Domain

Metal-dependent hydrolase, composite domain (IPR011059)

Short name: Metal-dep_hydrolase_composite

Domain relationships

None.

Description

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 [PMID: 11812140]; the alpha-subunit of urease, a virulence factor of gastric pathogens such as Helicobacter pylori (Campylobacter pylori) [PMID: 12127484]; D- and L-hydantoinases (dihydropyrimidinase), which catalyse the production of D- and L-amino acids, respectively [PMID: 12837777]; isoaspartyl dipeptidase from Escherichia coli, which functions in protein degradation [PMID: 12718528]; N-acetylglucosamine-6-phosphate deacetylase, which is an enzyme from the biosynthetic pathway to amino-sugar-nucleotides [PMID: 14557261]; and N-acyl-D-amino acid amidohydrolase (D-aminoacylase), involved in the synthesis of D-amino acids [PMID: 12454005].

GO terms

Biological Process

No terms assigned in this category.

Molecular Function

GO:0016810 hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
GENE3D
SUPERFAMILY