| Description | Two dehydratases, dihydroxy-acid dehydratase ( ) (gene ilvD or ILV3) and 6-phosphogluconate dehydratase ( ) (gene edd) have been shown to be evolutionary related [ ]. 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 []. The N-terminal part of the proteins contains a cysteine that could be involved in the binding of a 2Fe-2S iron-sulphur cluster [].This entry contains two signature patterns: the first pattern is located in the N-terminal half and contains a cysteine that could be involved in the binding of a 2Fe-2S iron-sulphur cluster; the second pattern is located in the C-terminal half. | Name | Dihydroxy-acid/6-phosphogluconate dehydratase, conserved site |
| Short Name | DiOHA_6PGluconate_deHydtase_CS | Type | Conserved_site |
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