Description

IPR037396 is a FMN hydroxy acid dehydrogenase domain.

<p>A number of oxidoreductases that act on alpha-hydroxy acids and which are FMN-containing flavoproteins have been shown to be structurally related [[cite:PUB00002617], [cite:PUB00000334], [cite:PUB00002664], [cite:PUB00037691]]; these enzymes are:</p> <ul> <li>Lactate dehydrogenase ([ec:1.1.2.3]), which consists of a dehydrogenase domain and a heme-binding domain called cytochrome b2 and which catalyzes the conversion of lactate into pyruvate.</li> <li>Glycolate oxidase ([ec:1.1.3.15]) ((S)-2-hydroxy-acid oxidase), a peroxisomal enzyme that catalyzes the conversion of glycolate and oxygen to glyoxylate and hydrogen peroxide.</li> <li>Long chain alpha-hydroxy acid oxidase from rat ([ec:1.1.3.15]), a peroxisomal enzyme.</li> <li>Lactate 2-monooxygenase ([ec:1.13.12.4]) (lactate oxidase) from Mycobacterium smegmatis, which catalyzes the conversion of lactate and oxygen to acetate, carbon dioxide and water.</li> <li>(S)-mandelate dehydrogenase from Pseudomonas putida (gene mdlB), which catalyzes the reduction of (S)-mandelate to benzoylformate.</li> </ul> <p>The first step in the reaction mechanism of these enzymes is the abstraction of the proton from the α-carbon of the substrate producing a carbanion which can subsequently attach to the N5 atom of FMN. A conserved histidine has been shown [[cite:PUB00002533]] to be involved in the removal of the proton. Three-dimensional structures of FMN-dependent alpha-hydroxy acid dehydrogenases show a common fold with a TIM barrel structure.</p> <p>This entry represents the FMN hydroxy acid dehydrogenase domain.</p>

This description is obtained from EB-eye REST.

Associated GO terms

Unable to find any GO terms for the transcript with the identifier.

Associated Lotus transcripts 7

Co-occuring domains 1

A list of co-occurring predicted domains within the L. japonicus gene space: