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P50651 (RIR2A_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ribonucleoside-diphosphate reductase small chain A

EC=1.17.4.1
Alternative name(s):
Ribonucleoside-diphosphate reductase R2A subunit
Short name=AtRNR2
Short name=Protein R2at
Ribonucleotide reductase small subunit A
Gene names
Name:RNR2A
Synonyms:RNR2
Ordered Locus Names:At3g23580
ORF Names:MDB19.6
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length341 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. Ref.5 Ref.7

Catalytic activity

2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin.

Cofactor

Binds 2 iron ions per subunit. Ref.5

Enzyme regulation

Inhibited by phenol, paracetamol, 2,4,6-trimethylphenol, resveratrol, furfuryl mercaptan, 2-thiophenthiol, phenylhydrazine, and hydroxyurea. Ref.6

Pathway

Genetic information processing; DNA replication.

Subunit structure

Heterotetramer of two R1 and two R2 chains. A radical transfer pathway may occur between Tyr-125 of protein R2 and R1. Homodimer contains a dinuclear non-heme iron center and a stable tyrosyl radical essential for activity. A transfer pathway may occur between Tyr-125 of protein R2 and R1. Ref.5

Subcellular location

Cytoplasm By similarity.

Tissue specificity

Expressed in rosette leaves, cauline leaves, stems and flowers. Ref.7

Developmental stage

Accumulated during S phase of the cell cycle. Ref.1

Miscellaneous

A substrate-binding catalytic site, located on R1, is formed only in the presence of the second subunit R2.

Sequence similarities

Belongs to the ribonucleoside diphosphate reductase small chain family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 341341Ribonucleoside-diphosphate reductase small chain A
PRO_0000190466

Sites

Active site1251 By similarity
Metal binding871Iron 1 By similarity
Metal binding1181Iron 1 By similarity
Metal binding1181Iron 2 By similarity
Metal binding1211Iron 1 By similarity
Metal binding1801Iron 2 By similarity
Metal binding2141Iron 2 By similarity
Metal binding2171Iron 2 By similarity

Experimental info

Sequence conflict951Missing in CAA54549. Ref.1
Sequence conflict1791V → A in CAA54549. Ref.1
Sequence conflict2251Y → I in CAA54549. Ref.1
Sequence conflict230 – 2323KQL → LHV in CAA54549. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P50651 [UniParc].

Last modified January 10, 2003. Version 2.
Checksum: 3214A88AE7B7776A

FASTA34139,370
        10         20         30         40         50         60 
MGSLKEGQGR DMEEGESEEP LLMAQNQRFT MFPIRYKSIW EMYKKAEASF WTAEEVDLST 

        70         80         90        100        110        120 
DVQQWEALTD SEKHFISHIL AFFAASDGIV LENLAARFLN DVQVPEARAF YGFQIAMENI 

       130        140        150        160        170        180 
HSEMYSLLLE TFIKDSKEKD RLFNAIETIP CISKKAKWCL DWIQSPMSFA VRLVAFACVE 

       190        200        210        220        230        240 
GIFFSGSFCA IFWLKKRGLM PGLTFSNELI SRDEGLHCDF ACLLYSLLQK QLPLEKVYQI 

       250        260        270        280        290        300 
VHEAVEIETE FVCKALPCDL IGMNSNLMSQ YIQFVADRLL VTLGCERTYK AENPFDWMEF 

       310        320        330        340 
ISLQGKTNFF EKRVGEYQKA SVMSNLQNGN QNYEFTTEED F 

« Hide

References

« Hide 'large scale' references
[1]"Molecular characterization and cell cycle-regulated expression of a cDNA clone from Arabidopsis thaliana homologous to the small subunit of ribonucleotide reductase."
Philipps G., Clement B., Gigot C.
FEBS Lett. 358:67-70(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE.
Strain: cv. Columbia.
[2]"Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence features of the regions of 4,504,864 bp covered by sixty P1 and TAC clones."
Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.
DNA Res. 7:131-135(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[5]"Ribonucleotide reductase from the higher plant Arabidopsis thaliana: expression of the R2 component and characterization of its iron-radical center."
Sauge-Merle S., Laulhere J.-P., Coves J., Le Pape L., Menage S., Fontecave M.
J. Biol. Inorg. Chem. 2:586-594(1997)
Cited for: FUNCTION, COFACTOR, SUBUNIT.
[6]"Reactivity studies of the tyrosyl radical in ribonucleotide reductase from Mycobacterium tuberculosis and Arabidopsis thaliana -- comparison with Escherichia coli and mouse."
Elleingand E., Gerez C., Un S., Knuepling M., Lu G., Salem J., Rubin H., Sauge-Merle S., Laulhere J.-P., Fontecave M.
Eur. J. Biochem. 258:485-490(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION.
[7]"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] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X77336 mRNA. Translation: CAA54549.1.
AB023036 Genomic DNA. Translation: BAB02776.1.
CP002686 Genomic DNA. Translation: AEE76779.1.
AF372971 mRNA. Translation: AAK50108.1.
AY143893 mRNA. Translation: AAN28832.1.
PIRS68538.
RefSeqNP_189000.1. NM_113261.3.
UniGeneAt.8049.

3D structure databases

ProteinModelPortalP50651.
SMRP50651. Positions 18-299.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid7269. 1 interaction.
STRING3702.AT3G23580.1-P.

Proteomic databases

PaxDbP50651.
PRIDEP50651.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT3G23580.1; AT3G23580.1; AT3G23580.
GeneID821937.
KEGGath:AT3G23580.

Organism-specific databases

GeneFarm2083. 386.
TAIRAT3G23580.

Phylogenomic databases

eggNOGCOG0208.
HOGENOMHOG000255975.
InParanoidP50651.
KOK10808.
OMAWIANESK.
PhylomeDBP50651.
ProtClustDBPLN02492.

Enzyme and pathway databases

BioCycARA:AT3G23580-MONOMER.
MetaCyc:AT3G23580-MONOMER.
UniPathwayUPA00326.

Gene expression databases

GenevestigatorP50651.

Family and domain databases

Gene3D1.10.620.20. 1 hit.
InterProIPR009078. Ferritin-like_SF.
IPR012348. RNR-rel.
IPR000358. RNR_small.
[Graphical view]
PANTHERPTHR23409. PTHR23409. 1 hit.
PfamPF00268. Ribonuc_red_sm. 1 hit.
[Graphical view]
SUPFAMSSF47240. SSF47240. 1 hit.
PROSITEPS00368. RIBORED_SMALL. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRIR2A_ARATH
AccessionPrimary (citable) accession number: P50651
Secondary accession number(s): Q9LUH0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 10, 2003
Last modified: February 19, 2014
This is version 119 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names