RIR2_TRYBB
ID RIR2_TRYBB Reviewed; 337 AA.
AC O15910; O15880;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 94.
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; Synonyms=NRDB;
OS Trypanosoma brucei brucei.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX NCBI_TaxID=5702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=427;
RX PubMed=9192674; DOI=10.1073/pnas.94.13.6959;
RA Hofer A., Schmidt P.P., Graslund A., Thelander L.;
RT "Cloning and characterization of the R1 and R2 subunits of ribonucleotide
RT reductase from Trypanosoma brucei.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:6959-6964(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9315738; DOI=10.1016/s0014-5793(97)01036-3;
RA Dormeyer M., Schoneck R., Dittmar G.A.G., Krauth-Siegel R.L.;
RT "Cloning, sequencing and expression of ribonucleotide reductase R2 from
RT Trypanosoma brucei.";
RL FEBS Lett. 414:449-453(1997).
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; U80911; AAB70705.1; -; mRNA.
DR EMBL; Y10768; CAA71741.1; -; Genomic_DNA.
DR AlphaFoldDB; O15910; -.
DR SMR; O15910; -.
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..337
FT /note="Ribonucleoside-diphosphate reductase small chain"
FT /id="PRO_0000190460"
FT ACT_SITE 123
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10014"
FT BINDING 85
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10014"
FT BINDING 116
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10014"
FT BINDING 116
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 119
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10014"
FT BINDING 178
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 212
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 215
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT CONFLICT 8..10
FT /note="CSR -> RSA (in Ref. 2; CAA71741)"
FT /evidence="ECO:0000305"
FT CONFLICT 43
FT /note="E -> K (in Ref. 2; CAA71741)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 337 AA; 39009 MW; BD39919280C65CAE CRC64;
MPPKSHKCSR KEGEVEEPLL TENPDRYVIF PIKYPDIWQK YKEAESSIWT VEEIDLGNDM
TDWEKLDDGE RHFIKHVLAF FAASDGIVLE NLAERFMCEV QVPEVRCFYG FQIAMENIHS
ETYSVLIDTY VVDPDEKQRL LHAIRTIPCI EKKAKWAIEW IGSQTSFPTR LVAFAAVEGI
FFSGSFCAIF WLKKRGLMPG LTFSNELISR DEGLHTDFAC LLYEKYIVNK LPRDRVLEII
CNAVSIEREF ICDALPVRLI GMNSQLMTQY IEFVADRLLV SLGYDRHYNS KNPFDFMDMI
SLQGKTNFFE KKVGEYQKAG VMSSERSSKV FSLDADF
