GenomeNet

Database: UniProt/TrEMBL
Entry: A0A0K2H832_GEOSE
LinkDB: A0A0K2H832_GEOSE
Original site: A0A0K2H832_GEOSE 
ID   A0A0K2H832_GEOSE        Unreviewed;       174 AA.
AC   A0A0K2H832;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   25-OCT-2017, entry version 11.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   ORFNames=GT50_06290 {ECO:0000313|EMBL:ALA69856.1};
OS   Geobacillus stearothermophilus 10.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=272567 {ECO:0000313|EMBL:ALA69856.1};
RN   [1] {ECO:0000313|EMBL:ALA69856.1, ECO:0000313|Proteomes:UP000065315}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=10 {ECO:0000313|EMBL:ALA69856.1,
RC   ECO:0000313|Proteomes:UP000065315};
RA   Lewis S.A., Clifton S.W., Najar F.Z., Roe B.A.;
RT   "Complete genome Sequence of Geobacillus stearothermophilus strain 10,
RT   a Yellowstone hot spring isolate.";
RL   Submitted (JUL-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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP008934; ALA69856.1; -; Genomic_DNA.
DR   RefSeq; WP_013524510.1; NZ_CP008934.1.
DR   ProteinModelPortal; A0A0K2H832; -.
DR   EnsemblBacteria; ALA69856; ALA69856; GT50_06290.
DR   KEGG; gse:GT50_06290; -.
DR   PATRIC; fig|272567.8.peg.1269; -.
DR   KO; K04565; -.
DR   Proteomes; UP000065315; 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:UP000065315};
KW   Copper {ECO:0000256|RuleBase:RU000393};
KW   Metal-binding {ECO:0000256|RuleBase:RU000393};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000393};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   DOMAIN       36    171       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   174 AA;  18097 MW;  0BB45FBF2D6A95A7 CRC64;
     MLRKTYGVVF AAALVLSGCG QENGTSRTVE MINADGDSIG TIELTEQAEG VRLKLDLEGL
     PPGEHAIHIH ENGSCKPPDF QSAGGHYNPD GKKHGLLHPE GAHAGDLPNI IVKDDGTVNV
     ELTAPNVTLK EGEKGSLLTK DGTSIVIHAK KDDGMTQPAG DAGGRIACGE IKSS
//
DBGET integrated database retrieval system