Homologous Superfamily

IlvD/EDD, N-terminal domain (IPR037237)

Short name: IlvD/EDD_N

Overlapping entries


Two dehydratases, dihydroxy-acid dehydratase (EC: (gene ilvD or ILV3) and 6-phosphogluconate dehydratase (EC: (gene edd) have been shown to be evolutionary related [PMID: 1624451]. 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 [PMID: 23233208]. The N-terminal part of the proteins contains a cysteine that could be involved in the binding of a 2Fe-2S iron-sulphur cluster [PMID: 8299945].

The structure of the N-terminal domain contains a large cluster of helices and a mixed beta-sheet of four strands where strands 3 and 4 are parallel.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.