Reviewed, UniProtKB/Swiss-Prot Q6Y657 (RIR2B_ARATH)

Names and origin

Protein names

Recommended name:
    Putative ribonucleoside-diphosphate reductase small chain B
    EC=1.17.4.1
Alternative name(s):
    Ribonucleotide reductase small subunit B
    Ribonucleoside-diphosphate reductase R2B subunit

Gene names

Name:	RNR2B
Ordered Locus Names:	At5g40942
ORF Names:	MMG1.4

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	333 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Uncertain.

General annotation (Comments)

Function	Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. Ref.1
Catalytic activity	2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin.
Cofactor	Binds 2 iron ions per subunit By similarity.
Pathway	Genetic information processing; DNA replication.
Subunit structure	Heterodimer of a large and a small chain By similarity.
Subcellular location	Cytoplasm By similarity.
Tissue specificity	Expressed in roots, rosette leaves, stems and flowers. Ref.1
Sequence similarities	Belongs to the ribonucleoside diphosphate reductase small chain family.
Caution	Could be the product of a pseudogene in cv. Columbia. The N-terminus is shortened due to a frameshift in position 140. The resulting sequence lacks the conserved features of the family.
Sequence caution	The sequence AAO42187.1 differs from that shown. Reason: Frameshift at position 140. The sequence AB023040 differs from that shown. Reason: Frameshift at position 140.

Ontologies

Keywords
Biological process	DNA replication
Cellular component	Cytoplasm
Ligand	Iron Metal-binding
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	DNA replication Inferred from electronic annotation. Source: UniProtKB-KW deoxyribonucleoside diphosphate metabolic process Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW ribonucleoside-diphosphate reductase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 333	333	Putative ribonucleoside-diphosphate reductase small chain B		PRO_0000254194
Sites
	Active site	114	1	By similarity
	Metal binding	76	1	Iron 1 By similarity
	Metal binding	107	1	Iron 1 By similarity
	Metal binding	107	1	Iron 2 By similarity
	Metal binding	110	1	Iron 1 By similarity
	Metal binding	169	1	Iron 2 By similarity
	Metal binding	203	1	Iron 2 By similarity
	Metal binding	206	1	Iron 2 By similarity
Experimental info
	Sequence conflict	221	1	L → F Ref.2
	Sequence conflict	221	1	L → F in AAO42187. Ref.3
	Sequence conflict	246	1	P → S Ref.2
	Sequence conflict	246	1	P → S in AAO42187. Ref.3
	Sequence conflict	275	1	A → G Ref.2
	Sequence conflict	275	1	A → G in AAO42187. Ref.3
	Sequence conflict	281	1	S → T Ref.2
	Sequence conflict	281	1	S → T in AAO42187. Ref.3
	Sequence conflict	311	1	I → V Ref.2
	Sequence conflict	311	1	I → V in AAO42187. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q6Y657-1 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: CA20B044F92DB922	FASTA	333	38,331
	10 20 30 40 50 60 MPSMPEEPIL TPTPDRFCMF PIQYPQIWEM YKKAEASFWT AEEVDLSQDN RDWENSLTND 70 80 90 100 110 120 ERHFIKHVLA FFAASDGIVL ENLSTRFMSD VQISEARAFY GFQIAIENIH SEMYSLLLDT 130 140 150 160 170 180 YIKDNKERDH LFRAIETIPC VTKKAEWAMK WINGSQSFAE RIVAFACVEG IFFSGSFCSI 190 200 210 220 230 240 FWLKKRGLMP GLTFSNELIS RDEGLHCDFA CLIYSLLRTK LDEDRLKAIV CDAVEIEREF 250 260 270 280 290 300 VCDALPCALV GMNRELMSQY IEFVADRLLA ALGCAKVYGV SNPFDWMELI SLQGKTNFFE 310 320 330 KRVGEYQKAS IMSSVHGNAA FNDDHVFKLD EDF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Arabidopsis ribonucleotide reductases are critical for cell cycle progression, DNA damage repair, and plant development." Wang C., Liu Z. Plant Cell 18:350-365(2006) [PubMed: 16399800] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, FUNCTION. Strain: cv. Landsberg erecta.
[2]	"Structural analysis of Arabidopsis thaliana chromosome 5. XI." Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H., Tabata S. Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AY178109 mRNA. Translation: AAO62422.1. AB023040 Genomic DNA. No translation available. BT004167 mRNA. Translation: AAO42187.1. Frameshift.
IPI	IPI00544341.
3D structure databases
HSSP	HSSP built from PDB template 1JK0 based on UniProtKB P49723.
ModBase	Search...
Protein-protein interaction databases
STRING	Q6Y657.
Organism-specific databases
GeneFarm	2199. 386.
TAIR	At5g40942.
Enzyme and pathway databases
BRENDA	1.17.4.1. 302. 1.17.4.2. 302.
Gene expression databases
Genevestigator	Q6Y657.
Family and domain databases
InterPro	IPR012348. Ribncl_red_rel. IPR000358. Ribonucl_redctse. [Graphical view]
Gene3D	G3DSA:1.10.620.20. Ribncl_red_rel. 1 hit.
PANTHER	PTHR23409. Ribonucl_redctse. 1 hit.
Pfam	PF00268. Ribonuc_red_sm. 1 hit. [Graphical view]
PROSITE	PS00368. RIBORED_SMALL. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

RIR2B_ARATH

Accession

Primary (citable) accession number: Q6Y657
Secondary accession number(s): Q84W71

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2006
Last sequence update:	July 5, 2004
Last modified:	October 13, 2009
This is version 35 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)