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SODF_PLAFA
ID   SODF_PLAFA              Reviewed;         198 AA.
AC   Q9TW89; Q9TVN6; Q9U524; Q9U525; Q9U526; Q9U527; Q9U528; Q9U529; Q9U530;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Superoxide dismutase [Fe];
DE            EC=1.15.1.1;
DE   AltName: Full=FeSOD;
GN   Name=SODB;
OS   Plasmodium falciparum.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX   NCBI_TaxID=5833;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Isolate Gabon 1, Isolate Gabon 10, Isolate Gabon 11,
RC   Isolate Gabon 12, Isolate Gabon 13, Isolate Gabon 14, Isolate Gabon 15,
RC   Isolate Gabon 16, Isolate Gabon 17, Isolate Gabon 18, Isolate Gabon 19,
RC   Isolate Gabon 2, Isolate Gabon 20, Isolate Gabon 21, Isolate Gabon 22,
RC   Isolate Gabon 23, Isolate Gabon 24, Isolate Gabon 25, Isolate Gabon 26,
RC   Isolate Gabon 3, Isolate Gabon 4, Isolate Gabon 5, Isolate Gabon 6,
RC   Isolate Gabon 7, Isolate Gabon 8, and Isolate Gabon 9;
RX   PubMed=10585544; DOI=10.1111/j.1574-6968.1999.tb08850.x;
RA   Baert C.B., Deloron P., Viscogliosi E., Dauchez M., Camus D., Dive D.;
RT   "Analysis of genetic diversity at the iron-containing superoxide dismutase
RT   locus in Plasmodium falciparum wild isolates.";
RL   FEMS Microbiol. Lett. 181:237-243(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; AF113142; AAD03746.1; -; Genomic_DNA.
DR   EMBL; AF113143; AAD03747.1; -; Genomic_DNA.
DR   EMBL; AF113144; AAD03748.1; -; Genomic_DNA.
DR   EMBL; AF113145; AAD03749.1; -; Genomic_DNA.
DR   EMBL; AF113146; AAD03750.1; -; Genomic_DNA.
DR   EMBL; AF113147; AAD03751.1; -; Genomic_DNA.
DR   EMBL; AF113148; AAD03752.1; -; Genomic_DNA.
DR   EMBL; AF113149; AAD03753.1; -; Genomic_DNA.
DR   EMBL; AF113150; AAD03754.1; -; Genomic_DNA.
DR   EMBL; AF113151; AAD03755.1; -; Genomic_DNA.
DR   EMBL; AF113152; AAD03756.1; -; Genomic_DNA.
DR   EMBL; AF113153; AAD03757.1; -; Genomic_DNA.
DR   EMBL; AF113154; AAD03758.1; -; Genomic_DNA.
DR   EMBL; AF113155; AAD03759.1; -; Genomic_DNA.
DR   EMBL; AF113156; AAD03760.1; -; Genomic_DNA.
DR   EMBL; AF113157; AAD03761.1; -; Genomic_DNA.
DR   EMBL; AF113158; AAD03762.1; -; Genomic_DNA.
DR   EMBL; AF113159; AAD03763.1; -; Genomic_DNA.
DR   EMBL; AF113160; AAD03764.1; -; Genomic_DNA.
DR   EMBL; AF113161; AAD03765.1; -; Genomic_DNA.
DR   EMBL; AF113162; AAD03766.1; -; Genomic_DNA.
DR   EMBL; AF113163; AAD03767.1; -; Genomic_DNA.
DR   EMBL; AF113164; AAD03768.1; -; Genomic_DNA.
DR   EMBL; AF113165; AAD03769.1; -; Genomic_DNA.
DR   EMBL; AF113166; AAD03770.1; -; Genomic_DNA.
DR   EMBL; AF113167; AAD03771.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9TW89; -.
DR   SMR; Q9TW89; -.
DR   ChEMBL; CHEMBL6077; -.
DR   EnsemblProtists; CAD51224; CAD51224; PF3D7_0814900.
DR   VEuPathDB; PlasmoDB:PF3D7_0814900; -.
DR   VEuPathDB; PlasmoDB:Pf7G8-2_000230200; -.
DR   VEuPathDB; PlasmoDB:Pf7G8_080019900; -.
DR   VEuPathDB; PlasmoDB:PfCD01_080020400; -.
DR   VEuPathDB; PlasmoDB:PfDd2_080020000; -.
DR   VEuPathDB; PlasmoDB:PfGA01_080018500; -.
DR   VEuPathDB; PlasmoDB:PfGB4_080019600; -.
DR   VEuPathDB; PlasmoDB:PfGN01_080020500; -.
DR   VEuPathDB; PlasmoDB:PfHB3_080020300; -.
DR   VEuPathDB; PlasmoDB:PfIT_080019800; -.
DR   VEuPathDB; PlasmoDB:PfKE01_080020400; -.
DR   VEuPathDB; PlasmoDB:PfKH01_080019900; -.
DR   VEuPathDB; PlasmoDB:PfKH02_080020400; -.
DR   VEuPathDB; PlasmoDB:PfML01_080020400; -.
DR   VEuPathDB; PlasmoDB:PfNF135_000021500; -.
DR   VEuPathDB; PlasmoDB:PfNF166_080018700; -.
DR   VEuPathDB; PlasmoDB:PfNF54_080018700; -.
DR   VEuPathDB; PlasmoDB:PfSD01_080020200; -.
DR   VEuPathDB; PlasmoDB:PfSN01_080019400; -.
DR   VEuPathDB; PlasmoDB:PfTG01_080020700; -.
DR   OMA; KWGSFDK; -.
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_0000290111"
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"
FT   VARIANT         19
FT                   /note="I -> V (in strain: isolate Gabon 25)"
FT   VARIANT         20
FT                   /note="S -> G (in strain: isolate Gabon 24)"
FT   VARIANT         24
FT                   /note="L -> I (in strain: isolate Gabon 23)"
FT   VARIANT         84
FT                   /note="D -> G (in strain: isolate Gabon 20)"
FT   VARIANT         108
FT                   /note="K -> E (in strain: isolate Gabon 21)"
FT   VARIANT         135
FT                   /note="V -> A (in strain: isolate Gabon 21)"
FT   VARIANT         151
FT                   /note="G -> S (in strain: isolate Gabon 20)"
FT   VARIANT         166
FT                   /note="I -> T (in strain: isolate Gabon 26)"
FT   VARIANT         167
FT                   /note="D -> N (in strain: isolate Gabon 22)"
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
 
 
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