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Database: UniProt
Entry: X7Y6P1_MYCKA
LinkDB: X7Y6P1_MYCKA
Original site: X7Y6P1_MYCKA 
ID   X7Y6P1_MYCKA            Unreviewed;       236 AA.
AC   X7Y6P1;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   05-DEC-2018, entry version 19.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   ORFNames=I547_1866 {ECO:0000313|EMBL:EUA02704.1};
OS   Mycobacterium kansasii 824.
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1299328 {ECO:0000313|EMBL:EUA02704.1, ECO:0000313|Proteomes:UP000022044};
RN   [1] {ECO:0000313|EMBL:EUA02704.1, ECO:0000313|Proteomes:UP000022044}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=824 {ECO:0000313|EMBL:EUA02704.1,
RC   ECO:0000313|Proteomes:UP000022044};
RA   Brown-Elliot B., Wallace R., Lenaerts A., Ordway D., DeGroote M.A.,
RA   Parker T., Sizemore C., Tallon L.J., Sadzewicz L.K., Sengamalay N.,
RA   Fraser C.M., Hine E., Shefchek K.A., Das S.P., 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:RU000393}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:18421; EC=1.15.1.1;
CC         Evidence={ECO:0000256|RuleBase:RU000393};
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC         Evidence={ECO:0000256|RuleBase:RU000393};
CC       Note=Binds 1 copper ion per subunit.
CC       {ECO:0000256|RuleBase:RU000393};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU000393};
CC       Note=Binds 1 zinc ion per subunit.
CC       {ECO:0000256|RuleBase:RU000393};
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000256|RuleBase:RU000393}.
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:EUA02704.1}.
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DR   EMBL; JANY01000001; EUA02704.1; -; Genomic_DNA.
DR   EnsemblBacteria; EUA02704; EUA02704; I547_1866.
DR   PATRIC; fig|1299328.3.peg.1802; -.
DR   Proteomes; UP000022044; 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   Gene3D; 2.60.40.200; -; 1.
DR   InterPro; IPR036423; SOD-like_Cu/Zn_dom_sf.
DR   InterPro; IPR024134; SOD_Cu/Zn_/chaperone.
DR   InterPro; IPR018152; SOD_Cu/Zn_BS.
DR   InterPro; IPR001424; SOD_Cu_Zn_dom.
DR   PANTHER; PTHR10003; PTHR10003; 1.
DR   Pfam; PF00080; Sod_Cu; 1.
DR   SUPFAM; SSF49329; SSF49329; 1.
DR   PROSITE; PS00332; SOD_CU_ZN_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000022044};
KW   Copper {ECO:0000256|RuleBase:RU000393};
KW   Metal-binding {ECO:0000256|RuleBase:RU000393};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000393,
KW   ECO:0000313|EMBL:EUA02704.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000022044};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   SIGNAL        1     34       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        35    236       Superoxide dismutase [Cu-Zn].
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5004981124.
FT   DOMAIN       76    233       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   236 AA;  23309 MW;  EFD21F3497727365 CRC64;
     MPAGHRPVVA ATLSALSAAA CVALVSACSS PQHASTTPGT TPSIWTGSPA PSEGNGHQEG
     VPGAQGLTTQ LRAPDGTEVA TAKFEFGNGF ATVTIVTTGT GHLTPGFHGV HIHQAGKCEP
     NSVAPSGGAP GDFLSAGGHF QVPGRAKAGQ SSGDLTSLQV RGDGSGTLVT TTDAFTMDDL
     VSGEKTAIII HAGADNFANI PADRYNQANG TPGPDQTTLT TGDAGKRVAC GVIGSG
//
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