ID   SODF_PLAVI              Reviewed;         198 AA.
AC   Q9Y1A9;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Superoxide dismutase [Fe];
DE            EC=1.15.1.1;
DE   AltName: Full=FeSOD;
GN   Name=SODB;
OS   Plasmodium vivax.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX   NCBI_TaxID=5855;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10599926; DOI=10.1007/s004360050675;
RA   Baert C.B., Deloron P., Viscogliosi E., Delgado-Viscogliosi P., Camus D.,
RA   Dive D.;
RT   "Cloning and characterization of iron-containing superoxide dismutase from
RT   the human malaria species Plasmodium ovale, P. malariae and P. vivax.";
RL   Parasitol. Res. 85:1018-1024(1999).
CC   -!- FUNCTION: Destroys superoxide anion radicals which are normally
CC       produced within the cells and which are toxic to biological systems.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:18421; EC=1.15.1.1;
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC       Note=Binds 1 Fe cation per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC       {ECO:0000305}.
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DR   EMBL; AF139529; AAD43524.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9Y1A9; -.
DR   SMR; Q9Y1A9; -.
DR   VEuPathDB; PlasmoDB:PVP01_1425500; -.
DR   VEuPathDB; PlasmoDB:PVX_123030; -.
DR   eggNOG; KOG0876; Eukaryota.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR   Gene3D; 1.10.287.990; -; 1.
DR   Gene3D; 3.55.40.20; -; 1.
DR   InterPro; IPR001189; Mn/Fe_SOD.
DR   InterPro; IPR019833; Mn/Fe_SOD_BS.
DR   InterPro; IPR019832; Mn/Fe_SOD_C.
DR   InterPro; IPR019831; Mn/Fe_SOD_N.
DR   InterPro; IPR036324; Mn/Fe_SOD_N_sf.
DR   InterPro; IPR036314; SOD_C_sf.
DR   Pfam; PF02777; Sod_Fe_C; 1.
DR   Pfam; PF00081; Sod_Fe_N; 1.
DR   PIRSF; PIRSF000349; SODismutase; 1.
DR   PRINTS; PR01703; MNSODISMTASE.
DR   SUPFAM; SSF46609; SSF46609; 1.
DR   SUPFAM; SSF54719; SSF54719; 1.
DR   PROSITE; PS00088; SOD_MN; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Iron; Metal-binding; Oxidoreductase.
FT   CHAIN           1..198
FT                   /note="Superoxide dismutase [Fe]"
FT                   /id="PRO_0000290114"
FT   BINDING         27
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         74
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         158
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         162
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   198 AA;  22734 MW;  0C636B66E6044D3B CRC64;
     MVITLPKLKY ALNALSPHIS EETLNFHYNK HHAGYVNKLN TLIKDTPFAE KSLLDIVKES
     SGAIFNNAAQ IWNHTFYWDS MGPDCGGEPH GEIKEKIQED FGSFNNFKEQ FSNILCGHFG
     SGWGWLALNN NNKLVILQTH DAGNPIKDNT GIPILTCDIW EHAYYIDYRN DRASYVKAWW
     NLVNWNFANE NLKKAMQK