ID   RIR2_TOBAC              Reviewed;         329 AA.
AC   P49730;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Ribonucleoside-diphosphate reductase small chain;
DE            EC=1.17.4.1;
DE   AltName: Full=Ribonucleoside-diphosphate reductase R2 subunit;
DE   AltName: Full=Ribonucleotide reductase small subunit;
OS   Nicotiana tabacum (Common tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4097;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Bright Yellow 2;
RX   PubMed=9862497; DOI=10.1023/a:1006083318906;
RA   Chaboute M.-E., Combettes B., Clement B., Gigot C., Philipps G.;
RT   "Molecular characterization of tobacco ribonucleotide reductase RNR1 and
RT   RNR2 cDNAs and cell cycle-regulated expression in synchronized plant
RT   cells.";
RL   Plant Mol. Biol. 38:797-806(1998).
CC   -!- FUNCTION: Provides the precursors necessary for DNA synthesis.
CC       Catalyzes the biosynthesis of deoxyribonucleotides from the
CC       corresponding ribonucleotides.
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.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- INDUCTION: Maximum level of expression in mid-S phase.
CC   -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase small
CC       chain family. {ECO:0000305}.
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DR   EMBL; X92443; CAA63194.1; -; mRNA.
DR   PIR; T03688; T03688.
DR   RefSeq; NP_001312237.1; NM_001325308.1.
DR   AlphaFoldDB; P49730; -.
DR   SMR; P49730; -.
DR   STRING; 4097.P49730; -.
DR   PRIDE; P49730; -.
DR   GeneID; 107781035; -.
DR   KEGG; nta:107781035; -.
DR   UniPathway; UPA00326; -.
DR   Proteomes; UP000084051; Unplaced.
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; Reference proteome.
FT   CHAIN           1..329
FT                   /note="Ribonucleoside-diphosphate reductase small chain"
FT                   /id="PRO_0000190467"
FT   ACT_SITE        113
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10014"
FT   BINDING         75
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10014"
FT   BINDING         106
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10014"
FT   BINDING         106
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         109
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10014"
FT   BINDING         168
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         202
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         205
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   329 AA;  37608 MW;  65E7A4183AF045FD CRC64;
     MPLIPEEPLL ASSPDRFCMF PIQYPQIWEM YKKALASFWT AEEVDLSSDT RHWETLTPGE
     RHFITHVLAF FAASDGIVLE NLAGRFMKEV QVAEARAFYG FQIAIENIHS EMYSLLLESY
     IKDSDEKSRL FRAVETNPCV EKKAKWALRW IDGSETFAER LVAFACVEGI FFSGSFCAIF
     WLKKRGLMPG LTFSNELISR DEGLHCDFAC LLYSLLRTKL TEERVKGIVA DAVEIEREFV
     CDALPCALVG MNGDLMSKYI EFVADRLLDA LGYDKLYNAQ NPFDWMELIS LQGKTNFFEK
     RVGEYQKASV MSSLNGNGAT HEFKLDEDF