CarD is involved in carbapenem antibiotic biosynthesis, but its exact function is unknown. Belongs to the proline dehydrogenase family and likely binds a FAD as a cofactor. Localized in the cytoplasm; Function 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 [...]

Aspartate aminotransferase or Transaminase A or Glutamic-aspartic transaminase or Glutamic-oxaloacetic transaminase converts the L-aspartic acid and the 2-oxoglutarate into L-glutamate and oxaloacetate using the Pyridoxal phosphate as cofactor bound by covalent linkage to a lysine residue; Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family; Localized in the cytoplasm; High confidence in function and specificity.

Aspartate aminotransferase or Transaminase A or Glutamic-aspartic transaminase or Glutamic-oxaloacetic transaminase converts the L-aspartic acid and the 2-oxoglutarate into L-glutamate and oxaloacetate using the Pyridoxal phosphate as cofactor bound by covalent linkage to a lysine residue; Belongs to the class-I 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.

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 [...]

Pyrroline-5-carboxylate reductase; Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline.