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Database: UniProt
Entry: Q8P0D4
LinkDB: Q8P0D4
Original site: Q8P0D4 
ID   SODM_STRP8              Reviewed;         201 AA.
AC   Q8P0D4;
DT   25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   05-DEC-2018, entry version 96.
DE   RecName: Full=Superoxide dismutase [Mn];
DE            EC=1.15.1.1;
GN   Name=sodA; OrderedLocusNames=spyM18_1414;
OS   Streptococcus pyogenes serotype M18 (strain MGAS8232).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=186103;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGAS8232;
RX   PubMed=11917108; DOI=10.1073/pnas.062526099;
RA   Smoot J.C., Barbian K.D., Van Gompel J.J., Smoot L.M., Chaussee M.S.,
RA   Sylva G.L., Sturdevant D.E., Ricklefs S.M., Porcella S.F.,
RA   Parkins L.D., Beres S.B., Campbell D.S., Smith T.M., Zhang Q.,
RA   Kapur V., Daly J.A., Veasy L.G., Musser J.M.;
RT   "Genome sequence and comparative microarray analysis of serotype M18
RT   group A Streptococcus strains associated with acute rheumatic fever
RT   outbreaks.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:4668-4673(2002).
CC   -!- FUNCTION: Destroys superoxide anion radicals which are normally
CC       produced within the cells and which are toxic to biological
CC       systems.
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       Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000305}.
CC   -!- CAUTION: Although found extracellularly, no signal sequence is
CC       present. An alternative secretory pathway may be used.
CC       {ECO:0000305}.
DR   EMBL; AE009949; AAL98003.1; -; Genomic_DNA.
DR   RefSeq; WP_011017948.1; NC_003485.1.
DR   ProteinModelPortal; Q8P0D4; -.
DR   SMR; Q8P0D4; -.
DR   EnsemblBacteria; AAL98003; AAL98003; spyM18_1414.
DR   KEGG; spm:spyM18_1414; -.
DR   HOGENOM; HOG000013583; -.
DR   KO; K04564; -.
DR   OMA; YEGWKGE; -.
DR   BioCyc; SPYO186103:G1FZQ-1260-MONOMER; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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   Manganese; Metal-binding; Oxidoreductase; Secreted.
FT   INIT_MET      1      1       Removed. {ECO:0000250}.
FT   CHAIN         2    201       Superoxide dismutase [Mn].
FT                                /FTId=PRO_0000160104.
FT   METAL        27     27       Manganese. {ECO:0000250}.
FT   METAL        81     81       Manganese. {ECO:0000250}.
FT   METAL       163    163       Manganese. {ECO:0000250}.
FT   METAL       167    167       Manganese. {ECO:0000250}.
SQ   SEQUENCE   201 AA;  22653 MW;  7550586B0E7ED53F CRC64;
     MAIILPELPY AYDALEPQFD AETMSLHHDK HHATYVANTN AALEKHPEIG ENLEELLADV
     TKIPEDIRQA LINNGGGHLN HALFWELLSP EKQDVTPDVA QAIDDAFGSF DAFKEQFTAA
     ATGRFGSGWA WLVVNKEGQL EITSTANQDT PISEGKKPIL ALDVWEHAYY LNYRNVRPNY
     IKAFFEIINW KKVSELYQAA K
//
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