InterPro: IPR011059 Metal-dependent hydrolase, composite domain

The composite domain of metal-dependent hydrolases has a pseudo-barrel fold that is interrupted by the catalytic beta/alpha barrel domain. This domain is found in a variety of bacterial and fungal enzymes, including: cytosine deaminase, an enzyme that is important in the pyrimidine salvage pathway [1]; the alpha-subunit of urease, a virulence factor of gastric pathogens such as Helicobacter pylori (Campylobacter pylori) [2]; D- and L-hydantoinases (dihydropyrimidinase), which catalyse the production of D- and L-amino acids, respectively [3]; isoaspartyl dipeptidase from Escherichia coli, which functions in protein degradation [4]; N-acetylglucosamine-6-phosphate deacetylase, which is an enzyme from the biosynthetic pathway to amino-sugar-nucleotides [5]; and N-acyl-D-amino acid amidohydrolase (D-aminoacylase), involved in the synthesis of D-amino acids [6].