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Entry: A0A0P9CUS5_9GAMM
LinkDB: A0A0P9CUS5_9GAMM
Original site: A0A0P9CUS5_9GAMM 
ID   A0A0P9CUS5_9GAMM        Unreviewed;       169 AA.
AC   A0A0P9CUS5;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   05-DEC-2018, entry version 15.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   ORFNames=SAMN05661077_2646 {ECO:0000313|EMBL:SCY60422.1};
OS   Thiohalorhabdus denitrificans.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiohalorhabdus.
OX   NCBI_TaxID=381306 {ECO:0000313|EMBL:SCY60422.1};
RN   [1] {ECO:0000313|EMBL:SCY60422.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HL 19 {ECO:0000313|EMBL:SCY60422.1};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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:
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; FMUN01000008; SCY60422.1; -; Genomic_DNA.
DR   RefSeq; WP_074471458.1; NZ_LJCP01000009.1.
DR   EnsemblBacteria; KPV40423; KPV40423; AN478_06415.
DR   PATRIC; fig|381306.5.peg.2704; -.
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   PRINTS; PR00068; CUZNDISMTASE.
DR   SUPFAM; SSF49329; SSF49329; 1.
DR   PROSITE; PS00332; SOD_CU_ZN_2; 1.
PE   3: Inferred from homology;
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}.
SQ   SEQUENCE   169 AA;  17510 MW;  D5EAE50F40943E3F CRC64;
     MRVTEGMGLA AVAAVLLGGL AGPAHAGDAS AELQDTDGEA VGEVKLKESP HGVLVHAELE
     GMPEGTHAFH IHETGRCEPP FKSAGGHFNP EDKAHGFMSE EGYHAGDMPN IHVSDSGDLE
     VEYFAPGVEL DELLDEDGGA ILVHEGGDDY ETDPAGDAGS RIACGVIED
//
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