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InterPro: IPR012348 Ribonucleotide reductase-related

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UniProtKB

Matches:

3736 proteins

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

Accession

IPR012348 Ribncl_red_rel

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Gene3D	G3DSA:1.10.620.20	Ribncl_red_rel	3736
Signatures in BioMart

InterPro Relationships Help

Parent

IPR009078 Ferritin/ribonucleotide reductase-like

Found in

IPR000358 Ribonucleotide reductase
IPR003430 Methane/phenol/toluene hydroxylase
IPR005067 Fatty acid desaturase, type 2
IPR012078 Methane/phenol monooxygenase, hydroxylase component

Contains

IPR005803 Stearoyl-ACP desaturase, conserved site

GO Term annotation Help

Process

GO:0055114 oxidation reduction

Function

GO:0016491 oxidoreductase activity

InterPro annotation

Entry Details in BioMart

Abstract

The R2 protein of ribonucleotide reductase catalyses the reduction of all four ribonucleotides to deoxyribonucleotides for use in DNA synthesis. This catalysis involves generating and storing a tyrosyl radical, which is essential for ribonucleotide reduction. The crystal structure consists of a core of four helices in a closed bundle with a left-handed twist and one crossover connection, and a bimetal-ion centre in the middle of the bundle [1].

This entry represents a family of proteins that are structurally related to the R2 protein of class I ribonucleotide reductase, which includes the alpha and beta subunits of methane monooxygenase hydrolase, and delta 9-stearoyl-acyl carrier protein desaturase [2].

Structural links Help

PDB - click here

SCOP: a.25.1.2

CATH: 1.10.620.20

Database links Help

Enzyme: EC:1

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR012348

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P09938 Ribonucleoside-diphosphate reductase small chain 1

P11157 Ribonucleoside-diphosphate reductase subunit M2

P31350 Ribonucleoside-diphosphate reductase subunit M2

P42170 Ribonucleoside-diphosphate reductase small chain

P48592 Ribonucleoside-diphosphate reductase subunit M2

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR009078	Ferritin/ribonucleotide reductase-like
IPR000358	Ribonucleotide reductase
IPR012348	Ribonucleotide reductase-related
	SWISS-MODEL
	PDB Chain
	ModBase
	CATH Domain
	SCOP Domain

Publications Open in usermanual
1.	Kauppi B, Nielsen BB, Ramaswamy S, Larsen IK, Thelander M, Thelander L, Eklund H. The three-dimensional structure of mammalian ribonucleotide reductase protein R2 reveals a more-accessible iron-radical site than Escherichia coli R2. J. Mol. Biol. 262 706-20 1996 [PubMed: 8876648] http://dx.doi.org/10.1006/jmbi.1996.0546
2.	Nordlund P, Eklund H. Di-iron-carboxylate proteins. Curr. Opin. Struct. Biol. 5 758-66 1995 [PubMed: 8749363] http://dx.doi.org/10.1016/0959-440X(95)80008-5

Additional Reading Open in usermanual
	Sazinsky MH, Lippard SJ. Product bound structures of the soluble methane monooxygenase hydroxylase from Methylococcus capsulatus (Bath): protein motion in the alpha-subunit. J. Am. Chem. Soc. 127 2005 5814-25 [PubMed: 15839679] http://dx.doi.org/10.1021/ja044099b
	Murray LJ, Garcia-Serres R, McCormick MS, Davydov R, Naik SG, Kim SH, Hoffman BM, Huynh BH, Lippard SJ. Dioxygen activation at non-heme diiron centers: oxidation of a proximal residue in the I100W variant of toluene/o-xylene monooxygenase hydroxylase. Biochemistry 46 2007 14795-809 [PubMed: 18044971] http://dx.doi.org/10.1021/bi7017128
	Guy JE, Abreu IA, Moche M, Lindqvist Y, Whittle E, Shanklin J. A single mutation in the castor Delta9-18:0-desaturase changes reaction partitioning from desaturation to oxidase chemistry. Proc. Natl. Acad. Sci. U.S.A. 103 2006 17220-4 [PubMed: 17088542] http://dx.doi.org/10.1073/pnas.0607165103
	McCormick MS, Sazinsky MH, Condon KL, Lippard SJ. X-ray crystal structures of manganese(II)-reconstituted and native toluene/o-xylene monooxygenase hydroxylase reveal rotamer shifts in conserved residues and an enhanced view of the protein interior. J. Am. Chem. Soc. 128 2006 15108-10 [PubMed: 17117860] http://dx.doi.org/10.1021/ja064837r
	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