Domain

Cytidine and deoxycytidylate deaminase domain (IPR002125)

Short name: CMP_dCMP_dom

Domain relationships

Description

Cytidine deaminase (EC 3.5.4.5) (cytidine aminohydrolase) catalyses the hydrolysis of cytidine into uridine and ammonia while deoxycytidylate deaminase (EC 3.5.4.12) (dCMP deaminase) hydrolyses dCMP into dUMP. Both enzymes are known to bind zinc and to require it for their catalytic activity [PMID: 1567863, PMID: 8428902]. The deaminases possess either one or two conserved zinc-coordinating (Z) motifs, with the consensus amino acid signature H-x(1)-E-x(24,28)-P-C-x(2,4)-C. This motif is required for catalytic activity. Zinc coordination is mediated by a histidine and two cysteines [PMID: 20152150]. The CMP/dCMP-type deaminase domain consists of a central beta-sheet with one or more alpha helices on each side [PMID: 11851403].

This entry represents the CMP/dCMP-type deaminase domain. Some enzymes, such as riboflavin biosynthesis protein PYRR, have a non-functional deaminase domain that lacks the catalytically essential zinc-binding residues [PMID: 23150645].

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PROSITE profiles
Pfam