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 [...]

Threonine dehydratase; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA.

Phosphoserine aminotransferase; Catalyzes the reversible conversion of 3- phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4- phosphonooxybutanoate to phosphohydroxythreonine; Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. SerC subfamily.

The L-allo-threonine aldolase is an enzyme involved in the Glycine metabolism. It converts the L-allo-Threonine and the threonine to glycine; Uses a pyridoxal phosphate group as cofactor; Localized in the cytoplasm; High confidence in function and specificity.

The threonine synthase catalyzes the transformation of homoserine-phosphate into threonine; Uses the pyridoxal phosphate as cofactor (vitamin B6) attached to a conserved lysine residue; Belongs to the serine/threonine dehydratase family; Localized in the cytoplasm; High confidence in function and specificity.

This enzyme belongs to the NAD-dependent epimerase/dehydratase family, which is included in the Rossmann fold Superfamily. The proteins in this family use nucleotide-sugar substrates for a variety of chemical reactions; Localized in the cytoplasm; Family membership.

Serine racemase; Catalyzes the synthesis of D-serine from L-serine; Use the pyridoxal phosphate as cofactor (vitamin B6); Belongs to the serine/threonine dehydratase family; Localized in the cytoplasm; High confidence in function and specificity.

3-Isopropylmalate dehydratase, small subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. Belongs to the LeuD family. LeuD type 1 subfamily.