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Conserved domains on  [gi|18408985|ref|NP_564926|]
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Thioesterase superfamily protein [Arabidopsis thaliana]

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 ...
 50-186 1.28e-35

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: 121.54  E-value: 1.28e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408985  50 MSEF-HEVELKVRDYELDQFGVVNNAVYANYCQHGRHEFLESIGINCDEVARSGEALAISELTMKFLSPLRSGDKFVVKA 128
Cdd:COG0824   1 MTLFtFETPIRVRFGDTDAMGHVNNANYLRYFEEARTEFLRALGLSYAELEEEGIGLVVVEAEIDYLRPARYGDELTVET 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 18408985 129 RISGTSAARIYFDHFIFKLPNQEPILEAKGIAVWLD-NKYRPVRIPSSIRSKFVHFLRQ 186
Cdd:COG0824  81 RVVRLGGSSLTFEYEIFRADDGELLATGETVLVFVDlETGRPVPLPDELRAALEALLAA 139
 
Name Accession Description Interval E-value
FadM COG0824
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ...
 50-186 1.28e-35

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: 121.54  E-value: 1.28e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408985  50 MSEF-HEVELKVRDYELDQFGVVNNAVYANYCQHGRHEFLESIGINCDEVARSGEALAISELTMKFLSPLRSGDKFVVKA 128
Cdd:COG0824   1 MTLFtFETPIRVRFGDTDAMGHVNNANYLRYFEEARTEFLRALGLSYAELEEEGIGLVVVEAEIDYLRPARYGDELTVET 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 18408985 129 RISGTSAARIYFDHFIFKLPNQEPILEAKGIAVWLD-NKYRPVRIPSSIRSKFVHFLRQ 186
Cdd:COG0824  81 RVVRLGGSSLTFEYEIFRADDGELLATGETVLVFVDlETGRPVPLPDELRAALEALLAA 139
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
 54-164 1.38e-29

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: 105.38  E-value: 1.38e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408985  54 HEVELKVRDYELDQFGVVNNAVYANYCQHGRHEFLESIGINCDEVARSGEALAISELTMKFLSPLRSGDKFVVKARISGT 133
Cdd:cd00586   1 FTLEIRVRFGDTDAAGHVNNARYLRYFEEAREEFLRELGLGYDELEEQGLGLVVVELEIDYLRPLRLGDRLTVETRVLRL 80

                        90       100       110
                ....*....|....*....|....*....|.
gi 18408985 134 SAARIYFDHFIFKlPNQEPILEAKGIAVWLD 164
Cdd:cd00586  81 GRKSFTFEQEIFR-EDGELLATAETVLVCVD 110
4HBT_2 pfam13279
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ...
 60-180 9.80e-19

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: 77.77  E-value: 9.80e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408985    60 VRDYELDQFGVVNNAVYANYCQHGRHEFLESIGINCDEVARSGEALAISELTMKFLSPLRSGDKFVVKARISGTSAARIY 139
Cdd:pfam13279   1 VRPGDIDANGHMNNARYLRYFEEARDRFLERLGLDLAYREALGIGLILAEAHVRYRRELKLGDELTVETRLIDWDAKRFH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 18408985   140 FDHFIFKlPNQEPILEAKGIAVWLD-NKYRPVRIPSSIRSKF 180
Cdd:pfam13279  81 LEHRFLS-PDGKLVATAETRLVFVDyETRKPAPIPEELLEAL 121
TIGR00051 TIGR00051
acyl-CoA thioester hydrolase, YbgC/YbaW family; This model describes a subset of related ...
 58-173 4.76e-11

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: 57.43  E-value: 4.76e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408985    58 LKVRDYELDQFGVVNNAVYANYCQHGRHEFLESIGINCDEVARSGEALAISELTMKFLSPLRSGDKFVVKARISGTSAAR 137
Cdd:TIGR00051   2 VRVYYEDTDAQGIVYHANYLRYCERARTEFLRSLGFPQSVLRAEGVAFVVVNINIEYKKPARLDDVLEIRTQIEELNGFS 81

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 18408985   138 IYFDHFIFKLPNqEPILEAKGIAVWLD-NKYRPVRIP 173
Cdd:TIGR00051  82 FVFSQEIFNEDE-ALLKAATVIVVCVDpKKQKPVAIP 117
 
Name Accession Description Interval E-value
FadM COG0824
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ...
 50-186 1.28e-35

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: 121.54  E-value: 1.28e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408985  50 MSEF-HEVELKVRDYELDQFGVVNNAVYANYCQHGRHEFLESIGINCDEVARSGEALAISELTMKFLSPLRSGDKFVVKA 128
Cdd:COG0824   1 MTLFtFETPIRVRFGDTDAMGHVNNANYLRYFEEARTEFLRALGLSYAELEEEGIGLVVVEAEIDYLRPARYGDELTVET 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 18408985 129 RISGTSAARIYFDHFIFKLPNQEPILEAKGIAVWLD-NKYRPVRIPSSIRSKFVHFLRQ 186
Cdd:COG0824  81 RVVRLGGSSLTFEYEIFRADDGELLATGETVLVFVDlETGRPVPLPDELRAALEALLAA 139
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
 54-164 1.38e-29

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: 105.38  E-value: 1.38e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408985  54 HEVELKVRDYELDQFGVVNNAVYANYCQHGRHEFLESIGINCDEVARSGEALAISELTMKFLSPLRSGDKFVVKARISGT 133
Cdd:cd00586   1 FTLEIRVRFGDTDAAGHVNNARYLRYFEEAREEFLRELGLGYDELEEQGLGLVVVELEIDYLRPLRLGDRLTVETRVLRL 80

                        90       100       110
                ....*....|....*....|....*....|.
gi 18408985 134 SAARIYFDHFIFKlPNQEPILEAKGIAVWLD 164
Cdd:cd00586  81 GRKSFTFEQEIFR-EDGELLATAETVLVCVD 110
4HBT_2 pfam13279
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ...
 60-180 9.80e-19

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: 77.77  E-value: 9.80e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408985    60 VRDYELDQFGVVNNAVYANYCQHGRHEFLESIGINCDEVARSGEALAISELTMKFLSPLRSGDKFVVKARISGTSAARIY 139
Cdd:pfam13279   1 VRPGDIDANGHMNNARYLRYFEEARDRFLERLGLDLAYREALGIGLILAEAHVRYRRELKLGDELTVETRLIDWDAKRFH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 18408985   140 FDHFIFKlPNQEPILEAKGIAVWLD-NKYRPVRIPSSIRSKF 180
Cdd:pfam13279  81 LEHRFLS-PDGKLVATAETRLVFVDyETRKPAPIPEELLEAL 121
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 68-153 7.45e-12

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: 58.42  E-value: 7.45e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408985    68 FGVVNNAVYANYCQHGRHEFLESIGincdevaRSGEALAISELTMKFLSPLRSGDKFVVKARISGTSAARIYFDHFIFKL 147
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLG-------GSQQVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDE 73


                  ....*.
gi 18408985   148 PNQEPI 153
Cdd:pfam03061  74 DGRLVA 79
TIGR00051 TIGR00051
acyl-CoA thioester hydrolase, YbgC/YbaW family; This model describes a subset of related ...
 58-173 4.76e-11

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: 57.43  E-value: 4.76e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408985    58 LKVRDYELDQFGVVNNAVYANYCQHGRHEFLESIGINCDEVARSGEALAISELTMKFLSPLRSGDKFVVKARISGTSAAR 137
Cdd:TIGR00051   2 VRVYYEDTDAQGIVYHANYLRYCERARTEFLRSLGFPQSVLRAEGVAFVVVNINIEYKKPARLDDVLEIRTQIEELNGFS 81

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 18408985   138 IYFDHFIFKLPNqEPILEAKGIAVWLD-NKYRPVRIP 173
Cdd:TIGR00051  82 FVFSQEIFNEDE-ALLKAATVIVVCVDpKKQKPVAIP 117
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 54-161 1.76e-10

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: 55.56  E-value: 1.76e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408985  54 HEVELKVRDYELDQFGVVNNAVYANYCQHGRHEFLESIGIncdevarSGEALAISELTMKFLSPLRSGDKFVVKARISGT 133
Cdd:cd03440   1 FVLRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLGG-------RGLGAVTLSLDVRFLRPVRPGDTLTVEAEVVRV 73

                        90       100
                ....*....|....*....|....*...
gi 18408985 134 SAARIYFDHFIFKlPNQEPILEAKGIAV 161
Cdd:cd03440  74 GRSSVTVEVEVRN-EDGKLVATATATFV 100
FatA COG3884
Acyl-ACP thioesterase [Lipid transport and metabolism];
54-180 5.33e-06

Acyl-ACP thioesterase [Lipid transport and metabolism];


Pssm-ID: 443092 [Multi-domain]  Cd Length: 242  Bit Score: 45.33  E-value: 5.33e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408985  54 HEVELKVRDYELDQFGVVNNAVYANYCQH--GRHefLESIGINCDEVARSGEALAISELTMKFLSPLRSGDKFVVKARIS 131
Cdd:COG3884   1 YEKEYRVRYYEVDFNGRLRLPALLNYLQDaaTEH--AEALGFGIDDLEEKGLAWVLSRYQIEIDRYPRWGEKITVETWPS 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 18408985 132 GTSAARIYFDhFIFKLPNQEPILEAKGIAVWLD-NKYRPVRIPSSIRSKF 180
Cdd:COG3884  79 GYNRFFAYRD-FRILDEDGELLARATSIWVLIDlETRRPVRIPDEILEPY 127
 
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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