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Database: UniProt
Entry: K0D6Z6_ALTMS
LinkDB: K0D6Z6_ALTMS
Original site: K0D6Z6_ALTMS 
ID   K0D6Z6_ALTMS            Unreviewed;       180 AA.
AC   K0D6Z6;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   10-APR-2019, entry version 30.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   OrderedLocusNames=AMBLS11_14265 {ECO:0000313|EMBL:AFT79422.1};
OS   Alteromonas macleodii (strain Black Sea 11).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Alteromonas.
OX   NCBI_TaxID=1004785 {ECO:0000313|EMBL:AFT79422.1, ECO:0000313|Proteomes:UP000006295};
RN   [1] {ECO:0000313|Proteomes:UP000006295}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Black Sea 11 {ECO:0000313|Proteomes:UP000006295};
RX   PubMed=23019517; DOI=10.1038/srep00696;
RA   Lopez-Perez M., Gonzaga A., Martin-Cuadrado A.B., Onyshchenko O.,
RA   Ghavidel A., Ghai R., Rodriguez-Valera F.;
RT   "Genomes of surface isolates of Alteromonas macleodii: the life of a
RT   widespread marine opportunistic copiotroph.";
RL   Sci. Rep. 2:696-696(2012).
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:
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         Evidence={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; CP003845; AFT79422.1; -; Genomic_DNA.
DR   RefSeq; WP_014999311.1; NC_018692.1.
DR   STRING; 1004785.AMBLS11_14265; -.
DR   EnsemblBacteria; AFT79422; AFT79422; AMBLS11_14265.
DR   KEGG; amk:AMBLS11_14265; -.
DR   PATRIC; fig|1004785.3.peg.2986; -.
DR   KO; K04565; -.
DR   OMA; HKGDIGN; -.
DR   OrthoDB; 2015673at2; -.
DR   BioCyc; AMAC1004785:G1HAT-2917-MONOMER; -.
DR   Proteomes; UP000006295; 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:UP000006295};
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     23       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        24    180       Superoxide dismutase [Cu-Zn].
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5003829943.
FT   DOMAIN       43    179       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   180 AA;  18854 MW;  023C12F4612EBCE9 CRC64;
     MKKRLISTLA GSLSLVLSAS SFAGHHEIGG KEVVMNNLET GMSMGTVMIS SYDDDGVVFT
     PNLSGLTPGI HGFHVHQNGD CSPAMKDGKK VSGGAAGGHF DPEETGKHRA PWSEKGHEGD
     LPVLYVDENG NATQPIFAPE LELEDIEGRA LMIHAGGDNY SDSPKKLGGG GDRVACGVIR
//
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