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Conserved domains on  [gi|398364771|ref|NP_009654|]
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uncharacterized protein YBR096W [Saccharomyces cerevisiae S288C]

Protein Classification

acyl-CoA thioesterase( domain architecture ID 10088366)

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
PubMed:  15307895
SCOP:  3000149

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
 73-175 3.26e-16

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: 71.87  E-value: 3.26e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364771  73 PFECDFYFHKSNSTYFAELDISRGNLMCKIFQKLMLNSKHYPYIPVANVFTNFLKEIKPFQKYSVSSRIICWDEKWIYVM 152
Cdd:cd00586    9 FGDTDAAGHVNNARYLRYFEEAREEFLRELGLGYDELEEQGLGLVVVELEIDYLRPLRLGDRLTVETRVLRLGRKSFTFE 88

                         90       100
                 ....*....|....*....|...
gi 398364771 153 SRFTIKKGTVLCSlSLTKYVLKD 175
Cdd:cd00586   89 QEIFREDGELLAT-AETVLVCVD 110
 
Name Accession Description Interval E-value
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
 73-175 3.26e-16

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: 71.87  E-value: 3.26e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364771  73 PFECDFYFHKSNSTYFAELDISRGNLMCKIFQKLMLNSKHYPYIPVANVFTNFLKEIKPFQKYSVSSRIICWDEKWIYVM 152
Cdd:cd00586    9 FGDTDAAGHVNNARYLRYFEEAREEFLRELGLGYDELEEQGLGLVVVELEIDYLRPLRLGDRLTVETRVLRLGRKSFTFE 88

                         90       100
                 ....*....|....*....|...
gi 398364771 153 SRFTIKKGTVLCSlSLTKYVLKD 175
Cdd:cd00586   89 QEIFREDGELLAT-AETVLVCVD 110
4HBT_2 pfam13279
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ...
 75-165 3.10e-10

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: 55.81  E-value: 3.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364771   75 ECDFYFHKSNSTYFAELDISRGNLMCK--IFQKLMLNSKHYPYIpvANVFTNFLKEIKPFQKYSVSSRIICWDEKWIYVM 152
Cdd:pfam13279   5 DIDANGHMNNARYLRYFEEARDRFLERlgLDLAYREALGIGLIL--AEAHVRYRRELKLGDELTVETRLIDWDAKRFHLE 82

                          90
                  ....*....|...
gi 398364771  153 SRFTIKKGTVLCS 165
Cdd:pfam13279  83 HRFLSPDGKLVAT 95
FadM COG0824
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ...
 73-182 2.18e-05

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: 42.96  E-value: 2.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364771  73 PFECDFYFHKSNSTYFAELDISRGNLM--CKIFQKLMLNSKHYPyiPVANVFTNFLKEIKPFQKYSVSSRIICWDEKWIY 150
Cdd:COG0824   14 FGDTDAMGHVNNANYLRYFEEARTEFLraLGLSYAELEEEGIGL--VVVEAEIDYLRPARYGDELTVETRVVRLGGSSLT 91

                         90       100       110
                 ....*....|....*....|....*....|..
gi 398364771 151 VMSRFTIKKGTVLCSLSLTKYVLKDgRKTIKP 182
Cdd:COG0824   92 FEYEIFRADDGELLATGETVLVFVD-LETGRP 122
 
Name Accession Description Interval E-value
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
 73-175 3.26e-16

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: 71.87  E-value: 3.26e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364771  73 PFECDFYFHKSNSTYFAELDISRGNLMCKIFQKLMLNSKHYPYIPVANVFTNFLKEIKPFQKYSVSSRIICWDEKWIYVM 152
Cdd:cd00586    9 FGDTDAAGHVNNARYLRYFEEAREEFLRELGLGYDELEEQGLGLVVVELEIDYLRPLRLGDRLTVETRVLRLGRKSFTFE 88

                         90       100
                 ....*....|....*....|...
gi 398364771 153 SRFTIKKGTVLCSlSLTKYVLKD 175
Cdd:cd00586   89 QEIFREDGELLAT-AETVLVCVD 110
4HBT_2 pfam13279
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ...
 75-165 3.10e-10

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: 55.81  E-value: 3.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364771   75 ECDFYFHKSNSTYFAELDISRGNLMCK--IFQKLMLNSKHYPYIpvANVFTNFLKEIKPFQKYSVSSRIICWDEKWIYVM 152
Cdd:pfam13279   5 DIDANGHMNNARYLRYFEEARDRFLERlgLDLAYREALGIGLIL--AEAHVRYRRELKLGDELTVETRLIDWDAKRFHLE 82

                          90
                  ....*....|...
gi 398364771  153 SRFTIKKGTVLCS 165
Cdd:pfam13279  83 HRFLSPDGKLVAT 95
FadM COG0824
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ...
 73-182 2.18e-05

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: 42.96  E-value: 2.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364771  73 PFECDFYFHKSNSTYFAELDISRGNLM--CKIFQKLMLNSKHYPyiPVANVFTNFLKEIKPFQKYSVSSRIICWDEKWIY 150
Cdd:COG0824   14 FGDTDAMGHVNNANYLRYFEEARTEFLraLGLSYAELEEEGIGL--VVVEAEIDYLRPARYGDELTVETRVVRLGGSSLT 91

                         90       100       110
                 ....*....|....*....|....*....|..
gi 398364771 151 VMSRFTIKKGTVLCSLSLTKYVLKDgRKTIKP 182
Cdd:COG0824   92 FEYEIFRADDGELLATGETVLVFVD-LETGRP 122
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 72-169 8.22e-03

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: 34.76  E-value: 8.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364771  72 SPFECDFYFHKSNSTYFAELDISRGNLMckifqklMLNSKHYPYIPVANVFTNFLKEIKPFQKYSVSSRIICWDEKWIYV 151
Cdd:cd03440    8 TPEDIDGGGIVHGGLLLALADEAAGAAA-------ARLGGRGLGAVTLSLDVRFLRPVRPGDTLTVEAEVVRVGRSSVTV 80

                         90
                 ....*....|....*...
gi 398364771 152 MSRFTIKKGTVLCSLSLT 169
Cdd:cd03440   81 EVEVRNEDGKLVATATAT 98
 
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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