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InterPro: IPR006263 Cytidine deaminase, homodimeric

Protein matches Help

UniProtKB

Matches:

237 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR006263 Cyt_deam_dimer

Type

Family

Signatures Help

Database	ID	Name	Proteins
TIGRFAMs	TIGR01355	cyt_deam_dimer	237
Signatures in BioMart

InterPro Relationships Help

Children

IPR020797 Cytidine deaminase, bacteria

Contains

IPR002125 CMP/dCMP deaminase, zinc-binding
IPR013171 Cytidine/deoxycytidylate deaminase, zinc-binding domain
IPR016192 APOBEC/CMP deaminase, zinc-binding
IPR016193 Cytidine deaminase-like

GO Term annotation Help

Process

GO:0046087 cytidine metabolic process

Function

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

InterPro annotation

Entry Details in BioMart

Abstract

This family represents the homodimeric form of cytidine deaminase, a zinc metalloprotein found in Escherichia coli [1] and in Arabidopsis thaliana (Mouse-ear cress). A related, homotetrameric form with a much smaller subunit is found most bacteria and in animals, IPR006262. Both types may act on deoxycytidine as well as cytidine.

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

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR006263

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.	Carlow DC, Carter CW Jr, Mejlhede N, Neuhard J, Wolfenden R. Cytidine deaminases from B. subtilis and E. coli: compensating effects of changing zinc coordination and quaternary structure. Biochemistry 38 12258-65 1999 [PubMed: 10493793] http://dx.doi.org/10.1021/bi990819t

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

InterPro 23.1