H
IPR029069

HotDog domain superfamily

InterPro entry
Short nameHotDog_dom_sf
Overlapping entries
 

Description

The HotDog superfamily represents a domain found in thioesterases and thiol ester dehydratase-isomerases. This domain is also known as the 'hot dog' fold from the study of the structure of Escherichia coli beta-hydroxydecanoyl thiol ester dehydrase (FabA)
[1]
. It contains the seven-stranded antiparallel β-sheet 'bun', which wraps around a five-turn α-helical 'sausage'. Proteins containing this domain include numerous prokaryotic, archaeal and eukaryotic proteins involved in several related, but distinct, catalytic activities, from metabolic roles such as thioester hydrolysis in fatty acid metabolism, to degradation of phenylacetic acid and the environmental pollutant 4-chlorobenzoate. It also includes FapR, a non-catalytic bacterial homologue that is involved in transcriptional regulation of fatty acid biosynthesis
[2]
.

References

1.Structure of a dehydratase-isomerase from the bacterial pathway for biosynthesis of unsaturated fatty acids: two catalytic activities in one active site. Leesong M, Henderson BS, Gillig JR, Schwab JM, Smith JL. Structure 4, 253-64, (1996). View articlePMID: 8805534

2.The Hotdog fold: wrapping up a superfamily of thioesterases and dehydratases. Dillon SC, Bateman A. BMC Bioinformatics 5, 109, (2004). View articlePMID: 15307895

Cross References

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