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Database: UniProt/TrEMBL
Entry: Q57EG8_BRUAB
LinkDB: Q57EG8_BRUAB
Original site: Q57EG8_BRUAB 
ID   Q57EG8_BRUAB            Unreviewed;       199 AA.
AC   Q57EG8;
DT   10-MAY-2005, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2005, sequence version 1.
DT   25-OCT-2017, entry version 80.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   OrderedLocusNames=BruAb1_0588 {ECO:0000313|EMBL:AAX73966.1};
OS   Brucella abortus biovar 1 (strain 9-941).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Brucellaceae; Brucella.
OX   NCBI_TaxID=262698 {ECO:0000313|EMBL:AAX73966.1, ECO:0000313|Proteomes:UP000000540};
RN   [1] {ECO:0000313|EMBL:AAX73966.1, ECO:0000313|Proteomes:UP000000540}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=9-941 {ECO:0000313|EMBL:AAX73966.1,
RC   ECO:0000313|Proteomes:UP000000540};
RX   PubMed=15805518; DOI=10.1128/JB.187.8.2715-2726.2005;
RA   Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L.,
RA   Qing Z., Li L.L., Kapur V., Alt D.P., Olsen S.C.;
RT   "Completion of the genome sequence of Brucella abortus and comparison
RT   to the highly similar genomes of Brucella melitensis and Brucella
RT   suis.";
RL   J. Bacteriol. 187:2715-2726(2005).
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; AE017223; AAX73966.1; -; Genomic_DNA.
DR   RefSeq; WP_002963716.1; NC_006932.1.
DR   ProteinModelPortal; Q57EG8; -.
DR   EnsemblBacteria; AAX73966; AAX73966; BruAb1_0588.
DR   KEGG; bmb:BruAb1_0588; -.
DR   HOGENOM; HOG000013584; -.
DR   KO; K04564; -.
DR   OMA; KWGSFDK; -.
DR   Proteomes; UP000000540; 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   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   Complete proteome {ECO:0000313|Proteomes:UP000000540};
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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