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Database: UniProt
Entry: Q68WK0
LinkDB: Q68WK0
Original site: Q68WK0 
ID   SODF_RICTY              Reviewed;         209 AA.
AC   Q68WK0;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   16-JAN-2019, entry version 80.
DE   RecName: Full=Superoxide dismutase [Mn/Fe];
DE            EC=1.15.1.1;
GN   Name=sodB; OrderedLocusNames=RT0523;
OS   Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=257363;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-144 / Wilmington;
RX   PubMed=15317790; DOI=10.1128/JB.186.17.5842-5855.2004;
RA   McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K.,
RA   Fox G.E., McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C.,
RA   Sodergren E., Gill R., Hume J., Morgan M., Fan G., Amin A.G.,
RA   Gibbs R.A., Hong C., Yu X.-J., Walker D.H., Weinstock G.M.;
RT   "Complete genome sequence of Rickettsia typhi and comparison with
RT   sequences of other Rickettsiae.";
RL   J. Bacteriol. 186:5842-5855(2004).
CC   -!- FUNCTION: Destroys superoxide anion radicals which are normally
CC       produced within the cells and which are toxic to biological
CC       systems.
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   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250};
CC       Note=Binds 1 Mn(2+) or Fe(2+) ion per subunit. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000305}.
DR   EMBL; AE017197; AAU03992.1; -; Genomic_DNA.
DR   RefSeq; WP_011190973.1; NC_006142.1.
DR   ProteinModelPortal; Q68WK0; -.
DR   SMR; Q68WK0; -.
DR   STRING; 257363.RT0523; -.
DR   PRIDE; Q68WK0; -.
DR   EnsemblBacteria; AAU03992; AAU03992; RT0523.
DR   KEGG; rty:RT0523; -.
DR   eggNOG; ENOG4105CK4; Bacteria.
DR   eggNOG; COG0605; LUCA.
DR   HOGENOM; HOG000013584; -.
DR   KO; K04564; -.
DR   OMA; KWGSFDK; -.
DR   OrthoDB; 1440645at2; -.
DR   BioCyc; RTYP257363:G1G0L-530-MONOMER; -.
DR   Proteomes; UP000000604; Chromosome.
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; Iron; Manganese; Metal-binding; Oxidoreductase.
FT   CHAIN         1    209       Superoxide dismutase [Mn/Fe].
FT                                /FTId=PRO_0000286503.
FT   METAL        38     38       Manganese or iron. {ECO:0000250}.
FT   METAL        90     90       Manganese or iron. {ECO:0000250}.
FT   METAL       172    172       Manganese or iron. {ECO:0000250}.
FT   METAL       176    176       Manganese or iron. {ECO:0000250}.
SQ   SEQUENCE   209 AA;  24737 MW;  1EB8AB024554EB8A CRC64;
     MTYCRKANQT SYPFILPDLP YAKESFKPHF TCETFDYHHG KHHNSYVQNL NNLLKDREEL
     QKKDLEGIIK WSSKNSEVTV FNNASQIWNH TFFWYSIKPH GGGKPSGKVF EQISQDFGSF
     EQFCEQFKQE ALGQFGSGWV WVVYNNNKLQ IIKTSNADTP IVNLMKPILV CDVWEHAYYI
     DYRNKRSDYI DIFISHMINW KFVEDNLIQ
//
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