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Database: UniProt/TrEMBL
Entry: Q2YMR6_BRUA2
LinkDB: Q2YMR6_BRUA2
Original site: Q2YMR6_BRUA2 
ID   Q2YMR6_BRUA2            Unreviewed;       199 AA.
AC   Q2YMR6;
DT   07-FEB-2006, integrated into UniProtKB/TrEMBL.
DT   07-FEB-2006, sequence version 1.
DT   25-OCT-2017, entry version 75.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   OrderedLocusNames=BAB1_0591 {ECO:0000313|EMBL:CAJ10547.1};
OS   Brucella abortus (strain 2308).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Brucellaceae; Brucella.
OX   NCBI_TaxID=359391 {ECO:0000313|EMBL:CAJ10547.1, ECO:0000313|Proteomes:UP000002719};
RN   [1] {ECO:0000313|EMBL:CAJ10547.1, ECO:0000313|Proteomes:UP000002719}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2308 {ECO:0000313|EMBL:CAJ10547.1,
RC   ECO:0000313|Proteomes:UP000002719};
RX   PubMed=16299333; DOI=10.1128/IAI.73.12.8353-8361.2005;
RG   Microbial Genomics Group;
RG   Lawrence Livermore National Laboratory;
RG   and the Genome Analysis Group;
RG   Oak Ridge National Laboratory;
RA   Chain P., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.,
RA   Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT   "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL   Infect. Immun. 73:8353-8361(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; AM040264; CAJ10547.1; -; Genomic_DNA.
DR   RefSeq; WP_002963716.1; NZ_KN046823.1.
DR   ProteinModelPortal; Q2YMR6; -.
DR   PRIDE; Q2YMR6; -.
DR   EnsemblBacteria; CAJ10547; CAJ10547; BAB1_0591.
DR   KEGG; bmf:BAB1_0591; -.
DR   PATRIC; fig|359391.11.peg.2903; -.
DR   HOGENOM; HOG000013584; -.
DR   KO; K04564; -.
DR   OMA; KWGSFDK; -.
DR   Proteomes; UP000002719; 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:UP000002719};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414,
KW   ECO:0000313|EMBL:CAJ10547.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002719}.
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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