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Database: UniProt/TrEMBL
Entry: D3QX02_ECOCB
LinkDB: D3QX02_ECOCB
Original site: D3QX02_ECOCB 
ID   D3QX02_ECOCB            Unreviewed;       328 AA.
AC   D3QX02;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   28-FEB-2018, entry version 46.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   OrderedLocusNames=G2583_2433 {ECO:0000313|EMBL:ADD56991.1};
OS   Escherichia coli O55:H7 (strain CB9615 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=701177 {ECO:0000313|EMBL:ADD56991.1, ECO:0000313|Proteomes:UP000001521};
RN   [1] {ECO:0000313|EMBL:ADD56991.1, ECO:0000313|Proteomes:UP000001521}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CB9615 / EPEC {ECO:0000313|Proteomes:UP000001521};
RX   PubMed=20090843; DOI=10.1371/journal.pone.0008700;
RA   Zhou Z., Li X., Liu B., Beutin L., Xu J., Ren Y., Feng L., Lan R.,
RA   Reeves P.R., Wang L.;
RT   "Derivation of Escherichia coli O157:H7 from its O55:H7 precursor.";
RL   PLoS ONE 5:E8700-E8700(2010).
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; CP001846; ADD56991.1; -; Genomic_DNA.
DR   ProteinModelPortal; D3QX02; -.
DR   EnsemblBacteria; ADD56991; ADD56991; G2583_2433.
DR   KEGG; eok:G2583_2433; -.
DR   HOGENOM; HOG000263449; -.
DR   KO; K04565; -.
DR   OMA; SIGKIMI; -.
DR   Proteomes; UP000001521; 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; 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   Complete proteome {ECO:0000313|Proteomes:UP000001521};
KW   Copper {ECO:0000256|RuleBase:RU000393};
KW   Metal-binding {ECO:0000256|RuleBase:RU000393};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000393};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   DOMAIN      189    327       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   328 AA;  34182 MW;  8155DB839511DFF6 CRC64;
     MFADVMVRVT GFAFVTSTPS AVSAPEDSKP SGGVCSCSPA RQTAVTPCIT GLPSVSVSGV
     LFTRILCNPF TGPSIGPSPM ASITLIICVD LRLSFASTGV CALPPPLPIM FLSIGIINRS
     DRILHSYCAI SSERCLLPCN QQAQSVNGIN EGFMKCKIIA AIAMLTAASC GYAAEQEVPM
     NLVSADGKEV SIGKITIQET PYGLLFTPAL HSLSEGIHGF HVHEKGNCAP ALKDGKPVAA
     LSAGGHFDPK NTGKHLGPWS PDGHLGDLPA LFVTHDGKAN YPVLAPRLNS LKEIKGRSLM
     LHAGGDNHHD HPEPLGGGGA RMACGIIQ
//
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