Glutamate 5-kinase; Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate.

1-pyrroline-5-carboxylate dehydrogenase is involved in L-proline degradation. It catalyzes the reaction: 1-pyrroline-5-carboxylate + NAD+ + H2O = L-glutamate + NADH. Belongs to the aldehyde dehydrogenase family and uses NAD as cofactor. Localized in the cytoplasm; High confidence in function and specificity.

Gamma-glutamyl phosphate reductase; Catalyzes the NADPH-dependent reduction of L-glutamate 5- phosphate into L-glutamate 5-semialdehyde and phosphate. The product spontaneously undergoes cyclization to form 1-pyrroline-5-carboxylate. Belongs to the gamma-glutamyl phosphate reductase family.

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 [...]

Glutamine synthetase (GS), also known as Glutamate-ammonia ligase, plays an essential role in the metabolism of nitrogen by catalyzing the condensation of glutamate and ammonia to form glutamine. Belongs to the GS class II which is usually found in eukaryotes and in bacteria belonging to the Rhizobiaceae, Frankiaceae, and Streptomycetaceae families. GSII are octamer of identical subunits. Localized in the cytoplasm; High confidence in function and specificity.

Glutamate synthase [NADPH] small 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 (GltA) and a small subunit. GltB binds NADP(H) as a cofactor. Localized in the cytoplasm; High con [...]

Acetylornithine aminotransferase catalyzes the transfer of an amino group from acetylornithine to alpha-ketoglutarate, yielding N-acetyl-glutamic-5-semi-aldehyde and glutamic acid. This is the fourth step in the arginine biosynthesis pathway. ArgD is also involved in the urea cycle. This enzyme uses the pyridoxal phosphate as cofactor linked to a conserved lysine residue. Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. Localized in the cytoplasm; High confidence in function and specificity.

Glutamate dehydrogenase catalyzes the NAD- and/or NADP-dependent reversible deamination of L-glutamate into alpha-ketoglutarate. It is involved with either ammonia assimilation or glutamate catabolism. Forms a homohexamer and binds one NAD(P) cofactor by subunit. Localized in the cytoplasm; High confidence in function and specificity; Belongs to the Glu/Leu/Phe/Val dehydrogenases family.

Glutamate dehydrogenase catalyzes the NAD- and/or NADP-dependent reversible deamination of L-glutamate into alpha-ketoglutarate. It is involved with either ammonia assimilation or glutamate catabolism. Forms a homohexamer and binds one NAD(P) cofactor by subunit. Localized in the cytoplasm; High confidence in function and specificity; Belongs to the Glu/Leu/Phe/Val dehydrogenases family.