ID   SODM2_STAAB             Reviewed;         199 AA.
AC   Q2YUU9;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Superoxide dismutase [Mn/Fe] 2;
DE            EC=1.15.1.1 {ECO:0000250|UniProtKB:P80293};
GN   Name=sodM; OrderedLocusNames=SAB0072;
OS   Staphylococcus aureus (strain bovine RF122 / ET3-1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=273036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=bovine RF122 / ET3-1;
RX   PubMed=17971880; DOI=10.1371/journal.pone.0001120;
RA   Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.;
RT   "Molecular correlates of host specialization in Staphylococcus aureus.";
RL   PLoS ONE 2:E1120-E1120(2007).
CC   -!- FUNCTION: Destroys superoxide anion radicals which are normally
CC       produced within the cells and which are toxic to biological systems.
CC       Catalyzes the dismutation of superoxide anion radicals into O2 and H2O2
CC       by successive reduction and oxidation of the transition metal ion at
CC       the active site. {ECO:0000250|UniProtKB:P80293}.
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:0000250|UniProtKB:P80293};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20697;
CC         Evidence={ECO:0000250|UniProtKB:P80293};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:P80293};
CC       Name=Fe(3+); Xref=ChEBI:CHEBI:29034;
CC         Evidence={ECO:0000250|UniProtKB:P80293};
CC       Note=Binds 1 Mn(2+) or Fe(3+) ion per subunit.
CC       {ECO:0000250|UniProtKB:P80293};
CC   -!- SUBUNIT: Homodimer. Can also form a heterodimer with SodA (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC       {ECO:0000305}.
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DR   EMBL; AJ938182; CAI79760.1; -; Genomic_DNA.
DR   RefSeq; WP_000874683.1; NC_007622.1.
DR   AlphaFoldDB; Q2YUU9; -.
DR   SMR; Q2YUU9; -.
DR   KEGG; sab:SAB0072; -.
DR   HOGENOM; CLU_031625_0_0_9; -.
DR   OMA; HNQFWEM; -.
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; 3.55.40.20; -; 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
FT                   /note="Superoxide dismutase [Mn/Fe] 2"
FT                   /id="PRO_0000293964"
FT   BINDING         27
FT                   /ligand="Fe(3+)"
FT                   /ligand_id="ChEBI:CHEBI:29034"
FT                   /evidence="ECO:0000250|UniProtKB:P80293"
FT   BINDING         27
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:P80293"
FT   BINDING         81
FT                   /ligand="Fe(3+)"
FT                   /ligand_id="ChEBI:CHEBI:29034"
FT                   /evidence="ECO:0000250|UniProtKB:P80293"
FT   BINDING         81
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:P80293"
FT   BINDING         161
FT                   /ligand="Fe(3+)"
FT                   /ligand_id="ChEBI:CHEBI:29034"
FT                   /evidence="ECO:0000250|UniProtKB:P80293"
FT   BINDING         161
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:P80293"
FT   BINDING         165
FT                   /ligand="Fe(3+)"
FT                   /ligand_id="ChEBI:CHEBI:29034"
FT                   /evidence="ECO:0000250|UniProtKB:P80293"
FT   BINDING         165
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:P80293"
SQ   SEQUENCE   199 AA;  23040 MW;  366B86F577A3C635 CRC64;
     MAFKLPNLPY AYDALEPYID QRTMEFHHDK HHNTYVTKLN ATVEGTELEH QSLADMIANL
     DKVPEAMRMS VRNNGGGHFN HSLFWEILSP NSEEKGGVID DIKAQWGTLD EFKNEFANKA
     TTLFGSGWTW LVVNNGKLEI VTTPNQDNPL TEGKTPILLF DVWEHAYYLK YQNKRPDYMT
     AFWNIVNWKK VDELYQAAK