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Database: UniProt
Entry: Q8VQ15
LinkDB: Q8VQ15
Original site: Q8VQ15 
ID   SODM_STAEP              Reviewed;         199 AA.
AC   Q8VQ15; Q54103; Q8VLL5;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   05-DEC-2018, entry version 61.
DE   RecName: Full=Superoxide dismutase [Mn/Fe];
DE            EC=1.15.1.1;
GN   Name=sodA;
OS   Staphylococcus epidermidis.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1282;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Chiou J., Yang C.-W., Chiou J.-F.;
RT   "Cloning, sequencing, and characterization of sodA gene from
RT   Staphylococcus epidermidis.";
RL   Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-68.
RC   STRAIN=BN 280;
RX   PubMed=8764488; DOI=10.1111/j.1574-6968.1996.tb08345.x;
RA   Heidrich C., Hantke K., Bierbaum G., Sahl H.-G.;
RT   "Identification and analysis of a gene encoding a Fur-like protein of
RT   Staphylococcus epidermidis.";
RL   FEMS Microbiol. Lett. 140:253-259(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 18-160, AND CATALYTIC ACTIVITY.
RC   STRAIN=ATCC 14990 / DSM 20044 / CIP 81.55, NEM2008, NEM2009, and
RC   NEM2010;
RX   PubMed=11724835; DOI=10.1128/JCM.39.12.4296-4301.2001;
RA   Poyart C., Quesne G., Boumaila C., Trieu-Cuot P.;
RT   "Rapid and accurate species-level identification of coagulase-negative
RT   staphylococci by using the sodA gene as a target.";
RL   J. Clin. Microbiol. 39:4296-4301(2001).
RN   [4]
RP   CATALYTIC ACTIVITY AS A SUPEROXIDE DISMUTASE.
RC   STRAIN=HAC111, HAC112, HAC113, HAC114, HAC115, HAC33, HAC36, and
RC   HAC94;
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).
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:11724835,
CC         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:0000250}.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000305}.
DR   EMBL; AF462457; AAL68691.1; -; Genomic_DNA.
DR   EMBL; X97011; CAA65734.1; -; Genomic_DNA.
DR   EMBL; AJ343906; CAC86481.1; -; Genomic_DNA.
DR   EMBL; AJ343946; CAC86528.1; -; Genomic_DNA.
DR   EMBL; AJ343947; CAC86529.1; -; Genomic_DNA.
DR   EMBL; AJ343948; CAC86530.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q8VQ15; -.
DR   SMR; Q8VQ15; -.
DR   eggNOG; ENOG4105CK4; Bacteria.
DR   eggNOG; COG0605; LUCA.
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   Iron; Manganese; Metal-binding; Oxidoreductase; Stress response.
FT   CHAIN         1    199       Superoxide dismutase [Mn/Fe].
FT                                /FTId=PRO_0000223465.
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}.
FT   CONFLICT     12     12       F -> Y (in Ref. 2; CAA65734).
FT                                {ECO:0000305}.
FT   CONFLICT     22     22       E -> Q (in Ref. 2 and 3). {ECO:0000305}.
FT   CONFLICT     41     42       AV -> SA (in Ref. 2 and 3).
FT                                {ECO:0000305}.
FT   CONFLICT     66     66       D -> N (in Ref. 3; CAC86481/CAC86528/
FT                                CAC86529/CAC86530). {ECO:0000305}.
FT   CONFLICT     89     89       T -> S (in Ref. 3; CAC86481/CAC86528/
FT                                CAC86529/CAC86530). {ECO:0000305}.
FT   CONFLICT    100    100       E -> D (in Ref. 3; CAC86481/CAC86528/
FT                                CAC86529/CAC86530). {ECO:0000305}.
FT   CONFLICT    150    150       L -> I (in Ref. 3; CAC86481/CAC86528/
FT                                CAC86529/CAC86530). {ECO:0000305}.
SQ   SEQUENCE   199 AA;  22706 MW;  36B438907574560F CRC64;
     MAFELPKLPY AFDALEPHID KETMEIHHDK HHNTYVTKLN AVVEGTDLEA KSIEEIVANL
     DSVPSDIQTA VRNNGGGHLN HSLFWELLTP NSEEKGEVVE KIKEQWGSLD EFKKEFADKA
     AARFGSGWAW LVVNNGQLEI VTTPNQDNPL TEGKTPILGL DVWEHAYYLK YQNKRPDYIS
     AFWNVVNWEK VDELYNAAK
//
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