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Database: UniProt/TrEMBL
Entry: X8BFL4_MYCAV
LinkDB: X8BFL4_MYCAV
Original site: X8BFL4_MYCAV 
ID   X8BFL4_MYCAV            Unreviewed;       207 AA.
AC   X8BFL4;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   25-OCT-2017, entry version 22.
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:EUA42023.1};
GN   ORFNames=I549_0121 {ECO:0000313|EMBL:EUA42023.1};
OS   Mycobacterium avium subsp. avium 2285 (R).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=1299330 {ECO:0000313|EMBL:EUA42023.1, ECO:0000313|Proteomes:UP000019908};
RN   [1] {ECO:0000313|EMBL:EUA42023.1, ECO:0000313|Proteomes:UP000019908}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2285 (R) {ECO:0000313|Proteomes:UP000019908};
RA   Zelazny A., Olivier K., Holland S., Lenaerts A., Ordway D.,
RA   DeGroote M.A., Parker T., Sizemore C., Tallon L.J., Sadzewicz L.K.,
RA   Sengamalay N., Fraser C.M., Hine E., Shefchek K.A., Das S.P.,
RA   Tettelin H.;
RL   Submitted (DEC-2013) 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:EUA42023.1}.
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DR   EMBL; JAOE01000001; EUA42023.1; -; Genomic_DNA.
DR   RefSeq; WP_038430292.1; NZ_CP009493.1.
DR   EnsemblBacteria; EUA42023; EUA42023; I549_0121.
DR   KEGG; mavr:LA63_00890; -.
DR   PATRIC; fig|1299330.3.peg.123; -.
DR   KO; K04564; -.
DR   Proteomes; UP000019908; 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   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:UP000019908};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414,
KW   ECO:0000313|EMBL:EUA42023.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019908}.
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;  23043 MW;  07AC90AFB5EABDC3 CRC64;
     MAKYTLPDLD WDYAALEPHI SGQINEIHHT KHHATYVKGV NDALAKLEEA RANEDHAAIF
     LNEKNLAFHL GGHVNHSIWW KNLSPDGGDK PTGELAAAID DAFGSFDKFR AQFSAAANGL
     QGSGWAVLGY DTLGSRLLTF QLYDQQANVP LGIIPLLQVD MWEHAFYLQY KNVKADYVKA
     FWNVVNWADV QKRYAAATSK AQGLIFG
//
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