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Udp N-acetylglucosamine O-acyltransferase; Domain 2
This is domain 2, or the C-terminal domain, of Udp N-acetylglucosamine O-acyltransferase. This enzyme is a zinc-dependent enzyme that catalyses the deacetylation of UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine to form UDP-3-O-(R-hydroxymyristoyl)glucosamine and acetate. [1]. 15705580. UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase functions through a general acid-base catalyst pair mechanism. Hernick M, Gennadios HA, Whittington DA, Rusche KM, Christianson DW, Fierke CA;. J Biol Chem. 2005;280:16969-16978. (from Pfam)
transferase-like hexapeptide repeat-containing protein
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase is involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell
Catalyzes the addition of (R)-3-hydroxytetradecanoyl to the glucosamine disaccharide in lipid A biosynthesis
This HMM describes LpxA, an enzyme for the biosynthesis of lipid A, a component oflipopolysaccharide (LPS) in the outer membrane outer leaflet of most Gram-negative bacteria. Some differences are found between lipid A of different species, but this protein represents the first step (from UDP-N-acetyl-D-glucosamine) and appears to be conserved in function. Proteins from this family contain many copies of the bacterial transferase hexapeptide repeat (PF00132).
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