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Database: UniProt/TrEMBL
Entry: H2IMS5_VIBSJ
LinkDB: H2IMS5_VIBSJ
Original site: H2IMS5_VIBSJ 
ID   H2IMS5_VIBSJ            Unreviewed;       173 AA.
AC   H2IMS5;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   28-MAR-2018, entry version 38.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   ORFNames=VEJY3_23531 {ECO:0000313|EMBL:AEX25115.1};
OS   Vibrio sp. (strain EJY3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Vibrio.
OX   NCBI_TaxID=1116375 {ECO:0000313|EMBL:AEX25115.1, ECO:0000313|Proteomes:UP000006799};
RN   [1] {ECO:0000313|EMBL:AEX25115.1, ECO:0000313|Proteomes:UP000006799}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EJY3 {ECO:0000313|EMBL:AEX25115.1,
RC   ECO:0000313|Proteomes:UP000006799};
RX   PubMed=22535948; DOI=10.1128/JB.00303-12;
RA   Roh H., Yun E.J., Lee S., Ko H.J., Kim S., Kim B.Y., Song H.,
RA   Lim K.I., Kim K.H., Choi I.G.;
RT   "Genome sequence of Vibrio sp. strain EJY3, an agarolytic marine
RT   bacterium metabolizing 3,6-anhydro-L-galactose as a sole carbon
RT   source.";
RL   J. Bacteriol. 194:2773-2774(2012).
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; CP003242; AEX25115.1; -; Genomic_DNA.
DR   RefSeq; WP_014234951.1; NC_016614.1.
DR   STRING; 1116375.VEJY3_23531; -.
DR   EnsemblBacteria; AEX25115; AEX25115; VEJY3_23531.
DR   KEGG; vej:VEJY3_23531; -.
DR   PATRIC; fig|1116375.3.peg.4671; -.
DR   eggNOG; ENOG4108Z7T; Bacteria.
DR   eggNOG; COG2032; LUCA.
DR   KO; K04565; -.
DR   BioCyc; VSP1116375:G1H2F-4856-MONOMER; -.
DR   Proteomes; UP000006799; 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; 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:UP000006799};
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:UP000006799};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   SIGNAL        1     24       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        25    173       Superoxide dismutase [Cu-Zn].
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5003561455.
FT   DOMAIN       35    172       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   173 AA;  17939 MW;  ED1AA7162631D445 CRC64;
     MLKGLLRISA PVTLIGMIAP AAIAQSITMT DLNTNKSVGT VELSESQYGV VFSPQLTSIP
     AGLHGFHVHV NPSCESAEKD GKNVLGGAAG GHYDPQNTGK HGYPWTDDNH LGDLPPLYAD
     MEGNAVSPVV APRLKLSDLK GRALMIHAGG DNHSDQPAKL GGGGARIVCG VIE
//
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