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InterPro: IPR013171 Cytidine/deoxycytidylate deaminase, zinc-binding domain

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Matches:

301 proteins

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Architectures
Accession List
Matches in BioMart

Accession

IPR013171 Cyd/dCyd_deaminase_Zn_bd

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF08211	dCMP_cyt_deam_2	301
Signatures in BioMart

InterPro Relationships Help

Found in

IPR006263 Cytidine deaminase, homodimeric
IPR016193 Cytidine deaminase-like
IPR020797 Cytidine deaminase, bacteria

GO Term annotation Help

Function

GO:0004126 cytidine deaminase activity
GO:0008270 zinc ion binding

InterPro annotation

Entry Details in BioMart

Abstract

This region contains the zinc-binding domain of cytidine and deoxycytidylate deaminase.

Cytidine deaminase (EC:3.5.4.5) (cytidine aminohydrolase) catalyzes the hydrolysis of cytidine into uridine and ammonia while deoxycytidylate deaminase (EC:3.5.4.12) (dCMP deaminase) hydrolyzes dCMP into dUMP. Both enzymes are known to bind zinc and to require it for their catalytic activity [1, 2]. These two enzymes do not share any sequence similarity with the exception of a region that contains three conserved histidine and cysteine residues which are thought to be involved in the binding of the catalytic zinc ion.

Structural links Help

PDB - click here

SCOP: c.97.1.1

CATH: 3.40.140.10

Database links Help

Enzyme: EC:3.5.4.5

Blocks: IPB013171

Pfam Clan: CL0109.8

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR013171

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P0ABF6 Cytidine deaminase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR013171	Cytidine/deoxycytidylate deaminase, zinc-binding domain
IPR002125	CMP/dCMP deaminase, zinc-binding
IPR016193	Cytidine deaminase-like
IPR016192	APOBEC/CMP deaminase, zinc-binding
IPR006263	Cytidine deaminase, homodimeric
IPR020797	Cytidine deaminase, bacteria
	PDB Chain
	ModBase
	CATH Domain
	SCOP Domain

Publications Open in usermanual
1.	Yang C, Carlow D, Wolfenden R, Short SA. Cloning and nucleotide sequence of the Escherichia coli cytidine deaminase (ccd) gene. Biochemistry 31 4168-74 1992 [PubMed: 1567863] http://dx.doi.org/10.1021/bi00132a003
2.	Moore JT, Silversmith RE, Maley GF, Maley F. T4-phage deoxycytidylate deaminase is a metalloprotein containing two zinc atoms per subunit. J. Biol. Chem. 268 2288-91 1993 [PubMed: 8428902] http://intl.jbc.org/cgi/reprint/268/4/2288.pdf

Additional Reading Open in usermanual
	Xiang S, Short SA, Wolfenden R, Carter CW Jr. The structure of the cytidine deaminase-product complex provides evidence for efficient proton transfer and ground-state destabilization. Biochemistry 36 1997 4768-74 [PubMed: 9125497] http://dx.doi.org/10.1021/bi963091e
	Xiang S, Short SA, Wolfenden R, Carter CW Jr. Cytidine deaminase complexed to 3-deazacytidine: a "valence buffer" in zinc enzyme catalysis. Biochemistry 35 1996 1335-41 [PubMed: 8634261] http://dx.doi.org/10.1021/bi9525583
	Xiang S, Short SA, Wolfenden R, Carter CW Jr. Transition-state selectivity for a single hydroxyl group during catalysis by cytidine deaminase. Biochemistry 34 1995 4516-23 [PubMed: 7718553] http://dx.doi.org/10.1021/bi00014a003
	Bhattacharya S, Navaratnam N, Morrison JR, Scott J, Taylor WR. Cytosine nucleoside/nucleotide deaminases and apolipoprotein B mRNA editing. Trends Biochem. Sci. 19 1994 105-6 [PubMed: 8203015] http://dx.doi.org/10.1016/0968-0004(94)90200-3

InterPro 23.1