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Entry: A0A1A9I1X2_9BACT
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ID   A0A1A9I1X2_9BACT        Unreviewed;       204 AA.
AC   A0A1A9I1X2;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   13-FEB-2019, 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=A8C56_05795 {ECO:0000313|EMBL:ANH80564.1};
OS   Niabella ginsenosidivorans.
OC   Bacteria; Bacteroidetes; Chitinophagia; Chitinophagales;
OC   Chitinophagaceae; Niabella.
OX   NCBI_TaxID=1176587 {ECO:0000313|EMBL:ANH80564.1, ECO:0000313|Proteomes:UP000077667};
RN   [1] {ECO:0000313|EMBL:ANH80564.1, ECO:0000313|Proteomes:UP000077667}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BS26 {ECO:0000313|EMBL:ANH80564.1,
RC   ECO:0000313|Proteomes:UP000077667};
RA   Im W.T., Siddiqi M.Z.;
RT   "Niabella ginsenosidivorans BS26 whole genome sequencing.";
RL   Submitted (MAY-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; CP015772; ANH80564.1; -; Genomic_DNA.
DR   RefSeq; WP_067753247.1; NZ_CP015772.1.
DR   EnsemblBacteria; ANH80564; ANH80564; A8C56_05795.
DR   KEGG; nia:A8C56_05795; -.
DR   KO; K04565; -.
DR   OrthoDB; 2015673at2; -.
DR   BioCyc; GCF_001654455:G1ETT-1160-MONOMER; -.
DR   Proteomes; UP000077667; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
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   Complete proteome {ECO:0000313|Proteomes:UP000077667};
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:UP000077667};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   SIGNAL        1     23       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        24    204       Superoxide dismutase [Cu-Zn].
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5008389730.
FT   DOMAIN       68    201       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   204 AA;  21262 MW;  C99E0C258BEDE2BE CRC64;
     MKKTIFAAGV AALFILASCG NNSSEKSGTD STTVSTTKID SSATAPAAPA PEGTQVAVAN
     LQSTADSTKN LGTAKFYKLA DGKIRLDVEI NMPERADSNV AVHFHEHGDC GMKGENSHGH
     WNPTKSKHGE WGSASFHSGD IGNIKLDAQG HGTKSVTTDL WSVDQGDKDI IGRAVIVHGG
     TDDYKTQPTG NSGPRVGCGV ITKL
//
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