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Database: UniProt/TrEMBL
Entry: Q7MFM9_VIBVY
LinkDB: Q7MFM9_VIBVY
Original site: Q7MFM9_VIBVY 
ID   Q7MFM9_VIBVY            Unreviewed;       170 AA.
AC   Q7MFM9;
DT   15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2003, sequence version 1.
DT   07-JUN-2017, entry version 103.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   OrderedLocusNames=VVA0291 {ECO:0000313|EMBL:BAC96317.1};
OS   Vibrio vulnificus (strain YJ016).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Vibrio.
OX   NCBI_TaxID=196600 {ECO:0000313|EMBL:BAC96317.1, ECO:0000313|Proteomes:UP000002675};
RN   [1] {ECO:0000313|EMBL:BAC96317.1, ECO:0000313|Proteomes:UP000002675}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJ016 {ECO:0000313|EMBL:BAC96317.1,
RC   ECO:0000313|Proteomes:UP000002675};
RX   PubMed=14656965; DOI=10.1101/gr.1295503;
RA   Chen C.Y., Wu K.M., Chang Y.C., Chang C.H., Tsai H.C., Liao T.L.,
RA   Liu Y.M., Chen H.J., Shen A.B., Li J.C., Su T.L., Shao C.P., Lee C.T.,
RA   Hor L.I., Tsai S.F.;
RT   "Comparative genome analysis of Vibrio vulnificus, a marine
RT   pathogen.";
RL   Genome Res. 13:2577-2587(2003).
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: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
CC       {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}.
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DR   EMBL; BA000038; BAC96317.1; -; Genomic_DNA.
DR   RefSeq; WP_011151698.1; NC_005140.1.
DR   ProteinModelPortal; Q7MFM9; -.
DR   EnsemblBacteria; BAC96317; BAC96317; BAC96317.
DR   GeneID; 2621413; -.
DR   KEGG; vvy:VVA0291; -.
DR   PATRIC; fig|196600.6.peg.3499; -.
DR   HOGENOM; HOG000263449; -.
DR   KO; K04565; -.
DR   OMA; HKGDIGN; -.
DR   OrthoDB; POG091H05JR; -.
DR   BioCyc; VVUL196600:GJ9W-3683-MONOMER; -.
DR   Proteomes; UP000002675; Chromosome II.
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; IPR018152; SOD_Cu/Zn_BS.
DR   InterPro; IPR001424; SOD_Cu_Zn_dom.
DR   Pfam; PF00080; Sod_Cu; 1.
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:UP000002675};
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:UP000002675};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   SIGNAL        1     19       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        20    170       Superoxide dismutase [Cu-Zn].
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5004288442.
FT   DOMAIN       32    169       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   170 AA;  17613 MW;  5AA2C93F1176704A CRC64;
     MNKHTLLAAI LLYSTSSFAQ SLSVDMKDLS SNQTLGTVTI SSSDYGTVFT PDLKGLPSGL
     HGFHLHANGS CESSNKDGKV VLGGAAGGHY DPQNSGKHGY PWTEDNHLGD LPALFVDASG
     NASQPVLAPR VALKDVQGRA LMIHAGADNH SDHPMPLGGG GARIVCGVIK
//
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