CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase; Identified by match to protein family HMM PF01066; match to protein family HMM TIGR00560; Belongs to the CDP-alcohol phosphatidyltransferase class-I family.

CDP-diacylglycerol-glycerol-3-phosphate; Identified by match to protein family HMM PF01066.

Phosphatidylinositol synthase; Catalyzes the conjugation of the 1'-hydroxyl group of D-myo- inositol-3-phosphate (also named L-myo-inositol-1-phosphate) with a lipid tail of cytidine diphosphate diacylglycerol (CDP-DAG), forming phosphatidylinositol phosphate (PIP) and CMP. PIP is a precursor of phosphatidylinositol (PI) which is an essential lipid for mycobacteria required for formation of their cell wall. Is essential to the survival of M.smegmatis. Belongs to the CDP-alcohol phosphatidyltransferase class-I family.

Phosphatidate cytidylyltransferase; Identified by match to protein family HMM PF01148; Belongs to the CDS family.

Cell division control protein Cdc48; Identified by match to protein family HMM PF00004; match to protein family HMM PF02359; Belongs to the AAA ATPase family.

Phosphoserine phosphatase; Identified by match to protein family HMM PF00702; match to protein family HMM PF01842; match to protein family HMM TIGR00338; match to protein family HMM TIGR01488.

Cystathionine beta-synthase; Identified by match to protein family HMM PF00291; match to protein family HMM PF00571; match to protein family HMM TIGR01137.

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.

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.