GenomeNet

Database: UniProt
Entry: I2AXN5_FRANT
LinkDB: I2AXN5_FRANT
Original site: I2AXN5_FRANT 
ID   I2AXN5_FRANT            Unreviewed;       185 AA.
AC   I2AXN5;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   10-APR-2019, entry version 38.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   OrderedLocusNames=OOM_0393 {ECO:0000313|EMBL:AFJ42932.1};
OS   Francisella noatunensis subsp. orientalis (strain Toba 04).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Francisellaceae; Francisella.
OX   NCBI_TaxID=1163389 {ECO:0000313|EMBL:AFJ42932.1};
RN   [1] {ECO:0000313|EMBL:AFJ42932.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Toba 04 {ECO:0000313|EMBL:AFJ42932.1};
RA   Jonassen I., Nilsen F., Sridhar S., Sharma A., Kongshaug H.;
RT   "Whole genome characterisation of Francisella noatunensis subsp.
RT   orientalis.";
RL   Submitted (FEB-2012) 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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; CP003402; AFJ42932.1; -; Genomic_DNA.
DR   RefSeq; WP_014714479.1; NC_017909.1.
DR   STRING; 1163389.OOM_0393; -.
DR   EnsemblBacteria; AFJ42932; AFJ42932; OOM_0393.
DR   KEGG; fna:OOM_0393; -.
DR   PATRIC; fig|1163389.3.peg.471; -.
DR   KO; K04565; -.
DR   OMA; SIGKIMI; -.
DR   BioCyc; FNOA1163389:G1H58-391-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   ECO:0000313|EMBL:AFJ42932.1}; Zinc {ECO:0000256|RuleBase:RU000393}.
FT   DOMAIN       47    183       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   185 AA;  20261 MW;  38BE7F437E57BBB5 CRC64;
     MGNFCKLLGV SMCTFLLSNC SLFHEKKQYN FNHDFELIVH MKEVKTQKEV GTVTISPYIH
     DGKQEGMLII PYLYNLPASS VHGMHIHINP SCDDDGMAAG GHWDPDNTGK HLGPYKDDGH
     KGDLPELVVN ADGTATEPVV APRLDSLEEL EGHSLMIHEG GDNYSDTPKP LGGGGTRMWC
     GVITD
//
DBGET integrated database retrieval system