Protein Domain : N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA IPR023881

Type	Family
Description	Members of this protein family are BshA, a glycosyltransferase required for bacillithiol biosynthesis. BshA catalyzes the formation of the first intermediate, GlcNAc-Mal, using L-malate and the glucosamine donor substrate UDP-N-acetylglucosamine (UDP-GlcNAc) as substrates. Bacillithiol is a low-molecular-weight thiol, an analogue of glutathione and mycothiol, and is found largely in the Firmicutes [ ]. This family is most closely related to the GT1 family of glycosyltransferases [ ]. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. Glycosyltransferases may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities reflect a wide range of biological functions. The protein structure for members of the GT1 family has a GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic centre and permits a high degree of flexibility [].
Short Name	Thiol_BshA