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Database: UniProt/TrEMBL
Entry: E6WDI1_PANSA
LinkDB: E6WDI1_PANSA
Original site: E6WDI1_PANSA 
ID   E6WDI1_PANSA            Unreviewed;       172 AA.
AC   E6WDI1;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   25-OCT-2017, entry version 45.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   OrderedLocusNames=Pat9b_1690 {ECO:0000313|EMBL:ADU69006.1};
OS   Pantoea sp. (strain At-9b).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Pantoea.
OX   NCBI_TaxID=592316 {ECO:0000313|EMBL:ADU69006.1, ECO:0000313|Proteomes:UP000001624};
RN   [1] {ECO:0000313|EMBL:ADU69006.1, ECO:0000313|Proteomes:UP000001624}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=At-9b {ECO:0000313|EMBL:ADU69006.1,
RC   ECO:0000313|Proteomes:UP000001624};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L.,
RA   Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., Pinto A.,
RA   Currie C., Woyke T.;
RT   "Complete sequence chromosome of Pantoea sp. At-9b.";
RL   Submitted (DEC-2010) 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; CP002433; ADU69006.1; -; Genomic_DNA.
DR   RefSeq; WP_013508863.1; NC_014837.1.
DR   ProteinModelPortal; E6WDI1; -.
DR   STRING; 592316.Pat9b_1690; -.
DR   EnsemblBacteria; ADU69006; ADU69006; Pat9b_1690.
DR   KEGG; pao:Pat9b_1690; -.
DR   eggNOG; ENOG4108Z7T; Bacteria.
DR   eggNOG; COG2032; LUCA.
DR   HOGENOM; HOG000263449; -.
DR   KO; K04565; -.
DR   OMA; HKGDIGN; -.
DR   OrthoDB; POG091H05JR; -.
DR   BioCyc; PSP592316:GI0L-1731-MONOMER; -.
DR   Proteomes; UP000001624; 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; PS00087; SOD_CU_ZN_1; 1.
DR   PROSITE; PS00332; SOD_CU_ZN_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000001624};
KW   Copper {ECO:0000256|RuleBase:RU000393};
KW   Metal-binding {ECO:0000256|RuleBase:RU000393};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000393};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001624};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   SIGNAL        1     19       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        20    172       Superoxide dismutase [Cu-Zn].
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5003212038.
FT   DOMAIN       35    172       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   172 AA;  17494 MW;  9D169D1C87E19E8C CRC64;
     MNRILIAVLA LFCSGVAQAA SEQVTLHKVT EQGIGAAIGK VTISETPWGL QFTPELSGLP
     PGIHGFHVHA KGSCEPGESG GKMVAAGAAG GHLDPANTGK HLGPYANGHL GDLPALFVTD
     EGKADYPVLA PRIKSLSEIK GKALMVHMGG DNHADHPQPL GGGGARFACG VI
//
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