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Conserved domains on  [gi|1827488696|dbj|GFI33140|]
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fluoroacetyl-CoA thioesterase [Lachnospiraceae bacterium]

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];
1-129 4.50e-51

Predicted thioesterase [General function prediction only];


:

Pssm-ID: 444247  Cd Length: 129  Bit Score: 158.04  E-value: 4.50e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827488696   1 MLETGIKGYQEFTVTEADTAKAHKSGTLNVLATPRMAALMEETAWKSVAESLEPGMGTVGIQLNLEHLAPTPVGMKVWCE 80
Cdd:COG5496     1 ELKPGLTATFEFTVTEEDTAAALGSGDVPVLATPAMIALMEWAAREALDPHLPEGETTVGTEVDVKHLAPTPVGMTVTVT 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1827488696  81 TVLTKIDGRKLTFSITAFDETGKIGAAVHDRFMIEETKFQSKADKKKQK 129
Cdd:COG5496    81 AELTEVDGRRLTFEVEAFDEAGLIGEGTHERFIVNKEKFMAKAAEKAAK 129
 
Name Accession Description Interval E-value
COG5496 COG5496
Predicted thioesterase [General function prediction only];
1-129 4.50e-51

Predicted thioesterase [General function prediction only];


Pssm-ID: 444247  Cd Length: 129  Bit Score: 158.04  E-value: 4.50e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827488696   1 MLETGIKGYQEFTVTEADTAKAHKSGTLNVLATPRMAALMEETAWKSVAESLEPGMGTVGIQLNLEHLAPTPVGMKVWCE 80
Cdd:COG5496     1 ELKPGLTATFEFTVTEEDTAAALGSGDVPVLATPAMIALMEWAAREALDPHLPEGETTVGTEVDVKHLAPTPVGMTVTVT 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1827488696  81 TVLTKIDGRKLTFSITAFDETGKIGAAVHDRFMIEETKFQSKADKKKQK 129
Cdd:COG5496    81 AELTEVDGRRLTFEVEAFDEAGLIGEGTHERFIVNKEKFMAKAAEKAAK 129
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 11-104 1.19e-07

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: 46.31  E-value: 1.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827488696  11 EFTVTEADTAKAhksGTLNVLATprmAALMEETAWKSVAESLEPGMGTVGIQLNLEHLAPTPVGMKVWCETVLTKIDGRK 90
Cdd:cd03440     4 RLTVTPEDIDGG---GIVHGGLL---LALADEAAGAAAARLGGRGLGAVTLSLDVRFLRPVRPGDTLTVEAEVVRVGRSS 77

                          90
                  ....*....|....
gi 1827488696  91 LTFSITAFDETGKI 104
Cdd:cd03440    78 VTVEVEVRNEDGKL 91
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 28-106 2.97e-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: 44.94  E-value: 2.97e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1827488696  28 LNVLATPRMAALMEETAWKSVAESLEPGMGTVGIQLNLEHLAPTPVGMKVWCETVLTKIDGRKLTFSITAFDETGKIGA 106
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSQQVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDEDGRLVA 79
 
Name Accession Description Interval E-value
COG5496 COG5496
Predicted thioesterase [General function prediction only];
1-129 4.50e-51

Predicted thioesterase [General function prediction only];


Pssm-ID: 444247  Cd Length: 129  Bit Score: 158.04  E-value: 4.50e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827488696   1 MLETGIKGYQEFTVTEADTAKAHKSGTLNVLATPRMAALMEETAWKSVAESLEPGMGTVGIQLNLEHLAPTPVGMKVWCE 80
Cdd:COG5496     1 ELKPGLTATFEFTVTEEDTAAALGSGDVPVLATPAMIALMEWAAREALDPHLPEGETTVGTEVDVKHLAPTPVGMTVTVT 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1827488696  81 TVLTKIDGRKLTFSITAFDETGKIGAAVHDRFMIEETKFQSKADKKKQK 129
Cdd:COG5496    81 AELTEVDGRRLTFEVEAFDEAGLIGEGTHERFIVNKEKFMAKAAEKAAK 129
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 36-114 6.39e-09

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 50.71  E-value: 6.39e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1827488696  36 MAALMEETAWKSVAESLEPGMGTVGIQLNLEHLAPTPVGMKVWCETVLTKIDGRKLTFSITAFDETGKIGAAVHDRFMI 114
Cdd:COG2050    55 LAALADSAAGLAANSALPPGRRAVTIELNINFLRPARLGDRLTAEARVVRRGRRLAVVEVEVTDEDGKLVATATGTFAV 133
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 11-104 1.19e-07

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: 46.31  E-value: 1.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827488696  11 EFTVTEADTAKAhksGTLNVLATprmAALMEETAWKSVAESLEPGMGTVGIQLNLEHLAPTPVGMKVWCETVLTKIDGRK 90
Cdd:cd03440     4 RLTVTPEDIDGG---GIVHGGLL---LALADEAAGAAAARLGGRGLGAVTLSLDVRFLRPVRPGDTLTVEAEVVRVGRSS 77

                          90
                  ....*....|....
gi 1827488696  91 LTFSITAFDETGKI 104
Cdd:cd03440    78 VTVEVEVRNEDGKL 91
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 28-106 2.97e-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: 44.94  E-value: 2.97e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1827488696  28 LNVLATPRMAALMEETAWKSVAESLEPGMGTVGIQLNLEHLAPTPVGMKVWCETVLTKIDGRKLTFSITAFDETGKIGA 106
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSQQVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDEDGRLVA 79
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 36-114 2.41e-06

PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several proteins responsible for phenylacetic acid (PA) degradation in bacteria. Although orthologs of PaaI exist in archaea and eukaryotes, their function has not been determined. Sequence similarity between PaaI, E. coli medium chain acyl-CoA thioesterase II, and human thioesterase III suggests they all belong to the same thioesterase superfamily. The conserved fold present in these thioesterases is referred to as an asymmetric hot dog fold, similar to those of 4-hydroxybenzoyl-CoA thioesterase (4HBT) and the beta-hydroxydecanoyl-ACP dehydratases (FabA/FabZ).


Pssm-ID: 239527 [Multi-domain]  Cd Length: 113  Bit Score: 43.32  E-value: 2.41e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1827488696  36 MAALMEETAWKSVAESLEPGMGTVGIQLNLEHLAPTPVGmKVWCETVLTKIDGRKLTFSITAFDETGKIGAAVHDRFMI 114
Cdd:cd03443    36 IATLADTAGGLAALSALPPGALAVTVDLNVNYLRPARGG-DLTARARVVKLGRRLAVVEVEVTDEDGKLVATARGTFAV 113
PS-DH pfam14765
Polyketide synthase dehydratase; This is the dehydratase domain of polyketide synthases. ...
 69-110 2.12e-03

Polyketide synthase dehydratase; This is the dehydratase domain of polyketide synthases. Structural analysis shows these DH domains are double hotdogs in which the active site contains a histidine from the N-terminal hotdog and an aspartate from the C-terminal hotdog. Studies have uncovered that a substrate tunnel formed between the DH domains may be essential for loading substrates and unloading products.


Pssm-ID: 434191  Cd Length: 296  Bit Score: 36.58  E-value: 2.12e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1827488696  69 APTPVGMKVWCETVLTKIDGRKLTFSITAFDETGKIGAAVHD 110
Cdd:pfam14765 242 RSLPPGEPLWVHARLERRGGRTIVGDLTLVDEDGRVVARIEG 283
 
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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