N-acetylornithine carbamoyltransferase catalyzes the convertion of N-acetylornithine to N-acetylcitrulline and has no catalytic activity with L-ornithine as substrate. ArgF' does not feature the SMG motif which is conserved in the canonical ArgF (L-ornithine to L- citrulline). In this alternative pathway, N-acetyl-L- citrulline is likely deacetylated by ArgE; Localized in the cytoplasm; High confidence in function and specificity.

Argininosuccinate lyase is involved in the eighth and last step of the arginine biosynthesis pathway. It converts the Omega-N-(L-arginino)succinate to fumarate and L-arginine; Belongs to the fumarate lyase family. Localized in the cytoplasm; High confidence in function and specificity.

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.

Argininosuccinate synthase (AS) is a urea cycle enzyme that catalyzes the penultimate step in arginine biosynthesis: the ATP-dependent ligation of citrulline to aspartate to form argininosuccinate, AMP and pyrophosphate; Belongs to the argininosuccinate synthase family, type 1 subfamily; Localized in the cytoplasm; High confidence in function and specificity.

Acetylornithine deacetylase, family M20A; Acetylornithine deacetylase catalyzes the fifth step of the arginine biosynthesis pathway, converting the 2-N-acetyl-L-ornithine to L-ornithine and acetate. L-ornithine is also a branchpoint in the synthesis of polyamines. ArgE binds two zinc ions per monomer of protein; Belongs to the family M20A of the metallopeptidases; Localized in the cytoplasm; High confidence in function and specificity.

Nitrogen regulatory protein P-II; P-II indirectly controls the transcription of the glutamine synthetase gene (glnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I-phosphate, the transcriptional activator of glnA. When P-II is uridylylated to P-II-UMP, these events are reversed. When the ratio of Gln to 2-ketoglutarate decreases, P-II is uridylylated to P-II-UMP, which causes the deadenylation of glutamine synthetase by glnE, so activating the enzyme; Forms a homotrimer; Localized in the cytoplasm; High confidence in function and specificity; Belongs to the P(II) protein family.

The N-Acetyltransferases catalyze the transfer of an acetyl group from acetyl-CoA to a substrate molecule. Belongs to Gcn5 or GNAT actyltransferase family. Localized in the cytoplasm; Family membership.

Acetylornithine aminotransferase is involved in the Urea cycle and metabolism of amino groups. It catalyzes the transfer of an amino group from acetylornithine to alpha-ketoglutarate, yielding N-acetyl-glutamic-5-semi-aldehyde and glutamic acid; 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.

Ornithine aminotransferase is involved in the Urea cycle and it is responsible for the fourth step in arginine biosynthesis. It catalyzes the transfer of an amino group from ornithine to a 2-oxo acid, yielding glutamic-5-semi-aldehyde and an L-amino acid; 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.