Conserved Protein Domain Family
hot_dog

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cl00509: hot_dog Superfamily (this model, PSSM-Id:412416 is obsolete and has been replaced by 469797)
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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.
Links
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Taxonomy: root
PubMed: 79 links
Protein: Related Protein
Related Structure
Statistics
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Accession: cl00509
PSSM Id: 412416
Name: hot_dog
Created: 8-Feb-2008
Updated: 24-Nov-2020
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