RI2BL_ARATH
ID RI2BL_ARATH Reviewed; 333 AA.
AC P0DKH3; Q6Y657; Q84W71;
DT 01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2014, sequence version 1.
DT 03-AUG-2022, entry version 23.
DE RecName: Full=Ribonucleoside-diphosphate reductase small chain B;
DE EC=1.17.4.1;
DE AltName: Full=Ribonucleoside-diphosphate reductase R2B subunit;
DE AltName: Full=Ribonucleotide reductase small subunit B;
GN Name=RNR2B;
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], TISSUE SPECIFICITY, FUNCTION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=cv. Landsberg erecta, and cv. Wassilewskija;
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).
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 -!- 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:0000250};
CC Note=Binds 2 iron ions per subunit. {ECO:0000250};
CC -!- PATHWAY: Genetic information processing; DNA replication.
CC -!- SUBUNIT: Heterodimer of a large and a small chain. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, rosette leaves, stems and
CC flowers. {ECO:0000269|PubMed:16399800}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype, due to the redundancy with
CC RNR2A and TSO2. Rnr2a and rnr2b double mutants have no visible
CC phenotype. {ECO:0000269|PubMed:16399800}.
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase small
CC chain family. {ECO:0000305}.
CC -!- CAUTION: In cv. Columbia, could be the product of a pseudogene (AC
CC P0DKH2) due to a frameshift in position 140. The resulting shorter
CC protein lacks the conserved features of the 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; AY178109; AAO62422.1; -; mRNA.
DR AlphaFoldDB; P0DKH3; -.
DR SMR; P0DKH3; -.
DR UniPathway; UPA00326; -.
DR ExpressionAtlas; P0DKH3; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IEA:UniProtKB-EC.
DR GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniPathway.
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 SUPFAM; SSF47240; SSF47240; 1.
DR PROSITE; PS00368; RIBORED_SMALL; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Deoxyribonucleotide synthesis; Iron; Metal-binding;
KW Oxidoreductase.
FT CHAIN 1..333
FT /note="Ribonucleoside-diphosphate reductase small chain B"
FT /id="PRO_0000430464"
FT ACT_SITE 114
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10014"
FT BINDING 76
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10014"
FT BINDING 107
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10014"
FT BINDING 107
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 110
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10014"
FT BINDING 169
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 203
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 206
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 333 AA; 38331 MW; CA20B044F92DB922 CRC64;
MPSMPEEPIL TPTPDRFCMF PIQYPQIWEM YKKAEASFWT AEEVDLSQDN RDWENSLTND
ERHFIKHVLA FFAASDGIVL ENLSTRFMSD VQISEARAFY GFQIAIENIH SEMYSLLLDT
YIKDNKERDH LFRAIETIPC VTKKAEWAMK WINGSQSFAE RIVAFACVEG IFFSGSFCSI
FWLKKRGLMP GLTFSNELIS RDEGLHCDFA CLIYSLLRTK LDEDRLKAIV CDAVEIEREF
VCDALPCALV GMNRELMSQY IEFVADRLLA ALGCAKVYGV SNPFDWMELI SLQGKTNFFE
KRVGEYQKAS IMSSVHGNAA FNDDHVFKLD EDF
