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InterPro: IPR013346 Ribonucleoside-diphosphate reductase, alpha subunit

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1789 proteins

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Accession

IPR013346 NrdE_NrdA

Type

Domain

Signatures Help

Database	ID	Name	Proteins
TIGRFAMs	TIGR02506	NrdE_NrdA	1789
Signatures in BioMart

InterPro Relationships Help

Parent

IPR000788 Ribonucleotide reductase large subunit, C-terminal

Contains

IPR013509 Ribonucleotide reductase large subunit, N-terminal

GO Term annotation Help

Process

GO:0055114 oxidation reduction

Component

GO:0005971 ribonucleoside-diphosphate reductase complex

InterPro annotation

Entry Details in BioMart

Abstract

This entry represents the alpha (large) chain of the class I ribonucleotide reductase (RNR). RNR's are responsible for the conversion of the ribose sugar of RNA into the deoxyribose sugar of DNA. This is the rate-limiting step of DNA biosynthesis. Class I RNR's generate the required radical (on tyrosine) via a "non-heme" iron cofactor which resides in the beta (small) subunit. The alpha subunit contains the catalytic and allosteric regulatory sites. The mechanism of this enzyme requires molecular oxygen [1]. Escherichia coli contains two versions of this enzyme which are regulated independently (NrdAB and NrdEF, where NrdA and NrdE are the large chains [2, 3]). Most organisms contain only one, but the application of the gene symbols NrdA and NrdE are somewhat arbitrary. This model identifies RNR's in diverse clades of bacteria, eukaryotes as well as numerous DNA viruses and phage.

Structural links Help

PDB - click here

SCOP: a.98.1.1 , c.7.1.2

Database links Help

Enzyme: EC:1.17.4.1

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR013346

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P07742 Ribonucleoside-diphosphate reductase large subunit

P21524 Ribonucleoside-diphosphate reductase large chain 1

P23921 Ribonucleoside-diphosphate reductase large subunit

P48591 Ribonucleoside-diphosphate reductase large subunit

Q03604 Ribonucleoside-diphosphate reductase large subunit

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR000788	Ribonucleotide reductase large subunit, C-terminal
IPR008926	Ribonucleotide reductase R1 subunit, N-terminal
IPR013509	Ribonucleotide reductase large subunit, N-terminal
IPR005144	ATP-cone
IPR013346	Ribonucleoside-diphosphate reductase, alpha subunit
	SWISS-MODEL
	PDB Chain
	ModBase

Publications Open in usermanual
1.	Smalley D, Rocha ER, Smith CJ. Aerobic-type ribonucleotide reductase in the anaerobe Bacteroides fragilis. J. Bacteriol. 184 895-903 2002 [PubMed: 11807048] http://dx.doi.org/10.1128/jb.184.4.895-903.2002
2.	Uhlin U, Eklund H. Structure of ribonucleotide reductase protein R1. Nature 370 533-9 1994 [PubMed: 8052308] http://dx.doi.org/10.1038/370533a0
3.	Jordan A, Aragall E, Gibert I, Barbe J. Promoter identification and expression analysis of Salmonella typhimurium and Escherichia coli nrdEF operons encoding one of two class I ribonucleotide reductases present in both bacteria. Mol. Microbiol. 19 777-90 1996 [PubMed: 8820648] http://dx.doi.org/10.1046/j.1365-2958.1996.424950.x

Additional Reading Open in usermanual
	Uppsten M, Farnegardh M, Jordan A, Eliasson R, Eklund H, Uhlin U. Structure of the large subunit of class Ib ribonucleotide reductase from Salmonella typhimurium and its complexes with allosteric effectors. J. Mol. Biol. 330 2003 87-97 [PubMed: 12818204] http://dx.doi.org/10.1016/S0022-2836(03)00538-2
	Persson AL, Eriksson M, Katterle B, Potsch S, Sahlin M, Sjoberg BM. A new mechanism-based radical intermediate in a mutant R1 protein affecting the catalytically essential Glu441 in Escherichia coli ribonucleotide reductase. J. Biol. Chem. 272 1997 31533-41 [PubMed: 9395490] http://dx.doi.org/10.1074/jbc.272.50.31533
	Eriksson M, Uhlin U, Ramaswamy S, Ekberg M, Regnstrom K, Sjoberg BM, Eklund H. Binding of allosteric effectors to ribonucleotide reductase protein R1: reduction of active-site cysteines promotes substrate binding. Structure 5 1997 1077-92 [PubMed: 9309223] http://dx.doi.org/10.1016/S0969-2126(97)00259-1
	Uppsten M, Farnegardh M, Domkin V, Uhlin U. The first holocomplex structure of ribonucleotide reductase gives new insight into its mechanism of action. J. Mol. Biol. 359 2006 365-77 [PubMed: 16631785] http://dx.doi.org/10.1016/j.jmb.2006.03.035

InterPro 23.1