RIR2_PLAF4
ID RIR2_PLAF4 Reviewed; 349 AA.
AC P50650;
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 chain;
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 Dd2).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=57267;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8265664; DOI=10.1073/pnas.90.24.12020;
RA Chakrabarti D., Schuster S.M., Chakrabarti R.;
RT "Cloning and characterization of subunit genes of ribonucleotide reductase,
RT a cell-cycle-regulated enzyme, from Plasmodium falciparum.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:12020-12024(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; U01322; AAA50170.1; -; mRNA.
DR PIR; B49412; B49412.
DR AlphaFoldDB; P50650; -.
DR SMR; P50650; -.
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 2: Evidence at transcript level;
KW Deoxyribonucleotide synthesis; Iron; Metal-binding; Oxidoreductase.
FT CHAIN 1..349
FT /note="Ribonucleoside-diphosphate reductase small chain"
FT /id="PRO_0000190459"
FT ACT_SITE 137
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10014"
FT BINDING 99
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10014"
FT BINDING 130
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10014"
FT BINDING 130
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 133
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10014"
FT BINDING 192
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 226
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 229
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 349 AA; 40595 MW; D21FE30B78F85889 CRC64;
MADVINISRI PIFSKQEREF SDLQKGKEIN EKILNKESDR FTLYPILYPD VWDFYKKAEA
SFWTAEEIDL SSDLKDFEKL NENEKHFIKH VLAFFAASDG IVLENLASKF LREVQITEAK
KFYSFQIAVE NIHSETYSLL IDNYIKDEKE RLNLFHAIEN IPAVKNKALW AAKWINDTNS
FAERIVANAC VEGILFSGSF CAIFWFKKQN KLHGLTFSNE LISRDEGLHT DFNCLIYSLL
DNKLPEQIIQ NIVKEAVEVE RSFICESLPC DLIGMNSRLM SQYIEFVADR LLECLGCSKI
FHSKNPFNWM DLISLQGKTN FFEKRVADYQ KSGVMAQRKD QVFCLNTEF
