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Database: UniProt
Entry: R7ZI56_LYSSH
LinkDB: R7ZI56_LYSSH
Original site: R7ZI56_LYSSH 
ID   R7ZI56_LYSSH            Unreviewed;       193 AA.
AC   R7ZI56;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   10-APR-2019, entry version 25.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   ORFNames=H131_03899 {ECO:0000313|EMBL:EON73775.1};
OS   Lysinibacillus sphaericus OT4b.31.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae;
OC   Lysinibacillus.
OX   NCBI_TaxID=1285586 {ECO:0000313|EMBL:EON73775.1, ECO:0000313|Proteomes:UP000013911};
RN   [1] {ECO:0000313|EMBL:EON73775.1, ECO:0000313|Proteomes:UP000013911}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OT4b.31 {ECO:0000313|EMBL:EON73775.1,
RC   ECO:0000313|Proteomes:UP000013911};
RA   Pena-Montenegro T.D., Dussan J.;
RT   "Draft genome of the heavy metal tolerant bacterium Lysinibacillus
RT   sphaericus strain OT4b.31.";
RL   Submitted (APR-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:EON73775.1}.
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DR   EMBL; AQPX01000008; EON73775.1; -; Genomic_DNA.
DR   RefSeq; WP_010857744.1; NZ_KB933398.1.
DR   STRING; 1285586.H131_03899; -.
DR   EnsemblBacteria; EON73775; EON73775; H131_03899.
DR   PATRIC; fig|1285586.5.peg.788; -.
DR   BioCyc; GCF_000392615:G1EFZ-788-MONOMER; -.
DR   Proteomes; UP000013911; 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   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   Complete proteome {ECO:0000313|Proteomes:UP000013911};
KW   Copper {ECO:0000256|RuleBase:RU000393};
KW   Metal-binding {ECO:0000256|RuleBase:RU000393};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000393};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   SIGNAL        1     22       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        23    193       Superoxide dismutase [Cu-Zn].
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5004461682.
FT   DOMAIN       56    192       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   193 AA;  20514 MW;  9DE7D4D32A2A09F8 CRC64;
     MKKITILIMS LTVFVGGCNF FDKSEKEVAV NANSQSNPNS NSNSPLTATA KVIGSNNESY
     GNAYFQEEDN GVMMTLALTG LPSGTHGIHI HTVGKCEPPT FESAGGHFNP TKKEHGKLNP
     KGYHLGDLPN LEIGEDGTVD LTFIAEGITL QKNMENSLFD EDGSALVIHE AADDYKTDPA
     GNSGARIACG VIQ
//
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