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Database: UniProt
Entry: A0A117SXI9_9BACL
LinkDB: A0A117SXI9_9BACL
Original site: A0A117SXI9_9BACL 
ID   A0A117SXI9_9BACL        Unreviewed;       204 AA.
AC   A0A117SXI9;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   16-JAN-2019, entry version 11.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=ATW55_06540 {ECO:0000313|EMBL:KUO95541.1};
OS   Acidibacillus ferrooxidans.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Acidibacillus.
OX   NCBI_TaxID=1765683 {ECO:0000313|EMBL:KUO95541.1};
RN   [1] {ECO:0000313|EMBL:KUO95541.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ITV001 {ECO:0000313|EMBL:KUO95541.1};
RA   Dall'Agnol H., Nancucheo I., Johnson B., Oliveira R., Leite L.,
RA   Pylro V., Nunes G.L., Tzotzos G., Fernandes G.R., Dutra J.,
RA   Orellana S.C., Oliveira G.;
RT   "Draft genome sequence of Acidibacillus ferrooxidans ITV001, isolated
RT   from a chalcopyrite acid mine drainage site in Brazil.";
RL   Submitted (DEC-2015) 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: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:KUO95541.1}.
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DR   EMBL; LPVJ01000048; KUO95541.1; -; Genomic_DNA.
DR   RefSeq; WP_067716675.1; NZ_LPVJ01000048.1.
DR   EnsemblBacteria; KUO95541; KUO95541; ATW55_06540.
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        3     90       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       97    197       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        27     27       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        82     82       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       165    165       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       169    169       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   204 AA;  22324 MW;  3AA9BC9954E6EC47 CRC64;
     MAFQTPALPY AVDALEPHID ARTMTVHHDG HHVTYTNNLN AALEAHPDLQ ARSAEDLIKN
     LNSLPEGIRT AVRNNGGGFI NHNLFWTILS PNGGGEPTGA LADAINAQFG SFAKFKEEFS
     KAATTRFGSG WAWLVVDQQG KLAIVSTANQ DNPLMDGQTP ILGLDVWEHA YYLKYQNKRA
     DYISAFFNVV NWSQVASNLE AAKA
//
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