GcvP2; Glycine cleavage system, dehydrogenase subunit GcvP2.

Putative glycine cleavage system T protein (aminomethyltransferase); Belongs to the GcvT family.

GcvP1; The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein.

LplA; Lipoate-protein ligase A LplA.

LipA; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.

PdhC; Dihydrolipoamide acetyltransferase PdhC (pyruvate dehydrogenase complex, E2 component).

LpdA; Lipoamide dehydrogenase LpdA (pyruvate dehydrogenase complex, E3 component).

LipB; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.

GlyA; 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.