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Database: UniProt
Entry: A0A0K1XGM9_9GAMM
LinkDB: A0A0K1XGM9_9GAMM
Original site: A0A0K1XGM9_9GAMM 
ID   A0A0K1XGM9_9GAMM        Unreviewed;       172 AA.
AC   A0A0K1XGM9;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   05-DEC-2018, entry version 12.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   ORFNames=AKN88_00365 {ECO:0000313|EMBL:AKX60491.1};
OS   Oblitimonas alkaliphila.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Oblitimonas.
OX   NCBI_TaxID=1697053 {ECO:0000313|EMBL:AKX60491.1, ECO:0000313|Proteomes:UP000063953};
RN   [1] {ECO:0000313|EMBL:AKX60491.1, ECO:0000313|Proteomes:UP000063953}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E5571 {ECO:0000313|EMBL:AKX60491.1,
RC   ECO:0000313|Proteomes:UP000063953};
RX   PubMed=26679585;
RA   Lauer A.C., Nicholson A.C., Humrighouse B.W., Emery B., Drobish A.,
RA   Juieng P., Loparev V., McQuiston J.R.;
RT   "Genome Sequences of Oblitimonas alkaliphila gen. nov. sp. nov.
RT   (Proposed), a Novel Bacterium of the Pseudomonadaceae Family.";
RL   Genome Announc. 3:e01474-15(2015).
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; CP012365; AKX60491.1; -; Genomic_DNA.
DR   EnsemblBacteria; AKX60491; AKX60491; AKN88_00365.
DR   PATRIC; fig|1698449.3.peg.71; -.
DR   Proteomes; UP000063953; 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:UP000063953};
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:UP000063953};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   DOMAIN       30    171       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   172 AA;  17570 MW;  9BF6A4A222444E7C CRC64;
     MAGIGANPSV LAADRSERLT IAVHATSEQG QGAALGTIKV EPTPYGLLFT PELKGLAAGL
     HGFHIHEHAN CAPSTDDQAK VVPAGAAGGH FDPEKTGQHL GPYDSAGHLG DLPALYVNAE
     GVADYPVLAP KLRELAQIKN RSIMIHAGGD NHSDHPAPLG GGGARMACGV IN
//
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