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Database: UniProt
Entry: P66832
LinkDB: P66832
Original site: P66832 
ID   SODM2_STAAW             Reviewed;         199 AA.
AC   P66832; Q99X82;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   05-DEC-2018, entry version 82.
DE   RecName: Full=Superoxide dismutase [Mn/Fe] 2;
DE            EC=1.15.1.1;
GN   Name=sodM; OrderedLocusNames=MW0107;
OS   Staphylococcus aureus (strain MW2).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=196620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MW2;
RX   PubMed=12044378; DOI=10.1016/S0140-6736(02)08713-5;
RA   Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A.,
RA   Nagai Y., Iwama N., Asano K., Naimi T., Kuroda H., Cui L.,
RA   Yamamoto K., Hiramatsu K.;
RT   "Genome and virulence determinants of high virulence community-
RT   acquired MRSA.";
RL   Lancet 359:1819-1827(2002).
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 SodA (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000305}.
DR   EMBL; BA000033; BAB93972.1; -; Genomic_DNA.
DR   RefSeq; WP_000874681.1; NC_003923.1.
DR   ProteinModelPortal; P66832; -.
DR   SMR; P66832; -.
DR   EnsemblBacteria; BAB93972; BAB93972; BAB93972.
DR   KEGG; sam:MW0107; -.
DR   HOGENOM; HOG000013583; -.
DR   KO; K04564; -.
DR   OMA; HNQFWEM; -.
DR   BioCyc; SAUR196620:G1G3G-120-MONOMER; -.
DR   Proteomes; UP000000418; Chromosome.
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   Complete proteome; Iron; Manganese; Metal-binding; Oxidoreductase;
KW   Stress response.
FT   CHAIN         1    199       Superoxide dismutase [Mn/Fe] 2.
FT                                /FTId=PRO_0000160084.
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;  23041 MW;  388566FB9943C635 CRC64;
     MAFKLPNLPY AYDALEPYID QRTMEFHHDK HHNTYVTKLN ATVEGTELEH QSLADMIANL
     DKVPEAMRMS VRNNGGGHFN HSLFWEILSP NSEEKGGVID DIKAQWGTLD EFKNEFANKA
     TTLFGSGWTW LVVNDGKLEI VTTPNQDNPL TEGKTPILLF DVWEHAYYLK YQNKRPDYMT
     AFWNIVNWKK VDELYQAAK
//
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