RIR2A_ARATH
ID RIR2A_ARATH Reviewed; 341 AA.
AC P50651; Q9LUH0;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2003, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Ribonucleoside-diphosphate reductase small chain A;
DE EC=1.17.4.1;
DE AltName: Full=Ribonucleoside-diphosphate reductase R2A subunit;
DE Short=AtRNR2;
DE Short=Protein R2at;
DE AltName: Full=Ribonucleotide reductase small subunit A;
GN Name=RNR2A; Synonyms=RNR2; OrderedLocusNames=At3g23580; ORFNames=MDB19.6;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=7821432; DOI=10.1016/0014-5793(94)01397-j;
RA Philipps G., Clement B., Gigot C.;
RT "Molecular characterization and cell cycle-regulated expression of a cDNA
RT clone from Arabidopsis thaliana homologous to the small subunit of
RT ribonucleotide reductase.";
RL FEBS Lett. 358:67-70(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP FUNCTION, COFACTOR, AND SUBUNIT.
RX DOI=10.1007/s007750050173;
RA Sauge-Merle S., Laulhere J.-P., Coves J., Le Pape L., Menage S.,
RA Fontecave M.;
RT "Ribonucleotide reductase from the higher plant Arabidopsis thaliana:
RT expression of the R2 component and characterization of its iron-radical
RT center.";
RL J. Biol. Inorg. Chem. 2:586-594(1997).
RN [6]
RP ACTIVITY REGULATION.
RX PubMed=9874215; DOI=10.1046/j.1432-1327.1998.2580485.x;
RA Elleingand E., Gerez C., Un S., Knuepling M., Lu G., Salem J., Rubin H.,
RA Sauge-Merle S., Laulhere J.-P., Fontecave M.;
RT "Reactivity studies of the tyrosyl radical in ribonucleotide reductase from
RT Mycobacterium tuberculosis and Arabidopsis thaliana -- comparison with
RT Escherichia coli and mouse.";
RL Eur. J. Biochem. 258:485-490(1998).
RN [7]
RP TISSUE SPECIFICITY, FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16399800; DOI=10.1105/tpc.105.037044;
RA Wang C., Liu Z.;
RT "Arabidopsis ribonucleotide reductases are critical for cell cycle
RT progression, DNA damage repair, and plant development.";
RL Plant Cell 18:350-365(2006).
RN [8]
RP INTERACTION WITH CSN7, SUBUNIT, AND TISSUE SPECIFICITY.
RX PubMed=21614643; DOI=10.1007/s11103-011-9795-8;
RA Halimi Y., Dessau M., Pollak S., Ast T., Erez T., Livnat-Levanon N.,
RA Karniol B., Hirsch J.A., Chamovitz D.A.;
RT "COP9 signalosome subunit 7 from Arabidopsis interacts with and regulates
RT the small subunit of ribonucleotide reductase (RNR2).";
RL Plant Mol. Biol. 77:77-89(2011).
CC -!- FUNCTION: Provides the precursors necessary for DNA synthesis.
CC Catalyzes the biosynthesis of deoxyribonucleotides from the
CC corresponding ribonucleotides. {ECO:0000269|PubMed:16399800,
CC ECO:0000269|Ref.5}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-
CC diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-
CC diphosphate; Xref=Rhea:RHEA:23252, Rhea:RHEA-COMP:10698, Rhea:RHEA-
CC COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:73316; EC=1.17.4.1;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10014};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000269|Ref.5};
CC Note=Binds 2 iron ions per subunit. {ECO:0000269|Ref.5};
CC -!- ACTIVITY REGULATION: Inhibited by phenol, paracetamol, 2,4,6-
CC trimethylphenol, resveratrol, furfuryl mercaptan, 2-thiophenthiol,
CC phenylhydrazine, and hydroxyurea. {ECO:0000269|PubMed:9874215}.
CC -!- PATHWAY: Genetic information processing; DNA replication.
CC -!- SUBUNIT: Homodimer and heterodimer with TSO2. Heterotetramer of two R1
CC and two R2 chains. A radical transfer pathway may occur between Tyr-125
CC of protein R2 and R1. Homodimer contains a dinuclear non-heme iron
CC center and a stable tyrosyl radical essential for activity. A transfer
CC pathway may occur between Tyr-125 of protein R2 and R1. Interacts with
CC CSN7. {ECO:0000269|PubMed:21614643, ECO:0000269|Ref.5}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in rosette leaves, cauline leaves, stems
CC and flowers. {ECO:0000269|PubMed:16399800,
CC ECO:0000269|PubMed:21614643}.
CC -!- DEVELOPMENTAL STAGE: Accumulated during S phase of the cell cycle.
CC {ECO:0000269|PubMed:7821432}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype, due to the redundancy with
CC RNR2B and TSO2. Rnr2a and rnr2b double mutants have no visible
CC phenotype. {ECO:0000269|PubMed:16399800}.
CC -!- MISCELLANEOUS: A substrate-binding catalytic site, located on R1, is
CC formed only in the presence of the second subunit R2.
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase small
CC chain family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X77336; CAA54549.1; -; mRNA.
DR EMBL; AB023036; BAB02776.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76779.1; -; Genomic_DNA.
DR EMBL; AF372971; AAK50108.1; -; mRNA.
DR EMBL; AY143893; AAN28832.1; -; mRNA.
DR PIR; S68538; S68538.
DR RefSeq; NP_189000.1; NM_113261.4.
DR AlphaFoldDB; P50651; -.
DR SMR; P50651; -.
DR BioGRID; 7269; 1.
DR STRING; 3702.AT3G23580.1; -.
DR PaxDb; P50651; -.
DR PRIDE; P50651; -.
DR ProteomicsDB; 236265; -.
DR EnsemblPlants; AT3G23580.1; AT3G23580.1; AT3G23580.
DR GeneID; 821937; -.
DR Gramene; AT3G23580.1; AT3G23580.1; AT3G23580.
DR KEGG; ath:AT3G23580; -.
DR Araport; AT3G23580; -.
DR TAIR; locus:2088040; AT3G23580.
DR eggNOG; KOG1567; Eukaryota.
DR HOGENOM; CLU_035339_2_1_1; -.
DR InParanoid; P50651; -.
DR OMA; PQLWEMY; -.
DR OrthoDB; 680824at2759; -.
DR PhylomeDB; P50651; -.
DR BioCyc; ARA:AT3G23580-MON; -.
DR BioCyc; MetaCyc:AT3G23580-MON; -.
DR BRENDA; 1.17.4.1; 399.
DR BRENDA; 1.17.4.2; 399.
DR UniPathway; UPA00326; -.
DR PRO; PR:P50651; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; P50651; baseline and differential.
DR Genevisible; P50651; AT.
DR GO; GO:0005971; C:ribonucleoside-diphosphate reductase complex; ISS:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IDA:TAIR.
DR GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; TAS:TAIR.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniPathway.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:TAIR.
DR GO; GO:0009259; P:ribonucleotide metabolic process; TAS:TAIR.
DR CDD; cd01049; RNRR2; 1.
DR Gene3D; 1.10.620.20; -; 1.
DR InterPro; IPR009078; Ferritin-like_SF.
DR InterPro; IPR012348; RNR-like.
DR InterPro; IPR033909; RNR_small.
DR InterPro; IPR030475; RNR_small_AS.
DR InterPro; IPR000358; RNR_small_fam.
DR PANTHER; PTHR23409; PTHR23409; 1.
DR Pfam; PF00268; Ribonuc_red_sm; 1.
DR PIRSF; PIRSF000355; NrdB; 1.
DR SUPFAM; SSF47240; SSF47240; 1.
DR PROSITE; PS00368; RIBORED_SMALL; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Deoxyribonucleotide synthesis; Iron; Metal-binding;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..341
FT /note="Ribonucleoside-diphosphate reductase small chain A"
FT /id="PRO_0000190466"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 125
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10014"
FT BINDING 87
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10014"
FT BINDING 118
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10014"
FT BINDING 118
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 121
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10014"
FT BINDING 180
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 214
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 217
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT CONFLICT 95
FT /note="Missing (in Ref. 1; CAA54549)"
FT /evidence="ECO:0000305"
FT CONFLICT 179
FT /note="V -> A (in Ref. 1; CAA54549)"
FT /evidence="ECO:0000305"
FT CONFLICT 225
FT /note="Y -> I (in Ref. 1; CAA54549)"
FT /evidence="ECO:0000305"
FT CONFLICT 230..232
FT /note="KQL -> LHV (in Ref. 1; CAA54549)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 341 AA; 39370 MW; 3214A88AE7B7776A CRC64;
MGSLKEGQGR DMEEGESEEP LLMAQNQRFT MFPIRYKSIW EMYKKAEASF WTAEEVDLST
DVQQWEALTD SEKHFISHIL AFFAASDGIV LENLAARFLN DVQVPEARAF YGFQIAMENI
HSEMYSLLLE TFIKDSKEKD RLFNAIETIP CISKKAKWCL DWIQSPMSFA VRLVAFACVE
GIFFSGSFCA IFWLKKRGLM PGLTFSNELI SRDEGLHCDF ACLLYSLLQK QLPLEKVYQI
VHEAVEIETE FVCKALPCDL IGMNSNLMSQ YIQFVADRLL VTLGCERTYK AENPFDWMEF
ISLQGKTNFF EKRVGEYQKA SVMSNLQNGN QNYEFTTEED F
