Transcriptional regulator belonging to the LysR family. Features a N-terminal helix-turn-helix DNA binding domain and a C-terminal LysR-like substrate binding domain. Localized in the cytoplasm; Specificity unclear.

Glutamate synthase [NADPH] large chain; Glutamate synthase is a key enzyme in the early stages of the assimilation of ammonia. It is a complex iron-sulfur flavoprotein catalyzing the reductive transfer of the amido nitrogen from L-glutamine to 2-oxoglutarate to form two molecules of L-glutamate via intramolecular channelling of ammonia from the amidotransferase domain to the FMN-binding domain. Glutamate synthase forms an aggregate of 4 catalytic active heterodimers, consisting of a large and a small subunit (GltB). GltA binds as cofactors a 3Fe-4S cluster, a FAD and a FMN. Localized i [...]

Peroxiredoxins are thiol peroxidase. They are involved in redox regulation of the cell. Can reduce H(2)O(2) and short chain organic, fatty acid, and phospholipid hydroperoxides. The peroxidase reaction comprises two steps centered around a redox- active cysteine called the peroxidatic cysteine. It attacks the peroxide substrate and is oxidized to S-hydroxycysteine (a sulfenic acid). The second step is the regeneration of cysteine from S-hydroxycysteine. This regeneration is due to thiol-containing reductants such as thioredoxin. Localized in the cytoplasm; Specificity unclear.

Sulfite reductase [NADPH] flavoprotein alpha-component; Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. The flavoprotein component catalyzes the electron flow from NADPH -> FAD -> FMN to the hemoprotein component.