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Database: UniProt/TrEMBL
Entry: Q5WSI1_LEGPL
LinkDB: Q5WSI1_LEGPL
Original site: Q5WSI1_LEGPL 
ID   Q5WSI1_LEGPL            Unreviewed;       192 AA.
AC   Q5WSI1;
DT   23-NOV-2004, integrated into UniProtKB/TrEMBL.
DT   23-NOV-2004, sequence version 1.
DT   05-JUL-2017, entry version 85.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   Name=sodB {ECO:0000313|EMBL:CAH17141.1};
GN   OrderedLocusNames=lpl2897 {ECO:0000313|EMBL:CAH17141.1};
OS   Legionella pneumophila (strain Lens).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=297245 {ECO:0000313|EMBL:CAH17141.1, ECO:0000313|Proteomes:UP000002517};
RN   [1] {ECO:0000313|EMBL:CAH17141.1, ECO:0000313|Proteomes:UP000002517}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lens {ECO:0000313|EMBL:CAH17141.1,
RC   ECO:0000313|Proteomes:UP000002517};
RX   PubMed=15467720; DOI=10.1038/ng1447;
RA   Cazalet C., Rusniok C., Bruggemann H., Zidane N., Magnier A., Ma L.,
RA   Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F.,
RA   Etienne J., Glaser P., Buchrieser C.;
RT   "Evidence in the Legionella pneumophila genome for exploitation of
RT   host cell functions and high genome plasticity.";
RL   Nat. Genet. 36:1165-1173(2004).
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; CR628337; CAH17141.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q5WSI1; -.
DR   EnsemblBacteria; CAH17141; CAH17141; lpl2897.
DR   KEGG; lpf:lpl2897; -.
DR   LegioList; lpl2897; -.
DR   HOGENOM; HOG000013584; -.
DR   KO; K04564; -.
DR   OMA; DHHGNVG; -.
DR   Proteomes; UP000002517; 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   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:UP000002517};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414}.
FT   DOMAIN        2     82       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       89    189       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        27     27       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        74     74       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       157    157       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       161    161       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   192 AA;  21639 MW;  D4CD16B580C646C9 CRC64;
     MTFTLPQLPY ALDALAPHVS KETLEYHYGK HHNTYVTNLN KLIPGTEFES MTLEEIIMKA
     KGGIFNNAAQ VWNHTFYWHS MSPNGGGEPK GRLAEAINKN FGSFAAFKEQ FSQTAATTFG
     SGWAWLVQDQ SGALKIISTS NAGTPMTEGL NALLTCDVWE HAYYIDYRNR RPDYIEAFWS
     LVNWDFASSN LK
//
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