Ribonucleoside-diphosphate reductase small chain A - Arabidopsis thaliana (Mouse-ear cress)

Contribute

Send feedback

Read comments (?) or add your own

P50651 (RIR2A_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 111. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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 names

Name:	RNR2A
Synonyms:	RNR2
Ordered Locus Names:	At3g23580
ORF Names:	MDB19.6

Organism

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

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	341 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	DNA replication
Cellular component	Cytoplasm
Ligand	Iron Metal-binding
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA repair Traceable author statement Ref.7. Source: TAIR DNA replication Inferred from electronic annotation. Source: UniProtKB-UniPathway deoxyribonucleoside diphosphate metabolic process Inferred from electronic annotation. Source: InterPro multicellular organismal development Inferred from mutant phenotype Ref.7. Source: TAIR regulation of cell cycle Inferred from mutant phenotype Ref.7. Source: TAIR ribonucleotide metabolic process Traceable author statement PubMed 10542051. Source: TAIR
Cellular_component	cytosol Inferred from direct assay PubMed 21166475. Source: TAIR ribonucleoside-diphosphate reductase complex Inferred from sequence or structural similarity PubMed 10542051. Source: TAIR
Molecular_function	ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor Inferred from direct assay PubMed 10542051. Source: TAIR transition metal ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 341

341

Ribonucleoside-diphosphate reductase small chain A

PRO_0000190466

Sites

Active site

125

By similarity

Metal binding

Iron 1 By similarity

Metal binding

118

Iron 1 By similarity

Metal binding

118

Iron 2 By similarity

Metal binding

121

Iron 1 By similarity

Metal binding

180

Iron 2 By similarity

Metal binding

214

Iron 2 By similarity

Metal binding

217

Iron 2 By similarity

Experimental info

Sequence conflict

Missing in CAA54549. Ref.1

Sequence conflict

179

V → A in CAA54549. Ref.1

Sequence conflict

225

Y → I in CAA54549. Ref.1

Sequence conflict

230 – 232

KQL → LHV in CAA54549. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P50651 [UniParc].

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

FASTA

341

39,370

        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' referencesShow '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. 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.
IPI	IPI00532435.
PIR	S68538.
RefSeq	NP_189000.1. NM_113261.3.
UniGene	At.8049.
3D structure databases
ProteinModelPortal	P50651.
SMR	P50651. Positions 18-299.
ModBase	Search...
Protein-protein interaction databases
STRING	3702.AT3G23580.1-P.
Proteomic databases
PaxDb	P50651.
PRIDE	P50651.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT3G23580.1; AT3G23580.1; AT3G23580.
GeneID	821937.
KEGG	ath:AT3G23580.
Organism-specific databases
GeneFarm	2083. 386.
TAIR	At3g23580.
Phylogenomic databases
eggNOG	COG0208.
HOGENOM	HOG000255975.
InParanoid	P50651.
KO	K10808.
OMA	ELEIEWA.
PhylomeDB	P50651.
ProtClustDB	PLN02492.
Enzyme and pathway databases
UniPathway	UPA00326.
Gene expression databases
Genevestigator	P50651.
GermOnline	AT3G23580. Arabidopsis thaliana.
Family and domain databases
Gene3D	1.10.620.20. 1 hit.
InterPro	IPR009078. Ferritin-like_SF. IPR012348. RNR-rel. IPR000358. RNR_small. [Graphical view]
PANTHER	PTHR23409. PTHR23409. 1 hit.
Pfam	PF00268. Ribonuc_red_sm. 1 hit. [Graphical view]
SUPFAM	SSF47240. Ferritin/RR_like. 1 hit.
PROSITE	PS00368. RIBORED_SMALL. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

RIR2A_ARATH

Accession

Primary (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:	May 1, 2013
This is version 111 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents