Catalyzes the formation of cystathionine from L-cysteine and O-succinyl-L-homoserine; Derived by automated computational analysis using gene prediction method: Protein Homology.

Cystathionine beta-lyase; Derived by automated computational analysis using gene prediction method: Protein Homology.

Cystathionine beta-lyase; Catalyzes the formation of L-homocysteine from cystathionine; Derived by automated computational analysis using gene prediction method: Protein Homology.

Serine hydroxymethyltransferase; Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.

Catalyzes the O-acetylation of serine; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the transferase hexapeptide repeat family.

Adenosylhomocysteinase; Derived by automated computational analysis using gene prediction method: Protein Homology.

B12-dependent methionine synthase; Catalyzes the transfer of a methyl group from methyl- cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate.

S-ribosylhomocysteinase; Involved in the synthesis of autoinducer 2 (AI-2) which is secreted by bacteria and is used to communicate both the cell density and the metabolic potential of the environment. The regulation of gene expression in response to changes in cell density is called quorum sensing. Catalyzes the transformation of S-ribosylhomocysteine (RHC) to homocysteine (HC) and 4,5-dihydroxy-2,3-pentadione (DPD). Belongs to the LuxS family.

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.