GenomeNet

Database: UniProt/TrEMBL
Entry: B6ERD2_ALISL
LinkDB: B6ERD2_ALISL
Original site: B6ERD2_ALISL 
ID   B6ERD2_ALISL            Unreviewed;       170 AA.
AC   B6ERD2;
DT   25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT   25-NOV-2008, sequence version 1.
DT   07-JUN-2017, entry version 55.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   Name=sodC {ECO:0000313|EMBL:CAQ81265.1};
GN   OrderedLocusNames=VSAL_II0511 {ECO:0000313|EMBL:CAQ81265.1};
OS   Aliivibrio salmonicida (strain LFI1238) (Vibrio salmonicida (strain
OS   LFI1238)).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Aliivibrio.
OX   NCBI_TaxID=316275 {ECO:0000313|EMBL:CAQ81265.1, ECO:0000313|Proteomes:UP000001730};
RN   [1] {ECO:0000313|EMBL:CAQ81265.1, ECO:0000313|Proteomes:UP000001730}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LFI1238 {ECO:0000313|EMBL:CAQ81265.1,
RC   ECO:0000313|Proteomes:UP000001730};
RX   PubMed=19099551; DOI=10.1186/1471-2164-9-616;
RA   Hjerde E., Lorentzen M.S., Holden M.T., Seeger K., Paulsen S.,
RA   Bason N., Churcher C., Harris D., Norbertczak H., Quail M.A.,
RA   Sanders S., Thurston S., Parkhill J., Willassen N.P., Thomson N.R.;
RT   "The genome sequence of the fish pathogen Aliivibrio salmonicida
RT   strain LFI1238 shows extensive evidence of gene decay.";
RL   BMC Genomics 9:616-616(2008).
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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; FM178380; CAQ81265.1; -; Genomic_DNA.
DR   RefSeq; WP_012551841.1; NC_011313.1.
DR   ProteinModelPortal; B6ERD2; -.
DR   STRING; 316275.VSAL_II0511; -.
DR   EnsemblBacteria; CAQ81265; CAQ81265; VSAL_II0511.
DR   KEGG; vsa:VSAL_II0511; -.
DR   eggNOG; ENOG4108Z7T; Bacteria.
DR   eggNOG; COG2032; LUCA.
DR   HOGENOM; HOG000263449; -.
DR   KO; K04565; -.
DR   OMA; HKGDIGN; -.
DR   OrthoDB; POG091H05JR; -.
DR   Proteomes; UP000001730; Chromosome 2.
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:UP000001730};
KW   Copper {ECO:0000256|RuleBase:RU000393};
KW   Metal-binding {ECO:0000256|RuleBase:RU000393};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000393,
KW   ECO:0000313|EMBL:CAQ81265.1}; 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_5002842543.
FT   DOMAIN       31    169       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   170 AA;  17761 MW;  C86E5671F2CAF10D CRC64;
     MFKKLLLTTL FVASAGASAS DISIEMKDLD SGKIVGYVSA EQNEYGVVFT PNLSGLPQGL
     HGFHVHENPS CDTSEKNGQT ILGGAAGGHY DPMKTGQHGF PWSNDSHLGD LPPLYVDMDG
     NAVQPVLSPK ITLANLSGRA LMIHAGSDNH SDHPKALGGG GARLVCGVIK
//
DBGET integrated database retrieval system