IPR029069
HotDog domain superfamily
InterPro entry
Short name | HotDog_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
Contributing Member Database Entry
- SUPERFAMILY:SSF54637
Representative structure
8ayv: Crystal structure of the Malonyl-ACP Decarboxylase MadB from Pseudomonas putida