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Database: UniProt/TrEMBL
Entry: B5FA40_VIBFM
LinkDB: B5FA40_VIBFM
Original site: B5FA40_VIBFM 
ID   B5FA40_VIBFM            Unreviewed;       170 AA.
AC   B5FA40;
DT   14-OCT-2008, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2008, sequence version 1.
DT   25-OCT-2017, entry version 61.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   Name=sodC_1 {ECO:0000313|EMBL:ACH65234.1};
GN   OrderedLocusNames=VFMJ11_2160 {ECO:0000313|EMBL:ACH65234.1};
OS   Vibrio fischeri (strain MJ11).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Aliivibrio.
OX   NCBI_TaxID=388396 {ECO:0000313|EMBL:ACH65234.1, ECO:0000313|Proteomes:UP000001857};
RN   [1] {ECO:0000313|Proteomes:UP000001857}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MJ11 {ECO:0000313|Proteomes:UP000001857};
RA   Mandel M.J., Stabb E.V., Ruby E.G., Ferriera S., Johnson J.,
RA   Kravitz S., Beeson K., Sutton G., Rogers Y.-H., Friedman R.,
RA   Frazier M., Venter J.C.;
RT   "Complete sequence of Vibrio fischeri strain MJ11.";
RL   Submitted (AUG-2008) 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: 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; CP001139; ACH65234.1; -; Genomic_DNA.
DR   RefSeq; WP_012532914.1; NC_011184.1.
DR   ProteinModelPortal; B5FA40; -.
DR   EnsemblBacteria; ACH65234; ACH65234; VFMJ11_2160.
DR   KEGG; vfm:VFMJ11_2160; -.
DR   HOGENOM; HOG000263449; -.
DR   KO; K04565; -.
DR   OMA; HKGDIGN; -.
DR   OrthoDB; POG091H05JR; -.
DR   Proteomes; UP000001857; Chromosome I.
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; 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:UP000001857};
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     21       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        22    170       Superoxide dismutase [Cu-Zn].
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5002833337.
FT   DOMAIN       32    169       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   170 AA;  17988 MW;  D61144686EE103F1 CRC64;
     MKKHTFFAAF CFLSTSSIAH SAIVNMTELN SKTPVGQITI TNTEYGTVFT PELSNLPSGL
     HGFHIHTNPS CESATINNKT ILGGAAGGHY DPENTGKHGF PWTTNNHLGD LPALYVDHHG
     MANQPVIAPR IKLSDLKGRS IMIHAGGDNH SDHPAALGGG GARLVCGVIK
//
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