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Database: UniProt/TrEMBL
Entry: S5IV82_VIBPH
LinkDB: S5IV82_VIBPH
Original site: S5IV82_VIBPH 
ID   S5IV82_VIBPH            Unreviewed;       171 AA.
AC   S5IV82;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   07-JUN-2017, entry version 27.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   ORFNames=M634_17025 {ECO:0000313|EMBL:AGQ92624.1};
OS   Vibrio parahaemolyticus O1:Kuk str. FDA_R31.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Vibrio.
OX   NCBI_TaxID=1338034 {ECO:0000313|EMBL:AGQ92624.1, ECO:0000313|Proteomes:UP000014929};
RN   [1] {ECO:0000313|EMBL:AGQ92624.1, ECO:0000313|Proteomes:UP000014929}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FDA_R31 {ECO:0000313|EMBL:AGQ92624.1};
RX   PubMed=25814612;
RA   Ludeke C.H., Kong N., Weimer B.C., Fischer M., Jones J.L.;
RT   "Complete Genome Sequences of a Clinical Isolate and an Environmental
RT   Isolate of Vibrio parahaemolyticus.";
RL   Genome Announc. 3:0-0(2015).
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; CP006005; AGQ92624.1; -; Genomic_DNA.
DR   RefSeq; WP_005462859.1; NC_021821.1.
DR   ProteinModelPortal; S5IV82; -.
DR   EnsemblBacteria; AGQ92624; AGQ92624; M634_17025.
DR   KEGG; vpf:M634_17025; -.
DR   KO; K04565; -.
DR   BioCyc; VPAR1338034-WGS:GSYU-33789-MONOMER; -.
DR   Proteomes; UP000014929; 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:UP000014929};
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    171       Superoxide dismutase [Cu-Zn].
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5004529982.
FT   DOMAIN       32    170       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   171 AA;  17487 MW;  2A99D8A540BED22A CRC64;
     MLKGLLCISA AAAFVMTPNA LAQSITMTDL GTNQAVGTVE LSESDYGIVF TPNLSGIPAG
     LHGFHVHANP SCDSAEKDGK TVVGGGAGGH YDPDNTGQHG FPWTDGNHLG DLPALYADME
     GNANQPVLAP RLKMSDLKGR ALMIHAGGDN HSDQPAKLGG GGARIVCGVI D
//
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