Glutamate synthase: Difference between revisions

The <scene name='72/727110/Cv/2'>Fd-GS structure contains 4 domains</scene>.  The N-terminal domain is an amidotransferase domain and contains an active site where <scene name='72/727110/Cv/3'>residue Cys1</scene> catalyzes the hydrolysis of glutamine to glutarate; a core domain; an FMN-binding domain which contains an Fe3S4 cluster and reduces the intermediate iminoglutarate to 2-oxoglutarate and produces a second molecule of glutarate and a C-terminal domain.  Residue M475 is located between the FMN and the Fe3S4 cluster.  It is is strictly conserved and may perform the electron transfer between the two centers.  The 2-oxoglutarate binds at the FMN-binding domain<ref>PMID:11967268</ref>.