ID   SODF_PLAF7              Reviewed;         198 AA.
AC   Q8IAY6;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Superoxide dismutase [Fe];
DE            EC=1.15.1.1;
DE   AltName: Full=FeSOD;
GN   Name=SODB; ORFNames=PF08_0071;
OS   Plasmodium falciparum (isolate 3D7).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX   NCBI_TaxID=36329;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3D7;
RX   PubMed=12368864; DOI=10.1038/nature01097;
RA   Gardner M.J., Hall N., Fung E., White O., Berriman M., Hyman R.W.,
RA   Carlton J.M., Pain A., Nelson K.E., Bowman S., Paulsen I.T., James K.D.,
RA   Eisen J.A., Rutherford K.M., Salzberg S.L., Craig A., Kyes S., Chan M.-S.,
RA   Nene V., Shallom S.J., Suh B., Peterson J., Angiuoli S., Pertea M.,
RA   Allen J., Selengut J., Haft D., Mather M.W., Vaidya A.B., Martin D.M.A.,
RA   Fairlamb A.H., Fraunholz M.J., Roos D.S., Ralph S.A., McFadden G.I.,
RA   Cummings L.M., Subramanian G.M., Mungall C., Venter J.C., Carucci D.J.,
RA   Hoffman S.L., Newbold C., Davis R.W., Fraser C.M., Barrell B.G.;
RT   "Genome sequence of the human malaria parasite Plasmodium falciparum.";
RL   Nature 419:498-511(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3D7;
RX   PubMed=12368867; DOI=10.1038/nature01095;
RA   Hall N., Pain A., Berriman M., Churcher C.M., Harris B., Harris D.,
RA   Mungall K.L., Bowman S., Atkin R., Baker S., Barron A., Brooks K.,
RA   Buckee C.O., Burrows C., Cherevach I., Chillingworth C., Chillingworth T.,
RA   Christodoulou Z., Clark L., Clark R., Corton C., Cronin A., Davies R.M.,
RA   Davis P., Dear P., Dearden F., Doggett J., Feltwell T., Goble A.,
RA   Goodhead I., Gwilliam R., Hamlin N., Hance Z., Harper D., Hauser H.,
RA   Hornsby T., Holroyd S., Horrocks P., Humphray S., Jagels K., James K.D.,
RA   Johnson D., Kerhornou A., Knights A., Konfortov B., Kyes S., Larke N.,
RA   Lawson D., Lennard N., Line A., Maddison M., Mclean J., Mooney P.,
RA   Moule S., Murphy L., Oliver K., Ormond D., Price C., Quail M.A.,
RA   Rabbinowitsch E., Rajandream M.A., Rutter S., Rutherford K.M., Sanders M.,
RA   Simmonds M., Seeger K., Sharp S., Smith R., Squares R., Squares S.,
RA   Stevens K., Taylor K., Tivey A., Unwin L., Whitehead S., Woodward J.R.,
RA   Sulston J.E., Craig A., Newbold C., Barrell B.G.;
RT   "Sequence of Plasmodium falciparum chromosomes 1, 3-9 and 13.";
RL   Nature 419:527-531(2002).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.52 ANGSTROMS) IN COMPLEX WITH IRON IONS, CATALYTIC
RP   ACTIVITY, AND SUBUNIT.
RX   PubMed=17020617; DOI=10.1186/1472-6807-6-20;
RA   Boucher I.W., Brzozowski A.M., Brannigan J.A., Schnick C., Smith D.J.,
RA   Kyes S.A., Wilkinson A.J.;
RT   "The crystal structure of superoxide dismutase from Plasmodium
RT   falciparum.";
RL   BMC Struct. Biol. 6:20-20(2006).
CC   -!- FUNCTION: Destroys superoxide anion radicals which are normally
CC       produced within the cells and which are toxic to biological systems.
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         Evidence={ECO:0000269|PubMed:17020617};
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC       Note=Binds 1 Fe cation per subunit.;
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17020617}.
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; AL844507; CAD51224.1; -; Genomic_DNA.
DR   RefSeq; XP_001349375.1; XM_001349339.1.
DR   PDB; 2BPI; X-ray; 2.52 A; A/B=1-198.
DR   PDBsum; 2BPI; -.
DR   AlphaFoldDB; Q8IAY6; -.
DR   SMR; Q8IAY6; -.
DR   IntAct; Q8IAY6; 1.
DR   MINT; Q8IAY6; -.
DR   STRING; 5833.PF08_0071; -.
DR   PRIDE; Q8IAY6; -.
DR   EnsemblProtists; CAD51224; CAD51224; PF3D7_0814900.
DR   GeneID; 2655270; -.
DR   KEGG; pfa:PF3D7_0814900; -.
DR   VEuPathDB; PlasmoDB:PF3D7_0814900; -.
DR   HOGENOM; CLU_031625_0_0_1; -.
DR   InParanoid; Q8IAY6; -.
DR   OMA; KWGSFDK; -.
DR   PhylomeDB; Q8IAY6; -.
DR   EvolutionaryTrace; Q8IAY6; -.
DR   Proteomes; UP000001450; Chromosome 8.
DR   GO; GO:0005829; C:cytosol; IDA:GeneDB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004784; F:superoxide dismutase activity; ISO:GeneDB.
DR   GO; GO:0006979; P:response to oxidative stress; ISS:GeneDB.
DR   GO; GO:0006801; P:superoxide metabolic process; ISS:GeneDB.
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   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Iron; Metal-binding; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..198
FT                   /note="Superoxide dismutase [Fe]"
FT                   /id="PRO_0000290110"
FT   BINDING         27
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT   BINDING         74
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT   BINDING         158
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT   BINDING         162
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT   TURN            12..18
FT                   /evidence="ECO:0007829|PDB:2BPI"
FT   HELIX           21..29
FT                   /evidence="ECO:0007829|PDB:2BPI"
FT   HELIX           31..43
FT                   /evidence="ECO:0007829|PDB:2BPI"
FT   TURN            47..50
FT                   /evidence="ECO:0007829|PDB:2BPI"
FT   HELIX           53..59
FT                   /evidence="ECO:0007829|PDB:2BPI"
FT   HELIX           62..79
FT                   /evidence="ECO:0007829|PDB:2BPI"
FT   HELIX           92..101
FT                   /evidence="ECO:0007829|PDB:2BPI"
FT   HELIX           104..117
FT                   /evidence="ECO:0007829|PDB:2BPI"
FT   STRAND          120..128
FT                   /evidence="ECO:0007829|PDB:2BPI"
FT   STRAND          134..140
FT                   /evidence="ECO:0007829|PDB:2BPI"
FT   TURN            145..149
FT                   /evidence="ECO:0007829|PDB:2BPI"
FT   STRAND          152..158
FT                   /evidence="ECO:0007829|PDB:2BPI"
FT   HELIX           161..163
FT                   /evidence="ECO:0007829|PDB:2BPI"
FT   HELIX           165..168
FT                   /evidence="ECO:0007829|PDB:2BPI"
FT   HELIX           172..179
FT                   /evidence="ECO:0007829|PDB:2BPI"
FT   TURN            180..182
FT                   /evidence="ECO:0007829|PDB:2BPI"
FT   HELIX           185..197
FT                   /evidence="ECO:0007829|PDB:2BPI"
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