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Database: UniProt/TrEMBL
Entry: A0A075P3Q3_9ALTE
LinkDB: A0A075P3Q3_9ALTE
Original site: A0A075P3Q3_9ALTE 
ID   A0A075P3Q3_9ALTE        Unreviewed;       181 AA.
AC   A0A075P3Q3;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-SEP-2017, entry version 18.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   ORFNames=EP13_17295 {ECO:0000313|EMBL:AIG00294.1};
OS   Alteromonas australica.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Alteromonas.
OX   NCBI_TaxID=589873 {ECO:0000313|EMBL:AIG00294.1, ECO:0000313|Proteomes:UP000056090};
RN   [1] {ECO:0000313|EMBL:AIG00294.1, ECO:0000313|Proteomes:UP000056090}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H 17 {ECO:0000313|EMBL:AIG00294.1,
RC   ECO:0000313|Proteomes:UP000056090};
RA   Gonzaga A., Lopez-Perez M., Rodriguez-Valera F.;
RT   "Genomes of Alteromonas australica, a world apart.";
RL   Submitted (JUN-2014) 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; CP008849; AIG00294.1; -; Genomic_DNA.
DR   RefSeq; WP_044058305.1; NZ_CP008849.1.
DR   EnsemblBacteria; AIG00294; AIG00294; EP13_17295.
DR   KEGG; aal:EP13_17295; -.
DR   KO; K04565; -.
DR   Proteomes; UP000056090; 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:UP000056090};
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:UP000056090};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   SIGNAL        1     23       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        24    181       Superoxide dismutase [Cu-Zn].
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5001708601.
FT   DOMAIN       41    179       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   181 AA;  18948 MW;  0FA52D1EB4A33931 CRC64;
     MNKRKITAMV GAVSLALSSA SFAAHHDDDH ISVVMKDLKT ESSMGTVKVS DYDDDGVVFT
     PNLKGLTPGI HGFHIHENGD CLATMKNGKT VLGGAAGGHF DPEATGQHKA PWSEAGHEGD
     LPTLYVDESG NATQPVFAPE LELEDIRGKA IMIHAGGDNY SDEPKKLGGG GPRVACGVIS
     E
//
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