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Database: UniProt
Entry: P0C0Q6
LinkDB: P0C0Q6
Original site: P0C0Q6 
ID   SODM_STAES              Reviewed;         199 AA.
AC   P0C0Q6; P0C0Q5; Q93CF4;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   05-DEC-2018, entry version 78.
DE   RecName: Full=Superoxide dismutase [Mn/Fe];
DE            EC=1.15.1.1;
GN   Name=sodA; OrderedLocusNames=SE_1240;
OS   Staphylococcus epidermidis (strain ATCC 12228).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], ENZYMATIC ACTIVITY, AND SUBUNIT.
RX   PubMed=11948161; DOI=10.1128/JB.184.9.2465-2472.2002;
RA   Wright Valderas M., Gatson J.W., Wreyford N., Hart M.E.;
RT   "The superoxide dismutase gene sodM is unique to Staphylococcus
RT   aureus: absence of sodM in coagulase-negative staphylococci.";
RL   J. Bacteriol. 184:2465-2472(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12228;
RX   PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA   Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J.,
RA   Qin Z.-Q., Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z.,
RA   Yuan Z.-H., Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT   "Genome-based analysis of virulence genes in a non-biofilm-forming
RT   Staphylococcus epidermidis strain (ATCC 12228).";
RL   Mol. Microbiol. 49:1577-1593(2003).
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         Evidence={ECO:0000269|PubMed:11948161};
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. {ECO:0000269|PubMed:11948161}.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000305}.
DR   EMBL; AF410177; AAL09677.1; -; Genomic_DNA.
DR   EMBL; AE015929; AAO04839.1; -; Genomic_DNA.
DR   RefSeq; NP_764795.1; NC_004461.1.
DR   RefSeq; WP_001831217.1; NC_004461.1.
DR   ProteinModelPortal; P0C0Q6; -.
DR   SMR; P0C0Q6; -.
DR   STRING; 176280.SE1240; -.
DR   EnsemblBacteria; AAO04839; AAO04839; SE_1240.
DR   GeneID; 1057028; -.
DR   KEGG; sep:SE1240; -.
DR   PATRIC; fig|176280.10.peg.1208; -.
DR   eggNOG; ENOG4105CK4; Bacteria.
DR   eggNOG; COG0605; LUCA.
DR   KO; K04564; -.
DR   OMA; KWGSFDK; -.
DR   BioCyc; SEPI176280:G1G05-1246-MONOMER; -.
DR   Proteomes; UP000001411; 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   1: Evidence at protein level;
KW   Complete proteome; Iron; Manganese; Metal-binding; Oxidoreductase;
KW   Stress response.
FT   CHAIN         1    199       Superoxide dismutase [Mn/Fe].
FT                                /FTId=PRO_0000160077.
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;  22722 MW;  E25419284F3378DD CRC64;
     MAFELPNLPY AYDALEPHID KQTMEIHHDK HHNTYVTKLN SAVEGTDLEA KSIEEIVANL
     DSVPSNIQTA VRNNGGGHLN HSLFWELLSP NSEEKGEVVD KIKEQWGSLD EFKKEFADKA
     AARFGSGWAW LVVNNGQLEI VTTPNQDNPI TEGKTPILGL DVWEHAYYLK YQNKRPDYIN
     AFWNVVNWEK VNELYNATK
//
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