ID   RIR2_LEIAM              Reviewed;         345 AA.
AC   O46310;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   27-MAR-2024, entry version 99.
DE   RecName: Full=Ribonucleoside-diphosphate reductase small subunit;
DE            EC=1.17.4.1;
DE   AltName: Full=Ribonucleotide reductase M2 subunit;
DE   AltName: Full=Ribonucleotide reductase small subunit;
OS   Leishmania amazonensis.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX   NCBI_TaxID=5659;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9497060; DOI=10.1016/s0166-6851(97)00159-x;
RA   Lye L.-F., Hsieh Y.-H., Su K.-E., Lee S.T.;
RT   "Cloning and functional analysis of the ribonucleotide reductase gene small
RT   subunit from hydroxyurea-resistant Leishmania mexicana amazonensis.";
RL   Mol. Biochem. Parasitol. 90:353-358(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   -!- SUBUNIT: Heterodimer of a large and a small subunit. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase small
CC       chain 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; AF005247; AAC08302.1; -; Genomic_DNA.
DR   AlphaFoldDB; O46310; -.
DR   SMR; O46310; -.
DR   VEuPathDB; TriTrypDB:LAMA_000549400; -.
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:UniProtKB-KW.
DR   CDD; cd01049; RNRR2; 1.
DR   Gene3D; 1.10.620.20; Ribonucleotide Reductase, subunit A; 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; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE SMALL CHAIN; 1.
DR   PANTHER; PTHR23409:SF18; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE SUBUNIT M2; 1.
DR   Pfam; PF00268; Ribonuc_red_sm; 1.
DR   SUPFAM; SSF47240; Ferritin-like; 1.
DR   PROSITE; PS00368; RIBORED_SMALL; 1.
PE   3: Inferred from homology;
KW   Deoxyribonucleotide synthesis; Iron; Metal-binding; Oxidoreductase.
FT   CHAIN           1..345
FT                   /note="Ribonucleoside-diphosphate reductase small subunit"
FT                   /id="PRO_0000190457"
FT   ACT_SITE        131
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10014"
FT   BINDING         93
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10014"
FT   BINDING         124
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10014"
FT   BINDING         124
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         127
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10014"
FT   BINDING         186
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         220
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         223
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   345 AA;  39651 MW;  D0829B1BFE9EA115 CRC64;
     MKPVAAGAEV LPADKVAQGT NAEEEPLQQE NPFRYVLFPI QYHDIWRKYK EQESCIWTVE
     EIDLGNDMKD WATLNDGERH FIKHVLAFFA GSDGIVIENL AQRFMSDVKV PEARAFYGFQ
     LMMENIHSET YSVLLDTYIT DSEEKLRLLH AIQTIPCIQK KAEWPVRWIG SSASFQQRLI
     GFAAVEGIFF SGSFCALFWL KKRGLMPGLT FSNELISRDE GLHTDFACLL YNSHIKHKLP
     RERVLEIIVD AVNIEREFIC DALPVRLIGM NAELMAQYIE FVADRLLVSL GEEKHYRSTQ
     PFDFMEMISL QGKTNFFEKR VGEYQKAGVM STEGTSKKFS LSEDF
//