InterPro domain: IPR029767

This entry includes UDP-N-acetylglucosamine 2-epimerase WecB from Enterobacteriaceae and UDP-2,3-diacetamido-2,3-dideoxy-D-glucuronate 2-epimerase WbpI from Pseudomonas aeruginosa. WecB is involved in the enterobacterial common antigen biosynthesis, which is part of bacterial outer membrane biogenesis. It catalyses the reversible epimerization at C-2 of UDP-N-acetylglucosamine (UDP-GlcNAc) and thereby provides bacteria with UDP-N-acetylmannosamine (UDP-ManNAc), the activated donor of ManNAc residues [ 1 ]. WbpI is involved in the LPS O-antigen biosynthesis, which is part of bacterial outer membrane biogenesis. It catalyses the epimerization of UDP-2,3-diacetamido-2,3-dideoxy-alpha-D-glucuronic acid (UDP-alpha-D-GlcNAc3NAcA) to UDP-2,3-diacetamido-2,3-dideoxy-alpha-D-mannuronic acid (UDP-alpha-D-ManNAc3NAcA) [ 2 ].

1. Active site mutants of the "non-hydrolyzing" UDP-N-acetylglucosamine 2-epimerase from Escherichia coli. Biochim. Biophys. Acta 1700, 85-91
2. Identification and biochemical characterization of two novel UDP-2,3-diacetamido-2,3-dideoxy-alpha-D-glucuronic acid 2-epimerases from respiratory pathogens. Biochem. J. 405, 123-30