ID   RIR2_PLAFG              Reviewed;         322 AA.
AC   P50649;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Ribonucleoside-diphosphate reductase small subunit;
DE            EC=1.17.4.1;
DE   AltName: Full=Ribonucleotide reductase R2 subunit;
DE   AltName: Full=Ribonucleotide reductase small subunit;
GN   Name=RNR2;
OS   Plasmodium falciparum (isolate FCR-3 / Gambia).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX   NCBI_TaxID=5838;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8415692; DOI=10.1073/pnas.90.20.9280;
RA   Rubin H., Salem J.S., Li L.S., Yang F.D., Mama S., Wang Z.M., Fisher A.,
RA   Hamann C.S., Cooperman B.S.;
RT   "Cloning, sequence determination, and regulation of the ribonucleotide
RT   reductase subunits from Plasmodium falciparum: a target for antimalarial
RT   therapy.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:9280-9284(1993).
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 subunit.
CC   -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase small
CC       chain family. {ECO:0000305}.
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DR   EMBL; L22058; AAA29754.1; -; Genomic_DNA.
DR   AlphaFoldDB; P50649; -.
DR   SMR; P50649; -.
DR   UniPathway; UPA00326; -.
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   3: Inferred from homology;
KW   Deoxyribonucleotide synthesis; Iron; Metal-binding; Oxidoreductase.
FT   CHAIN           1..322
FT                   /note="Ribonucleoside-diphosphate reductase small subunit"
FT                   /id="PRO_0000190458"
FT   ACT_SITE        108
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10014"
FT   BINDING         70
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10014"
FT   BINDING         101
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10014"
FT   BINDING         101
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         104
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10014"
FT   BINDING         163
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         197
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         200
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   322 AA;  37372 MW;  73AD1257E294A013 CRC64;
     MRRILNKESD RFTLYPILYP DVFPFYKKAE ACFWTAEEID YSSDLKDFEK LNENEKHFIK
     HVLAFFAASD GIVLENLAVS FLREVQITEA KKFYSFQIAV ENIHSETYSL LIDNYIKDEK
     ERLNLFHAIE NIPAVKNKAL WAAKWINDTN SFAERIVANA CVEGILFSGS FCAIFWFKKQ
     NKLHGLTFSN ELISRDEGLH TDFNCLIYSL LDNKLPEQMV QNIVKEAGGV EVEKSFICES
     LPCDLIGMNS RLMSQYIEFV ADRLLECLGC SKIFHSKNPF NWMDLISLQG KTNFFEKRVA
     DYQKSGVMAQ RKDHVFCLNT EF