InterPro domain: IPR042096

Two dehydratases, dihydroxy-acid dehydratase ( 4.2.1.9 ) (gene ilvD or ILV3) and 6-phosphogluconate dehydratase ( 4.2.1.12 ) (gene edd) have been shown to be evolutionary related [ 1 ]. Dihydroxy-acid dehydratase catalyses the fourth step in the biosynthesis of isoleucine and valine, the dehydratation of 2,3-dihydroxy-isovaleic acid into alpha-ketoisovaleric acid. 6-Phosphogluconate dehydratase catalyses the first step in the Entner-Doudoroff pathway, the dehydratation of 6-phospho-D-gluconate into 6-phospho-2-dehydro-3-deoxy-D-gluconate. Another protein containing this signature is Escherichia coli YjhG, which has been identified as a D-xylonate dehydratase [ 2 ].

This entry represents the C-terminal domain found in dihydroxy-acid dehydratase. It consists of 8 beta strands and 5 alpha helices.

1. Molecular characterization of the Entner-Doudoroff pathway in Escherichia coli: sequence analysis and localization of promoters for the edd-eda operon. J. Bacteriol. 174, 4638-46
2. Biosynthesis of ethylene glycol in Escherichia coli. Appl. Microbiol. Biotechnol. 97, 3409-17