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Database: UniProt
Entry: I7WJU2_STRCB
LinkDB: I7WJU2_STRCB
Original site: I7WJU2_STRCB 
ID   I7WJU2_STRCB            Unreviewed;       201 AA.
AC   I7WJU2;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   16-JAN-2019, entry version 28.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=SCAZ3_07795 {ECO:0000313|EMBL:EIQ82250.1};
OS   Streptococcus canis FSL Z3-227.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=482234 {ECO:0000313|EMBL:EIQ82250.1, ECO:0000313|Proteomes:UP000004423};
RN   [1] {ECO:0000313|EMBL:EIQ82250.1, ECO:0000313|Proteomes:UP000004423}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSL Z3-227 {ECO:0000313|EMBL:EIQ82250.1,
RC   ECO:0000313|Proteomes:UP000004423};
RX   PubMed=22666370; DOI=10.1371/journal.pone.0037607;
RA   Lefebure T., Richards V.P., Lang P., Pavinski-Bitar P., Stanhope M.J.;
RT   "Gene Repertoire Evolution of Streptococcus pyogenes Inferred from
RT   Phylogenomic Analysis with Streptococcus canis and Streptococcus
RT   dysgalactiae.";
RL   PLoS ONE 7:E37607-E37607(2012).
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:
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:0000256|RuleBase:RU000414};
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000256|RuleBase:RU000414}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EIQ82250.1}.
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DR   EMBL; AIDX01000001; EIQ82250.1; -; Genomic_DNA.
DR   RefSeq; WP_003044189.1; NZ_AIDX01000001.2.
DR   EnsemblBacteria; EIQ82250; EIQ82250; SCAZ3_07795.
DR   PATRIC; fig|482234.3.peg.204; -.
DR   BioCyc; SCAN482234:G129Y-168-MONOMER; -.
DR   Proteomes; UP000004423; Unassembled WGS sequence.
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 {ECO:0000313|Proteomes:UP000004423};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414}.
FT   DOMAIN        5     89       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       97    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;  22594 MW;  404A46CEAB345691 CRC64;
     MAIILPELPY AYDALEPQFD AETMTLHHDK HHATYVANAN AALEKHPEIG ENLKELLADV
     TKIPADIRQA LINNGGGHLN HALFWELLSP EKQEITADVA QAIDEAFGSF DAFKEQFTAA
     ATGRFGSGWA WLVVNKEGQL EITSTANQDT PISEGKKPIL ALDVWEHAYY LNYRNVRPNY
     IKAFFEIINW KKVSELYQAA K
//
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