GenomeNet

Database: UniProt
Entry: Q9TW89
LinkDB: Q9TW89
Original site: Q9TW89 
ID   SODF_PLAFA              Reviewed;         198 AA.
AC   Q9TW89; Q9TVN6; Q9U524; Q9U525; Q9U526; Q9U527; Q9U528; Q9U529;
AC   Q9U530;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   05-DEC-2018, entry version 82.
DE   RecName: Full=Superoxide dismutase [Fe];
DE            EC=1.15.1.1;
DE   AltName: Full=FeSOD;
GN   Name=SODB;
OS   Plasmodium falciparum.
OC   Eukaryota; 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,
RC   Isolate Gabon 15, Isolate Gabon 16, Isolate Gabon 17,
RC   Isolate Gabon 18, Isolate Gabon 19, Isolate Gabon 2, Isolate Gabon 20,
RC   Isolate Gabon 21, Isolate Gabon 22, Isolate Gabon 23,
RC   Isolate Gabon 24, Isolate Gabon 25, Isolate Gabon 26, Isolate Gabon 3,
RC   Isolate Gabon 4, Isolate Gabon 5, Isolate Gabon 6, Isolate Gabon 7,
RC   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
RT   dismutase 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
CC       systems. {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
CC       family. {ECO:0000305}.
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   ProteinModelPortal; Q9TW89; -.
DR   SMR; Q9TW89; -.
DR   ChEMBL; CHEMBL6077; -.
DR   eggNOG; KOG0876; Eukaryota.
DR   eggNOG; COG0605; LUCA.
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   3: Inferred from homology;
KW   Cytoplasm; Iron; Metal-binding; Oxidoreductase.
FT   CHAIN         1    198       Superoxide dismutase [Fe].
FT                                /FTId=PRO_0000290111.
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   VARIANT      19     19       I -> V (in strain: isolate Gabon 25).
FT   VARIANT      20     20       S -> G (in strain: isolate Gabon 24).
FT   VARIANT      24     24       L -> I (in strain: isolate Gabon 23).
FT   VARIANT      84     84       D -> G (in strain: isolate Gabon 20).
FT   VARIANT     108    108       K -> E (in strain: isolate Gabon 21).
FT   VARIANT     135    135       V -> A (in strain: isolate Gabon 21).
FT   VARIANT     151    151       G -> S (in strain: isolate Gabon 20).
FT   VARIANT     166    166       I -> T (in strain: isolate Gabon 26).
FT   VARIANT     167    167       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
//
DBGET integrated database retrieval system