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Protein

Ribonucleoside-diphosphate reductase small chain A

Gene

RNR2A

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: 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: DNA replication

This protein is involved in the pathway DNA replication, which is part of Genetic information processing.
View all proteins of this organism that are known to be involved in the pathway DNA replication and in Genetic information processing.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi87Iron 1PROSITE-ProRule annotation1
Metal bindingi118Iron 1PROSITE-ProRule annotation1
Metal bindingi118Iron 2By similarity1
Metal bindingi121Iron 1PROSITE-ProRule annotation1
Active sitei125PROSITE-ProRule annotation1
Metal bindingi180Iron 2By similarity1
Metal bindingi214Iron 2By similarity1
Metal bindingi217Iron 2By similarity1

GO - Molecular functioni

GO - Biological processi

  • deoxyribonucleotide biosynthetic process Source: GO_Central
  • DNA repair Source: TAIR
  • DNA replication Source: UniProtKB-UniPathway
  • multicellular organism development Source: TAIR
  • regulation of cell cycle Source: TAIR
  • 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.
BRENDAi1.17.4.1. 399.
1.17.4.2. 399.
ReactomeiR-ATH-113510. E2F mediated regulation of DNA replication.
R-ATH-499943. Synthesis and interconversion of nucleotide di- and triphosphates.
R-ATH-69205. G1/S-Specific Transcription.
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
Proteomesi
  • UP000006548 Componenti: Chromosome 3

Organism-specific databases

TAIRiAT3G23580.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: TAIR
  • 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)DescriptionActionsGraphical viewLength
ChainiPRO_00001904661 – 341Ribonucleoside-diphosphate reductase small chain AAdd BLAST341

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

GenevisibleiP50651. AT.

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 interactor.
STRINGi3702.AT3G23580.1.

Structurei

3D structure databases

ProteinModelPortaliP50651.
SMRiP50651.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1567. Eukaryota.
COG0208. LUCA.
HOGENOMiHOG000255975.
InParanoidiP50651.
KOiK10808.
OMAiIRYKSIW.
OrthoDBiEOG09360F7K.
PhylomeDBiP50651.

Family and domain databases

CDDicd01049. RNRR2. 1 hit.
Gene3Di1.10.620.20. 1 hit.
InterProiIPR009078. Ferritin-like_SF.
IPR012348. RNR-rel.
IPR033909. RNR_small.
IPR030475. RNR_small_AS.
IPR000358. RNR_small_fam.
[Graphical view]
PANTHERiPTHR23409. PTHR23409. 1 hit.
PfamiPF00268. Ribonuc_red_sm. 1 hit.
[Graphical view]
PIRSFiPIRSF000355. NrdB. 1 hit.
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)DescriptionActionsGraphical viewLength
Sequence conflicti95Missing in CAA54549 (PubMed:7821432).Curated1
Sequence conflicti179V → A in CAA54549 (PubMed:7821432).Curated1
Sequence conflicti225Y → I in CAA54549 (PubMed:7821432).Curated1
Sequence conflicti230 – 232KQL → LHV in CAA54549 (PubMed:7821432).Curated3

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_113261.4.
UniGeneiAt.8049.

Genome annotation databases

EnsemblPlantsiAT3G23580.1; AT3G23580.1; AT3G23580.
GeneIDi821937.
GrameneiAT3G23580.1; AT3G23580.1; AT3G23580.
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.
PIRiS68538.
RefSeqiNP_189000.1. NM_113261.4.
UniGeneiAt.8049.

3D structure databases

ProteinModelPortaliP50651.
SMRiP50651.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi7269. 1 interactor.
STRINGi3702.AT3G23580.1.

Proteomic databases

PaxDbiP50651.
PRIDEiP50651.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT3G23580.1; AT3G23580.1; AT3G23580.
GeneIDi821937.
GrameneiAT3G23580.1; AT3G23580.1; AT3G23580.
KEGGiath:AT3G23580.

Organism-specific databases

TAIRiAT3G23580.

Phylogenomic databases

eggNOGiKOG1567. Eukaryota.
COG0208. LUCA.
HOGENOMiHOG000255975.
InParanoidiP50651.
KOiK10808.
OMAiIRYKSIW.
OrthoDBiEOG09360F7K.
PhylomeDBiP50651.

Enzyme and pathway databases

UniPathwayiUPA00326.
BioCyciARA:AT3G23580-MONOMER.
MetaCyc:AT3G23580-MONOMER.
BRENDAi1.17.4.1. 399.
1.17.4.2. 399.
ReactomeiR-ATH-113510. E2F mediated regulation of DNA replication.
R-ATH-499943. Synthesis and interconversion of nucleotide di- and triphosphates.
R-ATH-69205. G1/S-Specific Transcription.

Miscellaneous databases

PROiP50651.

Gene expression databases

GenevisibleiP50651. AT.

Family and domain databases

CDDicd01049. RNRR2. 1 hit.
Gene3Di1.10.620.20. 1 hit.
InterProiIPR009078. Ferritin-like_SF.
IPR012348. RNR-rel.
IPR033909. RNR_small.
IPR030475. RNR_small_AS.
IPR000358. RNR_small_fam.
[Graphical view]
PANTHERiPTHR23409. PTHR23409. 1 hit.
PfamiPF00268. Ribonuc_red_sm. 1 hit.
[Graphical view]
PIRSFiPIRSF000355. NrdB. 1 hit.
SUPFAMiSSF47240. SSF47240. 1 hit.
PROSITEiPS00368. RIBORED_SMALL. 1 hit.
[Graphical view]
ProtoNetiSearch...

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 30, 2016
This is version 137 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.