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Database: UniProt/TrEMBL
Entry: A0A0H3MFU6_MYCBP
LinkDB: A0A0H3MFU6_MYCBP
Original site: A0A0H3MFU6_MYCBP 
ID   A0A0H3MFU6_MYCBP        Unreviewed;       207 AA.
AC   A0A0H3MFU6;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   07-JUN-2017, entry version 11.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   Name=sodA {ECO:0000313|EMBL:CAL73899.1};
GN   OrderedLocusNames=BCG_3909 {ECO:0000313|EMBL:CAL73899.1};
OS   Mycobacterium bovis (strain BCG / Pasteur 1173P2).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=410289 {ECO:0000313|EMBL:CAL73899.1, ECO:0000313|Proteomes:UP000001472};
RN   [1] {ECO:0000313|EMBL:CAL73899.1, ECO:0000313|Proteomes:UP000001472}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BCG / Pasteur 1173P2 {ECO:0000313|Proteomes:UP000001472};
RX   PubMed=17372194; DOI=10.1073/pnas.0700869104;
RA   Brosch R., Gordon S.V., Garnier T., Eiglmeier K., Frigui W.,
RA   Valenti P., Dos Santos S., Duthoy S., Lacroix C., Garcia-Pelayo C.,
RA   Inwald J.K., Golby P., Garcia J.N., Hewinson R.G., Behr M.A.,
RA   Quail M.A., Churcher C., Barrell B.G., Parkhill J., Cole S.T.;
RT   "Genome plasticity of BCG and impact on vaccine efficacy.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:5596-5601(2007).
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; AM408590; CAL73899.1; -; Genomic_DNA.
DR   RefSeq; WP_010950947.1; NC_008769.1.
DR   ProteinModelPortal; A0A0H3MFU6; -.
DR   SMR; A0A0H3MFU6; -.
DR   EnsemblBacteria; CAL73899; CAL73899; BCG_3909.
DR   KEGG; mbb:BCG_3909; -.
DR   KO; K04564; -.
DR   OMA; KWGSFDK; -.
DR   Proteomes; UP000001472; Chromosome.
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:UP000001472};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414,
KW   ECO:0000313|EMBL:CAL73899.1}.
FT   DOMAIN        3     84       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       91    193       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        28     28       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        76     76       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   207 AA;  23022 MW;  DEE8E4621DABE54A CRC64;
     MAEYTLPDLD WDYGALEPHI SGQINELHHS KHHATYVKGA NDAVAKLEEA RAKEDHSAIL
     LNEKNLAFNL AGHVNHTIWW KNLSPNGGDK PTGELAAAIA DAFGSFDKFR AQFHAAATTV
     QGSGWAALGW DTLGNKLLIF QVYDHQTNFP LGIVPLLLLD MWEHAFYLQY KNVKVDFAKA
     FWNVVNWADV QSRYAAATSQ TKGLTFG
//
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