLERLGLDLAYREALGIGLILAEAHVRYRRELKLGDELTVETRLIDWDAKRFHLEH-RFLSPDGKLVATAETRL 100

                          90       100
                  ....*....|....*....|.
gi 1524589160 111 AFFDPLAKRKTKLPEVLRNVL 131
Cdd:pfam13279 101 VFVDYETRKPAPIPEELLEAL 121
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 4-111 6.99e-09

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: 49.78  E-value: 6.99e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524589160   4 HETKIRVRYGETDQMGYLYYGYYALYYEQGRGDAMRSLGFtykeleeQGTIMPVASMHCEYLRPAHYDDLITVKTILKEL 83
Cdd:cd03440     1 FVLRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLGG-------RGLGAVTLSLDVRFLRPVRPGDTLTVEAEVVRV 73

                          90       100
                  ....*....|....*....|....*...
gi 1524589160  84 pDGHFTTFHSELYNEAGKLINRGSVTLA 111
Cdd:cd03440    74 -GRSSVTVEVEVRNEDGKLVATATATFV 100
PRK10800 PRK10800
acyl-CoA thioesterase YbgC; Provisional
 8-124 9.12e-08

acyl-CoA thioesterase YbgC; Provisional


Pssm-ID: 182742  Cd Length: 130  Bit Score: 47.82  E-value: 9.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524589160   8 IRVRYGETDQMGYLYYGYYALYYEQGRGDAMRSLGFTYKELEEQGTIMPVASMHCEYLRPAHYDDLITVKTILKELpDGH 87
Cdd:PRK10800    7 VRVYYEDTDAGGVVYHASYVAFYERARTEMLRHHHFSQQALLAERVAFVVRKMTVEYYAPARLDDMLEVQSEITSM-RGT 85

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1524589160  88 FTTFHSELYNEAGKLINRGSVTLAFFDPLAKRKTKLP 124
Cdd:PRK10800   86 SLTFTQRIVNAEGTLLNEAEVLIVCVDPLKMKPRALP 122
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 31-103 4.66e-07

Thioesterase superfamily; This family contains a wide variety of enzymes, principally thioesterases. This family includes 4HBT (EC 3.1.2.23) which catalyzes the final step in the biosynthesis of 4-hydroxybenzoate from 4-chlorobenzoate in the soil dwelling microbe Pseudomonas CBS-3. This family includes various cytosolic long-chain acyl-CoA thioester hydrolases. Long-chain acyl-CoA hydrolases hydrolyse palmitoyl-CoA to CoA and palmitate, they also catalyze the hydrolysis of other long chain fatty acyl-CoA thioesters.


Pssm-ID: 427116 [Multi-domain]  Cd Length: 79  Bit Score: 44.55  E-value: 4.66e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1524589160  31 EQGRGDAMRSLGFTYKeleeqgtIMPVASMHCEYLRPAHYDDLITVKTILKELpDGHFTTFHSELYNEAGKLI 103
Cdd:pfam03061  14 DEAAGAAARRLGGSQQ-------VVVVVELSIDFLRPARLGDRLTVEARVVRL-GRTSAVVEVEVRDEDGRLV 78
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 50-115 5.75e-03

Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 34.92  E-value: 5.75e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1524589160  50 EQGTIMPVASMHCEYLRPAHYDDLITVK-TILKElpDGHFTTFHSELYNEAGKLINRGSVTLAFFDP 115
Cdd:COG2050    72 PPGRRAVTIELNINFLRPARLGDRLTAEaRVVRR--GRRLAVVEVEVTDEDGKLVATATGTFAVLPK 136
 
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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