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Database: UniProt
Entry: A0A0G0E2C0_9BACT
LinkDB: A0A0G0E2C0_9BACT
Original site: A0A0G0E2C0_9BACT 
ID   A0A0G0E2C0_9BACT        Unreviewed;       222 AA.
AC   A0A0G0E2C0;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   16-JAN-2019, entry version 14.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=UR67_C0007G0055 {ECO:0000313|EMBL:KKP69350.1};
OS   candidate division CPR3 bacterium GW2011_GWF2_35_18.
OC   Bacteria; candidate division CPR3.
OX   NCBI_TaxID=1618350 {ECO:0000313|EMBL:KKP69350.1};
RN   [1] {ECO:0000313|EMBL:KKP69350.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a
RT   large radiation of phyla.";
RL   Nature 0:0-0(2015).
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems.
CC       {ECO:0000256|RuleBase:RU000414}.
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:RU000414};
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000256|RuleBase:RU000414}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KKP69350.1}.
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DR   EMBL; LBQB01000007; KKP69350.1; -; Genomic_DNA.
DR   EnsemblBacteria; KKP69350; KKP69350; UR67_C0007G0055.
DR   PATRIC; fig|1618350.3.peg.937; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR   Gene3D; 1.10.287.990; -; 1.
DR   Gene3D; 2.40.500.20; -; 1.
DR   InterPro; IPR001189; Mn/Fe_SOD.
DR   InterPro; IPR019833; Mn/Fe_SOD_BS.
DR   InterPro; IPR019832; Mn/Fe_SOD_C.
DR   InterPro; IPR019831; Mn/Fe_SOD_N.
DR   InterPro; IPR036324; Mn/Fe_SOD_N_sf.
DR   InterPro; IPR036314; SOD_C_sf.
DR   Pfam; PF02777; Sod_Fe_C; 1.
DR   Pfam; PF00081; Sod_Fe_N; 1.
DR   PIRSF; PIRSF000349; SODismutase; 1.
DR   PRINTS; PR01703; MNSODISMTASE.
DR   SUPFAM; SSF46609; SSF46609; 1.
DR   SUPFAM; SSF54719; SSF54719; 1.
DR   PROSITE; PS00088; SOD_MN; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414}.
FT   DOMAIN       21    108       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN      119    215       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        45     45       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       100    100       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       183    183       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       187    187       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   222 AA;  25878 MW;  3B4C57DBE145F6AE CRC64;
     MFNILYSYLI SVSMSGENIM FTLPKLLYSY ADLEPYIDAR TMEIHYSKHH QTYVDKLNLA
     LKDHDELSKK TVEELLISLE SIPKEIQTAV RNNGGGHYNH SFFWKVMKPK GGGESNGILS
     PIIDKELGGF INFHDKFTSE ALNRFGSGWT WLSLDENKHL KIHSTANQDS PLLEGLKPIL
     ALDLWEHAYY LHYQNRRADY IKSWWHVVNW EQVEQNYLDA TR
//
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