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Database: UniProt/SWISS-PROT
Entry: SODC1_SALT4
LinkDB: SODC1_SALT4
Original site: SODC1_SALT4 
ID   SODC1_SALT4             Reviewed;         177 AA.
AC   E8XDJ8; O33803; O50545; P53636;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-APR-2011, sequence version 1.
DT   16-JAN-2019, entry version 44.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] 1;
DE            EC=1.15.1.1;
DE   AltName: Full=sodCI;
DE   Flags: Precursor;
GN   Name=sodC1; Synonyms=sodC; OrderedLocusNames=STM474_1035;
OS   Salmonella typhimurium (strain 4/74).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=909946;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=4/74;
RX   PubMed=9379906; DOI=10.1046/j.1365-2958.1997.5151877.x;
RA   Farrant J.L., Sansone A., Canvin J.R., Pallen M.J., Langford P.R.,
RA   Wallis T.S., Dougan G., Kroll J.S.;
RT   "Bacterial copper- and zinc-cofactored superoxide dismutase
RT   contributes to the pathogenesis of systemic salmonellosis.";
RL   Mol. Microbiol. 25:785-796(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4/74;
RX   PubMed=21478351; DOI=10.1128/JB.00394-11;
RA   Richardson E.J., Limaye B., Inamdar H., Datta A., Manjari K.S.,
RA   Pullinger G.D., Thomson N.R., Joshi R.R., Watson M., Stevens M.P.;
RT   "Genome sequences of Salmonella enterica serovar typhimurium,
RT   Choleraesuis, Dublin, and Gallinarum strains of well- defined
RT   virulence in food-producing animals.";
RL   J. Bacteriol. 193:3162-3163(2011).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 77-163.
RC   STRAIN=4/74;
RX   PubMed=8869506; DOI=10.1111/j.1574-6968.1996.tb08052.x;
RA   Canvin J., Langford P.R., Wilks K.E., Kroll J.S.;
RT   "Identification of sodC encoding periplasmic [Cu,Zn]-superoxide
RT   dismutase in Salmonella.";
RL   FEMS Microbiol. Lett. 136:215-220(1996).
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological 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=Cu cation; Xref=ChEBI:CHEBI:23378;
CC       Note=Binds 1 copper ion per subunit.;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC       Note=Binds 1 zinc ion per subunit.;
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Periplasm.
CC   -!- MISCELLANEOUS: Encoded by a cryptic bacteriophage.
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000305}.
DR   EMBL; Y13121; CAA73588.1; -; Genomic_DNA.
DR   EMBL; CP002487; ADX16741.1; -; Genomic_DNA.
DR   EMBL; X94327; CAA63988.1; -; Genomic_DNA.
DR   RefSeq; WP_000877926.1; NC_016857.1.
DR   ProteinModelPortal; E8XDJ8; -.
DR   SMR; E8XDJ8; -.
DR   PRIDE; E8XDJ8; -.
DR   EnsemblBacteria; ADX16741; ADX16741; STM474_1035.
DR   KEGG; seb:STM474_1035; -.
DR   PATRIC; fig|909946.3.peg.1066; -.
DR   KO; K04565; -.
DR   OMA; SIGKIMI; -.
DR   BioCyc; SENT909946:G1GRD-1074-MONOMER; -.
DR   Proteomes; UP000008978; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR   CDD; cd00305; Cu-Zn_Superoxide_Dismutase; 1.
DR   Gene3D; 2.60.40.200; -; 1.
DR   InterPro; IPR036423; SOD-like_Cu/Zn_dom_sf.
DR   InterPro; IPR024134; SOD_Cu/Zn_/chaperone.
DR   InterPro; IPR018152; SOD_Cu/Zn_BS.
DR   InterPro; IPR001424; SOD_Cu_Zn_dom.
DR   PANTHER; PTHR10003; PTHR10003; 1.
DR   Pfam; PF00080; Sod_Cu; 1.
DR   SUPFAM; SSF49329; SSF49329; 1.
DR   PROSITE; PS00332; SOD_CU_ZN_2; 1.
PE   3: Inferred from homology;
KW   Antioxidant; Complete proteome; Copper; Disulfide bond; Metal-binding;
KW   Oxidoreductase; Periplasm; Signal; Zinc.
FT   SIGNAL        1     20       {ECO:0000255}.
FT   CHAIN        21    177       Superoxide dismutase [Cu-Zn] 1.
FT                                /FTId=PRO_0000408966.
FT   METAL        69     69       Copper; catalytic. {ECO:0000250}.
FT   METAL        71     71       Copper; catalytic. {ECO:0000250}.
FT   METAL        94     94       Copper; catalytic. {ECO:0000250}.
FT   METAL        94     94       Zinc; structural. {ECO:0000250}.
FT   METAL       103    103       Zinc; structural. {ECO:0000250}.
FT   METAL       112    112       Zinc; structural. {ECO:0000250}.
FT   METAL       115    115       Zinc; structural. {ECO:0000250}.
FT   METAL       150    150       Copper; catalytic. {ECO:0000250}.
FT   DISULFID     76    172       {ECO:0000250}.
FT   CONFLICT    148    148       M -> T (in Ref. 3; CAA63988).
FT                                {ECO:0000305}.
SQ   SEQUENCE   177 AA;  18370 MW;  1EC743EE2AB38CAE CRC64;
     MKYTILSLVA GALISCSAMA ENTLTVKMND ALSSGTGENI GEITVSETPY GLLFTPHLNG
     LTPGIHGFHV HTNPSCMPGM KDGKEVPALM AGGHLDPEKT GKHLGPYNDK GHLGDLPGLV
     VNADGTATYP LLAPRLKSLS ELKGHSLMIH KGGDNYSDKP APLGGGGARF ACGVIEK
//
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