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Database: UniProt/TrEMBL
Entry: A0A1S1Z5T6_BRUAO
LinkDB: A0A1S1Z5T6_BRUAO
Original site: A0A1S1Z5T6_BRUAO 
ID   A0A1S1Z5T6_BRUAO        Unreviewed;       199 AA.
AC   A0A1S1Z5T6;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-SEP-2017, entry version 4.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=BFJ58_12300 {ECO:0000313|EMBL:OHX82796.1};
OS   Brucella abortus.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Brucellaceae; Brucella.
OX   NCBI_TaxID=235 {ECO:0000313|EMBL:OHX82796.1, ECO:0000313|Proteomes:UP000179475};
RN   [1] {ECO:0000313|EMBL:OHX82796.1, ECO:0000313|Proteomes:UP000179475}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Br.a-1549/11-Geo {ECO:0000313|EMBL:OHX82796.1,
RC   ECO:0000313|Proteomes:UP000179475};
RA   Sidamonidze K., Jun H., Nikolich M.;
RT   "Brucella abortus genome assembly.";
RL   Submitted (SEP-2016) 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: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
CC       {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:OHX82796.1}.
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DR   EMBL; MIJI01000030; OHX82796.1; -; Genomic_DNA.
DR   RefSeq; WP_002963716.1; NZ_MIJN01000023.1.
DR   KEGG; babb:DK48_1523; -.
DR   KEGG; babc:DO78_501; -.
DR   KEGG; babs:DK51_876; -.
DR   KEGG; babt:DK49_356; -.
DR   KO; K04564; -.
DR   Proteomes; UP000179475; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
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   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   Complete proteome {ECO:0000313|Proteomes:UP000179475};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414}.
FT   DOMAIN        3     85       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       95    191       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        27     27       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        77     77       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       160    160       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       164    164       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   199 AA;  22540 MW;  8C5D1A240858D546 CRC64;
     MAFELPALPY DYDALAPFMS RETLEYHHDK HHQAYVTNGN KLLEGSGLEG KSFEEIVKES
     FGKNQALFNN AGQHYNHIHF WKWMKKDGGG KKLPGKLEKA FDSDLGGYDK FRADFIAAGA
     GQFGSGWAWL SVKDGKLEIS KTPNGENPLV HGAAPILGVD VWEHSYYIDY RNARPKYLEA
     FVDSLVNWDY VLEMYEKAA
//
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