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Database: UniProt
Entry: O13401
LinkDB: O13401
Original site: O13401 
ID   SODM_CANAX              Reviewed;         234 AA.
AC   O13401;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   05-DEC-2018, entry version 85.
DE   RecName: Full=Superoxide dismutase [Mn], mitochondrial;
DE            EC=1.15.1.1;
DE   Flags: Precursor;
GN   Name=SOD2;
OS   Candida albicans (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Debaryomycetaceae;
OC   Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5476;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, AND
RP   CHARACTERIZATION.
RX   PubMed=10076057; DOI=10.1016/S0304-4165(98)00161-5;
RA   Rhie G.E., Hwang C.S., Brady M.J., Kim S.T., Kim Y.R., Huh W.K.,
RA   Baek Y.U., Lee B.H., Lee J.S., Kang S.O.;
RT   "Manganese-containing superoxide dismutase and its gene from Candida
RT   albicans.";
RL   Biochim. Biophys. Acta 1426:409-419(1999).
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   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000305}.
DR   EMBL; AF031478; AAB86583.1; -; Genomic_DNA.
DR   ProteinModelPortal; O13401; -.
DR   SMR; O13401; -.
DR   Allergome; 9599; Cand a MnSOD.
DR   GO; GO:0005759; C:mitochondrial matrix; 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   Direct protein sequencing; Manganese; Metal-binding; Mitochondrion;
KW   Oxidoreductase; Transit peptide.
FT   TRANSIT       1     34       Mitochondrion.
FT   CHAIN        35    234       Superoxide dismutase [Mn], mitochondrial.
FT                                /FTId=PRO_0000032882.
FT   METAL        60     60       Manganese. {ECO:0000250}.
FT   METAL       108    108       Manganese. {ECO:0000250}.
FT   METAL       198    198       Manganese. {ECO:0000250}.
FT   METAL       202    202       Manganese. {ECO:0000250}.
SQ   SEQUENCE   234 AA;  26174 MW;  EFBFC2D769C1D9C1 CRC64;
     MFSIRSSSRV LLKASSATTR ATLNAAASKT FTRSKYSLPE LDYEFSATEP YISGQINEIH
     YTKHHQTYVN NLNASIEQAV EAKSKGEVKK LVALEKAINF NGGGYLNHCL WWKNLAPVSQ
     GGGQPPSEDS KLGKQIVKQF GSLDKLIEIT NGKLAGIQGS GWAFIVKNKA NGDTIDVITT
     ANQDTVTDPN LVPLIAIDAW EHAYYLQYQN VKADYFKNLW HVINWKEAER RFEF
//
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