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Database: UniProt/TrEMBL
Entry: E6XRG2_SHEP2
LinkDB: E6XRG2_SHEP2
Original site: E6XRG2_SHEP2 
ID   E6XRG2_SHEP2            Unreviewed;       173 AA.
AC   E6XRG2;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   28-FEB-2018, entry version 45.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
DE   Flags: Precursor;
GN   OrderedLocusNames=Sput200_3650 {ECO:0000313|EMBL:ADV56030.1};
OS   Shewanella putrefaciens (strain 200).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=399804 {ECO:0000313|EMBL:ADV56030.1, ECO:0000313|Proteomes:UP000008209};
RN   [1] {ECO:0000313|EMBL:ADV56030.1, ECO:0000313|Proteomes:UP000008209}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=200 {ECO:0000313|EMBL:ADV56030.1,
RC   ECO:0000313|Proteomes:UP000008209};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Munk A.C., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N.,
RA   Mikhailova N., Kolker E., Lawrence C., McCue L.A., DiChristina T.,
RA   Nealson K., Fredrickson J.K., Woyke T.;
RT   "Complete sequence of Shewanella putrefaciens 200.";
RL   Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
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; CP002457; ADV56030.1; -; Genomic_DNA.
DR   RefSeq; WP_011920158.1; NC_017566.1.
DR   ProteinModelPortal; E6XRG2; -.
DR   EnsemblBacteria; ADV56030; ADV56030; Sput200_3650.
DR   KEGG; shp:Sput200_3650; -.
DR   PATRIC; fig|399804.5.peg.3777; -.
DR   KO; K04565; -.
DR   OMA; HKGDIGN; -.
DR   OrthoDB; POG091H05JR; -.
DR   Proteomes; UP000008209; 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:UP000008209};
KW   Copper {ECO:0000256|RuleBase:RU000393};
KW   Metal-binding {ECO:0000256|RuleBase:RU000393};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000393};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   SIGNAL        1     20       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        21    173       Superoxide dismutase [Cu-Zn].
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5003213394.
FT   DOMAIN       33    172       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   173 AA;  17911 MW;  C97A4CE079BD6A43 CRC64;
     MNKLHLASLS ILLLSGTAFA QESQVTMELL NAEGNTPIGT ISLNDSEFGL VLTPNLSSLT
     PGVHGFHVHQ TGNCEPVTKD GKTVLGGGAG GHYDPDNTGK HGTPWSTDNH KGDLPPLYVD
     EHGKATTAVL APRLKVNDVK GKSLMVHVGG DNHSDHPAPL GGGGARMACG VIK
//
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