Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P50651

- RIR2A_ARATH

UniProt

P50651 - RIR2A_ARATH

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Ribonucleoside-diphosphate reductase small chain A

Gene

RNR2A

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.2 Publications

Catalytic activityi

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

Cofactori

Fe cation1 PublicationNote: Binds 2 iron ions per subunit.1 Publication

Enzyme regulationi

Inhibited by phenol, paracetamol, 2,4,6-trimethylphenol, resveratrol, furfuryl mercaptan, 2-thiophenthiol, phenylhydrazine, and hydroxyurea.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi87 – 871Iron 1PROSITE-ProRule annotation
Metal bindingi118 – 1181Iron 1PROSITE-ProRule annotation
Metal bindingi118 – 1181Iron 2By similarity
Metal bindingi121 – 1211Iron 1PROSITE-ProRule annotation
Active sitei125 – 1251PROSITE-ProRule annotation
Metal bindingi180 – 1801Iron 2By similarity
Metal bindingi214 – 2141Iron 2By similarity
Metal bindingi217 – 2171Iron 2By similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor Source: TAIR

GO - Biological processi

  1. deoxyribonucleoside diphosphate metabolic process Source: InterPro
  2. DNA repair Source: TAIR
  3. DNA replication Source: UniProtKB-UniPathway
  4. multicellular organismal development Source: TAIR
  5. regulation of cell cycle Source: TAIR
  6. ribonucleotide metabolic process Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

DNA replication

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

BioCyciARA:AT3G23580-MONOMER.
MetaCyc:AT3G23580-MONOMER.
ReactomeiREACT_190968. G1/S-Specific Transcription.
REACT_237242. Synthesis and interconversion of nucleotide di- and triphosphates.
REACT_249737. E2F mediated regulation of DNA replication.
UniPathwayiUPA00326.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:RNR2A
Synonyms:RNR2
Ordered Locus Names:At3g23580
ORF Names:MDB19.6
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 3

Organism-specific databases

TAIRiAT3G23580.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytosol Source: TAIR
  2. ribonucleoside-diphosphate reductase complex Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

No visible phenotype, due to the redundancy with RNR2B and TSO2. Rnr2a and rnr2b double mutants have no visible phenotype.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 341341Ribonucleoside-diphosphate reductase small chain APRO_0000190466Add
BLAST

Proteomic databases

PaxDbiP50651.
PRIDEiP50651.

Expressioni

Tissue specificityi

Expressed in rosette leaves, cauline leaves, stems and flowers.2 Publications

Developmental stagei

Accumulated during S phase of the cell cycle.1 Publication

Gene expression databases

GenevestigatoriP50651.

Interactioni

Subunit structurei

Homodimer and heterodimer with TSO2. 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. Interacts with CSN7.2 Publications

Protein-protein interaction databases

BioGridi7269. 1 interaction.
STRINGi3702.AT3G23580.1-P.

Structurei

3D structure databases

ProteinModelPortaliP50651.
SMRiP50651. Positions 18-299.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0208.
HOGENOMiHOG000255975.
InParanoidiP50651.
KOiK10808.
OMAiDWAINWI.
PhylomeDBiP50651.

Family and domain databases

Gene3Di1.10.620.20. 1 hit.
InterProiIPR009078. Ferritin-like_SF.
IPR012348. RNR-rel.
IPR000358. RNR_small.
[Graphical view]
PANTHERiPTHR23409. PTHR23409. 1 hit.
PfamiPF00268. Ribonuc_red_sm. 1 hit.
[Graphical view]
SUPFAMiSSF47240. SSF47240. 1 hit.
PROSITEiPS00368. RIBORED_SMALL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P50651-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGSLKEGQGR DMEEGESEEP LLMAQNQRFT MFPIRYKSIW EMYKKAEASF
60 70 80 90 100
WTAEEVDLST DVQQWEALTD SEKHFISHIL AFFAASDGIV LENLAARFLN
110 120 130 140 150
DVQVPEARAF YGFQIAMENI HSEMYSLLLE TFIKDSKEKD RLFNAIETIP
160 170 180 190 200
CISKKAKWCL DWIQSPMSFA VRLVAFACVE GIFFSGSFCA IFWLKKRGLM
210 220 230 240 250
PGLTFSNELI SRDEGLHCDF ACLLYSLLQK QLPLEKVYQI VHEAVEIETE
260 270 280 290 300
FVCKALPCDL IGMNSNLMSQ YIQFVADRLL VTLGCERTYK AENPFDWMEF
310 320 330 340
ISLQGKTNFF EKRVGEYQKA SVMSNLQNGN QNYEFTTEED F
Length:341
Mass (Da):39,370
Last modified:January 10, 2003 - v2
Checksum:i3214A88AE7B7776A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti95 – 951Missing in CAA54549. (PubMed:7821432)Curated
Sequence conflicti179 – 1791V → A in CAA54549. (PubMed:7821432)Curated
Sequence conflicti225 – 2251Y → I in CAA54549. (PubMed:7821432)Curated
Sequence conflicti230 – 2323KQL → LHV in CAA54549. (PubMed:7821432)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS68538.
RefSeqiNP_189000.1. NM_113261.3.
UniGeneiAt.8049.

Genome annotation databases

EnsemblPlantsiAT3G23580.1; AT3G23580.1; AT3G23580.
GeneIDi821937.
KEGGiath:AT3G23580.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
PIRi S68538.
RefSeqi NP_189000.1. NM_113261.3.
UniGenei At.8049.

3D structure databases

ProteinModelPortali P50651.
SMRi P50651. Positions 18-299.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 7269. 1 interaction.
STRINGi 3702.AT3G23580.1-P.

Proteomic databases

PaxDbi P50651.
PRIDEi P50651.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT3G23580.1 ; AT3G23580.1 ; AT3G23580 .
GeneIDi 821937.
KEGGi ath:AT3G23580.

Organism-specific databases

GeneFarmi 2083. 386.
TAIRi AT3G23580.

Phylogenomic databases

eggNOGi COG0208.
HOGENOMi HOG000255975.
InParanoidi P50651.
KOi K10808.
OMAi DWAINWI.
PhylomeDBi P50651.

Enzyme and pathway databases

UniPathwayi UPA00326 .
BioCyci ARA:AT3G23580-MONOMER.
MetaCyc:AT3G23580-MONOMER.
Reactomei REACT_190968. G1/S-Specific Transcription.
REACT_237242. Synthesis and interconversion of nucleotide di- and triphosphates.
REACT_249737. E2F mediated regulation of DNA replication.

Gene expression databases

Genevestigatori P50651.

Family and domain databases

Gene3Di 1.10.620.20. 1 hit.
InterProi IPR009078. Ferritin-like_SF.
IPR012348. RNR-rel.
IPR000358. RNR_small.
[Graphical view ]
PANTHERi PTHR23409. PTHR23409. 1 hit.
Pfami PF00268. Ribonuc_red_sm. 1 hit.
[Graphical view ]
SUPFAMi SSF47240. SSF47240. 1 hit.
PROSITEi PS00368. RIBORED_SMALL. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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, DISRUPTION PHENOTYPE.
  8. "COP9 signalosome subunit 7 from Arabidopsis interacts with and regulates the small subunit of ribonucleotide reductase (RNR2)."
    Halimi Y., Dessau M., Pollak S., Ast T., Erez T., Livnat-Levanon N., Karniol B., Hirsch J.A., Chamovitz D.A.
    Plant Mol. Biol. 77:77-89(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CSN7, SUBUNIT, TISSUE SPECIFICITY.

Entry informationi

Entry nameiRIR2A_ARATH
AccessioniPrimary (citable) accession number: P50651
Secondary accession number(s): Q9LUH0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 10, 2003
Last modified: November 26, 2014
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3