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Database: UniProt
Entry: X7ZW09_MYCXE
LinkDB: X7ZW09_MYCXE
Original site: X7ZW09_MYCXE 
ID   X7ZW09_MYCXE            Unreviewed;       190 AA.
AC   X7ZW09;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   16-JAN-2019, entry version 18.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   ORFNames=I552_7291 {ECO:0000313|EMBL:EUA22800.1};
OS   Mycobacterium xenopi 3993.
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1299333 {ECO:0000313|EMBL:EUA22800.1};
RN   [1] {ECO:0000313|EMBL:EUA22800.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3993 {ECO:0000313|EMBL:EUA22800.1};
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 (JAN-2014) 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:EUA22800.1}.
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DR   EMBL; JAOC01000028; EUA22800.1; -; Genomic_DNA.
DR   EnsemblBacteria; EUA22800; EUA22800; I552_7291.
DR   PATRIC; fig|1299333.3.peg.8368; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR   CDD; cd00305; Cu-Zn_Superoxide_Dismutase; 1.
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   Copper {ECO:0000256|RuleBase:RU000393};
KW   Metal-binding {ECO:0000256|RuleBase:RU000393};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000393,
KW   ECO:0000313|EMBL:EUA22800.1}; Zinc {ECO:0000256|RuleBase:RU000393}.
FT   DOMAIN       31    187       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   190 AA;  19464 MW;  5066BA0AFC51A62E CRC64;
     MDGFTCAAED ATRRGPVPPE SITTHLRAPD GTQVATAKFE FDPGYVTITV RTTGLGQLTP
     GFHGLHIHSV GKCEPNSVAP TGGPPGDFLS AGGHYQAPGH TGEPESGDLT SLQVRKDGAA
     LLVTTTDAFT KEDLVSGNKT AIIIHAGPDN FANIPPERYT QANGTPGPDA MTKSTGDAGK
     RVACGVIGSG
//
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