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Database: UniProt/TrEMBL
Entry: Q1J5Y1_STRPF
LinkDB: Q1J5Y1_STRPF
Original site: Q1J5Y1_STRPF 
ID   Q1J5Y1_STRPF            Unreviewed;       201 AA.
AC   Q1J5Y1;
DT   13-JUN-2006, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2006, sequence version 1.
DT   25-OCT-2017, entry version 74.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   Name=sodA {ECO:0000313|EMBL:ABF38202.1};
GN   OrderedLocusNames=MGAS10750_Spy1252 {ECO:0000313|EMBL:ABF38202.1};
OS   Streptococcus pyogenes serotype M4 (strain MGAS10750).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=370554 {ECO:0000313|EMBL:ABF38202.1, ECO:0000313|Proteomes:UP000002434};
RN   [1] {ECO:0000313|EMBL:ABF38202.1, ECO:0000313|Proteomes:UP000002434}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGAS10750 {ECO:0000313|EMBL:ABF38202.1,
RC   ECO:0000313|Proteomes:UP000002434};
RX   PubMed=16636287; DOI=10.1073/pnas.0510279103;
RA   Beres S.B., Richter E.W., Nagiec M.J., Sumby P., Porcella S.F.,
RA   DeLeo F.R., Musser J.M.;
RT   "Molecular genetic anatomy of inter- and intraserotype variation in
RT   the human bacterial pathogen group A Streptococcus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:7059-7064(2006).
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems.
CC       {ECO:0000256|RuleBase:RU000414}.
CC   -!- CATALYTIC ACTIVITY: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
CC       {ECO:0000256|RuleBase:RU000414}.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000256|RuleBase:RU000414}.
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DR   EMBL; CP000262; ABF38202.1; -; Genomic_DNA.
DR   RefSeq; WP_002983977.1; NC_008024.1.
DR   ProteinModelPortal; Q1J5Y1; -.
DR   EnsemblBacteria; ABF38202; ABF38202; MGAS10750_Spy1252.
DR   KEGG; spi:MGAS10750_Spy1252; -.
DR   HOGENOM; HOG000013583; -.
DR   KO; K04564; -.
DR   OMA; DSPLMHG; -.
DR   OrthoDB; POG091H03Q7; -.
DR   Proteomes; UP000002434; Chromosome.
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 {ECO:0000313|Proteomes:UP000002434};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414,
KW   ECO:0000313|EMBL:ABF38202.1}.
FT   DOMAIN        5     89       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       98    195       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        27     27       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        81     81       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       163    163       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       167    167       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   201 AA;  22667 MW;  77005A39597B806F CRC64;
     MAIILPELPY AYDALEPQFD AETMTLHHDK HHATYVANTN AALEKHPEIG ENLEELLADV
     TKIPEDIRQA LINNGGGHLN HALFWELLSP EKQDVTPDVA QAIDDAFGSF DAFKEQFTAA
     ATGRFGSGWA WLVVNKEGQL EITSTANQDT PISEGKKPIL ALDVWEHAYY LNYRNVRPNY
     IKAFFEIINW KKVSELYQAA K
//
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