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Entry: A0A1L4BQW6_9GAMM
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ID   A0A1L4BQW6_9GAMM        Unreviewed;       186 AA.
AC   A0A1L4BQW6;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   13-FEB-2019, entry version 10.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   ORFNames=F7310_02190 {ECO:0000313|EMBL:API86234.1};
OS   Francisella sp. TX077310.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Francisellaceae; Francisella.
OX   NCBI_TaxID=573570 {ECO:0000313|EMBL:API86234.1};
RN   [1] {ECO:0000313|EMBL:API86234.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TX077310 {ECO:0000313|EMBL:API86234.1};
RX   PubMed=27881415;
RA   Challacombe J.F., Petersen J.M., Gallegos-Graves V., Hodge D.,
RA   Pillai S., Kuske C.R.;
RT   "Whole genome relationships among Francisella bacteria of diverse
RT   origin define new species and provide specific regions for
RT   detection.";
RL   Appl. Environ. Microbiol. 0:0-0(2016).
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; CP016796; API86234.1; -; Genomic_DNA.
DR   RefSeq; WP_072711432.1; NZ_CP016796.1.
DR   KEGG; frx:F7310_02190; -.
DR   KO; K04565; -.
DR   OrthoDB; 2015673at2; -.
DR   BioCyc; GCF_001895265:G1FG6-440-MONOMER; -.
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; PS00087; SOD_CU_ZN_1; 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}.
FT   DOMAIN       47    184       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   186 AA;  20009 MW;  D4CC23C429A98671 CRC64;
     MTINKSYKIL GLGIAIILLT GFSLFEEGSY DRGHDGELIV HMKSTDTGKE VGTITISPYI
     QNDKQQGMLI TPHLYNLPKS GTHGMHIHIN PSCADKGKAA GGHWDPQENG KHLGPYNENG
     HKGDLPVLIV NPNGTANKPV LAPKLDSLEE LVGHSLMIHE GSDNYSDNPK PLGGGGKRVW
     CGVISD
//
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