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
//
