Glutamate synthase

spinqualitylabelsall models Ferredoxin-dependent glutamate synthase containing a Fe3S4 cluster complex with FMN, 2-oxoglutarate (PDB code 1llw) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Function Glutamate synthase (GS) is an iron-sulfur flavoprotein which catalyzes the reverse reaction which converts L-glutamine, 2-oxoglutarate and NADPH to L-glutarate and NADP. . Fd-dependent glutamate synthase catalyzes the reverse reaction converting L-glutamate and oxidized ferredoxin to L-glutamine, 2-oxoglutarate and oxidized ferredoxin. Fd-GS uses FMN as a cofactor. Structural highlights The Fd-GS structure contains 4 domains. The N-terminal domain is an amidotransferase domain and contains an active site where residue Cys1 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. FMN binding site The 2-oxoglutarate binds at the FMN-binding domain.

3D structures of glutamate synthase

Updated on 29-March-2026

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• Glutamate synthase
  • 1ea0 – AbGS α subunit + FMN + oxo-glutarate – Azospirillum brasilense
    
  • 6s6s, 6s6t, 6s6u, 6s6x – AbGS α+β subunits + FAD + FMN + Fe3S4 + Fe4S4 – CryoEM
    
  • 2vdc – AbGS α+β subunits + FAD + FMN + Fe3S4 + Fe4S4 + oxoglutarate – CryoEM
    
  • 7mfm, 7mft – GS + glutamate dehydrogenase – Bacillus subtilis - CryoEM
    
• Fd-dependent glutamate synthase
  • 1llw, 1ofd – SyGS + FMN + 2-αoxoglutarate – Synechocystis
    
  • 1llz, 1lm1 – SyGS + FMN
    
  • 1ofe – SyGS + FMN + 2-oxglutarate + oxo-norleucine
    

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