Diaminopimelate epimerase; Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L- lysine.

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.

2,3,4,5-Tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase; DapD is involved in L-Lysine and diaminopimelate biosynthesis. It catalyzes the reaction: Succinyl-CoA + (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + H2O = CoA + N-succinyl-L-2-amino-6-oxoheptanedioate. Localized in the cytoplasm; High confidence in function and specificity; Belongs to the transferase hexapeptide repeat family.

Prephenate dehydratase catalyzes the decarboxylation of prephenate to phenylpyruvate. PheA is involved in L-phenylalanine biosynthesis. It features a C- terminal ACT domain. ACT domains are linked to a wide range of metabolic enzymes that are regulated by amino acid concentration. Localized in the cytoplasm; High confidence in function and specificity.

Bifunctional enzyme including 3-deoxy-7-phosphoheptulonate synthase (DAHP synthase) in N-terminus and chorismate mutase in C-terminus. DAHP synthase catalyzes the first step in the common pathway leading to the biosynthesis of aromatic compounds, the stereospecific condensation of phosphoenolpyruvate and D-erythrose-4-phosphate giving rise to 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP). Chorismate mutase catalyzes the conversion of chorismate to prephenate in the pathway of tyrosine and phenylalanine biosynthesis. Localized in the cytoplasm; High confidence in function and speci [...]

ThrA is a fusion-protein between aspartate kinase I (N-terminal) and homoserine dehydrogenase I (C-terminal) involved in L-Lysine and L-threonine biosynthesis pathways. Aspartate kinase I converts L-aspartate to 4-phospho-L-aspartate and belongs to the amino acid kinase family. Homoserine dehydrogenase I converts the L-homoserine to L-aspartate 4-semialdehyde. Homoserine dehydrogenase I is composed of a substrate-binding domain belonging to Homoserine dehydrogenase family and a NAD-binding domain (Rossman fold). ThrA features also two central regulatory ACT domains; Localized in the cy [...]

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 [...]

Bifunctional protein: Malic enzyme (N-terminal domain, 1 to 550) and Phosphate acetyl/butaryl transferase (C-terminal domain, 550 to 765); High confidence in function and specificity.

Phosphoserine phosphatase / D-3-phosphoglycerate dehydrogenase; Catalyzes the reversible oxidation of 3-phospho-D-glycerate to 3-phosphonooxypyruvate, the first step of the phosphorylated L- serine biosynthesis pathway. Also catalyzes the reversible oxidation of 2-hydroxyglutarate to 2-oxoglutarate; Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family.