Glutamate synthase domain (IPR002932)

Short name: Glu_synthdom

Overlapping homologous superfamilies

Domain relationships



Ferredoxin-dependent glutamate synthase (GltS) has been implicated in a number of functions including photorespiration in Arabidopsis where it may also play a role in primary nitrogen assimilation in roots [PMID: 9596633]. GltS is a complex iron-sulfur flavoprotein that catalyzes the reductive synthesis of L-glutamate from 2-oxoglutarate and L-glutamine via intramolecular channelling of ammonia, a reaction in the plant, yeast and bacterial pathway for ammonia assimilation. It is a multifunctional enzyme that functions through three distinct active centres, carrying out L-glutamine hydrolysis, conversion of 2-oxoglutarate into L-glutamate, and electron uptake from an electron donor [PMID: 15581577, PMID: 15052410, PMID: 12702341].

This domain is expressed as a separate subunit in the glutamate synthase alpha subunit from archaebacteria, or part of a large multidomain enzyme in other organisms. It contains a putative FMN binding site and Fe-S cluster [PMID: 12455964, PMID: 8923741].

GO terms

Biological Process

GO:0006537 glutamate biosynthetic process
GO:0055114 oxidation-reduction process

Molecular Function

GO:0015930 glutamate synthase activity
GO:0016638 oxidoreductase activity, acting on the CH-NH2 group of donors

Cellular Component

No terms assigned in this category.

Contributing signatures

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