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Database: UniProt/TrEMBL
Entry: K9RPN8_SYNP3
LinkDB: K9RPN8_SYNP3
Original site: K9RPN8_SYNP3 
ID   K9RPN8_SYNP3            Unreviewed;       229 AA.
AC   K9RPN8;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   25-OCT-2017, entry version 25.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   OrderedLocusNames=Syn6312_0675 {ECO:0000313|EMBL:AFY59895.1};
OS   Synechococcus sp. (strain ATCC 27167 / PCC 6312).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=195253 {ECO:0000313|EMBL:AFY59895.1, ECO:0000313|Proteomes:UP000010379};
RN   [1] {ECO:0000313|Proteomes:UP000010379}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27167 / PCC 6312 {ECO:0000313|Proteomes:UP000010379};
RX   PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA   Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E.,
RA   Calteau A., Cai F., Tandeau de Marsac N., Rippka R., Herdman M.,
RA   Sivonen K., Coursin T., Laurent T., Goodwin L., Nolan M.,
RA   Davenport K.W., Han C.S., Rubin E.M., Eisen J.A., Woyke T., Gugger M.,
RA   Kerfeld C.A.;
RT   "Improving the coverage of the cyanobacterial phylum using diversity-
RT   driven genome sequencing.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
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; CP003558; AFY59895.1; -; Genomic_DNA.
DR   RefSeq; WP_015123439.1; NC_019680.1.
DR   EnsemblBacteria; AFY59895; AFY59895; Syn6312_0675.
DR   KEGG; syne:Syn6312_0675; -.
DR   PATRIC; fig|195253.3.peg.706; -.
DR   KO; K04564; -.
DR   OrthoDB; POG091H03Q7; -.
DR   BioCyc; SSP195253:GLM1-650-MONOMER; -.
DR   Proteomes; UP000010379; 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:UP000010379};
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:UP000010379};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     20       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        21    229       Superoxide dismutase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5003935212.
FT   DOMAIN       28    115       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN      122    223       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        52     52       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       107    107       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       190    190       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       194    194       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   229 AA;  25792 MW;  B40A09CE97591644 CRC64;
     MVWCSTALAS WALFPPKTLA ASSPTGVYVL PPLPYAYNAL EPYIDAETME FHHDKHHAAY
     VNNLNAALQK YPQWSGLRIE ELLEKLDQLP NDIRQTVRNN GGGHANHSLF WESMSPAAGG
     KPRGKLATAM QARFGSFEDF QAQFNSAGLK QFGSGWVWLG LGQDGTLQVF TTPNQDSPLS
     QGITPLLGND VWEHAYYLSY RNRRDQYLQA WWNVVNWDKI GERYEQATG
//
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