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Database: UniProt
Entry: A7N4I4_VIBCB
LinkDB: A7N4I4_VIBCB
Original site: A7N4I4_VIBCB 
ID   A7N4I4_VIBCB            Unreviewed;       170 AA.
AC   A7N4I4;
DT   02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT   02-OCT-2007, sequence version 1.
DT   10-APR-2019, entry version 81.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   OrderedLocusNames=VIBHAR_06578 {ECO:0000313|EMBL:ABU74469.1};
OS   Vibrio campbellii (strain ATCC BAA-1116 / BB120).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Vibrio.
OX   NCBI_TaxID=338187 {ECO:0000313|EMBL:ABU74469.1, ECO:0000313|Proteomes:UP000008152};
RN   [1] {ECO:0000313|EMBL:ABU74469.1, ECO:0000313|Proteomes:UP000008152}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1116 / BB120 {ECO:0000313|Proteomes:UP000008152};
RG   The Vibrio harveyi Genome Sequencing Project;
RA   Bassler B., Clifton S.W., Fulton L., Delehaunty K., Fronick C.,
RA   Harrison M., Markivic C., Fulton R., Tin-Wollam A.-M., Shah N.,
RA   Pepin K., Nash W., Thiruvilangam P., Bhonagiri V., Waters C., Tu K.C.,
RA   Irgon J., Wilson R.K.;
RL   Submitted (AUG-2007) 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}.
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DR   EMBL; CP000790; ABU74469.1; -; Genomic_DNA.
DR   RefSeq; WP_012129993.1; NC_022270.1.
DR   ProteinModelPortal; A7N4I4; -.
DR   EnsemblBacteria; ABU74469; ABU74469; VIBHAR_06578.
DR   GeneID; 5558573; -.
DR   KEGG; vca:M892_19470; -.
DR   KEGG; vha:VIBHAR_06578; -.
DR   PATRIC; fig|338187.25.peg.3819; -.
DR   eggNOG; ENOG4108Z7T; Bacteria.
DR   eggNOG; COG2032; LUCA.
DR   HOGENOM; HOG000263449; -.
DR   KO; K04565; -.
DR   OMA; HKGDIGN; -.
DR   OrthoDB; 2015673at2; -.
DR   BioCyc; VCAM338187:G1HKJ-3876-MONOMER; -.
DR   Proteomes; UP000008152; 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; 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:UP000008152};
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     19       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        20    170       Superoxide dismutase [Cu-Zn].
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5002711366.
FT   DOMAIN       32    169       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   170 AA;  17334 MW;  1CF92D1526E27A6E CRC64;
     MKLSALMAAC VLLSGSALAD ELTVEMTDLA TGKSVGEVAI TTSDYGTVFT PNLSGLPSGA
     HGFHIHANGS CDSRIKDGKT VLGGAAGGHY DPKGTGQHGF PWTDGNHLGD LPAMYVDANG
     MANQPVLAPR VKLADVKGRA LMVHFGGDNH SDHPAKLGGG GARMVCGVIK
//
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