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Database: UniProt/TrEMBL
Entry: S4Z1V6_9MYCO
LinkDB: S4Z1V6_9MYCO
Original site: S4Z1V6_9MYCO 
ID   S4Z1V6_9MYCO            Unreviewed;       207 AA.
AC   S4Z1V6;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   25-OCT-2017, entry version 26.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=OEM_01970 {ECO:0000313|EMBL:AGP61733.1};
OS   Mycobacterium yongonense 05-1390.
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=1138871 {ECO:0000313|EMBL:AGP61733.1, ECO:0000313|Proteomes:UP000014801};
RN   [1] {ECO:0000313|EMBL:AGP61733.1, ECO:0000313|Proteomes:UP000014801}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=05-1390 {ECO:0000313|EMBL:AGP61733.1};
RX   PubMed=23929490;
RA   Kim B.J., Kim B.R., Lee S.Y., Seok S.H., Kook Y.H., Kim B.J.;
RT   "Whole-Genome Sequence of a Novel Species, Mycobacterium yongonense
RT   DSM 45126T.";
RL   Genome Announc. 1:e00604-13(2013).
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; CP003347; AGP61733.1; -; Genomic_DNA.
DR   RefSeq; WP_007771867.1; NC_021715.1.
DR   SMR; S4Z1V6; -.
DR   EnsemblBacteria; AGP61733; AGP61733; OEM_01970.
DR   GeneID; 31527606; -.
DR   KEGG; myo:OEM_01970; -.
DR   PATRIC; fig|1138871.3.peg.194; -.
DR   KO; K04564; -.
DR   OrthoDB; POG091H03Q7; -.
DR   BioCyc; MYON1138871:G13HF-200-MONOMER; -.
DR   Proteomes; UP000014801; 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   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:UP000014801};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414,
KW   ECO:0000313|EMBL:AGP61733.1}.
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;  23131 MW;  A4FE9F20DB54695E CRC64;
     MAEYTLPDLD WDYAALEPHI SGQINEIHHS KHHATYVKGV NDALSKLEEA RANEDHAAIF
     LNEKNLAFHL GGHVNHSIWW KNLSPDGGDK PTGELAAAID DAFGSFDRFR AQFSAAANGL
     QGSGWAVLGY DTLGNRLLTF QLYDQQANVP LGIIPLLQVD MWEHAFYLQY KNVKADYVKA
     FWNVVNWADV QKRYAAATSK TQGLIFG
//
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