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Database: UniProt/TrEMBL
Entry: B1LE68_ECOSM
LinkDB: B1LE68_ECOSM
Original site: B1LE68_ECOSM 
ID   B1LE68_ECOSM            Unreviewed;       174 AA.
AC   B1LE68;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   07-JUN-2017, entry version 65.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   Name=sodC_2 {ECO:0000313|EMBL:ACB16536.1};
GN   OrderedLocusNames=EcSMS35_3163 {ECO:0000313|EMBL:ACB16536.1};
OS   Escherichia coli (strain SMS-3-5 / SECEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=439855 {ECO:0000313|EMBL:ACB16536.1, ECO:0000313|Proteomes:UP000007011};
RN   [1] {ECO:0000313|EMBL:ACB16536.1, ECO:0000313|Proteomes:UP000007011}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SMS-3-5 / SECEC {ECO:0000313|Proteomes:UP000007011};
RX   PubMed=18708504; DOI=10.1128/JB.00661-08;
RA   Fricke W.F., Wright M.S., Lindell A.H., Harkins D.M., Baker-Austin C.,
RA   Ravel J., Stepanauskas R.;
RT   "Insights into the environmental resistance gene pool from the genome
RT   sequence of the multidrug-resistant environmental isolate Escherichia
RT   coli SMS-3-5.";
RL   J. Bacteriol. 190:6779-6794(2008).
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems.
CC       {ECO:0000256|RuleBase:RU000393}.
CC   -!- CATALYTIC ACTIVITY: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
CC       {ECO:0000256|RuleBase:RU000393}.
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC         Evidence={ECO:0000256|RuleBase:RU000393};
CC       Note=Binds 1 copper ion per subunit.
CC       {ECO:0000256|RuleBase:RU000393};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU000393};
CC       Note=Binds 1 zinc ion per subunit.
CC       {ECO:0000256|RuleBase:RU000393};
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000256|RuleBase:RU000393}.
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DR   EMBL; CP000970; ACB16536.1; -; Genomic_DNA.
DR   RefSeq; WP_000823671.1; NC_010498.1.
DR   ProteinModelPortal; B1LE68; -.
DR   EnsemblBacteria; ACB16536; ACB16536; EcSMS35_3163.
DR   KEGG; ecm:EcSMS35_3163; -.
DR   HOGENOM; HOG000263449; -.
DR   KO; K04565; -.
DR   OMA; SIGKIMI; -.
DR   Proteomes; UP000007011; Chromosome.
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; IPR018152; SOD_Cu/Zn_BS.
DR   InterPro; IPR001424; SOD_Cu_Zn_dom.
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   Complete proteome {ECO:0000313|Proteomes:UP000007011};
KW   Copper {ECO:0000256|RuleBase:RU000393};
KW   Metal-binding {ECO:0000256|RuleBase:RU000393};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000393,
KW   ECO:0000313|EMBL:ACB16536.1}; Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   SIGNAL        1     19       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        20    174       Superoxide dismutase [Cu-Zn].
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5002767397.
FT   DOMAIN       34    173       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   174 AA;  18328 MW;  C39CDAD54E4462E1 CRC64;
     MKRKLIAFVI LATSSCGYAA TKDVTMNLVD SDGKERNIGK ITIQKTPYGL LFTPDLHSLP
     AGIHGFHVHE NASCAPALKD GKTVAALSAG GHFDPEKTGK HLGPWSPDGH LGDLPALYVT
     HDGKATYPVL APRLSELKEL DGRSLMLHAG GDNHDDHPEP LGGGGARIAC GIIP
//
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