ID   SODF_PLAFX              Reviewed;         198 AA.
AC   Q27740;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Superoxide dismutase [Fe];
DE            EC=1.15.1.1;
DE   AltName: Full=FeSOD;
GN   Name=SODB;
OS   Plasmodium falciparum (isolate HB3).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX   NCBI_TaxID=137071;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-30, CATALYTIC ACTIVITY,
RP   AND SUBUNIT.
RX   PubMed=8920001; DOI=10.1016/0166-6851(95)02552-9;
RA   Becuwe P., Gratepanche S., Fourmaux M.-N., Van Beeumen J., Samyn B.,
RA   Mercereau-Puijalon O., Touzel J.P., Slomianny C., Camus D., Dive D.;
RT   "Characterization of iron-dependent endogenous superoxide dismutase of
RT   Plasmodium falciparum.";
RL   Mol. Biochem. Parasitol. 76:125-134(1996).
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:8920001};
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:0000269|PubMed:8920001}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC       {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; Z49819; CAA89971.1; -; mRNA.
DR   PIR; S55499; S55499.
DR   PDB; 2GOJ; X-ray; 2.00 A; A/B=2-198.
DR   PDBsum; 2GOJ; -.
DR   AlphaFoldDB; Q27740; -.
DR   SMR; Q27740; -.
DR   EvolutionaryTrace; Q27740; -.
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   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Direct protein sequencing; Iron; Metal-binding;
KW   Oxidoreductase.
FT   CHAIN           1..198
FT                   /note="Superoxide dismutase [Fe]"
FT                   /id="PRO_0000290112"
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   TURN            12..18
FT                   /evidence="ECO:0007829|PDB:2GOJ"
FT   HELIX           21..29
FT                   /evidence="ECO:0007829|PDB:2GOJ"
FT   HELIX           31..43
FT                   /evidence="ECO:0007829|PDB:2GOJ"
FT   TURN            47..50
FT                   /evidence="ECO:0007829|PDB:2GOJ"
FT   HELIX           53..59
FT                   /evidence="ECO:0007829|PDB:2GOJ"
FT   HELIX           62..79
FT                   /evidence="ECO:0007829|PDB:2GOJ"
FT   HELIX           92..101
FT                   /evidence="ECO:0007829|PDB:2GOJ"
FT   HELIX           104..117
FT                   /evidence="ECO:0007829|PDB:2GOJ"
FT   STRAND          120..128
FT                   /evidence="ECO:0007829|PDB:2GOJ"
FT   STRAND          134..140
FT                   /evidence="ECO:0007829|PDB:2GOJ"
FT   TURN            145..149
FT                   /evidence="ECO:0007829|PDB:2GOJ"
FT   STRAND          152..158
FT                   /evidence="ECO:0007829|PDB:2GOJ"
FT   HELIX           161..163
FT                   /evidence="ECO:0007829|PDB:2GOJ"
FT   HELIX           165..168
FT                   /evidence="ECO:0007829|PDB:2GOJ"
FT   HELIX           172..179
FT                   /evidence="ECO:0007829|PDB:2GOJ"
FT   TURN            180..182
FT                   /evidence="ECO:0007829|PDB:2GOJ"
FT   HELIX           185..196
FT                   /evidence="ECO:0007829|PDB:2GOJ"
SQ   SEQUENCE   198 AA;  22734 MW;  0C768B66E6044D3B CRC64;
     MVITLPKLKY ALNALSPHIS EETLNFHYNK HHAGYVNKLN TLIKDTPFAE KSLLDIVKES
     SGAIFNNAAQ IWNHTFYWDS MGPDCGGEPH GEIKEKIQED FGSFNNFKEQ FSNILCGHFG
     SGWGWLALNN NNKLVILQTH DAGNPIKDNT GIPILTCDIW EHAYYIDYRN DRASYVKAWW
     NLVNWNFANE NLKKAMKK