InterPro domain: IPR029069

This superfamily represents a domain found in thioesterases and thiol ester dehydratase-isomerases. This domain is also knonwn 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 beta-sheet 'bun', which wraps around a five-turn alpha-helical 'sausage'. Proteins containing this domain includes 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 ].

1. Structure of a dehydratase-isomerase from the bacterial pathway for biosynthesis of unsaturated fatty acids: two catalytic activities in one active site. Structure 4, 253-64
2. The Hotdog fold: wrapping up a superfamily of thioesterases and dehydratases. BMC Bioinformatics 5, 109