Asparagine synthase (glutamine-hdrolysing) catalyses the conversion of aspartate to asparagine from glutamine as amido-N-donor. Contains a N-terminal class-2 glutamine amidotransferase domain (GATase domain). Forms a homodimer. 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.

Adenylosuccinate synthase; Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP; Belongs to the adenylosuccinate synthetase family.

Aspartate carbamoyltransferase catalyzes the conversion of aspartate and carbamoyl phosphate to carbamoylaspartate (). This is the second step in the de novo biosynthesis of pyrimidine nucleotides; Localized in the cytoplasm; High confidence in function and specificity; Belongs to the aspartate/ornithine carbamoyltransferase superfamily. ATCase family.

Asparaginase, which is found in various plant, animal and bacterial cells, catalyses the deamination of asparagine to yield aspartic acid and an ammonium ion; 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.

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.

Conserved hypothetical protein; Localized in the cytoplasm.

Homoserine O-acetyltransferase / Aspartokinase / Homoserine dehydrogenase; This enzyme is a modular protein with a homoserine O-acetyltransferase module (N-terminal) that catalyses the homoserine acetylation and belongs to the alpha/beta hydrolase fold family, an aspartate kinase module (central) that catalyzes the phosphorylation of aspartate and belongs to the amino acid kinase family and, in C- terminal part, a homoserine dehydrogenase module that catalyzes the NAD-dependent reduction of aspartate beta- semialdehyde into homoserine. This module is composed of a substrate-binding dom [...]