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Database: UniProt
Entry: Q6G913
LinkDB: Q6G913
Original site: Q6G913 
ID   SODM1_STAAS             Reviewed;         199 AA.
AC   Q6G913;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   05-DEC-2018, entry version 81.
DE   RecName: Full=Superoxide dismutase [Mn/Fe] 1;
DE            EC=1.15.1.1;
GN   Name=sodA; OrderedLocusNames=SAS1491;
OS   Staphylococcus aureus (strain MSSA476).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282459;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MSSA476;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T.,
RA   Churcher C., Clark L., Corton C., Cronin A., Doggett J., Dowd L.,
RA   Feltwell T., Hance Z., Harris B., Hauser H., Holroyd S., Jagels K.,
RA   James K.D., Lennard N., Line A., Mayes R., Moule S., Mungall K.,
RA   Ormond D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Sanders M.,
RA   Sharp S., Simmonds M., Stevens K., Whitehead S., Barrell B.G.,
RA   Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains:
RT   evidence for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
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=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250};
CC       Note=Binds 1 Mn(2+) or Fe(2+) ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer. Can also form a heterodimer with SodM (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000305}.
DR   EMBL; BX571857; CAG43292.1; -; Genomic_DNA.
DR   RefSeq; WP_000863556.1; NC_002953.3.
DR   ProteinModelPortal; Q6G913; -.
DR   SMR; Q6G913; -.
DR   KEGG; sas:SAS1491; -.
DR   HOGENOM; HOG000013583; -.
DR   KO; K04564; -.
DR   OMA; KWGSFDK; -.
DR   BioCyc; SAUR282459:G1G3P-1633-MONOMER; -.
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   Iron; Manganese; Metal-binding; Oxidoreductase; Stress response.
FT   CHAIN         1    199       Superoxide dismutase [Mn/Fe] 1.
FT                                /FTId=PRO_0000160073.
FT   METAL        27     27       Manganese or iron. {ECO:0000250}.
FT   METAL        81     81       Manganese or iron. {ECO:0000250}.
FT   METAL       161    161       Manganese or iron. {ECO:0000250}.
FT   METAL       165    165       Manganese or iron. {ECO:0000250}.
SQ   SEQUENCE   199 AA;  22711 MW;  F2CEC7B4701AC559 CRC64;
     MAFELPKLPY AFDALEPHFD KETMEIHHDR HHNTYVTKLN AAVEGTDLES KSIEEIVANL
     DSVPANIQTA VRNNGGGHLN HSLFWELLSP NSEEKGTVVE KIKEQWGSLE EFKKEFADKA
     AARFGSGWAW LVVNNGQLEI VTTPNQDNPL TEGKTPILGL DVWEHAYYLK YQNKRPDYIG
     AFWNVVNWEK VDELYNATK
//
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