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InterPro: IPR011962 Deoxycytidine triphosphate deaminase

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UniProtKB

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929 proteins

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Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
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Accession List
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Accession

IPR011962 dCTP_deam

Type

Family

Signatures Help

Database	ID	Name	Proteins
HAMAP	MF_00146	dCTP_deam	733
TIGRFAMs	TIGR02274	dCTP_deam	929
Signatures in BioMart

InterPro Relationships Help

Contains

IPR008180 DeoxyUTP pyrophosphatase domain

GO Term annotation Help

Process

GO:0006229 dUTP biosynthetic process

Function

GO:0005515 protein binding
GO:0008829 dCTP deaminase activity

InterPro annotation

Entry Details in BioMart

Abstract

This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA. It does probably not deaminate dCTP.

Members of this family include the Escherichia coli monofunctional deoxycytidine triphosphate deaminase (dCTP deaminase) and a Methanocaldococcus jannaschii (Methanococcus jannaschii) bifunctional dCTP deaminase (EC:3.5.4.13)/dUTP diphosphatase (EC:3.6.1.23).

For additional information please see [1].

Structural links Help

PDB - click here

SCOP: b.85.4.1

CATH: 2.70.40.10

Database links Help

Enzyme: EC:3.5.4.13

Taxonomic coverage Help

Example proteins Help

O07247 Deoxycytidine triphosphate deaminase

O71028 Probable deoxyuridine 5'-triphosphate nucleotidohydrolase

Q57872 dCTP deaminase, dUMP-forming

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR011962	Deoxycytidine triphosphate deaminase
IPR008180	DeoxyUTP pyrophosphatase domain
	SWISS-MODEL
	PDB Chain
	ModBase
	SCOP Domain
	CATH Domain

Publications Open in usermanual
1.	Bylund GO, Wipemo LC, Lundberg LA, Wikstrom PM. RimM and RbfA are essential for efficient processing of 16S rRNA in Escherichia coli. J. Bacteriol. 180 73-82 1998 [PubMed: 9422595] http://ukpmc.ac.uk/articlerender.cgi?tool=EBI&pubmedid=9422595

Additional Reading Open in usermanual
	Huffman JL, Li H, White RH, Tainer JA. Structural basis for recognition and catalysis by the bifunctional dCTP deaminase and dUTPase from Methanococcus jannaschii. J. Mol. Biol. 331 2003 885-96 [PubMed: 12909016] http://dx.doi.org/10.1016/S0022-2836(03)00789-7
	Johansson E, Fano M, Bynck JH, Neuhard J, Larsen S, Sigurskjold BW, Christensen U, Willemoes M. Structures of dCTP deaminase from Escherichia coli with bound substrate and product: reaction mechanism and determinants of mono- and bifunctionality for a family of enzymes. J. Biol. Chem. 280 2005 3051-9 [PubMed: 15539408] http://dx.doi.org/10.1074/jbc.M409534200
	Bjornberg O, Neuhard J, Nyman PO. A bifunctional dCTP deaminase-dUTP nucleotidohydrolase from the hyperthermophilic archaeon Methanocaldococcus jannaschii. J. Biol. Chem. 278 2003 20667-72 [PubMed: 12670946] http://dx.doi.org/10.1074/jbc.M213010200
	Johansson E, Bjornberg O, Nyman PO, Larsen S. Structure of the bifunctional dCTP deaminase-dUTPase from Methanocaldococcus jannaschii and its relation to other homotrimeric dUTPases. J. Biol. Chem. 278 2003 27916-22 [PubMed: 12756253] http://dx.doi.org/10.1074/jbc.M304361200

InterPro 23.1