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Database: UniProt
Entry: A0A0L0QRZ7_VIRPA
LinkDB: A0A0L0QRZ7_VIRPA
Original site: A0A0L0QRZ7_VIRPA 
ID   A0A0L0QRZ7_VIRPA        Unreviewed;       206 AA.
AC   A0A0L0QRZ7;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   16-JAN-2019, entry version 13.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   ORFNames=AFK71_07140 {ECO:0000313|EMBL:KNE21430.1};
OS   Virgibacillus pantothenticus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Virgibacillus.
OX   NCBI_TaxID=1473 {ECO:0000313|EMBL:KNE21430.1, ECO:0000313|Proteomes:UP000036780};
RN   [1] {ECO:0000313|Proteomes:UP000036780}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 26 {ECO:0000313|Proteomes:UP000036780};
RA   Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J.,
RA   Ge C., Shi H., Pan Z., Liu X.;
RT   "Fjat-10053 dsm26.";
RL   Submitted (JUL-2015) 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:KNE21430.1}.
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DR   EMBL; LGTO01000005; KNE21430.1; -; Genomic_DNA.
DR   RefSeq; WP_050350859.1; NZ_LGTO01000005.1.
DR   EnsemblBacteria; KNE21430; KNE21430; AFK71_07140.
DR   PATRIC; fig|1473.5.peg.4450; -.
DR   OrthoDB; 2015673at2; -.
DR   Proteomes; UP000036780; 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   PRINTS; PR00068; CUZNDISMTASE.
DR   SUPFAM; SSF49329; SSF49329; 1.
DR   PROSITE; PS00087; SOD_CU_ZN_1; 1.
DR   PROSITE; PS00332; SOD_CU_ZN_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000036780};
KW   Copper {ECO:0000256|RuleBase:RU000393};
KW   Metal-binding {ECO:0000256|RuleBase:RU000393};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000393};
KW   Reference proteome {ECO:0000313|Proteomes:UP000036780};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   SIGNAL        1     25       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        26    206       Superoxide dismutase [Cu-Zn].
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5005546470.
FT   DOMAIN       66    202       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   206 AA;  22310 MW;  4AE76CB61F2D5E14 CRC64;
     MHKQTINIII ATMCLFVLSA CNTTDDERTQ GSEELEKLQS NEAEQKTTNV ERDSSKKVMV
     SLKDRKQQEV ATAIVTEEEQ GVRIKLAGEN FTPGKHGFHI HETGSCEEPD FSSAGEHFNP
     TNRSHGKKAP GGPHAGDLPN IEAADDGTVT ADFLNEMVTL KPGEDHSLVK EGGTALVIHS
     DKDDYKTQPA GNAGERIACG VIKEAK
//
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