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InterPro: IPR013344 Ribonucleoside-diphosphate reductase, adenosylcobalamin-dependent

Protein matches Help

UniProtKB

Matches:

618 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

IPR013344 RDP_Rdtase_AdoCbl-dep

Type

Domain

Signatures Help

Database	ID	Name	Proteins
TIGRFAMs	TIGR02504	NrdJ_Z	618
Signatures in BioMart

InterPro Relationships Help

Parent

IPR000788 Ribonucleotide reductase large subunit, C-terminal

Contains

IPR013509 Ribonucleotide reductase large subunit, N-terminal
IPR015146 Ribonucleotide reductase, stirrup
IPR015147 PI-PfuI intein endonuclease, subdomain

GO Term annotation Help

Process

GO:0055114 oxidation reduction

Function

GO:0000166 nucleotide binding
GO:0004748 ribonucleoside-diphosphate reductase activity
GO:0016960 class II ribonucleotide reductase activity
GO:0031419 cobalamin binding

InterPro annotation

Entry Details in BioMart

Abstract

This entry represents a group of adenosylcobalamin (AdoCbl or coenzymeB12)-dependent ribonucleotide reductases (Class II RNRs) related to the characterised species from Pyrococcus [1], Thermoplasma [2], Corynebacterium [3] and Deinococcus [4]. 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. This model identifies genes in a wide range of deeply branching bacteria. All are structurally related to the class I (non-haem iron-dependent) RNRs. In most species this gene is known as NrdJ, while in mycobacteria it is called NrdZ.

Structural links Help

PDB - click here

SCOP: b.86.1.2 , d.50.3.1 , d.95.2.2

CATH: 2.170.16.10 , 3.10.28.10 , 3.30.160.90

Database links Help

Enzyme: EC:1.17.4.1

CluSTr: ALLvsALL:65588:84

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR013344

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O54196 Vitamin B12-dependent ribonucleotide reductase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR000788	Ribonucleotide reductase large subunit, C-terminal
IPR013678	Ribonucleotide reductase class II vitamin B12-dependent
IPR013344	Ribonucleoside-diphosphate reductase, adenosylcobalamin-dependent
	SWISS-MODEL
	ModBase

Publications Open in usermanual
1.	Riera J, Robb FT, Weiss R, Fontecave M. Ribonucleotide reductase in the archaeon Pyrococcus furiosus: a critical enzyme in the evolution of DNA genomes? Proc. Natl. Acad. Sci. U.S.A. 94 475-8 1997 [PubMed: 9012808] http://dx.doi.org/10.1073/pnas.94.2.475
2.	Tauer A, Benner SA. The B12-dependent ribonucleotide reductase from the archaebacterium Thermoplasma acidophila: an evolutionary solution to the ribonucleotide reductase conundrum. Proc. Natl. Acad. Sci. U.S.A. 94 53-8 1997 [PubMed: 8990160] http://dx.doi.org/10.1073/pnas.94.1.53
3.	Tsai PK, Hogenkamp HP. The purification and characterization of an adenosylcobalamin-dependent ribonucleoside diphosphate reductase from Corynebacterium nephridii. J. Biol. Chem. 255 1273-8 1980 [PubMed: 6986368] http://intl.jbc.org/cgi/content/abstract/255/4/1273
4.	Jordan A, Torrents E, Jeanthon C, Eliasson R, Hellman U, Wernstedt C, Barbe J, Gibert I, Reichard P. B12-dependent ribonucleotide reductases from deeply rooted eubacteria are structurally related to the aerobic enzyme from Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 94 13487-92 1997 [PubMed: 9391052] http://dx.doi.org/10.1073/pnas.94.25.13487

Additional Reading Open in usermanual
	Ichiyanagi K, Ishino Y, Ariyoshi M, Komori K, Morikawa K. Crystal structure of an archaeal intein-encoded homing endonuclease PI-PfuI. J. Mol. Biol. 300 2000 889-901 [PubMed: 10891276] http://dx.doi.org/10.1006/jmbi.2000.3873

InterPro 23.1