InterPro domain: IPR011059

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 ].

1. The structure of Escherichia coli cytosine deaminase. J. Mol. Biol. 315, 687-97
2. Transcriptional and mutational analysis of the Helicobacter pylori urease promoter. FEMS Microbiol. Lett. 213, 27-32
3. Crystal structure of D-Hydantoinase from Burkholderia pickettii at a resolution of 2.7 Angstroms: insights into the molecular basis of enzyme thermostability. J. Bacteriol. 185, 4038-49
4. High-resolution X-ray structure of isoaspartyl dipeptidase from Escherichia coli. Biochemistry 42, 4874-82
5. The three-dimensional structure of the N-acetylglucosamine-6-phosphate deacetylase, NagA, from Bacillus subtilis: a member of the urease superfamily. J. Biol. Chem. 279, 2809-16
6. Crystal structure of D-aminoacylase from Alcaligenes faecalis DA1. A novel subset of amidohydrolases and insights into the enzyme mechanism. J. Biol. Chem. 278, 4957-62