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Database: UniProt/TrEMBL
Entry: A4VWL6_STRSY
LinkDB: A4VWL6_STRSY
Original site: A4VWL6_STRSY 
ID   A4VWL6_STRSY            Unreviewed;       189 AA.
AC   A4VWL6;
DT   29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2007, sequence version 1.
DT   25-OCT-2017, entry version 65.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   OrderedLocusNames=SSU05_1539 {ECO:0000313|EMBL:ABP90505.1};
OS   Streptococcus suis (strain 05ZYH33).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=391295 {ECO:0000313|EMBL:ABP90505.1, ECO:0000313|Proteomes:UP000000243};
RN   [1] {ECO:0000313|EMBL:ABP90505.1, ECO:0000313|Proteomes:UP000000243}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=05ZYH33 {ECO:0000313|EMBL:ABP90505.1,
RC   ECO:0000313|Proteomes:UP000000243};
RX   PubMed=17375201; DOI=10.1371/journal.pone.0000315;
RG   BGI;
RA   Chen C., Tang J., Dong W., Wang C., Feng Y., Wang J., Zheng F.,
RA   Pan X., Liu D., Li M., Song Y., Zhu X., Sun H., Feng T., Guo Z.,
RA   Ju A., Ge J., Dong Y., Sun W., Jiang Y., Wang J., Yan J., Yang H.,
RA   Wang X., Gao G.F., Yang R., Wang J., Yu J.;
RT   "A glimpse of streptococcal toxic shock syndrome from comparative
RT   genomics of S. suis 2 Chinese isolates.";
RL   PLoS ONE 2:E315-E315(2007).
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; CP000407; ABP90505.1; -; Genomic_DNA.
DR   STRING; 391295.SSU05_1539; -.
DR   EnsemblBacteria; ABP90505; ABP90505; SSU05_1539.
DR   KEGG; ssu:SSU05_1539; -.
DR   eggNOG; ENOG4105CK4; Bacteria.
DR   eggNOG; COG0605; LUCA.
DR   HOGENOM; HOG000013583; -.
DR   KO; K04564; -.
DR   OMA; KWGSFDK; -.
DR   OrthoDB; POG091H03Q7; -.
DR   BioCyc; SSUI391295:GHI8-1593-MONOMER; -.
DR   Proteomes; UP000000243; 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:UP000000243};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000243}.
FT   DOMAIN        3     77       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       85    183       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        15     15       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        69     69       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       151    151       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       155    155       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   189 AA;  21130 MW;  D5D6F8375E2BA9F4 CRC64;
     MPLEPHIDAE TMTLHHDKHH ATYVANANAA LEKHPEIGED LVALLSDVEQ IPSDIRQALI
     NNGGGHLNHA LFWELLSPEK TEISAELAAD IDATFGSFDA FKEAFTAAAT TRFGSGWAFL
     VVNKEGKLEV ISTANQDTPI MQGLKPILAL DVWEHAYYLN YRNVRPNYIK AFFEVINWDK
     VNELYKAAK
//
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