Description

IPR012220 is a Glutamate synthase, eukaryotic.

<p>This group represents the eukaryotic type of glutamate synthase (NADH-GOGAT, [ec:1.4.1.14]). This pyridine-linked form is found in both photosynthetic and nonphotosynthetic eukaryotes. It displays a single-subunit structure corresponding to the fusion of the small and the large bacterial subunits.</p> <p>Glutamate synthase (GOGAT, GltS) is a complex iron-sulphur flavoprotein that catalyses the reductive synthesis of L-glutamate from 2-oxoglutarate and L-glutamine via intramolecular channelling of ammonia, a reaction in the bacterial, yeast and plant pathways for ammonia assimilation [[cite:PUB00013982]]. GOGAT is a multifunctional enzyme that functions through three distinct active centres carrying out multiple reaction steps: L-glutamine hydrolysis, conversion of 2-oxoglutarate into L-glutamate, and electron uptake from an electron donor [[cite:PUB00008698]]. The small subunit functions as a FAD-dependent NADPH oxidoreductase, which serves to transfer reducing equivalents to the site of glutamate synthesis on the large subunit through the enzyme [3Fe-4S] cluster (on the large subunit) and at least one of its [4Fe-4S] centres [[cite:PUB00009386], [cite:PUB00015747]]. The large subunit contains the GltS L-glutamine amidotransferase (GAT) site where L-Gln binds and is hydrolysed to yield L-Glu and ammonia. The latter is transferred through the intramolecular ammonia tunnel [[cite:PUB00013982]] to the glutamate synthase site where 2-OG binds, is converted to the iminoglutarate (2-IG) intermediate, and reduced to L-Glu by receiving reducing equivalents from the reduced FMN cofactor at this site [[cite:PUB00015837]].</p> <p>There are four classes of GOGAT [[cite:PUB00009386], [cite:PUB00015710]]:</p> <p>1. Bacterial NADPH-dependent GOGAT (NADPH-GOGAT, [ec:1.4.1.13]). This standard bacterial NADPH-GOGAT is composed of a large (alpha, GltB) subunit and a small (beta, GltD) subunit.</p> <p>2. Ferredoxin-dependent form in cyanobacteria and plants (Fd-GOGAT from photosynthetic cells, [ec:1.4.7.1]) displays a single-subunit structure corresponding to the large bacterial subunit.</p> <p>3. Pyridine-linked form in both photosynthetic and nonphotosynthetic eukaryotes (eukaryotic GOGAT or NADH-GOGAT, [ec:1.4.1.14]) displays a single-subunit structure corresponding to the fusion of the small and the large bacterial subunits.</p> <p>4. The archaeal type with stand-alone proteins corresponding to the N-terminal, FMN-binding, and the C-terminal domains of the large subunit [[cite:PUB00015710], [cite:PUB00009386]] ([interpro:IPR012375], [interpro:IPR012061]), and to the small subunit.</p> <p>The large subunit of GOGAT consists of three domains: N-terminal domain (amidotransferase domain [interpro:IPR017932]); central (consisting of [interpro:IPR006982] and the FMN-binding domain [interpro:IPR002932]), and the C-terminal domain ([interpro:IPR002489]).</p> <p>The N-terminal amidotransferase domain is characterised by a four layer α/β/β/α architecture and is similar to other Ntn-amidotransferases [[cite:PUB00008698]]. It contains the typical catalytic centre of Ntn-amidotransferases, and the N-terminal Cys-1 catalyses the hydrolysis of L-glutamine generating ammonia and the first molecule of L-glutamate [[cite:PUB00008698]].</p>

This description is obtained from EB-eye REST.

Associated GO terms

GO predictions are based solely on the InterPro-to-GO mappings published by EMBL-EBI, which are in turn based on the mapping of predicted domains to the InterPro dataset. The InterPro-to-GO mapping was last updated on April 27, 2020, while the GO metadata was last updated on April 27, 2020.

Associated Lotus transcripts 6

Co-occuring domains 1

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