UDP-N-acetylmuramoylalanyl-D-glutamate-2, 6-diaminopimelate ligase; Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. Belongs to the MurCDEF family. MurE subfamily.

Aminotransferases use 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; Specificity unclear.

Carbamoyl-phosphate synthase catalyses the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. It is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. Binds three magnesium ion as cofactor. Localized in the cytoplasm; High confidence in function and specificity.

Conserved hypothetical periplasmic protein; Functions as a peptidoglycan terminase that cleaves nascent peptidoglycan strands endolytically to terminate their elongation.

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.

Aspartate-semialdehyde dehydrogenase; Catalyzes the NADPH-dependent formation of L-aspartate- semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl- 4-phosphate; Belongs to the aspartate-semialdehyde dehydrogenase family.

Dihydrodipicolinate reductase reduces the alpha, beta-unsaturated cyclic imine, dihydro-dipicolinate. This reaction is the second committed step in the biosynthesis of L-lysine and its precursor meso- diaminopimelate, which are critical for both protein and cell wall biosynthesis. DapB activity is repressed by lysine. It forms a homotetramer and binds one NAD(P) per subunit as cofactor. Localized in the cytoplasm; High confidence in function and specificity.

Dihydrodipicolinate synthetase; Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).

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 [...]