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Database: UniProt
Entry: Q27740
LinkDB: Q27740
Original site: Q27740 
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   05-DEC-2018, entry version 76.
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; 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
RP   ACTIVITY, 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
CC       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
CC       family. {ECO:0000305}.
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   ProteinModelPortal; 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; 2.40.500.20; -; 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;
KW   Metal-binding; Oxidoreductase.
FT   CHAIN         1    198       Superoxide dismutase [Fe].
FT                                /FTId=PRO_0000290112.
FT   METAL        27     27       Iron. {ECO:0000250}.
FT   METAL        74     74       Iron. {ECO:0000250}.
FT   METAL       158    158       Iron. {ECO:0000250}.
FT   METAL       162    162       Iron. {ECO:0000250}.
FT   TURN         12     18       {ECO:0000244|PDB:2GOJ}.
FT   HELIX        21     29       {ECO:0000244|PDB:2GOJ}.
FT   HELIX        31     43       {ECO:0000244|PDB:2GOJ}.
FT   TURN         47     50       {ECO:0000244|PDB:2GOJ}.
FT   HELIX        53     59       {ECO:0000244|PDB:2GOJ}.
FT   HELIX        62     79       {ECO:0000244|PDB:2GOJ}.
FT   HELIX        92    101       {ECO:0000244|PDB:2GOJ}.
FT   HELIX       104    117       {ECO:0000244|PDB:2GOJ}.
FT   STRAND      120    128       {ECO:0000244|PDB:2GOJ}.
FT   STRAND      134    140       {ECO:0000244|PDB:2GOJ}.
FT   TURN        145    149       {ECO:0000244|PDB:2GOJ}.
FT   STRAND      152    158       {ECO:0000244|PDB:2GOJ}.
FT   HELIX       161    163       {ECO:0000244|PDB:2GOJ}.
FT   HELIX       165    168       {ECO:0000244|PDB:2GOJ}.
FT   HELIX       172    179       {ECO:0000244|PDB:2GOJ}.
FT   TURN        180    182       {ECO:0000244|PDB:2GOJ}.
FT   HELIX       185    196       {ECO:0000244|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
//
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