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Conserved domains on  [gi|501423648|ref|WP_012448318|]
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hotdog fold domain-containing protein [Natranaerobius thermophilus]

Protein Classification

hotdog fold domain-containing protein( domain architecture ID 10130798)

hotdog fold domain-containing protein belonging to the hotdog fold superfamily of thioesterases and dehydratases, similar to beta-alanyl-CoA:ammonia lyase that catalyzes the deamination of beta-alanyl-CoA to reversibly form ammonia and acrylyl-CoA

CATH:  3.10.129.10
Gene Ontology:  GO:0016836
PubMed:  15307895

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 7-91 2.76e-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: 50.94  E-value: 2.76e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501423648   7 ATIRLRMNEKDVHyAGGIVNGSKMLDLFGDVATELLIRNDGDEGLFR-AYQEVEFLAPVKSGDFIEARGEITRVGNSSRE 85
Cdd:cd03440    1 FVLRLTVTPEDID-GGGIVHGGLLLALADEAAGAAAARLGGRGLGAVtLSLDVRFLRPVRPGDTLTVEAEVVRVGRSSVT 79


                 ....*.
gi 501423648  86 MKFEAY 91
Cdd:cd03440   80 VEVEVR 85
 
Name Accession Description Interval E-value
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 7-91 2.76e-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: 50.94  E-value: 2.76e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501423648   7 ATIRLRMNEKDVHyAGGIVNGSKMLDLFGDVATELLIRNDGDEGLFR-AYQEVEFLAPVKSGDFIEARGEITRVGNSSRE 85
Cdd:cd03440    1 FVLRLTVTPEDID-GGGIVHGGLLLALADEAAGAAAARLGGRGLGAVtLSLDVRFLRPVRPGDTLTVEAEVVRVGRSSVT 79


                 ....*.
gi 501423648  86 MKFEAY 91
Cdd:cd03440   80 VEVEVR 85
FadM COG0824
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ...
 2-92 4.19e-08

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: 48.74  E-value: 4.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501423648   2 EKPVEATIRLRMNEKDvhyAGGIVNGSKMLDLFGDVATELLIR--------NDGDEGLFRAYQEVEFLAPVKSGDFIEAR 73
Cdd:COG0824    3 LFTFETPIRVRFGDTD---AMGHVNNANYLRYFEEARTEFLRAlglsyaelEEEGIGLVVVEAEIDYLRPARYGDELTVE 79

                         90
                 ....*....|....*....
gi 501423648  74 GEITRVGNSSREMKFEAYK 92
Cdd:COG0824   80 TRVVRLGGSSLTFEYEIFR 98
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 22-92 7.79e-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: 43.78  E-value: 7.79e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501423648   22 GGIVNGSKMLDLFGDVATELLIRNDGDEGLFRAYQ-EVEFLAPVKSGDFIEARGEITRVGNSSREMKFEAYK 92
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSQQVVVVVElSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRD 72
 
Name Accession Description Interval E-value
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 7-91 2.76e-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: 50.94  E-value: 2.76e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501423648   7 ATIRLRMNEKDVHyAGGIVNGSKMLDLFGDVATELLIRNDGDEGLFR-AYQEVEFLAPVKSGDFIEARGEITRVGNSSRE 85
Cdd:cd03440    1 FVLRLTVTPEDID-GGGIVHGGLLLALADEAAGAAAARLGGRGLGAVtLSLDVRFLRPVRPGDTLTVEAEVVRVGRSSVT 79


                 ....*.
gi 501423648  86 MKFEAY 91
Cdd:cd03440   80 VEVEVR 85
FadM COG0824
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ...
 2-92 4.19e-08

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: 48.74  E-value: 4.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501423648   2 EKPVEATIRLRMNEKDvhyAGGIVNGSKMLDLFGDVATELLIR--------NDGDEGLFRAYQEVEFLAPVKSGDFIEAR 73
Cdd:COG0824    3 LFTFETPIRVRFGDTD---AMGHVNNANYLRYFEEARTEFLRAlglsyaelEEEGIGLVVVEAEIDYLRPARYGDELTVE 79

                         90
                 ....*....|....*....
gi 501423648  74 GEITRVGNSSREMKFEAYK 92
Cdd:COG0824   80 TRVVRLGGSSLTFEYEIFR 98
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
 21-92 6.09e-07

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: 44.90  E-value: 6.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501423648  21 AGGIVNGSKMLDLFGDVATELLIRNDGDEGLFRAYQ--------EVEFLAPVKSGDFIEARGEITRVGNSSREMKFEAYK 92
Cdd:cd00586   14 AAGHVNNARYLRYFEEAREEFLRELGLGYDELEEQGlglvvvelEIDYLRPLRLGDRLTVETRVLRLGRKSFTFEQEIFR 93
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 22-92 7.79e-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: 43.78  E-value: 7.79e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501423648   22 GGIVNGSKMLDLFGDVATELLIRNDGDEGLFRAYQ-EVEFLAPVKSGDFIEARGEITRVGNSSREMKFEAYK 92
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSQQVVVVVElSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRD 72
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 57-107 1.52e-05

Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes deacylate long-chain fatty acids by hydrolyzing acyl-CoA thioesters to free fatty acids and CoA-SH. Eukaryotic members of this family are expressed in brain, testis, and brown adipose tissues. The archeal and eukaryotic members of this family have two tandem copies of the conserved hot dog fold, while most bacterial members have only one copy.


Pssm-ID: 239526 [Multi-domain]  Cd Length: 123  Bit Score: 41.40  E-value: 1.52e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 501423648  57 EVEFLAPVKSGDFIEARGEITRVGNSSREMKFEAYKVIENAGIEEQTSACN 107
Cdd:cd03442   57 RIDFLKPVRVGDVVELSARVVYTGRTSMEVGVEVEAEDPLTGERRLVTSAY 107
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
57-91 3.92e-05

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 40.55  E-value: 3.92e-05
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 501423648  57 EVEFLAPVKSGDFIEARGEITRVGNSSREMKFEAY 91
Cdd:COG1607   56 SVDFLRPVRVGDIVELYARVVRVGRTSMEVGVEVW 90
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 6-126 8.57e-04

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 36.84  E-value: 8.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501423648   6 EATIRLRMNEKDVHYaGGIVNG---SKMLDLFGDVATELLIrnDGDEGLFRAYQEVEFLAPVKSGDFIEARGEITRVGNS 82
Cdd:COG2050   32 RAVLRLPVRPEHLNP-PGTVHGgalAALADSAAGLAANSAL--PPGRRAVTIELNINFLRPARLGDRLTAEARVVRRGRR 108

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 501423648  83 SREMKFEAYKvienagieeqtsacnvlEEPVLVCKAKGTCVVPK 126
Cdd:COG2050  109 LAVVEVEVTD-----------------EDGKLVATATGTFAVLP 135
 
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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