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Database: UniProt/TrEMBL
Entry: B0CKP7_BRUSI
LinkDB: B0CKP7_BRUSI
Original site: B0CKP7_BRUSI 
ID   B0CKP7_BRUSI            Unreviewed;       199 AA.
AC   B0CKP7;
DT   26-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   26-FEB-2008, sequence version 1.
DT   07-JUN-2017, entry version 58.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   Name=sodB {ECO:0000313|EMBL:ABY37677.1};
GN   OrderedLocusNames=BSUIS_A0594 {ECO:0000313|EMBL:ABY37677.1};
OS   Brucella suis (strain ATCC 23445 / NCTC 10510).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Brucellaceae; Brucella.
OX   NCBI_TaxID=470137 {ECO:0000313|EMBL:ABY37677.1, ECO:0000313|Proteomes:UP000008545};
RN   [1] {ECO:0000313|EMBL:ABY37677.1, ECO:0000313|Proteomes:UP000008545}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23445 / NCTC 10510 {ECO:0000313|Proteomes:UP000008545};
RA   Setubal J.C., Bowns C., Boyle S., Crasta O.R., Czar M.J.,
RA   Dharmanolla C., Gillespie J.J., Kenyon R.W., Lu J., Mane S.,
RA   Mohapatra S., Nagrani S., Purkayastha A., Rajasimha H.K.,
RA   Shallom J.M., Shallom S., Shukla M., Snyder E.E., Sobral B.W.,
RA   Wattam A.R., Will R., Williams K., Yoo H., Bruce D., Detter C.,
RA   Munk C., Brettin T.S.;
RT   "Brucella suis ATCC 23445 whole genome shotgun sequencing project.";
RL   Submitted (DEC-2007) 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}.
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DR   EMBL; CP000911; ABY37677.1; -; Genomic_DNA.
DR   RefSeq; WP_004690660.1; NC_010169.1.
DR   ProteinModelPortal; B0CKP7; -.
DR   EnsemblBacteria; ABY37677; ABY37677; BSUIS_A0594.
DR   KEGG; bmt:BSUIS_A0594; -.
DR   HOGENOM; HOG000013584; -.
DR   KO; K04564; -.
DR   OMA; KWGSFDK; -.
DR   Proteomes; UP000008545; Chromosome I.
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:UP000008545};
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;  22448 MW;  5C7DF3E9CB75F26B CRC64;
     MAFELPALPY DYDALAPFMS RETLEYHHDK HHQAYVTNGN KLLEGSGLAG KSLEEIVKES
     FGKNQALFNN AGQHYNHIHF WKWMKKDGGG KKLPGKLEKA FDSDLGGYDK FRADFIAAGA
     GQFGSGWAWL SVKDGKLEIS KTPNGENPLV HGAAPILGVD VWEHSYYIDY RNARPKYLEA
     FVDSLVNWDY VLEMYEKAA
//
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