ID   SODM_STACA              Reviewed;         201 AA.
AC   Q9F326; Q5IBS1;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Superoxide dismutase [Mn/Fe];
DE            EC=1.15.1.1 {ECO:0000250|UniProtKB:P80293};
GN   Name=sodA; Synonyms=sod;
OS   Staphylococcus carnosus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1281;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=833;
RX   PubMed=11556918; DOI=10.1046/j.1365-2672.2001.01411.x;
RA   Barriere C., Leroy-Setrin S., Talon R.;
RT   "Characterization of catalase and superoxide dismutase in Staphylococcus
RT   carnosus 833 strain.";
RL   J. Appl. Microbiol. 91:514-519(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 18-161.
RC   STRAIN=CIT S00-298;
RX   PubMed=16488037; DOI=10.1016/j.ijfoodmicro.2005.12.006;
RA   Corbiere Morot-Bizot S., Leroy S., Talon R.;
RT   "Staphylococcal community of a small unit manufacturing traditional dry
RT   fermented sausages.";
RL   Int. J. Food Microbiol. 108:210-217(2006).
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. {ECO:0000250}.
CC   -!- MISCELLANEOUS: SOD activity increases in mid-exponential growth-phase.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC       {ECO:0000305}.
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DR   EMBL; AJ295150; CAC14833.1; -; Genomic_DNA.
DR   EMBL; AY795886; AAW32466.1; -; Genomic_DNA.
DR   RefSeq; WP_015900423.1; NZ_LISV01000002.1.
DR   AlphaFoldDB; Q9F326; -.
DR   SMR; Q9F326; -.
DR   GeneID; 60545135; -.
DR   PATRIC; fig|1281.6.peg.252; -.
DR   OMA; KWGSFDK; -.
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..201
FT                   /note="Superoxide dismutase [Mn/Fe]"
FT                   /id="PRO_0000293968"
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         162
FT                   /ligand="Fe(3+)"
FT                   /ligand_id="ChEBI:CHEBI:29034"
FT                   /evidence="ECO:0000250|UniProtKB:P80293"
FT   BINDING         162
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:P80293"
FT   BINDING         166
FT                   /ligand="Fe(3+)"
FT                   /ligand_id="ChEBI:CHEBI:29034"
FT                   /evidence="ECO:0000250|UniProtKB:P80293"
FT   BINDING         166
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:P80293"
SQ   SEQUENCE   201 AA;  22980 MW;  4F23EF7BF19556A4 CRC64;
     MAFELPNLPY EFDALEPYID KETMEIHHDK HHNTYVTKLN AAIEGTDLEN KSIEEIVANL
     DSVPSDIQTA VRNNGGGHLN HSLFWQLLTP NSEEKGTVID KIKEEWGSLD KFKDEFAKKA
     AGQFGSGWAW LVVDKDGKLE IVSTPNQDNP ITEGKTPILG LDVWEHAYYL KYQNKRPDYI
     DAFWNVVNWN KVDELYEAAT K