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Database: UniProt/SWISS-PROT
Entry: SODM_STRP6
LinkDB: SODM_STRP6
Original site: SODM_STRP6 
ID   SODM_STRP6              Reviewed;         201 AA.
AC   Q5XBF8;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-OCT-2017, entry version 82.
DE   RecName: Full=Superoxide dismutase [Mn];
DE            EC=1.15.1.1;
GN   Name=sodA; OrderedLocusNames=M6_Spy1120;
OS   Streptococcus pyogenes serotype M6 (strain ATCC BAA-946 / MGAS10394).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=286636;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-946 / MGAS10394;
RX   PubMed=15272401; DOI=10.1086/422697;
RA   Banks D.J., Porcella S.F., Barbian K.D., Beres S.B., Philips L.E.,
RA   Voyich J.M., DeLeo F.R., Martin J.M., Somerville G.A., Musser J.M.;
RT   "Progress toward characterization of the group A Streptococcus
RT   metagenome: complete genome sequence of a macrolide-resistant serotype
RT   M6 strain.";
RL   J. Infect. Dis. 190:727-738(2004).
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: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
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; CP000003; AAT87255.1; -; Genomic_DNA.
DR   RefSeq; WP_011184668.1; NC_006086.1.
DR   ProteinModelPortal; Q5XBF8; -.
DR   SMR; Q5XBF8; -.
DR   EnsemblBacteria; AAT87255; AAT87255; M6_Spy1120.
DR   KEGG; spa:M6_Spy1120; -.
DR   HOGENOM; HOG000013583; -.
DR   KO; K04564; -.
DR   OMA; DSPLMHG; -.
DR   Proteomes; UP000001167; Chromosome.
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   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; Manganese; Metal-binding; Oxidoreductase; Secreted.
FT   INIT_MET      1      1       Removed. {ECO:0000250}.
FT   CHAIN         2    201       Superoxide dismutase [Mn].
FT                                /FTId=PRO_0000160103.
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;  22651 MW;  4A719FAF1584F995 CRC64;
     MAIILPELPY AYDALEPQFD AETMTLHHDK HHATYVANAN AALEKHPEIG ENLEELLADV
     TKIPEDIRQA LINNGGGHLN HALFWELLSP EKQDITPDVA QAIDDAFGSF DAFKEQFTAA
     ATGRFGSGWA WLVVNKEGQL EITSTANQDT PISEGKKPIL ALDVWEHAYY LNYRNVRPNY
     IKAFFEIINW KKVSELYQAA K
//
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