N-acetylglucosamine-6-phosphate deacetylases (NAGPase) catalyze the hydrolysis of N-acetyl-D-glucosamine-6-phosphate to form D-glucosamine-6-phosphate and acetate. Amino sugars, like glucosamine or N-acetylglucosamine are used by bacteria for cell wall and lipid A synthesis. Bacteria use also N-acetylglucosamine as a carbon source producing similar growth rates as glucose. The structure of IDP01334 closely resembles the structures of protein homologs from E.coli and B.subtilis. The protein monomer forms two structural domains. The bigger domain comprises the central part of the protein and forms an barrel enclosing the catalytic site of the enzyme. The small domain consists of the N and C termini and forms a -strand barrel. Our structure includes a nickel ion in the position of one of two iron ions found in N-acetylglucosamine-6-phosphate deacetylase from Bacillus subtilis, 2VHL.