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Database: UniProt/TrEMBL
Entry: F8HDW8_STRE5
LinkDB: F8HDW8_STRE5
Original site: F8HDW8_STRE5 
ID   F8HDW8_STRE5            Unreviewed;       201 AA.
AC   F8HDW8;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   25-OCT-2017, entry version 32.
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:AEJ53670.1};
GN   OrderedLocusNames=Ssal_01389 {ECO:0000313|EMBL:AEJ53670.1};
OS   Streptococcus salivarius (strain 57.I).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1046629 {ECO:0000313|EMBL:AEJ53670.1, ECO:0000313|Proteomes:UP000000293};
RN   [1] {ECO:0000313|EMBL:AEJ53670.1, ECO:0000313|Proteomes:UP000000293}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=57.I {ECO:0000313|EMBL:AEJ53670.1,
RC   ECO:0000313|Proteomes:UP000000293};
RX   PubMed=21914897; DOI=10.1128/JB.05670-11;
RA   Geng J., Huang S.C., Li S., Hu S., Chen Y.Y.;
RT   "Complete genome sequence of the ureolytic Streptococcus salivarius
RT   strain 57.I.";
RL   J. Bacteriol. 193:5596-5597(2011).
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; CP002888; AEJ53670.1; -; Genomic_DNA.
DR   STRING; 1046629.Ssal_01389; -.
DR   EnsemblBacteria; AEJ53670; AEJ53670; Ssal_01389.
DR   KEGG; stf:Ssal_01389; -.
DR   PATRIC; fig|1046629.4.peg.1224; -.
DR   eggNOG; ENOG4105CK4; Bacteria.
DR   eggNOG; COG0605; LUCA.
DR   KO; K04564; -.
DR   OMA; KWGSFDK; -.
DR   BioCyc; SSAL1046629:GLLG-1257-MONOMER; -.
DR   Proteomes; UP000000293; 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:UP000000293};
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       95    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;  22320 MW;  15B0C21169C11306 CRC64;
     MAIILPDLPY AYDALEPYID AETMTLHHDK HHATYVANAN AALEKHPEIG EDLEALLADV
     EQIPADIRQA LINNGGGHLN HALFWELLSP EKQEPTAEVA AAINEAFGSF EAFQEAFTAA
     ATTRFGSGWA WLVVNAEGKL EVVSTANQDT PISDGKKPIL ALDVWEHAYY LNYRNVRPNY
     IKAFFEIINW NKVAELYAAA K
//
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