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Database: UniProt
Entry: Q2FGH0
LinkDB: Q2FGH0
Original site: Q2FGH0 
ID   SODM1_STAA3             Reviewed;         199 AA.
AC   Q2FGH0;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   05-DEC-2018, entry version 71.
DE   RecName: Full=Superoxide dismutase [Mn/Fe] 1;
DE            EC=1.15.1.1;
GN   Name=sodA; OrderedLocusNames=SAUSA300_1513;
OS   Staphylococcus aureus (strain USA300).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=367830;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=USA300;
RX   PubMed=16517273; DOI=10.1016/S0140-6736(06)68231-7;
RA   Diep B.A., Gill S.R., Chang R.F., Phan T.H., Chen J.H., Davidson M.G.,
RA   Lin F., Lin J., Carleton H.A., Mongodin E.F., Sensabaugh G.F.,
RA   Perdreau-Remington F.;
RT   "Complete genome sequence of USA300, an epidemic clone of community-
RT   acquired meticillin-resistant Staphylococcus aureus.";
RL   Lancet 367:731-739(2006).
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; CP000255; ABD22195.1; -; Genomic_DNA.
DR   RefSeq; WP_000863556.1; NZ_CP027476.1.
DR   ProteinModelPortal; Q2FGH0; -.
DR   SMR; Q2FGH0; -.
DR   PRIDE; Q2FGH0; -.
DR   EnsemblBacteria; ABD22195; ABD22195; SAUSA300_1513.
DR   KEGG; saa:SAUSA300_1513; -.
DR   HOGENOM; HOG000013583; -.
DR   KO; K04564; -.
DR   OMA; KWGSFDK; -.
DR   Proteomes; UP000001939; 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] 1.
FT                                /FTId=PRO_0000293962.
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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