v5.1.0.3
Glycine data from LIS
Type | Domain |
Description | 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 [ ]. 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 [, , ].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 [ , ]. |
Short Name | Glu_synthdom |